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Conserved domains on  [gi|489495878|ref|WP_003400794|]
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MULTISPECIES: non-ribosomal peptide synthetase Nrp [Mycobacterium]

Protein Classification

non-ribosomal peptide synthetase( domain architecture ID 19416104)

non-ribosomal peptide synthetase is a modular multidomain enzyme that acts as an assembly line to catalyze the biosynthesis of complex natural products

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK12467 super family cl36129
peptide synthase; Provisional
 575-2027 0e+00

peptide synthase; Provisional


The actual alignment was detected with superfamily member PRK12467:

Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 994.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  575 AYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARLVRSAAMKTGDLAA 654
Cdd:PRK12467  659 AYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEA 738

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  655 LVDDLVARETTIVDLPTAVWQLLCADGDAIdaiGRSRLRQIVIGGEAIRCSAVDKWLEsaASQGISLLSSYGPTEATVVA 734
Cdd:PRK12467  739 FAALMADQGVTVLKIVPSHLQALLQASRVA---LPRPQRALVCGGEALQVDLLARVRA--LGPGARLINHYGPTETTVGV 813

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  735 TFLPivCDQTTMDGALLRLGRPILPNTVFL-----------AFGEVVIVGDLVADGYLGIDG--------DGFGtvtaAD 795
Cdd:PRK12467  814 STYE--LSDEERDFGNVPIGQPLANLGLYIldhylnpvpvgVVGELYIGGAGLARGYHRRPAltaerfvpDPFG----AD 887

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  796 GSRrrAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAVELHSGS----LGVWFKSQRTRE 871
Cdd:PRK12467  888 GGR--LYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDaglqLVAYLVPAAVAD 965

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  872 GEQDAAAATRIRLVLVSL----GVSSFFVVgVPNIPRKPNGKIDSDNLPRLPQWSAAGLNTAETGQRAAGLSQIWSRQLG 947
Cdd:PRK12467  966 GAEHQATRDELKAQLRQVlpdyMVPAHLLL-LDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTELEKRLAAIWADVLK 1044

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  948 -RAIGPDSSLLGEGIGSLDLIRILPETRRYLGWRLSLLDLIGADTAANLADyAPTPDAPTgedRFRPLVAAQRPAAIPLS 1026
Cdd:PRK12467 1045 vERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQ-AVAAQQQG---AQPALPDVDRDQPLPLS 1120

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1027 FAQRRLWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVDGVPRQLVIEARRADLGCDIVDA 1106
Cdd:PRK12467 1121 YAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLTLEEPLLLA 1200

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1107 TAWPADRLQRAIEEAARHSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYASRCAGRAPDWAP 1186
Cdd:PRK12467 1201 ADKDEAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPA 1280

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1187 LPVQYVDYTLWQREILGDLDDsdspiAAQLAYWENALAGMPERLRLPTARPYPPVADQRGASLVVDWPASVQQQVRRIAR 1266
Cdd:PRK12467 1281 LPIQYADYAVWQRQWMDAGER-----ARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALAR 1355

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1267 QHNATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGRSDPALDNLVGFFVNTLVLRVNLAGDPSFAELLGQVRARSLAAYE 1346
Cdd:PRK12467 1356 REGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQA 1435

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1347 NQDVPFEVLVDRLKPTRALTHHPLIQVMLAWQ-DNPVGQLNLGDLQATPMPIDTRTARMDLVFSLAErfsegsEPAGIGG 1425
Cdd:PRK12467 1436 HQDLPFEQLVEALQPERSLSHSPLFQVMFNHQrDDHQAQAQLPGLSVESLSWESQTAQFDLTLDTYE------SSEGLQA 1509

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1426 AVEYRTDVFEAQAIDVLIERLRKVLVAVAAAPERTVSSIDALDGTERARLDEWGNRAvlTAPAPTPVSIPQMLAAQVARI 1505
Cdd:PRK12467 1510 SLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNAT--HTGYPLARLVHQLIEDQAAAT 1587

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1506 PEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFML 1585
Cdd:PRK12467 1588 PEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMI 1667

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1586 GDAVPVAAVTTAGLRSRL-AGHDLPIIdVVDA----LAAYPGTPPPM-PAAVNLAYILYTSGTTGEPKGVGITHRNVTRL 1659
Cdd:PRK12467 1668 EDSGIELLLTQSHLQARLpLPDGLRSL-VLDQeddwLEGYSDSNPAVnLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNR 1746

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1660 FASLPAR--LSAAQVWSQCHSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAEHVSVLTQTPAAVAMLpTQ 1737
Cdd:PRK12467 1747 LCATQEAyqLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQL-LQ 1825

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1738 GLESVA-------LVVAGEACPAALVDRW---APGRVMLNAYGPTETTICAA---ISAPLRPGSGMPPIGVPVSGAALFV 1804
Cdd:PRK12467 1826 MDEQVEhplslrrVVCGGEALEVEALRPWlerLPDTGLFNLYGPTETAVDVThwtCRRKDLEGRDSVPIGQPIANLSTYI 1905

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1805 LDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFGGSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGY 1884
Cdd:PRK12467 1906 LDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGF 1985

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1885 RIELGEVATALAELAGVGQAVVIAREDRPGdKRLVGYATEIAPGAVDPAG--------LRAQLAQRLPGYLVPAAVVVID 1956
Cdd:PRK12467 1986 RIELGEIEARLREQGGVREAVVIAQDGANG-KQLVAYVVPTDPGLVDDDEaqvalraiLKNHLKASLPEYMVPAHLVFLA 2064

                        1450      1460      1470      1480      1490      1500      1510
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489495878 1957 ALPLTVNGKLDHRALPAPEYGD-TNGYRAPAGPVEKTVAGIFARVLGLERVGVDDSFFELGGDSLAAMRVIA 2027
Cdd:PRK12467 2065 RMPLTPNGKLDRKALPAPDASElQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVS 2136
Thioester-redct TIGR01746
thioester reductase domain; This model includes the terminal domain from the fungal alpha ...
 2109-2511 8.77e-122

thioester reductase domain; This model includes the terminal domain from the fungal alpha aminoadipate reductase enzyme (also known as aminoadipate semialdehyde dehydrogenase) which is involved in the biosynthesis of lysine, as well as the reductase-containing component of the myxochelin biosynthetic gene cluster, MxcG. The mechanism of reduction involves activation of the substrate by adenylation and transfer to a covalently-linked pantetheine cofactor as a thioester. This thioester is then reduced to give an aldehyde (thus releasing the product) and a regenerated pantetheine thiol. (In myxochelin biosynthesis this aldehyde is further reduced to an alcohol or converted to an amine by an aminotransferase.) This is a fundamentally different reaction than beta-ketoreductase domains of polyketide synthases which act at a carbonyl two carbons removed from the thioester and forms an alcohol as a product. This domain is invariably found at the C-terminus of the proteins which contain it (presumably because it results in the release of the product). The majority of hits to this model are non-ribosomal peptide synthetases in which this domain is similarly located proximal to a thiolation domain (pfam00550). In some cases this domain is found at the end of a polyketide synthetase enzyme, but is unlike ketoreductase domains which are found before the thiolase domains. Exceptions to this observed relationship with the thiolase domain include three proteins which consist of stand-alone reductase domains (GP|466833 from M. leprae, GP|435954 from Anabaena and OMNI|NTL02SC1199 from Strep. coelicolor) and one protein (OMNI|NTL01NS2636 from Nostoc) which contains N-terminal homology with a small group of hypothetical proteins but no evidence of a thiolation domain next to the putative reductase domain. Below the noise cutoff to this model are proteins containing more distantly related ketoreductase and dehydratase/epimerase domains. It has been suggested that a NADP-binding motif can be found in the N-terminal portion of this domain that may form a Rossman-type fold.


:

Pssm-ID: 273787 [Multi-domain]  Cd Length: 367  Bit Score: 389.85  E-value: 8.77e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2109 TVLLTGATGFLGRYLVLELLRRLdVDGRLICLVRAESDEDARRRLEKTFDSgdpELLRHFkELAADRLEVVAGDKSEPDL 2188
Cdd:TIGR01746    1 TVLLTGATGFLGAYLLEELLRRS-TRAKVICLVRADSEEHAMERLREALRS---YRLWHE-NLAMERIEVVAGDLSKPRL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2189 GLDQPMWRRLAETVDLIVDSAAMVN-AFPYHELFGPNVAGTAELIRIALTTKLKPFTYVSTADVGAAIEPSAFtedadIR 2267
Cdd:TIGR01746   76 GLSDAEWERLAENVDTIVHNGALVNhVYPYSELRGANVLGTVEVLRLAASGRAKPLHYVSTISVGAAIDLSTG-----VT 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2268 VISPTRTVDGGWAGGYGTSKWAGEVLLREANDLcALPVAVFRCGMILADtSYAGQLNMSDWVTRMVLSLMATGIAprsfy 2347
Cdd:TIGR01746  151 EDDATVTPYPGLAGGYTQSKWVAELLVREASDR-GLPVTIVRPGRILGD-SYTGAWNSSDILWRMVKGCLALGAY----- 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2348 ePDSEGNrqraHFDGLPVTFVAEAIAVLGARVAGSslAGFATYHVMNPhdDGIGLDEYVDWLIEAGYPIrRIDDFAEWLQ 2427
Cdd:TIGR01746  224 -PQSPEL----TEDLTPVDFVARAIVALSSRPAAS--AGGIVFHVVNP--NPVPLDEFLEWLERAGYNL-RLVSFDEWLQ 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2428 RFEASLGALPDRqRRHSVLPMLLASNSQRLQPlkptrgcsaPTDRFRAAVRAAKVGSDKDNPDIPHVSAPTIINYVTNLQ 2507
Cdd:TIGR01746  294 RLEDSDTAKRDS-RRYPLLPLLHFTGDAFESD---------ETDTRNLDSRSTAEALEGDGIREPSITAPLLHLYLQYLK 363


                   ....
gi 489495878  2508 LLGL 2511
Cdd:TIGR01746  364 EIGF 367
AFD_class_I super family cl17068
Adenylate forming domain, Class I superfamily; This family includes acyl- and aryl-CoA ligases, ...
 473-622 1.66e-03

Adenylate forming domain, Class I superfamily; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


The actual alignment was detected with superfamily member cd05906:

Pssm-ID: 473059 [Multi-domain]  Cd Length: 540  Bit Score: 43.81  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  473 AWLVQRGAAPGDVLVFTDDDTDKTIDLLIACHLAG---CGYSVCDTADEISVRTNAItEH-----GDGILVT---VVDVA 541
Cdd:cd05906    54 AGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGfvpAPLTVPPTYDEPNARLRKL-RHiwqllGSPVVLTdaeLVAEF 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  542 ATQLAVVGHDELRKVVDERVTQVTHDALLATKT----AYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVL 617
Cdd:cd05906   133 AGLETLSGLPGIRVLSIEELLDTAADHDLPQSRpddlALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFL 212


                  ....*
gi 489495878  618 QCAPL 622
Cdd:cd05906   213 NWVPL 217
 
Name Accession Description Interval E-value
PRK12467 PRK12467
peptide synthase; Provisional
 575-2027 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 994.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  575 AYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARLVRSAAMKTGDLAA 654
Cdd:PRK12467  659 AYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEA 738

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  655 LVDDLVARETTIVDLPTAVWQLLCADGDAIdaiGRSRLRQIVIGGEAIRCSAVDKWLEsaASQGISLLSSYGPTEATVVA 734
Cdd:PRK12467  739 FAALMADQGVTVLKIVPSHLQALLQASRVA---LPRPQRALVCGGEALQVDLLARVRA--LGPGARLINHYGPTETTVGV 813

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  735 TFLPivCDQTTMDGALLRLGRPILPNTVFL-----------AFGEVVIVGDLVADGYLGIDG--------DGFGtvtaAD 795
Cdd:PRK12467  814 STYE--LSDEERDFGNVPIGQPLANLGLYIldhylnpvpvgVVGELYIGGAGLARGYHRRPAltaerfvpDPFG----AD 887

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  796 GSRrrAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAVELHSGS----LGVWFKSQRTRE 871
Cdd:PRK12467  888 GGR--LYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDaglqLVAYLVPAAVAD 965

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  872 GEQDAAAATRIRLVLVSL----GVSSFFVVgVPNIPRKPNGKIDSDNLPRLPQWSAAGLNTAETGQRAAGLSQIWSRQLG 947
Cdd:PRK12467  966 GAEHQATRDELKAQLRQVlpdyMVPAHLLL-LDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTELEKRLAAIWADVLK 1044

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  948 -RAIGPDSSLLGEGIGSLDLIRILPETRRYLGWRLSLLDLIGADTAANLADyAPTPDAPTgedRFRPLVAAQRPAAIPLS 1026
Cdd:PRK12467 1045 vERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQ-AVAAQQQG---AQPALPDVDRDQPLPLS 1120

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1027 FAQRRLWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVDGVPRQLVIEARRADLGCDIVDA 1106
Cdd:PRK12467 1121 YAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLTLEEPLLLA 1200

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1107 TAWPADRLQRAIEEAARHSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYASRCAGRAPDWAP 1186
Cdd:PRK12467 1201 ADKDEAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPA 1280

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1187 LPVQYVDYTLWQREILGDLDDsdspiAAQLAYWENALAGMPERLRLPTARPYPPVADQRGASLVVDWPASVQQQVRRIAR 1266
Cdd:PRK12467 1281 LPIQYADYAVWQRQWMDAGER-----ARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALAR 1355

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1267 QHNATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGRSDPALDNLVGFFVNTLVLRVNLAGDPSFAELLGQVRARSLAAYE 1346
Cdd:PRK12467 1356 REGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQA 1435

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1347 NQDVPFEVLVDRLKPTRALTHHPLIQVMLAWQ-DNPVGQLNLGDLQATPMPIDTRTARMDLVFSLAErfsegsEPAGIGG 1425
Cdd:PRK12467 1436 HQDLPFEQLVEALQPERSLSHSPLFQVMFNHQrDDHQAQAQLPGLSVESLSWESQTAQFDLTLDTYE------SSEGLQA 1509

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1426 AVEYRTDVFEAQAIDVLIERLRKVLVAVAAAPERTVSSIDALDGTERARLDEWGNRAvlTAPAPTPVSIPQMLAAQVARI 1505
Cdd:PRK12467 1510 SLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNAT--HTGYPLARLVHQLIEDQAAAT 1587

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1506 PEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFML 1585
Cdd:PRK12467 1588 PEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMI 1667

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1586 GDAVPVAAVTTAGLRSRL-AGHDLPIIdVVDA----LAAYPGTPPPM-PAAVNLAYILYTSGTTGEPKGVGITHRNVTRL 1659
Cdd:PRK12467 1668 EDSGIELLLTQSHLQARLpLPDGLRSL-VLDQeddwLEGYSDSNPAVnLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNR 1746

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1660 FASLPAR--LSAAQVWSQCHSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAEHVSVLTQTPAAVAMLpTQ 1737
Cdd:PRK12467 1747 LCATQEAyqLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQL-LQ 1825

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1738 GLESVA-------LVVAGEACPAALVDRW---APGRVMLNAYGPTETTICAA---ISAPLRPGSGMPPIGVPVSGAALFV 1804
Cdd:PRK12467 1826 MDEQVEhplslrrVVCGGEALEVEALRPWlerLPDTGLFNLYGPTETAVDVThwtCRRKDLEGRDSVPIGQPIANLSTYI 1905

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1805 LDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFGGSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGY 1884
Cdd:PRK12467 1906 LDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGF 1985

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1885 RIELGEVATALAELAGVGQAVVIAREDRPGdKRLVGYATEIAPGAVDPAG--------LRAQLAQRLPGYLVPAAVVVID 1956
Cdd:PRK12467 1986 RIELGEIEARLREQGGVREAVVIAQDGANG-KQLVAYVVPTDPGLVDDDEaqvalraiLKNHLKASLPEYMVPAHLVFLA 2064

                        1450      1460      1470      1480      1490      1500      1510
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489495878 1957 ALPLTVNGKLDHRALPAPEYGD-TNGYRAPAGPVEKTVAGIFARVLGLERVGVDDSFFELGGDSLAAMRVIA 2027
Cdd:PRK12467 2065 RMPLTPNGKLDRKALPAPDASElQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVS 2136
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 1006-2210 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 975.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1006 TGEDRFRPLVAAQRPAAIPLSFAQRRLWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVDG 1085
Cdd:COG1020     1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1086 VPRQLVIEARRADLG--CDIVDATAWPADRLQRAIEEAARHSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVA 1163
Cdd:COG1020    81 RPVQVIQPVVAAPLPvvVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1164 PLTADLSAAYASRCAGRAPDWAPLPVQYVDYTLWQREilgdlDDSDSPIAAQLAYWENALAGMPERLRLPTARPYPPVAD 1243
Cdd:COG1020   161 LLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQRE-----WLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQS 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1244 QRGASLVVDWPASVQQQVRRIARQHNATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGRSDPALDNLVGFFVNTLVLRVN 1323
Cdd:COG1020   236 YRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVD 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1324 LAGDPSFAELLGQVRARSLAAYENQDVPFEVLVDRLKPTRALTHHPLIQVMLAWQDNPVGQLNLGDLQATPMPIDTRTAR 1403
Cdd:COG1020   316 LSGDPSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAK 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1404 MDLVFSLAERfsegsePAGIGGAVEYRTDVFEAQAIDVLIERLRKVLVAVAAAPERTVSSIDALDGTERARLDEWGNRAv 1483
Cdd:COG1020   396 FDLTLTVVET------GDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNAT- 468

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1484 lTAPAPTPVSIPQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVL 1563
Cdd:COG1020   469 -AAPYPADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVL 547

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1564 KTGAAYLPIDPANPPPRVAFMLGDAVPVAAVTTAGLRSRLAGHDLPIIDV-VDALAAYPGTPPPMPAAV-NLAYILYTSG 1641
Cdd:COG1020   548 KAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVPVLALdALALAAEPATNPPVPVTPdDLAYVIYTSG 627

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1642 TTGEPKGVGITHRNVTRLFASLPAR--LSAAQVWSQCHSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAE 1719
Cdd:COG1020   628 STGRPKGVMVEHRALVNLLAWMQRRygLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARH 707

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1720 HVSVLTQTPAAVAMLPTQGLESVA----LVVAGEACPAALVDRWA---PGRVMLNAYGPTETTICAAIS--APLRPGSGM 1790
Cdd:COG1020   708 RVTVLNLTPSLLRALLDAAPEALPslrlVLVGGEALPPELVRRWRarlPGARLVNLYGPTETTVDSTYYevTPPDADGGS 787

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1791 PPIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFGGSGARMYRTGDLVCWRADGQLE 1870
Cdd:COG1020   788 VPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGARLYRTGDLARWLPDGNLE 867

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1871 FLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATEIAPGAVDPAGLRAQLAQRLPGYLVPA 1950
Cdd:COG1020   868 FLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPA 947

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1951 AVVVIDALPLTVNGKLDHRALPAPEYGDTNGYRAPAGPVEKTVAGIFARVLGLERVGVDDSFFELGGDSLAAMRVIAAIN 2030
Cdd:COG1020   948 AVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAA 1027

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2031 TTLNADLPVRALLHASSTRGLSQLLGRDARPTSDPRLVSVHGDNPTEVHASDLTLDRFIDADTLATAVNLPGPSPELRTV 2110
Cdd:COG1020  1028 RLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLL 1107

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2111 LLTGATGFLGRYLVLELLRRLDVDGRLICLVRAESDEDARRRLEKTFDSGDPELLRHFKELAADRLEVVAGDKSEPDLGL 2190
Cdd:COG1020  1108 LLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLL 1187

                        1210      1220
                  ....*....|....*....|
gi 489495878 2191 DQPMWRRLAETVDLIVDSAA 2210
Cdd:COG1020  1188 LLLLLLLLLLLLLLLLLLLL 1207
carboxyl_red NF041592
carboxylic acid reductase;
1519-2512 0e+00

carboxylic acid reductase;


Pssm-ID: 469476 [Multi-domain]  Cd Length: 1161  Bit Score: 835.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1519 TYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPP-----------PRV----AF 1583
Cdd:NF041592   79 TYRELWDRVGAVAAALAGDPVRPGDRVAVLGFTSVDYTTIDLALIRLGAVAVPLQTSAPVaqlrpivaetePRVlaasVD 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1584 MLGDAVPVAAVTT---------------------AGLRSRLAGHDL----PIIDVVDALAAYPGTPPPMPAAVN-LAYIL 1637
Cdd:NF041592  159 LLDDAVELVLTGPaprrlvvfdyhpevddhrealEAARARLADAGPvvveTLAEVLERGRALPAAPPPASDDDDpLALLI 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1638 YTSGTTGEPKGVGITHRNVTRLFaslpaRLSAAQVWSQC-------------HSYGFDAsaweIWGALLGGGRLVIVPES 1704
Cdd:NF041592  239 YTSGSTGAPKGAMYTERLVANMW-----RGSARAGWGPRavpsitlnfmpmsHVMGRGT----LYGTLARGGTAYFAARS 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1705 vaaspnDFHGLLvaEHVSVLTQT-----PAAVAML--------PTQGLESVALVVAGEACPAALVDRWAPGRVMlnaygp 1771
Cdd:NF041592  310 ------DLSTLL--EDLALVRPTelnfvPRVWDMLfqeyqselDRRAADGADRAAAEAAVKAELREDLLGGRFV------ 375

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1772 TETTICAAISAPLRPGS----GMPPI---GVPVSGAALF--------VLDSWL------------RPVPAGvagELYIAG 1824
Cdd:NF041592  376 SAMTGSAPISAEMKAFVesllDLHLHdgyGSTEAGGVFIdgrvrrppVLDYKLvdvpelgyfgtdRPHPRG---ELLVKT 452

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1825 AGVGVGYWRRAGLTASRFVACPFggsgarmYRTGDLVCWRADGQLEFLGRTDDQVKI-RGYRIELGEVATALAELAGVGQ 1903
Cdd:NF041592  453 TTMFPGYYKRPEVTAEVFDEDGF-------YRTGDIVAELGPDQLVYVDRRNNVLKLsQGEFVTVSKLEAVFGDSPLVRQ 525

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1904 AVVIAREDRPGDKRLVGYATEIAPGAVDPAGLRAQLAQ---------RLPGYLVPAAVVvIDALPLTV-NGKL-DHRALP 1972
Cdd:NF041592  526 IYVYGNSARAYLLAVVVPTEEALARHGDAAELKALIAEslqrvareaGLQSYEIPRDFL-IETTPFTLeNGLLtGIRKLA 604

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1973 APE----YGD-------------TNGYRA-----PAGPVEKTVAGIFARVLGLERVGV--DDSFFELGGDSLAAMRVIAA 2028
Cdd:NF041592  605 RPKlkerYGErleqlytelaagqADELRAlrrsgADRPVLETVGRAAAALLGAAAADLrpDAHFTDLGGDSLSALTFSNL 684

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2029 INTTLNADLPVRALLH-ASSTRGL-----SQLLGRDARPTSDprlvSVHGDNPTEVHASDLTLDRFIDADTLATAVNLPG 2102
Cdd:NF041592  685 LHEIFGVEVPVGVIVSpATDLRALadyieAERASGAKRPTFA----SVHGRDATEVRAADLTLDKFIDAATLAAAPSLPG 760

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2103 PSPELRTVLLTGATGFLGRYLVLELLRRLD-VDGRLICLVRAESDEDARRRLEKTFDSGDPELLRHFKELAADRLEVVAG 2181
Cdd:NF041592  761 PSGEVRTVLLTGATGFLGRYLALEWLERLAlVGGTLICLVRAKDDAAARARLDATFDSGDPELLAHYRELAADHLEVLAG 840

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2182 DKSEPDLGLDQPMWRRLAETVDLIVDSAAMVN-AFPYHELFGPNVAGTAELIRIALTTKLKPFTYVSTADVGAAIEPSAF 2260
Cdd:NF041592  841 DKGEPDLGLDRATWQRLADTVDLIVDPAALVNhVLPYSQLFGPNVVGTAELIRLALTTRLKPFTYLSTIGVGAQIEPGAF 920

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2261 TEDADIRVISPTRTVDGGWAGGYGTSKWAGEVLLREANDLCALPVAVFRCGMILADTSYAGQLNMSDWVTRMVLSLMATG 2340
Cdd:NF041592  921 TEDADIREISPVRAIDDSYANGYGNSKWAGEVLLREAHDLCGLPVAVFRCDMILADTRYAGQLNLPDMFTRLMLSLVATG 1000

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2341 IAPRSFYEPDSEGNRQRAHFDGLPVTFVAEAIAVLGARVAgsslAGFATYHVMNPHDDGIGLDEYVDWLIEAGYPIRRID 2420
Cdd:NF041592 1001 IAPGSFYELDADGNRQRAHYDGLPVDFIAEAIATLGARVT----DGFETYHVMNPHDDGIGLDEFVDWLIEAGHPIQRID 1076

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2421 DFAEWLQRFEASLGALPDRQRRHSVLPMLLASNsqrlQPLKPTRGCSAPTDRFRAAVRAAKVGSDKdnpDIPHVSAPTII 2500
Cdd:NF041592 1077 DYADWLQRFETALRALPERQRQASLLPLLHNYR----RPAPPIRGSIAPTDRFRAAVQEAKIGPDK---DIPHLTPALIV 1149

                        1130
                  ....*....|..
gi 489495878 2501 NYVTNLQLLGLL 2512
Cdd:NF041592 1150 KYVTDLRLLGLL 1161
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
 1023-1457 0e+00

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 660.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1023 IPLSFAQRRLWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVDGVPRQLVIEARRADLGCD 1102
Cdd:cd19540     2 IPLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLPAAEARPDLT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1103 IVDATAwpaDRLQRAIEEAARHSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYASRCAGRAP 1182
Cdd:cd19540    82 VVDVTE---DELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRAP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1183 DWAPLPVQYVDYTLWQREILGDLDDSDSPIAAQLAYWENALAGMPERLRLPTARPYPPVADQRGASLVVDWPASVQQQVR 1262
Cdd:cd19540   159 DWAPLPVQYADYALWQRELLGDEDDPDSLAARQLAYWRETLAGLPEELELPTDRPRPAVASYRGGTVEFTIDAELHARLA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1263 RIARQHNATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGRSDPALDNLVGFFVNTLVLRVNLAGDPSFAELLGQVRARSL 1342
Cdd:cd19540   239 ALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDL 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1343 AAYENQDVPFEVLVDRLKPTRALTHHPLIQVMLAWQDNPVGQLNLGDLQATPMPIDTRTARMDLVFSLAERFSEGSEPAG 1422
Cdd:cd19540   319 AAFAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFTLTERRDADGAPAG 398

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 489495878 1423 IGGAVEYRTDVFEAQAIDVLIERLRKVLVAVAAAP 1457
Cdd:cd19540   399 LTGELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 1519-1906 6.06e-146

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 460.58  E-value: 6.06e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1519 TYRELDEASNRLAHRL-AGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVTTA 1597
Cdd:TIGR01733    1 TYRELDERANRLARHLrAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1598 GLRSRLAGHDLPIIDVVDAL------AAYPGTPPPMPAAVNLAYILYTSGTTGEPKGVGITHRNVTRLFASLPAR--LSA 1669
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDPLElaalddAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRygLDP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1670 AQVWSQCHSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAEH-VSVLTQTPAAVAMLPTQGLESVA----L 1744
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHpVTVLNLTPSLLALLAAALPPALAslrlV 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1745 VVAGEACPAALVDRWA---PGRVMLNAYGPTETTICAA---ISAPLRPGSGMPPIGVPVSGAALFVLDSWLRPVPAGVAG 1818
Cdd:TIGR01733  241 ILGGEALTPALVDRWRargPGARLINLYGPTETTVWSTatlVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1819 ELYIAGAGVGVGYWRRAGLTASRFVACPF-GGSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAE 1897
Cdd:TIGR01733  321 ELYIGGPGVARGYLNRPELTAERFVPDPFaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400


                   ....*....
gi 489495878  1898 LAGVGQAVV 1906
Cdd:TIGR01733  401 HPGVREAVV 409
Thioester-redct TIGR01746
thioester reductase domain; This model includes the terminal domain from the fungal alpha ...
 2109-2511 8.77e-122

thioester reductase domain; This model includes the terminal domain from the fungal alpha aminoadipate reductase enzyme (also known as aminoadipate semialdehyde dehydrogenase) which is involved in the biosynthesis of lysine, as well as the reductase-containing component of the myxochelin biosynthetic gene cluster, MxcG. The mechanism of reduction involves activation of the substrate by adenylation and transfer to a covalently-linked pantetheine cofactor as a thioester. This thioester is then reduced to give an aldehyde (thus releasing the product) and a regenerated pantetheine thiol. (In myxochelin biosynthesis this aldehyde is further reduced to an alcohol or converted to an amine by an aminotransferase.) This is a fundamentally different reaction than beta-ketoreductase domains of polyketide synthases which act at a carbonyl two carbons removed from the thioester and forms an alcohol as a product. This domain is invariably found at the C-terminus of the proteins which contain it (presumably because it results in the release of the product). The majority of hits to this model are non-ribosomal peptide synthetases in which this domain is similarly located proximal to a thiolation domain (pfam00550). In some cases this domain is found at the end of a polyketide synthetase enzyme, but is unlike ketoreductase domains which are found before the thiolase domains. Exceptions to this observed relationship with the thiolase domain include three proteins which consist of stand-alone reductase domains (GP|466833 from M. leprae, GP|435954 from Anabaena and OMNI|NTL02SC1199 from Strep. coelicolor) and one protein (OMNI|NTL01NS2636 from Nostoc) which contains N-terminal homology with a small group of hypothetical proteins but no evidence of a thiolation domain next to the putative reductase domain. Below the noise cutoff to this model are proteins containing more distantly related ketoreductase and dehydratase/epimerase domains. It has been suggested that a NADP-binding motif can be found in the N-terminal portion of this domain that may form a Rossman-type fold.


Pssm-ID: 273787 [Multi-domain]  Cd Length: 367  Bit Score: 389.85  E-value: 8.77e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2109 TVLLTGATGFLGRYLVLELLRRLdVDGRLICLVRAESDEDARRRLEKTFDSgdpELLRHFkELAADRLEVVAGDKSEPDL 2188
Cdd:TIGR01746    1 TVLLTGATGFLGAYLLEELLRRS-TRAKVICLVRADSEEHAMERLREALRS---YRLWHE-NLAMERIEVVAGDLSKPRL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2189 GLDQPMWRRLAETVDLIVDSAAMVN-AFPYHELFGPNVAGTAELIRIALTTKLKPFTYVSTADVGAAIEPSAFtedadIR 2267
Cdd:TIGR01746   76 GLSDAEWERLAENVDTIVHNGALVNhVYPYSELRGANVLGTVEVLRLAASGRAKPLHYVSTISVGAAIDLSTG-----VT 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2268 VISPTRTVDGGWAGGYGTSKWAGEVLLREANDLcALPVAVFRCGMILADtSYAGQLNMSDWVTRMVLSLMATGIAprsfy 2347
Cdd:TIGR01746  151 EDDATVTPYPGLAGGYTQSKWVAELLVREASDR-GLPVTIVRPGRILGD-SYTGAWNSSDILWRMVKGCLALGAY----- 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2348 ePDSEGNrqraHFDGLPVTFVAEAIAVLGARVAGSslAGFATYHVMNPhdDGIGLDEYVDWLIEAGYPIrRIDDFAEWLQ 2427
Cdd:TIGR01746  224 -PQSPEL----TEDLTPVDFVARAIVALSSRPAAS--AGGIVFHVVNP--NPVPLDEFLEWLERAGYNL-RLVSFDEWLQ 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2428 RFEASLGALPDRqRRHSVLPMLLASNSQRLQPlkptrgcsaPTDRFRAAVRAAKVGSDKDNPDIPHVSAPTIINYVTNLQ 2507
Cdd:TIGR01746  294 RLEDSDTAKRDS-RRYPLLPLLHFTGDAFESD---------ETDTRNLDSRSTAEALEGDGIREPSITAPLLHLYLQYLK 363


                   ....
gi 489495878  2508 LLGL 2511
Cdd:TIGR01746  364 EIGF 367
SDR_e1 cd05235
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins ...
 2109-2425 6.56e-98

extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins identified as putative polyketide sythases fatty acid synthases (FAS), and nonribosomal peptide synthases, among others. However, unlike the usual ketoreductase modules of FAS and polyketide synthase, these domains are related to the extended SDRs, and have canonical NAD(P)-binding motifs and an active site tetrad. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187546 [Multi-domain]  Cd Length: 290  Bit Score: 317.67  E-value: 6.56e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2109 TVLLTGATGFLGRYLVLELLRRLDVdGRLICLVRAESDEDARRRLEKTFDSGDpelLRHFKELAADRLEVVAGDKSEPDL 2188
Cdd:cd05235     1 TVLLTGATGFLGAYLLRELLKRKNV-SKIYCLVRAKDEEAALERLIDNLKEYG---LNLWDELELSRIKVVVGDLSKPNL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2189 GLDQPMWRRLAETVDLIVDSAAMVNAF-PYHELFGPNVAGTAELIRIALTTKLKPFTYVSTADVGAAIEPSAFTEDADir 2267
Cdd:cd05235    77 GLSDDDYQELAEEVDVIIHNGANVNWVyPYEELKPANVLGTKELLKLAATGKLKPLHFVSTLSVFSAEEYNALDDEES-- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2268 viSPTRTVDGGWAGGYGTSKWAGEVLLREANDLcALPVAVFRCGMILADtSYAGQLNMSDWVTRMVLSLMATGIAPRSfy 2347
Cdd:cd05235   155 --DDMLESQNGLPNGYIQSKWVAEKLLREAANR-GLPVAIIRPGNIFGD-SETGIGNTDDFFWRLLKGCLQLGIYPIS-- 228

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489495878 2348 epdsegnrqRAHFDGLPVTFVAEAIAVLgarvAGSSLAGFATYHVMNPHddGIGLDEYVDWLIEAGYPIRRIDDFaEW 2425
Cdd:cd05235   229 ---------GAPLDLSPVDWVARAIVKL----ALNESNEFSIYHLLNPP--LISLNDLLDALEEKGYSIKEVSYE-EW 290
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 1023-1475 1.53e-93

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 311.96  E-value: 1.53e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1023 IPLSFAQRRLWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFP-AVDGVPRQLVIEARRADLgc 1101
Cdd:pfam00668    5 YPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIrQENGEPVQVILEERPFEL-- 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1102 DIVDATAWPADRLQRAIEEAAR----HSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYASRC 1177
Cdd:pfam00668   83 EIIDISDLSESEEEEAIEAFIQrdlqSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLL 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1178 AGRAPDWAPLPvQYVDYTLWQREILGDLDdsdspIAAQLAYWENALAGMPERLRLPTARPYPPVADQRGASLVVDWPASV 1257
Cdd:pfam00668  163 KGEPLPLPPKT-PYKDYAEWLQQYLQSED-----YQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDT 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1258 QQQVRRIARQHNATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGRSDPALDNLVGFFVNTLVLRVNLAGDPSFAELLGQV 1337
Cdd:pfam00668  237 EELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRV 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1338 RARSLAAYENQDVPFEVLVDRLKPTRALTHHPLIQVMLA-----WQDNPVGQLNLGDLQATPMPIDTRTARMDLVFSLAE 1412
Cdd:pfam00668  317 QEDLLSAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSfqnylGQDSQEEEFQLSELDLSVSSVIEEEAKYDLSLTASE 396

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489495878  1413 RfsEGsepaGIGGAVEYRTDVFEAQAIDVLIERLRKVLVAVAAAPERTVSSIDALDGTERARL 1475
Cdd:pfam00668  397 R--GG----GLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKL 453
Lys2b COG3320
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ...
 2108-2396 6.66e-90

Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary metabolites biosynthesis, transport and catabolism]; Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 442549 [Multi-domain]  Cd Length: 265  Bit Score: 293.65  E-value: 6.66e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2108 RTVLLTGATGFLGRYLVLELLRRldVDGRLICLVRAESDEDARRRLEKTFDSGDPELlrhfkELAADRLEVVAGDKSEPD 2187
Cdd:COG3320     1 RTVLLTGATGFLGAHLLRELLRR--TDARVYCLVRASDEAAARERLEALLERYGLWL-----ELDASRVVVVAGDLTQPR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2188 LGLDQPMWRRLAETVDLIVDSAAMVN-AFPYHELFGPNVAGTAELIRIALTTKLKPFTYVSTADVGAAIEPSAFTEDADI 2266
Cdd:COG3320    74 LGLSEAEFQELAEEVDAIVHLAALVNlVAPYSELRAVNVLGTREVLRLAATGRLKPFHYVSTIAVAGPADRSGVFEEDDL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2267 RvisptrtVDGGWAGGYGTSKWAGEVLLREANDLcALPVAVFRCGMILADTSyAGQLNMSDWVTRMVLSLMATGIAPrsf 2346
Cdd:COG3320   154 D-------EGQGFANGYEQSKWVAEKLVREARER-GLPVTIYRPGIVVGDSR-TGETNKDDGFYRLLKGLLRLGAAP--- 221

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 489495878 2347 yepdsegNRQRAHFDGLPVTFVAEAIAVLGARVAgsslAGFATYHVMNPH 2396
Cdd:COG3320   222 -------GLGDARLNLVPVDYVARAIVHLSRQPE----AAGRTFHLTNPQ 260
NAD_binding_4 pfam07993
Male sterility protein; This family represents the C-terminal region of the male sterility ...
 2112-2372 2.94e-77

Male sterility protein; This family represents the C-terminal region of the male sterility protein in a number of arabidopsis and drosophila. A sequence-related jojoba acyl CoA reductase is also included.


Pssm-ID: 462334 [Multi-domain]  Cd Length: 257  Bit Score: 257.15  E-value: 2.94e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2112 LTGATGFLGRYLVLELLRRLDVDGRLICLVRAESDEDARRRLEKTFDSGDPELLrhFKELAADRLEVVAGDKSEPDLGLD 2191
Cdd:pfam07993    1 LTGATGFLGKVLLEKLLRSTPDVKKIYLLVRAKDGESALERLRQELEKYPLFDA--LLKEALERIVPVAGDLSEPNLGLS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2192 QPMWRRLAETVDLIVDSAAMVN-AFPYHELFGPNVAGTAELIRIALTTK-LKPFTYVSTAdVGAAIEPSAFTEDA----- 2264
Cdd:pfam07993   79 EEDFQELAEEVDVIIHSAATVNfVEPYDDARAVNVLGTREVLRLAKQGKqLKPFHHVSTA-YVNGERGGLVEEKPypege 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2265 -DIRVISPTRTVDGGWAGGYGTSKWAGEVLLREANDlCALPVAVFRCGMILADtSYAGQLNMSDWVTRMVLSLMATGIAP 2343
Cdd:pfam07993  158 dDMLLDEDEPALLGGLPNGYTQTKWLAEQLVREAAR-RGLPVVIYRPSIITGE-PKTGWINNFDFGPRGLLGGIGKGVLP 235

                          250       260
                   ....*....|....*....|....*....
gi 489495878  2344 RSFYEPDsegnrqrAHFDGLPVTFVAEAI 2372
Cdd:pfam07993  236 SILGDPD-------AVLDLVPVDYVANAI 257
PLN02503 PLN02503
fatty acyl-CoA reductase 2
 2111-2251 8.29e-11

fatty acyl-CoA reductase 2


Pssm-ID: 215279 [Multi-domain]  Cd Length: 605  Bit Score: 67.58  E-value: 8.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2111 LLTGATGFLGRYLVLELLRRLDVDGRLICLVRAESDEDARRRLEKtfDSGDPELLRHFKE--------LAADRLEVVAGD 2182
Cdd:PLN02503  123 LITGATGFLAKVLIEKILRTNPDVGKIYLLIKAKDKEAAIERLKN--EVIDAELFKCLQEthgksyqsFMLSKLVPVVGN 200

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489495878 2183 KSEPDLGLDQPMWRRLAETVDLIVDSAAMvNAFP--YHELFGPNVAGTAELIRIALT-TKLKPFTYVSTADV 2251
Cdd:PLN02503  201 VCESNLGLEPDLADEIAKEVDVIINSAAN-TTFDerYDVAIDINTRGPCHLMSFAKKcKKLKLFLQVSTAYV 271
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 1993-2057 2.05e-06

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 48.02  E-value: 2.05e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489495878   1993 VAGIFARVLGL---ERVGVDDSFFELGGDSLAAMRVIAAINTTLNADLPVRALLHASSTRGLSQLLGR 2057
Cdd:smart00823   17 VREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
 473-622 1.66e-03

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 43.81  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  473 AWLVQRGAAPGDVLVFTDDDTDKTIDLLIACHLAG---CGYSVCDTADEISVRTNAItEH-----GDGILVT---VVDVA 541
Cdd:cd05906    54 AGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGfvpAPLTVPPTYDEPNARLRKL-RHiwqllGSPVVLTdaeLVAEF 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  542 ATQLAVVGHDELRKVVDERVTQVTHDALLATKT----AYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVL 617
Cdd:cd05906   133 AGLETLSGLPGIRVLSIEELLDTAADHDLPQSRpddlALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFL 212


                  ....*
gi 489495878  618 QCAPL 622
Cdd:cd05906   213 NWVPL 217
 
Name Accession Description Interval E-value
PRK12467 PRK12467
peptide synthase; Provisional
 575-2027 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 994.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  575 AYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARLVRSAAMKTGDLAA 654
Cdd:PRK12467  659 AYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEA 738

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  655 LVDDLVARETTIVDLPTAVWQLLCADGDAIdaiGRSRLRQIVIGGEAIRCSAVDKWLEsaASQGISLLSSYGPTEATVVA 734
Cdd:PRK12467  739 FAALMADQGVTVLKIVPSHLQALLQASRVA---LPRPQRALVCGGEALQVDLLARVRA--LGPGARLINHYGPTETTVGV 813

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  735 TFLPivCDQTTMDGALLRLGRPILPNTVFL-----------AFGEVVIVGDLVADGYLGIDG--------DGFGtvtaAD 795
Cdd:PRK12467  814 STYE--LSDEERDFGNVPIGQPLANLGLYIldhylnpvpvgVVGELYIGGAGLARGYHRRPAltaerfvpDPFG----AD 887

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  796 GSRrrAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAVELHSGS----LGVWFKSQRTRE 871
Cdd:PRK12467  888 GGR--LYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDaglqLVAYLVPAAVAD 965

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  872 GEQDAAAATRIRLVLVSL----GVSSFFVVgVPNIPRKPNGKIDSDNLPRLPQWSAAGLNTAETGQRAAGLSQIWSRQLG 947
Cdd:PRK12467  966 GAEHQATRDELKAQLRQVlpdyMVPAHLLL-LDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTELEKRLAAIWADVLK 1044

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  948 -RAIGPDSSLLGEGIGSLDLIRILPETRRYLGWRLSLLDLIGADTAANLADyAPTPDAPTgedRFRPLVAAQRPAAIPLS 1026
Cdd:PRK12467 1045 vERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQ-AVAAQQQG---AQPALPDVDRDQPLPLS 1120

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1027 FAQRRLWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVDGVPRQLVIEARRADLGCDIVDA 1106
Cdd:PRK12467 1121 YAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLTLEEPLLLA 1200

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1107 TAWPADRLQRAIEEAARHSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYASRCAGRAPDWAP 1186
Cdd:PRK12467 1201 ADKDEAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPA 1280

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1187 LPVQYVDYTLWQREILGDLDDsdspiAAQLAYWENALAGMPERLRLPTARPYPPVADQRGASLVVDWPASVQQQVRRIAR 1266
Cdd:PRK12467 1281 LPIQYADYAVWQRQWMDAGER-----ARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALAR 1355

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1267 QHNATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGRSDPALDNLVGFFVNTLVLRVNLAGDPSFAELLGQVRARSLAAYE 1346
Cdd:PRK12467 1356 REGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQA 1435

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1347 NQDVPFEVLVDRLKPTRALTHHPLIQVMLAWQ-DNPVGQLNLGDLQATPMPIDTRTARMDLVFSLAErfsegsEPAGIGG 1425
Cdd:PRK12467 1436 HQDLPFEQLVEALQPERSLSHSPLFQVMFNHQrDDHQAQAQLPGLSVESLSWESQTAQFDLTLDTYE------SSEGLQA 1509

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1426 AVEYRTDVFEAQAIDVLIERLRKVLVAVAAAPERTVSSIDALDGTERARLDEWGNRAvlTAPAPTPVSIPQMLAAQVARI 1505
Cdd:PRK12467 1510 SLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNAT--HTGYPLARLVHQLIEDQAAAT 1587

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1506 PEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFML 1585
Cdd:PRK12467 1588 PEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMI 1667

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1586 GDAVPVAAVTTAGLRSRL-AGHDLPIIdVVDA----LAAYPGTPPPM-PAAVNLAYILYTSGTTGEPKGVGITHRNVTRL 1659
Cdd:PRK12467 1668 EDSGIELLLTQSHLQARLpLPDGLRSL-VLDQeddwLEGYSDSNPAVnLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNR 1746

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1660 FASLPAR--LSAAQVWSQCHSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAEHVSVLTQTPAAVAMLpTQ 1737
Cdd:PRK12467 1747 LCATQEAyqLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQL-LQ 1825

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1738 GLESVA-------LVVAGEACPAALVDRW---APGRVMLNAYGPTETTICAA---ISAPLRPGSGMPPIGVPVSGAALFV 1804
Cdd:PRK12467 1826 MDEQVEhplslrrVVCGGEALEVEALRPWlerLPDTGLFNLYGPTETAVDVThwtCRRKDLEGRDSVPIGQPIANLSTYI 1905

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1805 LDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFGGSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGY 1884
Cdd:PRK12467 1906 LDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGF 1985

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1885 RIELGEVATALAELAGVGQAVVIAREDRPGdKRLVGYATEIAPGAVDPAG--------LRAQLAQRLPGYLVPAAVVVID 1956
Cdd:PRK12467 1986 RIELGEIEARLREQGGVREAVVIAQDGANG-KQLVAYVVPTDPGLVDDDEaqvalraiLKNHLKASLPEYMVPAHLVFLA 2064

                        1450      1460      1470      1480      1490      1500      1510
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489495878 1957 ALPLTVNGKLDHRALPAPEYGD-TNGYRAPAGPVEKTVAGIFARVLGLERVGVDDSFFELGGDSLAAMRVIA 2027
Cdd:PRK12467 2065 RMPLTPNGKLDRKALPAPDASElQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVS 2136
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 1006-2210 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 975.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1006 TGEDRFRPLVAAQRPAAIPLSFAQRRLWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVDG 1085
Cdd:COG1020     1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1086 VPRQLVIEARRADLG--CDIVDATAWPADRLQRAIEEAARHSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVA 1163
Cdd:COG1020    81 RPVQVIQPVVAAPLPvvVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1164 PLTADLSAAYASRCAGRAPDWAPLPVQYVDYTLWQREilgdlDDSDSPIAAQLAYWENALAGMPERLRLPTARPYPPVAD 1243
Cdd:COG1020   161 LLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQRE-----WLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQS 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1244 QRGASLVVDWPASVQQQVRRIARQHNATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGRSDPALDNLVGFFVNTLVLRVN 1323
Cdd:COG1020   236 YRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVD 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1324 LAGDPSFAELLGQVRARSLAAYENQDVPFEVLVDRLKPTRALTHHPLIQVMLAWQDNPVGQLNLGDLQATPMPIDTRTAR 1403
Cdd:COG1020   316 LSGDPSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAK 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1404 MDLVFSLAERfsegsePAGIGGAVEYRTDVFEAQAIDVLIERLRKVLVAVAAAPERTVSSIDALDGTERARLDEWGNRAv 1483
Cdd:COG1020   396 FDLTLTVVET------GDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNAT- 468

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1484 lTAPAPTPVSIPQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVL 1563
Cdd:COG1020   469 -AAPYPADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVL 547

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1564 KTGAAYLPIDPANPPPRVAFMLGDAVPVAAVTTAGLRSRLAGHDLPIIDV-VDALAAYPGTPPPMPAAV-NLAYILYTSG 1641
Cdd:COG1020   548 KAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVPVLALdALALAAEPATNPPVPVTPdDLAYVIYTSG 627

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1642 TTGEPKGVGITHRNVTRLFASLPAR--LSAAQVWSQCHSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAE 1719
Cdd:COG1020   628 STGRPKGVMVEHRALVNLLAWMQRRygLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARH 707

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1720 HVSVLTQTPAAVAMLPTQGLESVA----LVVAGEACPAALVDRWA---PGRVMLNAYGPTETTICAAIS--APLRPGSGM 1790
Cdd:COG1020   708 RVTVLNLTPSLLRALLDAAPEALPslrlVLVGGEALPPELVRRWRarlPGARLVNLYGPTETTVDSTYYevTPPDADGGS 787

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1791 PPIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFGGSGARMYRTGDLVCWRADGQLE 1870
Cdd:COG1020   788 VPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGARLYRTGDLARWLPDGNLE 867

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1871 FLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATEIAPGAVDPAGLRAQLAQRLPGYLVPA 1950
Cdd:COG1020   868 FLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPA 947

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1951 AVVVIDALPLTVNGKLDHRALPAPEYGDTNGYRAPAGPVEKTVAGIFARVLGLERVGVDDSFFELGGDSLAAMRVIAAIN 2030
Cdd:COG1020   948 AVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAA 1027

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2031 TTLNADLPVRALLHASSTRGLSQLLGRDARPTSDPRLVSVHGDNPTEVHASDLTLDRFIDADTLATAVNLPGPSPELRTV 2110
Cdd:COG1020  1028 RLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLL 1107

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2111 LLTGATGFLGRYLVLELLRRLDVDGRLICLVRAESDEDARRRLEKTFDSGDPELLRHFKELAADRLEVVAGDKSEPDLGL 2190
Cdd:COG1020  1108 LLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLL 1187

                        1210      1220
                  ....*....|....*....|
gi 489495878 2191 DQPMWRRLAETVDLIVDSAA 2210
Cdd:COG1020  1188 LLLLLLLLLLLLLLLLLLLL 1207
PRK12467 PRK12467
peptide synthase; Provisional
 1020-2075 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 851.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1020 PAAIPLSFAQRRLWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVDGVPRQLVIEARRADL 1099
Cdd:PRK12467   47 FERIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTI 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1100 GCDIVDATAwPADR---LQRAIEEAARHSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYASR 1176
Cdd:PRK12467  127 PLDDLANEQ-GRAResqIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAY 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1177 CAGRAPDWAPLPVQYVDYTLWQREILgdlddSDSPIAAQLAYWENALAGMPERLRLPTARPYPPVADQRGASLVVDWPAS 1256
Cdd:PRK12467  206 SQGREPSLPALPIQYADYAIWQRSWL-----EAGERERQLAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQA 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1257 VQQQVRRIARQHNATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGRSDPALDNLVGFFVNTLVLRVNLAGDPSFAELLGQ 1336
Cdd:PRK12467  281 LSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQ 360

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1337 VRARSLAAYENQDVPFEVLVDRLKPTRALTHHPLIQVMLAWQDNPVGQLN-----LGDLQATPMPIDTRTARMDLVFSLA 1411
Cdd:PRK12467  361 VKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQNTATGGRDregaqLPGLTVEELSWARHTAQFDLALDTY 440

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1412 ErfsegsEPAGIGGAVEYRTDVFEAQAIDVLIERLRKVLVAVAAAPERTVSSIDALDGTERARLDEWGNravLTAPAPTP 1491
Cdd:PRK12467  441 E------SAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWN---APATEYAP 511

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1492 VSIPQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLP 1571
Cdd:PRK12467  512 DCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVP 591

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1572 IDPANPPPRVAFMLGDAVPVAAVTTAGLRSRLAGHD----LPIIDVVDALAAYPGTPPPMPAAV-NLAYILYTSGTTGEP 1646
Cdd:PRK12467  592 LDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVPAglrsLCLDEPADLLCGYSGHNPEVALDPdNLAYVIYTSGSTGQP 671

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1647 KGVGITHRNVTRLFASLPAR--LSAAQVWSQCHSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAEHVSVL 1724
Cdd:PRK12467  672 KGVAISHGALANYVCVIAERlqLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVL 751

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1725 TQTPAAVAML-----PTQGLESVALVVAGEACPAALVDRW---APGRVMLNAYGPTETTICAA---ISAPLRPgSGMPPI 1793
Cdd:PRK12467  752 KIVPSHLQALlqasrVALPRPQRALVCGGEALQVDLLARVralGPGARLINHYGPTETTVGVStyeLSDEERD-FGNVPI 830

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1794 GVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFGGSGARMYRTGDLVCWRADGQLEFLG 1873
Cdd:PRK12467  831 GQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGADGGRLYRTGDLARYRADGVIEYLG 910

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1874 RTDDQVKIRGYRIELGEVATALAELAGVGQAVVIArEDRPGDKRLVGY-----ATEIAPGAVDPAGLRAQLAQRLPGYLV 1948
Cdd:PRK12467  911 RMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLA-QPGDAGLQLVAYlvpaaVADGAEHQATRDELKAQLRQVLPDYMV 989

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1949 PAAVVVIDALPLTVNGKLDHRALPAPE-YGDTNGYRAPAGPVEKTVAGIFARVLGLERVGVDDSFFELGGDSLAAMRVIA 2027
Cdd:PRK12467  990 PAHLLLLDSLPLTPNGKLDRKALPKPDaSAVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVIS 1069

                        1050      1060      1070      1080
                  ....*....|....*....|....*....|....*....|....*...
gi 489495878 2028 AINTTLNADLPVRALLHASSTRGLSQLLGRDArPTSDPRLVSVHGDNP 2075
Cdd:PRK12467 1070 RVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQ-QGAQPALPDVDRDQP 1116
carboxyl_red NF041592
carboxylic acid reductase;
1519-2512 0e+00

carboxylic acid reductase;


Pssm-ID: 469476 [Multi-domain]  Cd Length: 1161  Bit Score: 835.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1519 TYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPP-----------PRV----AF 1583
Cdd:NF041592   79 TYRELWDRVGAVAAALAGDPVRPGDRVAVLGFTSVDYTTIDLALIRLGAVAVPLQTSAPVaqlrpivaetePRVlaasVD 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1584 MLGDAVPVAAVTT---------------------AGLRSRLAGHDL----PIIDVVDALAAYPGTPPPMPAAVN-LAYIL 1637
Cdd:NF041592  159 LLDDAVELVLTGPaprrlvvfdyhpevddhrealEAARARLADAGPvvveTLAEVLERGRALPAAPPPASDDDDpLALLI 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1638 YTSGTTGEPKGVGITHRNVTRLFaslpaRLSAAQVWSQC-------------HSYGFDAsaweIWGALLGGGRLVIVPES 1704
Cdd:NF041592  239 YTSGSTGAPKGAMYTERLVANMW-----RGSARAGWGPRavpsitlnfmpmsHVMGRGT----LYGTLARGGTAYFAARS 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1705 vaaspnDFHGLLvaEHVSVLTQT-----PAAVAML--------PTQGLESVALVVAGEACPAALVDRWAPGRVMlnaygp 1771
Cdd:NF041592  310 ------DLSTLL--EDLALVRPTelnfvPRVWDMLfqeyqselDRRAADGADRAAAEAAVKAELREDLLGGRFV------ 375

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1772 TETTICAAISAPLRPGS----GMPPI---GVPVSGAALF--------VLDSWL------------RPVPAGvagELYIAG 1824
Cdd:NF041592  376 SAMTGSAPISAEMKAFVesllDLHLHdgyGSTEAGGVFIdgrvrrppVLDYKLvdvpelgyfgtdRPHPRG---ELLVKT 452

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1825 AGVGVGYWRRAGLTASRFVACPFggsgarmYRTGDLVCWRADGQLEFLGRTDDQVKI-RGYRIELGEVATALAELAGVGQ 1903
Cdd:NF041592  453 TTMFPGYYKRPEVTAEVFDEDGF-------YRTGDIVAELGPDQLVYVDRRNNVLKLsQGEFVTVSKLEAVFGDSPLVRQ 525

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1904 AVVIAREDRPGDKRLVGYATEIAPGAVDPAGLRAQLAQ---------RLPGYLVPAAVVvIDALPLTV-NGKL-DHRALP 1972
Cdd:NF041592  526 IYVYGNSARAYLLAVVVPTEEALARHGDAAELKALIAEslqrvareaGLQSYEIPRDFL-IETTPFTLeNGLLtGIRKLA 604

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1973 APE----YGD-------------TNGYRA-----PAGPVEKTVAGIFARVLGLERVGV--DDSFFELGGDSLAAMRVIAA 2028
Cdd:NF041592  605 RPKlkerYGErleqlytelaagqADELRAlrrsgADRPVLETVGRAAAALLGAAAADLrpDAHFTDLGGDSLSALTFSNL 684

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2029 INTTLNADLPVRALLH-ASSTRGL-----SQLLGRDARPTSDprlvSVHGDNPTEVHASDLTLDRFIDADTLATAVNLPG 2102
Cdd:NF041592  685 LHEIFGVEVPVGVIVSpATDLRALadyieAERASGAKRPTFA----SVHGRDATEVRAADLTLDKFIDAATLAAAPSLPG 760

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2103 PSPELRTVLLTGATGFLGRYLVLELLRRLD-VDGRLICLVRAESDEDARRRLEKTFDSGDPELLRHFKELAADRLEVVAG 2181
Cdd:NF041592  761 PSGEVRTVLLTGATGFLGRYLALEWLERLAlVGGTLICLVRAKDDAAARARLDATFDSGDPELLAHYRELAADHLEVLAG 840

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2182 DKSEPDLGLDQPMWRRLAETVDLIVDSAAMVN-AFPYHELFGPNVAGTAELIRIALTTKLKPFTYVSTADVGAAIEPSAF 2260
Cdd:NF041592  841 DKGEPDLGLDRATWQRLADTVDLIVDPAALVNhVLPYSQLFGPNVVGTAELIRLALTTRLKPFTYLSTIGVGAQIEPGAF 920

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2261 TEDADIRVISPTRTVDGGWAGGYGTSKWAGEVLLREANDLCALPVAVFRCGMILADTSYAGQLNMSDWVTRMVLSLMATG 2340
Cdd:NF041592  921 TEDADIREISPVRAIDDSYANGYGNSKWAGEVLLREAHDLCGLPVAVFRCDMILADTRYAGQLNLPDMFTRLMLSLVATG 1000

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2341 IAPRSFYEPDSEGNRQRAHFDGLPVTFVAEAIAVLGARVAgsslAGFATYHVMNPHDDGIGLDEYVDWLIEAGYPIRRID 2420
Cdd:NF041592 1001 IAPGSFYELDADGNRQRAHYDGLPVDFIAEAIATLGARVT----DGFETYHVMNPHDDGIGLDEFVDWLIEAGHPIQRID 1076

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2421 DFAEWLQRFEASLGALPDRQRRHSVLPMLLASNsqrlQPLKPTRGCSAPTDRFRAAVRAAKVGSDKdnpDIPHVSAPTII 2500
Cdd:NF041592 1077 DYADWLQRFETALRALPERQRQASLLPLLHNYR----RPAPPIRGSIAPTDRFRAAVQEAKIGPDK---DIPHLTPALIV 1149

                        1130
                  ....*....|..
gi 489495878 2501 NYVTNLQLLGLL 2512
Cdd:NF041592 1150 KYVTDLRLLGLL 1161
PRK12316 PRK12316
peptide synthase; Provisional
 372-2027 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 821.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  372 SVLDEEQRTLNLAIWNRADLPAcKTHPKVAERIAAALesmaamwdrpiamivndwfgigpdgtrcqgdwpARQPSTPAWF 451
Cdd:PRK12316 1978 ALLDAGERQRILADWDRTPEAY-PRGPGVHQRIAEQA---------------------------------ARAPEAIAVV 2023

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  452 LDSARGVHQFLGRR--RFVYPwvawLVQRGAAPGDVLVFTDDDTDKTIDLLIACHLAGCGYSVCDTADEISVRTNAITEH 529
Cdd:PRK12316 2024 FGDQHLSYAELDSRanRLAHR----LRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDS 2099

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  530 GDGILVTVVDVAA--------TQLAVVGHDELRKVVDERVTQVTHDALLAtktaYIMPTSGTTGQPKLVRISHGSLAVFC 601
Cdd:PRK12316 2100 GAALLLTQRHLLErlplpagvARLPLDRDAEWADYPDTAPAVQLAGENLA----YVIYTSGSTGLPKGVAVSHGALVAHC 2175

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  602 DAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGAR-LVRSAAMKTGDlaALVDDLVARETTIVDLPTAVWQLLcAD 680
Cdd:PRK12316 2176 QAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARvLIRDDELWDPE--QLYDEMERHGVTILDFPPVYLQQL-AE 2252

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  681 GDAIDAiGRSRLRQIVIGGEAIRCSAVDKWLESAasQGISLLSSYGPTEATVVATfLPIVCDQTTMDGALLRLGRPILPN 760
Cdd:PRK12316 2253 HAERDG-RPPAVRVYCFGGEAVPAASLRLAWEAL--RPVYLFNGYGPTEAVVTPL-LWKCRPQDPCGAAYVPIGRALGNR 2328

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  761 TVFL-----------AFGEVVIVGDLVADGYLGIDG--------DGFGTVTAadgsrrRAFATGDRVTVDAEGFPVFSGR 821
Cdd:PRK12316 2329 RAYIldadlnllapgMAGELYLGGEGLARGYLNRPGltaerfvpDPFSASGE------RLYRTGDLARYRADGVVEYLGR 2402

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  822 KDAVVKISGKRVDIAEVTRRIAEDPAVSDVAVELHSGSLG---VWFKSQRTREGEQDAAAATRIRLVLVSLGVSSFFVVg 898
Cdd:PRK12316 2403 IDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGkqlVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVV- 2481

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  899 VPNIPRKPNGKIDSDNLPRLPQWSAAGLNTAETGQRAAGLSQIWSRQLG-RAIGPDSSLLGEGIGSLDLIRILPETRRYL 977
Cdd:PRK12316 2482 LERLPLNPNGKLDRKALPKPDVSQLRQAYVAPQEGLEQRLAAIWQAVLKvEQVGLDDHFFELGGHSLLATQVVSRVRQDL 2561

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  978 GWRLSLLDLIGADTAANLADYAPTPDAPtgedRFRPLVAAQRPAAIPLSFAQRRLWFLDQLQRPAPVYNMAVALRLRGYL 1057
Cdd:PRK12316 2562 GLEVPLRILFERPTLAAFAASLESGQTS----RAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVL 2637

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1058 DTEALGAAVADVVGRHESLRTVFPAVDGVPRQlVIEARRAdLGCDIVDATAWPADRLQRAIEEAARHSFDLATEIPLRTW 1137
Cdd:PRK12316 2638 DQAALEQAFDALVLRHETLRTRFVEVGEQTRQ-VILPNMS-LRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVR 2715

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1138 LFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYASRCAGRAPDWAPLPVQYVDYTLWQREILgdlddSDSPIAAQLA 1217
Cdd:PRK12316 2716 LLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYADYAAWQRAWM-----DSGEGARQLD 2790

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1218 YWENALAGMPERLRLPTARPYPPVADQRGASLVVDWPASVQQQVRRIARQHNATSFMVVAAGLAVLLSKLSGSPDVAVGF 1297
Cdd:PRK12316 2791 YWRERLGGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGV 2870

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1298 PIAGRSDPALDNLVGFFVNTLVLRVNLAGDPSFAELLGQVRARSLAAYENQDVPFEVLVDRLKPTRALTHHPLIQVMLAW 1377
Cdd:PRK12316 2871 PIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNH 2950

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1378 QDNPVGQLNLGDLQATPMPIDTRTARMDLVFSLAErfsegsEPAGIGGAVEYRTDVFEAQAIDVLIERLRKVLVAVAAAP 1457
Cdd:PRK12316 2951 QSGERAAAQLPGLHIESFAWDGAATQFDLALDTWE------SAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENP 3024

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1458 ERTVSSIDALDGTERARLDEWGNRAvlTAPAPTPVSIPQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGC 1537
Cdd:PRK12316 3025 QRSVDELAMLDAEERGQLLEAWNAT--AAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIER 3102

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1538 GAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVTTAGLRSRLAGHDLPIIDVVDAL 1617
Cdd:PRK12316 3103 GVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDE 3182

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1618 AAYPGTPPPMPAAVNLAYILYTSGTTGEPKGVGITHRNVTRLFASLPA--RLSAAQVWSQCHSYGFDASAWEIWGALLGG 1695
Cdd:PRK12316 3183 NYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQayGLGVGDRVLQFTTFSFDVFVEELFWPLMSG 3262

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1696 GRLVIVPESVAASPNDFHGLLVAEHVSVLTQTPAAVAML----PTQGLESVALVVA-GEACPAALVDRWAPGRVMLNAYG 1770
Cdd:PRK12316 3263 ARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFleeeDAHRCTSLKRIVCgGEALPADLQQQVFAGLPLYNLYG 3342

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1771 PTETTICAAISAPLRPGSGMPPIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFgGS 1850
Cdd:PRK12316 3343 PTEATITVTHWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPF-VP 3421

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1851 GARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRpgdkRLVGYATEIAPGAV 1930
Cdd:PRK12316 3422 GERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGR----QLVAYVVPEDEAGD 3497

                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1931 DPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRALPAPEYGDT-NGYRAPAGPVEKTVAGIFARVLGLERVGVD 2009
Cdd:PRK12316 3498 LREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLqQDYVAPVNELERRLAAIWADVLKLEQVGLT 3577

                        1690
                  ....*....|....*...
gi 489495878 2010 DSFFELGGDSLAAMRVIA 2027
Cdd:PRK12316 3578 DNFFELGGDSIISLQVVS 3595
PRK12316 PRK12316
peptide synthase; Provisional
 1013-2027 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 789.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1013 PLVAAQRPAA-IPLSFAQRRLWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVDGVPRQLV 1091
Cdd:PRK12316   39 PIPAGVSSAErDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQV 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1092 IEARraDLGCDIVDATAWP-ADRLQRAIEEAARHS---FDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTA 1167
Cdd:PRK12316  119 PLDR--PLEVEFEDCSGLPeAEQEARLRDEAQRESlqpFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIE 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1168 DLSAAYASRCAGRAPDWAPLPVQYVDYTLWQREILgdlddSDSPIAAQLAYWENALAGMPERLRLPTARPYPPVADQRGA 1247
Cdd:PRK12316  197 EFSRFYSAYATGAEPGLPALPIQYADYALWQRSWL-----EAGEQERQLEYWRAQLGEEHPVLELPTDHPRPAVPSYRGS 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1248 SLVVDWPASVQQQVRRIARQHNATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGRSDPALDNLVGFFVNTLVLRVNLAGD 1327
Cdd:PRK12316  272 RYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGR 351

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1328 PSFAELLGQVRARSLAAYENQDVPFEVLVDRLKPTRALTHHPLIQVMLAWQDNPVGQ---LNLGDLQATPMPIDTRTARM 1404
Cdd:PRK12316  352 TRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYNHQPLVADIealDTVAGLEFGQLEWKSRTTQF 431

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1405 DLVFSLAERfsegsePAGIGGAVEYRTDVFEAQAIDVLIERLRKVLVAVAAAPERTVSSIDALDGTERARLDEWGNRAvl 1484
Cdd:PRK12316  432 DLTLDTYEK------GGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNAT-- 503

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1485 TAPAPTPVSIPQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLK 1564
Cdd:PRK12316  504 AAEYPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILK 583

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1565 TGAAYLPIDPANPPPRVAFMLGDAVPVAAVTTAGLRSRL---AGHDLPIIDVVDA-LAAYPGTPPPMPA-AVNLAYILYT 1639
Cdd:PRK12316  584 AGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLplaAGVQVLDLDRPAAwLEGYSEENPGTELnPENLAYVIYT 663

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1640 SGTTGEPKGVGITHRN-VTRLFASLPA-RLSAAQVWSQCHSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLV 1717
Cdd:PRK12316  664 SGSTGKPKGAGNRHRAlSNRLCWMQQAyGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELIN 743

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1718 AEHVSVLTQTPAAV-AMLPTQGLESVA----LVVAGEACPAALVDRW---APGRVMLNAYGPTETTICAAISAPLRPGSG 1789
Cdd:PRK12316  744 REGVDTLHFVPSMLqAFLQDEDVASCTslrrIVCSGEALPADAQEQVfakLPQAGLYNLYGPTEAAIDVTHWTCVEEGGD 823

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1790 MPPIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFgGSGARMYRTGDLVCWRADGQL 1869
Cdd:PRK12316  824 SVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPF-VAGERMYRTGDLARYRADGVI 902

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1870 EFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREdrpgDKRLVGYATEIAPGAVDPAGLRAQLAQRLPGYLVP 1949
Cdd:PRK12316  903 EYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVLESEGGDWREALKAHLAASLPEYMVP 978

                         970       980       990      1000      1010      1020      1030
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489495878 1950 AAVVVIDALPLTVNGKLDHRALPAPEYGDTN-GYRAPAGPVEKTVAGIFARVLGLERVGVDDSFFELGGDSLAAMRVIA 2027
Cdd:PRK12316  979 AQWLALERLPLTPNGKLDRKALPAPEASVAQqGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVS 1057
PRK05691 PRK05691
peptide synthase; Validated
 575-2027 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 769.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  575 AYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARLVRSAAMKTGDLAA 654
Cdd:PRK05691 1276 AYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQR 1355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  655 LVDDLVARETTIVDLPTAVWQLLCadgDAIDAIGRSRLRQIVIGGEAIRCSAVDKWLESAAsqGISLLSSYGPTEATVVA 734
Cdd:PRK05691 1356 IAELVQQYGVTTLHFVPPLLQLFI---DEPLAAACTSLRRLFSGGEALPAELRNRVLQRLP--QVQLHNRYGPTETAINV 1430

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  735 TFLPIVCDqttmDGALLRLGRPiLPNTVFLAF------------GEVVIVGDLVADGYLGIDG--------DGFGTVTAa 794
Cdd:PRK05691 1431 THWQCQAE----DGERSPIGRP-LGNVLCRVLdaelnllppgvaGELCIGGAGLARGYLGRPAltaerfvpDPLGEDGA- 1504

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  795 dgsrrRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAVELHSGSLGVWFKSQRTREGEQ 874
Cdd:PRK05691 1505 -----RLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEAGQ 1579

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  875 DAAAAtRIRLVLvSLGVSSFFV----VGVPNIPRKPNGKIDSDNLPrLPQWSAaGLNTAETGQRAAGLSQIWSRQLG-RA 949
Cdd:PRK05691 1580 EAEAE-RLKAAL-AAELPEYMVpaqlIRLDQMPLGPSGKLDRRALP-EPVWQQ-REHVEPRTELQQQIAAIWREVLGlPR 1655

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  950 IGPDSSLLGEGIGSLDLIRILPETRRYLGWRLSLLDLIGADTAANLADYAPTPDAPTGEDRFRPLVAAQRPAAIPLSFAQ 1029
Cdd:PRK05691 1656 VGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQVARIQAAGERNSQGAIARVDRSQPVPLSYSQ 1735

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1030 RRLWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVDGVPRQLVieARRADLGCDIVDATAW 1109
Cdd:PRK05691 1736 QRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQV--AEDSGLRMDWQDFSAL 1813

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1110 PAD----RLQRAIEEAARHSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYASRCAGRAPDWA 1185
Cdd:PRK05691 1814 PADarqqRLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDRESPLE 1893

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1186 PLPVQYVDYTLWQREILgdlddSDSPIAAQLAYWENALAGMPERLRLPTARPYPPVADQRGASLVVDWPASVQQQVRRIA 1265
Cdd:PRK05691 1894 PLPVQYLDYSVWQRQWL-----ESGERQRQLDYWKAQLGNEHPLLELPADRPRPPVQSHRGELYRFDLSPELAARVRAFN 1968

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1266 RQHNATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGRSDPALDNLVGFFVNTLVLRVNLAGDPSFAELLGQVRARSLAAY 1345
Cdd:PRK05691 1969 AQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQ 2048

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1346 ENQDVPFEVLVDRLKPTRALTHHPLIQVMLAWQDNPVGQL-NLGDLQATPMPIDTRTARMDL---VFSLAERfsegsepa 1421
Cdd:PRK05691 2049 SHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEFQQSrQLAGMTVEYLVNDARATKFDLnleVTDLDGR-------- 2120

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1422 gIGGAVEYRTDVFEAQAIDVLIERLRKVLVAVAAAPERTVSSIDALDGTERARLdeWGNRAVLTAPAPTPVSIPQMLAAQ 1501
Cdd:PRK05691 2121 -LGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQL--LDSLAGEAGEARLDQTLHGLFAAQ 2197

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1502 VARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRV 1581
Cdd:PRK05691 2198 AARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERL 2277

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1582 AFMLGDAVPVAAVTTAGLRSRLAghDLP-------IIDVVDALAAYPGTPPP-MPAAVNLAYILYTSGTTGEPKGVGITH 1653
Cdd:PRK05691 2278 HYMIEDSGIGLLLSDRALFEALG--ELPagvarwcLEDDAAALAAYSDAPLPfLSLPQHQAYLIYTSGSTGKPKGVVVSH 2355

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1654 RNVTRLFASLPARLSAAQVWSQCHSYG--FDASAWEIWGALLGGGRLVIVPESVAASpNDFHGLLVAEHVSVLTQTPAAV 1731
Cdd:PRK05691 2356 GEIAMHCQAVIERFGMRADDCELHFYSinFDAASERLLVPLLCGARVVLRAQGQWGA-EEICQLIREQQVSILGFTPSYG 2434

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1732 AMLP----TQGLE-SVALVV-AGEACPAALVDR----WAPgRVMLNAYGPTETTICA-AISAP--LRPGSGMPPIGVPVS 1798
Cdd:PRK05691 2435 SQLAqwlaGQGEQlPVRMCItGGEALTGEHLQRirqaFAP-QLFFNAYGPTETVVMPlACLAPeqLEEGAASVPIGRVVG 2513

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1799 GAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFGGSGARMYRTGDLVCWRADGQLEFLGRTDDQ 1878
Cdd:PRK05691 2514 ARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAADGGRLYRTGDLVRLRADGLVEYVGRIDHQ 2593

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1879 VKIRGYRIELGEVATALAELAGVGQAVVIAReDRPGDKRLVGY-ATEIAPG-----AVDPAGLRAQLAQRLPGYLVPAAV 1952
Cdd:PRK05691 2594 VKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYlVSAVAGQddeaqAALREALKAHLKQQLPDYMVPAHL 2672

                        1450      1460      1470      1480      1490      1500      1510
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489495878 1953 VVIDALPLTVNGKLDHRALPAPEYG-DTNGYRAPAGPVEKTVAGIFARVLGLERVGVDDSFFELGGDSLAAMRVIA 2027
Cdd:PRK05691 2673 ILLDSLPLTANGKLDRRALPAPDPElNRQAYQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVS 2748
PRK05691 PRK05691
peptide synthase; Validated
 568-2057 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 730.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  568 ALLATKTAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYG--WGAHDTVLQCAPLTSDISV-----EEIFGGAACgar 640
Cdd:PRK05691  162 ALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGLiggllQPIFSGVPC--- 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  641 LVRSAAMKTGDLAALVDDLVARETTIVDLPTAVWQLlCADGDAIDAIGR---SRLRQIVIGGEAIRCSAVDKWLESAASQ 717
Cdd:PRK05691  239 VLMSPAYFLERPLRWLEAISEYGGTISGGPDFAYRL-CSERVSESALERldlSRWRVAYSGSEPIRQDSLERFAEKFAAC 317

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  718 GI---SLLSSYGPTEATVVATF---------------------------LPIVCDQTTMDGALLRLGRP----ILPNTVF 763
Cdd:PRK05691  318 GFdpdSFFASYGLAEATLFVSGgrrgqgipaleldaealarnraepgtgSVLMSCGRSQPGHAVLIVDPqsleVLGDNRV 397

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  764 lafGEVVIVGDLVADGYLGIDGDGFGTVTAADGsrRRAFATGDrVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIA 843
Cdd:PRK05691  398 ---GEIWASGPSIAHGYWRNPEASAKTFVEHDG--RTWLRTGD-LGFLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVE 471

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  844 EDPA------VSDVAVElHSGSLGVWFKSQRTREGEQDAAAAT---RIRLVLVSLGVSSFFVVGVPN---IPRKPNGKID 911
Cdd:PRK05691  472 REVEvvrkgrVAAFAVN-HQGEEGIGIAAEISRSVQKILPPQAlikSIRQAVAEACQEAPSVVLLLNpgaLPKTSSGKLQ 550

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  912 S------------DNLPRLPQWSAAGLNTAETG--QRAAGLSQIWSRQLG-RAIGPDSSLLGEGIGSLDLIRILPETRRY 976
Cdd:PRK05691  551 RsacrlrladgslDSYALFPALQAVEAAQTAASgdELQARIAAIWCEQLKvEQVAADDHFFLLGGNSIAATQVVARLRDE 630

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  977 LGWRLSL--------LDLIGADTAANLADYAPTPDAptgedrfrpLVAAQRPAAIPLSFAQRRLWFLDQLQRPAPVYNMA 1048
Cdd:PRK05691  631 LGIDLNLrqlfeaptLAAFSAAVARQLAGGGAAQAA---------IARLPRGQALPQSLAQNRLWLLWQLDPQSAAYNIP 701

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1049 VALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVDGVPRQLVIEArrADLGCDIVDATAWPAD----RLQRAIEEAARH 1124
Cdd:PRK05691  702 GGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQ--GEFALQRIDLSDLPEAereaRAAQIREEEARQ 779

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1125 SFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYASRCAGRAPDWAPLPVQYVDYTLWQREILgd 1204
Cdd:PRK05691  780 PFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGAWQRQWL-- 857

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1205 lddSDSPIAAQLAYWENALAGMPERLRLPTARPYPPVADQRGASLVVDWPASVQQQVRRIARQHNATSFMVVAAGLAVLL 1284
Cdd:PRK05691  858 ---AQGEAARQLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALL 934

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1285 SKLSGSPDVAVGFPIAGRSDPALDNLVGFFVNTLVLRVNLAGDPSFAELLGQVRARSLAAYENQDVPFEVLVDRLKPTRa 1364
Cdd:PRK05691  935 HRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAR- 1013

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1365 ltHHPLIQVMLAWQDNPVGQL-NLGDLQATPMPIDTRTARMDLvfslaERFSEGSEPAGIGGAVEYRTDVFEAQAIDVLI 1443
Cdd:PRK05691 1014 --EQGLFQVMFNHQQRDLSALrRLPGLLAEELPWHSREAKFDL-----QLHSEEDRNGRLTLSFDYAAELFDAATIERLA 1086

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1444 ERLRKVLVAVAAAPERTVSSIDALDGTERARLDEWGnravlTAP-APTPVSIPQMLAAQVARIPEAEAVCCGDASMTYRE 1522
Cdd:PRK05691 1087 EHFLALLEQVCEDPQRALGDVQLLDAAERAQLAQWG-----QAPcAPAQAWLPELLNEQARQTPERIALVWDGGSLDYAE 1161

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1523 LDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVTTAGLRSR 1602
Cdd:PRK05691 1162 LHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLER 1241

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1603 LAGHDLPIIDVVDAL--AAYPGTPPPMP-AAVNLAYILYTSGTTGEPKGVGITHRNVTRLFASLPA--RLSAAQVWSQCH 1677
Cdd:PRK05691 1242 LPQAEGVSAIALDSLhlDSWPSQAPGLHlHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQAtyALDDSDVLMQKA 1321

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1678 SYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAEHVSVLTQTPAAVAMLPTQGLESVA-----LVVAGEACP 1752
Cdd:PRK05691 1322 PISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACtslrrLFSGGEALP 1401

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1753 AALVDR---WAPGRVMLNAYGPTETTICAAISAPLRPGSGMPPIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGV 1829
Cdd:PRK05691 1402 AELRNRvlqRLPQVQLHNRYGPTETAINVTHWQCQAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLAR 1481

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1830 GYWRRAGLTASRFVACPFGGSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAR 1909
Cdd:PRK05691 1482 GYLGRPALTAERFVPDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVR 1561

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1910 EDRPGdKRLVGYATEIAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRALPAPEYgDTNGYRAPAGPV 1989
Cdd:PRK05691 1562 EGAAG-AQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVW-QQREHVEPRTEL 1639

                        1530      1540      1550      1560      1570      1580
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489495878 1990 EKTVAGIFARVLGLERVGVDDSFFELGGDSLAAMRVIAAINTTLNADLPVRALLHASSTRGLSQLLGR 2057
Cdd:PRK05691 1640 QQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQVAR 1707
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
 1023-1457 0e+00

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 660.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1023 IPLSFAQRRLWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVDGVPRQLVIEARRADLGCD 1102
Cdd:cd19540     2 IPLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLPAAEARPDLT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1103 IVDATAwpaDRLQRAIEEAARHSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYASRCAGRAP 1182
Cdd:cd19540    82 VVDVTE---DELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRAP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1183 DWAPLPVQYVDYTLWQREILGDLDDSDSPIAAQLAYWENALAGMPERLRLPTARPYPPVADQRGASLVVDWPASVQQQVR 1262
Cdd:cd19540   159 DWAPLPVQYADYALWQRELLGDEDDPDSLAARQLAYWRETLAGLPEELELPTDRPRPAVASYRGGTVEFTIDAELHARLA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1263 RIARQHNATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGRSDPALDNLVGFFVNTLVLRVNLAGDPSFAELLGQVRARSL 1342
Cdd:cd19540   239 ALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDL 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1343 AAYENQDVPFEVLVDRLKPTRALTHHPLIQVMLAWQDNPVGQLNLGDLQATPMPIDTRTARMDLVFSLAERFSEGSEPAG 1422
Cdd:cd19540   319 AAFAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFTLTERRDADGAPAG 398

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 489495878 1423 IGGAVEYRTDVFEAQAIDVLIERLRKVLVAVAAAP 1457
Cdd:cd19540   399 LTGELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 1506-1972 0e+00

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 612.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1506 PEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFML 1585
Cdd:cd17652     1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1586 GDAVPVAAVTTAGlrsrlaghdlpiidvvdalaaypgtpppmpaavNLAYILYTSGTTGEPKGVGITHRNVTRLFASLPA 1665
Cdd:cd17652    81 ADARPALLLTTPD---------------------------------NLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIA 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1666 RLS--AAQVWSQCHSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAEHVSVLTQTPAAVAMLPTQGLES-V 1742
Cdd:cd17652   128 AFDvgPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPDDLPDlR 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1743 ALVVAGEACPAALVDRWAPGRVMLNAYGPTETTICAAISAPLrPGSGMPPIGVPVSGAALFVLDSWLRPVPAGVAGELYI 1822
Cdd:cd17652   208 TLVVAGEACPAELVDRWAPGRRMINAYGPTETTVCATMAGPL-PGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYI 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1823 AGAGVGVGYWRRAGLTASRFVACPFGGSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVG 1902
Cdd:cd17652   287 AGAGLARGYLNRPGLTAERFVADPFGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVA 366

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1903 QAVVIAREDRPGDKRLVGYATEIAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRALP 1972
Cdd:cd17652   367 EAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 1022-1457 3.20e-176

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 546.95  E-value: 3.20e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1022 AIPLSFAQRRLWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVDGVPRQLVIEARRADLgc 1101
Cdd:cd19531     1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPL-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1102 DIVDATAWPAD----RLQRAIEEAARHSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYASRC 1177
Cdd:cd19531    79 PVVDLSGLPEAereaEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1178 AGRAPDWAPLPVQYVDYTLWQREILgdlddSDSPIAAQLAYWENALAGMPERLRLPTARPYPPVADQRGASLVVDWPASV 1257
Cdd:cd19531   159 AGRPSPLPPLPIQYADYAVWQREWL-----QGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAEL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1258 QQQVRRIARQHNATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGRSDPALDNLVGFFVNTLVLRVNLAGDPSFAELLGQV 1337
Cdd:cd19531   234 TAALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARV 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1338 RARSLAAYENQDVPFEVLVDRLKPTRALTHHPLIQVMLAWQDNPVGQLNLGDLQATPMPIDTRTARMDLVFSLAERfseg 1417
Cdd:cd19531   314 RETALEAYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTET---- 389

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 489495878 1418 sePAGIGGAVEYRTDVFEAQAIDVLIERLRKVLVAVAAAP 1457
Cdd:cd19531   390 --DGGLRGSLEYNTDLFDAATIERMAGHFQTLLEAIVADP 427
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
 1023-1457 4.68e-173

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 538.39  E-value: 4.68e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1023 IPLSFAQRRLWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVDGVPRQLVIEARRADLGCD 1102
Cdd:cd19538     2 IPLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEATPKLE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1103 IVDAtawPADRLQRAIEEAARHSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYASRCAGRAP 1182
Cdd:cd19538    82 IKEV---DEEELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1183 DWAPLPVQYVDYTLWQREILGDLDDSDSPIAAQLAYWENALAGMPERLRLPTARPYPPVADQRGASLVVDWPASVQQQVR 1262
Cdd:cd19538   159 ELAPLPVQYADYALWQQELLGDESDPDSLIARQLAYWKKQLAGLPDEIELPTDYPRPAESSYEGGTLTFEIDSELHQQLL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1263 RIARQHNATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGRSDPALDNLVGFFVNTLVLRVNLAGDPSFAELLGQVRARSL 1342
Cdd:cd19538   239 QLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNL 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1343 AAYENQDVPFEVLVDRLKPTRALTHHPLIQVMLAWQDNPVGQLNLGDLQATPMPIDTRTARMDLVFSLAERFSEGSePAG 1422
Cdd:cd19538   319 EAYEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGLEAKLELRTVGSAKFDLTFELREQYNDGT-PNG 397

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 489495878 1423 IGGAVEYRTDVFEAQAIDVLIERLRKVLVAVAAAP 1457
Cdd:cd19538   398 IEGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1021-2076 5.88e-172

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 566.98  E-value: 5.88e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1021 AAIPLSFAQRRLWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVDGVPRQlVIEARRADLG 1100
Cdd:PRK10252    6 QHLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQ-WVDPALTFPL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1101 CDIVD--ATAWPADRLQRAIEEAARHSFDLATEIPL-RTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYASRC 1177
Cdd:PRK10252   85 PEIIDlrTQPDPHAAAQALMQADLQQDLRVDSGKPLvFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1178 AGRAPDWAPLPVQ------YVDY---TLWQREilgdlddsdspiaaqLAYWENALAGMPERLRLPTARPYPPVADQRGAS 1248
Cdd:PRK10252  165 RGEPTPASPFTPFadvveeYQRYrasEAWQRD---------------AAFWAEQRRQLPPPASLSPAPLPGRSASADILR 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1249 LVVDWPASVQQQVRRIARQHNATSfmVVAAGLAVLLSKLSGSPDVAVGFPIAGRSDPALDNLVGFFVNTLVLRVNLAGDP 1328
Cdd:PRK10252  230 LKLEFTDGAFRQLAAQASGVQRPD--LALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQE 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1329 SFAELLGQVRARSLAAYENQDVPFEVLV---DRLKPTRALtHHPLIQVMLAWQdnpvgQLNLGDLQATPMPIDTRTARmD 1405
Cdd:PRK10252  308 TLPELATRLAAQLKKMRRHQRYDAEQIVrdsGRAAGDEPL-FGPVLNIKVFDY-----QLDFPGVQAQTHTLATGPVN-D 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1406 LVFSLAerfseGSEPAGIGGAVEYRTDVFEAQAIDVLIERLRKVLVAVAAAPERTVSSIDALDGTERARLDEWGNRAVlt 1485
Cdd:PRK10252  381 LELALF-----PDEHGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQLAQVNATAV-- 453

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1486 aPAPtPVSIPQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKT 1565
Cdd:PRK10252  454 -EIP-ETTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEA 531

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1566 GAAYLPIDPANPPPRVAFMLGDAVPVAAVTTAGLRSRLAGHDLPIIDVVDALAAYPGTPP-PMPAAVNLAYILYTSGTTG 1644
Cdd:PRK10252  532 GAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLAPQGAAPlQLSQPHHTAYIIFTSGSTG 611

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1645 EPKGVGITHRN-VTRLF---ASLParLSAAQVWSQCHSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAEH 1720
Cdd:PRK10252  612 RPKGVMVGQTAiVNRLLwmqNHYP--LTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYG 689

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1721 VSVLTQTP----AAVAMLPTQGLESVALVVA-----GEACPAALVDRW-----APgrvMLNAYGPTEtticAAISAPLRP 1786
Cdd:PRK10252  690 VTTTHFVPsmlaAFVASLTPEGARQSCASLRqvfcsGEALPADLCREWqqltgAP---LHNLYGPTE----AAVDVSWYP 762

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1787 GSGMP---------PIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFGgSGARMYRT 1857
Cdd:PRK10252  763 AFGEElaavrgssvPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFA-PGERMYRT 841

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1858 GDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAR-----EDRPGD-KRLVGYATEIAPGAVD 1931
Cdd:PRK10252  842 GDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqaAATGGDaRQLVGYLVSQSGLPLD 921

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1932 PAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRALPAPEYGDTNGYRAPAGPVEKTVAGIFARVLGLERVGVDDS 2011
Cdd:PRK10252  922 TSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQVPGRAPKTGTETIIAAAFSSLLGCDVVDADAD 1001

                        1050      1060      1070      1080      1090      1100
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489495878 2012 FFELGGDSLAAMRVIAAINTTLNADLPVRALLHASSTRGLSQLLG----RDARPTSDPRLVSVHGDNPT 2076
Cdd:PRK10252 1002 FFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDaeedESRRLGFGTILPLREGDGPT 1070
PRK12467 PRK12467
peptide synthase; Provisional
 1013-2052 8.72e-172

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 593.68  E-value: 8.72e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1013 PLVAAQRPAAIPLSFAQRRLWFLDQLQRPAPVYNMAVALRLRGyLDTEALGAAVADVVGRHESLRTVFPAVDGVPRQLVI 1092
Cdd:PRK12467 2637 PVAVGDIEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFLWDGELEEPLQV 2715

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1093 EARRADLGCDIVDATAWP--ADRLQRAIEEAARHSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLS 1170
Cdd:PRK12467 2716 VYKQARLPFSRLDWRDRAdlEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVL 2795

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1171 AAYAsrcaGRAPdwAPLPVQYVDYTLW-QREilgdlddsdsPIAAQLAYWENALAGMPERLRLPTARPYPPVADQRG-AS 1248
Cdd:PRK12467 2796 QRYF----GQPP--PAREGRYRDYIAWlQAQ----------DAEASEAFWKEQLAALEEPTRLARALYPAPAEAVAGhGA 2859

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1249 LVVDWPASVQQQVRRIARQHNATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGRsdPA----LDNLVGFFVNTLVLRVNL 1324
Cdd:PRK12467 2860 HYLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGR--PAqlrgAEQQLGLFINTLPVIASP 2937

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1325 AGDPSFAELLGQVRARSLAAYENQDVP-FEVLVDRLKPTRALthhplIQVMLAWQDNPVGQlNLGDLQATPMPIDTRTAR 1403
Cdd:PRK12467 2938 RAEQTVSDWLQQVQAQNLALREFEHTPlADIQRWAGQGGEAL-----FDSILVFENYPISE-ALKQGAPSGLRFGAVSSR 3011

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1404 ------MDLVFSLAERFSegsepagiggaVEYRTD--VFEAQAIDVLIERLRKVLVAVAAAPERTVSSIDALDGTERARL 1475
Cdd:PRK12467 3012 eqtnypLTLAVGLGDTLE-----------LEFSYDrqHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQV 3080

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1476 DEWGNRAVLTAPAPTPVSipQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPA 1555
Cdd:PRK12467 3081 LHAWNATAAAYPSERLVH--QLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEM 3158

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1556 VVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVTTAGLRSRL--AGHDLPIIDVVDALAAYP-GTPPPMPAAVN 1632
Cdd:PRK12467 3159 IVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLpaPAGDTALTLDRLDLNGYSeNNPSTRVMGEN 3238

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1633 LAYILYTSGTTGEPKGVGITHRNVTRLFASLPA--RLSAAQVWSQCHSYGFDASAWEIWGALLGGGRLVIVPESVAaSPN 1710
Cdd:PRK12467 3239 LAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEayELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLW-DPE 3317

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1711 DFHGLLVAEHVSVLTQTPAAV-AMLPTQGLESVA----LVVAGEACPAA---LVDRWAPGRVMLNAYGPTETTICA---A 1779
Cdd:PRK12467 3318 ELWQAIHAHRISIACFPPAYLqQFAEDAGGADCAsldiYVFGGEAVPPAafeQVKRKLKPRGLTNGYGPTEAVVTVtlwK 3397

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1780 ISAPLRPGSGMPPIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFGGSGARMYRTGD 1859
Cdd:PRK12467 3398 CGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSGSGGRLYRTGD 3477

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1860 LVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAReDRPGDKRLVGYATEIAPGAVDPAGLRAQL 1939
Cdd:PRK12467 3478 LARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPADPQGDWRETLRDHL 3556

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1940 AQRLPGYLVPAAVVVIDALPLTVNGKLDHRALPAPEYGDTNGYRAPAGPVEKTVAGIFARVLGLERVGVDDSFFELGGDS 2019
Cdd:PRK12467 3557 AASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDS 3636

                        1050      1060      1070
                  ....*....|....*....|....*....|...
gi 489495878 2020 LAAMRVIAAINTTLNADLPVRALLHASSTRGLS 2052
Cdd:PRK12467 3637 LLALQVLSRIRQSLGLKLSLRDLMSAPTIAELA 3669
PRK12316 PRK12316
peptide synthase; Provisional
 1013-2055 2.89e-171

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 592.70  E-value: 2.89e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1013 PLVAAQRPAAIPLSFAQRRLWFLDQLQRPAPVYNMAVALRLRGyLDTEALGAAVADVVGRHESLRTVFPAVDGVPRQLVI 1092
Cdd:PRK12316 4093 PLPLGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFVWQGELGRPLQV 4171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1093 EARRADLGCDIVDATAWPadRLQRAIEEAA----RHSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTAD 1168
Cdd:PRK12316 4172 VHKQVSLPFAELDWRGRA--DLQAALDALAaaerERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGE 4249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1169 LSAAYAsrcaGRAPdwAPLPVQYVDYTLWqreilgdLDDSDSpiAAQLAYWENALAGMPERLRLPTARPYPPVADQRG-A 1247
Cdd:PRK12316 4250 VLERYS----GRPP--AQPGGRYRDYIAW-------LQRQDA--AASEAFWREQLAALDEPTRLAQAIARADLRSANGyG 4314

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1248 SLVVDWPASVQQQVRRIARQHNATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGRSD--PALDNLVGFFVNTLVLRVNLA 1325
Cdd:PRK12316 4315 EHVRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAelPGIEGQIGLFINTLPVIATPR 4394

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1326 GDPSFAELLGQVRARSLAAYENQDVPFEvlvdRLKPTRALTHHPLIQVMLAWQDNPVGQLnlgdLQatpmpidtRTARMD 1405
Cdd:PRK12316 4395 AQQSVVEWLQQVQRQNLALREHEHTPLY----EIQRWAGQGGEALFDSLLVFENYPVSEA----LQ--------QGAPGG 4458

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1406 LVFSLAERFSEGSEP----AGIGGAVE----YRTDVFEAQAIDVLIERLRKVLVAVAAAPERTVSSIDALDGTERARLDE 1477
Cdd:PRK12316 4459 LRFGEVTNHEQTNYPltlaVGLGETLSlqfsYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVA 4538

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1478 WGNRAvlTAPAPTPVSIPQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVV 1557
Cdd:PRK12316 4539 LWNRT--DAGYPATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMV 4616

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1558 AMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVTTAGLRSRL---AGHDLPIIDVVDALAAYPGTPPPMPAAV-NL 1633
Cdd:PRK12316 4617 GLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLpipDGLASLALDRDEDWEGFPAHDPAVRLHPdNL 4696

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1634 AYILYTSGTTGEPKGVGITHRNVTRLFASLPAR--LSAAQVWSQCHSYGFDASAWEIWGALLGGGRLVIVPESvAASPND 1711
Cdd:PRK12316 4697 AYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERyeLTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDS-LWDPER 4775

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1712 FHGLLVAEHVSVLTQTPAAVAML---PTQGLESVALVVA---GEACPAALVDRW---APGRVMLNAYGPTETTI---CAA 1779
Cdd:PRK12316 4776 LYAEIHEHRVTVLVFPPVYLQQLaehAERDGEPPSLRVYcfgGEAVAQASYDLAwraLKPVYLFNGYGPTETTVtvlLWK 4855

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1780 ISAPLRPGSGMPPIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFGGSGARMYRTGD 1859
Cdd:PRK12316 4856 ARDGDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGGRLYRTGD 4935

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1860 LVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDrPGDKRLVGY----ATEIAPGAVDPAGL 1935
Cdd:PRK12316 4936 LARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEG-AVGKQLVGYvvpqDPALADADEAQAEL 5014

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1936 RAQ----LAQRLPGYLVPAAVVVIDALPLTVNGKLDHRALPAPEYG-DTNGYRAPAGPVEKTVAGIFARVLGLERVGVDD 2010
Cdd:PRK12316 5015 RDElkaaLRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASlLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDD 5094

                        1050      1060      1070      1080
                  ....*....|....*....|....*....|....*....|....*
gi 489495878 2011 SFFELGGDSLAAMRVIAAINTTLNADLPVRALLHASSTRGLSQLL 2055
Cdd:PRK12316 5095 NFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAAFVELA 5139
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 1506-1971 2.50e-165

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 517.47  E-value: 2.50e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1506 PEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFML 1585
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1586 GDAVPVAAVTTAGlrsrlaghdlpiidvvdalaaypgtpppmpaavNLAYILYTSGTTGEPKGVGITHRNVTRLFASLPA 1665
Cdd:cd05930    81 EDSGAKLVLTDPD---------------------------------DLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQE 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1666 R--LSAAQVWSQCHSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAEHVSVLTQTPAAVAMLPTQGLESVA 1743
Cdd:cd05930   128 AypLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAAL 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1744 -----LVVAGEACPAALVDRWA---PGRVMLNAYGPTETTICAAI--SAPLRPGSGMPPIGVPVSGAALFVLDSWLRPVP 1813
Cdd:cd05930   208 pslrlVLVGGEALPPDLVRRWRellPGARLVNLYGPTEATVDATYyrVPPDDEEDGRVPIGRPIPNTRVYVLDENLRPVP 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1814 AGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFGGsGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVAT 1893
Cdd:cd05930   288 PGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGP-GERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEA 366

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489495878 1894 ALAELAGVGQAVVIAREDRPGDKRLVGYATEIAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:cd05930   367 ALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
PRK12316 PRK12316
peptide synthase; Provisional
 1013-2075 2.16e-159

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 554.95  E-value: 2.16e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1013 PLVAAQRPAAIPLSFAQRRLWFLDQLQRPAPVYNMAVALRLRGyLDTEALGAAVADVVGRHESLRTVFPAVDGVPRQLVI 1092
Cdd:PRK12316 1547 PLPAGEIADIYPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFLWQDGLEQPLQV 1625

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1093 EARRADLGCDIVDATAWP--ADRLQRAIEEAARHSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLS 1170
Cdd:PRK12316 1626 IHKQVELPFAELDWRGREdlGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVL 1705

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1171 AAYAsrcaGRAPdwAPLPVQYVDYTLWqreilgdLDDSDSpiAAQLAYWENALAG--MPERLRLPTARPYPPVAdqrGAS 1248
Cdd:PRK12316 1706 QRYA----GQPV--AAPGGRYRDYIAW-------LQRQDA--AASEAFWKEQLAAleEPTRLAQAARTEDGQVG---YGD 1767

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1249 LVVDWPASVQQQVRRIARQHNATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGRSD--PALDNLVGFFVNTLVLRVNLAG 1326
Cdd:PRK12316 1768 HQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAelPGIEQQIGLFINTLPVIAAPRP 1847

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1327 DPSFAELLGQVRARSLAAYENQDVP-FEVlvdrlKPTRALTHHPLIQVMLAWQDNPVGQ-LNLGdlqatpmpidtrtARM 1404
Cdd:PRK12316 1848 DQSVADWLQEVQALNLALREHEHTPlYDI-----QRWAGQGGEALFDSLLVFENYPVAEaLKQG-------------APA 1909

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1405 DLVFSLAERFSEGSEPAGIGG------AVEYRTD--VFEAQAIDVLIERLRKVLVAVAAAPERTVSSIDALDGTERARLD 1476
Cdd:PRK12316 1910 GLVFGRVSNHEQTNYPLTLAVtlgetlSLQYSYDrgHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRIL 1989

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1477 EWGNRAvlTAPAPTPVSIPQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAV 1556
Cdd:PRK12316 1990 ADWDRT--PEAYPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELV 2067

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1557 VAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVTTAGLRSRL---AGHDLPIIDVVDALAAYPGT-PPPMPAAVN 1632
Cdd:PRK12316 2068 VALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLplpAGVARLPLDRDAEWADYPDTaPAVQLAGEN 2147

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1633 LAYILYTSGTTGEPKGVGITHrnvTRLFASLPA-----RLSAAQVWSQCHSYGFDASAWEIWGALLGGGRLVI------V 1701
Cdd:PRK12316 2148 LAYVIYTSGSTGLPKGVAVSH---GALVAHCQAageryELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIrddelwD 2224

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1702 PESVAASPNDfHGLLVAEHVSVLTQTPAAVAMLPTQGLESVALVVAGEACPAALVDRWA---PGRVMLNAYGPTETTICA 1778
Cdd:PRK12316 2225 PEQLYDEMER-HGVTILDFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWealRPVYLFNGYGPTEAVVTP 2303

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1779 AI--SAPLRP-GSGMPPIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFGGSGARMY 1855
Cdd:PRK12316 2304 LLwkCRPQDPcGAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGERLY 2383

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1856 RTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAReDRPGDKRLVGYATEIAPGAVDPAGL 1935
Cdd:PRK12316 2384 RTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAEDLLAEL 2462

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1936 RAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRALPAPEYGDT-NGYRAPAGPVEKTVAGIFARVLGLERVGVDDSFFE 2014
Cdd:PRK12316 2463 RAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLrQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFE 2542

                        1050      1060      1070      1080      1090      1100
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489495878 2015 LGGDSLAAMRVIAAINTTLNADLPVRALLHASSTRGLSQLLGRDARPTSdPRLVSVHGDNP 2075
Cdd:PRK12316 2543 LGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAASLESGQTSRA-PVLQKVTRVQP 2602
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 1496-1971 2.16e-156

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 493.64  E-value: 2.16e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1496 QMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPA 1575
Cdd:cd12117     1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1576 NPPPRVAFMLGDAVPVAAVTTAGLRSRLAGhDLPIIDVVDALAAYPGTPPPMPA-AVNLAYILYTSGTTGEPKGVGITHR 1654
Cdd:cd12117    81 LPAERLAFMLADAGAKVLLTDRSLAGRAGG-LEVAVVIDEALDAGPAGNPAVPVsPDDLAYVMYTSGSTGRPKGVAVTHR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1655 NVTRLFASLP-ARLSAAQVWSQCHSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAEHVSVLTQTPAAVAM 1733
Cdd:cd12117   160 GVVRLVKNTNyVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALFNQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1734 LPTQGLESVA----LVVAGEACPAALVDRW---APGRVMLNAYGPTETTICAA--ISAPLRPGSGMPPIGVPVSGAALFV 1804
Cdd:cd12117   240 LADEDPECFAglreLLTGGEVVSPPHVRRVlaaCPGLRLVNGYGPTENTTFTTshVVTELDEVAGSIPIGRPIANTRVYV 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1805 LDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFGGsGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGY 1884
Cdd:cd12117   320 LDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGP-GERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGF 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1885 RIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATeiAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNG 1964
Cdd:cd12117   399 RIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVV--AEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANG 476


                  ....*..
gi 489495878 1965 KLDHRAL 1971
Cdd:cd12117   477 KVDRRAL 483
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 1506-1971 6.22e-155

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 487.97  E-value: 6.22e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1506 PEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFML 1585
Cdd:cd17643     1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1586 GDAVPVAAVTTAGlrsrlaghdlpiidvvdalaaypgtpppmpaavNLAYILYTSGTTGEPKGVGITHRNVTRLFASLPA 1665
Cdd:cd17643    81 ADSGPSLLLTDPD---------------------------------DLAYVIYTSGSTGRPKGVVVSHANVLALFAATQR 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1666 --RLSAAQVWSQCHSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAEHVSVLTQTPAA------VAMLPTQ 1737
Cdd:cd17643   128 wfGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAfyqlveAADRDGR 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1738 GLESVALVV-AGEACPAALVDRWA-----PGRVMLNAYGPTETTICA---AISAPLRPGSGMPPIGVPVSGAALFVLDSW 1808
Cdd:cd17643   208 DPLALRYVIfGGEALEAAMLRPWAgrfglDRPQLVNMYGITETTVHVtfrPLDAADLPAAAASPIGRPLPGLRVYVLDAD 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1809 LRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFGGSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIEL 1888
Cdd:cd17643   288 GRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIEL 367

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1889 GEVATALAELAGVGQAVVIAREDRPGDKRLVGYATEIAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDH 1968
Cdd:cd17643   368 GEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDR 447


                  ...
gi 489495878 1969 RAL 1971
Cdd:cd17643   448 AAL 450
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 1506-1971 1.44e-146

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 465.23  E-value: 1.44e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1506 PEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFML 1585
Cdd:cd12116     1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1586 GDAVPVAAVTTAGLRSRLAGHDLPIIDVVDALAAYPGTPPPMPAAVNLAYILYTSGTTGEPKGVGITHRNVTRLFASLPA 1665
Cdd:cd12116    81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1666 RLS--AAQVWSQCHSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAEHVSVLTQTPAAVAMLPT---QGLE 1740
Cdd:cd12116   161 RLGlgPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDagwQGRA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1741 SVALVVAGEACPAALVDRW-APGRVMLNAYGPTETTICAAIsAPLRPGSGMPPIGVPVSGAALFVLDSWLRPVPAGVAGE 1819
Cdd:cd12116   241 GLTALCGGEALPPDLAARLlSRVGSLWNLYGPTETTIWSTA-ARVTAAAGPIPIGRPLANTQVYVLDAALRPVPPGVPGE 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1820 LYIAGAGVGVGYWRRAGLTASRFVACPFGGSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELA 1899
Cdd:cd12116   320 LYIGGDGVAQGYLGRPALTAERFVPDPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHP 399

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489495878 1900 GVGQAVVIAREDRpGDKRLVGYATEIAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:cd12116   400 GVAQAAVVVREDG-GDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 1498-1972 3.46e-146

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 464.89  E-value: 3.46e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1498 LAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANP 1577
Cdd:cd17651     1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1578 PPRVAFMLGDAVPVAAVTTAGLRSRLAGHDLPIIDVVDALAAYPGTPPPMPA--AVNLAYILYTSGTTGEPKGVGITHRN 1655
Cdd:cd17651    81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAEPDPAldADDLAYVIYTSGSTGRPKGVVMPHRS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1656 VTRLFASLPARLSAAQ--VWSQCHSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAEHVS-VLTQTPAAVA 1732
Cdd:cd17651   161 LANLVAWQARASSLGPgaRTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISrVFLPTVALRA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1733 MLPTQGLESVA------LVVAGEACP-AALVDRWA---PGRVMLNAYGPTETTICAAISAPLRPGSGM--PPIGVPVSGA 1800
Cdd:cd17651   241 LAEHGRPLGVRlaalryLLTGGEQLVlTEDLREFCaglPGLRLHNHYGPTETHVVTALSLPGDPAAWPapPPIGRPIDNT 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1801 ALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFGGsGARMYRTGDLVCWRADGQLEFLGRTDDQVK 1880
Cdd:cd17651   321 RVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVP-GARMYRTGDLARWLPDGELEFLGRADDQVK 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1881 IRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATEIAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPL 1960
Cdd:cd17651   400 IRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPL 479

                         490
                  ....*....|..
gi 489495878 1961 TVNGKLDHRALP 1972
Cdd:cd17651   480 TPNGKLDRRALP 491
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 1519-1906 6.06e-146

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 460.58  E-value: 6.06e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1519 TYRELDEASNRLAHRL-AGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVTTA 1597
Cdd:TIGR01733    1 TYRELDERANRLARHLrAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1598 GLRSRLAGHDLPIIDVVDAL------AAYPGTPPPMPAAVNLAYILYTSGTTGEPKGVGITHRNVTRLFASLPAR--LSA 1669
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDPLElaalddAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRygLDP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1670 AQVWSQCHSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAEH-VSVLTQTPAAVAMLPTQGLESVA----L 1744
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHpVTVLNLTPSLLALLAAALPPALAslrlV 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1745 VVAGEACPAALVDRWA---PGRVMLNAYGPTETTICAA---ISAPLRPGSGMPPIGVPVSGAALFVLDSWLRPVPAGVAG 1818
Cdd:TIGR01733  241 ILGGEALTPALVDRWRargPGARLINLYGPTETTVWSTatlVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1819 ELYIAGAGVGVGYWRRAGLTASRFVACPF-GGSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAE 1897
Cdd:TIGR01733  321 ELYIGGPGVARGYLNRPELTAERFVPDPFaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400


                   ....*....
gi 489495878  1898 LAGVGQAVV 1906
Cdd:TIGR01733  401 HPGVREAVV 409
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 1495-1971 1.85e-141

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 451.34  E-value: 1.85e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1495 PQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDP 1574
Cdd:cd17646     1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1575 ANPPPRVAFMLGDAVPVAAVTTAGLRSRLAGHDLPIIDVVDALAAYPGTPP-PMPAAVNLAYILYTSGTTGEPKGVGITH 1653
Cdd:cd17646    81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPlVPPRPDNLAYVIYTSGSTGRPKGVMVTH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1654 RNVTRLFASLPAR--LSAAQVWSQCHSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAEHVSVLTQTP--- 1728
Cdd:cd17646   161 AGIVNRLLWMQDEypLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPsml 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1729 -AAVAMLPTQGLESVALVV-AGEACPAALVDRWA--PGRVMLNAYGPTETTIcAAISAPLRPGSGMP--PIGVPVSGAAL 1802
Cdd:cd17646   241 rVFLAEPAAGSCASLRRVFcSGEALPPELAARFLalPGAELHNLYGPTEAAI-DVTHWPVRGPAETPsvPIGRPVPNTRL 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1803 FVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFgGSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIR 1882
Cdd:cd17646   320 YVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPF-GPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIR 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1883 GYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATEIAPGA-VDPAGLRAQLAQRLPGYLVPAAVVVIDALPLT 1961
Cdd:cd17646   399 GFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAgPDTAALRAHLAERLPEYMVPAAFVVLDALPLT 478

                         490
                  ....*....|
gi 489495878 1962 VNGKLDHRAL 1971
Cdd:cd17646   479 ANGKLDRAAL 488
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 1496-1975 1.02e-134

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 432.14  E-value: 1.02e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1496 QMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPA 1575
Cdd:cd17655     1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1576 NPPPRVAFMLGDAVPVAAVTTAGLRSRLAGHDLPIIDVVDALAAYPGTP-PPMPAAVNLAYILYTSGTTGEPKGVGITHR 1654
Cdd:cd17655    81 YPEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENlEPVSKSDDLAYVIYTSGSTGKPKGVMIEHR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1655 NVTRLFASLPARLSAAQV--WSQCHSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAEHVSVLTQTPAAVA 1732
Cdd:cd17655   161 GVVNLVEWANKVIYQGEHlrVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1733 MLP----TQGLESVALVVAGEACPAALVDRW----APGRVMLNAYGPTETTICAAI--SAPLRPGSGMPPIGVPVSGAAL 1802
Cdd:cd17655   241 LLDaaddSEGLSLKHLIVGGEALSTELAKKIielfGTNPTITNAYGPTETTVDASIyqYEPETDQQVSVPIGKPLGNTRI 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1803 FVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFGgSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIR 1882
Cdd:cd17655   321 YILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFV-PGERMYRTGDLARWLPDGNIEFLGRIDHQVKIR 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1883 GYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATEIAPgaVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTV 1962
Cdd:cd17655   400 GYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKE--LPVAQLREFLARELPDYMIPSYFIKLDEIPLTP 477

                         490
                  ....*....|...
gi 489495878 1963 NGKLDHRALPAPE 1975
Cdd:cd17655   478 NGKVDRKALPEPD 490
PRK05691 PRK05691
peptide synthase; Validated
 1013-2055 6.17e-133

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 470.03  E-value: 6.17e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1013 PLVAAQRPAAIPLSFAQRRLWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVDGVPRQLVI 1092
Cdd:PRK05691 3248 PVPAAEIEDVYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGETMLQVI 3327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1093 EaRRADLGCDIVDATAWPAD----RLQRAIEEAARHSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTAD 1168
Cdd:PRK05691 3328 H-KPGRTPIDYLDWRGLPEDgqeqRLQALHKQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMND 3406

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1169 LSAAYASRCAGRAPDWAPLPvQYVDYTLW-QREilgDLDDSDspiaaqlAYWENALAGMPERLRLPTARPY-PPVADQRG 1246
Cdd:PRK05691 3407 FFEIYTALGEGREAQLPVPP-RYRDYIGWlQRQ---DLAQAR-------QWWQDNLRGFERPTPIPSDRPFlREHAGDSG 3475

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1247 ASLVVD----WPASVQQQVRRIARQHNATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGR--SDPALDNLVGFFVNTLVL 1320
Cdd:PRK05691 3476 GMVVGDcytrLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRpvSMPQMQRTVGLFINSIAL 3555

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1321 RVNLAGDP---SFAELLGQVRARSLAAYENQDVPfevLVDRLKPTRALTHHPLIQVMLAWQDNPVGQLNLGDLQATPMPI 1397
Cdd:PRK05691 3556 RVQLPAAGqrcSVRQWLQGLLDSNMELREYEYLP---LVAIQECSELPKGQPLFDSLFVFENAPVEVSVLDRAQSLNASS 3632

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1398 DTrtARMDLVFSLAERFSEGSEpagIGGAVEYRTDVFEAQAIDVLIERLRKVLVAVAAAPERTVSSIDALDGTERARLDE 1477
Cdd:PRK05691 3633 DS--GRTHTNFPLTAVCYPGDD---LGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGEQERDFLLD 3707

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1478 WGNRAvlTAPAPTPVSIPQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVV 1557
Cdd:PRK05691 3708 GCNRS--ERDYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLG 3785

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1558 AMVAVLKTGAAYLPIDPANPPPRVAFMLG-DAVPVAAVTTA------GLRSRLAGHDLPIIDV---VDALAAYPGTPPPM 1627
Cdd:PRK05691 3786 MIVGSFKAGAGYLPLDPGLPAQRLQRIIElSRTPVLVCSAAcreqarALLDELGCANRPRLLVweeVQAGEVASHNPGIY 3865

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1628 PAAVNLAYILYTSGTTGEPKGVGITHRN-VTRLFASLP-ARLSAAQVWSQCHSYGFDASAWEIWGALLGGGRLVIVPESV 1705
Cdd:PRK05691 3866 SGPDNLAYVIYTSGSTGLPKGVMVEQRGmLNNQLSKVPyLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAI 3945

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1706 AASPNDFHGLLVAEHVSVLTQTPAAV-AML--PTQGLESVA-LVVAGEACPAALVDRWA---PGRVMLNAYGPTETTICA 1778
Cdd:PRK05691 3946 AHDPQGLLAHVQAQGITVLESVPSLIqGMLaeDRQALDGLRwMLPTGEAMPPELARQWLqryPQIGLVNAYGPAECSDDV 4025

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1779 A---ISAPLRPGSGMPpIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFGGSGARMY 1855
Cdd:PRK05691 4026 AffrVDLASTRGSYLP-IGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFGAPGERLY 4104

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1856 RTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREdRPGDKRLVGYATEiAPGAVDPAGL 1935
Cdd:PRK05691 4105 RTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQE-GVNGKHLVGYLVP-HQTVLAQGAL 4182

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1936 RAQLAQR----LPGYLVPAAVVVIDALPLTVNGKLDHRALPAPEYGDTNG--YRAPAGPVEKTVAGIFARVLGLERVGVD 2009
Cdd:PRK05691 4183 LERIKQRlraeLPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSqaYLAPRNELEQTLATIWADVLKVERVGVH 4262

                        1050      1060      1070      1080
                  ....*....|....*....|....*....|....*....|....*.
gi 489495878 2010 DSFFELGGDSLAAMRVIAAINTTLNADLPVRALLHASSTRGLSQLL 2055
Cdd:PRK05691 4263 DNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYI 4308
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 1496-1971 4.29e-129

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 414.02  E-value: 4.29e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1496 QMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPA 1575
Cdd:cd12115     3 DLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1576 NPPPRVAFMLGDAVPVAAVTTAGlrsrlaghdlpiidvvdalaaypgtpppmpaavNLAYILYTSGTTGEPKGVGITHRN 1655
Cdd:cd12115    83 YPPERLRFILEDAQARLVLTDPD---------------------------------DLAYVIYTSGSTGRPKGVAIEHRN 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1656 -VTRLFASlpARLSAAQVWSQ---CHSYGFDASAWEIWGALLGGGRLVIVpESVAASPNdfhgLLVAEHVSVLTQTPAAV 1731
Cdd:cd12115   130 aAAFLQWA--AAAFSAEELAGvlaSTSICFDLSVFELFGPLATGGKVVLA-DNVLALPD----LPAAAEVTLINTVPSAA 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1732 AMLPTQGL--ESVALV-VAGEACPAALVDRW---APGRVMLNAYGPTETTICAAISAPLRPGSGMPPIGVPVSGAALFVL 1805
Cdd:cd12115   203 AELLRHDAlpASVRVVnLAGEPLPRDLVQRLyarLQVERVVNLYGPSEDTTYSTVAPVPPGASGEVSIGRPLANTQAYVL 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1806 DSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFGGsGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYR 1885
Cdd:cd12115   283 DRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGP-GARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFR 361

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1886 IELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATEIAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGK 1965
Cdd:cd12115   362 IELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGK 441


                  ....*.
gi 489495878 1966 LDHRAL 1971
Cdd:cd12115   442 IDRSAL 447
Thioester-redct TIGR01746
thioester reductase domain; This model includes the terminal domain from the fungal alpha ...
 2109-2511 8.77e-122

thioester reductase domain; This model includes the terminal domain from the fungal alpha aminoadipate reductase enzyme (also known as aminoadipate semialdehyde dehydrogenase) which is involved in the biosynthesis of lysine, as well as the reductase-containing component of the myxochelin biosynthetic gene cluster, MxcG. The mechanism of reduction involves activation of the substrate by adenylation and transfer to a covalently-linked pantetheine cofactor as a thioester. This thioester is then reduced to give an aldehyde (thus releasing the product) and a regenerated pantetheine thiol. (In myxochelin biosynthesis this aldehyde is further reduced to an alcohol or converted to an amine by an aminotransferase.) This is a fundamentally different reaction than beta-ketoreductase domains of polyketide synthases which act at a carbonyl two carbons removed from the thioester and forms an alcohol as a product. This domain is invariably found at the C-terminus of the proteins which contain it (presumably because it results in the release of the product). The majority of hits to this model are non-ribosomal peptide synthetases in which this domain is similarly located proximal to a thiolation domain (pfam00550). In some cases this domain is found at the end of a polyketide synthetase enzyme, but is unlike ketoreductase domains which are found before the thiolase domains. Exceptions to this observed relationship with the thiolase domain include three proteins which consist of stand-alone reductase domains (GP|466833 from M. leprae, GP|435954 from Anabaena and OMNI|NTL02SC1199 from Strep. coelicolor) and one protein (OMNI|NTL01NS2636 from Nostoc) which contains N-terminal homology with a small group of hypothetical proteins but no evidence of a thiolation domain next to the putative reductase domain. Below the noise cutoff to this model are proteins containing more distantly related ketoreductase and dehydratase/epimerase domains. It has been suggested that a NADP-binding motif can be found in the N-terminal portion of this domain that may form a Rossman-type fold.


Pssm-ID: 273787 [Multi-domain]  Cd Length: 367  Bit Score: 389.85  E-value: 8.77e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2109 TVLLTGATGFLGRYLVLELLRRLdVDGRLICLVRAESDEDARRRLEKTFDSgdpELLRHFkELAADRLEVVAGDKSEPDL 2188
Cdd:TIGR01746    1 TVLLTGATGFLGAYLLEELLRRS-TRAKVICLVRADSEEHAMERLREALRS---YRLWHE-NLAMERIEVVAGDLSKPRL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2189 GLDQPMWRRLAETVDLIVDSAAMVN-AFPYHELFGPNVAGTAELIRIALTTKLKPFTYVSTADVGAAIEPSAFtedadIR 2267
Cdd:TIGR01746   76 GLSDAEWERLAENVDTIVHNGALVNhVYPYSELRGANVLGTVEVLRLAASGRAKPLHYVSTISVGAAIDLSTG-----VT 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2268 VISPTRTVDGGWAGGYGTSKWAGEVLLREANDLcALPVAVFRCGMILADtSYAGQLNMSDWVTRMVLSLMATGIAprsfy 2347
Cdd:TIGR01746  151 EDDATVTPYPGLAGGYTQSKWVAELLVREASDR-GLPVTIVRPGRILGD-SYTGAWNSSDILWRMVKGCLALGAY----- 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2348 ePDSEGNrqraHFDGLPVTFVAEAIAVLGARVAGSslAGFATYHVMNPhdDGIGLDEYVDWLIEAGYPIrRIDDFAEWLQ 2427
Cdd:TIGR01746  224 -PQSPEL----TEDLTPVDFVARAIVALSSRPAAS--AGGIVFHVVNP--NPVPLDEFLEWLERAGYNL-RLVSFDEWLQ 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2428 RFEASLGALPDRqRRHSVLPMLLASNSQRLQPlkptrgcsaPTDRFRAAVRAAKVGSDKDNPDIPHVSAPTIINYVTNLQ 2507
Cdd:TIGR01746  294 RLEDSDTAKRDS-RRYPLLPLLHFTGDAFESD---------ETDTRNLDSRSTAEALEGDGIREPSITAPLLHLYLQYLK 363


                   ....
gi 489495878  2508 LLGL 2511
Cdd:TIGR01746  364 EIGF 367
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 1500-1971 6.97e-118

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 381.27  E-value: 6.97e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1500 AQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPP 1579
Cdd:cd17653     5 RIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1580 RVAFMLGDAVPVAAVTTAglrsrlAGHDlpiidvvdalaaypgtpppmpaavnLAYILYTSGTTGEPKGVGITHRNVTRL 1659
Cdd:cd17653    85 RIQAILRTSGATLLLTTD------SPDD-------------------------LAYIIFTSGSTGIPKGVMVPHRGVLNY 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1660 FASLPARLSA------AQVWsqchSYGFDASAWEIWGALLGGGRLVIvpesvAASPNDF-HgllVAEHVSVLTQTPAAVA 1732
Cdd:cd17653   134 VSQPPARLDVgpgsrvAQVL----SIAFDACIGEIFSTLCNGGTLVL-----ADPSDPFaH---VARTVDALMSTPSILS 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1733 MLPTQGLESVALV-VAGEACPAALVDRWAPGRVMLNAYGPTETTICAAISApLRPGSGMpPIGVPVSGAALFVLDSWLRP 1811
Cdd:cd17653   202 TLSPQDFPNLKTIfLGGEAVPPSLLDRWSPGRRLYNAYGPTECTISSTMTE-LLPGQPV-TIGKPIPNSTCYILDADLQP 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1812 VPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFgGSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGE- 1890
Cdd:cd17653   280 VPEGVVGEICISGVQVARGYLGNPALTASKFVPDPF-WPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEi 358

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1891 VATALAELAGVGQAVVIAREDrpgdkRLVGYATeiaPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRA 1970
Cdd:cd17653   359 EEVVLQSQPEVTQAAAIVVNG-----RLVAFVT---PETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKA 430


                  .
gi 489495878 1971 L 1971
Cdd:cd17653   431 L 431
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 1506-1972 1.12e-117

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 381.33  E-value: 1.12e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1506 PEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFML 1585
Cdd:cd17649     1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1586 GDAvpvaavttaGLRSRLAGHdlpiidvvdalaaypgtpppmPAavNLAYILYTSGTTGEPKGVGITHRNVTRLFASLPA 1665
Cdd:cd17649    81 EDS---------GAGLLLTHH---------------------PR--QLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAE 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1666 --RLSAAQVWSQCHSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAEHVSVLTQTPA--------AVAMLP 1735
Cdd:cd17649   129 ryGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAylqqlaeeADRTGD 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1736 TQGLESVALVVAGEACPAALVDRWAPGRVML-NAYGPTETTICAA---ISAPLRPGSGMPPIGVPVSGAALFVLDSWLRP 1811
Cdd:cd17649   209 GRPPSLRLYIFGGEALSPELLRRWLKAPVRLfNAYGPTEATVTPLvwkCEAGAARAGASMPIGRPLGGRSAYILDADLNP 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1812 VPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFGGSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEV 1891
Cdd:cd17649   289 VPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEI 368

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1892 ATALAELAGVGQAVVIAReDRPGDKRLVGY--ATEIAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHR 1969
Cdd:cd17649   369 EAALLEHPGVREAAVVAL-DGAGGKQLVAYvvLRAAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRK 447


                  ...
gi 489495878 1970 ALP 1972
Cdd:cd17649   448 ALP 450
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 1506-1971 3.45e-117

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 379.89  E-value: 3.45e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1506 PEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFML 1585
Cdd:cd17650     1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1586 GDAvpvaavttaglrsrlaGHDLPIIDvvdalaayPGtpppmpaavNLAYILYTSGTTGEPKGVGITHRNVTRL------ 1659
Cdd:cd17650    81 EDS----------------GAKLLLTQ--------PE---------DLAYVIYTSGTTGKPKGVMVEHRNVAHAahawrr 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1660 ---FASLPARLSaaqvwsQCHSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAEHVSVLTQTPA----AVA 1732
Cdd:cd17650   128 eyeLDSFPVRLL------QMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPAlirpVMA 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1733 MLPTQGLESVA---LVVAGEACPAA----LVDRWAPGRVMLNAYGPTETTICAAI---SAPLRPGSGMPPIGVPVSGAAL 1802
Cdd:cd17650   202 YVYRNGLDLSAmrlLIVGSDGCKAQdfktLAARFGQGMRIINSYGVTEATIDSTYyeeGRDPLGDSANVPIGRPLPNTAM 281

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1803 FVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFGgSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIR 1882
Cdd:cd17650   282 YVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFA-PGERMYRTGDLARWRADGNVELLGRVDHQVKIR 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1883 GYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYAteIAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTV 1962
Cdd:cd17650   361 GFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYV--VAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTP 438


                  ....*....
gi 489495878 1963 NGKLDHRAL 1971
Cdd:cd17650   439 NGKVDRRAL 447
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 1493-1972 1.05e-116

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 379.09  E-value: 1.05e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1493 SIPQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPI 1572
Cdd:cd17644     1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1573 DPANPPPRVAFMLGDAVpvaavttaglrsrlaghdlpiidvVDALAAYPGtpppmpaavNLAYILYTSGTTGEPKGVGIT 1652
Cdd:cd17644    81 DPNYPQERLTYILEDAQ------------------------ISVLLTQPE---------NLAYVIYTSGSTGKPKGVMIE 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1653 HRNVTRLFASLPARL---SAAQVwSQCHSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAEHVSVLTQTPA 1729
Cdd:cd17644   128 HQSLVNLSHGLIKEYgitSSDRV-LQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPA 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1730 AVAMLPTQGLESVA--------LVVAGEACPAALVDRWA----PGRVMLNAYGPTETTICAAISAPLRPGSGM---PPIG 1794
Cdd:cd17644   207 YWHLLVLELLLSTIdlpsslrlVIVGGEAVQPELVRQWQknvgNFIQLINVYGPTEATIAATVCRLTQLTERNitsVPIG 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1795 VPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFGGS-GARMYRTGDLVCWRADGQLEFLG 1873
Cdd:cd17644   287 RPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSSeSERLYKTGDLARYLPDGNIEYLG 366

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1874 RTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATEIAPGAVDPAGLRAQLAQRLPGYLVPAAVV 1953
Cdd:cd17644   367 RIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFV 446

                         490
                  ....*....|....*....
gi 489495878 1954 VIDALPLTVNGKLDHRALP 1972
Cdd:cd17644   447 VLEELPLTPNGKIDRRALP 465
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 1506-1972 6.06e-109

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 356.32  E-value: 6.06e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1506 PEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAG-PGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFM 1584
Cdd:cd17648     1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1585 LGDAVPVAAVTTAglrsrlaghdlpiidvvdalaaypgtpppmpaaVNLAYILYTSGTTGEPKGVGITHRNVTRLFASLP 1664
Cdd:cd17648    81 LEDTGARVVITNS---------------------------------TDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLS 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1665 ARL----SAAQVWSQCHSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAEHVSVLTQTPAAVAMLPTQGLE 1740
Cdd:cd17648   128 ERYfgrdNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQYDLARLP 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1741 SVALV-VAGEACPAALVDRWA---PGRVmLNAYGPTETTICAAIsaplRPGSGMPP----IGVPVSGAALFVLDSWLRPV 1812
Cdd:cd17648   208 HLKRVdAAGEEFTAPVFEKLRsrfAGLI-INAYGPTETTVTNHK----RFFPGDQRfdksLGRPVRNTKCYVLNDAMKRV 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1813 PAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFG-------GSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYR 1885
Cdd:cd17648   283 PVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQteqerarGRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQR 362

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1886 IELGEVATALAELAGVGQAVVIARED-----RPGDKRLVGYATeIAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPL 1960
Cdd:cd17648   363 IEPGEVEAALASYPGVRECAVVAKEDasqaqSRIQKYLVGYYL-PEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPV 441

                         490
                  ....*....|..
gi 489495878 1961 TVNGKLDHRALP 1972
Cdd:cd17648   442 TINGKLDVRALP 453
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 1494-1971 3.06e-105

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 346.84  E-value: 3.06e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1494 IPQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPID 1573
Cdd:cd05918     1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1574 PANPPPRVAFMLGDavpvaavTTAGLrsrlaghdlpiidvvdALAAYPGtpppmpaavNLAYILYTSGTTGEPKGVGITH 1653
Cdd:cd05918    81 PSHPLQRLQEILQD-------TGAKV----------------VLTSSPS---------DAAYVIFTSGSTGKPKGVVIEH 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1654 RNV-TRLFASLPA-RLSAAQVWSQCHSYGFDASAWEIWGALLGGGRLVIVPESvaASPNDFHGLLVAEHVSVLTQTPAAV 1731
Cdd:cd05918   129 RALsTSALAHGRAlGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEE--DRLNDLAGFINRLRVTWAFLTPSVA 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1732 AMLPTQGLESV-ALVVAGEACPAALVDRWAPGRVMLNAYGPTETTICAAISAPLRPGSGmPPIGVPVsGAALFVLD--SW 1808
Cdd:cd05918   207 RLLDPEDVPSLrTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAATVSPVVPSTDP-RNIGRPL-GATCWVVDpdNH 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1809 LRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPF------GGSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIR 1882
Cdd:cd05918   285 DRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAwlkqegSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIR 364

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1883 GYRIELGEVATALAE-LAGVGQAVV--IAREDRPGDKRLVG--YATEIAPGAVDP---------------AGLRAQLAQR 1942
Cdd:cd05918   365 GQRVELGEIEHHLRQsLPGAKEVVVevVKPKDGSSSPQLVAfvVLDGSSSGSGDGdslflepsdefralvAELRSKLRQR 444

                         490       500
                  ....*....|....*....|....*....
gi 489495878 1943 LPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:cd05918   445 LPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
 1019-1457 3.54e-104

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 342.15  E-value: 3.54e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1019 RPAAIPLSFAQRRLWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVDGVPRQLVIEARRAD 1098
Cdd:cd19546     1 RPDEVPATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRILDADAAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1099 LGCDIVDATAwpaDRLQRAIEEAARHSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYASRCA 1178
Cdd:cd19546    81 PELPVVPATE---EELPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARRE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1179 GRAPDWAPLPVQYVDYTLWQREILGDLDDSDSPIAAQLAYWENALAGMPERLRLPTARPYPPVADQRGASLVVDWPASVQ 1258
Cdd:cd19546   158 GRAPERAPLPLQFADYALWERELLAGEDDRDSLIGDQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVH 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1259 QQVRRIARQHNATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGRSDP-ALDNLVGFFVNTLVLRVNLAGDPSFAELLGQV 1337
Cdd:cd19546   238 ARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDEEgDLEGMVGPFARPLALRTDLSGDPTFRELLGRV 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1338 RARSLAAYENQDVPFEVLVDRLKPTRALTHHPLIQVMLAWQDNPVGQLN---LGDLQATPMPIDTRTARMDLVFSLAERF 1414
Cdd:cd19546   318 REAVREARRHQDVPFERLAELLALPPSADRHPVFQVALDVRDDDNDPWDapeLPGLRTSPVPLGTEAMELDLSLALTERR 397

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 489495878 1415 SEGSEPAGIGGAVEYRTDVFEAQAIDVLIERLRKVLVAVAAAP 1457
Cdd:cd19546   398 NDDGDPDGLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 1506-1971 2.13e-103

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 341.17  E-value: 2.13e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1506 PEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFML 1585
Cdd:cd12114     1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1586 GDAVPVAAVTTAGLRSRLAGHDLPIIDVVDALAAYPGTPPPMPAAVNLAYILYTSGTTGEPKGVGITHRNVTRLFASLPA 1665
Cdd:cd12114    81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1666 R--LSAAQVWSQCHSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAEHVSVLTQTPAAVAML------PTQ 1737
Cdd:cd12114   161 RfaVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLldvleaAQA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1738 GLESVALV-VAGEACPAALVDRW---APGRVMLNAYGPTETTICAAIS--APLRPGSGMPPIGVPVSGAALFVLDSWLRP 1811
Cdd:cd12114   241 LLPSLRLVlLSGDWIPLDLPARLralAPDARLISLGGATEASIWSIYHpiDEVPPDWRSIPYGRPLANQRYRVLDPRGRD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1812 VPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFGGsgaRMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEV 1891
Cdd:cd12114   321 CPDWVPGELWIGGRGVALGYLGDPELTAARFVTHPDGE---RLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEI 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1892 ATALAELAGVGQAVVIAReDRPGDKRLVGYATEIAPGA-VDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRA 1970
Cdd:cd12114   398 EAALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDNDGTpIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAA 476


                  .
gi 489495878 1971 L 1971
Cdd:cd12114   477 L 477
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
 1023-1457 4.11e-102

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 335.50  E-value: 4.11e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1023 IPLSFAQRRLWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVD-GVPRQLVIEARRADLGC 1101
Cdd:cd19539     2 IPLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDgGVPRQEILPPGPAPLEV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1102 -DIVDATAWPADRLQRAIEEAARHSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYASRCAGR 1180
Cdd:cd19539    82 rDLSDPDSDRERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1181 APDWAPLPVQYVDYTLWQREILGDlddsdSPIAAQLAYWENALAGMpERLRLPTARPYPPVADQRGASLVVDWPASVQQQ 1260
Cdd:cd19539   162 AAPLPELRQQYKEYAAWQREALAA-----PRAAELLDFWRRRLRGA-EPTALPTDRPRPAGFPYPGADLRFELDAELVAA 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1261 VRRIARQHNATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGRSDPALDNLVGFFVNTLVLRVNLAGDPSFAELLGQVRAR 1340
Cdd:cd19539   236 LRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKA 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1341 SLAAYENQDVPFEVLVDRLKPTRALTHHPLIQVMLAWQDNPVGQLNL-GDLQATPMPIDTRTARMDLVFSLAErfsegsE 1419
Cdd:cd19539   316 LVDAQRHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGELELaGGLSYTEGSDIPDGAKFDLNLTVTE------E 389

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 489495878 1420 PAGIGGAVEYRTDVFEAQAIDVLIERLRKVLVAVAAAP 1457
Cdd:cd19539   390 GTGLRGSLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 1502-1971 1.61e-101

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 334.60  E-value: 1.61e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1502 VARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRV 1581
Cdd:cd05945     1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1582 AFMLGDAVPVAAVTtaglrsrlAGHDLpiidvvdalaaypgtpppmpaavnlAYILYTSGTTGEPKGVGITHRNVTRLFA 1661
Cdd:cd05945    81 REILDAAKPALLIA--------DGDDN-------------------------AYIIFTSGSTGRPKGVQISHDNLVSFTN 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1662 SLPAR--LSAAQVWSQCHSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAEHVSVLTQTPAAVAMLPT--- 1736
Cdd:cd05945   128 WMLSDfpLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLLspt 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1737 ---QGLESVALVV-AGEACPAALVDRW---APGRVMLNAYGPTETTI-CAAISAPLRPGSGMP--PIGVPVSGAALFVLD 1806
Cdd:cd05945   208 ftpESLPSLRHFLfCGEVLPHKTARALqqrFPDARIYNTYGPTEATVaVTYIEVTPEVLDGYDrlPIGYAKPGAKLVILD 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1807 SWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFvacpFGGSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRI 1886
Cdd:cd05945   288 EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAF----FPDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRI 363

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1887 ELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATEIAPG-AVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGK 1965
Cdd:cd05945   364 ELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAeAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGK 443


                  ....*.
gi 489495878 1966 LDHRAL 1971
Cdd:cd05945   444 IDRKAL 449
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 1496-1972 3.20e-100

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 330.67  E-value: 3.20e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1496 QMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPA 1575
Cdd:cd17645     2 QLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1576 NPPPRVAFMLGDAVPVAAVTTAGlrsrlaghdlpiidvvdalaaypgtpppmpaavNLAYILYTSGTTGEPKGVGITHRN 1655
Cdd:cd17645    82 YPGERIAYMLADSSAKILLTNPD---------------------------------DLAYVIYTSGSTGLPKGVMIEHHN 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1656 VTRL-------FASLPARLSAaqVWSqchSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAEHVSVltqtp 1728
Cdd:cd17645   129 LVNLcewhrpyFGVTPADKSL--VYA---SFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITI----- 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1729 aavAMLPTQGLE--------SVALVVAGEACPAALVDRwapGRVMLNAYGPTETTICAAiSAPLRPGSGMPPIGVPVSGA 1800
Cdd:cd17645   199 ---SFLPTGAAEqfmqldnqSLRVLLTGGDKLKKIERK---GYKLVNNYGPTENTVVAT-SFEIDKPYANIPIGKPIDNT 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1801 ALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFGgSGARMYRTGDLVCWRADGQLEFLGRTDDQVK 1880
Cdd:cd17645   272 RVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFV-PGERMYRTGDLAKFLPDGNIEFLGRLDQQVK 350

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1881 IRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATeiAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPL 1960
Cdd:cd17645   351 IRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT--APEEIPHEELREWLKNDLPDYMIPTYFVHLKALPL 428

                         490
                  ....*....|..
gi 489495878 1961 TVNGKLDHRALP 1972
Cdd:cd17645   429 TANGKVDRKALP 440
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 1228-2449 4.54e-100

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 355.53  E-value: 4.54e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1228 ERLRLPTARPYP-----PVADQrgaslVVDWPASVQQQVRRIARQHNATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGR 1302
Cdd:TIGR03443    4 ERLDNPTLSVLPhdylrPANNR-----LVEATYSLQLPSAEVTAGGGSTPFIILLAAFAALVYRLTGDEDIVLGTSSNKS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1303 SDPaldnlvgffvntLVLRVNLAGDPSFAELLGQVRARSLAAYENQDVPFEVLVDRLKPTRALTHHPLIqVMLAWQDNPV 1382
Cdd:TIGR03443   79 GRP------------FVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPPL-FRLAFQDAPD 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1383 GQlnlgdlQATPMPIDTRtarmDLVFSLAerfseGSEPAGIGGAVeYRTDVFEAQAIDVLIERLRKVLVAVAAAPERTVS 1462
Cdd:TIGR03443  146 NQ------QTTYSTGSTT----DLTVFLT-----PSSPELELSIY-YNSLLFSSDRITIVADQLAQLLSAASSNPDEPIG 209

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1463 SIDALDGTERARLdewgnravltaPAPTPV--------SIPQMLAAQVARIP------EAEAVCCGDA---SMTYRELDE 1525
Cdd:TIGR03443  210 KVSLITPSQKSLL-----------PDPTKDldwsgfrgAIHDIFADNAEKHPdrtcvvETPSFLDPSSktrSFTYKQINE 278

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1526 ASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVT--TAG----- 1598
Cdd:TIGR03443  279 ASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIVieKAGtldql 358

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1599 ----------LRSR-----------LAGHDLPIiDVVDALAAY-------------PGTPPPMPaavnlayilYTSGTTG 1644
Cdd:TIGR03443  359 vrdyidkeleLRTEipalalqddgsLVGGSLEG-GETDVLAPYqalkdtptgvvvgPDSNPTLS---------FTSGSEG 428

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1645 EPKGVGITHRNVTRLFASLPAR--LSAAQVWSQCHSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAEHVS 1722
Cdd:TIGR03443  429 IPKGVLGRHFSLAYYFPWMAKRfgLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGAT 508

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1723 VLTQTPAAVAMLPTQglesvalvvAGEACPA---------ALVDR-------WAPGRVMLNAYGPTET-------TICAA 1779
Cdd:TIGR03443  509 VTHLTPAMGQLLSAQ---------ATTPIPSlhhaffvgdILTKRdclrlqtLAENVCIVNMYGTTETqravsyfEIPSR 579

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1780 ISAP--LRPGSGMPPIGVPVSGAALFVLDSWLRPVPAGVA--GELYIAGAGVGVGYWRRAGLTASRFVACPFG------- 1848
Cdd:TIGR03443  580 SSDStfLKNLKDVMPAGKGMKNVQLLVVNRNDRTQTCGVGevGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVdpshwid 659

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1849 --------------GSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPG 1914
Cdd:TIGR03443  660 ldkennkperefwlGPRDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDE 739

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1915 DKRLVGY--------ATEIAPGAVDPA--------GL----------RAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDH 1968
Cdd:TIGR03443  740 EPTLVSYivpqdksdELEEFKSEVDDEessdpvvkGLikyrklikdiREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDK 819

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1969 RALPAP---------EYGDTNGYRAPAGPVEKTVAGIFARVL--GLERVGVDDSFFELGGDSLAAMRVIAAINTTLNADL 2037
Cdd:TIGR03443  820 PALPFPdtaqlaavaKNRSASAADEEFTETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKKLNVEL 899

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2038 PVRALLHASSTRGLSQLLGR--DARPTSDprlvsvHGDNPTEVHASDLTLDRFIDADTL--------ATAVNLPGPSPel 2107
Cdd:TIGR03443  900 PLGLIFKSPTIKGFAKEVDRlkKGEELAD------EGDSEIEEEETVLELDYAKDAKTLvdslpksyPSRKELDASTP-- 971

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2108 RTVLLTGATGFLGRYLVLELL-RRLDVDGRLICLVRAESDEDARRRLEK---TFDSGDPELlrhfkelaADRLEVVAGDK 2183
Cdd:TIGR03443  972 ITVFLTGATGFLGSFILRDLLtRRSNSNFKVFAHVRAKSEEAGLERLRKtgtTYGIWDEEW--------ASRIEVVLGDL 1043

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2184 SEPDLGLDQPMWRRLAETVDLIVDSAAMVN-AFPYHELFGPNVAGTAELIRIALTTKLKPFTYVSTAdvgAAIEPSAFTE 2262
Cdd:TIGR03443 1044 SKEKFGLSDEKWSDLTNEVDVIIHNGALVHwVYPYSKLRDANVIGTINVLNLCAEGKAKQFSFVSST---SALDTEYYVN 1120

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2263 DADIRV------ISPTRTVDG---GWAGGYGTSKWAGEVLLREANDLcALPVAVFRCGMILADtSYAGQLNMSDWVTRMV 2333
Cdd:TIGR03443 1121 LSDELVqaggagIPESDDLMGsskGLGTGYGQSKWVAEYIIREAGKR-GLRGCIVRPGYVTGD-SKTGATNTDDFLLRML 1198

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2334 lslmaTGIAPRSFYePDSEGNrqrahFDGLPVTFVAEaiAVLGARVAGSSLAGFATYHVMNpHdDGIGLDEYVDWLIEAG 2413
Cdd:TIGR03443 1199 -----KGCIQLGLI-PNINNT-----VNMVPVDHVAR--VVVAAALNPPKESELAVAHVTG-H-PRIRFNDFLGTLKTYG 1263

                         1370      1380      1390
                   ....*....|....*....|....*....|....*.
gi 489495878  2414 YPIrRIDDFAEWLQRFEASlgaLPDRQRRHSVLPML 2449
Cdd:TIGR03443 1264 YDV-EIVDYVHWRKSLERF---VIERSEDNALFPLL 1295
SDR_e1 cd05235
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins ...
 2109-2425 6.56e-98

extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins identified as putative polyketide sythases fatty acid synthases (FAS), and nonribosomal peptide synthases, among others. However, unlike the usual ketoreductase modules of FAS and polyketide synthase, these domains are related to the extended SDRs, and have canonical NAD(P)-binding motifs and an active site tetrad. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187546 [Multi-domain]  Cd Length: 290  Bit Score: 317.67  E-value: 6.56e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2109 TVLLTGATGFLGRYLVLELLRRLDVdGRLICLVRAESDEDARRRLEKTFDSGDpelLRHFKELAADRLEVVAGDKSEPDL 2188
Cdd:cd05235     1 TVLLTGATGFLGAYLLRELLKRKNV-SKIYCLVRAKDEEAALERLIDNLKEYG---LNLWDELELSRIKVVVGDLSKPNL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2189 GLDQPMWRRLAETVDLIVDSAAMVNAF-PYHELFGPNVAGTAELIRIALTTKLKPFTYVSTADVGAAIEPSAFTEDADir 2267
Cdd:cd05235    77 GLSDDDYQELAEEVDVIIHNGANVNWVyPYEELKPANVLGTKELLKLAATGKLKPLHFVSTLSVFSAEEYNALDDEES-- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2268 viSPTRTVDGGWAGGYGTSKWAGEVLLREANDLcALPVAVFRCGMILADtSYAGQLNMSDWVTRMVLSLMATGIAPRSfy 2347
Cdd:cd05235   155 --DDMLESQNGLPNGYIQSKWVAEKLLREAANR-GLPVAIIRPGNIFGD-SETGIGNTDDFFWRLLKGCLQLGIYPIS-- 228

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489495878 2348 epdsegnrqRAHFDGLPVTFVAEAIAVLgarvAGSSLAGFATYHVMNPHddGIGLDEYVDWLIEAGYPIRRIDDFaEW 2425
Cdd:cd05235   229 ---------GAPLDLSPVDWVARAIVKL----ALNESNEFSIYHLLNPP--LISLNDLLDALEEKGYSIKEVSYE-EW 290
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 1506-1972 1.60e-96

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 321.35  E-value: 1.60e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1506 PEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFML 1585
Cdd:cd17656     2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1586 GDAVPVAAVTTAGLRSRLA---GHDLPIIDVVdalaaYPGTPPPMPAAVN---LAYILYTSGTTGEPKGVGITHRNVTRL 1659
Cdd:cd17656    82 LDSGVRVVLTQRHLKSKLSfnkSTILLEDPSI-----SQEDTSNIDYINNsddLLYIIYTSGTTGKPKGVQLEHKNMVNL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1660 FA---SLPARLSAAQVWsQCHSYGFDASAWEIWGALLGGGRLVIVPESVAaspndfhgLLVAEHVSVLTQTPAAVAMLPT 1736
Cdd:cd17656   157 LHferEKTNINFSDKVL-QFATCSFDVCYQEIFSTLLSGGTLYIIREETK--------RDVEQLFDLVKRHNIEVVFLPV 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1737 QGLESVA---------------LVVAGEACPAA--LVDRWAPGRVML-NAYGPTETTICAAIS-APLRPGSGMPPIGVPV 1797
Cdd:cd17656   228 AFLKFIFserefinrfptcvkhIITAGEQLVITneFKEMLHEHNVHLhNHYGPSETHVVTTYTiNPEAEIPELPPIGKPI 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1798 SGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFGgSGARMYRTGDLVCWRADGQLEFLGRTDD 1877
Cdd:cd17656   308 SNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFD-PNERMYRTGDLARYLPDGNIEFLGRADH 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1878 QVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYAteIAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDA 1957
Cdd:cd17656   387 QVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYF--VMEQELNISQLREYLAKQLPEYMIPSFFVPLDQ 464

                         490
                  ....*....|....*
gi 489495878 1958 LPLTVNGKLDHRALP 1972
Cdd:cd17656   465 LPLTPNGKVDRKALP 479
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 1023-1475 1.53e-93

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 311.96  E-value: 1.53e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1023 IPLSFAQRRLWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFP-AVDGVPRQLVIEARRADLgc 1101
Cdd:pfam00668    5 YPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIrQENGEPVQVILEERPFEL-- 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1102 DIVDATAWPADRLQRAIEEAAR----HSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYASRC 1177
Cdd:pfam00668   83 EIIDISDLSESEEEEAIEAFIQrdlqSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLL 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1178 AGRAPDWAPLPvQYVDYTLWQREILGDLDdsdspIAAQLAYWENALAGMPERLRLPTARPYPPVADQRGASLVVDWPASV 1257
Cdd:pfam00668  163 KGEPLPLPPKT-PYKDYAEWLQQYLQSED-----YQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDT 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1258 QQQVRRIARQHNATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGRSDPALDNLVGFFVNTLVLRVNLAGDPSFAELLGQV 1337
Cdd:pfam00668  237 EELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRV 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1338 RARSLAAYENQDVPFEVLVDRLKPTRALTHHPLIQVMLA-----WQDNPVGQLNLGDLQATPMPIDTRTARMDLVFSLAE 1412
Cdd:pfam00668  317 QEDLLSAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSfqnylGQDSQEEEFQLSELDLSVSSVIEEEAKYDLSLTASE 396

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489495878  1413 RfsEGsepaGIGGAVEYRTDVFEAQAIDVLIERLRKVLVAVAAAPERTVSSIDALDGTERARL 1475
Cdd:pfam00668  397 R--GG----GLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKL 453
Lys2b COG3320
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ...
 2108-2396 6.66e-90

Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary metabolites biosynthesis, transport and catabolism]; Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 442549 [Multi-domain]  Cd Length: 265  Bit Score: 293.65  E-value: 6.66e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2108 RTVLLTGATGFLGRYLVLELLRRldVDGRLICLVRAESDEDARRRLEKTFDSGDPELlrhfkELAADRLEVVAGDKSEPD 2187
Cdd:COG3320     1 RTVLLTGATGFLGAHLLRELLRR--TDARVYCLVRASDEAAARERLEALLERYGLWL-----ELDASRVVVVAGDLTQPR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2188 LGLDQPMWRRLAETVDLIVDSAAMVN-AFPYHELFGPNVAGTAELIRIALTTKLKPFTYVSTADVGAAIEPSAFTEDADI 2266
Cdd:COG3320    74 LGLSEAEFQELAEEVDAIVHLAALVNlVAPYSELRAVNVLGTREVLRLAATGRLKPFHYVSTIAVAGPADRSGVFEEDDL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2267 RvisptrtVDGGWAGGYGTSKWAGEVLLREANDLcALPVAVFRCGMILADTSyAGQLNMSDWVTRMVLSLMATGIAPrsf 2346
Cdd:COG3320   154 D-------EGQGFANGYEQSKWVAEKLVREARER-GLPVTIYRPGIVVGDSR-TGETNKDDGFYRLLKGLLRLGAAP--- 221

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 489495878 2347 yepdsegNRQRAHFDGLPVTFVAEAIAVLGARVAgsslAGFATYHVMNPH 2396
Cdd:COG3320   222 -------GLGDARLNLVPVDYVARAIVHLSRQPE----AAGRTFHLTNPQ 260
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 1494-1973 3.90e-89

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 299.03  E-value: 3.90e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1494 IPQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPID 1573
Cdd:COG0318     1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1574 PANPPPRVAFMLGDAVPVAAVTtaglrsrlaghdlpiidvvdalaaypgtpppmpaavnlAYILYTSGTTGEPKGVGITH 1653
Cdd:COG0318    81 PRLTAEELAYILEDSGARALVT--------------------------------------ALILYTSGTTGRPKGVMLTH 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1654 RNVTRLFASLPA--RLSAAQVWSQC----HSYGFdasAWEIWGALLGGGRLVIVPesvAASPNDFHGLLVAEHVSVLTQT 1727
Cdd:COG0318   123 RNLLANAAAIAAalGLTPGDVVLVAlplfHVFGL---TVGLLAPLLAGATLVLLP---RFDPERVLELIERERVTVLFGV 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1728 PAAVAML------PTQGLESVALVV-AGEACPAALVDRW--APGRVMLNAYGPTETTICAAISAPLRPGSGMPPIGVPVS 1798
Cdd:COG0318   197 PTMLARLlrhpefARYDLSSLRLVVsGGAPLPPELLERFeeRFGVRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLP 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1799 GAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVacpfGGsgarMYRTGDLVCWRADGQLEFLGRTDDQ 1878
Cdd:COG0318   277 GVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR----DG----WLRTGDLGRLDEDGYLYIVGRKKDM 348

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1879 VKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATeIAPGA-VDPAGLRAQLAQRLPGYLVPAAVVVIDA 1957
Cdd:COG0318   349 IISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVV-LRPGAeLDAEELRAFLRERLARYKVPRRVEFVDE 427

                         490
                  ....*....|....*.
gi 489495878 1958 LPLTVNGKLDHRALPA 1973
Cdd:COG0318   428 LPRTASGKIDRRALRE 443
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 1023-1457 1.96e-88

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 296.24  E-value: 1.96e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1023 IPLSFAQRRLWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVDGVPRQLVIEAR-RADLG- 1100
Cdd:cd19066     2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTvRFRIEi 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1101 CDIVDATAWPAdRLQRAIEEAARHSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYASRCAGR 1180
Cdd:cd19066    82 IDLRNLADPEA-RLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1181 aPDWAPLPVQYVDYTLWQREILGDLDdsdspIAAQLAYWENALAGMPERLRLPTARPYPPVADQRGASLVVDWPASVQQQ 1260
Cdd:cd19066   161 -PTLPPPVGSYADYAAWLEKQLESEA-----AQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKR 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1261 VRRIARQHNATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGRSDPALDNLVGFFVNTLVLRVNLAGDPSFAELLGQVRAR 1340
Cdd:cd19066   235 LREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQ 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1341 SLAAYENQDVPFEVLVDRLKPTRALTHHPLIQVMLAWQDNPvGQLNLGDLQATPMPIDTRTARMdlVFSLAERFSEGSeP 1420
Cdd:cd19066   315 SREAIEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQ-QQLGKTGGFIFTTPVYTSSEGT--VFDLDLEASEDP-D 390

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 489495878 1421 AGIGGAVEYRTDVFEAQAIDVLIERLRKVLVAVAAAP 1457
Cdd:cd19066   391 GDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
AMP-binding pfam00501
AMP-binding enzyme;
1498-1882 1.03e-86

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 290.75  E-value: 1.03e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1498 LAAQVARIPEAEAVCCGD-ASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPAN 1576
Cdd:pfam00501    1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1577 PPPRVAFMLGDAVPVAAVTTA------GLRSRLAGHDLPIIDVVDALAAYPGT--------------PPPMPAAVNLAYI 1636
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDalkleeLLEALGKLEVVKLVLVLDRDPVLKEEplpeeakpadvpppPPPPPDPDDLAYI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1637 LYTSGTTGEPKGVGITHRNVTRLFASL------PARLSAAQVWSQCHSYGFDAS-AWEIWGALLGGGRLVIVPESVAASP 1709
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIkrvrprGFGLGPDDRVLSTLPLFHDFGlSLGLLGPLLAGATVVLPPGFPALDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1710 NDFHGLLVAEHVSVLTQTPAAVAMLPTQGLESVA-------LVVAGEACPAALVDRWAP--GRVMLNAYGPTETTICAAI 1780
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRAllsslrlVLSGGAPLPPELARRFRElfGGALVNGYGLTETTGVVTT 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1781 SAPL-RPGSGMPPIGVPVSGAALFVLD-SWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVAcpfggsgARMYRTG 1858
Cdd:pfam00501  321 PLPLdEDLRSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE-------DGWYRTG 393

                          410       420
                   ....*....|....*....|....
gi 489495878  1859 DLVCWRADGQLEFLGRTDDQVKIR 1882
Cdd:pfam00501  394 DLGRRDEDGYLEIVGRKKDQIKLG 417
NAD_binding_4 pfam07993
Male sterility protein; This family represents the C-terminal region of the male sterility ...
 2112-2372 2.94e-77

Male sterility protein; This family represents the C-terminal region of the male sterility protein in a number of arabidopsis and drosophila. A sequence-related jojoba acyl CoA reductase is also included.


Pssm-ID: 462334 [Multi-domain]  Cd Length: 257  Bit Score: 257.15  E-value: 2.94e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2112 LTGATGFLGRYLVLELLRRLDVDGRLICLVRAESDEDARRRLEKTFDSGDPELLrhFKELAADRLEVVAGDKSEPDLGLD 2191
Cdd:pfam07993    1 LTGATGFLGKVLLEKLLRSTPDVKKIYLLVRAKDGESALERLRQELEKYPLFDA--LLKEALERIVPVAGDLSEPNLGLS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2192 QPMWRRLAETVDLIVDSAAMVN-AFPYHELFGPNVAGTAELIRIALTTK-LKPFTYVSTAdVGAAIEPSAFTEDA----- 2264
Cdd:pfam07993   79 EEDFQELAEEVDVIIHSAATVNfVEPYDDARAVNVLGTREVLRLAKQGKqLKPFHHVSTA-YVNGERGGLVEEKPypege 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2265 -DIRVISPTRTVDGGWAGGYGTSKWAGEVLLREANDlCALPVAVFRCGMILADtSYAGQLNMSDWVTRMVLSLMATGIAP 2343
Cdd:pfam07993  158 dDMLLDEDEPALLGGLPNGYTQTKWLAEQLVREAAR-RGLPVVIYRPSIITGE-PKTGWINNFDFGPRGLLGGIGKGVLP 235

                          250       260
                   ....*....|....*....|....*....
gi 489495878  2344 RSFYEPDsegnrqrAHFDGLPVTFVAEAI 2372
Cdd:pfam07993  236 SILGDPD-------AVLDLVPVDYVANAI 257
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1024-1393 9.32e-76

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 259.31  E-value: 9.32e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1024 PLSFAQRRLWFLDQ-LQRPApVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPA--VDGVPRQLVIEARRADLg 1100
Cdd:cd19532     3 PMSFGQSRFWFLQQyLEDPT-TFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTdpEDGEPMQGVLASSPLRL- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1101 cDIVDATawPADRLQRAIEEAARHSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYASRcagr 1180
Cdd:cd19532    81 -EHVQIS--DEAEVEEEFERLKNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQ---- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1181 apDWAPLPVQYVDYTLWQREIL--GDLDDsdspiaaQLAYWENALAGMPER---LRLPTARPYPPVA--DQRGASLVVDw 1253
Cdd:cd19532   154 --PLLPPPLQYLDFAARQRQDYesGALDE-------DLAYWKSEFSTLPEPlplLPFAKVKSRPPLTryDTHTAERRLD- 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1254 pASVQQQVRRIARQHNATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGRSDPALDNLVGFFVNTLVLRVNLAGDPSFAEL 1333
Cdd:cd19532   224 -AALAARIKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADV 302

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1334 LGQVRARSLAAYENQDVPFEVLVDRLKPTRALTHHPLIQVMLAWQDNPVGQLNLGDLQAT 1393
Cdd:cd19532   303 LKETRDKAYAALAHSRVPFDVLLDELGVPRSATHSPLFQVFINYRQGVAESRPFGDCELE 362
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 1025-1271 6.72e-73

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 244.18  E-value: 6.72e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1025 LSFAQRRLWFLDQlqrPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVDGVPRQLVIEArrADLGCDIV 1104
Cdd:COG4908     1 LSPAQKRFLFLEP---GSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPD--ADLPLEVV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1105 DATAWPA----DRLQRAIEEAARHSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYASRCAGR 1180
Cdd:COG4908    76 DLSALPEpereAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1181 APDWAPLPVQYVDYTLWQREILGDLDdsdspIAAQLAYWENALAGMPERLRLPTARPYPPVADQRGASLVVDWPASVQQQ 1260
Cdd:COG4908   156 PPPLPELPIQYADYAAWQRAWLQSEA-----LEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEA 230

                         250
                  ....*....|.
gi 489495878 1261 VRRIARQHNAT 1271
Cdd:COG4908   231 LKALAKAHGAT 241
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1023-1378 6.50e-69

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 239.85  E-value: 6.50e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1023 IPLSFAQRRLWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVDGVPRQLVIEARRADLGCD 1102
Cdd:cd20483     2 RPMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIVI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1103 IVDATAWPADRLQRAIEEAARHSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYASRCAGRAP 1182
Cdd:cd20483    82 DLSEAADPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGRDL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1183 D-WAPLPVQYVDYTLWQREILgdlddSDSPIAAQLAYWENALAGMPERLR-LPTA-RPYPPVADQRGASLVVDWPASVQQ 1259
Cdd:cd20483   162 AtVPPPPVQYIDFTLWHNALL-----QSPLVQPLLDFWKEKLEGIPDASKlLPFAkAERPPVKDYERSTVEATLDKELLA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1260 QVRRIARQHNATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGRSDPALDNLVGFFVNTLVLRVNLAGDPSFAELLGQVRA 1339
Cdd:cd20483   237 RMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKT 316

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 489495878 1340 RSLAAYENQDVPFEVLVDRLKPTRALTHHPLIQVMLAWQ 1378
Cdd:cd20483   317 TCLEAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQ 355
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 575-1281 1.04e-66

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 250.54  E-value: 1.04e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  575 AYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARLVRSAAMKTGDLAA 654
Cdd:COG1020   620 AYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAA 699

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  655 LVDDLVARETTIVDLPTAVWQLLCADGDAidaiGRSRLRQIVIGGEAIRCSAVDKWLEsaASQGISLLSSYGPTEATVVA 734
Cdd:COG1020   700 LAELLARHRVTVLNLTPSLLRALLDAAPE----ALPSLRLVLVGGEALPPELVRRWRA--RLPGARLVNLYGPTETTVDS 773

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  735 TFLPivCDQTTMDGALLRLGRPIlPNTVFL------------AFGEVVIVGDLVADGYLGIDG--------DGFGtvtaA 794
Cdd:COG1020   774 TYYE--VTPPDADGGSVPIGRPI-ANTRVYvldahlqpvpvgVPGELYIGGAGLARGYLNRPEltaerfvaDPFG----F 846

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  795 DGSrrRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAVELHSGSLG----VWFKSQRTR 870
Cdd:COG1020   847 PGA--RLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGdkrlVAYVVPEAG 924

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  871 EGEQDAAAATRIRLVLVSLGVSSFFVVgVPNIPRKPNGKIDSDNLPRLPQWSAAGLNTAETGQRAAGLSQIWSRQLGRAI 950
Cdd:COG1020   925 AAAAAALLRLALALLLPPYMVPAAVVL-LLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVV 1003

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  951 GPDSSLLGEGIGSLDLIRILPETRRYLGWRLSLLDLIGADTAANLADYAPTPDAPTGedrfRPLVAAQRPAAIPLSFAQR 1030
Cdd:COG1020  1004 GDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAA----APLAAAAAPLPLPPLLLSL 1079

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1031 RLWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVDGVPRQLVIEARRADLGCDIVDATAWP 1110
Cdd:COG1020  1080 LALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLA 1159

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1111 ADRLQRAIEEAARHSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYASRCAGRAPDWAPLPVQ 1190
Cdd:COG1020  1160 AAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLA 1239

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1191 YVDYTLWQREiLGDLDDSDSPIAAQLAYWENALAGMPERLRLPTARPYPPVADQRGASLVVDWPASVQQQVRRIARQHNA 1270
Cdd:COG1020  1240 LLALAALLAL-AALAALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLL 1318

                         730
                  ....*....|.
gi 489495878 1271 TSFMVVAAGLA 1281
Cdd:COG1020  1319 LLLALLLLALL 1329
PRK12316 PRK12316
peptide synthase; Provisional
 359-1339 1.50e-66

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 252.57  E-value: 1.50e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  359 ATDIGPVEGMTVASVLDEEQRTLNLAIWNRADLPACKTHPKVAERIAAALESMAAMWDRPIAMIVND------------- 425
Cdd:PRK12316 2957 AAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENpqrsvdelamlda 3036

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  426 --WFGIGPDGTRCQGDWP-------------ARQPSTPAWFLDSARGVHQFLGRRrfVYPWVAWLVQRGAAPgDVLVFTD 490
Cdd:PRK12316 3037 eeRGQLLEAWNATAAEYPlergvhrlfeeqvERTPDAVALAFGEQRLSYAELNRR--ANRLAHRLIERGVGP-DVLVGVA 3113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  491 DDTDKTIDL-LIACHLAGCGYSVCDTADEISVRTNAITEHGDGILVTVVDVAATQLAVVGHDELRKVVDERVTQVTHDAL 569
Cdd:PRK12316 3114 VERSLEMVVgLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDENYAEANPAIRT 3193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  570 LATKTAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARLVRSAAMKT 649
Cdd:PRK12316 3194 MPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDW 3273

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  650 GDLAALVDDLvarETTIVDLPTAVWQLLCADGDAIDAIGRSRLRQIVIGGEAIRCSAVDKWLesaasQGISLLSSYGPTE 729
Cdd:PRK12316 3274 RDPALLVELI---NSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVF-----AGLPLYNLYGPTE 3345

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  730 ATVVATFLPIVCDQTtmdgALLRLGRPILPNTVFL-----------AFGEVVIVGDLVADGYL---GIDGDGFGTVTAAD 795
Cdd:PRK12316 3346 ATITVTHWQCVEEGK----DAVPIGRPIANRACYIldgslepvpvgALGELYLGGEGLARGYHnrpGLTAERFVPDPFVP 3421

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  796 GSrrRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAVELHSGSLGVWFKSQRTREGEQD 875
Cdd:PRK12316 3422 GE--RLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQLVAYVVPEDEAGDLR 3499

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  876 AAAATRIRLVLVSLGVSSFFVVgVPNIPRKPNGKIDSDNLPRLpqwSAAGLNT---AETGQRAAGLSQIWSRQLGRA-IG 951
Cdd:PRK12316 3500 EALKAHLKASLPEYMVPAHLLF-LERMPLTPNGKLDRKALPRP---DAALLQQdyvAPVNELERRLAAIWADVLKLEqVG 3575

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  952 PDSSLLGEGIGSLDLIRILPETRRyLGWRLSLLDLIGADTAANLADYAPTPDAP-------TGEdrfRPLVAAQRpAAIP 1024
Cdd:PRK12316 3576 LTDNFFELGGDSIISLQVVSRARQ-AGIRFTPKDLFQHQTIQGLARVARVGGGVavdqgpvSGE---TLLLPIQQ-QFFE 3650

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1025 LSFAQRRLWFLDQLqrpapvynmavaLRLRGYLDTEALGAAVADVVGRHESLRTVFPAVDG--VPRQLVIEARRADLgcd 1102
Cdd:PRK12316 3651 EPVPERHHWNQSLL------------LKPREALDAAALEAALQALVEHHDALRLRFVEDAGgwTAEHLPVELGGALL--- 3715

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1103 iVDATAWPADRLQRAIEEAARhSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYASRCAGRAP 1182
Cdd:PRK12316 3716 -WRAELDDAEELERLGEEAQR-SLDLADGPLLRALLATLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAP 3793

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1183 DWAPLPVQYVDYTLWQREILGdlddsDSPIAAQLAYWENALAGMPERLRL--PTARPYPPVADQRGASLVVDWPASVQQQ 1260
Cdd:PRK12316 3794 RLPAKTSSFKAWAERLQEHAR-----GEALKAELAYWQEQLQGVSSELPCdhPQGALQNRHAASVQTRLDRELTRRLLQQ 3868

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1261 VRRIAR-QHNAtsfmVVAAGLAVLLSKLSGSPDVAVGFPIAGR----SDPALDNLVGFFVNTLVLRVNLAGD--PSFAEL 1333
Cdd:PRK12316 3869 APAAYRtQVND----LLLTALARVVCRWTGEASALVQLEGHGRedlfADIDLSRTVGWFTSLFPVRLSPVEDlgASIKAI 3944


                  ....*.
gi 489495878 1334 LGQVRA 1339
Cdd:PRK12316 3945 KEQLRA 3950
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 1024-1457 7.96e-64

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 224.77  E-value: 7.96e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1024 PLSFAQRRLWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVF-PAVDGVPRQLVIEARRADLgcD 1102
Cdd:cd19543     3 PLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFvWEGLGEPLQVVLKDRKLPW--R 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1103 IVDATAWPADRLQRAIEEAA----RHSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYASRCA 1178
Cdd:cd19543    81 ELDLSHLSEAEQEAELEALAeedrERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1179 GRAPDwAPLPVQYVDYTLWqreilgdLDDSDSpiAAQLAYWENALAGMPERLRLPTARPYPPVADQRGASLVVDWPASVQ 1258
Cdd:cd19543   161 GQPPS-LPPVRPYRDYIAW-------LQRQDK--EAAEAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELT 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1259 QQVRRIARQHNATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGR-SD-PALDNLVGFFVNTLVLRVNLAGDPSFAELLGQ 1336
Cdd:cd19543   231 ARLQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRpAElPGIETMVGLFINTLPVRVRLDPDQTVLELLKD 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1337 VRARSLAAYENQDVPfevLVDRLKptRALTHHPLIQVMLAWQDNPVGQLNLGDLQATPMPIDTRTARMDLVFSLAERFSE 1416
Cdd:cd19543   311 LQAQQLELREHEYVP---LYEIQA--WSEGKQALFDHLLVFENYPVDESLEEEQDEDGLRITDVSAEEQTNYPLTVVAIP 385

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 489495878 1417 GSEpagIGGAVEYRTDVFEAQAIDVLIERLRKVLVAVAAAP 1457
Cdd:cd19543   386 GEE---LTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
1506-1971 7.09e-63

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 224.77  E-value: 7.09e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1506 PEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFML 1585
Cdd:PRK04813   16 PDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIEMII 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1586 GDAVPVAAVTTAGLRsrLAGHDLPIIDVVDALAA-YPGTPPPMPAAV---NLAYILYTSGTTGEPKGVGITHRNV----- 1656
Cdd:PRK04813   96 EVAKPSLIIATEELP--LEILGIPVITLDELKDIfATGNPYDFDHAVkgdDNYYIIFTSGTTGKPKGVQISHDNLvsftn 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1657 --TRLFAslparLSAAQVW-SQChSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAEHVSVLTQTPAAVAM 1733
Cdd:PRK04813  174 wmLEDFA-----LPEGPQFlNQA-PYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVWVSTPSFADM 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1734 ---LPTQGLESV-ALVV---AGEACPA----ALVDRWAPGRVMlNAYGPTETTIcaAISA------------PLrpgsgm 1790
Cdd:PRK04813  248 cllDPSFNEEHLpNLTHflfCGEELPHktakKLLERFPSATIY-NTYGPTEATV--AVTSieitdemldqykRL------ 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1791 pPIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFvacpFGGSGARMYRTGDLVcWRADGQLE 1870
Cdd:PRK04813  319 -PIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAF----FTFDGQPAYHTGDAG-YLEDGLLF 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1871 FLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIaredrPGDK-----RLVGYateIAPGAVD-------PAGLRAQ 1938
Cdd:PRK04813  393 YQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVV-----PYNKdhkvqYLIAY---VVPKEEDferefelTKAIKKE 464

                         490       500       510
                  ....*....|....*....|....*....|...
gi 489495878 1939 LAQRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:PRK04813  465 LKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 1633-1967 7.86e-63

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 218.69  E-value: 7.86e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1633 LAYILYTSGTTGEPKGVGITHRNVTRLFASL--PARLSAAQVWSQCHSYGFDASAWEIWGALLGGGRLVIVPESVAASPN 1710
Cdd:cd04433     2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALaaSGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1711 DfhgLLVAEHVSVLTQTPAAVAMLPTQGLES-------VALVVAGEACPAALVDRW--APGRVMLNAYGPTETTICAAIS 1781
Cdd:cd04433    82 E---LIEREKVTILLGVPTLLARLLKAPESAgydlsslRALVSGGAPLPPELLERFeeAPGIKLVNGYGLTETGGTVATG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1782 APLRPGSGMPPIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFvacpfggsGARMYRTGDLV 1861
Cdd:cd04433   159 PPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD--------EDGWYRTGDLG 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1862 CWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATEIAPGAVDPAGLRAQLAQ 1941
Cdd:cd04433   231 RLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRE 310

                         330       340
                  ....*....|....*....|....*.
gi 489495878 1942 RLPGYLVPAAVVVIDALPLTVNGKLD 1967
Cdd:cd04433   311 RLAPYKVPRRVVFVDALPRTASGKID 336
PRK12316 PRK12316
peptide synthase; Provisional
 575-1327 5.51e-58

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 224.07  E-value: 5.51e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  575 AYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARLVRSAAMKTGDLAA 654
Cdd:PRK12316  658 AYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAK 737

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  655 LVdDLVARE--TTIVDLPTAVWQLLCADGDAidaiGRSRLRQIVIGGEAIRCSAVDKwLESAASQGiSLLSSYGPTEATV 732
Cdd:PRK12316  738 LV-ELINREgvDTLHFVPSMLQAFLQDEDVA----SCTSLRRIVCSGEALPADAQEQ-VFAKLPQA-GLYNLYGPTEAAI 810

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  733 VATFLPIVCDqttmDGALLRLGRPILPNTVFL-----------AFGEVVIVGDLVADGYLG---IDGDGFGTVTAADGSR 798
Cdd:PRK12316  811 DVTHWTCVEE----GGDSVPIGRPIANLACYIldanlepvpvgVLGELYLAGRGLARGYHGrpgLTAERFVPSPFVAGER 886

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  799 RraFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAVELHSGSLGVWFKSQRTREGEQDAAA 878
Cdd:PRK12316  887 M--YRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQLVGYVVLESEGGDWREAL 964

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  879 ATRIRLVLVSLGVSSFFVVgVPNIPRKPNGKIDSDNLPRLPQWSAAGLNTAETGQRAAGLSQIWSRQLG-RAIGPDSSLL 957
Cdd:PRK12316  965 KAHLAASLPEYMVPAQWLA-LERLPLTPNGKLDRKALPAPEASVAQQGYVAPRNALERTLAAIWQDVLGvERVGLDDNFF 1043

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  958 GEGIGSLDLIRILPETRRyLGWRLSLLDLIGADTAANLADYAptpdaptgedRFRPLVAA-QRPAA--IPLSFAQRRLWF 1034
Cdd:PRK12316 1044 ELGGDSIVSIQVVSRARQ-AGIQLSPRDLFQHQTIRSLALVA----------KAGQATAAdQGPASgeVALAPVQRWFFE 1112

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1035 LDQLQRPApvYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVDGVPRQLVIEARRADLgcdIVDATAWPADRL 1114
Cdd:PRK12316 1113 QAIPQRQH--WNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGWQQAYAAPQAGEV---LWQRQAASEEEL 1187

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1115 QRAIEEAARhSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYASRCAGrapdwapLPVQYVDY 1194
Cdd:PRK12316 1188 LALCEEAQR-SLDLEQGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLDAD-------LPARTSSY 1259

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1195 TLWQREilgdLDDSDSPIAAQLAYWENALAGMPErlRLPTARPYPPVADQRGASLVVDWPASVQQQVRRIARQHNATSFM 1274
Cdd:PRK12316 1260 QAWARR----LHEHAGARAEELDYWQAQLEDAPH--ELPCENPDGALENRHERKLELRLDAERTRQLLQEAPAAYRTQVN 1333

                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 489495878 1275 -VVAAGLAVLLSKLSGSPDVAVGFPIAGRSDPA----LDNLVGFFVNTLVLRVNLAGD 1327
Cdd:PRK12316 1334 dLLLTALARVTCRWSGQASVLVQLEGHGREDLFedidLSRTVGWFTSLFPVRLTPAAD 1391
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
 1024-1457 8.45e-57

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 204.14  E-value: 8.45e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1024 PLSFAQRRLWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVDGVPRQLVIEARRADLgcDI 1103
Cdd:cd19533     3 PLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPI--RH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1104 VDATAWPADR--LQRAIEEAARHSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYASRCAGRA 1181
Cdd:cd19533    81 IDLSGDPDPEgaAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGRP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1182 PDWAPLPvQYVDYtlwqreILGDLDDSDSP-IAAQLAYWENALAGMPERLRLPTARPYPPVADQRGAslvVDWPASVQQQ 1260
Cdd:cd19533   161 APPAPFG-SFLDL------VEEEQAYRQSErFERDRAFWTEQFEDLPEPVSLARRAPGRSLAFLRRT---AELPPELTRT 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1261 VRRIARQHNATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGRSDPALDNLVGFFVNTLVLRVNLAGDPSFAELLGQVRAR 1340
Cdd:cd19533   231 LLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRE 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1341 SLAAYENQDVPFEVLVDRLKPTRALTH--HPLIQVMlAWQdnpvGQLNLGDLQATPMPIDTRTARmDLVFSLAERFSEGs 1418
Cdd:cd19533   311 LRSLLRHQRYRYEDLRRDLGLTGELHPlfGPTVNYM-PFD----YGLDFGGVVGLTHNLSSGPTN-DLSIFVYDRDDES- 383

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 489495878 1419 epaGIGGAVEYRTDVFEAQAIDVLIERLRKVLVAVAAAP 1457
Cdd:cd19533   384 ---GLRIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
1517-1971 9.28e-52

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 193.40  E-value: 9.28e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1517 SMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVTT 1596
Cdd:COG0365    39 TLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITA 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1597 AGLRSRlaGHDLPIIDVVDALAA------------YPGTPPPMPAAVNL---------------------AYILYTSGTT 1643
Cdd:COG0365   119 DGGLRG--GKVIDLKEKVDEALEelpslehvivvgRTGADVPMEGDLDWdellaaasaefepeptdaddpLFILYTSGTT 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1644 GEPKGVGITHRNVTrLFASLPARL-----------SAAQV-WSQCHSYGfdasaweIWGALLGGGRLVIVPES-VAASPN 1710
Cdd:COG0365   197 GKPKGVVHTHGGYL-VHAATTAKYvldlkpgdvfwCTADIgWATGHSYI-------VYGPLLNGATVVLYEGRpDFPDPG 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1711 DFHGLLVAEHVSVLTQTPAAVAMLPTQGLESVA---------LVVAGEACPAALVDRW--APGRVMLNAYGPTETT---I 1776
Cdd:COG0365   269 RLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKkydlsslrlLGSAGEPLNPEVWEWWyeAVGVPIVDGWGQTETGgifI 348

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1777 CAAISAPLRPGSgmppIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVG--VGYWRRAGLTASRFVACPFGgsgarM 1854
Cdd:COG0365   349 SNLPGLPVKPGS----MGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPWPGmfRGYWNDPERYRETYFGRFPG-----W 419

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1855 YRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATeIAPGAVDPAG 1934
Cdd:COG0365   420 YRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVV-LKPGVEPSDE 498

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 489495878 1935 LRAQL----AQRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:COG0365   499 LAKELqahvREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 558-911 2.50e-51

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 188.89  E-value: 2.50e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  558 DERVTQVTHDA----LL--ATKTAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEI 631
Cdd:cd05930    73 AERLAYILEDSgaklVLtdPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEI 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  632 FGGAACGARLVRSAAMKTGDLAALVDDLVARETTIVDLPTAVWQLLCADGDAIDAigrSRLRQIVIGGEAIRCSAVDKWL 711
Cdd:cd05930   153 FGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAAL---PSLRLVLVGGEALPPDLVRRWR 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  712 EsaASQGISLLSSYGPTEATVVATFlpIVCDQTTMDGALLRLGRPIlPNTVFL------------AFGEVVIVGDLVADG 779
Cdd:cd05930   230 E--LLPGARLVNLYGPTEATVDATY--YRVPPDDEEDGRVPIGRPI-PNTRVYvldenlrpvppgVPGELYIGGAGLARG 304

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  780 YLGIDGDgfgtvTAA------DGSRRRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:cd05930   305 YLNRPEL-----TAErfvpnpFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAV 379

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489495878  854 ELHSGSLGvwfkSQR-----TREGEQDAAAAT---RIRLVLVSLGVSSFFVVgVPNIPRKPNGKID 911
Cdd:cd05930   380 VAREDGDG----EKRlvayvVPDEGGELDEEElraHLAERLPDYMVPSAFVV-LDALPLTPNGKVD 440
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 575-916 7.29e-50

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 184.88  E-value: 7.29e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  575 AYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARLVRSAAMKTGDLAA 654
Cdd:cd17649    97 AYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADE 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  655 LVDDLVARETTIVDLPTAVWQLLCADGDAIDAIGRSRLRQIVIGGEAIRCSAVDKWLesaaSQGISLLSSYGPTEATVVA 734
Cdd:cd17649   177 LAEMVRELGVTVLDLPPAYLQQLAEEADRTGDGRPPSLRLYIFGGEALSPELLRRWL----KAPVRLFNAYGPTEATVTP 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  735 TFLPIVCDqTTMDGALLRLGRPILPNTVFL-----------AFGEVVIVGDLVADGYLGIDG--------DGFGtvtaAD 795
Cdd:cd17649   253 LVWKCEAG-AARAGASMPIGRPLGGRSAYIldadlnpvpvgVTGELYIGGEGLARGYLGRPEltaerfvpDPFG----AP 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  796 GSrrRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAVELHSGSLG-------VWfkSQR 868
Cdd:cd17649   328 GS--RLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGkqlvayvVL--RAA 403

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 489495878  869 TREGEQDAAAATRIRLVLVSLGVSSFFVVgVPNIPRKPNGKIDSDNLP 916
Cdd:cd17649   404 AAQPELRAQLRTALRASLPDYMVPAHLVF-LARLPLTPNGKLDRKALP 450
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 500-853 7.34e-50

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 183.62  E-value: 7.34e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878   500 LIACHLAGCGYSVCDTADEISvRTNAITEHGD-GILVTVVDVAATQLAVVGH------DELRKVVDERVTQVTHDALLAT 572
Cdd:TIGR01733   42 ILAVLKAGAAYVPLDPAYPAE-RLAFILEDAGaRLLLTDSALASRLAGLVLPvilldpLELAALDDAPAPPPPDAPSGPD 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878   573 KTAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARL-VRSAAMkTGD 651
Cdd:TIGR01733  121 DLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLvVPPEDE-ERD 199

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878   652 LAALVDDLVA-RETTIVDLPTAVWQLLcadgDAIDAIGRSRLRQIVIGGEAIRCSAVDKWLESAasQGISLLSSYGPTEA 730
Cdd:TIGR01733  200 DAALLAALIAeHPVTVLNLTPSLLALL----AAALPPALASLRLVILGGEALTPALVDRWRARG--PGARLINLYGPTET 273

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878   731 TVVATFLPiVCDQTTMDGALLRLGRPIlPNTVFL------------AFGEVVIVGDLVADGYLGIDG---DGFGTVTAAD 795
Cdd:TIGR01733  274 TVWSTATL-VDPDDAPRESPVPIGRPL-ANTRLYvldddlrpvpvgVVGELYIGGPGVARGYLNRPEltaERFVPDPFAG 351

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 489495878   796 GSRRRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:TIGR01733  352 GDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
 1494-1971 9.78e-50

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 185.07  E-value: 9.78e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1494 IPQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPID 1573
Cdd:cd05936     1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1574 PANPPPRVAFMLGDAVPVAAVTTAGLRSRLAghdlpiidvvdalAAYPGTPPPMPAAVNLAYILYTSGTTGEPKGVGITH 1653
Cdd:cd05936    81 PLYTPRELEHILNDSGAKALIVAVSFTDLLA-------------AGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTH 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1654 RNVTrlfaslpARLSAAQVWSQC---------------HSYGFDASaweIWGALLGGGRLVIVPEsvaASPNDFHGLLVA 1718
Cdd:cd05936   148 RNLV-------ANALQIKAWLEDllegddvvlaalplfHVFGLTVA---LLLPLALGATIVLIPR---FRPIGVLKEIRK 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1719 EHVSVLTQTPAAVAMLPTQ------GLESVALVVAGEA-CPAALVDRW--APGRVMLNAYGPTET---TICAAISAPLRP 1786
Cdd:cd05936   215 HRVTIFPGVPTMYIALLNApefkkrDFSSLRLCISGGApLPVEVAERFeeLTGVPIVEGYGLTETspvVAVNPLDGPRKP 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1787 GSgmppIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVacpfggSGArmYRTGDLVCWRAD 1866
Cdd:cd05936   295 GS----IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV------DGW--LRTGDIGYMDED 362

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1867 GQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATEIAPGAVDPAGLRAQLAQRLPGY 1946
Cdd:cd05936   363 GYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGY 442

                         490       500
                  ....*....|....*....|....*
gi 489495878 1947 LVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:cd05936   443 KVPRQVEFRDELPKSAVGKILRREL 467
PRK12467 PRK12467
peptide synthase; Provisional
 575-1199 1.54e-49

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 196.15  E-value: 1.54e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  575 AYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARLVrSAAMKTGDLAA 654
Cdd:PRK12467 3240 AYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLV-VRDNDLWDPEE 3318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  655 LVDDLVARETTIVDLPTAVWQLLCADGDAIDAigrSRLRQIVIGGEAIRCSAVDKwLESAASQgISLLSSYGPTEATVVA 734
Cdd:PRK12467 3319 LWQAIHAHRISIACFPPAYLQQFAEDAGGADC---ASLDIYVFGGEAVPPAAFEQ-VKRKLKP-RGLTNGYGPTEAVVTV 3393

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  735 TFLPIVCDQTTMDGAlLRLGRPILPNTVFL-----------AFGEVVIVGDLVADGYL---GIDGDGFGTvTAADGSRRR 800
Cdd:PRK12467 3394 TLWKCGGDAVCEAPY-APIGRPVAGRSIYVldgqlnpvpvgVAGELYIGGVGLARGYHqrpSLTAERFVA-DPFSGSGGR 3471

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  801 AFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAVELHSGSLGVWFKSQRTREGEQDAAAAT 880
Cdd:PRK12467 3472 LYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPADPQGDWRET 3551

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  881 RIRLVLVSLG---VSSFFVVgVPNIPRKPNGKIDSDNLPRlPQWSAAGLNTAETGQRAAGLSQIWSRQLGRA-IGPDSSL 956
Cdd:PRK12467 3552 LRDHLAASLPdymVPAQLLV-LAAMPLGPNGKVDRKALPD-PDAKGSREYVAPRSEVEQQLAAIWADVLGVEqVGVTDNF 3629

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  957 LGEGIGSLDLIRILPETRRYLGWRLSLLDLIGADTAANLADYAPTPDAPtgedrfrplvaaQRPAaiplsfaqrrlwfld 1036
Cdd:PRK12467 3630 FELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYSPLGDVP------------VNLL--------------- 3682

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1037 qlqrpapvynmavalrlrgyLDTEALGAAVADVVGRHESLRTVFpavDGVPRQLVIEarradlgcdivdatawpadrlqr 1116
Cdd:PRK12467 3683 --------------------LDLNRLETGFPALFCRHEGLGTVF---DYEPLAVILE----------------------- 3716

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1117 aieeaarhsfdlateiplrtwlfriaDDEHVLVAVAHHIAADGWSVapltadlsaayasrcagraPDWAPLPVQYVDYTL 1196
Cdd:PRK12467 3717 --------------------------GDRHVLGLTCRHLLDDGWQD-------------------TSLQAMAVQYADYIL 3751


                  ...
gi 489495878 1197 WQR 1199
Cdd:PRK12467 3752 WQQ 3754
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
 1502-1967 1.69e-49

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 183.58  E-value: 1.69e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1502 VARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRV 1581
Cdd:cd17631     5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1582 AFMLGDAvpvaavttaglRSRLAGHDLpiidvvdalaaypgtpppmpaavnlAYILYTSGTTGEPKGVGITHRNVT---- 1657
Cdd:cd17631    85 AYILADS-----------GAKVLFDDL-------------------------ALLMYTSGTTGRPKGAMLTHRNLLwnav 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1658 RLFASLPAR-----LSAAQVwsqCHSYGFDASaweIWGALLGGGRLVIVPESVAASpndFHGLLVAEHVSVLTQTPAAVA 1732
Cdd:cd17631   129 NALAALDLGpddvlLVVAPL---FHIGGLGVF---TLPTLLRGGTVVILRKFDPET---VLDLIERHRVTSFFLVPTMIQ 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1733 ML------PTQGLESV-ALVVAGEACPAALVDRW-APGRVMLNAYGPTETTICAAISAP----LRPGSgmppIGVPVSGA 1800
Cdd:cd17631   200 ALlqhprfATTDLSSLrAVIYGGAPMPERLLRALqARGVKFVQGYGMTETSPGVTFLSPedhrRKLGS----AGRPVFFV 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1801 ALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFvacpFGGsgarMYRTGDLVCWRADGQLEFLGRTDDQVK 1880
Cdd:cd17631   276 EVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF----RDG----WFHTGDLGRLDEDGYLYIVDRKKDMII 347

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1881 IRGYRIELGEVATALAELAGVGQAVVIARED-RPGDkrlVGYA-TEIAPGA-VDPAGLRAQLAQRLPGYLVPAAVVVIDA 1957
Cdd:cd17631   348 SGGENVYPAEVEDVLYEHPAVAEVAVIGVPDeKWGE---AVVAvVVPRPGAeLDEDELIAHCRERLARYKIPKSVEFVDA 424

                         490
                  ....*....|
gi 489495878 1958 LPLTVNGKLD 1967
Cdd:cd17631   425 LPRNATGKIL 434
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
 1515-1971 3.37e-49

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 183.06  E-value: 3.37e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1515 DASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAvpvaav 1594
Cdd:cd17654    14 DTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKC------ 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1595 ttagLRSRLAGHDLpiiDVVDALAAYPGTPP-PMPAAVNLAYILYTSGTTGEPKGVGITHRNVTRLFASLPA--RLSAAQ 1671
Cdd:cd17654    88 ----HVSYLLQNKE---LDNAPLSFTPEHRHfNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSlfNITSED 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1672 VWSQCHSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAEH-VSVLTQTPAAVAMLPTQ--------GLESV 1742
Cdd:cd17654   161 ILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILFKRHrITVLQATPTLFRRFGSQsikstvlsATSSL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1743 A-LVVAGEACPAALVDR-WAP---GRVMLNAYGPTETTiCAAISAPLRPGSGMPPIGVPVSGAALFVLDSwlrpVPAGVA 1817
Cdd:cd17654   241 RvLALGGEPFPSLVILSsWRGkgnRTRIFNIYGITEVS-CWALAYKVPEEDSPVQLGSPLLGTVIEVRDQ----NGSEGT 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1818 GELYIAG-AGVGvgywrragltasrFVACPFGGSGARMYRTGDLVCwRADGQLEFLGRTDDQVKIRGYRIELGEVATALA 1896
Cdd:cd17654   316 GQVFLGGlNRVC-------------ILDDEVTVPKGTMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQVIE 381

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489495878 1897 ELAGVgQAVVIAREDrpgDKRLVGYATeiAPGAVDPAGLRAQLAQrLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:cd17654   382 SCLGV-ESCAVTLSD---QQRLIAFIV--GESSSSRIHKELQLTL-LSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
 1497-1973 4.00e-46

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 175.74  E-value: 4.00e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1497 MLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPAN 1576
Cdd:TIGR03098    5 LLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLL 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1577 PPPRVAFMLGDAVPVAAVTTAGLRSRL-----AGHDLPIIDVVDALA-AYPGTPPPMPAAV------------------N 1632
Cdd:TIGR03098   85 KAEQVAHILADCNVRLLVTSSERLDLLhpalpGCHDLRTLIIVGDPAhASEGHPGEEPASWpkllalgdadpphpvidsD 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1633 LAYILYTSGTTGEPKGVGITHRNVT----------------RLFASLParlsaaqvwsqchsYGFDASAWEIWGALLGGG 1696
Cdd:TIGR03098  165 MAAILYTSGSTGRPKGVVLSHRNLVagaqsvatylenrpddRLLAVLP--------------LSFDYGFNQLTTAFYVGA 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1697 RLVIVPESVaasPNDFHGLLVAEHVSVLTQTPAAVAML-----PTQGLESVA-LVVAGEACPAALVDR---WAPGRVMLN 1767
Cdd:TIGR03098  231 TVVLHDYLL---PRDVLKALEKHGITGLAAVPPLWAQLaqldwPESAAPSLRyLTNSGGAMPRATLSRlrsFLPNARLFL 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1768 AYGPTE---TTICAAISAPLRPGSgmppIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVA 1844
Cdd:TIGR03098  308 MYGLTEafrSTYLPPEEVDRRPDS----IGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRP 383

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1845 CPFGGSGARMYRT----GDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVG 1920
Cdd:TIGR03098  384 LPPFPGELHLPELavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVL 463

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 489495878  1921 YATEIAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRALPA 1973
Cdd:TIGR03098  464 VVTPPGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 1510-1971 6.23e-45

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 169.95  E-value: 6.23e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1510 AVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAV 1589
Cdd:cd05919     3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1590 PVAAVTTAglrsrlaghdlpiidvvDALAaypgtpppmpaavnlaYILYTSGTTGEPKGVGITHRNvTRLFASLPAR--- 1666
Cdd:cd05919    83 ARLVVTSA-----------------DDIA----------------YLLYSSGTTGPPKGVMHAHRD-PLLFADAMAReal 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1667 --------LSAAQVWsqcHSYGFDASaweIWGALLGGGRLVIVPESVaaSPNDFHGLLVAEHVSVLTQTPAAVA-MLPTQ 1737
Cdd:cd05919   129 gltpgdrvFSSAKMF---FGYGLGNS---LWFPLAVGASAVLNPGWP--TAERVLATLARFRPTVLYGVPTFYAnLLDSC 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1738 GLESVAL------VVAGEACPAALVDRWAP--GRVMLNAYGPTET--TICAAISAPLRPGSgmppIGVPVSGAALFVLDS 1807
Cdd:cd05919   201 AGSPDALrslrlcVSAGEALPRGLGERWMEhfGGPILDGIGATEVghIFLSNRPGAWRLGS----TGRPVPGYEIRLVDE 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1808 WLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVacpfGGsgarMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIE 1887
Cdd:cd05919   277 EGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN----GG----WYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVS 348

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1888 LGEVATALAELAGVGQAVVIAREDRPGDKRLVGY---ATEIAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNG 1964
Cdd:cd05919   349 PVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFvvlKSPAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATG 428


                  ....*..
gi 489495878 1965 KLDHRAL 1971
Cdd:cd05919   429 KLQRFKL 435
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 1491-1971 5.74e-44

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 169.21  E-value: 5.74e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1491 PVSIPQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYL 1570
Cdd:PRK06187    5 PLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLH 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1571 PIDPANPPPRVAFMLGDA-----------VPVAavttAGLRSRL--------------AGHDLPIIDVVDALAAYPGTPP 1625
Cdd:PRK06187   85 PINIRLKPEEIAYILNDAedrvvlvdsefVPLL----AAILPQLptvrtvivegdgpaAPLAPEVGEYEELLAAASDTFD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1626 -PMPAAVNLAYILYTSGTTGEPKGVGITHRNVT--RLFASLPARLSAAQVW----SQCHSYGfdasaweiWG----ALLG 1694
Cdd:PRK06187  161 fPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFlhSLAVCAWLKLSRDDVYlvivPMFHVHA--------WGlpylALMA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1695 GGRLVIV----PESVAAspndfhgLLVAEHVSVLTQTPAAVAML------PTQGLESVALVVAG-EACPAALVDRWA--P 1761
Cdd:PRK06187  233 GAKQVIPrrfdPENLLD-------LIETERVTFFFAVPTIWQMLlkapraYFVDFSSLRLVIYGgAALPPALLREFKekF 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1762 GRVMLNAYGPTETTICAAIsapLRPGSGMPPI-------GVPVSGAALFVLDSWLRPVPA--GVAGELYIAGAGVGVGYW 1832
Cdd:PRK06187  306 GIDLVQGYGMTETSPVVSV---LPPEDQLPGQwtkrrsaGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYW 382

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1833 RRAGLTASRFVacpfGGsgarMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDR 1912
Cdd:PRK06187  383 NRPEATAETID----GG----WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDE 454

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1913 PGDKRLVGYaTEIAPGA-VDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:PRK06187  455 KWGERPVAV-VVLKPGAtLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 475-916 1.28e-42

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 164.82  E-value: 1.28e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  475 LVQRGAAPGDVLVFTDDDTDKTIDLLIACHLAGCGYSVCDTA--DEisvRTNAITEHGDGILVTVVDVAATQLAVVGHDE 552
Cdd:cd17651    37 LRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAypAE---RLAFMLADAGPVLVLTHPALAGELAVELVAV 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  553 LRKVVDERVTQVTHD---ALLATKTAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVE 629
Cdd:cd17651   114 TLLDQPGAAAGADAEpdpALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQ 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  630 EIFGGAACGARLVRSAAMKTGDLAALVDDLVARETTIVDLPTAVWQLLCADGDAIDAIGrSRLRQIVIGGEAIRC-SAVD 708
Cdd:cd17651   194 EIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRL-AALRYLLTGGEQLVLtEDLR 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  709 KWLesAASQGISLLSSYGPTEATVV-ATFLPIVCDQTtmdGALLRLGRPIlPNT---VFLAF---------GEVVIVGDL 775
Cdd:cd17651   273 EFC--AGLPGLRLHNHYGPTETHVVtALSLPGDPAAW---PAPPPIGRPI-DNTrvyVLDAAlrpvppgvpGELYIGGAG 346

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  776 VADGYLGIDG--------DGFGTvtaadgsRRRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPA 847
Cdd:cd17651   347 LARGYLNRPEltaerfvpDPFVP-------GARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPG 419

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489495878  848 VSDVAVELHSGSLG----VWFKSQRTREGEQDAAAATRIRLVLVSLGVSSFFVVgVPNIPRKPNGKIDSDNLP 916
Cdd:cd17651   420 VREAVVLAREDRPGekrlVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVL-LDALPLTPNGKLDRRALP 491
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1525-1971 1.66e-42

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 163.38  E-value: 1.66e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1525 EASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAA----YLPIDPANPPPRVAFMLGDAVPVAAVTTAGLR 1600
Cdd:cd05922     1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1601 SRL------AGHDLPIIDVVDALAAYPGTPPPMPAAVNLAYILYTSGTTGEPKGVGITHRNVTRLFASLPARL--SAAQV 1672
Cdd:cd05922    81 DRLrdalpaSPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLgiTADDR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1673 WSQCHSYGFDASAWEIWGALLGGGRLVIVPESVAasPNDFHGLLVAEHVSVLTQTPAAVAMLPTQGLESVAL------VV 1746
Cdd:cd05922   161 ALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVL--DDAFWEDLREHGATGLAGVPSTYAMLTRLGFDPAKLpslrylTQ 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1747 AGEACPAALVDRWA---PGRVMLNAYGPTETTICAAISAPLRPGSGMPPIGVPVSGAALFVLDSWLRPVPAGVAGELYIA 1823
Cdd:cd05922   239 AGGRLPQETIARLRellPGAQVYVMYGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHR 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1824 GAGVGVGYWRR-AGLTAsrfvacpfGGSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVG 1902
Cdd:cd05922   319 GPNVMKGYWNDpPYRRK--------EGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLII 390

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489495878 1903 QAVVIAREDRPGDkRLVGYATeiAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:cd05922   391 EAAAVGLPDPLGE-KLALFVT--APDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1022-1457 8.62e-42

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 160.56  E-value: 8.62e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1022 AIPLSFAQRRLWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVDGVPRQLVIEARraDLGC 1101
Cdd:cd20484     1 RSPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSK--PLSF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1102 DIVDATAWPADRLQRAIEEAARHSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYASRCAGRA 1181
Cdd:cd20484    79 QEEDISSLKESEIIAYLREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1182 PDWAPLPVQYVDYTLWQREILGDLDDsdspiAAQLAYWENALAGMPERLRLPTARPYPPVADQRGASLVVDWPASVQQQV 1261
Cdd:cd20484   159 PTLASSPASYYDFVAWEQDMLAGAEG-----EEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQI 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1262 RRIARQHNATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGRSDPALDNLVGFFVNTLVLRVNLAGDPSFAELLGQVRARS 1341
Cdd:cd20484   234 KSFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTV 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1342 LAAYENQDVPFEVLVDRLKPTRALTHHPLIQVMLAWQdNPVGQLNLGDLQA---TPMPID-----TRTARMDLVFSLAEr 1413
Cdd:cd20484   314 LDGLDHAAYPFPAMVRDLNIPRSQANSPVFQVAFFYQ-NFLQSTSLQQFLAeyqDVLSIEfvegiHQEGEYELVLEVYE- 391

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 489495878 1414 fsegsEPAGIGGAVEYRTDVFEAQAIDVLIERLRKVLVAVAAAP 1457
Cdd:cd20484   392 -----QEDRFTLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
 1517-1971 1.10e-41

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 162.15  E-value: 1.10e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1517 SMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVTT 1596
Cdd:cd05959    29 SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVS 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1597 AGLRSRLA------GHDLPIIDVVDALAAYPGTP----------PPMPAAV----NLAYILYTSGTTGEPKGVGITHRNV 1656
Cdd:cd05959   109 GELAPVLAaaltksEHTLVVLIVSGGAGPEAGALllaelvaaeaEQLKPAAthadDPAFWLYSSGSTGRPKGVVHLHADI 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1657 tRLFASLPAR-----------LSAAQVWsqcHSYGFDASaweIWGALLGGGRLVIVPESVAasPNDFHGLLVAEHVSVLT 1725
Cdd:cd05959   189 -YWTAELYARnvlgireddvcFSAAKLF---FAYGLGNS---LTFPLSVGATTVLMPERPT--PAAVFKRIRRYRPTVFF 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1726 QTPAAVA-ML-----PTQGLESVALVV-AGEACPAALVDRWAP--GRVMLNAYGPTET--TICAAISAPLRPGSGmppiG 1794
Cdd:cd05959   260 GVPTLYAaMLaapnlPSRDLSSLRLCVsAGEALPAEVGERWKArfGLDILDGIGSTEMlhIFLSNRPGRVRYGTT----G 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1795 VPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVacpfGGsgarMYRTGDLVCWRADGQLEFLGR 1874
Cdd:cd05959   336 KPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ----GE----WTRTGDKYVRDDDGFYTYAGR 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1875 TDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGY---ATEIAPGAVDPAGLRAQLAQRLPGYLVPAA 1951
Cdd:cd05959   408 ADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFvvlRPGYEDSEALEEELKEFVKDRLAPYKYPRW 487

                         490       500
                  ....*....|....*....|
gi 489495878 1952 VVVIDALPLTVNGKLDHRAL 1971
Cdd:cd05959   488 IVFVDELPKTATGKIQRFKL 507
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 574-915 1.91e-40

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 157.08  E-value: 1.91e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  574 TAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARLV---RSAAMKTG 650
Cdd:cd17643    95 LAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVvvpYEVARSPE 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  651 DLAALVDDlvARETTIVDLPTAVWQLLCAdgDAIDAIGRSRLRQIVIGGEAIRCSAVDKWLESAASQGISLLSSYGPTEA 730
Cdd:cd17643   175 DFARLLRD--EGVTVLNQTPSAFYQLVEA--ADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLDRPQLVNMYGITET 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  731 TVVATFLPIVCDQTTmDGALLRLGRPILPNTVFL-----------AFGEVVIVGDLVADGYLGIDG---DGFGTVTAADG 796
Cdd:cd17643   251 TVHVTFRPLDAADLP-AAAASPIGRPLPGLRVYVldadgrpvppgVVGELYVSGAGVARGYLGRPEltaERFVANPFGGP 329

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  797 SRRRaFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAVELHSGSLGvwfkSQR------TR 870
Cdd:cd17643   330 GSRM-YRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPG----DTRlvayvvAD 404

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 489495878  871 EGEQDAAAATR--IRLVLVSLGVSSFFvVGVPNIPRKPNGKIDSDNL 915
Cdd:cd17643   405 DGAAADIAELRalLKELLPDYMVPARY-VPLDALPLTVNGKLDRAAL 450
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 559-911 4.41e-40

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 156.25  E-value: 4.41e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  559 ERVTQVTH----DALLATKT--AYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIF 632
Cdd:cd05945    78 ERIREILDaakpALLIADGDdnAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLY 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  633 GGAACGARLVRSAAMKTGDLAALVDDLVARETTI-VDLPTAVWQLLCADGDAIDAIGRsrLRQIVIGGEAIRCSAVDKWL 711
Cdd:cd05945   158 PALASGATLVPVPRDATADPKQLFRFLAEHGITVwVSTPSFAAMCLLSPTFTPESLPS--LRHFLFCGEVLPHKTARALQ 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  712 EsaASQGISLLSSYGPTEATVVATF-------------LPI-----VCDQTTMDGAllrlGRPILPNTVflafGEVVIVG 773
Cdd:cd05945   236 Q--RFPDARIYNTYGPTEATVAVTYievtpevldgydrLPIgyakpGAKLVILDED----GRPVPPGEK----GELVISG 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  774 DLVADGYLGIDGDGFGTVTAADGsrRRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSD-VA 852
Cdd:cd05945   306 PSVSKGYLNNPEKTAAAFFPDEG--QRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEaVV 383

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489495878  853 VELHSGSLGVWFKSQRTREGEQDAAAATRIRLVLVSL----GVSSFFVVgVPNIPRKPNGKID 911
Cdd:cd05945   384 VPKYKGEKVTELIAFVVPKPGAEAGLTKAIKAELAERlppyMIPRRFVY-LDELPLNANGKID 445
PRK05691 PRK05691
peptide synthase; Validated
 575-1323 9.44e-40

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 163.80  E-value: 9.44e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  575 AYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARLVRSAAMKTG--DL 652
Cdd:PRK05691 2336 AYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQGQWGaeEI 2415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  653 AALVddlvaRETTIVDL---PTAVWQL---LCADGDaidaigRSRLRQIVIGGEAIRCSAVDKWleSAASQGISLLSSYG 726
Cdd:PRK05691 2416 CQLI-----REQQVSILgftPSYGSQLaqwLAGQGE------QLPVRMCITGGEALTGEHLQRI--RQAFAPQLFFNAYG 2482

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  727 PTEaTVVATFLPIVCDQTTMDGALLRLGRPILPNTVFL-----------AFGEVVIVGDLVADGY---LGIDGDGF-GTV 791
Cdd:PRK05691 2483 PTE-TVVMPLACLAPEQLEEGAASVPIGRVVGARVAYIldadlalvpqgATGELYVGGAGLAQGYhdrPGLTAERFvADP 2561

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  792 TAADGSRrrAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSD---VAVELHSGSLGVWFKSQR 868
Cdd:PRK05691 2562 FAADGGR--LYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREavvLALDTPSGKQLAGYLVSA 2639

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  869 TREGEQDAAAATR------IRLVLVSLGVSSFFVVgVPNIPRKPNGKIDSDNLPrLPQWSAAGLN-TAETGQRAAGLSQI 941
Cdd:PRK05691 2640 VAGQDDEAQAALRealkahLKQQLPDYMVPAHLIL-LDSLPLTANGKLDRRALP-APDPELNRQAyQAPRSELEQQLAQI 2717

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  942 WSRQLG-RAIGPDSSLLGEGIGSLDLIRILPETRRyLGWRLSLLDLIGADTAANLADYAPTPDAPTGEDrfrplvaAQRP 1020
Cdd:PRK05691 2718 WREVLNvERVGLGDNFFELGGDSILSIQVVSRARQ-LGIHFSPRDLFQHQTVQTLAAVATHSEAAQAEQ-------GPLQ 2789

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1021 AAIPLSFAQRrlWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVDGVPR---------QLV 1091
Cdd:PRK05691 2790 GASGLTPIQH--WFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGRWQaeyravtaqELL 2867

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1092 IEARRADLGcdivDATAWPADrLQRaieeaarhSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSA 1171
Cdd:PRK05691 2868 WQVTVADFA----ECAALFAD-AQR--------SLDLQQGPLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQA 2934

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1172 AYASRCAGRAPdwaPLPVQYVDYTLWQrEILGDLDDSDSpIAAQLAYWENALAGmpERLRLPTARPYPPVADQRGASLVV 1251
Cdd:PRK05691 2935 LYRQLSAGAEP---ALPAKTSAFRDWA-ARLQAYAGSES-LREELGWWQAQLGG--PRAELPCDRPQGGNLNRHAQTVSV 3007

                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489495878 1252 DWPASVQQQV--RRIARQHNATSFMVVAAgLAVLLSKLSGSPDVAVGFPIAGRS----DPALDNLVGFFVNTLVLRVN 1323
Cdd:PRK05691 3008 RLDAERTRQLlqQAPAAYRTQVNDLLLTA-LARVLCRWSGQPSVLVQLEGHGREalfdDIDLTRSVGWFTSAYPLRLT 3084
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
 1517-1971 1.35e-39

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 154.37  E-value: 1.35e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1517 SMTYRELDEASNRLAHRL-AGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPvaavt 1595
Cdd:cd05941    11 SITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEP----- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1596 taglrsrlaghdlpiidvvdalaaypgtpppmPAAVNLAYILYTSGTTGEPKGVGITHRNVTRLFASLparlsaAQVWS- 1674
Cdd:cd05941    86 --------------------------------SLVLDPALILYTSGTTGRPKGVVLTHANLAANVRAL------VDAWRw 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1675 -------QC----HSYG-FDASAweiwGALLGGGRLVIVPESVAASPNdfhGLLVAEHVSVLTQTP-------AAVAMLP 1735
Cdd:cd05941   128 teddvllHVlplhHVHGlVNALL----CPLFAGASVEFLPKFDPKEVA---ISRLMPSITVFMGVPtiytrllQYYEAHF 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1736 TQ-------GLESVALVVAGEAC-PAALVDRWAP--GRVMLNAYGPTETTIcaAISAPL----RPGS-GMPPIGVPVsga 1800
Cdd:cd05941   201 TDpqfaraaAAERLRLMVSGSAAlPVPTLEEWEAitGHTLLERYGMTEIGM--ALSNPLdgerRPGTvGMPLPGVQA--- 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1801 aLFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFggsgarmYRTGDLVCWRADGQLEFLGRT-DDQV 1879
Cdd:cd05941   276 -RIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW-------FKTGDLGVVDEDGYYWILGRSsVDII 347

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1880 KIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGY-ATEIAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDAL 1958
Cdd:cd05941   348 KSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVvVLRAGAAALSLEELKEWAKQRLAPYKRPRRLILVDEL 427

                         490
                  ....*....|...
gi 489495878 1959 PLTVNGKLDHRAL 1971
Cdd:cd05941   428 PRNAMGKVNKKEL 440
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 575-916 4.23e-39

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 154.02  E-value: 4.23e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  575 AYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARLVRSAAMKTGDLAA 654
Cdd:cd17655   140 AYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQA 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  655 LVDDLVARETTIVDLPTAVWQLLcadgDAIDAIGRSRLRQIVIGGEAIRCSAVDKWLESAASQgISLLSSYGPTEATVVA 734
Cdd:cd17655   220 LTQYIRQNRITIIDLTPAHLKLL----DAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTN-PTITNAYGPTETTVDA 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  735 TFLPivCDQTTMDGALLRLGRPILPNTVFLA-----------FGEVVIVGDLVADGYLGIDgdgfgTVTAAD------GS 797
Cdd:cd17655   295 SIYQ--YEPETDQQVSVPIGKPLGNTRIYILdqygrpqpvgvAGELYIGGEGVARGYLNRP-----ELTAEKfvddpfVP 367

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  798 RRRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV-----ELHSGSLGVWFKSQR--TR 870
Cdd:cd17655   368 GERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVViarkdEQGQNYLCAYIVSEKelPV 447

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 489495878  871 EGEQDAAAATrirlvLVSLGVSSFFvVGVPNIPRKPNGKIDSDNLP 916
Cdd:cd17655   448 AQLREFLARE-----LPDYMIPSYF-IKLDEIPLTPNGKVDRKALP 487
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 559-916 1.40e-38

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 152.20  E-value: 1.40e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  559 ERVTQVTHDA---LLATKT---AYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIF 632
Cdd:cd17644    87 ERLTYILEDAqisVLLTQPenlAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIY 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  633 GGAACGARLV-RSAAMKTgDLAALVDDLVARETTIVDLPTAVWQLLCADGDAIDAIGRSRLRQIVIGGEAIRCSAVDKWL 711
Cdd:cd17644   167 VTLLSGATLVlRPEEMRS-SLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLPSSLRLVIVGGEAVQPELVRQWQ 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  712 EsAASQGISLLSSYGPTEATVVATFLPIVCDQTTMDGALLrLGRPIlPNT---VFLAF---------GEVVIVGDLVADG 779
Cdd:cd17644   246 K-NVGNFIQLINVYGPTEATIAATVCRLTQLTERNITSVP-IGRPI-ANTqvyILDENlqpvpvgvpGELHIGGVGLARG 322

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  780 YLG---IDGDGFGTVTAADGSRRRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAVELH 856
Cdd:cd17644   323 YLNrpeLTAEKFISHPFNSSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVR 402

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489495878  857 SGSLG-----VWFKSQRTREGeqdaaAATRIRLVLVS----LGVSSFFVVgVPNIPRKPNGKIDSDNLP 916
Cdd:cd17644   403 EDQPGnkrlvAYIVPHYEESP-----STVELRQFLKAklpdYMIPSAFVV-LEELPLTPNGKIDRRALP 465
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1519-1972 3.44e-38

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 149.75  E-value: 3.44e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1519 TYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPanppprvafmlgdavpvaavttag 1598
Cdd:cd05934     5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINT------------------------ 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1599 lrsRLAGHDLP-IIDVVDALAAYpgtpppmpaaVNLAYILYTSGTTGEPKGVGITHRNVT----------------RLFA 1661
Cdd:cd05934    61 ---ALRGDELAyIIDHSGAQLVV----------VDPASILYTSGTTGPPKGVVITHANLTfagyysarrfglgeddVYLT 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1662 SLPARLSAAQVWSqchsygfdasaweIWGALLGGGRLVIVPesvAASPNDFHGLLVAEHVSVLTQTPAAVAML------P 1735
Cdd:cd05934   128 VLPLFHINAQAVS-------------VLAALSVGATLVLLP---RFSASRFWSDVRRYGATVTNYLGAMLSYLlaqppsP 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1736 TQGLESVALVVAGEACP---AALVDRWapGRVMLNAYGPTETTIC--AAISAPLRPGSgmppIGVPVSGAALFVLDSWLR 1810
Cdd:cd05934   192 DDRAHRLRAAYGAPNPPelhEEFEERF--GVRLLEGYGMTETIVGviGPRDEPRRPGS----IGRPAPGYEVRIVDDDGQ 265

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1811 PVPAGVAGELYIAGA---GVGVGYWRRAGLTASRFVacpfGGsgarMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIE 1887
Cdd:cd05934   266 ELPAGEPGELVIRGLrgwGFFKGYYNMPEATAEAMR----NG----WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENIS 337

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1888 LGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATEIAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLD 1967
Cdd:cd05934   338 SAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVA 417


                  ....*
gi 489495878 1968 HRALP 1972
Cdd:cd05934   418 KAQLR 422
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 475-911 3.44e-38

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 151.20  E-value: 3.44e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  475 LVQRGAAPGDVLVFTDDDTDKTIDLLIACHLAGCGYSVCDTADEISVRTNAITEHGDGILVT----VVDVAATQLAVVGH 550
Cdd:cd12117    39 LRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLTdrslAGRAGGLEVAVVID 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  551 DELrkvvDERVTQVTHDALLATKTAYIMPTSGTTGQPKLVRISHGSLAVFCdAISRAYGWGAHDTVLQCAPLTSDISVEE 630
Cdd:cd12117   119 EAL----DAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLV-KNTNYVTLGPDDRVLQTSPLAFDASTFE 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  631 IFGGAACGARLVRSAAMKTGDLAALVDDLVARETTIVDLPTAVWQLLcADgDAIDAIgrSRLRQIVIGGEAIRCSAVDKW 710
Cdd:cd12117   194 IWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALFNQL-AD-EDPECF--AGLRELLTGGEVVSPPHVRRV 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  711 LESAAsqGISLLSSYGPTEATVVATFLPIvcDQTTMDGALLRLGRPILPNTVFL-----------AFGEVVIVGDLVADG 779
Cdd:cd12117   270 LAACP--GLRLVNGYGPTENTTFTTSHVV--TELDEVAGSIPIGRPIANTRVYVldedgrpvppgVPGELYVGGDGLALG 345

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  780 YLGIDG---DGFgtVTAADGSRRRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAVELH 856
Cdd:cd12117   346 YLNRPAltaERF--VADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVR 423

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489495878  857 SGSLGvwfkSQR-----TREGEQDAAAA-TRIRLVLVSLGVSSFFVVgVPNIPRKPNGKID 911
Cdd:cd12117   424 EDAGG----DKRlvayvVAEGALDAAELrAFLRERLPAYMVPAAFVV-LDELPLTANGKVD 479
PRK12316 PRK12316
peptide synthase; Provisional
 575-1009 7.45e-38

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 157.81  E-value: 7.45e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  575 AYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARLVRSAAmKTGDLAA 654
Cdd:PRK12316 4697 AYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDD-SLWDPER 4775

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  655 LVDDLVARETTIVDLPTAVWQLLcADGDAIDAiGRSRLRQIVIGGEAIRCSAVDKWLESAASqgISLLSSYGPTEATVVA 734
Cdd:PRK12316 4776 LYAEIHEHRVTVLVFPPVYLQQL-AEHAERDG-EPPSLRVYCFGGEAVAQASYDLAWRALKP--VYLFNGYGPTETTVTV 4851

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  735 TFLPivCDQTTMDGA-LLRLGRPILPNTVFL-----------AFGEVVIVGDLVADGYLGIDG--------DGFGtvtaA 794
Cdd:PRK12316 4852 LLWK--ARDGDACGAaYMPIGTPLGNRSGYVldgqlnplpvgVAGELYLGGEGVARGYLERPAltaerfvpDPFG----A 4925

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  795 DGSrrRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAVELHSGSLGV----WFKSQRTR 870
Cdd:PRK12316 4926 PGG--RLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKqlvgYVVPQDPA 5003

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  871 EGEQDAAAA-------TRIRLVLVSLGVSSFFVVgVPNIPRKPNGKIDSDNlprLPQWSAAGLNTA------ETGQRAAG 937
Cdd:PRK12316 5004 LADADEAQAelrdelkAALRERLPEYMVPAHLVF-LARMPLTPNGKLDRKA---LPQPDASLLQQAyvaprsELEQQVAA 5079

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489495878  938 lsqIWSRQLG-RAIGPDSSLLGEGIGSLDLIRILPETRRYLGWRLSLLDLIGADTAANLADYAPTPDAPTGED 1009
Cdd:PRK12316 5080 ---IWAEVLQlERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAAFVELAAAAGSGDDEK 5149
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 531-911 1.84e-37

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 149.35  E-value: 1.84e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  531 DGILVTVVDVAATQLAVVGHDELRKVVDERVTQVTHDALLAT----KTAYIMPTSGTTGQPKLVRISHGSLAVFCDAISR 606
Cdd:cd17646    93 DAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLVPprpdNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQD 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  607 AYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARLVRSAAMKTGDLAALVDDLVARETTIVDLPTAVWQLLCADGDAIDA 686
Cdd:cd17646   173 EYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSMLRVFLAEPAAGSC 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  687 IGrsrLRQIVIGGEAIRCSAVDKWLESAasqGISLLSSYGPTEATVVATFLPivCDQTTMDGALLrLGRPIlPNTVFL-- 764
Cdd:cd17646   253 AS---LRRVFCSGEALPPELAARFLALP---GAELHNLYGPTEAAIDVTHWP--VRGPAETPSVP-IGRPV-PNTRLYvl 322

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  765 ----------AFGEVVIVGDLVADGYLGIDGdgfgtVTAA------DGSRRRAFATGDRVTVDAEGFPVFSGRKDAVVKI 828
Cdd:cd17646   323 ddalrpvpvgVPGELYLGGVQLARGYLGRPA-----LTAErfvpdpFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKI 397

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  829 SGKRVDIAEVTRRIAEDPAVSDVAVELHSGSLGV-----WFKSQRTREGEQDAAAATRIRLVLVSLGVSSFFVVgVPNIP 903
Cdd:cd17646   398 RGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAarlvgYVVPAAGAAGPDTAALRAHLAERLPEYMVPAAFVV-LDALP 476


                  ....*...
gi 489495878  904 RKPNGKID 911
Cdd:cd17646   477 LTANGKLD 484
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
 1517-1974 4.24e-37

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 148.82  E-value: 4.24e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1517 SMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVTT 1596
Cdd:cd17647    20 SFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLIVI 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1597 aglrsRLAGhdlpiidVVDAlaayPGTPPPMPaavnlayilYTSGTTGEPKGVGITHRNVTRLFASLPAR--LSAAQVWS 1674
Cdd:cd17647   100 -----RAAG-------VVVG----PDSNPTLS---------FTSGSEGIPKGVLGRHFSLAYYFPWMAKRfnLSENDKFT 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1675 QCHSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAEHVSVLTQTPAAVAMLPTQGLES---------VALV 1745
Cdd:cd17647   155 MLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQATTPfpklhhaffVGDI 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1746 VAGEACpaALVDRWAPGRVMLNAYGPTET---------TICAAISAPLRPGSGMPPIGVPVSGAALFVLDSWLRPVPAGV 1816
Cdd:cd17647   235 LTKRDC--LRLQTLAENVRIVNMYGTTETqravsyfevPSRSSDPTFLKNLKDVMPAGRGMLNVQLLVVNRNDRTQICGI 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1817 A--GELYIAGAGVGVGYWRRAGLTASRFVACPFGGSGA---------------------RMYRTGDLVCWRADGQLEFLG 1873
Cdd:cd17647   313 GevGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDHwnyldkdnnepwrqfwlgprdRLYRTGDLGRYLPNGDCECCG 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1874 RTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGY-------------ATEIAPGAVDPAG------ 1934
Cdd:cd17647   393 RADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYivprfdkpddesfAQEDVPKEVSTDPivkgli 472

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 489495878 1935 --------LRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRALPAP 1974
Cdd:cd17647   473 gyrklikdIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 1489-1971 5.76e-37

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 148.13  E-value: 5.76e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1489 PTPVSIPQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAA 1568
Cdd:PRK07656    2 NEWMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1569 YLPIDPANPPPRVAFMLGDAVPVAAVTTAGL--RSRLAGHDLPIIDVV-------------------DALAayPGTPPPM 1627
Cdd:PRK07656   82 VVPLNTRYTADEAAYILARGDAKALFVLGLFlgVDYSATTRLPALEHVviceteeddphtekmktftDFLA--AGDPAER 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1628 PAAVN---LAYILYTSGTTGEPKGVGITHRNVtrlfaslparLSAAQVWSQC----------------HSYGFDASaweI 1688
Cdd:PRK07656  160 APEVDpddVADILFTSGTTGRPKGAMLTHRQL----------LSNAADWAEYlgltegdrylaanpffHVFGYKAG---V 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1689 WGALLGGGRLVIVPesvAASPNDFHGLLVAEHVSVLTQTPA------AVAMLPTQGLESVALVVAGEAC-PAALVDRWA- 1760
Cdd:PRK07656  227 NAPLMRGATILPLP---VFDPDEVFRLIETERITVLPGPPTmynsllQHPDRSAEDLSSLRLAVTGAASmPVALLERFEs 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1761 --PGRVMLNAYGPTE----TTIC-AAISAPLRPGSgmppIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWR 1833
Cdd:PRK07656  304 elGVDIVLTGYGLSEasgvTTFNrLDDDRKTVAGT----IGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYD 379

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1834 RAGLTASrfvACPFGGsgarMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIARED-R 1912
Cdd:PRK07656  380 DPEATAA---AIDADG----WLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDeR 452

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489495878 1913 PGDkrlVGYATEIA-PGA-VDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:PRK07656  453 LGE---VGKAYVVLkPGAeLTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 574-911 7.00e-37

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 146.88  E-value: 7.00e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  574 TAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDIS-VEEIFGGAACGARLVrsaAMKTGDL 652
Cdd:COG0318   102 TALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLV---LLPRFDP 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  653 AALVDDLVARETTIVDLPTAVWQLLCADGDAiDAIGRSRLRQIVIGGEAIRCSAVDKWLESAasqGISLLSSYGPTEATV 732
Cdd:COG0318   179 ERVLELIERERVTVLFGVPTMLARLLRHPEF-ARYDLSSLRLVVSGGAPLPPELLERFEERF---GVRIVEGYGLTETSP 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  733 VATFLPIVCDQTT-------MDGALLRL----GRPILPNTVflafGEVVIVGDLVADGYLGiDGDGfgtvTA---ADGsr 798
Cdd:COG0318   255 VVTVNPEDPGERRpgsvgrpLPGVEVRIvdedGRELPPGEV----GEIVVRGPNVMKGYWN-DPEA----TAeafRDG-- 323

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  799 rrAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV-----ELHSGSLGVWFksqRTREGE 873
Cdd:COG0318   324 --WLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVvgvpdEKWGERVVAFV---VLRPGA 398

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 489495878  874 QDAAAATR--IRLVLVSLGVSSFFVVgVPNIPRKPNGKID 911
Cdd:COG0318   399 ELDAEELRafLRERLARYKVPRRVEF-VDELPRTASGKID 437
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 574-911 1.48e-36

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 146.53  E-value: 1.48e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  574 TAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARL-VRSAAMKTGDL 652
Cdd:cd05918   108 AAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLcIPSEEDRLNDL 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  653 AALVDDL----------VARETTIVDLPTavwqllcadgdaidaigrsrLRQIVIGGEAIRCSAVDKWlesaaSQGISLL 722
Cdd:cd05918   188 AGFINRLrvtwafltpsVARLLDPEDVPS--------------------LRTLVLGGEALTQSDVDTW-----ADRVRLI 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  723 SSYGPTEATVVATFLPIVCDQTTmdgalLRLGRPIlPNTVFL-------------AFGEVVIVGDLVADGYLG------- 782
Cdd:cd05918   243 NAYGPAECTIAATVSPVVPSTDP-----RNIGRPL-GATCWVvdpdnhdrlvpigAVGELLIEGPILARGYLNdpektaa 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  783 --IDGDGFGTvTAADGSRRRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAE-DPAVSDVAVEL--HS 857
Cdd:cd05918   317 afIEDPAWLK-QEGSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQsLPGAKEVVVEVvkPK 395

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489495878  858 GSLG----VWFKSQRTREGEQD-----------------AAAATRIRLVLVSLGVSSFFVVgVPNIPRKPNGKID 911
Cdd:cd05918   396 DGSSspqlVAFVVLDGSSSGSGdgdslflepsdefralvAELRSKLRQRLPSYMVPSVFLP-LSHLPLTASGKID 469
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 574-911 3.97e-35

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 138.57  E-value: 3.97e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  574 TAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARLVrsaaMKTGDLA 653
Cdd:cd04433     2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVV----LLPKFDP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  654 ALVDDLVARE--TTIVDLPTAVWqlLCADGDAIDAIGRSRLRQIVIGGEAIRCSAVDKWLEsaaSQGISLLSSYGPTEAT 731
Cdd:cd04433    78 EAALELIEREkvTILLGVPTLLA--RLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEE---APGIKLVNGYGLTETG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  732 VVATFLPIVCDQTTMDGAllrlGRPIL--------PNTVFLAF---GEVVIVGDLVADGYLGIDgdgfgtVTAADGSRRR 800
Cdd:cd04433   153 GTVATGPPDDDARKPGSV----GRPVPgvevrivdPDGGELPPgeiGELVVRGPSVMKGYWNNP------EATAAVDEDG 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  801 AFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV-----ELHSGSLGVWFksQRTREGEQD 875
Cdd:cd04433   223 WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVvgvpdPEWGERVVAVV--VLRPGADLD 300

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 489495878  876 AAA-ATRIRLVLVSLGVSSFFVVgVPNIPRKPNGKID 911
Cdd:cd04433   301 AEElRAHVRERLAPYKVPRRVVF-VDALPRTASGKID 336
PRK07798 PRK07798
acyl-CoA synthetase; Validated
 1493-1969 4.34e-35

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 143.10  E-value: 4.34e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1493 SIPQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPI 1572
Cdd:PRK07798    4 NIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1573 DPANPPPRVAFMLGDAVPVAAVTTAGLRSRLAG--HDLPIIDVV-------------------DALAAYPGTPPPMPAAV 1631
Cdd:PRK07798   84 NYRYVEDELRYLLDDSDAVALVYEREFAPRVAEvlPRLPKLRTLvvvedgsgndllpgavdyeDALAAGSPERDFGERSP 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1632 NLAYILYTSGTTGEPKGVGITHRNV------TRLFASLPARLSAAQVWSQCHSYGF-----------DASAWEIWGALLG 1694
Cdd:PRK07798  164 DDLYLLYTGGTTGMPKGVMWRQEDIfrvllgGRDFATGEPIEDEEELAKRAAAGPGmrrfpapplmhGAGQWAAFAALFS 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1695 GGRLVIVPESVAaspnDFHGLL--VAEH-VSVLTQT------PAAVAMLPTQG--LESVALVVAG-----EACPAALVDr 1758
Cdd:PRK07798  244 GQTVVLLPDVRF----DADEVWrtIEREkVNVITIVgdamarPLLDALEARGPydLSSLFAIASGgalfsPSVKEALLE- 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1759 WAPGRVMLNAYGPTETTICA-AISAPLRPGSGMPPIGVpvsGAALFVLDSWLRPVPAGVAGELYIAGAG-VGVGYWRRAG 1836
Cdd:PRK07798  319 LLPNVVLTDSIGSSETGFGGsGTVAKGAVHTGGPRFTI---GPRTVVLDEDGNPVEPGSGEIGWIARRGhIPLGYYKDPE 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1837 LTASRFvacpFGGSGARMYRTGDLVCWRADGQLEFLGRtdDQVKIR--GYRIELGEVATALAELAGVGQAVVIAREDRPG 1914
Cdd:PRK07798  396 KTAETF----PTIDGVRYAIPGDRARVEADGTITLLGR--GSVCINtgGEKVFPEEVEEALKAHPDVADALVVGVPDERW 469

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 489495878 1915 DKRLVGyATEIAPGA-VDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHR 1969
Cdd:PRK07798  470 GQEVVA-VVQLREGArPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKADYR 524
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 1519-1971 4.40e-35

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 140.94  E-value: 4.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1519 TYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVTTag 1598
Cdd:cd05972     2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1599 lrsrlaghdlpiidvvdalaaypgtpppmpaAVNLAYILYTSGTTGEPKGVGITHRnvtRLFASLParlsAAQVWSQCHS 1678
Cdd:cd05972    80 -------------------------------AEDPALIYFTSGTTGLPKGVLHTHS---YPLGHIP----TAAYWLGLRP 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1679 ----YGFDASAWE--IWGALLG---GGRLVIVPESVAASPNDFHGLLVAEHVSVLTQTPAAVAMLPTQGLESVAL----- 1744
Cdd:cd05972   122 ddihWNIADPGWAkgAWSSFFGpwlLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKFshlrl 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1745 -VVAGEACPAALVDRW--APGRVMLNAYGPTETTICAAIS--APLRPGSgmppIGVPVSGAALFVLDSWLRPVPAGVAGE 1819
Cdd:cd05972   202 vVSAGEPLNPEVIEWWraATGLPIRDGYGQTETGLTVGNFpdMPVKPGS----MGRPTPGYDVAIIDDDGRELPPGEEGD 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1820 LYIAGAGVG--VGYWRRAGLTASRFVacpfGGsgarMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAE 1897
Cdd:cd05972   278 IAIKLPPPGlfLGYVGDPEKTEASIR----GD----YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLE 349

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489495878 1898 LAGVGQAVVIAREDrPGDKRLVGYATEIAPGAVDPAGLRAQLA----QRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:cd05972   350 HPAVAEAAVVGSPD-PVRGEVVKAFVVLTSGYEPSEELAEELQghvkKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 1022-1409 8.19e-35

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 139.89  E-value: 8.19e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1022 AIPLSFAQRRLWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVD-GVPRQLVIEARRADLG 1100
Cdd:cd19536     1 MYPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGlGQPVQVVHRQAQVPVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1101 CDIVDATAWPADRLQRAIEEAARHSFDLATEIPLRTWLFRIADDEHVLVAVA-HHIAADGWSVAPLTADLSAAYASRCAG 1179
Cdd:cd19536    81 ELDLTPLEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERFLLVISdHHSILDGWSLYLLVKEILAVYNQLLEY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1180 RApdWAPLPVQ-YVDYTLWQREILGDlddsdspiAAQLAYWENALAGMperlRLPTArPYPPVADQRGASLVVDWPASVQ 1258
Cdd:cd19536   161 KP--LSLPPAQpYRDFVAHERASIQQ--------AASERYWREYLAGA----TLATL-PALSEAVGGGPEQDSELLVSVP 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1259 QQVR---RIARQHNATSFMVVAAgLAVLLSKLSGSPDVAVGFPIAGRSDPALD--NLVGFFVNTLVLRVNLAgDPSFAEL 1333
Cdd:cd19536   226 LPVRsrsLAKRSGIPLSTLLLAA-WALVLSRHSGSDDVVFGTVVHGRSEETTGaeRLLGLFLNTLPLRVTLS-EETVEDL 303

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489495878 1334 LGQVRARSLAAYENQDVPfevLVDRLKPTRALthhPLIQVMLAWQDNPVGqlnlgdlQATPMPIDTRTARMDLVFS 1409
Cdd:cd19536   304 LKRAQEQELESLSHEQVP---LADIQRCSEGE---PLFDSIVNFRHFDLD-------FGLPEWGSDEGMRRGLLFS 366
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
 1519-1975 1.13e-34

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 139.94  E-value: 1.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1519 TYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVTTAG 1598
Cdd:cd05969     2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1599 LRSRLAghdlpiidvvdalaayPGTPppmpaavnlAYILYTSGTTGEPKGVGITHRNVTRLFaslparLSAAQV------ 1672
Cdd:cd05969    82 LYERTD----------------PEDP---------TLLHYTSGTTGTPKGVLHVHDAMIFYY------FTGKYVldlhpd 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1673 ----------WSQCHSYGfdasaweIWGALLGGGRLVIVPESVaaSPNDFHGLLVAEHVSVLTQTPAAVAMLPTQG---- 1738
Cdd:cd05969   131 diywctadpgWVTGTVYG-------IWAPWLNGVTNVVYEGRF--DAESWYGIIERVKVTVWYTAPTAIRMLMKEGdela 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1739 ----LESVALVVA-GEAC-PAALvdRW---APGRVMLNAYGPTET---TICAAISAPLRPGSgmppIGVPVSGAALFVLD 1806
Cdd:cd05969   202 rkydLSSLRFIHSvGEPLnPEAI--RWgmeVFGVPIHDTWWQTETgsiMIANYPCMPIKPGS----MGKPLPGVKAAVVD 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1807 SWLRPVPAGVAGELYIAGA--GVGVGYWRRAGLTASRFVacpfGGsgarMYRTGDLVCWRADGQLEFLGRTDDQVKIRGY 1884
Cdd:cd05969   276 ENGNELPPGTKGILALKPGwpSMFRGIWNDEERYKNSFI----DG----WYLTGDLAYRDEDGYFWFVGRADDIIKTSGH 347

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1885 RIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATeIAPGAVDPAGLRAQL----AQRLPGYLVPAAVVVIDALPL 1960
Cdd:cd05969   348 RVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFIS-LKEGFEPSDELKEEIinfvRQKLGAHVAPREIEFVDNLPK 426

                         490
                  ....*....|....*
gi 489495878 1961 TVNGKLDHRALPAPE 1975
Cdd:cd05969   427 TRSGKIMRRVLKAKE 441
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 574-911 4.56e-34

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 138.58  E-value: 4.56e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  574 TAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARLVRSAAMKTGDLA 653
Cdd:cd12116   128 LAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPE 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  654 ALVDDLVARETTIVDLPTAVWQLLCADGDAidaiGRSRLRqIVIGGEAIRCSAVDKWLesaaSQGISLLSSYGPTEATVV 733
Cdd:cd12116   208 ALARLIEAHSITVMQATPATWRMLLDAGWQ----GRAGLT-ALCGGEALPPDLAARLL----SRVGSLWNLYGPTETTIW 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  734 ATFLPIvcdqtTMDGALLRLGRPIlPNTVFL------------AFGEVVIVGDLVADGYLGIDGDGFGTVTA--ADGSRR 799
Cdd:cd12116   279 STAARV-----TAAAGPIPIGRPL-ANTQVYvldaalrpvppgVPGELYIGGDGVAQGYLGRPALTAERFVPdpFAGPGS 352

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  800 RAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAVELHSGSLG------VWFKsqrtrEGE 873
Cdd:cd12116   353 RLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDrrlvayVVLK-----AGA 427

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 489495878  874 QDAAAATRIRL--VLVSLGVSSFFVVgVPNIPRKPNGKID 911
Cdd:cd12116   428 APDAAALRAHLraTLPAYMVPSAFVR-LDALPLTANGKLD 466
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 574-915 6.84e-34

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 137.44  E-value: 6.84e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  574 TAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARLVRSAAMKT-GDL 652
Cdd:cd17653   107 LAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADPSDPfAHV 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  653 AALVDDLVARETTIVDLPTAVWQllcadgdaidaigrsRLRQIVIGGEAIRCSAVDKWLEsaasqGISLLSSYGPTEATV 732
Cdd:cd17653   187 ARTVDALMSTPSILSTLSPQDFP---------------NLKTIFLGGEAVPPSLLDRWSP-----GRRLYNAYGPTECTI 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  733 VATFlpivcdQTTMDGALLRLGRPILPNTVFL-----------AFGEVVIVGDLVADGYLGID---GDGFGTVTAADGSr 798
Cdd:cd17653   247 SSTM------TELLPGQPVTIGKPIPNSTCYIldadlqpvpegVVGEICISGVQVARGYLGNPaltASKFVPDPFWPGS- 319

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  799 rRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRI-AEDPAVSDVAVELHSGSLgVWFKsqrTREGEQDAA 877
Cdd:cd17653   320 -RMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVlQSQPEVTQAAAIVVNGRL-VAFV---TPETVDVDG 394

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 489495878  878 AATRIRLVLVSLGVSSFFvVGVPNIPRKPNGKIDSDNL 915
Cdd:cd17653   395 LRSELAKHLPSYAVPDRI-IALDSFPLTANGKVDRKAL 431
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 1034-1457 7.17e-34

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 136.67  E-value: 7.17e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1034 FLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVF--PAVDGVPRQLVIeaRRADLGCDIVDatawpa 1111
Cdd:cd19542    11 MLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFveSSAEGTFLQVVL--KSLDPPIEEVE------ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1112 dRLQRAIEEAARHSFD---LATEIPLRTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYASRCAGRAPDWAplp 1188
Cdd:cd19542    83 -TDEDSLDALTRDLLDdptLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPPAPPFS--- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1189 vQYVDYTlwqreilgdlddSDSPIAAQLAYWENALAGMperlrlpTARPYPPVADQRGASLVVDWPASVQQQVRRIARQH 1268
Cdd:cd19542   159 -DYISYL------------QSQSQEESLQYWRKYLQGA-------SPCAFPSLSPKRPAERSLSSTRRSLAKLEAFCASL 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1269 NATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGR--SDPALDNLVGFFVNTLVLRVNLAGDPSFAELLGQVRARSLAAYE 1346
Cdd:cd19542   219 GVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRdlPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLP 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1347 NQDVPFEVLVDRLKPTRA-------LTHHPL--IQVMLAWQDNPVGQLNLGDLQATPMPIDTRTARMDLVFSLAerfseg 1417
Cdd:cd19542   299 HQHLSLREIQRALGLWPSgtlfntlVSYQNFeaSPESELSGSSVFELSAAEDPTEYPVAVEVEPSGDSLKVSLA------ 372

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 489495878 1418 sepagiggaveYRTDVFEAQAIDVLIERLRKVLVAVAAAP 1457
Cdd:cd19542   373 -----------YSTSVLSEEQAEELLEQFDDILEALLANP 401
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 575-916 1.29e-33

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 136.61  E-value: 1.29e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  575 AYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARLVRSAAMKTGDLAA 654
Cdd:cd17652    96 AYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEP 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  655 LVDDLVARETTIVDLPTAVWQLLCADGDAidaigrsRLRQIVIGGEAIRCSAVDKWlesaaSQGISLLSSYGPTEATVVA 734
Cdd:cd17652   176 LADLLREHRITHVTLPPAALAALPPDDLP-------DLRTLVVAGEACPAELVDRW-----APGRRMINAYGPTETTVCA 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  735 TFLpivcdQTTMDGALLRLGRPILPNTVFL-----------AFGEVVIVGDLVADGYLGIDG--------DGFGtvtaAD 795
Cdd:cd17652   244 TMA-----GPLPGGGVPPIGRPVPGTRVYVldarlrpvppgVPGELYIAGAGLARGYLNRPGltaerfvaDPFG----AP 314

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  796 GSrrRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAVELHSGSLGVwfksQR------T 869
Cdd:cd17652   315 GS--RMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGD----KRlvayvvP 388

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 489495878  870 REGEQDAAAATRIRLV--LVSLGVSSFFVVgVPNIPRKPNGKIDSDNLP 916
Cdd:cd17652   389 APGAAPTAAELRAHLAerLPGYMVPAAFVV-LDALPLTPNGKLDRRALP 436
PRK06188 PRK06188
acyl-CoA synthetase; Validated
 1482-1974 2.37e-33

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 137.81  E-value: 2.37e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1482 AVLTAPAPTPVSIPQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVA 1561
Cdd:PRK06188    2 ATMADLLHSGATYGHLLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1562 VLKTGAAYLPIDPANPPPRVAFMLGDAV-------PVAAVTTA-GLRSRLAG--HDLPIIDVVD-----ALAAYPGTPPP 1626
Cdd:PRK06188   82 AQLAGLRRTALHPLGSLDDHAYVLEDAGistlivdPAPFVERAlALLARVPSlkHVLTLGPVPDgvdllAAAAKFGPAPL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1627 MPAAV--NLAYILYTSGTTGEPKGVGITHRNVTRLFASL------PARLSAAQVWSQCHsygfdASAWEIWGALLGGGRL 1698
Cdd:PRK06188  162 VAAALppDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQlaewewPADPRFLMCTPLSH-----AGGAFFLPTLLRGGTV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1699 VIVPesvAASPNDF------HG----LLVAEHVSVLTQTPAavamLPTQGLESVALVVAGEA--CPAALV---DRWAPgr 1763
Cdd:PRK06188  237 IVLA---KFDPAEVlraieeQRitatFLVPTMIYALLDHPD----LRTRDLSSLETVYYGASpmSPVRLAeaiERFGP-- 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1764 VMLNAYGPTETTICAAIsapLRPGSGMPPI-------GVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAG 1836
Cdd:PRK06188  308 IFAQYYGQTEAPMVITY---LRKRDHDPDDpkrltscGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPE 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1837 LTASRFVacpfGGsgarMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAredRPGDK 1916
Cdd:PRK06188  385 ETAEAFR----DG----WLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIG---VPDEK 453

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489495878 1917 --RLVGYATEIAPGA-VDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRALPAP 1974
Cdd:PRK06188  454 wgEAVTAVVVLRPGAaVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRAR 514
PRK09088 PRK09088
acyl-CoA synthetase; Validated
 1519-1966 4.46e-33

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 136.09  E-value: 4.46e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1519 TYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVTTAG 1598
Cdd:PRK09088   24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDDA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1599 LRS-RLAGHDLP-IIDVVDALAAYPgTPPPMPAAVNLayILYTSGTTGEPKGVGITHRNV--TRLFASLPARLSAAQvws 1674
Cdd:PRK09088  104 VAAgRTDVEDLAaFIASADALEPAD-TPSIPPERVSL--ILFTSGTSGQPKGVMLSERNLqqTAHNFGVLGRVDAHS--- 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1675 qchSYGFDASAWEIWG-------ALLGGGRLVIVPESVAASPNDFHG---LLVAEHVSVltqtPAAVAMLPTQ-GLES-- 1741
Cdd:PRK09088  178 ---SFLCDAPMFHIIGlitsvrpVLAVGGSILVSNGFEPKRTLGRLGdpaLGITHYFCV----PQMAQAFRAQpGFDAaa 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1742 ----VALVVAGEACPAALVDRW-APGRVMLNAYGPTET-TI------CAAISAplRPGSGmppiGVPVSGAALFVLDSWL 1809
Cdd:PRK09088  251 lrhlTALFTGGAPHAAEDILGWlDDGIPMVDGFGMSEAgTVfgmsvdCDVIRA--KAGAA----GIPTPTVQTRVVDDQG 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1810 RPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFvacpfggSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELG 1889
Cdd:PRK09088  325 NDCPAGVPGELLLRGPNLSPGYWRRPQATARAF-------TGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPA 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1890 EVATALAELAGVGQAVVIARED-RPGDkrlVGY-ATEIAPG-AVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKL 1966
Cdd:PRK09088  398 EIEAVLADHPGIRECAVVGMADaQWGE---VGYlAIVPADGaPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKL 474
PRK07787 PRK07787
acyl-CoA synthetase; Validated
 1507-1975 8.67e-33

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 134.73  E-value: 8.67e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1507 EAEAVCCGDASMTYRELDEASNRLAHRLAGCGAgpgecVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLG 1586
Cdd:PRK07787   15 IADAVRIGGRVLSRSDLAGAATAVAERVAGARR-----VAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1587 DAVPVAAVttAGLRSRLAGhdLPIIDVvdALAAYPGTPPPMPAAVNLAYILYTSGTTGEPKGVGITHRNVTrlfASLPAr 1666
Cdd:PRK07787   90 DSGAQAWL--GPAPDDPAG--LPHVPV--RLHARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIA---ADLDA- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1667 LSAAQVWSQ----------CHSYGFdasAWEIWGALLGGGRLVIV----PESVAASPNDFHGLL--VAEHVSVLTQTPAA 1730
Cdd:PRK07787  160 LAEAWQWTAddvlvhglplFHVHGL---VLGVLGPLRIGNRFVHTgrptPEAYAQALSEGGTLYfgVPTVWSRIAADPEA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1731 vamlpTQGLESVALVVAGEAC-PAALVDRWA--PGRVMLNAYGPTET--TICAAISAPLRPGSgmppIGVPVSGAALFVL 1805
Cdd:PRK07787  237 -----ARALRGARLLVSGSAAlPVPVFDRLAalTGHRPVERYGMTETliTLSTRADGERRPGW----VGLPLAGVETRLV 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1806 DSWLRPVPAGVA--GELYIAGAGVGVGYWRRAGLTASRFVACPFggsgarmYRTGDLVCWRADGQLEFLGR-TDDQVKIR 1882
Cdd:PRK07787  308 DEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW-------FRTGDVAVVDPDGMHRIVGReSTDLIKSG 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1883 GYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYAteIAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTV 1962
Cdd:PRK07787  381 GYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYV--VGADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNA 458

                         490
                  ....*....|...
gi 489495878 1963 NGKLDHRALPAPE 1975
Cdd:PRK07787  459 MGKVLKKQLLSEG 471
PRK07514 PRK07514
malonyl-CoA synthase; Validated
 1518-1965 2.13e-32

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 134.23  E-value: 2.13e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1518 MTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVTT- 1596
Cdd:PRK07514   29 YTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCDp 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1597 ---AGLRSRLAGHDLPIIDVVDA------LAAYPGTPPPMPAAV----NLAYILYTSGTTGEPKGVGITHRNVtrlfasl 1663
Cdd:PRK07514  109 anfAWLSKIAAAAGAPHVETLDAdgtgslLEAAAAAPDDFETVPrgadDLAAILYTSGTTGRSKGAMLSHGNL------- 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1664 parLSAAQVWSQC----------------HSYG-FDASAweiwGALLGGGRLVIVPESVAAspndfhgllvaehvSVLTQ 1726
Cdd:PRK07514  182 ---LSNALTLVDYwrftpddvlihalpifHTHGlFVATN----VALLAGASMIFLPKFDPD--------------AVLAL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1727 TPAAVAML--PT--------QGL--ESVA---LVVAGEAcP--AALVDRWAP--GRVMLNAYGPTETtiCAAISAPL--- 1784
Cdd:PRK07514  241 MPRATVMMgvPTfytrllqePRLtrEAAAhmrLFISGSA-PllAETHREFQErtGHAILERYGMTET--NMNTSNPYdge 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1785 -RPGSgmppIGVPVSGAALFVLDSWL-RPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFggsgarmYRTGDLVC 1862
Cdd:PRK07514  318 rRAGT----VGFPLPGVSLRVTDPETgAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF-------FITGDLGK 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1863 WRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGV----------------GQAVVIAredRPGdkrlvgyateia 1926
Cdd:PRK07514  387 IDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVvesavigvphpdfgegVTAVVVP---KPG------------ 451

                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 489495878 1927 pGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGK 1965
Cdd:PRK07514  452 -AALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGK 489
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
 1517-1966 5.86e-32

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 131.73  E-value: 5.86e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1517 SMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVTT 1596
Cdd:cd05903     1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1597 aglrSRLAGHDlpiidvvdalaaypgtPPPMPAAVnlAYILYTSGTTGEPKGVGITHRNvtrLFASLPArlsaaqvwsQC 1676
Cdd:cd05903    81 ----ERFRQFD----------------PAAMPDAV--ALLLFTSGTTGEPKGVMHSHNT---LSASIRQ---------YA 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1677 HSYGFDASAwEIWGA-----LLGGGRLVIVPESVAAS--------PNDFHGLLVAEHVSVLTQTPAAVAMLPTQGLESVA 1743
Cdd:cd05903   127 ERLGLGPGD-VFLVAspmahQTGFVYGFTLPLLLGAPvvlqdiwdPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGE 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1744 -------LVVAGEACPAALVDRWAP--GRVMLNAYGPTETTICAAISAPLRPGSGMPPIGVPVSGAALFVLDSWLRPVPA 1814
Cdd:cd05903   206 plsrlrtFVCGGATVPRSLARRAAEllGAKVCSAYGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAP 285

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1815 GVAGELYIAGAGVGVGYWRRAGLTasrFVACPFGgsgarMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATA 1894
Cdd:cd05903   286 GVEGELLSRGPSVFLGYLDRPDLT---ADAAPEG-----WFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDL 357

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489495878 1895 LAELAGVGQAVVIAREDRPGDKRLVGYATEIAPGAVDPAGLRAQL-AQRLPGYLVPAAVVVIDALPLTVNGKL 1966
Cdd:cd05903   358 LLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKV 430
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
 1517-1966 6.23e-32

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 132.72  E-value: 6.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1517 SMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVP------ 1590
Cdd:cd05911    10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPkviftd 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1591 ---VAAVTTAG-----------LRSRLAGHdLPIIDVVDALAAYPGTPPPMP---AAVNLAYILYTSGTTGEPKGVGITH 1653
Cdd:cd05911    90 pdgLEKVKEAAkelgpkdkiivLDDKPDGV-LSIEDLLSPTLGEEDEDLPPPlkdGKDDTAAILYSSGTTGLPKGVCLSH 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1654 RNVT------------------RLFASLPARlsaaqvwsqcHSYGFDAsaweIWGALLGGGRLVIVPEsvaASPNDFHGL 1715
Cdd:cd05911   169 RNLIanlsqvqtflygndgsndVILGFLPLY----------HIYGLFT----TLASLLNGATVIIMPK---FDSELFLDL 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1716 LVAEHVSVLTQTPAAVAML------PTQGLESV-ALVVAGEACPAALVDRWA---PGRVMLNAYGPTETT--ICAAISAP 1783
Cdd:cd05911   232 IEKYKITFLYLVPPIAAALakspllDKYDLSSLrVILSGGAPLSKELQELLAkrfPNATIKQGYGMTETGgiLTVNPDGD 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1784 LRPGSgmppIGVPVSGAALFVLD----SWLRPvpaGVAGELYIAGAGVGVGYWRRAGLTASRFvacPFGGsgarMYRTGD 1859
Cdd:cd05911   312 DKPGS----VGRLLPNVEAKIVDddgkDSLGP---NEPGEICVRGPQVMKGYYNNPEATKETF---DEDG----WLHTGD 377

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1860 LVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATEIAPGAVDPAGLRAQL 1939
Cdd:cd05911   378 IGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYV 457

                         490       500
                  ....*....|....*....|....*....
gi 489495878 1940 AQRLPGY--LVpAAVVVIDALPLTVNGKL 1966
Cdd:cd05911   458 AKKVASYkqLR-GGVVFVDEIPKSASGKI 485
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
 1498-1971 1.28e-31

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 131.68  E-value: 1.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1498 LAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAayLPIDpANP 1577
Cdd:cd05920    21 LARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA--VPVL-ALP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1578 PPRVAFMLGDAVPVAAVTTAGLRsRLAGHDlPIIDVVDALAAYPGTpppmpaavnlAYILYTSGTTGEPKGVGITHRNV- 1656
Cdd:cd05920    98 SHRRSELSAFCAHAEAVAYIVPD-RHAGFD-HRALARELAESIPEV----------ALFLLSGGTTGTPKLIPRTHNDYa 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1657 ---------------TRLFASLPArlsaaqvwsqchSYGFDASAWEIWGALLGGGRLVIVPEsvaASPNDFHGLLVAEHV 1721
Cdd:cd05920   166 ynvrasaevcgldqdTVYLAVLPA------------AHNFPLACPGVLGTLLAGGRVVLAPD---PSPDAAFPLIEREGV 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1722 SVLTQTPAAVAML------PTQGLESVALVVAGEA---------CPAAL---VDRW---APGRVMLNAYGPTETTICAAI 1780
Cdd:cd05920   231 TVTALVPALVSLWldaaasRRADLSSLRLLQVGGArlspalarrVPPVLgctLQQVfgmAEGLLNYTRLDDPDEVIIHTQ 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1781 SAPLRPGSgmppigvpvsgaALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFggsgarmYRTGDL 1860
Cdd:cd05920   311 GRPMSPDD------------EIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF-------YRTGDL 371

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1861 VCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATeIAPGAVDPAGLRAQLA 1940
Cdd:cd05920   372 VRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVV-LRDPPPSAAQLRRFLR 450

                         490       500       510
                  ....*....|....*....|....*....|..
gi 489495878 1941 QR-LPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:cd05920   451 ERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
 1517-1971 1.36e-31

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 130.68  E-value: 1.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1517 SMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVTT 1596
Cdd:cd05935     1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1597 AGLRsrlaghdlpiidvvdalaaypgtpppmpaavNLAYILYTSGTTGEPKGVGITHRNVTrLFASLPAR---LSAAQVW 1673
Cdd:cd05935    81 SELD-------------------------------DLALIPYTSGTTGLPKGCMHTHFSAA-ANALQSAVwtgLTPSDVI 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1674 SQC----HSYGFDASaweIWGALLGGGRLVIvpesVAASPNDFHGLLVAEH-VSVLTQTPAAVA-MLPTQGLE----SVA 1743
Cdd:cd05935   129 LAClplfHVTGFVGS---LNTAVYVGGTYVL----MARWDRETALELIEKYkVTFWTNIPTMLVdLLATPEFKtrdlSSL 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1744 LVVA--GEACPAALVDRW--APGRVMLNAYGPTETTICAAISAPLRPGSGMppIGVPVSGAALFVLD-SWLRPVPAGVAG 1818
Cdd:cd05935   202 KVLTggGAPMPPAVAEKLlkLTGLRFVEGYGLTETMSQTHTNPPLRPKLQC--LGIP*FGVDARVIDiETGRELPPNEVG 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1819 ELYIAGAGVGVGYWRRAGLTASRFVACpfggSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAEL 1898
Cdd:cd05935   280 EIVVRGPQIFKGYWNRPEETEESFIEI----KGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKH 355

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489495878 1899 AGVGQAVVIARED-RPGD--KRLVGYATEIApGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:cd05935   356 PAI*EVCVISVPDeRVGEevKAFIVLRPEYR-GKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
 1493-1969 1.37e-31

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 133.20  E-value: 1.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1493 SIPQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPI 1572
Cdd:PRK05605   33 TLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEH 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1573 DPANPPPRVAFMLGD---AVPVA----AVTTAGLRSRLAGHDLPIIDVVDAL-----------------------AAYPG 1622
Cdd:PRK05605  113 NPLYTAHELEHPFEDhgaRVAIVwdkvAPTVERLRRTTPLETIVSVNMIAAMpllqrlalrlpipalrkaraaltGPAPG 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1623 T------------------PPPMPAAVNLAYILYTSGTTGEPKGVGITHRNvtrLFASL-------------PARLSAAq 1671
Cdd:PRK05605  193 TvpwetlvdaaiggdgsdvSHPRPTPDDVALILYTSGTTGKPKGAQLTHRN---LFANAaqgkawvpglgdgPERVLAA- 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1672 vWSQCHSYGFDASAWEiwgALLGGGRLVIVP--------ESVAASPNDFhglLVAehVSVLTQTPAAVAMLPTQGLESVA 1743
Cdd:PRK05605  269 -LPMFHAYGLTLCLTL---AVSIGGELVLLPapdidlilDAMKKHPPTW---LPG--VPPLYEKIAEAAEERGVDLSGVR 339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1744 LVVAGE-ACPAALVDRW--APGRVMLNAYGPTETT---ICAAISAPLRPGSgmppIGVPVSGAALFVLD--SWLRPVPAG 1815
Cdd:PRK05605  340 NAFSGAmALPVSTVELWekLTGGLLVEGYGLTETSpiiVGNPMSDDRRPGY----VGVPFPDTEVRIVDpeDPDETMPDG 415

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1816 VAGELYIAGAGVGVGYWRRAGLTASRFVAcpfggsgaRMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATAL 1895
Cdd:PRK05605  416 EEGELLVRGPQVFKGYWNRPEETAKSFLD--------GWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVL 487

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489495878 1896 AELAGVGQAVV--IAREDrpGDKRLVGyATEIAPGAV-DPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHR 1969
Cdd:PRK05605  488 REHPGVEDAAVvgLPRED--GSEEVVA-AVVLEPGAAlDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRR 561
AMP-binding pfam00501
AMP-binding enzyme;
473-829 2.46e-31

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 129.35  E-value: 2.46e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878   473 AWLVQRGAAPGDVLVFTDDDTDKTIDLLIACHLAGCGYSVCD---TADEISVRTNA------ITEH-----------GDG 532
Cdd:pfam00501   36 AGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNprlPAEELAYILEDsgakvlITDDalkleellealGKL 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878   533 ILVTVVDVAATQLAVVGHDELRKVVDERVTQVTHDALLATKTAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGW-- 610
Cdd:pfam00501  116 EVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRgf 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878   611 --GAHDTVLQCAPLTSDISVE-EIFGGAACGARLVRSAAMKTGDLAALVDDLVARETTIVDLPTAVWQLLcADGDAIDAI 687
Cdd:pfam00501  196 glGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATVVLPPGFPALDPAALLELIERYKVTVLYGVPTLLNML-LEAGAPKRA 274

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878   688 GRSRLRQIVIGGEAIRCSAVDKWLESAasqGISLLSSYGPTEATVVATFLPIVCDQTTMDGallRLGRPILPNTVFL--- 764
Cdd:pfam00501  275 LLSSLRLVLSGGAPLPPELARRFRELF---GGALVNGYGLTETTGVVTTPLPLDEDLRSLG---SVGRPLPGTEVKIvdd 348

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489495878   765 ---------AFGEVVIVGDLVADGYLGIDGDgfgtvTAADGSRRRAFATGDRVTVDAEGFPVFSGRKDAVVKIS 829
Cdd:pfam00501  349 etgepvppgEPGELCVRGPGVMKGYLNDPEL-----TAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 559-911 3.33e-31

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 129.74  E-value: 3.33e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  559 ERVTQVTHDALLA------TKTAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIF 632
Cdd:cd12115    86 ERLRFILEDAQARlvltdpDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELF 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  633 GGAACGARLVRSAamktgDLAALVDDLVARETTIVD-LPTAVWQLLcadgdAIDAIGRSrLRQIVIGGEAIRCSAVDKWl 711
Cdd:cd12115   166 GPLATGGKVVLAD-----NVLALPDLPAAAEVTLINtVPSAAAELL-----RHDALPAS-VRVVNLAGEPLPRDLVQRL- 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  712 eSAASQGISLLSSYGPTEATVVATFLPIvcdqTTMDGALLRLGRPILPNTVFL-----------AFGEVVIVGDLVADGY 780
Cdd:cd12115   234 -YARLQVERVVNLYGPSEDTTYSTVAPV----PPGASGEVSIGRPLANTQAYVldralqpvplgVPGELYIGGAGVARGY 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  781 LGIDG---DGFgtVTAADGSRRRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAVELHS 857
Cdd:cd12115   309 LGRPGltaERF--LPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIG 386

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 489495878  858 GSLG----VWFKSQRTREGEQDAAAATRIRLVLVSLGVSSFFVVgVPNIPRKPNGKID 911
Cdd:cd12115   387 DAAGerrlVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVR-LDALPLTPNGKID 443
PRK06178 PRK06178
acyl-CoA synthetase; Validated
 1492-1967 3.69e-31

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 131.70  E-value: 3.69e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1492 VSIPQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLP 1571
Cdd:PRK06178   33 RPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVP 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1572 IDPANPPPRVAFMLGDAVPVAAVTTAGL-------RSRLA-----------------------GHDLP------IIDVVD 1615
Cdd:PRK06178  113 VSPLFREHELSYELNDAGAEVLLALDQLapvveqvRAETSlrhvivtsladvlpaeptlplpdSLRAPrlaaagAIDLLP 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1616 ALAAYPGTPPPMPAAVN-LAYILYTSGTTGEPKGVGITHRNVTRLFAslpARLSAAQVWSQCH-SYGFDASAWeIWGALL 1693
Cdd:PRK06178  193 ALRACTAPVPLPPPALDaLAALNYTGGTTGMPKGCEHTQRDMVYTAA---AAYAVAVVGGEDSvFLSFLPEFW-IAGENF 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1694 G-------GGRLVIV----PESVAASPNDF---HGLLVAEHVSVLTQTPAaVAMLPTQGLESVALVVAGEACPAALVDRW 1759
Cdd:PRK06178  269 GllfplfsGATLVLLarwdAVAFMAAVERYrvtRTVMLVDNAVELMDHPR-FAEYDLSSLRQVRVVSFVKKLNPDYRQRW 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1760 --APGRVMLNA-YGPTETTICAAISAPLRPG----SGMPP-IGVPVSGAALFVLD-SWLRPVPAGVAGELYIAGAGVGVG 1830
Cdd:PRK06178  348 raLTGSVLAEAaWGMTETHTCDTFTAGFQDDdfdlLSQPVfVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKG 427

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1831 YWRRAGLTASRFVacpfGGsgarMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIARE 1910
Cdd:PRK06178  428 YWNKPEATAEALR----DG----WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRP 499

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489495878 1911 DRpgDKRLVGYA-TEIAPGA-VDPAGLRAQLAQRLPGYLVPaAVVVIDALPLTVNGKLD 1967
Cdd:PRK06178  500 DP--DKGQVPVAfVQLKPGAdLTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKVR 555
FAR-N_SDR_e cd05236
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding ...
 2108-2392 9.40e-31

fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding proteins, many of which may function as fatty acyl CoA reductases (FAR), acting on medium and long chain fatty acids, and have been reported to be involved in diverse processes such as biosynthesis of insect pheromones, plant cuticular wax production, and mammalian wax biosynthesis. In Arabidopsis thaliana, proteins with this particular architecture have also been identified as the MALE STERILITY 2 (MS2) gene product, which is implicated in male gametogenesis. Mutations in MS2 inhibit the synthesis of exine (sporopollenin), rendering plants unable to reduce pollen wall fatty acids to corresponding alcohols. This N-terminal domain shares the catalytic triad (but not the upstream Asn) and characteristic NADP-binding motif of the extended SDR family. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187547 [Multi-domain]  Cd Length: 320  Bit Score: 125.10  E-value: 9.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2108 RTVLLTGATGFLGRYLVLELLRRLDVDGRLICLVRAESDEDARRRLEKTFDSGDPELLRHFKELAADRLEVVAGDKSEPD 2187
Cdd:cd05236     1 KSVLITGATGFLGKVLLEKLLRSCPDIGKIYLLIRGKSGQSAEERLRELLKDKLFDRGRNLNPLFESKIVPIEGDLSEPN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2188 LGLDQPMWRRLAETVDLIVDSAAMVNaF--PYHELFGPNVAGTAELIRIALT-TKLKPFTYVSTA-------DVGAAIEP 2257
Cdd:cd05236    81 LGLSDEDLQTLIEEVNIIIHCAATVT-FdeRLDEALSINVLGTLRLLELAKRcKKLKAFVHVSTAyvngdrqLIEEKVYP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2258 SAFTEDA---------DIRVISPTRTVDGGWAGGYGTSKWAGEVLLREANDlcALPVAVFRCGMILADT-----SYAGQL 2323
Cdd:cd05236   160 PPADPEKlidilelmdDLELERATPKLLGGHPNTYTFTKALAERLVLKERG--NLPLVIVRPSIVGATLkepfpGWIDNF 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489495878 2324 NMSDwvtrMVLSLMATGIApRSFYepdsegNRQRAHFDGLPVTFVAEAIAVLGARVAGSSLAGFATYHV 2392
Cdd:cd05236   238 NGPD----GLFLAYGKGIL-RTMN------ADPNAVADIIPVDVVANALLAAAAYSGVRKPRELEVYHC 295
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
 1473-1966 1.72e-30

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 129.11  E-value: 1.72e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1473 ARLDEWGNRAVLTAPAP-TPVSIPQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFER 1551
Cdd:PRK06155    1 GEPLGAGLAARAVDPLPpSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1552 CAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVTTAGLRSRLAGHDLP--------IIDVVDALAAYPG- 1622
Cdd:PRK06155   81 RIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGdlplpavwLLDAPASVSVPAGw 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1623 ---TPPPMPAAV--------NLAYILYTSGTTGEPKGVGITH-------RNVTRLFAslparLSAAQVWSQC----HSYG 1680
Cdd:PRK06155  161 staPLPPLDAPApaaavqpgDTAAILYTSGTTGPSKGVCCPHaqfywwgRNSAEDLE-----IGADDVLYTTlplfHTNA 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1681 FDAsaweIWGALLGGGRLVIVPESVAASpndFHGLLVAEHVSVLTQTPAAVAML---PTQGLES-----VALvvaGEACP 1752
Cdd:PRK06155  236 LNA----FFQALLAGATYVLEPRFSASG---FWPAVRRHGATVTYLLGAMVSILlsqPARESDRahrvrVAL---GPGVP 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1753 AALVD--RWAPGRVMLNAYGPTETT-ICAAISAPLRPGSgmppIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGA---G 1826
Cdd:PRK06155  306 AALHAafRERFGVDLLDGYGSTETNfVIAVTHGSQRPGS----MGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfA 381

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1827 VGVGYWRRAGLTASRFVACPFggsgarmyRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVV 1906
Cdd:PRK06155  382 FATGYFGMPEKTVEAWRNLWF--------HTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAV 453

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489495878 1907 IAREDRPGDKRlVGYATEIAPG-AVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKL 1966
Cdd:PRK06155  454 FPVPSELGEDE-VMAAVVLRDGtALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKV 513
PRK08316 PRK08316
acyl-CoA synthetase; Validated
 1493-1971 1.80e-30

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 128.90  E-value: 1.80e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1493 SIPQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPI 1572
Cdd:PRK08316   12 TIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1573 DPANPPPRVAFMLGDAVPVAAVTTAGLRSRL--------------------AGHDLPIIDVVDALAAYPGTPP-PMPAAV 1631
Cdd:PRK08316   92 NFMLTGEELAYILDHSGARAFLVDPALAPTAeaalallpvdtlilslvlggREAPGGWLDFADWAEAGSVAEPdVELADD 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1632 NLAYILYTSGTTGEPKGVGITHRNVTRLFAS--LPARLSAAQVWSQC----HSYGFDASAWEIwgaLLGGGRLVIVPesv 1705
Cdd:PRK08316  172 DLAQILYTSGTESLPKGAMLTHRALIAEYVSciVAGDMSADDIPLHAlplyHCAQLDVFLGPY---LYVGATNVILD--- 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1706 AASPNDFHGLLVAEHVSVLTQTPAA-VAMLPTQGLESVALVVAGEACPAA----------LVDRWaPGRVMLNAYGPTET 1774
Cdd:PRK08316  246 APDPELILRTIEAERITSFFAPPTVwISLLRHPDFDTRDLSSLRKGYYGAsimpvevlkeLRERL-PGLRFYNCYGQTEI 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1775 TICAAISAP----LRPGS-GMPPIGVPVSgaalfVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVacpfGG 1849
Cdd:PRK08316  325 APLATVLGPeehlRRPGSaGRPVLNVETR-----VVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFR----GG 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1850 sgarMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREdrpgDKRLVGYATEI---- 1925
Cdd:PRK08316  396 ----WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLP----DPKWIEAVTAVvvpk 467

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 489495878 1926 APGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:PRK08316  468 AGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKREL 513
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 1519-1971 2.20e-30

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 127.16  E-value: 2.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1519 TYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVTtag 1598
Cdd:cd05971     8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT--- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1599 lrsrlaghdlpiiDVVDalaaypgtpppmpaavNLAYILYTSGTTGEPKGVGITHRnvtRLFASLPARLSAAQVWSQCHS 1678
Cdd:cd05971    85 -------------DGSD----------------DPALIIYTSGTTGPPKGALHAHR---VLLGHLPGVQFPFNLFPRDGD 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1679 YGFDASAWEIWGALLGggrlVIVPES------VAASPNDFHG----LLVAEH-VSVLTQTPAAVAMLPTQG-------LE 1740
Cdd:cd05971   133 LYWTPADWAWIGGLLD----VLLPSLyfgvpvLAHRMTKFDPkaalDLMSRYgVTTAFLPPTALKMMRQQGeqlkhaqVK 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1741 SVALVVAGEACPAALVdRWAP---GRVMLNAYGPTETTI----CAAIsAPLRPGSgmppIGVPVSGAALFVLDSWLRPVP 1813
Cdd:cd05971   209 LRAIATGGESLGEELL-GWAReqfGVEVNEFYGQTECNLvignCSAL-FPIKPGS----MGKPIPGHRVAIVDDNGTPLP 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1814 AGVAGELYI--AGAGVGVGYWRRAGLTASRFVAcpfggsgaRMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEV 1891
Cdd:cd05971   283 PGEVGEIAVelPDPVAFLGYWNNPSATEKKMAG--------DWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEI 354

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1892 ATALAELAGVGQAVVIAREDrPGDKRLVGYATEIAPGAVDPAGLRAQL----AQRLPGYLVPAAVVVIDALPLTVNGKLD 1967
Cdd:cd05971   355 EECLLKHPAVLMAAVVGIPD-PIRGEIVKAFVVLNPGETPSDALAREIqelvKTRLAAHEYPREIEFVNELPRTATGKIR 433


                  ....
gi 489495878 1968 HRAL 1971
Cdd:cd05971   434 RREL 437
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
 1510-1971 2.78e-30

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 126.82  E-value: 2.78e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1510 AVCCGDASMTYRELDEASNRLAHRLAGCGAG-PGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDA 1588
Cdd:cd05958     3 CLRSPEREWTYRDLLALANRIANVLVGELGIvPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1589 VPVAAVttaglrsrlaghdlpiidVVDALAaypgtpppmpAAVNLAYILYTSGTTGEPKGVGITHRNVTrlfasLPARLS 1668
Cdd:cd05958    83 RITVAL------------------CAHALT----------ASDDICILAFTSGTTGAPKATMHFHRDPL-----ASADRY 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1669 AAQVWSQCHSYGFDASAWEIWGALLGGgrLVIVPESVAAS--------PNDFHGLLVAEHVSVLTQTP----AAVAMLPT 1736
Cdd:cd05958   130 AVNVLRLREDDRFVGSPPLAFTFGLGG--VLLFPFGVGASgvlleeatPDLLLSAIARYKPTVLFTAPtayrAMLAHPDA 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1737 QG--LESVALVV-AGEACPAALVDRW--APGRVMLNAYGPTET--TICAAISAPLRPGSgmppIGVPVSGAALFVLDSWL 1809
Cdd:cd05958   208 AGpdLSSLRKCVsAGEALPAALHRAWkeATGIPIIDGIGSTEMfhIFISARPGDARPGA----TGKPVPGYEAKVVDDEG 283

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1810 RPVPAGVAGELYIAGAgvgVGYWRRAGLTASRFVAcpfGGSGArmyrTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELG 1889
Cdd:cd05958   284 NPVPDGTIGRLAVRGP---TGCRYLADKRQRTYVQ---GGWNI----TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPP 353

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1890 EVATALAELAGVGQAVVIAREDRPGD---KRLVGYATEIAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKL 1966
Cdd:cd05958   354 EVEDVLLQHPAVAECAVVGHPDESRGvvvKAFVVLRPGVIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKL 433


                  ....*
gi 489495878 1967 DHRAL 1971
Cdd:cd05958   434 QRFAL 438
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
 1024-1450 6.17e-30

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 124.61  E-value: 6.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1024 PLSFAQRRLWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVDGVP-RQLVIEARRADLgCD 1102
Cdd:cd19537     3 ALSPIEREWWHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLrRSYSSSPPRVQR-VD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1103 IVDatawpadrlqraIEEAARHSFDLATEIPLRTwlfRIADDEhvLVAVAHHIAADGWSVAPLTADLSAAYasrcAGRAP 1182
Cdd:cd19537    82 TLD------------VWKEINRPFDLEREDPIRV---FISPDT--LLVVMSHIICDLTTLQLLLREVSAAY----NGKLL 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1183 dwAPLPVQYVDYTLWQREILGDlddsdspiaaQLAYWENALAGMPERL--RLPTARPYppvadqRGASLVVDWPASVQQQ 1260
Cdd:cd19537   141 --PPVRREYLDSTAWSRPASPE----------DLDFWSEYLSGLPLLNlpRRTSSKSY------RGTSRVFQLPGSLYRS 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1261 VRRIARQHNATS--FMVVAAGLAvlLSKLSGSPDVAVGFPIAGRSDPALDNLVGFFVNTLVLRV--NLAGDPSFAELLGQ 1336
Cdd:cd19537   203 LLQFSTSSGITLhqLALAAVALA--LQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRIrfPSSSDASAADFLRA 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1337 VRARSLAAYENQdVPFEVLVDRLKPTRALTHHPLIQVMLAWQDNPVGQLNLgDLQ-ATPMPIDTRTARmdlvFSLAERFS 1415
Cdd:cd19537   281 VRRSSQAALAHA-IPWHQLLEHLGLPPDSPNHPLFDVMVTFHDDRGVSLAL-PIPgVEPLYTWAEGAK----FPLMFEFT 354

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 489495878 1416 EGSEpAGIGGAVEYRTDVFEAQAIDVLIERLRKVL 1450
Cdd:cd19537   355 ALSD-DSLLLRLEYDTDCFSEEEIDRIESLILAAL 388
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
 1514-1971 2.83e-29

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 124.73  E-value: 2.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1514 GDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAA 1593
Cdd:cd05926    11 STPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1594 VTTAG-----LRSRL--------AGHDLPIIDVV---DALAAYPG-----TPPPMPAAVNLAYILYTSGTTGEPKGVGIT 1652
Cdd:cd05926    91 LTPKGelgpaSRAASklglaileLALDVGVLIRApsaESLSNLLAdkknaKSEGVPLPDDLALILHTSGTTGRPKGVPLT 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1653 HRNVTRLFASLPA--RLSAAQ----VWSQCHSYGFDASAWEIwgaLLGGGRLVIVPESvaaSPNDFHGLLVAEHVSVLTQ 1726
Cdd:cd05926   171 HRNLAASATNITNtyKLTPDDrtlvVMPLFHVHGLVASLLST---LAAGGSVVLPPRF---SASTFWPDVRDYNATWYTA 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1727 TPAAVAML-----PTQGLESVALVV---AGEACPAALVDRW-----APgrvMLNAYGPTETTiCAAISAPL-----RPGS 1788
Cdd:cd05926   245 VPTIHQILlnrpePNPESPPPKLRFirsCSASLPPAVLEALeatfgAP---VLEAYGMTEAA-HQMTSNPLppgprKPGS 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1789 gmppIGVPVsGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFggsgarmYRTGDLVCWRADGQ 1868
Cdd:cd05926   321 ----VGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW-------FRTGDLGYLDADGY 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1869 LEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAredRPGDKrlvgYATEIA-------PGAVDPAGLRAQLAQ 1941
Cdd:cd05926   389 LFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFG---VPDEK----YGEEVAaavvlreGASVTEEELRAFCRK 461

                         490       500       510
                  ....*....|....*....|....*....|
gi 489495878 1942 RLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:cd05926   462 HLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
MupV_like_SDR_e cd05263
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ...
 2110-2395 2.63e-28

Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family domains have the characteristic active site tetrad and a well-conserved NAD(P)-binding motif. This subgroup is not well characterized, its members are annotated as having a variety of putative functions. One characterized member is Pseudomonas fluorescens MupV a protein involved in the biosynthesis of Mupirocin, a polyketide-derived antibiotic. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187573 [Multi-domain]  Cd Length: 293  Bit Score: 117.47  E-value: 2.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2110 VLLTGATGFLGRYLVLELLRRldvDGRLICLVRAESDEDARRRLEKTfdsgdpellrhfkELAADRLEVVAGDKSEPDLG 2189
Cdd:cd05263     1 VFVTGGTGFLGRHLVKRLLEN---GFKVLVLVRSESLGEAHERIEEA-------------GLEADRVRVLEGDLTQPNLG 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2190 LDQPMWRRLAETVDLIVDSAAMVN-AFPYHELFGPNVAGTAELIRIALTTKLKPFTYVSTAdvGAAIEPS-AFTEDADir 2267
Cdd:cd05263    65 LSAAASRELAGKVDHVIHCAASYDfQAPNEDAWRTNIDGTEHVLELAARLDIQRFHYVSTA--YVAGNREgNIRETEL-- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2268 visptrTVDGGWAGGYGTSKWAGEVLLREANDlcALPVAVFRCGMILADtSYAGQLNMSDWVTRMVLSLMATGIAPRSfy 2347
Cdd:cd05263   141 ------NPGQNFKNPYEQSKAEAEQLVRAAAT--QIPLTVYRPSIVVGD-SKTGRIEKIDGLYELLNLLAKLGRWLPM-- 209

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 489495878 2348 ePDSEGNRqrahFDGLPVTFVAEAIavlgARVAGSSLAGFATYHVMNP 2395
Cdd:cd05263   210 -PGNKGAR----LNLVPVDYVADAI----VYLSKKPEANGQIFHLTDP 248
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
 1484-1977 3.28e-28

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 122.38  E-value: 3.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1484 LTAPAptpVSIPQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAG-CGAGPGECVALLFERCAPAVVAMVAV 1562
Cdd:PRK08314    5 LTLPE---TSLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1563 LKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVTTAGLRSRL--AGHDLPIIDVV-----DALAAYPG------------- 1622
Cdd:PRK08314   82 LRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVapAVGNLRLRHVIvaqysDYLPAEPEiavpawlraeppl 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1623 -------------------TPPPMPAAVN-LAYILYTSGTTGEPKGVGITHRNVTrlfaslpARLSAAQVWSQC------ 1676
Cdd:PRK08314  162 qalapggvvawkealaaglAPPPHTAGPDdLAVLPYTSGTTGVPKGCMHTHRTVM-------ANAVGSVLWSNStpesvv 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1677 -------HSYGFDASaweIWGALLGGGRLVIVP--ESVAAspndfhGLLVAEH-VSVLTQTPA-AVAMLPTQGLE----- 1740
Cdd:PRK08314  235 lavlplfHVTGMVHS---MNAPIYAGATVVLMPrwDREAA------ARLIERYrVTHWTNIPTmVVDFLASPGLAerdls 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1741 SVALVVAGEAC-PAA----LVDRWapGRVMLNAYGPTETTICAAISAPLRPGS---GMPPIGVPvsgaALFVLDSWLRPV 1812
Cdd:PRK08314  306 SLRYIGGGGAAmPEAvaerLKELT--GLDYVEGYGLTETMAQTHSNPPDRPKLqclGIPTFGVD----ARVIDPETLEEL 379

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1813 PAGVAGELYIAGAGVGVGYWRRAGLTASRFVACpfggSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVA 1892
Cdd:PRK08314  380 PPGEVGEIVVHGPQVFKGYWNRPEATAEAFIEI----DGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVE 455

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1893 TALAELAGVGQAVVIA-REDRPGD--KRLVGYATEiAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHR 1969
Cdd:PRK08314  456 NLLYKHPAIQEACVIAtPDPRRGEtvKAVVVLRPE-ARGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWR 534


                  ....*...
gi 489495878 1970 ALPAPEYG 1977
Cdd:PRK08314  535 QLQEQEKA 542
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 1514-1970 1.05e-27

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 120.81  E-value: 1.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1514 GDASMTYRELDEASNRLAHRLAGCGAgPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPP---PRVAFMLGDAVP 1590
Cdd:cd05931    21 REETLTYAELDRRARAIAARLQAVGK-PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGrhaERLAAILADAGP 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1591 VAAVTTAGLRSRLAGH-------DLPIIDVVDALAAYPGT--PPPMPAAVNLAYILYTSGTTGEPKGVGITHRNVtrlfa 1661
Cdd:cd05931   100 RVVLTTAAALAAVRAFaasrpaaGTPRLLVVDLLPDTSAAdwPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNL----- 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1662 slparlsAAQVWSQCHSYGFDASA----W-----------EIWGALLGGGRLVIVpesvaaSPNDFhgL--------LVA 1718
Cdd:cd05931   175 -------LANVRQIRRAYGLDPGDvvvsWlplyhdmgligGLLTPLYSGGPSVLM------SPAAF--LrrplrwlrLIS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1719 EHVSVLTQTPA-----AVAMLPTQGLESVAL------VVAGEACPAALVDRWA--------PGRVMLNAYGPTETTI--- 1776
Cdd:cd05931   240 RYRATISAAPNfaydlCVRRVRDEDLEGLDLsswrvaLNGAEPVRPATLRRFAeafapfgfRPEAFRPSYGLAEATLfvs 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1777 --------------CAAISAPLRPGSGMPPIGVPVSGAALFVLDSWLR--------PVPAGVAGELYIAGAGVGVGYWRR 1834
Cdd:cd05931   320 ggppgtgpvvlrvdRDALAGRAVAVAADDPAARELVSCGRPLPDQEVRivdpetgrELPDGEVGEIWVRGPSVASGYWGR 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1835 AGLTASRFVACPfGGSGARMYRTGDLvCWRADGQLEFLGRTDDQVKIRGYRI---ELGEVATALAELAGVGQAVVIARED 1911
Cdd:cd05931   400 PEATAETFGALA-ATDEGGWLRTGDL-GFLHDGELYITGRLKDLIIVRGRNHypqDIEATAEEAHPALRPGCVAAFSVPD 477

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489495878 1912 RPGDKRLVGYATEIAPGAVDPAGLRAQLAQRLP---GyLVPAAVVVI--DALPLTVNGKLDHRA 1970
Cdd:cd05931   478 DGEERLVVVAEVERGADPADLAAIAAAIRAAVArehG-VAPADVVLVrpGSIPRTSSGKIQRRA 540
benz_CoA_lig TIGR02262
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ...
 1517-1966 3.42e-27

benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.


Pssm-ID: 274059 [Multi-domain]  Cd Length: 505  Bit Score: 118.40  E-value: 3.42e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1517 SMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVTT 1596
Cdd:TIGR02262   30 SLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVS 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1597 AGLRS--RLAGHDLPIIDVV----------DALAAYPGTPPPM--PAAV---NLAYILYTSGTTGEPKGVGITHRNVtRL 1659
Cdd:TIGR02262  110 GALLPviKAALGKSPHLEHRvvvgrpeageVQLAELLATESEQfkPAATqadDPAFWLYSSGSTGMPKGVVHTHSNP-YW 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1660 FASLPAR-----------LSAAQVWsqcHSYGFdasaweiwgallggGRLVIVPESVAAS---------PNDFHGLLVAE 1719
Cdd:TIGR02262  189 TAELYARntlgireddvcFSAAKLF---FAYGL--------------GNALTFPMSVGATtvlmgerptPDAVFDRLRRH 251

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1720 HVSVLTQTPAAVA-ML-----PTQGLESVALVV-AGEACPAALVDRWAP--GRVMLNAYGPTETTICAAISAPLRPGSGM 1790
Cdd:TIGR02262  252 QPTIFYGVPTLYAaMLadpnlPSEDQVRLRLCTsAGEALPAEVGQRWQArfGVDIVDGIGSTEMLHIFLSNLPGDVRYGT 331

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1791 PpiGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVAcpfggsgaRMYRTGDLVCWRADGQLE 1870
Cdd:TIGR02262  332 S--GKPVPGYRLRLVGDGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTFQG--------EWTRSGDKYVRNDDGSYT 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  1871 FLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATEIAPGAVDPAGLRAQLAQRLPGYLVPA 1950
Cdd:TIGR02262  402 YAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTALETELKEHVKDRLAPYKYPR 481

                          490
                   ....*....|....*.
gi 489495878  1951 AVVVIDALPLTVNGKL 1966
Cdd:TIGR02262  482 WIVFVDDLPKTATGKI 497
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
 1496-1971 6.15e-27

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 117.61  E-value: 6.15e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1496 QMLAAQVARIPEAEAVC--CGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPID 1573
Cdd:cd05923     5 EMLRRAASRAPDACAIAdpARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALIN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1574 P-----------ANPPPRVAFMLGDAVPVAAVTTAGLRSrLAGHDLPIIDVVDALAAYPGTPPPMPAAVnlAYILYTSGT 1642
Cdd:cd05923    85 PrlkaaelaeliERGEMTAAVIAVDAQVMDAIFQSGVRV-LALSDLVGLGEPESAGPLIEDPPREPEQP--AFVFYTSGT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1643 TGEPKGVGITHRNVTR--LFASLPARLSAAQ------VWSQCHSYGFDASaweIWGALLGGGRLVIVPESvaaSPNDFHG 1714
Cdd:cd05923   162 TGLPKGAVIPQRAAESrvLFMSTQAGLRHGRhnvvlgLMPLYHVIGFFAV---LVAALALDGTYVVVEEF---DPADALK 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1715 LLVAEHVSVLTQTP-------AAVAMLPTQgLESV-ALVVAGEACPAALVDR---WAPGRVmLNAYGPTETTICAAISAP 1783
Cdd:cd05923   236 LIEQERVTSLFATPthldalaAAAEFAGLK-LSSLrHVTFAGATMPDAVLERvnqHLPGEK-VNIYGTTEAMNSLYMRDA 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1784 lRPGSGMPPiGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAG--VGVGYWRRAGLTASRFVAcpfggsgaRMYRTGDLV 1861
Cdd:cd05923   314 -RTGTEMRP-GFFSEVRIVRIGGSPDEALANGEEGELIVAAAAdaAFTGYLNQPEATAKKLQD--------GWYRTGDVG 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1862 CWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATeIAPGAVDPAGLRA-QLA 1940
Cdd:cd05923   384 YVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVV-PREGTLSADELDQfCRA 462

                         490       500       510
                  ....*....|....*....|....*....|.
gi 489495878 1941 QRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:cd05923   463 SELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
 1519-1966 1.18e-26

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 118.06  E-value: 1.18e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1519 TYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVTTAG 1598
Cdd:cd17634    86 SYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADG 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1599 LRSRlaGHDLPIIDVVDALAAYPGTPPP---------------------------------MPAAVNLA---YILYTSGT 1642
Cdd:cd17634   166 GVRA--GRSVPLKKNVDDALNPNVTSVEhvivlkrtgsdidwqegrdlwwrdliakaspehQPEAMNAEdplFILYTSGT 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1643 TGEPKGVGITHRNVTrlfaslparLSAAQVWSQCHSYG-------------FDASAWEIWGALLGGGRLVI---VPesVA 1706
Cdd:cd17634   244 TGKPKGVLHTTGGYL---------VYAATTMKYVFDYGpgdiywctadvgwVTGHSYLLYGPLACGATTLLyegVP--NW 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1707 ASPNDFHGLLVAEHVSVLTQTPAAVAMLPTQGLESVA---------LVVAGEAC-PAALvdRWA------PGRVMLNAYG 1770
Cdd:cd17634   313 PTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEgtdrsslriLGSVGEPInPEAY--EWYwkkigkEKCPVVDTWW 390

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1771 PTETT--ICA--AISAPLRPGSGMppigVPVSGAALFVLDSWLRPVPAGVAGELYIAGA--GVGVGYWRRAGLTASRFVA 1844
Cdd:cd17634   391 QTETGgfMITplPGAIELKAGSAT----RPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHERFEQTYFS 466

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1845 cPFGGsgarMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATe 1924
Cdd:cd17634   467 -TFKG----MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVV- 540

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 489495878 1925 IAPGAVDPAGLRAQL----AQRLPGYLVPAAVVVIDALPLTVNGKL 1966
Cdd:cd17634   541 LNHGVEPSPELYAELrnwvRKEIGPLATPDVVHWVDSLPKTRSGKI 586
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 473-911 1.23e-26

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 116.60  E-value: 1.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  473 AWLVQRGAAPGDVLVFTDDDTDKTIDLLIACHLAGCGYSVCDtADEISVRTNAITEHGdGILVTVVDVAATQLAVVGHDE 552
Cdd:cd12114    27 GALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVD-IDQPAARREAILADA-GARLVLTDGPDAQLDVAVFDV 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  553 LrkvVDERVTQVTHDALLATKT-----AYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDIS 627
Cdd:cd12114   105 L---ILDLDALAAPAPPPPVDVapddlAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFDLS 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  628 VEEIFGGAACGARLVRSAAMKTGDLAALVDDLVARETTIVDLPTAVWQLLCADGDAIDAIGRSrLRQIVIGGEAIRCSAV 707
Cdd:cd12114   182 VYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQALLPS-LRLVLLSGDWIPLDLP 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  708 DKWLESAAsqGISLLSSYGPTEATVVATFLPIvcDQTTMDGALLRLGRPiLPNTVF------------LAFGEVVIVGDL 775
Cdd:cd12114   261 ARLRALAP--DARLISLGGATEASIWSIYHPI--DEVPPDWRSIPYGRP-LANQRYrvldprgrdcpdWVPGELWIGGRG 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  776 VADGYLgidGDGFGT----VTAADGsrRRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDV 851
Cdd:cd12114   336 VALGYL---GDPELTaarfVTHPDG--ERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARA 410

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489495878  852 AV----ELHSGSLGVWFKSQrtREGEQDAAAATRIRLV--LVSLGVSSFFVVgVPNIPRKPNGKID 911
Cdd:cd12114   411 VVvvlgDPGGKRLAAFVVPD--NDGTPIAPDALRAFLAqtLPAYMIPSRVIA-LEALPLTANGKVD 473
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
 1633-1971 1.51e-26

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 116.28  E-value: 1.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1633 LAYILYTSGTTGEPKGVGITHRNVTRLFASLPARLSAAQVWSQC------HSYGFDASaweIWGALLGGGrlvivpeSVA 1706
Cdd:cd05909   149 PAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFgalpffHSFGLTGC---LWLPLLSGI-------KVV 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1707 ASPNDFHGLLVAE-----HVSVLTQTPA-----AVAMLPTQgLESVALVVAG-EACPAALVDRWAP--GRVMLNAYGPTE 1773
Cdd:cd05909   219 FHPNPLDYKKIPEliydkKATILLGTPTflrgyARAAHPED-FSSLRLVVAGaEKLKDTLRQEFQEkfGIRILEGYGTTE 297

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1774 TTICAAISAPL---RPGSgmppIGVPVSG-AALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFvacpfgg 1849
Cdd:cd05909   298 CSPVISVNTPQspnKEGT----VGRPLPGmEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF------- 366

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1850 sGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAG--VGQAVVIAREDRPGDKRLVGYATEIAp 1927
Cdd:cd05909   367 -GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPedNEVAVVSVPDGRKGEKIVLLTTTTDT- 444

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 489495878 1928 gavDPAGLRAQL-AQRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:cd05909   445 ---DPSSLNDILkNAGISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
 1514-1974 1.60e-26

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 116.72  E-value: 1.60e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1514 GDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAA 1593
Cdd:PRK12406    8 GDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1594 VTTAGLRSRLAGHDLPIIDVVDA------LAAY------------------------PGTPPPMPAAVNLayiLYTSGTT 1643
Cdd:PRK12406   88 IAHADLLHGLASALPAGVTVLSVptppeiAAAYrispalltppagaidwegwlaqqePYDGPPVPQPQSM---IYTSGTT 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1644 GEPKGVgithrnvtRLFASLPaRLSAAQVWSQCHSYGFDA------------SAWEIWG--ALLGGGRLVIVPEsvaASP 1709
Cdd:PRK12406  165 GHPKGV--------RRAAPTP-EQAAAAEQMRALIYGLKPgiralltgplyhSAPNAYGlrAGRLGGVLVLQPR---FDP 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1710 NDFHGLLVAEHVSVLTQTPAA---VAMLPTQ-----GLESVALVVAGEA-CPA----ALVDRWAPgrVMLNAYGPTET-- 1774
Cdd:PRK12406  233 EELLQLIERHRITHMHMVPTMfirLLKLPEEvrakyDVSSLRHVIHAAApCPAdvkrAMIEWWGP--VIYEYYGSTESga 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1775 -TICAAISAPLRPGSgmppIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVG-VGYW---------RRAGLTASrfv 1843
Cdd:PRK12406  311 vTFATSEDALSHPGT----VGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPdFTYHnkpekraeiDRGGFITS--- 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1844 acpfggsgarmyrtGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYaT 1923
Cdd:PRK12406  384 --------------GDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAV-V 448

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489495878 1924 EIAPGA-VDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRALPAP 1974
Cdd:PRK12406  449 EPQPGAtLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
 564-915 5.00e-26

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 114.11  E-value: 5.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  564 VTHDALLATKTAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARL-- 641
Cdd:cd17654   110 RHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLli 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  642 VRSAAMKTGDLAALVDDLVARETTIVDLPTAVWQLLCADGDAIDAIGRSRLRQIVIGGEAIRCSAVDK-WleSAASQGIS 720
Cdd:cd17654   190 VPTSVKVLPSKLADILFKRHRITVLQATPTLFRRFGSQSIKSTVLSATSSLRVLALGGEPFPSLVILSsW--RGKGNRTR 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  721 LLSSYGPTEATVVATFLPIVCDQTTmdgalLRLGRPILpntvflafGEVVIVGDLVADGYLGIDGDGF--------GTVT 792
Cdd:cd17654   268 IFNIYGITEVSCWALAYKVPEEDSP-----VQLGSPLL--------GTVIEVRDQNGSEGTGQVFLGGlnrvcildDEVT 334

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  793 AADGSRRrafATGDRVTVDaEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAVelhsgslgVWFKSQR---- 868
Cdd:cd17654   335 VPKGTMR---ATGDFVTVK-DGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAV--------TLSDQQRliaf 402

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 489495878  869 TREGEQDAAAATRIRLVLVSLGVSSFFVVGVPNIPRKPNGKIDSDNL 915
Cdd:cd17654   403 IVGESSSSRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
 1494-1971 8.65e-26

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 114.47  E-value: 8.65e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1494 IPQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPG-----------ECVALLFercapavvamvAV 1562
Cdd:COG1021    27 LGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGdrvvvqlpnvaEFVIVFF-----------AL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1563 LKTGAAylpidPANPPPR---------------VAFMLGDAVP----------VAAvTTAGLRSRLAGHDL-PIIDVVDA 1616
Cdd:COG1021    96 FRAGAI-----PVFALPAhrraeishfaeqseaVAYIIPDRHRgfdyralareLQA-EVPSLRHVLVVGDAgEFTSLDAL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1617 LAAYPGTPPPMPAAVNLAYILYTSGTTGEPKGVGITHR----NV------------TRLFASLPArlsaaqvwsqCHSYG 1680
Cdd:COG1021   170 LAAPADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDdylySVrasaeicgldadTVYLAALPA----------AHNFP 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1681 FdaSAWEIWGALLGGGRLVIVPEsvaASPNDFHGLLVAEHVSVLTQTPAAVAMLptqgLESVA-----------LVVAGE 1749
Cdd:COG1021   240 L--SSPGVLGVLYAGGTVVLAPD---PSPDTAFPLIERERVTVTALVPPLALLW----LDAAErsrydlsslrvLQVGGA 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1750 ACPAALVDRWAP--GRVMLNAYGPTETTICAAisaplRPGSgmPP------IGVPVSGA-ALFVLDSWLRPVPAGVAGEL 1820
Cdd:COG1021   311 KLSPELARRVRPalGCTLQQVFGMAEGLVNYT-----RLDD--PEevilttQGRPISPDdEVRIVDEDGNPVPPGEVGEL 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1821 YIAGAGVGVGYWRRAGLTASRFVACPFggsgarmYRTGDLVCWRADGQLEFLGRTDDQVkIR-GYRIELGEVATALAELA 1899
Cdd:COG1021   384 LTRGPYTIRGYYRAPEHNARAFTPDGF-------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHP 455

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489495878 1900 GVGQAVVIAREDrpgdkRLVGYAT----EIAPGAVDPAGLRAQLAQR-LPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:COG1021   456 AVHDAAVVAMPD-----EYLGERScafvVPRGEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 1518-1966 4.39e-25

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 111.07  E-value: 4.39e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1518 MTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVTTA 1597
Cdd:cd05973     1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1598 GLRSRLAGhdlpiidvvdalaaypgtpppmpaavNLAYILYTSGTTGEPKGVgithrnvtrlfaslPARLSAAQVWSQCH 1677
Cdd:cd05973    81 ANRHKLDS--------------------------DPFVMMFTSGTTGLPKGV--------------PVPLRALAAFGAYL 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1678 SYGFD----ASAWEI----W---------GALLGGGRLVIV-----PESV------------AASPNDFHGLLVAehvsv 1723
Cdd:cd05973   121 RDAVDlrpeDSFWNAadpgWayglyyaitGPLALGHPTILLeggfsVESTwrvierlgvtnlAGSPTAYRLLMAA----- 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1724 ltqtPAAVAMLPTQGLESVAlvVAGEACPAAlVDRWAPGRVML---NAYGPTETTICAA----ISAPLRPGSgmppIGVP 1796
Cdd:cd05973   196 ----GAEVPARPKGRLRRVS--SAGEPLTPE-VIRWFDAALGVpihDHYGQTELGMVLAnhhaLEHPVHAGS----AGRA 264

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1797 VSGAALFVLDSWLRPVPAGVAGELYIAGAGVGV----GYWRRAGLTASrfvacpfggsgARMYRTGDLVCWRADGQLEFL 1872
Cdd:cd05973   265 MPGWRVAVLDDDGDELGPGEPGRLAIDIANSPLmwfrGYQLPDTPAID-----------GGYYLTGDTVEFDPDGSFSFI 333

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1873 GRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDrPGDKRLVGYATEIAPGAVDPAGLRAQLA----QRLPGYLV 1948
Cdd:cd05973   334 GRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPD-PERTEVVKAFVVLRGGHEGTPALADELQlhvkKRLSAHAY 412

                         490
                  ....*....|....*...
gi 489495878 1949 PAAVVVIDALPLTVNGKL 1966
Cdd:cd05973   413 PRTIHFVDELPKTPSGKI 430
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 1519-1971 8.30e-25

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 111.57  E-value: 8.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1519 TYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDA---VPVAAVT 1595
Cdd:cd12119    27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAedrVVFVDRD 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1596 TAGLRSRLAGHdLPIIDVVDALAayPGTPPPMPAAVNL------------------------AYILYTSGTTGEPKGVGI 1651
Cdd:cd12119   107 FLPLLEAIAPR-LPTVEHVVVMT--DDAAMPEPAGVGVlayeellaaespeydwpdfdentaAAICYTSGTTGNPKGVVY 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1652 THRNVtrLFASLPARLSAAQVWSQCHSY-----GFDASAWEI-WGALLGGGRLVIvPeSVAASPNDFHGLLVAEHVSVlt 1725
Cdd:cd12119   184 SHRSL--VLHAMAALLTDGLGLSESDVVlpvvpMFHVNAWGLpYAAAMVGAKLVL-P-GPYLDPASLAELIEREGVTF-- 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1726 qtpaaVAMLPT--QGLES------------VALVVAGEACPAALVDRWAPGRV-MLNAYGPTETTICAAISAPLRPGSGM 1790
Cdd:cd12119   258 -----AAGVPTvwQGLLDhleangrdlsslRRVVIGGSAVPRSLIEAFEERGVrVIHAWGMTETSPLGTVARPPSEHSNL 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1791 PP---------IGVPVSGAALFVLDSWLRPVPA-GVA-GELYIAGAGVGVGYWRRAGLTASRFVacpfGGsgarMYRTGD 1859
Cdd:cd12119   333 SEdeqlalrakQGRPVPGVELRIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKNDEESEALTE----DG----WLRTGD 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1860 LVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATeIAPGA-VDPAGLRAQ 1938
Cdd:cd12119   405 VATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVV-LKEGAtVTAEELLEF 483

                         490       500       510
                  ....*....|....*....|....*....|...
gi 489495878 1939 LAQRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:cd12119   484 LADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 558-916 1.24e-24

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 109.95  E-value: 1.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  558 DERVTQVTHD---ALLATKT---AYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEI 631
Cdd:cd17645    84 GERIAYMLADssaKILLTNPddlAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEI 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  632 FGGAACGARL-VRSAAMKTgDLAALVDDLVARETTIVDLPTAVwqllcadGDAIDAIGRSRLRQIVIGGeaircsavDKw 710
Cdd:cd17645   164 FPHLTAGAALhVVPSERRL-DLDALNDYFNQEGITISFLPTGA-------AEQFMQLDNQSLRVLLTGG--------DK- 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  711 LESAASQGISLLSSYGPTEATVVATFLPIvcdqtTMDGALLRLGRPIlPNTVFLAFGEVVIVGDLVADGYLGIDGDGF-- 788
Cdd:cd17645   227 LKKIERKGYKLVNNYGPTENTVVATSFEI-----DKPYANIPIGKPI-DNTRVYILDEALQLQPIGVAGELCIAGEGLar 300

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  789 GTVTAADGSRR-----------RAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAVEL-- 855
Cdd:cd17645   301 GYLNRPELTAEkfivhpfvpgeRMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAke 380

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489495878  856 ---HSGSLGVWFKSQrtREGEQDAAAATrIRLVLVSLGVSSFFVVgVPNIPRKPNGKIDSDNLP 916
Cdd:cd17645   381 dadGRKYLVAYVTAP--EEIPHEELREW-LKNDLPDYMIPTYFVH-LKALPLTANGKVDRKALP 440
PRK06145 PRK06145
acyl-CoA synthetase; Validated
 1492-1971 2.08e-24

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 109.98  E-value: 2.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1492 VSIPQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLP 1571
Cdd:PRK06145    2 FNLSASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1572 IDPANPPPRVAFMLGDA------------VPVAAVTTAGLRSRLAGHDLPIIdvvdALAAYPGTPPPMPAAVNLAYILYT 1639
Cdd:PRK06145   82 INYRLAADEVAYILGDAgaklllvdeefdAIVALETPKIVIDAAAQADSRRL----AQGGLEIPPQAAVAPTDLVRLMYT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1640 SGTTGEPKGVGITHRNVTRLFASLPARLSAAQ------VWSQCHSYGFDASAWEIwgaLLGGGRLVIV----PESVAASP 1709
Cdd:PRK06145  158 SGTTDRPKGVMHSYGNLHWKSIDHVIALGLTAserllvVGPLYHVGAFDLPGIAV---LWVGGTLRIHrefdPEAVLAAI 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1710 NDfHGLLVAEHVSVLTqtpAAVAMLPTQ---GLESVALVVA-GEACPAALV---DRWAPGRVMLNAYGPTETTICAAISA 1782
Cdd:PRK06145  235 ER-HRLTCAWMAPVML---SRVLTVPDRdrfDLDSLAWCIGgGEKTPESRIrdfTRVFTRARYIDAYGLTETCSGDTLME 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1783 PLRPGSGMPPIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFvacpFGGsgarMYRTGDLVC 1862
Cdd:PRK06145  311 AGREIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF----YGD----WFRSGDVGY 382

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1863 WRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVI-AREDRPGDKrlVGYATEIAPGA-VDPAGLRAQLA 1940
Cdd:PRK06145  383 LDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIgVHDDRWGER--ITAVVVLNPGAtLTLEALDRHCR 460

                         490       500       510
                  ....*....|....*....|....*....|.
gi 489495878 1941 QRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:PRK06145  461 QRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
 1038-1353 3.41e-24

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 107.77  E-value: 3.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1038 LQRPApVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVF---PAVDGVprQLVIeaRRADLgcdivdatAWP-ADR 1113
Cdd:cd19545    16 ARQPG-AYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIvqsDSGGLL--QVVV--KESPI--------SWTeSTS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1114 LQRAIEEAARHSFDLATeiPL-RTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYASRCAGRAPDWAPLpVQYV 1192
Cdd:cd19545    83 LDEYLEEDRAAPMGLGG--PLvRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQPPPFSRF-VKYL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1193 DYTlwqreilgDLDDSDSpiaaqlaYWENALAG--MPERLRLPTARpYPPVADQRgASLVVDWPASVQQQVrriarqhna 1270
Cdd:cd19545   160 RQL--------DDEAAAE-------FWRSYLAGldPAVFPPLPSSR-YQPRPDAT-LEHSISLPSSASSGV--------- 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1271 TSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGRSDPA--LDNLVGFFVNTLVLRVNLAGDPSFAELLGQVRARSLAAyenq 1348
Cdd:cd19545   214 TLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVpgIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDM---- 289


                  ....*
gi 489495878 1349 dVPFE 1353
Cdd:cd19545   290 -IPFE 293
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
 1501-1966 8.82e-24

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 108.33  E-value: 8.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1501 QVAR----IPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPAN 1576
Cdd:PRK07786   22 QLARhalmQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1577 PPPRVAFMLGDAVPVAAVTTAGLRSRLAG--HDLPIIDVV--------------DALAAYPGTPPPmPAAV---NLAYIL 1637
Cdd:PRK07786  102 TPPEIAFLVSDCGAHVVVTEAALAPVATAvrDIVPLLSTVvvaggssddsvlgyEDLLAEAGPAHA-PVDIpndSPALIM 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1638 YTSGTTGEPKGVGITHRN-----VTRLFASlpaRLSAAqvwsqcHSYGFDASA-WEIWG------ALLGGGRLVIVPESv 1705
Cdd:PRK07786  181 YTSGTTGRPKGAVLTHANltgqaMTCLRTN---GADIN------SDVGFVGVPlFHIAGigsmlpGLLLGAPTVIYPLG- 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1706 AASPNDFHGLLVAEHVSVLTQTPA---AVAMLPTQGLESVAL-VVAGEACPA--ALVDRWA---PGRVMLNAYGPTE--- 1773
Cdd:PRK07786  251 AFDPGQLLDVLEAEKVTGIFLVPAqwqAVCAEQQARPRDLALrVLSWGAAPAsdTLLRQMAatfPEAQILAAFGQTEmsp 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1774 -TTICAAISAPLRPGSgmppIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVacpfGGsga 1852
Cdd:PRK07786  331 vTCMLLGEDAIRKLGS----VGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFA----GG--- 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1853 rMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATEIAPGA-VD 1931
Cdd:PRK07786  400 -WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAaLT 478

                         490       500       510
                  ....*....|....*....|....*....|....*
gi 489495878 1932 PAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKL 1966
Cdd:PRK07786  479 LEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
267-1021 9.28e-24

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 110.52  E-value: 9.28e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  267 RFGDSDLNVATCLVNSVAQTVRFPPFASVSDVVRTLDRGYVKAVRRRWLREEHYRRMYLAINRTSHVEALTLN---FIRE 343
Cdd:PRK10252  281 RLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAAQLKKMRRHQRYDAEQIVRDSGRAAGDEPLFGPVLNikvFDYQ 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  344 PCAPGLRPFLSEvpIATdiGPVEGMTVASVLDEeQRTLNLAIWNRADLPACKTHPKVAERIAAALESMAAMWDRPIAMI- 422
Cdd:PRK10252  361 LDFPGVQAQTHT--LAT--GPVNDLELALFPDE-HGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVd 435

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  423 ------------VNDWFGIGPDGTRCQ--GDWPARQPSTPAWfldsARGVHQFLGR--RRFVYPWVAWLVQRGAAPGDVL 486
Cdd:PRK10252  436 illpgeyaqlaqVNATAVEIPETTLSAlvAQQAAKTPDAPAL----ADARYQFSYRemREQVVALANLLRERGVKPGDSV 511

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  487 VFTDDDTDKTIDLLIACHLAGCGYSVCDTAdeisvrtnaiteHGDGILVTVVDVAATQLAVVGHDELRKVVD-ERVTQVT 565
Cdd:PRK10252  512 AVALPRSVFLTLALHAIVEAGAAWLPLDTG------------YPDDRLKMMLEDARPSLLITTADQLPRFADvPDLTSLC 579

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  566 HDALLAT------------KTAYIMPTSGTTGQPKLVRISHgslavfcDAI-------SRAYGWGAHDTVLQCAPLTSDI 626
Cdd:PRK10252  580 YNAPLAPqgaaplqlsqphHTAYIIFTSGSTGRPKGVMVGQ-------TAIvnrllwmQNHYPLTADDVVLQKTPCSFDV 652

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  627 SVEEIFGGAACGARLVRSAAMKTGDLAALvDDLVARE--TTIVDLPTAVWQLLCADGDAIDAIGRSRLRQIVIGGEAIRC 704
Cdd:PRK10252  653 SVWEFFWPFIAGAKLVMAEPEAHRDPLAM-QQFFAEYgvTTTHFVPSMLAAFVASLTPEGARQSCASLRQVFCSGEALPA 731

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  705 SAVDKWLESAASQgisLLSSYGPTEATVVATFLPIVC-DQTTMDGALLRLGRPILpNT---VFLAFGEVV---IVGDL-- 775
Cdd:PRK10252  732 DLCREWQQLTGAP---LHNLYGPTEAAVDVSWYPAFGeELAAVRGSSVPIGYPVW-NTglrILDARMRPVppgVAGDLyl 807

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  776 ----VADGYLGIDGdgfgtVTA----AD--GSRRRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAED 845
Cdd:PRK10252  808 tgiqLAQGYLGRPD-----LTAsrfiADpfAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQAL 882

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  846 PAVSDV---AVELHSGSLG-------VWFKSQRTREGEQDAAAATRIRLVLVSLGVSSFFvVGVPNIPRKPNGKIDSDNL 915
Cdd:PRK10252  883 PDVEQAvthACVINQAAATggdarqlVGYLVSQSGLPLDTSALQAQLRERLPPHMVPVVL-LQLDQLPLSANGKLDRKAL 961

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  916 PRLPQWSAAGLNTAETGQRAAgLSQIWSRQLGR-AIGPDSSLLGEGIGSLDLIRILPETRRYLGWRLSLLDLIGADTAAN 994
Cdd:PRK10252  962 PLPELKAQVPGRAPKTGTETI-IAAAFSSLLGCdVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAK 1040

                         810       820       830
                  ....*....|....*....|....*....|
gi 489495878  995 LA---DYAPTPDAPTGEDRFRPLVAAQRPA 1021
Cdd:PRK10252 1041 LAtllDAEEDESRRLGFGTILPLREGDGPT 1070
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
 1516-1911 2.11e-23

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 106.94  E-value: 2.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1516 ASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVT 1595
Cdd:cd05904    31 RALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFT 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1596 TAGLRSRLAGHDLPII----DVVDALAAYPGT---PPPMPAAVN-----LAYILYTSGTTGEPKGVGITHRNvtrLFASL 1663
Cdd:cd05904   111 TAELAEKLASLALPVVlldsAEFDSLSFSDLLfeaDEAEPPVVVikqddVAALLYSSGTTGRSKGVMLTHRN---LIAMV 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1664 parlsAAQVWSQ----------------CHSYGFdasAWEIWGALLGGGRLVIVPESvaaspnDFHGLL--VAEH-VSVL 1724
Cdd:cd05904   188 -----AQFVAGEgsnsdsedvflcvlpmFHIYGL---SSFALGLLRLGATVVVMPRF------DLEELLaaIERYkVTHL 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1725 TQTPAAVAMLPTQG------LESVALVVAGEA-CPAALVDRWA---PGRVMLNAYGPTETTICAA-----ISAPLRPGSg 1789
Cdd:cd05904   254 PVVPPIVLALVKSPivdkydLSSLRQIMSGAApLGKELIEAFRakfPNVDLGQGYGMTESTGVVAmcfapEKDRAKYGS- 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1790 mppIGVPVSGA-ALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVacpfggsGARMYRTGDLVCWRADGQ 1868
Cdd:cd05904   333 ---VGRLVPNVeAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATID-------KEGWLHTGDLCYIDEDGY 402

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 489495878 1869 LEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIARED 1911
Cdd:cd05904   403 LFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPD 445
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
 1517-1942 2.55e-23

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 105.76  E-value: 2.55e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1517 SMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVTt 1596
Cdd:cd05907     5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1597 aglrsrlaghdlpiidvvdalaaypgtpppmPAAVNLAYILYTSGTTGEPKGVGITHRNVTRLFASLPARLSAAQVWSQ- 1675
Cdd:cd05907    84 -------------------------------EDPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHl 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1676 -----CHSYGFDASaweIWGALLGGGRLV-------IVPESVAASPNDFHGLL-----VAEHVSVLTQTPAAVAMLPTQG 1738
Cdd:cd05907   133 sflplAHVFERRAG---LYVPLLAGARIYfassaetLLDDLSEVRPTVFLAVPrvwekVYAAIKVKAVPGLKRKLFDLAV 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1739 LESV-ALVVAGEACPAALVDRW-APGRVMLNAYGPTETTICAAISAP--LRPGSgmppIGVPVSGAALFVldswlrpvpa 1814
Cdd:cd05907   210 GGRLrFAASGGAPLPAELLHFFrALGIPVYEGYGLTETSAVVTLNPPgdNRIGT----VGKPLPGVEVRI---------- 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1815 GVAGELYIAGAGVGVGYWRRAGLTASRFVACPFggsgarmYRTGDLVCWRADGQLEFLGRTDD-QVKIRGYRIELGEVAT 1893
Cdd:cd05907   276 ADDGEILVRGPNVMLGYYKNPEATAEALDADGW-------LHTGDLGEIDEDGFLHITGRKKDlIITSGGKNISPEPIEN 348

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489495878 1894 ALAELAGVGQAVVIArEDRPG--------DKRLVGYATEIAPGAVDPAGLRAQLAQR 1942
Cdd:cd05907   349 ALKASPLISQAVVIG-DGRPFlvalivpdPEALEAWAEEHGIAYTDVAELAANPAVR 404
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
 1633-1971 2.87e-23

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 103.18  E-value: 2.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1633 LAYILYTSGTTGEPKGVGITHRNVTRLFASLPARLS--AAQVWSQCHSYGFDASAWEIWGALLGGGRLViVPESVAASPN 1710
Cdd:cd17630     2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGfgGGDSWLLSLPLYHVGGLAILVRSLLAGAELV-LLERNQALAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1711 DFHGLLVaEHVSVltqTPAAVAMLPTQGLESVAL------VVAGEACPAALVDRWAPGRV-MLNAYGPTETTICAAISAP 1783
Cdd:cd17630    81 DLAPPGV-THVSL---VPTQLQRLLDSGQGPAALkslravLLGGAPIPPELLERAADRGIpLYTTYGMTETASQVATKRP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1784 lrPGSGMPPIGVPVSGAALFVLDswlrpvpagvAGELYIAGAGVGVGYWRRAGLTasrfvacPFGGSGarMYRTGDLVCW 1863
Cdd:cd17630   157 --DGFGRGGVGVLLPGRELRIVE----------DGEIWVGGASLAMGYLRGQLVP-------EFNEDG--WFTTKDLGEL 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1864 RADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVgyATEIAPGAVDPAGLRAQLAQRL 1943
Cdd:cd17630   216 HADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPV--AVIVGRGPADPAELRAWLKDKL 293

                         330       340
                  ....*....|....*....|....*...
gi 489495878 1944 PGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:cd17630   294 ARFKLPKRIYPVPELPRTGGGKVDRRAL 321
PRK05691 PRK05691
peptide synthase; Validated
 1491-2057 9.60e-23

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 107.56  E-value: 9.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1491 PVSIPQMLAAQVARIPEAEAVCC------GDASMTYRELDEASNRLAHRLAGcGAGPGECVALLFERCAPAVVAMVAVLK 1564
Cdd:PRK05691    8 PLTLVQALQRRAAQTPDRLALRFladdpgEGVVLSYRDLDLRARTIAAALQA-RASFGDRAVLLFPSGPDYVAAFFGCLY 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1565 TGAAYLPidpANPPP--------RVAFMLGDAVPVAAVTTAGLR------SRLAGHDLPIIDVVDALAAYPGTPPPMPA- 1629
Cdd:PRK05691   87 AGVIAVP---AYPPEsarrhhqeRLLSIIADAEPRLLLTVADLRdsllqmEELAAANAPELLCVDTLDPALAEAWQEPAl 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1630 -AVNLAYILYTSGTTGEPKGVGITHRNVTrlfaslparlsaAQVWSQCHSYGFDASAWEI---WGAL-----LGGGRLVI 1700
Cdd:PRK05691  164 qPDDIAFLQYTSGSTALPKGVQVSHGNLV------------ANEQLIRHGFGIDLNPDDVivsWLPLyhdmgLIGGLLQP 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1701 ----VPeSVAASPNDFHGLLV------AEHVSVLTQTP--------AAVAMLPTQGLESVALVVA-------GEACPAAL 1755
Cdd:PRK05691  232 ifsgVP-CVLMSPAYFLERPLrwleaiSEYGGTISGGPdfayrlcsERVSESALERLDLSRWRVAysgsepiRQDSLERF 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1756 VDRWAPGRV----MLNAYGPTETTICAAISAP------LR------------PGSGMPPI--GVPVSGAALFVLD-SWLR 1810
Cdd:PRK05691  311 AEKFAACGFdpdsFFASYGLAEATLFVSGGRRgqgipaLEldaealarnraePGTGSVLMscGRSQPGHAVLIVDpQSLE 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1811 PVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACpfggSGARMYRTGDLVCWRaDGQLEFLGRTDDQVKIRG---YRIE 1887
Cdd:PRK05691  391 VLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEH----DGRTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGhnlYPQD 465

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1888 LGEVATALAELAGVGQAVVIAREDRPGDKrlVGYATEIAPG---AVDPAGLRAQLAQRLPGYL--VPAAVVVID--ALPL 1960
Cdd:PRK05691  466 IEKTVEREVEVVRKGRVAAFAVNHQGEEG--IGIAAEISRSvqkILPPQALIKSIRQAVAEACqeAPSVVLLLNpgALPK 543

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1961 TVNGKLDHRA---------------LPAPEYGDTNGYRAPAGPVEKTVAGIFARVLGLERVGVDDSFFELGGDSLAAMRV 2025
Cdd:PRK05691  544 TSSGKLQRSAcrlrladgsldsyalFPALQAVEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQV 623

                         650       660       670
                  ....*....|....*....|....*....|..
gi 489495878 2026 IAAINTTLNADLPVRALLHASSTRGLSQLLGR 2057
Cdd:PRK05691  624 VARLRDELGIDLNLRQLFEAPTLAAFSAAVAR 655
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
 1498-1966 2.42e-22

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 103.98  E-value: 2.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1498 LAAQVARIPEAEAVCCGDA------SMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLP 1571
Cdd:PRK13295   30 LDACVASCPDKTAVTAVRLgtgaprRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNP 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1572 IDPANPPPRVAFMLGDA------VPVA------AVTTAGLRSRLAghDLPIIDVVDALAA--------------YPGTPP 1625
Cdd:PRK13295  110 LMPIFRERELSFMLKHAeskvlvVPKTfrgfdhAAMARRLRPELP--ALRHVVVVGGDGAdsfeallitpaweqEPDAPA 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1626 PM----PAAVNLAYILYTSGTTGEPKGVGITHRNVTRLFASLPAR--LSAAQVW----SQCHSYGFdasaweIWGALLgg 1695
Cdd:PRK13295  188 ILarlrPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERlgLGADDVIlmasPMAHQTGF------MYGLMM-- 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1696 grlvivPESVAAS--------PNDFHGLLVAEHVS-VLTQTPAAVAMLPTQGLESVAL------VVAGEACPAALVDRW- 1759
Cdd:PRK13295  260 ------PVMLGATavlqdiwdPARAAELIRTEGVTfTMASTPFLTDLTRAVKESGRPVsslrtfLCAGAPIPGALVERAr 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1760 -APGRVMLNAYGPTE----TTICaaISAPLRPGSGMPpiGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRR 1834
Cdd:PRK13295  334 aALGAKIVSAWGMTEngavTLTK--LDDPDERASTTD--GCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKR 409

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1835 AGLTASRFVAcpfggsgarMYRTGDLVCWRADGQLEFLGRTDDqVKIRG-YRIELGEVATALAELAGVGQAVVIAREDRP 1913
Cdd:PRK13295  410 PQLNGTDADG---------WFDTGDLARIDADGYIRISGRSKD-VIIRGgENIPVVEIEALLYRHPAIAQVAIVAYPDER 479

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 489495878 1914 GDKRLVGYATEIAPGAVDPAGLRAQL-AQRLPGYLVPAAVVVIDALPLTVNGKL 1966
Cdd:PRK13295  480 LGERACAFVVPRPGQSLDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKI 533
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
1499-1966 4.60e-22

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 103.29  E-value: 4.60e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1499 AAQVARIPEAEAVCcgD---ASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPA 1575
Cdd:PRK06087   30 QQTARAMPDKIAVV--DnhgASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPS 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1576 NPPPRVAFMLGDAVPVAAVTTAGLRSR------LA-GHDLPIID---VVDALAA--------------YPGTPPPMPAAV 1631
Cdd:PRK06087  108 WREAELVWVLNKCQAKMFFAPTLFKQTrpvdliLPlQNQLPQLQqivGVDKLAPatsslslsqiiadyEPLTTAITTHGD 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1632 NLAYILYTSGTTGEPKGVGITHRNV---TRLFAS-----------LPARLSaaqvwsqcHSYGFDASaweIWGALLGGGR 1697
Cdd:PRK06087  188 ELAAVLFTSGTEGLPKGVMLTHNNIlasERAYCArlnltwqdvfmMPAPLG--------HATGFLHG---VTAPFLIGAR 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1698 LVIV----PESVAAspndfhgLLVAEHVS-VLTQTPAAVAML------PTQgLESVALVVAGEA-CPAALVDR-WAPGRV 1764
Cdd:PRK06087  257 SVLLdiftPDACLA-------LLEQQRCTcMLGATPFIYDLLnllekqPAD-LSALRFFLCGGTtIPKKVAREcQQRGIK 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1765 MLNAYGPTETtiCAAISAPL-RPGS-GMPPIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASrf 1842
Cdd:PRK06087  329 LLSVYGSTES--SPHAVVNLdDPLSrFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTAR-- 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1843 vACPFGGsgarMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYA 1922
Cdd:PRK06087  405 -ALDEEG----WYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYV 479

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 489495878 1923 TEIAP-GAVDPAGLRAQLA-QRLPGYLVPAAVVVIDALPLTVNGKL 1966
Cdd:PRK06087  480 VLKAPhHSLTLEEVVAFFSrKRVAKYKYPEHIVVIDKLPRTASGKI 525
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 1633-1971 8.87e-22

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 103.85  E-value: 8.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1633 LAYILYTSGTTGEPKGVGITHRNVT----------------RLFASLPArlsaaqvwsqCHSYGFDASaweIWGALLGGG 1696
Cdd:PRK08633  784 TATIIFSSGSEGEPKGVMLSHHNILsnieqisdvfnlrnddVILSSLPF----------FHSFGLTVT---LWLPLLEGI 850

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1697 RLVIVPesvaaSPNDFHGL--LVAEH-VSVLTQTPA-------AVAMLPTQgLESVALVVAG-EACPAALVDRWAP--GR 1763
Cdd:PRK08633  851 KVVYHP-----DPTDALGIakLVAKHrATILLGTPTflrlylrNKKLHPLM-FASLRLVVAGaEKLKPEVADAFEEkfGI 924

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1764 VMLNAYGPTETTICAAISAP------------LRPGSgmppIGVPVSGAALFVLD-SWLRPVPAGVAGELYIAGAGVGVG 1830
Cdd:PRK08633  925 RILEGYGATETSPVASVNLPdvlaadfkrqtgSKEGS----VGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKG 1000

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1831 YWRRAGLTASRFVACpfggSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGvGQAVVIARE 1910
Cdd:PRK08633 1001 YLGDPEKTAEVIKDI----DGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALG-GEEVVFAVT 1075

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489495878 1911 DRPGDKRLVGYATEIAPGAVDPAGLRAQLAQ-RLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:PRK08633 1076 AVPDEKKGEKLVVLHTCGAEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
 1506-1966 1.05e-21

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 101.80  E-value: 1.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1506 PEAEA-VCCGDAS----MTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLP--------- 1571
Cdd:cd05970    31 PDKLAlVWCDDAGeeriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPathqltakd 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1572 ----IDPANPPPRVAfMLGDAVP---VAAVTTAGLRSRLA--GHDLP--IIDVVDALA-AYPGTPPP----MPAAVNLAY 1635
Cdd:cd05970   111 ivyrIESADIKMIVA-IAEDNIPeeiEKAAPECPSKPKLVwvGDPVPegWIDFRKLIKnASPDFERPtansYPCGEDILL 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1636 ILYTSGTTGEPKGVgiTHRNVTRLfaslpARLSAAQVWSQCHS----YGFDASAW--EIWGALLG---GGRLVIVPESVA 1706
Cdd:cd05970   190 VYFSSGTTGMPKMV--EHDFTYPL-----GHIVTAKYWQNVREgglhLTVADTGWgkAVWGKIYGqwiAGAAVFVYDYDK 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1707 ASPNDFHGLLVAEHVSVLTQTPAAVAMLPTQGLESVAL------VVAGEACPAALVDRW--APGRVMLNAYGPTETTICA 1778
Cdd:cd05970   263 FDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLsslrycTTAGEALNPEVFNTFkeKTGIKLMEGFGQTETTLTI 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1779 AISAPLRPGSGmpPIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGA-----GVGVGYWRRAGLTASRFvacpFGGsgar 1853
Cdd:cd05970   343 ATFPWMEPKPG--SMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTAEVW----HDG---- 412

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1854 MYRTGDlVCWR-ADGQLEFLGRTDDQVKIRGYRIELGEVATAL--------AELAGV-----GQAV----VIAREDRPGD 1915
Cdd:cd05970   413 YYHTGD-AAWMdEDGYLWFVGRTDDLIKSSGYRIGPFEVESALiqhpavleCAVTGVpdpirGQVVkatiVLAKGYEPSE 491

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 489495878 1916 ---KRLVGYATEI-APgavdpaglraqlaqrlpgYLVPAAVVVIDALPLTVNGKL 1966
Cdd:cd05970   492 elkKELQDHVKKVtAP------------------YKYPRIVEFVDELPKTISGKI 528
PRK07788 PRK07788
acyl-CoA synthetase; Validated
 1496-1973 1.31e-21

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 101.93  E-value: 1.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1496 QMLAAQVARI-PEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDP 1574
Cdd:PRK07788   52 AGLVAHAARRaPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNT 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1575 ANPPPRVA----------------FM-LGDAVP--VAAVTTAGLRSRLAGHDLPIIDVVDALAAYPGTPPPMPAAVNLAY 1635
Cdd:PRK07788  132 GFSGPQLAevaaregvkalvyddeFTdLLSALPpdLGRLRAWGGNPDDDEPSGSTDETLDDLIAGSSTAPLPKPPKPGGI 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1636 ILYTSGTTGEPKGVgitHRNVTRLFASLPARLSA----AQVWSQCHSYGFDASAWEIWGALLGGGRLVIV-----PESVA 1706
Cdd:PRK07788  212 VILTSGTTGTPKGA---PRPEPSPLAPLAGLLSRvpfrAGETTLLPAPMFHATGWAHLTLAMALGSTVVLrrrfdPEATL 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1707 AspndfhglLVAEH-----VSV-------LTQTPAAVAMLPTQGLESValVVAGEACPAALVDRW--APGRVMLNAYGPT 1772
Cdd:PRK07788  289 E--------DIAKHkatalVVVpvmlsriLDLGPEVLAKYDTSSLKII--FVSGSALSPELATRAleAFGPVLYNLYGST 358

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1773 ETTIcAAISAP--LR--PGS-GMPPIGVPVSgaalfVLDSWLRPVPAGVAGELYIagagvgvgywrRAGLTASRFVAcpf 1847
Cdd:PRK07788  359 EVAF-ATIATPedLAeaPGTvGRPPKGVTVK-----ILDENGNEVPRGVVGRIFV-----------GNGFPFEGYTD--- 418

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1848 GGSGAR---MYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATE 1924
Cdd:PRK07788  419 GRDKQIidgLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVK 498

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 489495878 1925 IAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRALPA 1973
Cdd:PRK07788  499 APGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 558-916 2.03e-21

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 100.17  E-value: 2.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  558 DERVTQVTHD----ALLATKT--AYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDT--VLQCAPLTSDISVE 629
Cdd:cd17648    74 DERIQFILEDtgarVVITNSTdlAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGDeaVLFFSNYVFDFFVE 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  630 EIFGGAACGARLVRSAAMKTGDLAALVDDLVARETTIVDLPTAVWQLlcadgdaIDAIGRSRLRQIVIGGEAIRCSAVDK 709
Cdd:cd17648   154 QMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQ-------YDLARLPHLKRVDAAGEEFTAPVFEK 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  710 WLESAASQgisLLSSYGPTEATVVATFLPIVCDQTTmDGAllrLGRPiLPNTV------------FLAFGEVVIVGDLVA 777
Cdd:cd17648   227 LRSRFAGL---IINAYGPTETTVTNHKRFFPGDQRF-DKS---LGRP-VRNTKcyvlndamkrvpVGAVGELYLGGDGVA 298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  778 DGYLGID---GDGFGT------VTAADGSRRRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAV 848
Cdd:cd17648   299 RGYLNRPeltAERFLPnpfqteQERARGRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGV 378

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489495878  849 SDVAVELHSGSLGVWFKSQR-------TREG---EQDAAAATRIRLVLVSLGVssfFVVGVPNIPRKPNGKIDSDNLP 916
Cdd:cd17648   379 RECAVVAKEDASQAQSRIQKylvgyylPEPGhvpESDLLSFLRAKLPRYMVPA---RLVRLEGIPVTINGKLDVRALP 453
PRK07470 PRK07470
acyl-CoA synthetase; Validated
 1496-1966 2.07e-21

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 100.89  E-value: 2.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1496 QMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPA 1575
Cdd:PRK07470   11 HFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFR 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1576 NPPPRVAF---------MLGDA-----VPVAAVTTAGLRSRLAGHDLPI-IDVVDALAAYPGTPPPmPAAVNL---AYIL 1637
Cdd:PRK07470   91 QTPDEVAYlaeasgaraMICHAdfpehAAAVRAASPDLTHVVAIGGARAgLDYEALVARHLGARVA-NAAVDHddpCWFF 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1638 YTSGTTGEPKGVGITHRN----VTR----LFASLPARLSAAQVWSQCHSYGFDASAWEIWGA---LLGGGRLviVPESVA 1706
Cdd:PRK07470  170 FTSGTTGRPKAAVLTHGQmafvITNhladLMPGTTEQDASLVVAPLSHGAGIHQLCQVARGAatvLLPSERF--DPAEVW 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1707 AspndfhglLVAEH-VSVLTQTPAAVAMLPTQglESVA---------LVVAGeaCPAALVDRWAP----GRVMLNAYGPT 1772
Cdd:PRK07470  248 A--------LVERHrVTNLFTVPTILKMLVEH--PAVDrydhsslryVIYAG--APMYRADQKRAlaklGKVLVQYFGLG 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1773 ETTICAAISAPL------RPGSGMPPIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVacp 1846
Cdd:PRK07470  316 EVTGNITVLPPAlhdaedGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFR--- 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1847 fGGsgarMYRTGDLVCWRADGQLEFLGRTDDqVKIRG----YRIELGE---VATALAELA----------GVGQAVVIAR 1909
Cdd:PRK07470  393 -DG----WFRTGDLGHLDARGFLYITGRASD-MYISGgsnvYPREIEEkllTHPAVSEVAvlgvpdpvwgEVGVAVCVAR 466

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489495878 1910 EdrpgdkrlvgyateiaPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKL 1966
Cdd:PRK07470  467 D----------------GAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKI 507
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
 1515-1971 4.10e-21

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 99.59  E-value: 4.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1515 DASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAV 1594
Cdd:PRK08276    9 GEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1595 TTAGLRSRLAG------HDLPIIDVVD-----------ALAAYPGTPPPMPAAVnlAYILYTSGTTGEPKGVgithrnVT 1657
Cdd:PRK08276   89 VSAALADTAAElaaelpAGVPLLLVVAgpvpgfrsyeeALAAQPDTPIADETAG--ADMLYSSGTTGRPKGI------KR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1658 RLFASLPARLSAAQVWSQCHSYGFDA------------SAWEIWG--ALLGGGRLVIV----PESVAAspndfhglLVAE 1719
Cdd:PRK08276  161 PLPGLDPDEAPGMMLALLGFGMYGGPdsvylspaplyhTAPLRFGmsALALGGTVVVMekfdAEEALA--------LIER 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1720 HVSVLTQtpaavaMLPTQ---------------GLESVALVV-AGEACP----AALVDRWAPgrVMLNAYGPTE---TTI 1776
Cdd:PRK08276  233 YRVTHSQ------LVPTMfvrmlklpeevraryDVSSLRVAIhAAAPCPvevkRAMIDWWGP--IIHEYYASSEgggVTV 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1777 CAAISAPLRPGS-GMPPIGVpvsgaaLFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVacpfggsGARMY 1855
Cdd:PRK08276  305 ITSEDWLAHPGSvGKAVLGE------VRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARN-------PHGWV 371

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1856 RTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGyATEIAPGAVDPAGL 1935
Cdd:PRK08276  372 TVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA-VVQPADGADAGDAL 450

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 489495878 1936 RAQL----AQRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:PRK08276  451 AAELiawlRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
 1497-1973 4.22e-21

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 100.07  E-value: 4.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1497 MLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPAN 1576
Cdd:PRK13383   40 LLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEF 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1577 PPPRVAFMLGDAVPVAAVTTAGLRSRLAGHD--LPIIDVVDALAAYPGTPPPMPAAVNLayILYTSGTTGEPKGV----- 1649
Cdd:PRK13383  120 RSDALAAALRAHHISTVVADNEFAERIAGADdaVAVIDPATAGAEESGGRPAVAAPGRI--VLLTSGTTGKPKGVprapq 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1650 -----GITHRNVTRLFASLPARLSAAQvwSQCHSYGFDASAWEIwgaLLGGGRLV---IVPESVAASPNdfhgLLVAEHV 1721
Cdd:PRK13383  198 lrsavGVWVTILDRTRLRTGSRISVAM--PMFHGLGLGMLMLTI---ALGGTVLThrhFDAEAALAQAS----LHRADAF 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1722 SVLTQTPAAVAMLPTQ-----GLESVALVVA-GEACPAALVDRW--APGRVMLNAYGPTETTIcAAISAPLRPGSGMPPI 1793
Cdd:PRK13383  269 TAVPVVLARILELPPRvrarnPLPQLRVVMSsGDRLDPTLGQRFmdTYGDILYNGYGSTEVGI-GALATPADLRDAPETV 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1794 GVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYwrragltasrfvacpFGGSGAR----MYRTGDLVCWRADGQL 1869
Cdd:PRK13383  348 GKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRY---------------TDGGGKAvvdgMTSTGDMGYLDNAGRL 412

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1870 EFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATEIAPGAVDPAGLRAQLAQRLPGYLVP 1949
Cdd:PRK13383  413 FIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQP 492

                         490       500
                  ....*....|....*....|....
gi 489495878 1950 AAVVVIDALPLTVNGKLDHRALPA 1973
Cdd:PRK13383  493 RDINIVSSIPRNPTGKVLRKELPG 516
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
 1024-1343 6.03e-21

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 98.15  E-value: 6.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1024 PLSFAQRRLWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVD-GVPRQLViearRADLG-- 1100
Cdd:cd19547     3 PLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDrAEPLQYV----RDDLApp 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1101 CDIVDATAWPADR----LQRAIEEAARHSFDLAtEIPL-RTWLFRIADDEHVLVAVAHHIAADGWSVAPLTADLSAAYAS 1175
Cdd:cd19547    79 WALLDWSGEDPDRraelLERLLADDRAAGLSLA-DCPLyRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1176 RCAGRAPDWAPLPvQYVDYTLWQREILGDLDDSDSpiaaqlaYWENALAGMPerlrlPTARPYPPvADQRGA--SLVVDW 1253
Cdd:cd19547   158 LAHGREPQLSPCR-PYRDYVRWIRARTAQSEESER-------FWREYLRDLT-----PSPFSTAP-ADREGEfdTVVHEF 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1254 PASVQQQVRRIARQHNATSFMVVAAGLAVLLSKLSGSPDVAVGFPIAGRSdPAL---DNLVGFFVNTLVLRVNLAGDPSF 1330
Cdd:cd19547   224 PEQLTRLVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRP-PELegsEHMVGIFINTIPLRIRLDPDQTV 302

                         330
                  ....*....|...
gi 489495878 1331 AELLGQVRaRSLA 1343
Cdd:cd19547   303 TGLLETIH-RDLA 314
PRK06164 PRK06164
acyl-CoA synthetase; Validated
 1488-1964 8.06e-21

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 99.05  E-value: 8.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1488 APTPVSIPQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGA 1567
Cdd:PRK06164    6 APRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1568 AYLPIDPANPPPRVAFMLGDAVPVAAVTTAGLR-----SRLAGHD------LPIIDVVD---------------ALAAYP 1621
Cdd:PRK06164   86 TVIAVNTRYRSHEVAHILGRGRARWLVVWPGFKgidfaAILAAVPpdalppLRAIAVVDdaadatpapapgarvQLFALP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1622 GTPPP-----MPAAVNLAYILYT-SGTTGEPKGVGITHRNVTRLFASLPARLSAAQ------VWSQCHSYGFDASAweiw 1689
Cdd:PRK06164  166 DPAPPaaageRAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPgavllaALPFCGVFGFSTLL---- 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1690 GALLGGGRLVIVPESVAA-------SPNDFHGLLVAEHVSVLTQTPAAVAMLPTQGLESVALVVAGEACPAALVDrwAPG 1762
Cdd:PRK06164  242 GALAGGAPLVCEPVFDAArtaralrRHRVTHTFGNDEMLRRILDTAGERADFPSARLFGFASFAPALGELAALAR--ARG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1763 RVMLNAYGPTET-------TICAAISAPLRPGsgmppiGVPVSGAA-LFVLDSWLRPV-PAGVAGELYIAGAGVGVGYWR 1833
Cdd:PRK06164  320 VPLTGLYGSSEVqalvalqPATDPVSVRIEGG------GRPASPEArVRARDPQDGALlPDGESGEIEIRAPSLMRGYLD 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1834 RAGLTASRFVACPFggsgarmYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREdRP 1913
Cdd:PRK06164  394 NPDATARALTDDGY-------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAT-RD 465

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 489495878 1914 GDKRLVGYATEIAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNG 1964
Cdd:PRK06164  466 GKTVPVAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESA 516
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 574-911 1.22e-20

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 97.90  E-value: 1.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  574 TAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARLVRSAAMKTGDla 653
Cdd:cd05922   119 LALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDD-- 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  654 ALVDDLvaRETTIVDLP--TAVWQLLcaDGDAIDAIGRSRLRQIVIGGEAIRCSAVDKWLEsaASQGISLLSSYGPTEAT 731
Cdd:cd05922   197 AFWEDL--REHGATGLAgvPSTYAML--TRLGFDPAKLPSLRYLTQAGGRLPQETIARLRE--LLPGAQVYVMYGQTEAT 270

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  732 VVATFLPivcdQTTMDGALLRLGRPIlPNTVFLAF------------GEVVIVGDLVADGYLG-----IDGDGFGTVtaa 794
Cdd:cd05922   271 RRMTYLP----PERILEKPGSIGLAI-PGGEFEILdddgtptppgepGEIVHRGPNVMKGYWNdppyrRKEGRGGGV--- 342

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  795 dgsrrraFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAVELHSGSLGVWFKSQRTREGEQ 874
Cdd:cd05922   343 -------LHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLALFVTAPDKI 415

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 489495878  875 DAAAATRIRLVLVSLGVSSFFVVGVPNIPRKPNGKID 911
Cdd:cd05922   416 DPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVD 452
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 569-911 1.61e-20

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 97.15  E-value: 1.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  569 LLATKTAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDT-VLQCAPLTSDISVEEIFGGAACGARLVRSAAM 647
Cdd:cd17650    90 TQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVrLLQMASFSFDVFAGDFARSLLNGGTLVICPDE 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  648 KTGDLAALVDDLVARETTIVD-LPTAVWQLLcaDGDAIDAIGRSRLRQIVIGGEAirCSAVD-KWLESAASQGISLLSSY 725
Cdd:cd17650   170 VKLDPAALYDLILKSRITLMEsTPALIRPVM--AYVYRNGLDLSAMRLLIVGSDG--CKAQDfKTLAARFGQGMRIINSY 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  726 GPTEATVVATFLpivcdQTTMD----GALLRLGRPiLPNTVFL------------AFGEVVIVGDLVADGYLG---IDGD 786
Cdd:cd17650   246 GVTEATIDSTYY-----EEGRDplgdSANVPIGRP-LPNTAMYvlderlqpqpvgVAGELYIGGAGVARGYLNrpeLTAE 319

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  787 GFGTVTAADGSRrrAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAVEL------HSGSL 860
Cdd:cd17650   320 RFVENPFAPGER--MYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVredkggEARLC 397

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 489495878  861 GVWFKSQRTREGEQDAAAATRirlvLVSLGVSSFFVVgVPNIPRKPNGKID 911
Cdd:cd17650   398 AYVVAAATLNTAELRAFLAKE----LPSYMIPSYYVQ-LDALPLTPNGKVD 443
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
 1519-1977 1.87e-20

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 98.43  E-value: 1.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1519 TYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVTTAG 1598
Cdd:PRK04319   75 TYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPA 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1599 LRSRLAGHDLP-----------------IIDVVDALAAYPGTPPPMPAAVNLAYIL-YTSGTTGEPKGVGITHRNVTRLF 1660
Cdd:PRK04319  155 LLERKPADDLPslkhvllvgedveegpgTLDFNALMEQASDEFDIEWTDREDGAILhYTSGSTGKPKGVLHVHNAMLQHY 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1661 ASlpAR----LSAAQV--------WSQCHSYGfdasaweIWGALLGGGRLVIVPESVaaSPNDFHGLLVAEHVSVLTQTP 1728
Cdd:PRK04319  235 QT--GKyvldLHEDDVywctadpgWVTGTSYG-------IFAPWLNGATNVIDGGRF--SPERWYRILEDYKVTVWYTAP 303

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1729 AAVAMLPTQGLESVA----------LVVaGEAC-PAALvdRW---APGRVMLNAYGPTET---TICAAISAPLRPGSgmp 1791
Cdd:PRK04319  304 TAIRMLMGAGDDLVKkydlsslrhiLSV-GEPLnPEVV--RWgmkVFGLPIHDNWWMTETggiMIANYPAMDIKPGS--- 377

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1792 pIGVPVSGAALFVLDSWLRPVPAGVAGELYIAgAG---VGVGYWRraglTASRFVACPFGGsgarMYRTGDLVCWRADGQ 1868
Cdd:PRK04319  378 -MGKPLPGIEAAIVDDQGNELPPNRMGNLAIK-KGwpsMMRGIWN----NPEKYESYFAGD----WYVSGDSAYMDEDGY 447

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1869 LEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDrPgdkrLVGyatEIA-------PGAVDPAGLRAQLAQ 1941
Cdd:PRK04319  448 FWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPD-P----VRG---EIIkafvalrPGYEPSEELKEEIRG 519

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 489495878 1942 ----RLPGYLVPAAVVVIDALPLTVNGKLDHRALPAPEYG 1977
Cdd:PRK04319  520 fvkkGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAWELG 559
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
1482-1971 2.44e-20

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 97.65  E-value: 2.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1482 AVLTAPAPTPvSIPQMLAAQVARIPEAEAVCCGD--ASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAM 1559
Cdd:PRK05852    7 AAPMASDFGP-RIADLVEVAATRLPEAPALVVTAdrIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVAL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1560 VAVLKTGAAYLPIDPANPPP-----------RVAFMLGD--------AVPVAAVTTAGLRSRLAGHDLPIIDVVDALAAY 1620
Cdd:PRK05852   86 LAASRADLVVVPLDPALPIAeqrvrsqaagaRVVLIDADgphdraepTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPT 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1621 PGTPPPMPAAVNLAYILYTSGTTGEPKGVGITHRNVTrlfASLPARLSAAQVWSQ---------CHSYGFDASAWeiwgA 1691
Cdd:PRK05852  166 PATSTPEGLRPDDAMIMFTGGTTGLPKMVPWTHANIA---SSVRAIITGYRLSPRdatvavmplYHGHGLIAALL----A 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1692 LLGGGRLVIVPESVAASPNDFHGLLVAEHVSVLTQTPAAVAML--------------PTQGLESVALVVAGEACPAALVD 1757
Cdd:PRK05852  239 TLASGGAVLLPARGRFSAHTFWDDIKAVGATWYTAVPTIHQILleraatepsgrkpaALRFIRSCSAPLTAETAQALQTE 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1758 RWAPgrvMLNAYGPTETTICAAISAPLRPGSGMPPIGVP-----VSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYW 1832
Cdd:PRK05852  319 FAAP---VVCAFGMTEATHQVTTTQIEGIGQTENPVVSTglvgrSTGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYL 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1833 RRAGLTASRFVACPFggsgarmyRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDR 1912
Cdd:PRK05852  396 GDPTITAANFTDGWL--------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQ 467

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489495878 1913 PGDKRLVGYATEIAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:PRK05852  468 LYGEAVAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
2109-2417 3.41e-20

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 93.50  E-value: 3.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2109 TVLLTGATGFLGRYLVLELLRRldvDGRLICLVRaesDEDARRRLEktfdsgdpellrhfkelAADRLEVVAGDksepdl 2188
Cdd:COG0451     1 RILVTGGAGFIGSHLARRLLAR---GHEVVGLDR---SPPGAANLA-----------------ALPGVEFVRGD------ 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2189 GLDQPMWRRLAETVDLIVDSAAM--VNAFPYHELFGPNVAGTAELIRIALTTKLKPFTYVSTADV-GAAIEPsaFTEDAD 2265
Cdd:COG0451    52 LRDPEALAAALAGVDAVVHLAAPagVGEEDPDETLEVNVEGTLNLLEAARAAGVKRFVYASSSSVyGDGEGP--IDEDTP 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2266 IRVISPtrtvdggwaggYGTSKWAGEVLLREANDLCALPVAVFRCGMILadtsyaGQlNMSDWVTRMVLSLMATGIAPrs 2345
Cdd:COG0451   130 LRPVSP-----------YGASKLAAELLARAYARRYGLPVTILRPGNVY------GP-GDRGVLPRLIRRALAGEPVP-- 189

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489495878 2346 fYEPDSEGNRQRAHfdglpVTFVAEAIavlgARVAGSSLAGFATYHVMNphDDGIGLDEYVDWLIEA-GYPIR 2417
Cdd:COG0451   190 -VFGDGDQRRDFIH-----VDDVARAI----VLALEAPAAPGGVYNVGG--GEPVTLRELAEAIAEAlGRPPE 250
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 575-916 7.68e-20

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 95.62  E-value: 7.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  575 AYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARL--VRSAAMKtgDL 652
Cdd:cd17656   131 LYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLyiIREETKR--DV 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  653 AALVDDLVARETTIVDLPTAVWQLLCADGDAIDAIGRSrLRQIVIGGEAIRCSavDKWLESAASQGISLLSSYGPTEATV 732
Cdd:cd17656   209 EQLFDLVKRHNIEVVFLPVAFLKFIFSEREFINRFPTC-VKHIITAGEQLVIT--NEFKEMLHEHNVHLHNHYGPSETHV 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  733 VATFlpiVCDQTTMDGALLRLGRPILPNTVFL-----------AFGEVVIVGDLVADGYLGID---GDGFgtVTAADGSR 798
Cdd:cd17656   286 VTTY---TINPEAEIPELPPIGKPISNTWIYIldqeqqlqpqgIVGELYISGASVARGYLNRQeltAEKF--FPDPFDPN 360

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  799 RRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAVELHSGSLG-----VWFKSQRTREGE 873
Cdd:cd17656   361 ERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGekylcAYFVMEQELNIS 440

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 489495878  874 QdaaAATRIRLVLVSLGVSSFFvVGVPNIPRKPNGKIDSDNLP 916
Cdd:cd17656   441 Q---LREYLAKQLPEYMIPSFF-VPLDQLPLTPNGKVDRKALP 479
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
 1615-1971 7.89e-20

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 96.37  E-value: 7.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1615 DALAAYPGTP--PPMPAAVNLAYILYTSGTTGEPKGVGITHRNVTRLFASLPArLSAAQVWSQC----------HSYGFd 1682
Cdd:PRK05677  189 DALAKGAGQPvtEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRA-LMGSNLNEGCeiliaplplyHIYAF- 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1683 asAWEIWGALLGGGRLVIVPesvaaSPNDFHGLlvaehVSVLTQTPAA---------VAMLPTQG---LESVALVV---A 1747
Cdd:PRK05677  267 --TFHCMAMMLIGNHNILIS-----NPRDLPAM-----VKELGKWKFSgfvglntlfVALCNNEAfrkLDFSALKLtlsG 334

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1748 GEACPAALVDRW--APGRVMLNAYGPTETTICAAISAP--LRPGSgmppIGVPVSGAALFVLDSWLRPVPAGVAGELYIA 1823
Cdd:PRK05677  335 GMALQLATAERWkeVTGCAICEGYGMTETSPVVSVNPSqaIQVGT----IGIPVPSTLCKVIDDDGNELPLGEVGELCVK 410

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1824 GAGVGVGYWRRAGLTASRFVACPFggsgarmYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQ 1903
Cdd:PRK05677  411 GPQVMKGYWQRPEATDEILDSDGW-------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQ 483

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489495878 1904 AVVIAREDRPGDKRLVGYATEIAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:PRK05677  484 CAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
 1502-1971 9.80e-20

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 95.53  E-value: 9.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1502 VARIPEAEAVCCG--DASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPP 1579
Cdd:PRK13391    7 AQTTPDKPAVIMAstGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1580 RVAFMLGDAVPVAAVTTA--------------GLRSRL---AGHDLP-IIDVVDALAAYPGTppPMPAAVNLAYILYTSG 1641
Cdd:PRK13391   87 EAAYIVDDSGARALITSAakldvarallkqcpGVRHRLvldGDGELEgFVGYAEAVAGLPAT--PIADESLGTDMLYSSG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1642 TTGEPKGV-------------GITH--------RNVTRLFASLPARLSAAQVWSQ-CHSYG--------FDAsawEIWGA 1691
Cdd:PRK13391  165 TTGRPKGIkrplpeqppdtplPLTAflqrlwgfRSDMVYLSPAPLYHSAPQRAVMlVIRLGgtvivmehFDA---EQYLA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1692 LLGGGRLVivpesvaaspndfHGLLVAEHVSVLTQTPAAVAMlpTQGLESVALVVAGEA-CPA----ALVDRWAPgrVML 1766
Cdd:PRK13391  242 LIEEYGVT-------------HTQLVPTMFSRMLKLPEEVRD--KYDLSSLEVAIHAAApCPPqvkeQMIDWWGP--IIH 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1767 NAYGPTE---TTICAAISAPLRPGS-GMPPIGVPVsgaalfVLDSWLRPVPAGVAGELYIAGaGVGVGYWRRAGLTA-SR 1841
Cdd:PRK13391  305 EYYAATEglgFTACDSEEWLAHPGTvGRAMFGDLH------ILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAeAR 377

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1842 fvaCPFGGsgarMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRP-GD--KRL 1918
Cdd:PRK13391  378 ---HPDGT----WSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDlGEevKAV 450

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 489495878 1919 VGYATEIAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:PRK13391  451 VQPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
1501-1971 1.39e-19

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 94.64  E-value: 1.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1501 QVARI-PEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPP 1579
Cdd:PRK03640   10 QRAFLtPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSRE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1580 RVAFMLGDAVPVAAVTTAGLRSRLAGHdlpIIDVVDALAAYPGTPPPMPAAVNL---AYILYTSGTTGEPKGVGITHRNv 1656
Cdd:PRK03640   90 ELLWQLDDAEVKCLITDDDFEAKLIPG---ISVKFAELMNGPKEEAEIQEEFDLdevATIMYTSGTTGKPKGVIQTYGN- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1657 trLFAS-----LPARLSAAQVWSQC----HSYGFDAsaweIWGALLGGGRLVIVPesvAASPNDFHGLLVAEHVSVLTQT 1727
Cdd:PRK03640  166 --HWWSavgsaLNLGLTEDDCWLAAvpifHISGLSI----LMRSVIYGMRVVLVE---KFDAEKINKLLQTGGVTIISVV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1728 PaavAMLpTQGLEsvalVVAGEACPAALvdrwapgRVML----------------------NAYGPTETtiCAAISApLR 1785
Cdd:PRK03640  237 S---TML-QRLLE----RLGEGTYPSSF-------RCMLlgggpapkplleqckekgipvyQSYGMTET--ASQIVT-LS 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1786 PGSGMPPIGvpVSGAALF-----VLDSwLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFggsgarmyRTGDL 1860
Cdd:PRK03640  299 PEDALTKLG--SAGKPLFpcelkIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF--------KTGDI 367

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1861 VCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKrlVGYATEIAPGAVDPAGLRAQLA 1940
Cdd:PRK03640  368 GYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQ--VPVAFVVKSGEVTEEELRHFCE 445

                         490       500       510
                  ....*....|....*....|....*....|.
gi 489495878 1941 QRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:PRK03640  446 EKLAKYKVPKRFYFVEELPRNASGKLLRHEL 476
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
1506-1971 2.26e-19

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 94.16  E-value: 2.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1506 PEAEAVCCGDASMTYRELDEASNRLA----HRLagcGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRV 1581
Cdd:PRK06839   16 PDRIAIITEEEEMTYKQLHEYVSKVAayliYEL---NVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENEL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1582 AFMLGD-------AVPVAAVTTAGLRSRLA-GHDLPIIDVVDALAAYP-GTPPPMPAAVNLayILYTSGTTGEPKGVGIT 1652
Cdd:PRK06839   93 IFQLKDsgttvlfVEKTFQNMALSMQKVSYvQRVISITSLKEIEDRKIdNFVEKNESASFI--ICYTSGTTGKPKGAVLT 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1653 HRN-----VTRLFA-SLPARLSAAQVWSQCHSYGFDASAWEIWgalLGGGRlVIVPESVaaSPNDFHGLLVAEHVSVLTQ 1726
Cdd:PRK06839  171 QENmfwnaLNNTFAiDLTMHDRSIVLLPLFHIGGIGLFAFPTL---FAGGV-IIVPRKF--EPTKALSMIEKHKVTVVMG 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1727 TPAAVAML------PTQGLESVALVVAGEA-CPAALVDRWAP-GRVMLNAYGPTETT----ICAAISAPLRPGSgmppIG 1794
Cdd:PRK06839  245 VPTIHQALincskfETTNLQSVRWFYNGGApCPEELMREFIDrGFLFGQGFGMTETSptvfMLSEEDARRKVGS----IG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1795 VPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFggsgarmyRTGDLVCWRADGQLEFLGR 1874
Cdd:PRK06839  321 KPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWL--------CTGDLARVDEDGFVYIVGR 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1875 TDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATEIAPGAVDPAGLRAQLAQRLPGYLVPAAVVV 1954
Cdd:PRK06839  393 KKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVF 472

                         490
                  ....*....|....*..
gi 489495878 1955 IDALPLTVNGKLDHRAL 1971
Cdd:PRK06839  473 LKELPKNATGKIQKAQL 489
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
 472-910 2.45e-19

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 94.20  E-value: 2.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  472 VAWLVQRGAAPGDVLVFTDDDTDKTIDLLIACHLAGCGYSVCD---TADEIS-----VRTNAITEHGDGI---------- 533
Cdd:cd05911    24 AAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANpiyTADELAhqlkiSKPKVIFTDPDGLekvkeaakel 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  534 ----LVTVVDVAATQLAVVGHDELRKVVDERVTQVTHDALLATKTAYIMPTSGTTGQPKLVRISHGSL-AVFCDAISRAY 608
Cdd:cd05911   104 gpkdKIIVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVCLSHRNLiANLSQVQTFLY 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  609 GW-GAHDTVLQCAPLTsdisveEIFG------GAACGARLVrsaAMKTGDLAALVDDLVARETTIVDL--PTAVWQLLCA 679
Cdd:cd05911   184 GNdGSNDVILGFLPLY------HIYGlfttlaSLLNGATVI---IMPKFDSELFLDLIEKYKITFLYLvpPIAAALAKSP 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  680 DGDAIDAigrSRLRQIVIGGeaircSAVDKWLESAASQGIS---LLSSYGPTEATVVATFLPIVCDQTTMDGALLR---- 752
Cdd:cd05911   255 LLDKYDL---SSLRVILSGG-----APLSKELQELLAKRFPnatIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPnvea 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  753 -----LGRPIL-PNTVflafGEVVIVGDLVADGYLG--------IDGDGFgtvtaadgsrrraFATGDRVTVDAEGFPVF 818
Cdd:cd05911   327 kivddDGKDSLgPNEP----GEICVRGPQVMKGYYNnpeatketFDEDGW-------------LHTGDIGYFDEDGYLYI 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  819 SGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAVelhsgsLGVW--FKSQRTR------EGEQDAAAatriRLV-LVSL 889
Cdd:cd05911   390 VDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAV------IGIPdeVSGELPRayvvrkPGEKLTEK----EVKdYVAK 459

                         490       500
                  ....*....|....*....|....*.
gi 489495878  890 GVSSFF-----VVGVPNIPRKPNGKI 910
Cdd:cd05911   460 KVASYKqlrggVVFVDEIPKSASGKI 485
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1635-1969 2.49e-19

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 92.45  E-value: 2.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1635 YILYTSGTTGEPKGVGITHRNVTRLFASLPARLSAAQVWSQCHS------------------YGfdASAWEIWGALLGGG 1696
Cdd:cd05924     7 YILYTGGTTGMPKGVMWRQEDIFRMLMGGADFGTGEFTPSEDAHkaaaaaagtvmfpapplmHG--TGSWTAFGGLLGGQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1697 RLVIVpeSVAASPNDFHGLLVAEHVSVLTQTPAAVAMLPTQGLES---------VALVVAG----EACPAALVDRwAPGR 1763
Cdd:cd05924    85 TVVLP--DDRFDPEEVWRTIEKHKVTSMTIVGDAMARPLIDALRDagpydlsslFAISSGGallsPEVKQGLLEL-VPNI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1764 VMLNAYGPTETTIcaaisaplrPGSGMPPIGVPVSGAALF------VLDSWLRPVPAGVAGELYIAGAG-VGVGYWRRAG 1836
Cdd:cd05924   162 TLVDAFGSSETGF---------TGSGHSAGSGPETGPFTRanpdtvVLDDDGRVVPPGSGGVGWIARRGhIPLGYYGDEA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1837 LTASRFVACpfggSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDK 1916
Cdd:cd05924   233 KTAETFPEV----DGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQ 308

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 489495878 1917 RLVGYATEIAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHR 1969
Cdd:cd05924   309 EVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKADYR 361
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 1023-1231 4.69e-19

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 92.70  E-value: 4.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1023 IPLSFAQRrlWFLDQLQRPAPVYNMAVALRLRGYLDTEALGAAVADVVGRHESLRTVFPAVDGVPRQLVIEARRADLGCD 1102
Cdd:cd19534     2 VPLTPIQR--WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEELFRLE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1103 IVDATAWPADRLQRAIEEAARHSFDLATEIPLRTWLFRIADDEHVLVAVAHHIAADG--WSVapLTADLSAAYASRCAGR 1180
Cdd:cd19534    80 VVDLSSLAQAAAIEALAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGvsWRI--LLEDLEAAYEQALAGE 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 489495878 1181 APdwaPLP--VQYVDYTLWQREILGDLDDsdspiAAQLAYWENALAGMPERLR 1231
Cdd:cd19534   158 PI---PLPskTSFQTWAELLAEYAQSPAL-----LEELAYWRELPAADYWGLP 202
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
1485-1913 5.74e-19

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 93.63  E-value: 5.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1485 TAPAPTPVSIPQMLAAQVARIPEAEAVCCGDA----SMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMV 1560
Cdd:COG1022     4 FSDVPPADTLPDLLRRRAARFPDRVALREKEDgiwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1561 AVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAV--------TTAGLRSRL------------AGHDLPIIDVVDALAA- 1619
Cdd:COG1022    84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFvedqeqldKLLEVRDELpslrhivvldprGLRDDPRLLSLDELLAl 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1620 -----YPGTPPPMPAAVN---LAYILYTSGTTGEPKGVGITHRNVTRLFASLPARLSAAQVWSQ------CHSYGFdasA 1685
Cdd:COG1022   164 grevaDPAELEARRAAVKpddLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTlsflplAHVFER---T 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1686 WEIwGALLGGGRlVIVPESVAASPNDF-----HGLLV---------------AEHVSVLTQTPAAVAMlpTQGLESVALV 1745
Cdd:COG1022   241 VSY-YALAAGAT-VAFAESPDTLAEDLrevkpTFMLAvprvwekvyagiqakAEEAGGLKRKLFRWAL--AVGRRYARAR 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1746 VAGEACPAALVDRWAP--------------GRV------------------------MLNAYGPTETTICAAISAP--LR 1785
Cdd:COG1022   317 LAGKSPSLLLRLKHALadklvfsklrealgGRLrfavsggaalgpelarffralgipVLEGYGLTETSPVITVNRPgdNR 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1786 PGSgmppIGVPVSGAALFVLDSwlrpvpagvaGELYIAGAGVGVGYWRRAGLTASRFVAcpfGGSgarmYRTGDLVCWRA 1865
Cdd:COG1022   397 IGT----VGPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFDA---DGW----LHTGDIGELDE 455

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 489495878 1866 DGQLEFLGRTDDQVKIRGyrielGE-VA-----TALAELAGVGQAVVIArEDRP 1913
Cdd:COG1022   456 DGFLRITGRKKDLIVTSG-----GKnVApqpieNALKASPLIEQAVVVG-DGRP 503
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
 1490-1965 7.06e-19

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 92.75  E-value: 7.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1490 TPVSIPQMlAAQVarIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAY 1569
Cdd:cd12118     5 TPLSFLER-AAAV--YPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1570 LPIDPANPPPRVAFMLGDAVPVAAVTTaglrSRLAGHDLpiidvvdaLAAYPGTPPPMPA-------AVNlayilYTSGT 1642
Cdd:cd12118    82 NALNTRLDAEEIAFILRHSEAKVLFVD----REFEYEDL--------LAEGDPDFEWIPPadewdpiALN-----YTSGT 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1643 TGEPKGVGITHRNvtrlfASLPArLSAAQVWSQCHSYG-------FDASAW-EIWGALLGGGRLVIVPESVAASPNDfhg 1714
Cdd:cd12118   145 TGRPKGVVYHHRG-----AYLNA-LANILEWEMKQHPVylwtlpmFHCNGWcFPWTVAAVGGTNVCLRKVDAKAIYD--- 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1715 LLVAEHVSVLTQTPAAVAML---PTQGLES----VALVVAGEACPAALVDRWAP-GRVMLNAYGPTETTICAAISAPLRP 1786
Cdd:cd12118   216 LIEKHKVTHFCGAPTVLNMLanaPPSDARPlphrVHVMTAGAPPPAAVLAKMEElGFDVTHVYGLTETYGPATVCAWKPE 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1787 GSGMPP---------IGVPVSGA-ALFVLD-SWLRPVPA-GV-AGELYIAGAGVGVGYWRRAGLTASRFVacpfGGsgar 1853
Cdd:cd12118   296 WDELPTeerarlkarQGVRYVGLeEVDVLDpETMKPVPRdGKtIGEIVFRGNIVMKGYLKNPEATAEAFR----GG---- 367

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1854 MYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYaTEIAPGA-VDP 1932
Cdd:cd12118   368 WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAF-VELKEGAkVTE 446

                         490       500       510
                  ....*....|....*....|....*....|...
gi 489495878 1933 AGLRAQLAQRLPGYLVPAAVVVIDaLPLTVNGK 1965
Cdd:cd12118   447 EEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGK 478
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
 574-853 2.47e-18

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 90.73  E-value: 2.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  574 TAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTsdISVEEIFG---GAACGARLVRSAAMKTg 650
Cdd:cd05907    89 LATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLA--HVFERRAGlyvPLLAGARIYFASSAET- 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  651 dlaaLVDDL-VARETTIVDLPTaVWQLLCADGDAID-----------AIGrSRLRQIVIGGEAIRcSAVDKWLESAasqG 718
Cdd:cd05907   166 ----LLDDLsEVRPTVFLAVPR-VWEKVYAAIKVKAvpglkrklfdlAVG-GRLRFAASGGAPLP-AELLHFFRAL---G 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  719 ISLLSSYGPTEATvvatflPIVCDQTTMDGALLRLGRPILPNTVFLAF-GEVVIVGDLVADGYLGIDGDgfgtvTAADGS 797
Cdd:cd05907   236 IPVYEGYGLTETS------AVVTLNPPGDNRIGTVGKPLPGVEVRIADdGEILVRGPNVMLGYYKNPEA-----TAEALD 304

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489495878  798 RRRAFATGDRVTVDAEGFPVFSGRKDAVVKIS-GKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:cd05907   305 ADGWLHTGDLGEIDEDGFLHITGRKKDLIITSgGKNISPEPIENALKASPLISQAVV 361
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1636-1965 3.12e-18

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 88.87  E-value: 3.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1636 ILYTSGTTGEPKGVGITHRNVTRLFASLPARLSAAQVWSQC------HSYGfdaSAWEIWGALLGGGRLVIVPESvaasp 1709
Cdd:cd05917     7 IQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCipvplfHCFG---SVLGVLACLTHGATMVFPSPS----- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1710 ndFHGLLVAEHV-----SVLTQTPAA-VAMLPTQGLESVAL------VVAGEACPAALVDRwapgrvMLN---------A 1768
Cdd:cd05917    79 --FDPLAVLEAIekekcTALHGVPTMfIAELEHPDFDKFDLsslrtgIMAGAPCPPELMKR------VIEvmnmkdvtiA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1769 YGPTETTICAAISAPLRP--------GSGMPPIGVPVsgaalfvLDSWLRPVPA-GVAGELYIAGAGVGVGYWRRAGLTA 1839
Cdd:cd05917   151 YGMTETSPVSTQTRTDDSiekrvntvGRIMPHTEAKI-------VDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKTA 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1840 SRFvacpfggSGARMYRTGDLVCWRADGQLEFLGRTDDQVkIRG----YRIELGEVataLAELAGVGQAVVIA-REDRPG 1914
Cdd:cd05917   224 EAI-------DGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGgeniYPREIEEF---LHTHPKVSDVQVVGvPDERYG 292

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489495878 1915 DKrlVGYATEIAPGA-VDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGK 1965
Cdd:cd05917   293 EE--VCAWIRLKEGAeLTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGK 342
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 1518-1911 4.17e-18

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 89.55  E-value: 4.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1518 MTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPidpanppprvafmlgdavPVAAVTTA 1597
Cdd:cd05974     1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP------------------ATTLLTPD 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1598 GLRSRLAGHDLPIIDVVDALAAypgtPPPMpaavnLAYilYTSGTTGEPKGVGITHRN--VTRLFASLPARLSAAQVWSQ 1675
Cdd:cd05974    63 DLRDRVDRGGAVYAAVDENTHA----DDPM-----LLY--FTSGTTSKPKLVEHTHRSypVGHLSTMYWIGLKPGDVHWN 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1676 CHSYGFDASAWEIWGALLGGGRLVIVPESVAASPNDFHGLLVAEHVSVLTQTPAAVAMLPTQGLESVA-----LVVAGEA 1750
Cdd:cd05974   132 ISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDvklreVVGAGEP 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1751 CPAALVD--RWAPGRVMLNAYGPTETTICAAISA--PLRPGSgmppIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAG 1826
Cdd:cd05974   212 LNPEVIEqvRRAWGLTIRDGYGQTETTALVGNSPgqPVKAGS----MGRPLPGYRVALLDPDGAPATEGEVALDLGDTRP 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1827 VGV--GYWRRAGLTAsrfvacpfGGSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQA 1904
Cdd:cd05974   288 VGLmkGYAGDPDKTA--------HAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEA 359


                  ....*..
gi 489495878 1905 VVIARED 1911
Cdd:cd05974   360 AVVPSPD 366
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
 1515-1965 4.22e-18

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 89.72  E-value: 4.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1515 DASMTYRELDEASNRLAHRLAGCGAGPGECVALLFErcapavvamvavlktgaaylpidpaNPPPRVAFMLGdAVPVAAV 1594
Cdd:cd05940     1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFME-------------------------NRPEYVLLWLG-LVKIGAV 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1595 TtAGLRSRLAGhdlpiidvvDALAAYPGTPPPMPAAVNLAYILYTSGTTGEPKGVGITHR---NVTRLFASLPARLSAAQ 1671
Cdd:cd05940    55 A-ALINYNLRG---------ESLAHCLNVSSAKHLVVDAALYIYTSGTTGLPKAAIISHRrawRGGAFFAGSGGALPSDV 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1672 VWSQCHSYGFDASAWEIWGALLGGGRLVIvPESVAASpnDFHGLLVAEHVSV----------LTQTPAAvamlPTQGLES 1741
Cdd:cd05940   125 LYTCLPLYHSTALIVGWSACLASGATLVI-RKKFSAS--NFWDDIRKYQATIfqyigelcryLLNQPPK----PTERKHK 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1742 VALVVAGEACPAA---LVDRWAPGRVmLNAYGPTETTiCAAISAPLRPGS--GMPPIGVPVSGAALFVLD---------- 1806
Cdd:cd05940   198 VRMIFGNGLRPDIweeFKERFGVPRI-AEFYAATEGN-SGFINFFGKPGAigRNPSLLRKVAPLALVKYDlesgepirda 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1807 -SWLRPVPAGVAGEL--YIAGAGVGVGYWRRAGLTASRFVACpFgGSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRG 1883
Cdd:cd05940   276 eGRCIKVPRGEPGLLisRINPLEPFDGYTDPAATEKKILRDV-F-KKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKG 353

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1884 YRIELGEVATALAELAGVGQAVVIAREdRPGDKRLVGYATEI--APGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLT 1961
Cdd:cd05940   354 ENVSTTEVAAVLGAFPGVEEANVYGVQ-VPGTDGRAGMAAIVlqPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEIT 432


                  ....
gi 489495878 1962 VNGK 1965
Cdd:cd05940   433 GTFK 436
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
 1632-1966 7.38e-18

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 87.56  E-value: 7.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1632 NLAYILYTSGTTGEPKGVGITHRNVTRLFASlparlsaaqvWSQC----------------HSYGFDASaweIWGALLGG 1695
Cdd:cd17638     1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAA----------WADCadlteddryliinpffHTFGYKAG---IVACLLTG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1696 GrlVIVPESVAASPNDFHgLLVAEHVSVLTQTPA------AVAMLPTQGLESVALVVAGEA-CPAALVDRWA---PGRVM 1765
Cdd:cd17638    68 A--TVVPVAVFDVDAILE-AIERERITVLPGPPTlfqsllDHPGRKKFDLSSLRAAVTGAAtVPVELVRRMRselGFETV 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1766 LNAYGPTEtTICAAISaplRPGSGMPPI----GVPVSGAALFVLDswlrpvpagvAGELYIAGAGVGVGYWRRAGLTASR 1841
Cdd:cd17638   145 LTAYGLTE-AGVATMC---RPGDDAETVattcGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATAEA 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1842 FVACPFggsgarmYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIARED-RPGDkrlVG 1920
Cdd:cd17638   211 IDADGW-------LHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDeRMGE---VG 280

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 489495878 1921 YATEIA--PGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKL 1966
Cdd:cd17638   281 KAFVVArpGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
PRK08308 PRK08308
acyl-CoA synthetase; Validated
 1520-1975 8.80e-18

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 88.55  E-value: 8.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1520 YRELDEASNRLAHRLAGCGAGPGECVALLFercapavvamvAVLKTGAAYLPIDPANPpprvafmLGDAVPVAavTTAGL 1599
Cdd:PRK08308   21 YEEMEQFQEAAGNRFAVCLKDPFDIITLVF-----------FLKEKGASVLPIHPDTP-------KEAAIRMA--KRAGC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1600 RSRLAGHDLPIIDVVDALAAYPGtpppmpaavnlAYILYTSGTTGEPKGVGITHRNVTRLFASLPARLSAAQVWS---QC 1676
Cdd:PRK08308   81 HGLLYGESDFTKLEAVNYLAEEP-----------SLLQYSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETpivAC 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1677 ---HSYGFdasaweIWGALLG---GGRLVIVpesVAASPNDFHGLLVAEHVSVLTQTPA---AVAMLPTQGLESVALVVA 1747
Cdd:PRK08308  150 pvtHSYGL------ICGVLAAltrGSKPVII---TNKNPKFALNILRNTPQHILYAVPLmlhILGRLLPGTFQFHAVMTS 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1748 GEACPAALVDRW-APGRVMLNAYGPTETTiCAAISAPLRPGSGMppiGVPVSGAALfvldswlrpvpagvagelyiaGAG 1826
Cdd:PRK08308  221 GTPLPEAWFYKLrERTTYMMQQYGCSEAG-CVSICPDMKSHLDL---GNPLPHVSV---------------------SAG 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1827 VGVGYWRRAGLTASRfvacpfggsgaRMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVV 1906
Cdd:PRK08308  276 SDENAPEEIVVKMGD-----------KEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVV 344

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489495878 1907 IAREDRPGDKRLVgyATEIAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRALPAPE 1975
Cdd:PRK08308  345 YRGKDPVAGERVK--AKVISHEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELGE 411
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
 1519-1971 9.52e-18

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 89.65  E-value: 9.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1519 TYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTG--AAYLPIDPANPPPRVAF--------MLGDA 1588
Cdd:cd05906    41 SYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGfvPAPLTVPPTYDEPNARLrklrhiwqLLGSP 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1589 VpvaAVTTAGLRSRLAG-------HDLPIIDVVDALAAYPGTPPPMPAAVNLAYILYTSGTTGEPKGVGITHRNV-TRLF 1660
Cdd:cd05906   121 V---VLTDAELVAEFAGletlsglPGIRVLSIEELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNIlARSA 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1661 ASLPARLSAAQ----VWsqchsYGFD--ASAWE--IWGALLGGGRLVIVPESVAASPNDFHGLLVAEHVSVlTQTPA-AV 1731
Cdd:cd05906   198 GKIQHNGLTPQdvflNW-----VPLDhvGGLVElhLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTI-TWAPNfAF 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1732 AMLpTQGLESVA-----------LVVAGEACPAALVDRW--------APGRVMLNAYGPTETtiCAAI-------SAPLR 1785
Cdd:cd05906   272 ALL-NDLLEEIEdgtwdlsslryLVNAGEAVVAKTIRRLlrllepygLPPDAIRPAFGMTET--CSGViysrsfpTYDHS 348

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1786 PGSGMPPIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVAcpfGGsgarMYRTGDLvCWRA 1865
Cdd:cd05906   349 QALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTE---DG----WFRTGDL-GFLD 420

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1866 DGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQ----AVVIAREDRPGDKRLVGYATEIAPGAVDPAGLRA--QL 1939
Cdd:cd05906   421 NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsftaAFAVRDPGAETEELAIFFVPEYDLQDALSETLRAirSV 500

                         490       500       510
                  ....*....|....*....|....*....|....
gi 489495878 1940 AQRLPGyLVPAAVVVI--DALPLTVNGKLDHRAL 1971
Cdd:cd05906   501 VSREVG-VSPAYLIPLpkEEIPKTSLGKIQRSKL 533
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
535-853 1.71e-17

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 88.63  E-value: 1.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  535 VTVVDVAATQLAVVGHDELRKVVDERVTQVTHDALLATKTAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRA-YGWGAH 613
Cdd:COG0365   147 VIVVGRTGADVPMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYvLDLKPG 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  614 DTVLqCaplTSDI-------SVeeIFGGAACGARLV-RSAAMKTGDLAALVDdLVARE--TTIVDLPTAVWQLLCADGDA 683
Cdd:COG0365   227 DVFW-C---TADIgwatghsYI--VYGPLLNGATVVlYEGRPDFPDPGRLWE-LIEKYgvTVFFTAPTAIRALMKAGDEP 299

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  684 IDAIGRSRLRQIVIGGEAIRCSAVDKWLESAasqGISLLSSYGPTEAT-VVATFLPIV-----CDQTTMDGALLRL---- 753
Cdd:COG0365   300 LKKYDLSSLRLLGSAGEPLNPEVWEWWYEAV---GVPIVDGWGQTETGgIFISNLPGLpvkpgSMGKPVPGYDVAVvded 376

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  754 GRPILPNTVflafGEVVIVGDL--VADGYLGidgdgfgtvtaaDGSRRRA---------FATGDRVTVDAEGFPVFSGRK 822
Cdd:COG0365   377 GNPVPPGEE----GELVIKGPWpgMFRGYWN------------DPERYREtyfgrfpgwYRTGDGARRDEDGYFWILGRS 440

                         330       340       350
                  ....*....|....*....|....*....|.
gi 489495878  823 DAVVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:COG0365   441 DDVINVSGHRIGTAEIESALVSHPAVAEAAV 471
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
1518-1989 1.73e-17

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 89.32  E-value: 1.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1518 MTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVTTA 1597
Cdd:PRK06060   31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSD 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1598 GLRSRLAGHDL--PIIDVVDALAAYPGTPPPMPAAVnLAYILYTSGTTGEPKGVGITH-----------RNVTRLfasLP 1664
Cdd:PRK06060  111 ALRDRFQPSRVaeAAELMSEAARVAPGGYEPMGGDA-LAYATYTSGTTGPPKAAIHRHadpltfvdamcRKALRL---TP 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1665 AR--LSAAQVWsqcHSYGFDASaweIWGALLGGGRLVIVPESVAAspnDFHGLLVAE-HVSVLTQTPA----AVAMLPTQ 1737
Cdd:PRK06060  187 EDtgLCSARMY---FAYGLGNS---VWFPLATGGSAVINSAPVTP---EAAAILSARfGPSVLYGVPNffarVIDSCSPD 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1738 GLESVALVV-AGEACPAALVDRWAP---GRVMLNAYGPTET--TICAAISAPLRPGS---GMPPIGVPV---SGAAlfvl 1805
Cdd:PRK06060  258 SFRSLRCVVsAGEALELGLAERLMEffgGIPILDGIGSTEVgqTFVSNRVDEWRLGTlgrVLPPYEIRVvapDGTT---- 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1806 dswlrpVPAGVAGELYIAGAGVGVGYWRRAGltasrfvacPFGGSGARMyRTGDLVCWRADGQLEFLGRTDDQVKIRGYR 1885
Cdd:PRK06060  334 ------AGPGVEGDLWVRGPAIAKGYWNRPD---------SPVANEGWL-DTRDRVCIDSDGWVTYRCRADDTEVIGGVN 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1886 IELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATEIAPGAVDPAGLR---AQLAQRLPGYLVPAAVVVIDALPLTV 1962
Cdd:PRK06060  398 VDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRdlhRGLLNRLSAFKVPHRFAVVDRLPRTP 477

                         490       500
                  ....*....|....*....|....*..
gi 489495878 1963 NGKLDHRALPApeygdtngyRAPAGPV 1989
Cdd:PRK06060  478 NGKLVRGALRK---------QSPTKPI 495
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
 1503-1971 1.73e-17

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 88.20  E-value: 1.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1503 ARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANP---PP 1579
Cdd:cd05929     3 ARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPraeAC 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1580 RVAFMLGDAVPVAAVTTAGLRSRLAghdlpiiDVVDALAAYPGTPPPMPAAVNlaYILYTSGTTGEPKGV-----GITHR 1654
Cdd:cd05929    83 AIIEIKAAALVCGLFTGGGALDGLE-------DYEAAEGGSPETPIEDEAAGW--KMLYSGGTTGRPKGIkrglpGGPPD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1655 NVTRLFASLPARLSAAQVW----SQCHSYGFDASAweiwGALLGGGRLVIVPEsvaASPNDFHGLLVAEHVSVLTQTPAA 1730
Cdd:cd05929   154 NDTLMAAALGFGPGADSVYlspaPLYHAAPFRWSM----TALFMGGTLVLMEK---FDPEEFLRLIERYRVTFAQFVPTM 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1731 -VAMLPTQG-------LESVALVV-AGEACPAALVDRWAP--GRVMLNAYGPTE---TTICAAISAPLRPGSgmppIGVP 1796
Cdd:cd05929   227 fVRLLKLPEavrnaydLSSLKRVIhAAAPCPPWVKEQWIDwgGPIIWEYYGGTEgqgLTIINGEEWLTHPGS----VGRA 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1797 VSGaALFVLDSWLRPVPAGVAGELYIAGAGvGVGYWRR-AGLTASRfvacpfggsGARMYRT-GDLVCWRADGQLEFLGR 1874
Cdd:cd05929   303 VLG-KVHILDEDGNEVPPGEIGEVYFANGP-GFEYTNDpEKTAAAR---------NEGGWSTlGDVGYLDEDGYLYLTDR 371

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1875 TDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRL---VGYATEIAPGAVDPAGLRAQLAQRLPGYLVPAA 1951
Cdd:cd05929   372 RSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVhavVQPAPGADAGTALAEELIAFLRDRLSRYKCPRS 451

                         490       500
                  ....*....|....*....|
gi 489495878 1952 VVVIDALPLTVNGKLDHRAL 1971
Cdd:cd05929   452 IEFVAELPRDDTGKLYRRLL 471
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
501-853 2.00e-17

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 88.41  E-value: 2.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  501 IACHLAGCGYSVCDT--ADEisvRTNAITEHGDG---ILVTVVDVAATQLAVVGHDELRKVVDERVTQVTHDALLATKTA 575
Cdd:PRK04813   70 LGAVKAGHAYIPVDVssPAE---RIEMIIEVAKPsliIATEELPLEILGIPVITLDELKDIFATGNPYDFDHAVKGDDNY 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  576 YIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGarlvrsaamktGDLAAL 655
Cdd:PRK04813  147 YIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASG-----------GTLVAL 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  656 VDDLVARE----TTIVDLPTAVWQL------LCADGDAIDAIGRSRLRQIVIGGEAIRCSAVDKWLESAASQGIslLSSY 725
Cdd:PRK04813  216 PKDMTANFkqlfETLPQLPINVWVStpsfadMCLLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERFPSATI--YNTY 293

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  726 GPTEATVVATFLPI---VCDQTTMdgalLRLGRP--------------ILPNTvflAFGEVVIVGDLVADGYLGIDgdgf 788
Cdd:PRK04813  294 GPTEATVAVTSIEItdeMLDQYKR----LPIGYAkpdsplliideegtKLPDG---EQGEIVISGPSVSKGYLNNP---- 362

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489495878  789 gTVTAA-----DGsrRRAFATGDRVTVDaEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAV-SDVAV 853
Cdd:PRK04813  363 -EKTAEafftfDG--QPAYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVeSAVVV 429
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 531-853 2.00e-17

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 88.46  E-value: 2.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  531 DGILVTVVDVAATQLAVVGH-----DELRKVVDERVTQVTHDALLAT------------KTAYIMP-TSGTTGQPKLVRI 592
Cdd:cd12119   104 DRDFLPLLEAIAPRLPTVEHvvvmtDDAAMPEPAGVGVLAYEELLAAespeydwpdfdeNTAAAICyTSGTTGNPKGVVY 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  593 SHGSLAVFCDAISRAYGWGAH--DTVLQCAPLTSDISVEEIFGGAACGARLVRSAAMKTGDLAAlvdDLVARE--TTIVD 668
Cdd:cd12119   184 SHRSLVLHAMAALLTDGLGLSesDVVLPVVPMFHVNAWGLPYAAAMVGAKLVLPGPYLDPASLA---ELIEREgvTFAAG 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  669 LPTaVWQLLCADGDAIDAiGRSRLRQIVIGGEAIRCSAVDKWLEsaasQGISLLSSYGPTEATVVATF--LPIVCDQTTM 746
Cdd:cd12119   261 VPT-VWQGLLDHLEANGR-DLSSLRRVVIGGSAVPRSLIEAFEE----RGVRVIHAWGMTETSPLGTVarPPSEHSNLSE 334

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  747 DGAL-LRL--GRPIL--------PNTVFL-----AFGEVVIVGDLVADGYLGIDGDgfGTVTAADGsrrrAFATGDRVTV 810
Cdd:cd12119   335 DEQLaLRAkqGRPVPgvelrivdDDGRELpwdgkAVGELQVRGPWVTKSYYKNDEE--SEALTEDG----WLRTGDVATI 408

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 489495878  811 DAEGFPVFSGR-KDaVVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:cd12119   409 DEDGYLTITDRsKD-VIKSGGEWISSVELENAIMAHPAVAEAAV 451
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
1621-1971 2.66e-17

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 89.25  E-value: 2.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1621 PGTPPPMPAAVNLAYILYTSGTTGEPKGVGITHRNVTRLFASLPAR--LSAAQVWSQC----HSYGFDAsaweiwGALL- 1693
Cdd:PRK06814  783 PLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARidFSPEDKVFNAlpvfHSFGLTG------GLVLp 856

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1694 --GGGRLV---------IVPESV--------------------AASPNDFHgllvaehvsvltqtpaavamlptqgleSV 1742
Cdd:PRK06814  857 llSGVKVFlypsplhyrIIPELIydtnatilfgtdtflngyarYAHPYDFR---------------------------SL 909

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1743 ALVVAG-EACPAALVDRWAP--GRVMLNAYGPTETTICAAISAPL--RPGSgmppigvpvSGAALFVLDSWLRPVPaGV- 1816
Cdd:PRK06814  910 RYVFAGaEKVKEETRQTWMEkfGIRILEGYGVTETAPVIALNTPMhnKAGT---------VGRLLPGIEYRLEPVP-GId 979

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1817 -AGELYIAGAGVGVGYWRragLTASRFVACPFGGsgarMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATAL 1895
Cdd:PRK06814  980 eGGRLFVRGPNVMLGYLR---AENPGVLEPPADG----WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELA 1052

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489495878 1896 AELAGVGQAVVIAREDRPGDKRLVGYATeiAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:PRK06814 1053 AELWPDALHAAVSIPDARKGERIILLTT--ASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKIDYVAV 1126
PRK05691 PRK05691
peptide synthase; Validated
 575-918 3.36e-17

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 89.46  E-value: 3.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  575 AYIMPTSGTTGQPKLVRIS-HGSLAvfcDAISRA--YGWGAHDTVLQCAPLTSDISVEEIFGGAACGARLVRSAAMKTGD 651
Cdd:PRK05691 3872 AYVIYTSGSTGLPKGVMVEqRGMLN---NQLSKVpyLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHD 3948

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  652 LAALVDDLVARETTIVD-LPTAVWQLLCADGDAIDAigrsrLRQIVIGGEAIRCSAVDKWLESAAsqGISLLSSYGPTEA 730
Cdd:PRK05691 3949 PQGLLAHVQAQGITVLEsVPSLIQGMLAEDRQALDG-----LRWMLPTGEAMPPELARQWLQRYP--QIGLVNAYGPAEC 4021

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  731 TVVATFLPIvcDQTTMDGALLRLGRPILPNTVFL-----------AFGEVVIVGDLVADGYLGidgDGFGTVTA------ 793
Cdd:PRK05691 4022 SDDVAFFRV--DLASTRGSYLPIGSPTDNNRLYLldealelvplgAVGELCVAGTGVGRGYVG---DPLRTALAfvphpf 4096

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  794 -ADGsrRRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAVELHSGSLGVWFKSQRT-RE 871
Cdd:PRK05691 4097 gAPG--ERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNGKHLVGYLVpHQ 4174

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489495878  872 GEQDAAA-----ATRIRLVLVSLGVSSFFVVgVPNIPRKPNGKIDSDNLPRL 918
Cdd:PRK05691 4175 TVLAQGAlleriKQRLRAELPDYMVPLHWLW-LDRLPLNANGKLDRKALPAL 4225
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
 1493-1971 5.00e-17

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 87.38  E-value: 5.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1493 SIPQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPI 1572
Cdd:PRK07059   24 SLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1573 DPANPPPRVAFMLGD-----------------------AVPVAAVTTAGLRSRLAGHdlpIIDVV--------------- 1614
Cdd:PRK07059  104 NPLYTPRELEHQLKDsgaeaivvlenfattvqqvlaktAVKHVVVASMGDLLGFKGH---IVNFVvrrvkkmvpawslpg 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1615 -----DALAAYPGTP--PPMPAAVNLAYILYTSGTTGEPKGVGITHRNVTRLFASLPARLSAA--------QVWSQC--- 1676
Cdd:PRK07059  181 hvrfnDALAEGARQTfkPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAfekkprpdQLNFVCalp 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1677 --HSYGFDASAweiwgaLLG---GGRLVIVPesvaaSPNDFHGLLVAEHVSVLTQTPAAV----AMLPTQGLESV---AL 1744
Cdd:PRK07059  261 lyHIFALTVCG------LLGmrtGGRNILIP-----NPRDIPGFIKELKKYQVHIFPAVNtlynALLNNPDFDKLdfsKL 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1745 VVA---GEACPAALVDRW--APGRVMLNAYGPTETT---ICAAISAPLRPGSgmppIGVPVSGAALFVLDSWLRPVPAGV 1816
Cdd:PRK07059  330 IVAnggGMAVQRPVAERWleMTGCPITEGYGLSETSpvaTCNPVDATEFSGT----IGLPLPSTEVSIRDDDGNDLPLGE 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1817 AGELYIAGAGVGVGYWRRAGLTASRFVACPFggsgarmYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALA 1896
Cdd:PRK07059  406 PGEICIRGPQVMAGYWNRPDETAKVMTADGF-------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVA 478

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489495878 1897 ELAGVGQAVVIAREDRPGDKRLVGYATEIAPgAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:PRK07059  479 SHPGVLEVAAVGVPDEHSGEAVKLFVVKKDP-ALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
PRK07529 PRK07529
AMP-binding domain protein; Validated
 1491-1965 5.85e-17

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 87.32  E-value: 5.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1491 PVSIPQMLAAQVARIPEAEAVCC---GDA-----SMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAV 1562
Cdd:PRK07529   24 PASTYELLSRAAARHPDAPALSFlldADPldrpeTWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGG 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1563 LKTGAAYlPIDPANPPP---------------------------RVAFMLGDAVPVAAVTTAGLRSRLAG---------- 1605
Cdd:PRK07529  104 EAAGIAN-PINPLLEPEqiaellraagakvlvtlgpfpgtdiwqKVAEVLAALPELRTVVEVDLARYLPGpkrlavplir 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1606 --HDLPIIDVVDALAAYPGT---PPPMPAAVNLAYILYTSGTTGEPKGVGITHRNvtrlfaslparlSAAQVWSQCHSYG 1680
Cdd:PRK07529  183 rkAHARILDFDAELARQPGDrlfSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGN------------EVANAWLGALLLG 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1681 FDASAWEIWG---------------ALLGGGRLVIVPESVAASPNDFHGL--LVAEH-VSVLTQTPAAVAML---PTQG- 1738
Cdd:PRK07529  251 LGPGDTVFCGlplfhvnallvtglaPLARGAHVVLATPQGYRGPGVIANFwkIVERYrINFLSGVPTVYAALlqvPVDGh 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1739 -LESVALVVAGEA-CPAALVDRW--APGRVMLNAYGPTETT---ICAAISAPLRPGSgmppIGVPVSGAALFVL-----D 1806
Cdd:PRK07529  331 dISSLRYALCGAApLPVEVFRRFeaATGVRIVEGYGLTEATcvsSVNPPDGERRIGS----VGLRLPYQRVRVVilddaG 406

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1807 SWLRPVPAGVAGELYIAGAGVGVGYwrragLTASRFVACPFGGsgaRMYRTGDLVCWRADGQLEFLGRTDDQVkIR-GYR 1885
Cdd:PRK07529  407 RYLRDCAVDEVGVLCIAGPNVFSGY-----LEAAHNKGLWLED---GWLNTGDLGRIDADGYFWLTGRAKDLI-IRgGHN 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1886 IELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYaTEIAPGA-VDPAGLRAQLAQRLPGYL-VPAAVVVIDALPLTVN 1963
Cdd:PRK07529  478 IDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAY-VQLKPGAsATEAELLAFARDHIAERAaVPKHVRILDALPKTAV 556


                  ..
gi 489495878 1964 GK 1965
Cdd:PRK07529  557 GK 558
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
 1479-1961 1.94e-16

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 85.70  E-value: 1.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1479 GNRAVLTAPAPTPVSIPQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVA 1558
Cdd:PRK08279   24 GLKRTALITPDSKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1559 MVAVLKTGA----------------------------------AYLPIDPANPPPRVAFMLGDAVPVAAVTtaglrsrla 1604
Cdd:PRK08279  104 WLGLAKLGAvvallntqqrgavlahslnlvdakhlivgeelveAFEEARADLARPPRLWVAGGDTLDDPEG--------- 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1605 ghdlpIIDVVDALAAYPGTPPPMPAAVNL---AYILYTSGTTGEPKGVGITHRNVTRLFAS--LPARLSAAQVWSQC--- 1676
Cdd:PRK08279  175 -----YEDLAAAAAGAPTTNPASRSGVTAkdtAFYIYTSGTTGLPKAAVMSHMRWLKAMGGfgGLLRLTPDDVLYCClpl 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1677 -HSYGFDASaweiWGALLGGGRLVIVPESVAASpnDFHGLLVAEHVSV----------LTQTPAAvamlPTQGLESVALV 1745
Cdd:PRK08279  250 yHNTGGTVA----WSSVLAAGATLALRRKFSAS--RFWDDVRRYRATAfqyigelcryLLNQPPK----PTDRDHRLRLM 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1746 VAGEACP---AALVDRWAPGRVmLNAYGPTETTIcAAISAPLRPGS-------GMPPIGV---------PVSGAalfvlD 1806
Cdd:PRK08279  320 IGNGLRPdiwDEFQQRFGIPRI-LEFYAASEGNV-GFINVFNFDGTvgrvplwLAHPYAIvkydvdtgePVRDA-----D 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1807 SWLRPVPAGVAGELY--IAGAGVGVGYWRRAGlTASRFVACPFgGSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGY 1884
Cdd:PRK08279  393 GRCIKVKPGEVGLLIgrITDRGPFDGYTDPEA-SEKKILRDVF-KKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGE 470

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1885 RIELGEVATALAELAGVGQAVViaredrpgdkrlvgYATEIaPG----------------AVDPAGLRAQLAQRLPGYLV 1948
Cdd:PRK08279  471 NVATTEVENALSGFPGVEEAVV--------------YGVEV-PGtdgragmaaivladgaEFDLAALAAHLYERLPAYAV 535

                         570
                  ....*....|...
gi 489495878 1949 PAAVVVIDALPLT 1961
Cdd:PRK08279  536 PLFVRLVPELETT 548
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 1057-1350 2.16e-16

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 84.08  E-value: 2.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1057 LDTEALGAAVADVVGRHESLRTVFPAvDGvprQLVIEARRADLGCDIVDATAWPADRLQRAIE---EAARHSFdLATEip 1133
Cdd:cd19535    37 LDPDRLERAWNKLIARHPMLRAVFLD-DG---TQQILPEVPWYGITVHDLRGLSEEEAEAALEelrERLSHRV-LDVE-- 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1134 lRTWLFRIA-----DDEHVLvavahHI-----AADGWSVAPLTADLSAAYASRCAGRAPdwapLPVQYVDYTLWQREilg 1203
Cdd:cd19535   110 -RGPLFDIRlsllpEGRTRL-----HLsidllVADALSLQILLRELAALYEDPGEPLPP----LELSFRDYLLAEQA--- 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1204 dldDSDSPIAAQLAYWENALAGMPERLRLPTARPYPPVADQRGASLVVDWPASVQQQVRRIARQHNATSFMVVAAGLAVL 1283
Cdd:cd19535   177 ---LRETAYERARAYWQERLPTLPPAPQLPLAKDPEEIKEPRFTRREHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEV 253

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489495878 1284 LSKLSGSPDVAVGFPIAGR--SDPALDNLVGFFVNTLVLRVNLAGDPSFAELLGQVRARSLAAYENQDV 1350
Cdd:cd19535   254 LARWSGQPRFLLNLTLFNRlpLHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQLWEDLDHSSY 322
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
 575-853 2.28e-16

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 82.76  E-value: 2.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  575 AYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARLVrsaaMKTGDLAA 654
Cdd:cd17630     3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELV----LLERNQAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  655 LVDDLVARETTIVDLPTAVWQLLCADGDAIDaigRSRLRQIVIGGEAIrcSAVDkwLESAASQGISLLSSYGPTE--ATV 732
Cdd:cd17630    79 AEDLAPPGVTHVSLVPTQLQRLLDSGQGPAA---LKSLRAVLLGGAPI--PPEL--LERAADRGIPLYTTYGMTEtaSQV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  733 VATFLPIVCDQTT---MDGALLRLGRPilpntvflafGEVVIVGDLVADGYLGidgdgfgTVTAADGSRRRAFATGDRVT 809
Cdd:cd17630   152 ATKRPDGFGRGGVgvlLPGRELRIVED----------GEIWVGGASLAMGYLR-------GQLVPEFNEDGWFTTKDLGE 214

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 489495878  810 VDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:cd17630   215 LHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFV 258
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
 1636-1966 2.29e-16

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 83.08  E-value: 2.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1636 ILYTSGTTGEPKGVGITHRNvtrLFASLPARLSAAQVWSQ----------CHSYGfdaSAWEIWGALLGGGRLVIVPESV 1705
Cdd:cd17635     6 VIFTSGTTGEPKAVLLANKT---FFAVPDILQKEGLNWVVgdvtylplpaTHIGG---LWWILTCLIHGGLCVTGGENTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1706 AASpndFHGLLVAEHVSVLTQTPAAVAMLPT------QGLESVALVVAGEACPAALVDR---WAPGRVMLNAYGPTETTi 1776
Cdd:cd17635    80 YKS---LFKILTTNAVTTTCLVPTLLSKLVSelksanATVPSLRLIGYGGSRAIAADVRfieATGLTNTAQVYGLSETG- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1777 cAAISAPLRPGSG-MPPIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVacpfGGsgarMY 1855
Cdd:cd17635   156 -TALCLPTDDDSIeINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI----DG----WV 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1856 RTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKrLVGYATeIAPGAVDPAGL 1935
Cdd:cd17635   227 NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGE-LVGLAV-VASAELDENAI 304

                         330       340       350
                  ....*....|....*....|....*....|....
gi 489495878 1936 RAQ---LAQRLPGYLVPAAVVVIDALPLTVNGKL 1966
Cdd:cd17635   305 RALkhtIRRELEPYARPSTIVIVTDIPRTQSGKV 338
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
1493-1971 3.34e-16

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 84.54  E-value: 3.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1493 SIPQMLAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAG-CGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLP 1571
Cdd:PRK08751   26 TVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGeLQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVN 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1572 IDPANPPPRVAFMLGDA---------------------VPVAAVTTAGLRSRLAGHDLPIIDVV---------------- 1614
Cdd:PRK08751  106 VNPLYTPRELKHQLIDSgasvlvvidnfgttvqqviadTPVKQVITTGLGDMLGFPKAALVNFVvkyvkklvpeyringa 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1615 ----DALAAypGTPPPMP----AAVNLAYILYTSGTTGEPKGVGITHRNvtrlfasLPARLSAAQVWSQChSYGFDASAW 1686
Cdd:PRK08751  186 irfrEALAL--GRKHSMPtlqiEPDDIAFLQYTGGTTGVAKGAMLTHRN-------LVANMQQAHQWLAG-TGKLEEGCE 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1687 EIWGAL-------LGGGRLVIVP----ESVAASPNDFHGLlvaehVSVLTQTPAAV---------AMLPTQGLESVAL-- 1744
Cdd:PRK08751  256 VVITALplyhifaLTANGLVFMKiggcNHLISNPRDMPGF-----VKELKKTRFTAftgvntlfnGLLNTPGFDQIDFss 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1745 ----VVAGEACPAALVDRW--APGRVMLNAYGPTETTICAAISaPLRPGSGMPPIGVPVSGAALFVLDSWLRPVPAGVAG 1818
Cdd:PRK08751  331 lkmtLGGGMAVQRSVAERWkqVTGLTLVEAYGLTETSPAACIN-PLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIG 409

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1819 ELYIAGAGVGVGYWRRAGLTASRFVACPFggsgarmYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAEL 1898
Cdd:PRK08751  410 ELCIKGPQVMKGYWKRPEETAKVMDADGW-------LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMM 482

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489495878 1899 AGVGQAVVIAREDRPGdkrlvGYATEIAPGAVDPA----GLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:PRK08751  483 PGVLEVAAVGVPDEKS-----GEIVKVVIVKKDPAltaeDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
 1517-1971 3.48e-16

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 83.55  E-value: 3.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1517 SMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVaavtt 1596
Cdd:cd05912     1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVK----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1597 aglrsrlaghdlpiidvVDALAAypgtpppmpaavnlayILYTSGTTGEPKGVGITHRNVtrlFASlpARLSAAQV---- 1672
Cdd:cd05912    76 -----------------LDDIAT----------------IMYTSGTTGKPKGVQQTFGNH---WWS--AIGSALNLglte 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1673 ---WSQC----HSYGFDAsaweIWGALLGGGRLVIVPesvAASPNDFHGLLVAEHVSVLTQTPAAVAMLPTQGLESVA-- 1743
Cdd:cd05912   118 ddnWLCAlplfHISGLSI----LMRSVIYGMTVYLVD---KFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPnn 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1744 ---LVVAGEACPAALVDRWAP-GRVMLNAYGPTETT--ICAA--ISAPLRPGS-GMPPIGVPVSgaalFVLDSwlrpVPA 1814
Cdd:cd05912   191 lrcILLGGGPAPKPLLEQCKEkGIPVYQSYGMTETCsqIVTLspEDALNKIGSaGKPLFPVELK----IEDDG----QPP 262

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1815 GVAGELYIAGAGVGVGYWRRAGLTASRFVACPFggsgarmyRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATA 1894
Cdd:cd05912   263 YEVGEILLKGPNVTKGYLNRPDATEESFENGWF--------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEV 334

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489495878 1895 LAELAGVGQAVVIAREDRPGDKRLVGYAteIAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:cd05912   335 LLSHPAIKEAGVVGIPDDKWGQVPVAFV--VSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
PRK07867 PRK07867
acyl-CoA synthetase; Validated
 1594-1973 8.53e-16

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 83.19  E-value: 8.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1594 VTTAGLRSRLAGHD--LPIIDV-----VDALAAYPGTPPPM--PAAVNLAYILYTSGTTGEPKGVGITHRNVTRLFASLP 1664
Cdd:PRK07867  106 LTESAHAELLDGLDpgVRVINVdspawADELAAHRDAEPPFrvADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLA 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1665 AR--LSAAQVWSQC----HSYGFDAsAWEIwgALLGGGRLVIvPESVAASpndfhGLL-------------VAEHVSVLT 1725
Cdd:PRK07867  186 QRfgLGPDDVCYVSmplfHSNAVMA-GWAV--ALAAGASIAL-RRKFSAS-----GFLpdvrrygatyanyVGKPLSYVL 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1726 QTPAavamLPTQGLESVALVVAGEACPAAlVDRWAP--GRVMLNAYGPTETTICAAISAPLRPGSgmppIGVPVSGAALF 1803
Cdd:PRK07867  257 ATPE----RPDDADNPLRIVYGNEGAPGD-IARFARrfGCVVVDGFGSTEGGVAITRTPDTPPGA----LGPLPPGVAIV 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1804 VLDSwLRPVPAGVA------------GELY-IAGAGVGVGYWRRAGLTASRFVacpfGGsgarMYRTGDLVCWRADGQLE 1870
Cdd:PRK07867  328 DPDT-GTECPPAEDadgrllnadeaiGELVnTAGPGGFEGYYNDPEADAERMR----GG----VYWSGDLAYRDADGYAY 398

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1871 FLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRP-GDKrlVGYATEIAPGAV-DPAGLRAQLAQR--LPGY 1946
Cdd:PRK07867  399 FAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVvGDQ--VMAALVLAPGAKfDPDAFAEFLAAQpdLGPK 476

                         410       420
                  ....*....|....*....|....*..
gi 489495878 1947 LVPAAVVVIDALPLTVNGKLDHRALPA 1973
Cdd:PRK07867  477 QWPSYVRVCAELPRTATFKVLKRQLSA 503
PRK13382 PRK13382
bile acid CoA ligase;
1498-1974 8.78e-16

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 83.27  E-value: 8.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1498 LAAQVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANP 1577
Cdd:PRK13382   49 FAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFA 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1578 PPRVAFMLG--------------DAVPVAAVTTAGLRSRLAGHDLPIIDVVDALAAYPGTPPPMPAAVNLAYILYTSGTT 1643
Cdd:PRK13382  129 GPALAEVVTregvdtviydeefsATVDRALADCPQATRIVAWTDEDHDLTVEVLIAAHAGQRPEPTGRKGRVILLTSGTT 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1644 GEPKGV------------GITHRnvTRLFASLPARLSAAQVwsqcHSYGFdasAWEIWGALLgggRLVIV------PESV 1705
Cdd:PRK13382  209 GTPKGArrsgpggigtlkAILDR--TPWRAEEPTVIVAPMF----HAWGF---SQLVLAASL---ACTIVtrrrfdPEAT 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1706 AAspndfhglLVAEHvsvltqTPAAVAMLPT---QGLESVALV-------------VAGEACPAALV----DRWapGRVM 1765
Cdd:PRK13382  277 LD--------LIDRH------RATGLAVVPVmfdRIMDLPAEVrnrysgrslrfaaASGSRMRPDVViafmDQF--GDVI 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1766 LNAYGPTETT-ICAAISAPLR--PGSGmppiGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYwrragltasrf 1842
Cdd:PRK13382  341 YNNYNATEAGmIATATPADLRaaPDTA----GRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY----------- 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1843 vacpfgGSGAR------MYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDK 1916
Cdd:PRK13382  406 ------TSGSTkdfhdgFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQ 479

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 489495878 1917 RLVGYATEIAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRALPAP 1974
Cdd:PRK13382  480 RLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
 1636-1967 1.37e-15

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 80.42  E-value: 1.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1636 ILYTSGTTGEPKGVGITHRNVtrlfasLPARLSAAQVWSQCHSYGFDASA--WEIwGALLG-------GGRLVIVPesvA 1706
Cdd:cd17636     5 AIYTAAFSGRPNGALLSHQAL------LAQALVLAVLQAIDEGTVFLNSGplFHI-GTLMFtlatfhaGGTNVFVR---R 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1707 ASPNDFHGLLVAEHVS---VLTQTPAAVAMLPTQGLESV----ALVVAGEACPAALVDRWAPGRVMlNAYGPTETTICAA 1779
Cdd:cd17636    75 VDAEEVLELIEAERCThafLLPPTIDQIVELNADGLYDLsslrSSPAAPEWNDMATVDTSPWGRKP-GGYGQTEVMGLAT 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1780 ISAPLRPGSGMppIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVacpFGGsgarmYRTGD 1859
Cdd:cd17636   154 FAALGGGAIGG--AGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR---GGW-----HHTND 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1860 LVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDrPGDKRLVGYATEIAPGA-VDPAGLRAQ 1938
Cdd:cd17636   224 LGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPD-PRWAQSVKAIVVLKPGAsVTEAELIEH 302

                         330       340
                  ....*....|....*....|....*....
gi 489495878 1939 LAQRLPGYLVPAAVVVIDALPLTVNGKLD 1967
Cdd:cd17636   303 CRARIASYKKPKSVEFADALPRTAGGADD 331
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
 1517-1985 1.41e-15

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 82.92  E-value: 1.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1517 SMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVTT 1596
Cdd:cd05968    91 TLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITA 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1597 AGLRSRlaGHDLPIIDVVD-ALAAYP-----------GTPPPMPAAVNLAY---------------------ILYTSGTT 1643
Cdd:cd05968   171 DGFTRR--GREVNLKEEADkACAQCPtvekvvvvrhlGNDFTPAKGRDLSYdeeketagdgaertesedplmIIYTSGTT 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1644 GEPKGVGITHrnvtrlfASLParLSAAQVWSQCHS------------YGFDASAWEIWGALLGGGRLVI---VPESVAAs 1708
Cdd:cd05968   249 GKPKGTVHVH-------AGFP--LKAAQDMYFQFDlkpgdlltwftdLGWMMGPWLIFGGLILGATMVLydgAPDHPKA- 318

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1709 pnDFHGLLVAEH-VSVLTQTPAAVAMLPTQGLESVA------LVVAGEACPAALVDRW-------APGRV-MLNAYGPTE 1773
Cdd:cd05968   319 --DRLWRMVEDHeITHLGLSPTLIRALKPRGDAPVNahdlssLRVLGSTGEPWNPEPWnwlfetvGKGRNpIINYSGGTE 396

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1774 TT---ICAAISAPLRPGSgmppIGVPVSGAALFVLDSWLRPVPAGVaGELYIAGAGVGV--GYWRraglTASRFVACPFg 1848
Cdd:cd05968   397 ISggiLGNVLIKPIKPSS----FNGPVPGMKADVLDESGKPARPEV-GELVLLAPWPGMtrGFWR----DEDRYLETYW- 466

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1849 gsgARM---YRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATeI 1925
Cdd:cd05968   467 ---SRFdnvWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVV-L 542

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489495878 1926 APGAVDPAGLRAQLAQR----LPGYLVPAAVVVIDALPLTVNGKLDHRALPA----PEYGDTNGYRAP 1985
Cdd:cd05968   543 KPGVTPTEALAEELMERvadeLGKPLSPERILFVKDLPKTRNAKVMRRVIRAaylgKELGDLSSLENP 610
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
 1494-1966 2.13e-15

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 82.13  E-value: 2.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1494 IPQMLAAQVARIPEAEAVCCG--DASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLP 1571
Cdd:PRK12583   20 IGDAFDATVARFPDREALVVRhqALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1572 IDPANPPPRVAFMLGDAVPVAAVTTAGLRS--------------------RLAGHDLPIIDVVDALAaypGTPPP----- 1626
Cdd:PRK12583  100 INPAYRASELEYALGQSGVRWVICADAFKTsdyhamlqellpglaegqpgALACERLPELRGVVSLA---PAPPPgflaw 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1627 -----MPAAVNLA---------------YILYTSGTTGEPKGVGITHRNVTRLFASLPARLSAAQVWSQC------HSYG 1680
Cdd:PRK12583  177 helqaRGETVSREalaerqasldrddpiNIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCvpvplyHCFG 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1681 FDASaweIWGALLGGGRLVIvpesvaasPND-FHGLLVAEHVSVLTQTpaAVAMLPTQGLESV-----------AL---V 1745
Cdd:PRK12583  257 MVLA---NLGCMTVGACLVY--------PNEaFDPLATLQAVEEERCT--ALYGVPTMFIAELdhpqrgnfdlsSLrtgI 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1746 VAGEACPAALVDrwapgRVM--------LNAYGPTETT-----ICAAISAPLRPGSgmppIGVPVSGAALFVLDSWLRPV 1812
Cdd:PRK12583  324 MAGAPCPIEVMR-----RVMdemhmaevQIAYGMTETSpvslqTTAADDLERRVET----VGRTQPHLEVKVVDPDGATV 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1813 PAGVAGELYIAGAGVGVGYWRRAGLTASRFvacpfgGSGARMYrTGDLVCWRADGQLEFLGRTDDQVkIRG----YRIEL 1888
Cdd:PRK12583  395 PRGEIGELCTRGYSVMKGYWNNPEATAESI------DEDGWMH-TGDLATMDEQGYVRIVGRSKDMI-IRGgeniYPREI 466

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489495878 1889 GEVataLAELAGVGQAVVIAREDRPGDKRLVGYaTEIAPG-AVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKL 1966
Cdd:PRK12583  467 EEF---LFTHPAVADVQVFGVPDEKYGEEIVAW-VRLHPGhAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKV 541
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
1497-1971 3.17e-15

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 81.57  E-value: 3.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1497 MLAAQVAriPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGEC-------VALLFercapavVAMVAVLKTGAAy 1569
Cdd:PRK10946   30 ILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTalvqlgnVAEFY-------ITFFALLKLGVA- 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1570 lpidPAN------------------PPPRVA------FMLGDAVPVAAVTTAGLRSRLAGHDLPIIDVVDALAAYPGTPP 1625
Cdd:PRK10946  100 ----PVNalfshqrselnayasqiePALLIAdrqhalFSDDDFLNTLVAEHSSLRVVLLLNDDGEHSLDDAINHPAEDFT 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1626 PMP-AAVNLAYILYTSGTTGEPKGVGITH--------RNV--------TRLFASLPArlsaaqvwsqCHSYGFdaSAWEI 1688
Cdd:PRK10946  176 ATPsPADEVAFFQLSGGSTGTPKLIPRTHndyyysvrRSVeicgftpqTRYLCALPA----------AHNYPM--SSPGA 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1689 WGALLGGGRLVIVPESVAAS--PndfhglLVAEH-VSVLTQTPAAVAM------LPT--QGLESVALV-VAGEACPAALV 1756
Cdd:PRK10946  244 LGVFLAGGTVVLAPDPSATLcfP------LIEKHqVNVTALVPPAVSLwlqaiaEGGsrAQLASLKLLqVGGARLSETLA 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1757 DRwapgrvmlnaygptettICAAISAPLRPGSGM------------PPI------GVPVSGA-ALFVLDSWLRPVPAGVA 1817
Cdd:PRK10946  318 RR-----------------IPAELGCQLQQVFGMaeglvnytrlddSDErifttqGRPMSPDdEVWVADADGNPLPQGEV 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1818 GELYIAGAGVGVGYWRRAGLTASRFVACPFggsgarmYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAE 1897
Cdd:PRK10946  381 GRLMTRGPYTFRGYYKSPQHNASAFDANGF-------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLR 453

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489495878 1898 LAGVGQAVVIARED-RPGDKrlvGYATEIAPGAVDPAGLRAQL-AQRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:PRK10946  454 HPAVIHAALVSMEDeLMGEK---SCAFLVVKEPLKAVQLRRFLrEQGIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 540-910 7.73e-15

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 79.43  E-value: 7.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  540 VAATQLAVVGHDELRKVVDERVTQVTHDALL---ATKTAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAY-GWGAHDT 615
Cdd:cd05919    56 LARGAIAVVINPLLHPDDYAYIARDCEARLVvtsADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREAlGLTPGDR 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  616 VLQCAPLTSDISV-EEIFGGAACGARLVRSAAMKTGDlAALVDDLVARETTIVDLPTAVWQLLCADGDAIDAIgrSRLRQ 694
Cdd:cd05919   136 VFSSAKMFFGYGLgNSLWFPLAVGASAVLNPGWPTAE-RVLATLARFRPTVLYGVPTFYANLLDSCAGSPDAL--RSLRL 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  695 IVIGGEAIRCSAVDKWLESAasqGISLLSSYGPTEatVVATFLPIVCDQTTMD-------GALLRL----GRPILPNTVf 763
Cdd:cd05919   213 CVSAGEALPRGLGERWMEHF---GGPILDGIGATE--VGHIFLSNRPGAWRLGstgrpvpGYEIRLvdeeGHTIPPGEE- 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  764 lafGEVVIVGDLVADGYLgidgdgfgtvTAADGSRRRA----FATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVT 839
Cdd:cd05919   287 ---GDLLVRGPSAAVGYW----------NNPEKSRATFnggwYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVE 353

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489495878  840 RRIAEDPAVSDVAV----ELHSGS---LGVWFKSQRTREGEQDAAAATRIRLVLVSLGVSSFFVVgVPNIPRKPNGKI 910
Cdd:cd05919   354 SLIIQHPAVAEAAVvavpESTGLSrltAFVVLKSPAAPQESLARDIHRHLLERLSAHKVPRRIAF-VDELPRTATGKL 430
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
 1626-1971 8.01e-15

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 80.25  E-value: 8.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1626 PMPAAV-NLAYILYTSGTTGEPKGVGITHRNVTRLFASLPARLS-----AAQVWSQC-----------HSYGFDASAWEI 1688
Cdd:PRK12492  201 PVPVGLdDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSqlgpdGQPLMKEGqevmiaplplyHIYAFTANCMCM 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1689 wgaLLGGGRLVIVpesvaASPNDFHGLLVA----EHVSVLTQTPAAVAMLPTQGLESV---ALVV---AGEACPAALVDR 1758
Cdd:PRK12492  281 ---MVSGNHNVLI-----TNPRDIPGFIKElgkwRFSALLGLNTLFVALMDHPGFKDLdfsALKLtnsGGTALVKATAER 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1759 WA--PGRVMLNAYGPTETTICAAiSAPLRPGSGMPPIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAG 1836
Cdd:PRK12492  353 WEqlTGCTIVEGYGLTETSPVAS-TNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPE 431

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1837 LTASRFVAcpfggsgARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRI---ELGEVATALAELAGVgqAVVIAREDRP 1913
Cdd:PRK12492  432 ATAEALDA-------EGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVypnEIEDVVMAHPKVANC--AAIGVPDERS 502

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489495878 1914 GDK-RLVGYATEiapGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:PRK12492  503 GEAvKLFVVARD---PGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
PRK08162 PRK08162
acyl-CoA synthetase; Validated
 1499-1966 8.36e-15

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 79.99  E-value: 8.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1499 AAQVAriPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPP 1578
Cdd:PRK08162   27 AAEVY--PDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1579 PRVAFML--GDAVPV------AAVTTAGLRsRLAGHDLPIIDVVDAlaAYPGTPP-------------------PMPA-- 1629
Cdd:PRK08162  105 ASIAFMLrhGEAKVLivdtefAEVAREALA-LLPGPKPLVIDVDDP--EYPGGRFigaldyeaflasgdpdfawTLPAde 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1630 --AVNLAYilyTSGTTGEPKGVGITHR--------NVtrLFASLPARlsAAQVWS----QCHSYGFdasAWEIwgALLGG 1695
Cdd:PRK08162  182 wdAIALNY---TSGTTGNPKGVVYHHRgaylnalsNI--LAWGMPKH--PVYLWTlpmfHCNGWCF---PWTV--AARAG 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1696 grlVIV------PESVaaspndfHGLLVAEHVSVLTQTPAAVAML------PTQGLE-SVALVVAGEACPAALVDRWAP- 1761
Cdd:PRK08162  250 ---TNVclrkvdPKLI-------FDLIREHGVTHYCGAPIVLSALinapaeWRAGIDhPVHAMVAGAAPPAAVIAKMEEi 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1762 GRVMLNAYGPTET----TICAAisaplRPGSGMPPI----------GVP-VSGAALFVLDS-WLRPVPAG--VAGELYIA 1823
Cdd:PRK08162  320 GFDLTHVYGLTETygpaTVCAW-----QPEWDALPLderaqlkarqGVRyPLQEGVTVLDPdTMQPVPADgeTIGEIMFR 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1824 GAGVGVGYWRRAGLTASRFVacpfGGsgarMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQ 1903
Cdd:PRK08162  395 GNIVMKGYLKNPKATEEAFA----GG----WFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLV 466

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489495878 1904 AVVIARED-RPGDkrlVGYA-TEIAPGA-VDPAGLRAQLAQRLPGYLVPAAvVVIDALPLTVNGKL 1966
Cdd:PRK08162  467 AAVVAKPDpKWGE---VPCAfVELKDGAsATEEEIIAHCREHLAGFKVPKA-VVFGELPKTSTGKI 528
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
 1636-1967 8.48e-15

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 78.08  E-value: 8.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1636 ILYTSGTTGEPKGVGITHRNVtrlfasLPARLSAAQVWSQCHSygfDASA-----WEIWGALLG------GGRLVIV--- 1701
Cdd:cd17637     5 IIHTAAVAGRPRGAVLSHGNL------IAANLQLIHAMGLTEA---DVYLnmlplFHIAGLNLAlatfhaGGANVVMekf 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1702 -PESVAAspndfhgLLVAEHVSVLTQTPAAVAM-LPTQGLESVAL----VVAGEACPAAlVDRW---APGRvMLNAYGPT 1772
Cdd:cd17637    76 dPAEALE-------LIEEEKVTLMGSFPPILSNlLDAAEKSGVDLsslrHVLGLDAPET-IQRFeetTGAT-FWSLYGQT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1773 ETTICAAIS-APLRPGSGmppiGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVacpfGGsg 1851
Cdd:cd17637   147 ETSGLVTLSpYRERPGSA----GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFR----NG-- 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1852 arMYRTGDLVCWRADGQLEFLGRT--DDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDrPGDKRLVGYATEIAPGA 1929
Cdd:cd17637   217 --WHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPD-PKWGEGIKAVCVLKPGA 293

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 489495878 1930 -VDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLD 1967
Cdd:cd17637   294 tLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSID 332
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
 575-911 9.38e-15

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 79.19  E-value: 9.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  575 AYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLT-SDISVEEIFGGAACGARLVRSAAMKTGDLA 653
Cdd:cd17631   101 ALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFhIGGLGVFTLPTLLRGGTVVILRKFDPETVL 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  654 ALVDDlvARETTIVDLPTaVWQLLCADGDAiDAIGRSRLRQIVIGGEAIRCSAVDKWLEsaasQGISLLSSYGPTEATVV 733
Cdd:cd17631   181 DLIER--HRVTSFFLVPT-MIQALLQHPRF-ATTDLSSLRAVIYGGAPMPERLLRALQA----RGVKFVQGYGMTETSPG 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  734 ATFLPIVCDQTTMDGAllrlGRPIL---------------PNTVflafGEVVIVGDLVADGYLGIDgdgfgtVTAADGSR 798
Cdd:cd17631   253 VTFLSPEDHRRKLGSA----GRPVFfvevrivdpdgrevpPGEV----GEIVVRGPHVMAGYWNRP------EATAAAFR 318

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  799 RRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV----ELHSGSLGVWFKSQR--TREG 872
Cdd:cd17631   319 DGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVigvpDEKWGEAVVAVVVPRpgAELD 398

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 489495878  873 EQDAAAATRIRLVLVSLGVSSFFvvgVPNIPRKPNGKID 911
Cdd:cd17631   399 EDELIAHCRERLARYKIPKSVEF---VDALPRNATGKIL 434
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1632-1971 1.10e-14

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 78.29  E-value: 1.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1632 NLAYILYTSGTTGEPKGVGITHRNVTrlfaslparlsaAQVWSQCHSYGFD---------------ASAWEIWGALLGGG 1696
Cdd:cd05944     3 DVAAYFHTGGTTGTPKLAQHTHSNEV------------YNAWMLALNSLFDpddvllcglplfhvnGSVVTLLTPLASGA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1697 RLVIVPESVAASPN---DFHGLLVAEHVSVLTQTPAAVAML---PTQG-LESVALVVAGEA-CPAALVDRW--APGRVML 1766
Cdd:cd05944    71 HVVLAGPAGYRNPGlfdNFWKLVERYRITSLSTVPTVYAALlqvPVNAdISSLRFAMSGAApLPVELRARFedATGLPVV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1767 NAYGPTETTICAAIS---APLRPGS-GMPpigVPVSGAALFVLD---SWLRPVPAGVAGELYIAGAGVGVGYwrraglTA 1839
Cdd:cd05944   151 EGYGLTEATCLVAVNppdGPKRPGSvGLR---LPYARVRIKVLDgvgRLLRDCAPDEVGEICVAGPGVFGGY------LY 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1840 SRFVACPFGGSGarMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLV 1919
Cdd:cd05944   222 TEGNKNAFVADG--WLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPV 299

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 489495878 1920 GYaTEIAPGA-VDPAGLRAQLAQRLPGY-LVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:cd05944   300 AY-VQLKPGAvVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 1776-2063 1.29e-14

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 77.10  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1776 ICAAISAPLRPGSGMPPIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPF--GGSGAR 1853
Cdd:COG3433     1 IAIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVpyPAQPGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1854 MYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRpGDKRLVGYATEIAPGAVDPA 1933
Cdd:COG3433    81 QADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGA-GVGLLLIVGAVAALDGLAAA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1934 GLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRALPAPEYGDTNGYRAPAGPVEKT-----VAGIFARVLGL--ERV 2006
Cdd:COG3433   160 AALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALETAlteeeLRADVAELLGVdpEEI 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489495878 2007 GVDDSFFELGGDSLAAMRVIAAINTTlNADLPVRALLHASSTRGLSQLLGRDARPTS 2063
Cdd:COG3433   240 DPDDNLFDLGLDSIRLMQLVERWRKA-GLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
 1500-1966 2.58e-14

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 78.51  E-value: 2.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1500 AQVAriPEAEAVCCGDA--SMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANP 1577
Cdd:PRK13390    7 AQIA--PDRPAVIVAETgeQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1578 PPRVAFMLGDAVPVAAVTTAGLRSRLA--GHDLPI-------ID-VVDALAAYPGTPPPMPAAVNLAYILYTSGTTGEPK 1647
Cdd:PRK13390   85 APEADYIVGDSGARVLVASAALDGLAAkvGADLPLrlsfggeIDgFGSFEAALAGAGPRLTEQPCGAVMLYSSGTTGFPK 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1648 GV------------------------GITHRNVtrLFASLPARLSAAQVW-SQCHSYgfdasaweiwgallgGGRLVIVP 1702
Cdd:PRK13390  165 GIqpdlpgrdvdapgdpivaiarafyDISESDI--YYSSAPIYHAAPLRWcSMVHAL---------------GGTVVLAK 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1703 ESVAAspnDFHGLLVAEHVSVLTQTPAA-VAMLPTQG-------LESV-ALVVAGEACPA----ALVDRWAPgrVMLNAY 1769
Cdd:PRK13390  228 RFDAQ---ATLGHVERYRITVTQMVPTMfVRLLKLDAdvrtrydVSSLrAVIHAAAPCPVdvkhAMIDWLGP--IVYEYY 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1770 GPTETTICAAISAP---LRPGSgmppIGVPVSGaALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTA-SRFVAC 1845
Cdd:PRK13390  303 SSTEAHGMTFIDSPdwlAHPGS----VGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAaAQHPAH 377

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1846 PFGGSgarmyrTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDrPGDKRLVGYATEI 1925
Cdd:PRK13390  378 PFWTT------VGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPD-PEMGEQVKAVIQL 450

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 489495878 1926 APGaVDPAGLRAQ-----LAQRLPGYLVPAAVVVIDALPLTVNGKL 1966
Cdd:PRK13390  451 VEG-IRGSDELARelidyTRSRIAHYKAPRSVEFVDELPRTPTGKL 495
prpE PRK10524
propionyl-CoA synthetase; Provisional
 1635-1973 2.95e-14

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 78.84  E-value: 2.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1635 YILYTSGTTGEPKGVgitHRNV----TRLFASLP---------ARLSAAQV-WSQCHSYgfdasawEIWGALLGGgRLVI 1700
Cdd:PRK10524  237 YILYTSGTTGKPKGV---QRDTggyaVALATSMDtifggkageTFFCASDIgWVVGHSY-------IVYAPLLAG-MATI 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1701 VPESVAASPNDfhGL---LVAEH-VSVLTQTPAAVAMLPTQG--------LESV-ALVVAGEAC--PAAlvdRW---APG 1762
Cdd:PRK10524  306 MYEGLPTRPDA--GIwwrIVEKYkVNRMFSAPTAIRVLKKQDpallrkhdLSSLrALFLAGEPLdePTA---SWiseALG 380

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1763 RVMLNAYGPTET-----TICAAISA-PLRPGSgmpPiGVPVSGAALFVLDSWL-RPVPAGVAGELYIAGA---GVGVGYW 1832
Cdd:PRK10524  381 VPVIDNYWQTETgwpilAIARGVEDrPTRLGS---P-GVPMYGYNVKLLNEVTgEPCGPNEKGVLVIEGPlppGCMQTVW 456

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1833 RraglTASRFVACPFGGSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDR 1912
Cdd:PRK10524  457 G----DDDRFVKTYWSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDA 532

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489495878 1913 PGDKRLVGYATEIAPGAVDPAGLRAQL--------AQRLPGYLVPAAVVVIDALPLTVNGKLDHRALPA 1973
Cdd:PRK10524  533 LKGQVAVAFVVPKDSDSLADREARLALekeimalvDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQA 601
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
 1519-1912 6.52e-14

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 77.01  E-value: 6.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1519 TYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAylpidpanppprvafmlgDAVPVAAVTTAG 1598
Cdd:cd17640     7 TYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAV------------------DVVRGSDSSVEE 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1599 LRSRLAgHDLPIIDVVDAlaaypgtpppmpAAVNLAYILYTSGTTGEPKGVGITHRN----VTRLFASLPAR-----LSA 1669
Cdd:cd17640    69 LLYILN-HSESVALVVEN------------DSDDLATIIYTSGTTGNPKGVMLTHANllhqIRSLSDIVPPQpgdrfLSI 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1670 AQVWsqcHSYgfdASAWEIWGALLGGGRLV------------IVPESVAASPNDFHGLLVAEHVSVLTQTPA--AVAMLP 1735
Cdd:cd17640   136 LPIW---HSY---ERSAEYFIFACGCSQAYtsirtlkddlkrVKPHYIVSVPRLWESLYSGIQKQVSKSSPIkqFLFLFF 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1736 TQGLESVALVVAGEACPAAlVDRW--APGRVMLNAYGPTETTICAAISAPLRPGSGmpPIGVPVSGAALFVLDSWLR-PV 1812
Cdd:cd17640   210 LSGGIFKFGISGGGALPPH-VDTFfeAIGIEVLNGYGLTETSPVVSARRLKCNVRG--SVGRPLPGTEIKIVDPEGNvVL 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1813 PAGVAGELYIAGAGVGVGYWRRAGLTASrfvacPFGGSGarMYRTGDLVCWRADGQLEFLGRTDDQVKIR-GYRIELGEV 1891
Cdd:cd17640   287 PPGEKGIVWVRGPQVMKGYYKNPEATSK-----VLDSDG--WFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPI 359

                         410       420
                  ....*....|....*....|.
gi 489495878 1892 ATALAELAGVGQAVVIAREDR 1912
Cdd:cd17640   360 EEALMRSPFIEQIMVVGQDQK 380
PRK05857 PRK05857
fatty acid--CoA ligase;
1491-1973 6.53e-14

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 77.36  E-value: 6.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1491 PVSIPQMLAAQVARIPEAEAV--CCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAA 1568
Cdd:PRK05857   13 PSTVLDRVFEQARQQPEAIALrrCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1569 YLPIDPANPPPRVAFMLGDAVPVAAVTTAGLR---SRLAG--HDLPIIDVVDALAA----------YPGTPPPMPAAVNL 1633
Cdd:PRK05857   93 AVMADGNLPIAAIERFCQITDPAAALVAPGSKmasSAVPEalHSIPVIAVDIAAVTresehsldaaSLAGNADQGSEDPL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1634 AYIlYTSGTTGEPKGVGITHRNvtrlFASLPARLSAAQV-W-------------SQCHSYGFdasaWEIWGALLGGGRLV 1699
Cdd:PRK05857  173 AMI-FTSGTTGEPKAVLLANRT----FFAVPDILQKEGLnWvtwvvgettysplPATHIGGL----WWILTCLMHGGLCV 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1700 IVPESVAAspndFHGLLVAEHVSVLTQTPAAVAMLPTQgLESVALVV--------AGEACPAALVdRW--APGRVMLNAY 1769
Cdd:PRK05857  244 TGGENTTS----LLEILTTNAVATTCLVPTLLSKLVSE-LKSANATVpslrlvgyGGSRAIAADV-RFieATGVRTAQVY 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1770 GPTETTiCAAISAPLRPGS---------GMPPIGV-----PVSGAALFVLDSwlrpVPAGVAGELYIAGAGVGVGYWRRA 1835
Cdd:PRK05857  318 GLSETG-CTALCLPTDDGSivkieagavGRPYPGVdvylaATDGIGPTAPGA----GPSASFGTLWIKSPANMLGYWNNP 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1836 GLTASRFVacpfggsgARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDrPGD 1915
Cdd:PRK05857  393 ERTAEVLI--------DGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPD-EEF 463

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489495878 1916 KRLVGYATeIAPGAVDPAGLRAqLAQRLPGYL--------VPAAVVVIDALPLTVNGKLDHRALPA 1973
Cdd:PRK05857  464 GALVGLAV-VASAELDESAARA-LKHTIAARFrresepmaRPSTIVIVTDIPRTQSGKVMRASLAA 527
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
 1615-1979 7.58e-14

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 77.22  E-value: 7.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1615 DALAAYPGTPPPMP-AAVNLAYILYTSGTTGEPKGV-----------GITHRNV-----TRLFASlparlsAAQV-WSQC 1676
Cdd:cd05966   214 DLMAKQSPECEPEWmDSEDPLFILYTSGSTGKPKGVvhttggyllyaATTFKYVfdyhpDDIYWC------TADIgWITG 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1677 HSYGfdasaweIWGALLGGGRLVIVpESVAASPN-DFHGLLVAEH-VSVLTQTPAAVAMLPTQG--------LESVAL-- 1744
Cdd:cd05966   288 HSYI-------VYGPLANGATTVMF-EGTPTYPDpGRYWDIVEKHkVTIFYTAPTAIRALMKFGdewvkkhdLSSLRVlg 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1745 ----------------VVAGEACPaaLVDRWapgrvmlnayGPTET-TIC---AAISAPLRPGSGMPPI-GVPVSgaalf 1803
Cdd:cd05966   360 svgepinpeawmwyyeVIGKERCP--IVDTW----------WQTETgGIMitpLPGATPLKPGSATRPFfGIEPA----- 422

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1804 VLDSWLRPVPAGVAGELYIAGAGVGV-------------GYWRragltasrfvacPFGGsgarMYRTGDlVCWR-ADGQL 1869
Cdd:cd05966   423 ILDEEGNEVEGEVEGYLVIKRPWPGMartiygdheryedTYFS------------KFPG----YYFTGD-GARRdEDGYY 485

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1870 EFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYAT---EIAPGAVDPAGLRAQLAQRLPGY 1946
Cdd:cd05966   486 WITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTlkdGEEPSDELRKELRKHVRKEIGPI 565

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 489495878 1947 LVPAAVVVIDALPLTVNGK-----LDHRALPAPEYGDT 1979
Cdd:cd05966   566 ATPDKIQFVPGLPKTRSGKimrriLRKIAAGEEELGDT 603
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
 1635-1971 8.45e-14

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 76.97  E-value: 8.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1635 YILYTSGTTGEPKGVgitHRNVtrlfaslpARLSAAQVWSQCHSYG-------FDAS--AWEI------WGALLGG---- 1695
Cdd:cd05967   234 YILYTSGTTGKPKGV---VRDN--------GGHAVALNWSMRNIYGikpgdvwWAASdvGWVVghsyivYGPLLHGattv 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1696 ---GRLVIVPEsvaasPNDFHGLlVAEH-VSVLTQTPAAVAML---PTQG-------LESV-ALVVAGEACPAALVDrWA 1760
Cdd:cd05967   303 lyeGKPVGTPD-----PGAFWRV-IEKYqVNALFTAPTAIRAIrkeDPDGkyikkydLSSLrTLFLAGERLDPPTLE-WA 375

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1761 P---GRVMLNAYGPTET-----TICAAI-SAPLRPGSGmppiGVPVSGAALFVLDSWLRPVPAGVAGELYIAGA---GVG 1828
Cdd:cd05967   376 EntlGVPVIDHWWQTETgwpitANPVGLePLPIKAGSP----GKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPlppGCL 451

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1829 VGYWRRAGltasRFVACPFGGSGArMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIA 1908
Cdd:cd05967   452 LTLWKNDE----RFKKLYLSKFPG-YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVG 526

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489495878 1909 REDRPGDKRLVGYATEIAPGAVDPA----GLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:cd05967   527 VRDELKGQVPLGLVVLKEGVKITAEelekELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTL 593
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
 567-853 8.98e-14

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 76.17  E-value: 8.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  567 DALLATKTAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLtsdISVEEIFGGAAC----GARLV 642
Cdd:cd05941    84 EPSLVLDPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPL---HHVHGLVNALLCplfaGASVE 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  643 rsaaMKTGDLAALVD--DLVARETTIVDLPT------AVWQLLCADGDAIDAIGRSRLRQIVIGGEAIRCSAVDKWlesA 714
Cdd:cd05941   161 ----FLPKFDPKEVAisRLMPSITVFMGVPTiytrllQYYEAHFTDPQFARAAAAERLRLMVSGSAALPVPTLEEW---E 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  715 ASQGISLLSSYGPTEATV--------------VATFLPIVCDQTTMDGAllrlGRPILPNTVflafGEVVIVGDLVADGY 780
Cdd:cd05941   234 AITGHTLLERYGMTEIGMalsnpldgerrpgtVGMPLPGVQARIVDEET----GEPLPRGEV----GEIQVRGPSVFKEY 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  781 L--------GIDGDGFgtvtaadgsrrraFATGDRVTVDAEGFPVFSGR-KDAVVKISGKRVDIAEVTRRIAEDPAVSDV 851
Cdd:cd05941   306 WnkpeatkeEFTDDGW-------------FKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSEC 372


                  ..
gi 489495878  852 AV 853
Cdd:cd05941   373 AV 374
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
 1594-1973 1.02e-13

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 76.60  E-value: 1.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1594 VTTAGLRSRLAGHDLPIIDVVDA-LAAYPG--------TPPPMPAAVNLAYILYTSGTTGEPKGVGITHRNVTRLFASLP 1664
Cdd:PRK13388  104 VTDAEHRPLLDGLDLPGVRVLDVdTPAYAElvaaagalTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALT 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1665 AR--LSAAQVWSQC----HSYGFDASaweiWGALLGGGRLVIVPESVAASpndfhGLL-------------VAEHVSVLT 1725
Cdd:PRK13388  184 ERfgLTRDDVCYVSmplfHSNAVMAG----WAPAVASGAAVALPAKFSAS-----GFLddvrrygatyfnyVGKPLAYIL 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1726 QTPAAvamlPTQGLESVALVVAGEACP---AALVDRWapGRVMLNAYGPTETticaAISAPLRPGSgmPP--IGVPVSGA 1800
Cdd:PRK13388  255 ATPER----PDDADNPLRVAFGNEASPrdiAEFSRRF--GCQVEDGYGSSEG----AVIVVREPGT--PPgsIGRGAPGV 322

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1801 ALFVLDSwLRPVPAGV-------------AGELY-IAGAGVGVGYWRRAGLTASRFVacpfGGsgarMYRTGDLVCWRAD 1866
Cdd:PRK13388  323 AIYNPET-LTECAVARfdahgallnadeaIGELVnTAGAGFFEGYYNNPEATAERMR----HG----MYWSGDLAYRDAD 393

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1867 GQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIARED-RPGDKrlVGYATEIAPGA-VDPAGLRAQL-AQR- 1942
Cdd:PRK13388  394 GWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDeRVGDQ--VMAALVLRDGAtFDPDAFAAFLaAQPd 471

                         410       420       430
                  ....*....|....*....|....*....|.
gi 489495878 1943 LPGYLVPAAVVVIDALPLTVNGKLDHRALPA 1973
Cdd:PRK13388  472 LGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
557-853 2.00e-13

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 75.91  E-value: 2.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  557 VDERVTQVTHDALlATktayIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLtsdisveeifggAA 636
Cdd:COG1022   173 LEARRAAVKPDDL-AT----IIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPL------------AH 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  637 CGARLVRSAAMKTG-------DLAALVDDL-------------------------VARETTI--------VDL------- 669
Cdd:COG1022   236 VFERTVSYYALAAGatvafaeSPDTLAEDLrevkptfmlavprvwekvyagiqakAEEAGGLkrklfrwaLAVgrryara 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  670 ------PTAVWQLLCADGDAI------DAIGrSRLRQIVIGGEAIRcSAVDKWLESAasqGISLLSSYGPTEATVVATFl 737
Cdd:COG1022   316 rlagksPSLLLRLKHALADKLvfsklrEALG-GRLRFAVSGGAALG-PELARFFRAL---GIPVLEGYGLTETSPVITV- 389

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  738 pivcdqtTMDGALLR--LGRPILPNTVFLAF-GEVVIVGDLVADGYLG--------IDGDGFgtvtaadgsrrraFATGD 806
Cdd:COG1022   390 -------NRPGDNRIgtVGPPLPGVEVKIAEdGEILVRGPNVMKGYYKnpeataeaFDADGW-------------LHTGD 449

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 489495878  807 RVTVDAEGFPVFSGRKDAVVKIS-GKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:COG1022   450 IGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVV 497
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
 568-853 4.28e-13

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 74.92  E-value: 4.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  568 ALLATKTAYIMPTSGTTGQPKLVRISHGSLAVF-CDAISRAYGWGAHDTVLqcapLTSDISVEE-----IFGGAACGARL 641
Cdd:cd17634   228 AMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYaATTMKYVFDYGPGDIYW----CTADVGWVTghsylLYGPLACGATT 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  642 VRSAAMKTGDLAALVDDLVARE--TTIVDLPTAVWQLLCADGDAIDAIGRSRLRQIVIGGEAI---------------RC 704
Cdd:cd17634   304 LLYEGVPNWPTPARMWQVVDKHgvNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPInpeayewywkkigkeKC 383

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  705 SAVDKWLESAASQG-ISLLSSYGPTEATvvATFLPIVCDQTTMdgaLLRLGRPILPNTVflafGEVVIvGDLVADGYLGI 783
Cdd:cd17634   384 PVVDTWWQTETGGFmITPLPGAIELKAG--SATRPVFGVQPAV---VDNEGHPQPGGTE----GNLVI-TDPWPGQTRTL 453

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  784 DGDGFGTVTAADGSRRRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:cd17634   454 FGDHERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAV 523
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 574-910 6.74e-13

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 73.53  E-value: 6.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  574 TAYIMPTSGTTGQPKLVRISHGSLAVFcdaISRAYGW---GAHDTVLQCAP------LTSDIsveeiFGGAACGARLVrs 644
Cdd:cd05972    83 PALIYFTSGTTGLPKGVLHTHSYPLGH---IPTAAYWlglRPDDIHWNIADpgwakgAWSSF-----FGPWLLGATVF-- 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  645 aaMKTGD--LAALVDDLVARE--TTIVDLPTAVWQLLCADGDAIDaigRSRLRQIVIGGEAIRCSAVDKWLESAasqGIS 720
Cdd:cd05972   153 --VYEGPrfDAERILELLERYgvTSFCGPPTAYRMLIKQDLSSYK---FSHLRLVVSAGEPLNPEVIEWWRAAT---GLP 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  721 LLSSYGPTEAT-VVATFLPIVCDQTTMdgallrlGRPILPNTVFL--AFGEVVIVGDlvaDGYLGIDGD------GFGTV 791
Cdd:cd05972   225 IRDGYGQTETGlTVGNFPDMPVKPGSM-------GRPTPGYDVAIidDDGRELPPGE---EGDIAIKLPppglflGYVGD 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  792 TAADGSRRRA--FATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAVELHS----GSLGVWFK 865
Cdd:cd05972   295 PEKTEASIRGdyYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPdpvrGEVVKAFV 374

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 489495878  866 SQRTREGEQDAAAATRIRLVLVSLG--VSSFFVVGVPNIPRKPNGKI 910
Cdd:cd05972   375 VLTSGYEPSEELAEELQGHVKKVLApyKYPREIEFVEELPKTISGKI 421
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
 573-853 2.21e-12

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 71.61  E-value: 2.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  573 KTAYIMPTSGTTGQPKLVRISHGSlaVFCDAISRAYGWGAH--DTVLQCAPL--TSDISVeeIFGGA--ACGARLVRSAa 646
Cdd:cd05912    78 DIATIMYTSGTTGKPKGVQQTFGN--HWWSAIGSALNLGLTedDNWLCALPLfhISGLSI--LMRSViyGMTVYLVDKF- 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  647 mktgDLAALVDDLVARETTIVDL-PTAVWQLLCADGDAIDaigrSRLRQIVIGGEAIRCSAvdkwLESAASQGISLLSSY 725
Cdd:cd05912   153 ----DAEQVLHLINSGKVTIISVvPTMLQRLLEILGEGYP----NNLRCILLGGGPAPKPL----LEQCKEKGIPVYQSY 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  726 GPTE-ATVVATFLPivcdqttmDGALLRL---GRPILPNTVFLA--------FGEVVIVGDLVADGYLGiDGDGFGTVTA 793
Cdd:cd05912   221 GMTEtCSQIVTLSP--------EDALNKIgsaGKPLFPVELKIEddgqppyeVGEILLKGPNVTKGYLN-RPDATEESFE 291

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489495878  794 ADgsrrrAFATGDRVTVDAEGFP-VFSGRKDAVvkIS-GKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:cd05912   292 NG-----WFKTGDIGYLDEEGFLyVLDRRSDLI--ISgGENIYPAEIEEVLLSHPAIKEAGV 346
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
 539-910 2.57e-12

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 72.34  E-value: 2.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  539 DVAATQLAVVGH-----DELRKVVDERVTQVTHDALlatktAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGA- 612
Cdd:PRK07768  119 LAAAPVLEEKGIrvltvADLLAADPIDPVETGEDDL-----ALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVe 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  613 HDTVLQCAPLTSDIS-VEEIFGGAACGARLVRSAAMKTGDLAALVDDLVAR-ETTIVDLPTAVWQLLC------ADGDAI 684
Cdd:PRK07768  194 TDVMVSWLPLFHDMGmVGFLTVPMYFGAELVKVTPMDFLRDPLLWAELISKyRGTMTAAPNFAYALLArrlrrqAKPGAF 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  685 DAigrSRLRQIVIGGEAIRCSAVDKWLESAASQGI---SLLSSYGPTEATVVATFLPIVCDQT--TMDGALL-------- 751
Cdd:PRK07768  274 DL---SSLRFALNGAEPIDPADVEDLLDAGARFGLrpeAILPAYGMAEATLAVSFSPCGAGLVvdEVDADLLaalrravp 350

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  752 ----------RLGRPILPNTVFL-----------AFGEVVIVGDLVADGYLgiDGDGFGTVTAADGsrrrAFATGDRVTV 810
Cdd:PRK07768  351 atkgntrrlaTLGPPLPGLEVRVvdedgqvlpprGVGVIELRGESVTPGYL--TMDGFIPAQDADG----WLDTGDLGYL 424

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  811 DAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAV---SDVAVELHSGSLGVWFKSQRTREGEQDAAAATRIRL--- 884
Cdd:PRK07768  425 TEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVrpgNAVAVRLDAGHSREGFAVAVESNAFEDPAEVRRIRHqva 504

                         410       420       430
                  ....*....|....*....|....*....|
gi 489495878  885 --VLVSLGVSSFFVVGVP--NIPRKPNGKI 910
Cdd:PRK07768  505 heVVAEVGVRPRNVVVLGpgSIPKTPSGKL 534
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 574-853 3.26e-12

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 71.76  E-value: 3.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  574 TAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLtsdisveeiFGGAACGARLVRSAAMKTGDLA 653
Cdd:PRK06187  169 AAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPM---------FHVHAWGLPYLALMAGAKQVIP 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  654 ALVD-----DLVARE--TTIVDLPTaVWQLLcadGDAIDAIGR--SRLRQIVIGGEAIRCSAVDKWLESAasqGISLLSS 724
Cdd:PRK06187  240 RRFDpenllDLIETErvTFFFAVPT-IWQML---LKAPRAYFVdfSSLRLVIYGGAALPPALLREFKEKF---GIDLVQG 312

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  725 YGPTEATVVATFLPIVcDQTTMDGALLRL-GRPIL--------PNTVFL-----AFGEVVIVGDLVADGYLGIDGDGfgt 790
Cdd:PRK06187  313 YGMTETSPVVSVLPPE-DQLPGQWTKRRSaGRPLPgvearivdDDGDELppdggEVGEIIVRGPWLMQGYWNRPEAT--- 388

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489495878  791 vtaadgsrRRAFA-----TGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:PRK06187  389 --------AETIDggwlhTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAV 448
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
 1512-1971 3.79e-12

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 71.64  E-value: 3.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1512 CCGDAS-MTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVP 1590
Cdd:PRK08008   31 SGGVVRrYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQA 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1591 VAAVTTAG---------------LRSRL-----AGHDLPIIDVVDALAAYPGT---PPPMpAAVNLAYILYTSGTTGEPK 1647
Cdd:PRK08008  111 SLLVTSAQfypmyrqiqqedatpLRHICltrvaLPADDGVSSFTQLKAQQPATlcyAPPL-STDDTAEILFTSGTTSRPK 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1648 GVGITHRNVtrLFA----SLPARLSAAQVWSQCH-SYGFDASAWEIWGALLGGGRLVIVpESVAASPndFHGlLVAEHVS 1722
Cdd:PRK08008  190 GVVITHYNL--RFAgyysAWQCALRDDDVYLTVMpAFHIDCQCTAAMAAFSAGATFVLL-EKYSARA--FWG-QVCKYRA 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1723 VLTQtpAAVAMLPTQGLESVA--------------LVVAgEACPAALVDRWapGRVMLNAYGPTEtTICAAISAplRPGS 1788
Cdd:PRK08008  264 TITE--CIPMMIRTLMVQPPSandrqhclrevmfyLNLS-DQEKDAFEERF--GVRLLTSYGMTE-TIVGIIGD--RPGD 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1789 G--MPPIGVPVSGAALFVLDSWLRPVPAGVAGELYIAG-AGVGV--GYWRRAGLTASRFVAcpfGGsgarMYRTGDLVCW 1863
Cdd:PRK08008  336 KrrWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvPGKTIfkEYYLDPKATAKVLEA---DG----WLHTGDTGYV 408

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1864 RADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATeIAPGA-VDPAGLRAQLAQR 1942
Cdd:PRK08008  409 DEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVV-LNEGEtLSEEEFFAFCEQN 487

                         490       500
                  ....*....|....*....|....*....
gi 489495878 1943 LPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:PRK08008  488 MAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
 1633-1956 5.87e-12

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 70.71  E-value: 5.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1633 LAYILYTSGTTGEPKGVGITHRNVT------------------RLFASLParlsaaqvwsQCHSYGFDAsawEI----WG 1690
Cdd:cd17639    90 LACIMYTSGSTGNPKGVMLTHGNLVagiaglgdrvpellgpddRYLAYLP----------LAHIFELAA---ENvclyRG 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1691 ALLGGGR-LVIVPESVAASpndfHGLLVAEHVSVLTQTPA-------AV-AMLPTQGLES-----------VALVVAGEA 1750
Cdd:cd17639   157 GTIGYGSpRTLTDKSKRGC----KGDLTEFKPTLMVGVPAiwdtirkGVlAKLNPMGGLKrtlfwtayqskLKALKEGPG 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1751 CPA------ALVDRWAPGRV------------------------MLNAYGPTETTICAAISAP--LRPGSgmppIGVPVS 1798
Cdd:cd17639   233 TPLldelvfKKVRAALGGRLrymlsggaplsadtqeflnivlcpVIQGYGLTETCAGGTVQDPgdLETGR----VGPPLP 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1799 GAALFVLD------SWLRPVPAGvagELYIAGAGVGVGYWRRAGLTASRFvacpfggSGARMYRTGDLVCWRADGQLEFL 1872
Cdd:cd17639   309 CCEIKLVDweeggySTDKPPPRG---EILIRGPNVFKGYYKNPEKTKEAF-------DGDGWFHTGDIGEFHPDGTLKII 378

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1873 GRTDDQVKIR-GYRIELGEVATALAELAGVGQAVVIAREDR--------PGDKRLVGYATE-IAPGAVDPAGL------- 1935
Cdd:cd17639   379 DRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYADPDKsypvaivvPNEKHLTKLAEKhGVINSEWEELCedkklqk 458

                         410       420
                  ....*....|....*....|....*...
gi 489495878 1936 -------RAQLAQRLPGYLVPAAVVVID 1956
Cdd:cd17639   459 avlkslaETARAAGLEKFEIPQGVVLLD 486
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
 1485-1943 7.08e-12

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 71.06  E-value: 7.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1485 TAPAPTPVSIPQMLAAQVARIPEAEAVCCGDAS-----MTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAM 1559
Cdd:PRK08180   32 EPLGDYPRRLTDRLVHWAQEAPDRVFLAERGADggwrrLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLA 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1560 VAVLKTGAAYLPIDPAN-----PPPRVAFMLG-------------------DAVPVAAVTTAGLRSRLAGHD-LPIidvv 1614
Cdd:PRK08180  112 LAAMYAGVPYAPVSPAYslvsqDFGKLRHVLElltpglvfaddgaafaralAAVVPADVEVVAVRGAVPGRAaTPF---- 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1615 DALAAYPGTPPPMPA--AVN---LAYILYTSGTTGEPKGVGITHR----NVTRLFASLPARLSAAQV------WSqcHSY 1679
Cdd:PRK08180  188 AALLATPPTAAVDAAhaAVGpdtIAKFLFTSGSTGLPKAVINTHRmlcaNQQMLAQTFPFLAEEPPVlvdwlpWN--HTF 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1680 GfdASAweIWG-ALLGGGRLVI-----VPESVAASPNDFHGLLVAEHVSVltqtPAAVAMLpTQGLES------------ 1741
Cdd:PRK08180  266 G--GNH--NLGiVLYNGGTLYIddgkpTPGGFDETLRNLREISPTVYFNV----PKGWEML-VPALERdaalrrrffsrl 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1742 VALVVAGEACPAALVDRW------APGR--VMLNAYGPTETTICAAISAPLRPGSGMppIGVPVSGAALfvldswlRPVP 1813
Cdd:PRK08180  337 KLLFYAGAALSQDVWDRLdrvaeaTCGEriRMMTGLGMTETAPSATFTTGPLSRAGN--IGLPAPGCEV-------KLVP 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1814 AGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFggsgarmYRTGDLVCWrADGQ-----LEFLGRTDDQVKI-RGYRIE 1887
Cdd:PRK08180  408 VGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY-------YRSGDAVRF-VDPAdpergLMFDGRIAEDFKLsSGTWVS 479

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489495878 1888 LGEV-ATALAELAGVGQAVVIAREDR-----------PGDKRLVGYATEIAPGAV-DPAGLRAQLAQRL 1943
Cdd:PRK08180  480 VGPLrARAVSAGAPLVQDVVITGHDRdeigllvfpnlDACRRLAGLLADASLAEVlAHPAVRAAFRERL 548
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
 580-853 8.36e-12

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 70.55  E-value: 8.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  580 TSGTTGQPKLVRISHGS--LAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARLVRSAAMKTGdlaALVD 657
Cdd:PRK06018  185 TSGTTGDPKGVLYSHRSnvLHALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAPSMGTKLVMPGAKLDG---ASVY 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  658 DLVARE--TTIVDLPTaVWQLLCADGDAIDAiGRSRLRQIVIGGEAIRCSAVDKWLEsaasQGISLLSSYGPTEATVVAT 735
Cdd:PRK06018  262 ELLDTEkvTFTAGVPT-VWLMLLQYMEKEGL-KLPHLKMVVCGGSAMPRSMIKAFED----MGVEVRHAWGMTEMSPLGT 335

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  736 F--LPIVCDQTTMDGAL---LRLGRPilPNTVFL---------------AFGEVVIVGDLVADGYLGIDGDgfgtVTAAD 795
Cdd:PRK06018  336 LaaLKPPFSKLPGDARLdvlQKQGYP--PFGVEMkitddagkelpwdgkTFGRLKVRGPAVAAAYYRVDGE----ILDDD 409

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 489495878  796 GsrrrAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:PRK06018  410 G----FFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAV 463
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
 575-853 8.56e-12

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 69.82  E-value: 8.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  575 AYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLtsdISVEEIFG----GAACGARLVRSAAMKTG 650
Cdd:cd05935    87 ALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPL---FHVTGFVGslntAVYVGGTYVLMARWDRE 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  651 DLAALVDDLvaRETTIVDLPTAVWQLLCADGdaIDAIGRSRLRQIVIGGEAIRCSAVDKWLESAasqGISLLSSYGPTEA 730
Cdd:cd05935   164 TALELIEKY--KVTFWTNIPTMLVDLLATPE--FKTRDLSSLKVLTGGGAPMPPAVAEKLLKLT---GLRFVEGYGLTET 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  731 TVVATFLP-----IVCDQTTMDGALLRL-----GRPILPNTVflafGEVVIVGDLVADGYLGIDGDGFGTVTAADGsrRR 800
Cdd:cd05935   237 MSQTHTNPplrpkLQCLGIP*FGVDARVidietGRELPPNEV----GEIVVRGPQIFKGYWNRPEETEESFIEIKG--RR 310

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 489495878  801 AFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:cd05935   311 FFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCV 363
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1516-1874 9.40e-12

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 70.18  E-value: 9.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1516 ASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAAVT 1595
Cdd:cd05910     1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1596 taglrsrlaghdlpiidvvdalaaypgtpppMPAAVNLAYILYTSGTTGEPKGVGITHRNVtrlfaslparlsAAQVWSQ 1675
Cdd:cd05910    81 -------------------------------IPKADEPAAILFTSGSTGTPKGVVYRHGTF------------AAQIDAL 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1676 CHSYGFDASAWEIWG----ALLGG--GRLVIVPE-----SVAASPNDFHGLLVAEHVSVLTQTPAAVAMLPTQG------ 1738
Cdd:cd05910   118 RQLYGIRPGEVDLATfplfALFGPalGLTSVIPDmdptrPARADPQKLVGAIRQYGVSIVFGSPALLERVARYCaqhgit 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1739 LESVALVV-AGEACPAALVDRW----APGRVMLNAYGPTETTICAAI-SAPLRPGSGMPP-------IGVPVSGAALFVL 1805
Cdd:cd05910   198 LPSLRRVLsAGAPVPIALAARLrkmlSDEAEILTPYGATEALPVSSIgSRELLATTTAATsggagtcVGRPIPGVRVRII 277

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489495878 1806 D-------SW--LRPVPAGVAGELYIAGAGVGVGYWRRAglTASRFVACPFGGSGARmYRTGDLVCWRADGQLEFLGR 1874
Cdd:cd05910   278 EiddepiaEWddTLELPRGEIGEITVTGPTVTPTYVNRP--VATALAKIDDNSEGFW-HRMGDLGYLDDEGRLWFCGR 352
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 551-853 1.04e-11

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 69.63  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  551 DELRKVVDERVTQvthdaLLATKTAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLT-SDISVE 629
Cdd:cd05934    65 DELAYIIDHSGAQ-----LVVVDPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFhINAQAV 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  630 EIFGGAACGARLVRSAAMKTGDLAALVDDLVARETTIVDLPTAVwqLLCADGDAIDAIGRSRlrqiviggeAIRCSAVDK 709
Cdd:cd05934   140 SVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSY--LLAQPPSPDDRAHRLR---------AAYGAPNPP 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  710 WLESAASQ--GISLLSSYGPTEaTVVATFLPIvcDQTTMDGALlrlGRPilpntvflAFG-EVVIVGD---LVADGYLG- 782
Cdd:cd05934   209 ELHEEFEErfGVRLLEGYGMTE-TIVGVIGPR--DEPRRPGSI---GRP--------APGyEVRIVDDdgqELPAGEPGe 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  783 -----IDGDGFGT----VTAADGSRRRA--FATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDV 851
Cdd:cd05934   275 lvirgLRGWGFFKgyynMPEATAEAMRNgwFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREA 354


                  ..
gi 489495878  852 AV 853
Cdd:cd05934   355 AV 356
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 1984-2055 1.53e-11

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 62.18  E-value: 1.53e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489495878 1984 APAGPVEKTVAGIFARVLGL--ERVGVDDSFF-ELGGDSLAAMRVIAAINTTLNADLPVRALLHASSTRGLSQLL 2055
Cdd:COG0236     1 MPREELEERLAEIIAEVLGVdpEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYL 75
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 1991-2047 1.83e-11

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 61.43  E-value: 1.83e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 489495878  1991 KTVAGIFARVLGL--ERVGVDDSFFELGGDSLAAMRVIAAINTTLNADLPVRALLHASS 2047
Cdd:pfam00550    1 ERLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPT 59
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
 1632-1967 2.30e-11

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 67.43  E-value: 2.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1632 NLAYILYTSGTTGEPKGVGITHR--------NVTRLFASLPARLSAAQVWSQCHS-YGfdasaweIWGALLGGGRLVIvp 1702
Cdd:cd17633     1 NPFYIGFTSGTTGLPKAYYRSERswiesfvcNEDLFNISGEDAILAPGPLSHSLFlYG-------AISALYLGGTFIG-- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1703 eSVAASPNDFHGLLVAEHVSVLTQTPAAV-AMLPTQGLES--VALVVAGEACPAAL---VDRWAPGRVMLNAYGPTETTI 1776
Cdd:cd17633    72 -QRKFNPKSWIRKINQYNATVIYLVPTMLqALARTLEPESkiKSIFSSGQKLFESTkkkLKNIFPKANLIEFYGTSELSF 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1777 CAAISaplrPGSGMPP--IGVPVSGaalfvLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFvacpfggsgarm 1854
Cdd:cd17633   151 ITYNF----NQESRPPnsVGRPFPN-----VEIEIRNADGGEIGKIFVKSEMVFSGYVRGGFSNPDGW------------ 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1855 YRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVgyATEIAPGAVDPAg 1934
Cdd:cd17633   210 MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAV--ALYSGDKLTYKQ- 286

                         330       340       350
                  ....*....|....*....|....*....|...
gi 489495878 1935 LRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLD 1967
Cdd:cd17633   287 LKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIA 319
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
 575-853 2.48e-11

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 68.88  E-value: 2.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  575 AYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLtsdISVEEIFGGA----ACGARLVRSAAMKTG 650
Cdd:cd05926   152 ALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPL---FHVHGLVASLlstlAAGGSVVLPPRFSAS 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  651 DLAALVDDLVARETTIVdlPTaVWQLLCADGDAIDAIGRSRLRqiviggeAIR-CSA---VDKWLESAASQGISLLSSYG 726
Cdd:cd05926   229 TFWPDVRDYNATWYTAV--PT-IHQILLNRPEPNPESPPPKLR-------FIRsCSAslpPAVLEALEATFGAPVLEAYG 298

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  727 PTEAT--VVATFLPIVCDQTTMDG--------ALLRLGRPILPNTVflafGEVVIVGDLVADGYLGIDgdgfgTVTAADG 796
Cdd:cd05926   299 MTEAAhqMTSNPLPPGPRKPGSVGkpvgvevrILDEDGEILPPGVV----GEICLRGPNVTRGYLNNP-----EANAEAA 369

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489495878  797 SRRRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:cd05926   370 FKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVA 426
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
 1506-1913 2.77e-11

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 68.36  E-value: 2.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1506 PEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFML 1585
Cdd:PRK09029   17 PQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEELL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1586 gdavpvaavTTAGLRSRLAGHDLPIIDVVDAL--AAYPGTPPPMPAAVNLAYILYTSGTTGEPKGVGITHRN-------V 1656
Cdd:PRK09029   97 ---------PSLTLDFALVLEGENTFSALTSLhlQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAhlasaegV 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1657 TRLFA---------SLPArlsaaqvwsqchsygFDASAWEI-WGALLGGGRLViVPESvaaspNDF-HGLLVAEHVS-VL 1724
Cdd:PRK09029  168 LSLMPftaqdswllSLPL---------------FHVSGQGIvWRWLYAGATLV-VRDK-----QPLeQALAGCTHASlVP 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1725 TQtpaaVAMLPTQGLESVAL---VVAGEACPAALVDR--------WApgrvmlnAYGPTE--TTICAaisaplRPGSGMP 1791
Cdd:PRK09029  227 TQ----LWRLLDNRSEPLSLkavLLGGAAIPVELTEQaeqqgircWC-------GYGLTEmaSTVCA------KRADGLA 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1792 PIGVPVSGAALFVldswlrpvpagVAGELYIAGAGVGVGYWRRAGLTasrfvacPF-GGSGarMYRTGDLVCWRaDGQLE 1870
Cdd:PRK09029  290 GVGSPLPGREVKL-----------VDGEIWLRGASLALGYWRQGQLV-------PLvNDEG--WFATRDRGEWQ-NGELT 348

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 489495878 1871 FLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIARED-----RP 1913
Cdd:PRK09029  349 ILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADaefgqRP 396
PLN02479 PLN02479
acetate-CoA ligase
 1638-1992 3.74e-11

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 68.33  E-value: 3.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1638 YTSGTTGEPKGVGITHRNvtrlfASLPArLSAAQVWS--------------QCHSYGFdasAWEIwGALLGGG---RLVI 1700
Cdd:PLN02479  202 YTSGTTASPKGVVLHHRG-----AYLMA-LSNALIWGmnegavylwtlpmfHCNGWCF---TWTL-AALCGTNiclRQVT 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1701 VPESVAASPNDFHGLLVAEHV--SVLTQTPAAVAMLPTQglESVALVVAGEACPAALVDRWAP-GRVMLNAYGPTET--- 1774
Cdd:PLN02479  272 AKAIYSAIANYGVTHFCAAPVvlNTIVNAPKSETILPLP--RVVHVMTAGAAPPPSVLFAMSEkGFRVTHTYGLSETygp 349

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1775 -TICA----------AISAPLRPGSGMPPIGVpvsgAALFVLDS-WLRPVPA--GVAGELYIAGAGVGVGYWRRAGLTAS 1840
Cdd:PLN02479  350 sTVCAwkpewdslppEEQARLNARQGVRYIGL----EGLDVVDTkTMKPVPAdgKTMGEIVMRGNMVMKGYLKNPKANEE 425

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1841 RFVacpfGGsgarMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVG 1920
Cdd:PLN02479  426 AFA----NG----WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCA 497

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1921 YATeIAPGA--VDPAGLRAQLAQ----RLPGYLVPAAvVVIDALPLTVNGKLDHRALpapeygdtngyRAPA---GPVEK 1991
Cdd:PLN02479  498 FVT-LKPGVdkSDEAALAEDIMKfcreRLPAYWVPKS-VVFGPLPKTATGKIQKHVL-----------RAKAkemGPVKK 564


                  .
gi 489495878 1992 T 1992
Cdd:PLN02479  565 S 565
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 1636-1976 5.33e-11

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 67.88  E-value: 5.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1636 ILYTSGTTGEPKGVGITHRNVTrLFASLPAR----LSAAQVWSQCHSYGFDASAW----EIWGAllggGRLVIVPESVAA 1707
Cdd:cd05928   179 IYFTSGTTGSPKMAEHSHSSLG-LGLKVNGRywldLTASDIMWNTSDTGWIKSAWsslfEPWIQ----GACVFVHHLPRF 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1708 SPNDFHGLLVAEHVSVLTQTPAAVAMLPTQGLESVAL------VVAGEACPAALVDRWA--PGRVMLNAYGPTETT-ICA 1778
Cdd:cd05928   254 DPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKFpslqhcVTGGEPLNPEVLEKWKaqTGLDIYEGYGQTETGlICA 333

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1779 AISA-PLRPGSgmppIGVPVSGAALFVLDSWLRPVPAGVAGELyiagaGVGVGYWRRAGLTaSRFVACPFGGSGAR---M 1854
Cdd:cd05928   334 NFKGmKIKPGS----MGKASPPYDVQIIDDNGNVLPPGTEGDI-----GIRVKPIRPFGLF-SGYVDNPEKTAATIrgdF 403

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1855 YRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDrPGDKRLVGYATEIAPG--AVDP 1932
Cdd:cd05928   404 YLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPD-PIRGEVVKAFVVLAPQflSHDP 482

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 489495878 1933 AGLRAQLAQRLPG----YLVPAAVVVIDALPLTVNGKLDHRALPAPEY 1976
Cdd:cd05928   483 EQLTKELQQHVKSvtapYKYPRKVEFVQELPKTVTGKIQRNELRDKEW 530
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
 1519-1966 7.24e-11

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 67.42  E-value: 7.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1519 TYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDA---------- 1588
Cdd:PRK07008   41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAedryvlfdlt 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1589 -VPVAAVTTAGL-----------RSRLAGHDLPIIDVVDALAAYPGTPPPMPAAVNLA-YILYTSGTTGEPKGVGITHRN 1655
Cdd:PRK07008  121 fLPLVDALAPQCpnvkgwvamtdAAHLPAGSTPLLCYETLVGAQDGDYDWPRFDENQAsSLCYTSGTTGNPKGALYSHRS 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1656 vTRLFA---SLP------ARLSAAQVWSQCHsygfdASAWEI-WGALLGGGRLVIV-PESVAASpndFHGLLVAEHVSVL 1724
Cdd:PRK07008  201 -TVLHAygaALPdamglsARDAVLPVVPMFH-----VNAWGLpYSAPLTGAKLVLPgPDLDGKS---LYELIEAERVTFS 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1725 TQTPAAVAMLPTQ----GLESVAL---VVAGEACPAALVDRW--APGRVMLNAYGPTETTICAAISAPLRPGSGMPP--- 1792
Cdd:PRK07008  272 AGVPTVWLGLLNHmreaGLRFSTLrrtVIGGSACPPAMIRTFedEYGVEVIHAWGMTEMSPLGTLCKLKWKHSQLPLdeq 351

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1793 ------IGVPVSGAALFVLDSWLRPVP-AGVA-GELYIAGAGVGVGYWRRaglTASRFVACPFggsgarmyRTGDLVCWR 1864
Cdd:PRK07008  352 rkllekQGRVIYGVDMKIVGDDGRELPwDGKAfGDLQVRGPWVIDRYFRG---DASPLVDGWF--------PTGDVATID 420

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1865 ADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVgYATEIAPGA-VDPAGLRAQLAQRL 1943
Cdd:PRK07008  421 ADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPL-LVVVKRPGAeVTREELLAFYEGKV 499

                         490       500
                  ....*....|....*....|...
gi 489495878 1944 PGYLVPAAVVVIDALPLTVNGKL 1966
Cdd:PRK07008  500 AKWWIPDDVVFVDAIPHTATGKL 522
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
 1519-1965 7.77e-11

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 67.07  E-value: 7.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1519 TYRELDEASNRLAHRLAGC-GAGPGECVALLFERCAPAVVAMVAVLKTGAAylpidpanpPPRVAFMLGDAVPVAAVTTA 1597
Cdd:cd05937     7 TYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA---------PAFINYNLSGDPLIHCLKLS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1598 GLRsrlaghdLPIIDVVDalaaypgtpppmpaavnLAYILYTSGTTGEPKGVGITHRN--VTRLFASLPARLSAAQVWSQ 1675
Cdd:cd05937    78 GSR-------FVIVDPDD-----------------PAILIYTSGTTGLPKAAAISWRRtlVTSNLLSHDLNLKNGDRTYT 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1676 C----HSYGFDASAWEIwgaLLGGGRLVIV---------PESVAASPNDFhgLLVAEHVSVLTQTPAAvamlPTQGLESV 1742
Cdd:cd05937   134 CmplyHGTAAFLGACNC---LMSGGTLALSrkfsasqfwKDVRDSGATII--QYVGELCRYLLSTPPS----PYDRDHKV 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1743 ALVVAGEACPaalvDRWAPGRVMLNA------YGPTEtticaAISAPLRPGSGMPPIG-VPVSGAAL-------FVL--- 1805
Cdd:cd05937   205 RVAWGNGLRP----DIWERFRERFNVpeigefYAATE-----GVFALTNHNVGDFGAGaIGHHGLIRrwkfenqVVLvkm 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1806 -----DSWLRP-------VPAGVAGELYIA----GAGVGVGYWRRAGLTASRFVACPFGgSGARMYRTGDLVCWRADGQL 1869
Cdd:cd05937   276 dpetdDPIRDPktgfcvrAPVGEPGEMLGRvpfkNREAFQGYLHNEDATESKLVRDVFR-KGDIYFRTGDLLRQDADGRW 354

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1870 EFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIA-----REDRPGDKRLVGYATEIAPGAVDPAGLRAQLAQRLP 1944
Cdd:cd05937   355 YFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGvkvpgHDGRAGCAAITLEESSAVPTEFTKSLLASLARKNLP 434

                         490       500
                  ....*....|....*....|.
gi 489495878 1945 GYLVPAAVVVIDALPLTVNGK 1965
Cdd:cd05937   435 SYAVPLFLRLTEEVATTDNHK 455
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
1565-1971 8.00e-11

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 66.22  E-value: 8.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1565 TGAAYLPIdPANPPPRVAFMlgdavpvaavtTAGLRsrlAGHdlPIIDVVdalaaypgtpppmpaavnlAYILYTSGTTG 1644
Cdd:PRK07824    5 RAPALLPV-PAQDERRAALL-----------RDALR---VGE--PIDDDV-------------------ALVVATSGTTG 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1645 EPKGVGITHRNVTRLFASLPARLSAAQVWSqchsygFDASAWEIWG------ALLGGGRLVIVPESVAASPNDF----HG 1714
Cdd:PRK07824   49 TPKGAMLTAAALTASADATHDRLGGPGQWL------LALPAHHIAGlqvlvrSVIAGSEPVELDVSAGFDPTALpravAE 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1715 LLVAEHVSVLTQTPAAVAMLPTQGLESV----ALVVAGEACPAALVDRWAPGRVML-NAYGPTETTicaaisaplrpgSG 1789
Cdd:PRK07824  123 LGGGRRYTSLVPMQLAKALDDPAATAALaeldAVLVGGGPAPAPVLDAAAAAGINVvRTYGMSETS------------GG 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1790 MPPIGVPVSGAALFVLDswlrpvpagvaGELYIAGAGVGVGYwrRAGLTASrfvacPFGGSGarMYRTGDLVCWrADGQL 1869
Cdd:PRK07824  191 CVYDGVPLDGVRVRVED-----------GRIALGGPTLAKGY--RNPVDPD-----PFAEPG--WFRTDDLGAL-DDGVL 249

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1870 EFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIARED-RPGDKRLVGYATEIAPgAVDPAGLRAQLAQRLPGYLV 1948
Cdd:PRK07824  250 TVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDdRLGQRVVAAVVGDGGP-APTLEALRAHVARTLDRTAA 328

                         410       420
                  ....*....|....*....|...
gi 489495878 1949 PAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:PRK07824  329 PRELHVVDELPRRGIGKVDRRAL 351
PLN02503 PLN02503
fatty acyl-CoA reductase 2
 2111-2251 8.29e-11

fatty acyl-CoA reductase 2


Pssm-ID: 215279 [Multi-domain]  Cd Length: 605  Bit Score: 67.58  E-value: 8.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2111 LLTGATGFLGRYLVLELLRRLDVDGRLICLVRAESDEDARRRLEKtfDSGDPELLRHFKE--------LAADRLEVVAGD 2182
Cdd:PLN02503  123 LITGATGFLAKVLIEKILRTNPDVGKIYLLIKAKDKEAAIERLKN--EVIDAELFKCLQEthgksyqsFMLSKLVPVVGN 200

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489495878 2183 KSEPDLGLDQPMWRRLAETVDLIVDSAAMvNAFP--YHELFGPNVAGTAELIRIALT-TKLKPFTYVSTADV 2251
Cdd:PLN02503  201 VCESNLGLEPDLADEIAKEVDVIINSAAN-TTFDerYDVAIDINTRGPCHLMSFAKKcKKLKLFLQVSTAYV 271
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
 1515-1971 8.99e-11

Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 67.06  E-value: 8.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1515 DASMTYRELDEASNRLAHRLAGCGAGPGECVALLFErcapavvamvavlktgaaylpidpaNPPPRVAFMLGDAvpVAAV 1594
Cdd:cd05939     1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFME-------------------------NRLEFVALWLGLA--KIGV 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1595 TTAGLRSRLAGHDLP-----------IIDVVDALAAYPGTPPPMPAAVN----LAYIlYTSGTTGEPKGVGITHRNVTRL 1659
Cdd:cd05939    54 ETALINSNLRLESLLhcitvskakalIFNLLDPLLTQSSTEPPSQDDVNfrdkLFYI-YTSGTTGLPKAAVIVHSRYYRI 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1660 --FASLPARLSAAQVWSQC----HSYGfdasawEIWG---ALLGGGRLVIVPEsvaASPNDF------HGLLVAEHVSVL 1724
Cdd:cd05939   133 aaGAYYAFGMRPEDVVYDClplyHSAG------GIMGvgqALLHGSTVVIRKK---FSASNFwddcvkYNCTIVQYIGEI 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1725 TQTPAAVAMLPTQGLESVALVVAGEACPA---ALVDRWAPGRVMlNAYGPTE--------TTICAAISAPLRPGSGMPPI 1793
Cdd:cd05939   204 CRYLLAQPPSEEEQKHNVRLAVGNGLRPQiweQFVRRFGIPQIG-EFYGATEgnsslvniDNHVGACGFNSRILPSVYPI 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1794 GV----PVSGAALFVLDSWLRPVPAGVAGELyiagagVGV-----------GYWRRaGLTASRFVACPFgGSGARMYRTG 1858
Cdd:cd05939   283 RLikvdEDTGELIRDSDGLCIPCQPGEPGLL------VGKiiqndplrrfdGYVNE-GATNKKIARDVF-KKGDSAFLSG 354

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1859 DLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREdRPGDKRLVGYATEIAP-GAVDPAGLRA 1937
Cdd:cd05939   355 DVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVE-VPGVEGRAGMAAIVDPeRKVDLDRFSA 433

                         490       500       510
                  ....*....|....*....|....*....|....
gi 489495878 1938 QLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:cd05939   434 VLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDL 467
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
 1606-1965 1.28e-10

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 66.91  E-value: 1.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1606 HDLPIIDVV----DALAAYPGTPP---PMPAAVNLaYILYTSGTTGEPKGvgITHRNVTRLFASLPARLSAAQVWSQCHS 1678
Cdd:cd05943   218 PDLSKIAKAltleDFLATGAAGELefePLPFDHPL-YILYSSGTTGLPKC--IVHGAGGTLLQHLKEHILHCDLRPGDRL 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1679 YGFDASAWEIW----GALLGGGRLVIVPES-VAASPNDFHGLLVAEHVSVLTQTPAAVAMLPTQGLESV---------AL 1744
Cdd:cd05943   295 FYYTTCGWMMWnwlvSGLAVGATIVLYDGSpFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAethdlsslrTI 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1745 VVAGEACPA---ALVDRWAPGRVMLNAYGpTETTICAA-----ISAPLRPGsgmpPIGVPVSGAALFVLDSWLRPVPaGV 1816
Cdd:cd05943   375 LSTGSPLKPesfDYVYDHIKPDVLLASIS-GGTDIISCfvggnPLLPVYRG----EIQCRGLGMAVEAFDEEGKPVW-GE 448

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1817 AGELYIAGA--GVGVGYWRRAGltASRFVACPFggsgAR---MYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEV 1891
Cdd:cd05943   449 KGELVCTKPfpSMPVGFWNDPD--GSRYRAAYF----AKypgVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEI 522

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489495878 1892 ATALAELAGVGQAVVIAREDRPGDKRLVGYaTEIAPGAVDPAGLRAQLAQRLPGYL----VPAAVVVIDALPLTVNGK 1965
Cdd:cd05943   523 YRVVEKIPEVEDSLVVGQEWKDGDERVILF-VKLREGVELDDELRKRIRSTIRSALsprhVPAKIIAVPDIPRTLSGK 599
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
 473-910 1.67e-10

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 65.86  E-value: 1.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  473 AWLVQRGAAPGDVLVFTDDDTDKTIDLLIACHLAGcgysvcdtadeiSVRTNAITEHGDGILVTVVDVAATQLAVVghde 552
Cdd:cd05903    16 AGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIG------------AVTNPILPFFREHELAFILRRAKAKVFVV---- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  553 lrkvvDERVTQVTHDALLAtKTAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISveeiF 632
Cdd:cd05903    80 -----PERFRQFDPAAMPD-AVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTG----F 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  633 GGAACGARLVRSAA--MKTGDLAALVDDLVARETTIVDLPTAVWQLLCadgDAIDAIGR--SRLRQIVIGGEAIRCSAVD 708
Cdd:cd05903   150 VYGFTLPLLLGAPVvlQDIWDPDKALALMREHGVTFMMGATPFLTDLL---NAVEEAGEplSRLRTFVCGGATVPRSLAR 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  709 kwlESAASQGISLLSSYGPTEATVVATFLP-------IVCDQTTMDGALLRLGRPILPNTVFLAFGEVVIVGDLVADGYL 781
Cdd:cd05903   227 ---RAAELLGAKVCSAYGSTECPGAVTSITpapedrrLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYL 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  782 GiDGDgfgtvTAADGSRRRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAVelhsgslg 861
Cdd:cd05903   304 D-RPD-----LTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAV-------- 369

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489495878  862 VWFKSQRTreGEQDAA-AATR---------IRLVLVSLGVSSFF----VVGVPNIPRKPNGKI 910
Cdd:cd05903   370 VALPDERL--GERACAvVVTKsgalltfdeLVAYLDRQGVAKQYwperLVHVDDLPRTPSGKV 430
PLN02574 PLN02574
4-coumarate--CoA ligase-like
 1624-1971 1.68e-10

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 66.40  E-value: 1.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1624 PPPMPAAVNLAYILYTSGTTGEPKGVGITHRNV-------TRLFASLPARLSAAQVW----SQCHSYGFDASAWeiwgAL 1692
Cdd:PLN02574  191 PKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLiamvelfVRFEASQYEYPGSDNVYlaalPMFHIYGLSLFVV----GL 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1693 LGGGRLVIVPESVAASP-----NDF---HGLLVAEHVSVLTQTPAAVAMLPtqgLESVALVVAGeACPAA--LVDRWA-- 1760
Cdd:PLN02574  267 LSLGSTIVVMRRFDASDmvkviDRFkvtHFPVVPPILMALTKKAKGVCGEV---LKSLKQVSCG-AAPLSgkFIQDFVqt 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1761 -PGRVMLNAYGPTETTICAAISAPLRPGSGMPPIGVPVSGAALFVLDsWLRP--VPAGVAGELYIAGAGVGVGYWRRAGL 1837
Cdd:PLN02574  343 lPHVDFIQGYGMTESTAVGTRGFNTEKLSKYSSVGLLAPNMQAKVVD-WSTGclLPPGNCGELWIQGPGVMKGYLNNPKA 421

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1838 TASRFVACPFggsgarmYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKR 1917
Cdd:PLN02574  422 TQSTIDKDGW-------LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEI 494

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 489495878 1918 LVGYATEIAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:PLN02574  495 PVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
 1519-1943 2.70e-10

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 65.53  E-value: 2.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1519 TYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANP----------------PPRVA 1582
Cdd:cd05921    27 TYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSlmsqdlaklkhlfellKPGLV 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1583 F-----MLGDAVpvAAVTTAGLRSRLAGHDLPIIDVV--DALAAYPGTP--PPMPAAV---NLAYILYTSGTTGEPKGVG 1650
Cdd:cd05921   107 FaqdaaPFARAL--AAIFPLGTPLVVSRNAVAGRGAIsfAELAATPPTAavDAAFAAVgpdTVAKFLFTSGSTGLPKAVI 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1651 ITHRNVTR----------LFASLPARLSAAQVWSqcHSYGFDAsaweIWGALL-GGGRLVI-----VPESVAASPNDFHG 1714
Cdd:cd05921   185 NTQRMLCAnqamleqtypFFGEEPPVLVDWLPWN--HTFGGNH----NFNLVLyNGGTLYIddgkpMPGGFEETLRNLRE 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1715 LLVAEHVSVltqtPAAVAMLpTQGLES------------VALVVAGEACPAALVDRWAP------GR--VMLNAYGPTET 1774
Cdd:cd05921   259 ISPTVYFNV----PAGWEML-VAALEKdealrrrffkrlKLMFYAGAGLSQDVWDRLQAlavatvGEriPMMAGLGATET 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1775 TICAAISAPLRPGSGMppIGVPVSGAALfvldswlRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFggsgarm 1854
Cdd:cd05921   334 APTATFTHWPTERSGL--IGLPAPGTEL-------KLVPSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGF------- 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1855 YRTGDLVCWRADGQ----LEFLGRTDDQVKIR-GYRIELGEVATAL-AELAGVGQAVVIAREDR-----------PGDKR 1917
Cdd:cd05921   398 YCLGDAAKLADPDDpakgLVFDGRVAEDFKLAsGTWVSVGPLRARAvAACAPLVHDAVVAGEDRaevgalvfpdlLACRR 477

                         490       500
                  ....*....|....*....|....*.
gi 489495878 1918 LVGYATEIAPGAVDPAGLRAQLAQRL 1943
Cdd:cd05921   478 LVGLQEASDAEVLRHAKVRAAFRDRL 503
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
 1514-1970 3.37e-10

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 65.53  E-value: 3.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1514 GDaSMTYRELDEASNRLAH-----------RLAGCGA------GPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPAN 1576
Cdd:PRK12476   48 GD-TVAYRYLDHSHSAAGCaveltwtqlgvRLRAVGArlqqvaGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPE 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1577 PP---PRVAFMLGDAVPVAAVTTAGLR-------SRLAGHDLPIIDVVDALAAYPG---TPPPMPAAvNLAYILYTSGTT 1643
Cdd:PRK12476  127 LPghaERLDTALRDAEPTVVLTTTAAAeavegflRNLPRLRRPRVIAIDAIPDSAGesfVPVELDTD-DVSHLQYTSGST 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1644 GEPKGVGITHRNV-TRLfasLPARLSAAQVWSQCHSYGF-----DASAWEI-WGALLGGGRLVIVPESVAASPNDFHGLL 1716
Cdd:PRK12476  206 RPPVGVEITHRAVgTNL---VQMILSIDLLDRNTHGVSWlplyhDMGLSMIgFPAVYGGHSTLMSPTAFVRRPQRWIKAL 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1717 VAE--HVSVLTQTP------AAVAMLPTQG----LESVALVVAGEACPAALVDRWA--------PGRVMLNAYGPTETTI 1776
Cdd:PRK12476  283 SEGsrTGRVVTAAPnfayewAAQRGLPAEGddidLSNVVLIIGSEPVSIDAVTTFNkafapyglPRTAFKPSYGIAEATL 362

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1777 CAAISAP-------------------LRPGSGMPPIGVPVSGA-------ALFVLDSWLRPVPAGVAGELYIAGAGVGVG 1830
Cdd:PRK12476  363 FVATIAPdaepsvvyldreqlgagraVRVAADAPNAVAHVSCGqvarsqwAVIVDPDTGAELPDGEVGEIWLHGDNIGRG 442

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1831 YWRRAGLTASRFVA-----CPFGG------SGARMYRTGDLVCWRaDGQLEFLGRTDDQVKIRGYRIELGEVATALAELA 1899
Cdd:PRK12476  443 YWGRPEETERTFGAklqsrLAEGShadgaaDDGTWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIEATVAEAS 521

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1900 GVGQAVVIAREDRPGD--KRLVGYAtEIAPGA--VDPA----GLRAQLAQRlpgYLVPAA---VVVIDALPLTVNGKLDH 1968
Cdd:PRK12476  522 PMVRRGYVTAFTVPAEdnERLVIVA-ERAAGTsrADPApaidAIRAAVSRR---HGLAVAdvrLVPAGAIPRTTSGKLAR 597


                  ..
gi 489495878 1969 RA 1970
Cdd:PRK12476  598 RA 599
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
 574-853 3.59e-10

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 64.89  E-value: 3.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  574 TAYIMPTSGTTGQPKLVRISHGSL---AVFCDAISRAYGWGaHDTVLQCAPLTsdisveEIFGGAACGARLVRSAA---- 646
Cdd:cd05936   127 VAVLQYTSGTTGVPKGAMLTHRNLvanALQIKAWLEDLLEG-DDVVLAALPLF------HVFGLTVALLLPLALGAtivl 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  647 MKTGDLAALVDDLVA-RETTIVDLPTAVWQLLCAdgDAIDAIGRSRLRQIVIGGEAIRCSAVDKWLESAasqGISLLSSY 725
Cdd:cd05936   200 IPRFRPIGVLKEIRKhRVTIFPGVPTMYIALLNA--PEFKKRDFSSLRLCISGGAPLPVEVAERFEELT---GVPIVEGY 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  726 GPTEATVVATFLPIvcDQTTMDGAllrLGRPIL--------PNTVFLA---FGEVVIVGDLVADGYLGIDGDgfgtvTAA 794
Cdd:cd05936   275 GLTETSPVVAVNPL--DGPRKPGS---IGIPLPgtevkivdDDGEELPpgeVGELWVRGPQVMKGYWNRPEE-----TAE 344

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489495878  795 ---DGsrrrAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:cd05936   345 afvDG----WLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAV 402
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
 573-833 3.64e-10

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 65.05  E-value: 3.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  573 KTAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTsdisveEIFGGAAC-------GARLV-RS 644
Cdd:cd05909   148 DPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFF------HSFGLTGClwlpllsGIKVVfHP 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  645 AAMKTGDLAALVDDlvARETTIVDLPTAVWQLLcadgDAIDAIGRSRLRQIVIGGEAIRCSAVDKWLESaasQGISLLSS 724
Cdd:cd05909   222 NPLDYKKIPELIYD--KKATILLGTPTFLRGYA----RAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEK---FGIRILEG 292

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  725 YGPTEATVVatflpIVCDQTTMDGALLRLGRPiLPNTVF----------LAFGE---VVIVGDLVADGYLGIDGdgfGTV 791
Cdd:cd05909   293 YGTTECSPV-----ISVNTPQSPNKEGTVGRP-LPGMEVkivsvetheeVPIGEgglLLVRGPNVMLGYLNEPE---LTS 363

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 489495878  792 TAAdgsRRRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRV 833
Cdd:cd05909   364 FAF---GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMV 402
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
 1519-1880 5.95e-10

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 64.41  E-value: 5.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1519 TYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFML----GDAVPVA-- 1592
Cdd:cd05932     8 TWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLehseSKALFVGkl 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1593 ---AVTTAGLRSRLAGHDLPIIDVV-------DALAAYP---GTPPPMPAavNLAYILYTSGTTGEPKGV---------- 1649
Cdd:cd05932    88 ddwKAMAPGVPEGLISISLPPPSAAncqyqwdDLIAQHPpleERPTRFPE--QLATLIYTSGTTGQPKGVmltfgsfawa 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1650 ---GITHRNVT---RLFASLPARLSAAQVWsqchsygfdasaweIWGALLGGGRLVIVPESV--------AASPNDFHG- 1714
Cdd:cd05932   166 aqaGIEHIGTEendRMLSYLPLAHVTERVF--------------VEGGSLYGGVLVAFAESLdtfvedvqRARPTLFFSv 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1715 --LLVAEHVSVLTQTPAAV----------------AMLPTQGLESVALVVAGEA-CPAALVDrW--APGRVMLNAYGPTE 1773
Cdd:cd05932   232 prLWTKFQQGVQDKIPQQKlnlllkipvvnslvkrKVLKGLGLDQCRLAGCGSApVPPALLE-WyrSLGLNILEAYGMTE 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1774 TTICAAISAPLRPGSGMppIGVPVSGAALFVLDSwlrpvpagvaGELYIAGAGVGVGYWRRAGLTASRFVACPFggsgar 1853
Cdd:cd05932   311 NFAYSHLNYPGRDKIGT--VGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADGF------ 372

                         410       420
                  ....*....|....*....|....*..
gi 489495878 1854 mYRTGDLVCWRADGQLEFLGRTDDQVK 1880
Cdd:cd05932   373 -LRTGDKGELDADGNLTITGRVKDIFK 398
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
 574-853 6.22e-10

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 64.30  E-value: 6.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  574 TAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPL--TSDISVEEIFggAACGArlvrsaAMKTGD 651
Cdd:cd17640    90 LATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIwhSYERSAEYFI--FACGC------SQAYTS 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  652 LAALVDDLV-ARETTIVDLPTaVWQLL-------CADGDAID------AIGRSRLRQIVIGGEAIrCSAVDKWLESAasq 717
Cdd:cd17640   162 IRTLKDDLKrVKPHYIVSVPR-LWESLysgiqkqVSKSSPIKqflflfFLSGGIFKFGISGGGAL-PPHVDTFFEAI--- 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  718 GISLLSSYGPTEATvvatflPIVCDQTTMDGALLRLGRPIlPNTVF----------LAFGE---VVIVGDLVADGYLG-- 782
Cdd:cd17640   237 GIEVLNGYGLTETS------PVVSARRLKCNVRGSVGRPL-PGTEIkivdpegnvvLPPGEkgiVWVRGPQVMKGYYKnp 309

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489495878  783 ------IDGDGFgtvtaadgsrrraFATGDRVTVDAEGFPVFSGR-KDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:cd17640   310 eatskvLDSDGW-------------FNTGDLGWLTCGGELVLTGRaKDTIVLSNGENVEPQPIEEALMRSPFIEQIMV 374
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
 1519-1970 1.01e-09

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 63.86  E-value: 1.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1519 TYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAA--YLPidpaNPPPR------------VAFM 1584
Cdd:PRK07768   31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASltMLH----QPTPRtdlavwaedtlrVIGM 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1585 LGDAVPVAAVTTAGLRSRLAGHDLPIIDVVDALAAYPGTPPPMPAAvNLAYILYTSGTTGEPKGVGITHRNvtrLFASLP 1664
Cdd:PRK07768  107 IGAKAVVVGEPFLAAAPVLEEKGIRVLTVADLLAADPIDPVETGED-DLALMQLTSGSTGSPKAVQITHGN---LYANAE 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1665 ARLSAAQV---------WSQC-HSYGfdasaweiwgaLLGGgrlVIVP-----ESVAASPNDFHG------LLVAEHVSV 1723
Cdd:PRK07768  183 AMFVAAEFdvetdvmvsWLPLfHDMG-----------MVGF---LTVPmyfgaELVKVTPMDFLRdpllwaELISKYRGT 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1724 LTQTPA-AVAML-------PTQG---LESVALVVAG-EACPAALVDRWA--------PGRVMLNAYGPTETTIcaAISAP 1783
Cdd:PRK07768  249 MTAAPNfAYALLarrlrrqAKPGafdLSSLRFALNGaEPIDPADVEDLLdagarfglRPEAILPAYGMAEATL--AVSFS 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1784 lRPGSGM---------------------------PPIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYwrrag 1836
Cdd:PRK07768  327 -PCGAGLvvdevdadllaalrravpatkgntrrlATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY----- 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1837 LTASRFVAC--PFGgsgarMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGV--GQAVVIaREDR 1912
Cdd:PRK07768  401 LTMDGFIPAqdADG-----WLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVrpGNAVAV-RLDA 474

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489495878 1913 PGDKRLVGYATEIApGAVDPAG---LRAQLAQRLPGYL--VPAAVVVIDA--LPLTVNGKLDHRA 1970
Cdd:PRK07768  475 GHSREGFAVAVESN-AFEDPAEvrrIRHQVAHEVVAEVgvRPRNVVVLGPgsIPKTPSGKLRRAN 538
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
 1489-1975 1.24e-09

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 63.51  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1489 PTPVSIPQMlaaqVARIPEAEAVCCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAA 1568
Cdd:PRK06710   25 PLHKYVEQM----ASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGI 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1569 YLPIDPANPPPRVAFMLGDA-----------VP-VAAVTTAG-----LRSRLAGHdLP-----------------IIDVV 1614
Cdd:PRK06710  101 VVQTNPLYTERELEYQLHDSgakvilcldlvFPrVTNVQSATkiehvIVTRIADF-LPfpknllypfvqkkqsnlVVKVS 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1615 DALAAY----------PGTPPPMPAAVNLAYILYTSGTTGEPKGVGITHRNVTR--------LFASLPARLSAAQVWSQC 1676
Cdd:PRK06710  180 ESETIHlwnsvekevnTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSntlmgvqwLYNCKEGEEVVLGVLPFF 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1677 HSYGFDASaweIWGALLGGGRLVIVPEsvaaspndFHGLLVAEHVS--VLTQTPAA----VAMLPTQGLE-----SVALV 1745
Cdd:PRK06710  260 HVYGMTAV---MNLSIMQGYKMVLIPK--------FDMKMVFEAIKkhKVTLFPGAptiyIALLNSPLLKeydisSIRAC 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1746 VAGEA-CPAALVDRW--APGRVMLNAYGPTET---TICAAISAPLRPGSgmppIGVPV--SGAALFVLDSWlRPVPAGVA 1817
Cdd:PRK06710  329 ISGSApLPVEVQEKFetVTGGKLVEGYGLTESspvTHSNFLWEKRVPGS----IGVPWpdTEAMIMSLETG-EALPPGEI 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1818 GELYIAGAGVGVGYWRRAGLTASRFvacpfggsGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAE 1897
Cdd:PRK06710  404 GEIVVKGPQIMKGYWNKPEETAAVL--------QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYE 475

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489495878 1898 LAGVGQAVVIAREDrPGDKRLVGYATEIAPGAVDPAGLRAQLAQR-LPGYLVPAAVVVIDALPLTVNGKLDHRALPAPE 1975
Cdd:PRK06710  476 HEKVQEVVTIGVPD-PYRGETVKAFVVLKEGTECSEEELNQFARKyLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEE 553
PRK09274 PRK09274
peptide synthase; Provisional
 1488-1880 1.34e-09

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 63.38  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1488 APTPVSIPQMLAAQVARIPEAEAVCCGDA----------SMTYRELDEASNRLAHRLAGCGAGPG-----------ECVA 1546
Cdd:PRK09274    2 MASMANIARHLPRAAQERPDQLAVAVPGGrgadgklaydELSFAELDARSDAIAHGLNAAGIGRGmravlmvtpslEFFA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1547 LLFercapavvamvAVLKTGAAYLPIDPA--------------------NPPPRVA-FMLGDAVP-VAAVTTAGLRSRLA 1604
Cdd:PRK09274   82 LTF-----------ALFKAGAVPVLVDPGmgiknlkqclaeaqpdafigIPKAHLArRLFGWGKPsVRRLVTVGGRLLWG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1605 GHDLPIIDVVDALAAYPG--TPPPMPAAvnlayILYTSGTTGEPKGVGITHRNvtrlFAslpARLSAAQvwsqcHSYGFD 1682
Cdd:PRK09274  151 GTTLATLLRDGAAAPFPMadLAPDDMAA-----ILFTSGSTGTPKGVVYTHGM----FE---AQIEALR-----EDYGIE 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1683 ASawEI----------WGALLGGGrlVIVPESVA-----ASPNDFHGLLVAEHVSVLTQTPAAVAMLPTQG------LES 1741
Cdd:PRK09274  214 PG--EIdlptfplfalFGPALGMT--SVIPDMDPtrpatVDPAKLFAAIERYGVTNLFGSPALLERLGRYGeangikLPS 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1742 VALV-VAGEACPAALVDRW----APGRVMLNAYGPTE---------TTICAAISAPLRPGSGMpPIGVPVSGAALFV--- 1804
Cdd:PRK09274  290 LRRViSAGAPVPIAVIERFramlPPDAEILTPYGATEalpissiesREILFATRAATDNGAGI-CVGRPVDGVEVRIiai 368

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1805 ----LDSW--LRPVPAGVAGELYIAGAGVGVGYWRRAGLTAsrfVACPFGGSGARMYRTGDLVCWRADGQLEFLGRTDDQ 1878
Cdd:PRK09274  369 sdapIPEWddALRLATGEIGEIVVAGPMVTRSYYNRPEATR---LAKIPDGQGDVWHRMGDLGYLDAQGRLWFCGRKAHR 445


                  ..
gi 489495878 1879 VK 1880
Cdd:PRK09274  446 VE 447
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
 1052-1346 2.24e-09

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 62.07  E-value: 2.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1052 RLRGYLDteALGAavadVVGRHESLRTVFpAVDGVPR--QLVIeaRRADLGCDIV--DATAWPADRLQRAIEeAARHSFD 1127
Cdd:cd19544    37 RLDAFLA--ALQQ----VIDRHDILRTAI-LWEGLSEpvQVVW--RQAELPVEELtlDPGDDALAQLRARFD-PRRYRLD 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1128 LaTEIPLrtWLFRIADDEH----VLVAVAHHIAADGWSVAPLTADLSAayasRCAGRAPDWAPlPVQYVDYTLWQReilg 1203
Cdd:cd19544   107 L-RQAPL--LRAHVAEDPAngrwLLLLLFHHLISDHTSLELLLEEIQA----ILAGRAAALPP-PVPYRNFVAQAR---- 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1204 dlddSDSPIAAQLAYWENALAGMPErlrlPTArPYPpVADQRG-------ASLVVDwpASVQQQVRRIARQHNAT--SFM 1274
Cdd:cd19544   175 ----LGASQAEHEAFFREMLGDVDE----PTA-PFG-LLDVQGdgsditeARLALD--AELAQRLRAQARRLGVSpaSLF 242

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489495878 1275 VVAAGLavLLSKLSGSPDVAVGFPIAGR--SDPALDNLVGFFVNTLVLRVNLAGDpSFAELLGQVRAR--SLAAYE 1346
Cdd:cd19544   243 HLAWAL--VLARCSGRDDVVFGTVLSGRmqGGAGADRALGMFINTLPLRVRLGGR-SVREAVRQTHARlaELLRHE 315
PRK07787 PRK07787
acyl-CoA synthetase; Validated
 574-853 2.46e-09

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 62.31  E-value: 2.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  574 TAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDIS-VEEIFGGAACGARLVRSAAMKTGDL 652
Cdd:PRK07787  130 PALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGlVLGVLGPLRIGNRFVHTGRPTPEAY 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  653 AAlvdDLVARETTIVDLPTaVWQLLCADGDAIDAIGRSRLrqIVIGGEAIRCSAVDKWlesAASQGISLLSSYGPTEaTV 732
Cdd:PRK07787  210 AQ---ALSEGGTLYFGVPT-VWSRIAADPEAARALRGARL--LVSGSAALPVPVFDRL---AALTGHRPVERYGMTE-TL 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  733 VATFLPIVCDQ------TTMDGALLRL----GRPILPNTVflAFGEVVIVGDLVADGYLG--------IDGDGFgtvtaa 794
Cdd:PRK07787  280 ITLSTRADGERrpgwvgLPLAGVETRLvdedGGPVPHDGE--TVGELQVRGPTLFDGYLNrpdataaaFTADGW------ 351

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  795 dgsrrraFATGDRVTVDAEGFPVFSGRKDA-VVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:PRK07787  352 -------FRTGDVAVVDPDGMHRIVGRESTdLIKSGGYRIGAGEIETALLGHPGVREAAV 404
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
 1890-1965 2.85e-09

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 55.63  E-value: 2.85e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489495878  1890 EVATALAELAGVGQAVVIAREDRPGDKRLVGYATEIAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGK 1965
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
PRK06188 PRK06188
acyl-CoA synthetase; Validated
 442-853 3.05e-09

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 62.31  E-value: 3.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  442 ARQPSTPAWFLDSARGVHQFLGRR--RFVYPWVAWlvqrGAAPGDVLVFTDDDTDKTIDLLIACHLAGCGY-------SV 512
Cdd:PRK06188   23 KRYPDRPALVLGDTRLTYGQLADRisRYIQAFEAL----GLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRtalhplgSL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  513 CDTADEIS--------VRTNAITEHGDGILvtvvDVAATQLAVVGHDELRKVVD--ERVTQVTH----DALLATKTAYIM 578
Cdd:PRK06188   99 DDHAYVLEdagistliVDPAPFVERALALL----ARVPSLKHVLTLGPVPDGVDllAAAAKFGPaplvAAALPPDIAGLA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  579 PTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSdisveeifggaaCGARLVRSAAMKTGDL------ 652
Cdd:PRK06188  175 YTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSH------------AGGAFFLPTLLRGGTVivlakf 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  653 -AALVDDLVARE----TTIVdlPTAVWQLLcaDGDAIDAIGRSRLRQIVIGGEAIrcsAVDKWLESAASQGISLLSSYGP 727
Cdd:PRK06188  243 dPAEVLRAIEEQritaTFLV--PTMIYALL--DHPDLRTRDLSSLETVYYGASPM---SPVRLAEAIERFGPIFAQYYGQ 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  728 TEATVVATFLPIVCDQTTMDGALLRLGRPILPNTVFL-----------AFGEVVIVGDLVADGYLGIDGDgfgtvTAadg 796
Cdd:PRK06188  316 TEAPMVITYLRKRDHDPDDPKRLTSCGRPTPGLRVALldedgrevaqgEVGEICVRGPLVMDGYWNRPEE-----TA--- 387

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489495878  797 srrRAFA-----TGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:PRK06188  388 ---EAFRdgwlhTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAV 446
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
 1514-1988 3.79e-09

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 62.05  E-value: 3.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1514 GDaSMTYRELDEASNR-----------LAHRLAGCGA------GPGECVALLFERCAPAVVAMVAVLKTGAAYLPI-DPA 1575
Cdd:PRK07769   35 GD-KLAYRFLDFSTERdgvardltwsqFGARNRAVGArlqqvtKPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPA 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1576 NP--PPRVAFMLGDAVPVAAVTTAG--------LRSRLAgHDLPIIDVVDALAAYPGTP--PPMPAAVNLAYILYTSGTT 1643
Cdd:PRK07769  114 EPghVGRLHAVLDDCTPSAILTTTDsaegvrkfFRARPA-KERPRVIAVDAVPDEVGATwvPPEANEDTIAYLQYTSGST 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1644 GEPKGVGITHR----NVTRLFASLPARLSAAQV-W-SQCHSYGFDASaweIWGALLGGGRLVIVPES-----------VA 1706
Cdd:PRK07769  193 RIPAGVQITHLnlptNVLQVIDALEGQEGDRGVsWlPFFHDMGLITV---LLPALLGHYITFMSPAAfvrrpgrwireLA 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1707 ASPNDFHGLLVA------EHvsvltqtpAAVAMLPTQG-----LESVALVVAG-EACPAALV----DRWAPgrvmlnaYG 1770
Cdd:PRK07769  270 RKPGGTGGTFSAapnfafEH--------AAARGLPKDGeppldLSNVKGLLNGsEPVSPASMrkfnEAFAP-------YG 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1771 PTETTIcaaisaplRPGSGMP-------------------------------------PIGVPVSGAALFVLDSWL---- 1809
Cdd:PRK07769  335 LPPTAI--------KPSYGMAeatlfvsttpmdeeptviyvdrdelnagrfvevpadaPNAVAQVSAGKVGVSEWAvivd 406

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1810 ----RPVPAGVAGELYIAGAGVGVGYWRRAGLTASRF---VACPFGGS-------GARMYRTGDLVCWrADGQLEFLGRT 1875
Cdd:PRK07769  407 petaSELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqniLKSRLSEShaegapdDALWVRTGDYGVY-FDGELYITGRV 485

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1876 DDQVKIRG---YRIEL-------------GEVAtALAELAGVGQAVV-------IAREDRPGDKRLVGYAtEIAPGA--V 1930
Cdd:PRK07769  486 KDLVIIDGrnhYPQDLeytaqeatkalrtGYVA-AFSVPANQLPQVVfddshagLKFDPEDTSEQLVIVA-ERAPGAhkL 563

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1931 DPA----GLRAQLAQR--LPG---YLVPAAvvvidALPLTVNGKLDHRALPApEYGDTN---GYRAPAGP 1988
Cdd:PRK07769  564 DPQpiadDIRAAIAVRhgVTVrdvLLVPAG-----SIPRTSSGKIARRACRA-AYLDGSlrsGYGQPAFP 627
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 534-853 5.78e-09

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 61.04  E-value: 5.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  534 LVTVVDVAATQLavvGHDELRKVVDE------RVTQVTHdallATKTAYIMPTSGTTGQPKLVRISHGSLAVfcDAISRA 607
Cdd:cd05974    48 LGAVVIPATTLL---TPDDLRDRVDRggavyaAVDENTH----ADDPMLLYFTSGTTSKPKLVEHTHRSYPV--GHLSTM 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  608 Y----------------GWGAHDTVLQCAPLTSDISVeEIFGGAACGARLVrsaamktgdLAALVDdlvARETTIVDLPT 671
Cdd:cd05974   119 YwiglkpgdvhwnisspGWAKHAWSCFFAPWNAGATV-FLFNYARFDAKRV---------LAALVR---YGVTTLCAPPT 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  672 aVWQLLCADGDAIDAIGrsrLRQIVIGGEAIRCSAVDKwleSAASQGISLLSSYGPTEATVVATFLPivcDQTTMDGAll 751
Cdd:cd05974   186 -VWRMLIQQDLASFDVK---LREVVGAGEPLNPEVIEQ---VRRAWGLTIRDGYGQTETTALVGNSP---GQPVKAGS-- 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  752 rLGRPIL--------PNTVFLAFGEVVIV-GDLVADGYL-GIDGDGFGTVTAADGSRRRafaTGDRVTVDAEGFPVFSGR 821
Cdd:cd05974   254 -MGRPLPgyrvalldPDGAPATEGEVALDlGDTRPVGLMkGYAGDPDKTAHAMRGGYYR---TGDIAMRDEDGYLTYVGR 329

                         330       340       350
                  ....*....|....*....|....*....|..
gi 489495878  822 KDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:cd05974   330 ADDVFKSSDYRISPFELESVLIEHPAVAEAAV 361
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 2110-2310 5.89e-09

NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 59.23  E-value: 5.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2110 VLLTGATGFLGRYLVLELLRRldvDGRLICLVRAESDEDARRRLEKTFDSGD----PELLRHFKELAADrlEVV-AGDKS 2184
Cdd:pfam01370    1 ILVTGATGFIGSHLVRRLLEK---GYEVIGLDRLTSASNTARLADLRFVEGDltdrDALEKLLADVRPD--AVIhLAAVG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2185 EPDLGLDQPmwrrlaetVDLIVDsaamvnafpyhelfgpNVAGTAELIRIALTTKLKPFTYVSTADVGAAIEPSAFTEDA 2264
Cdd:pfam01370   76 GVGASIEDP--------EDFIEA----------------NVLGTLNLLEAARKAGVKRFLFASSSEVYGDGAEIPQEETT 131

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 489495878  2265 DIRVISPTRtvdggwagGYGTSKWAGEVLLREANDLCALPVAVFRC 2310
Cdd:pfam01370  132 LTGPLAPNS--------PYAAAKLAGEWLVLAYAAAYGLRAVILRL 169
PRK08315 PRK08315
AMP-binding domain protein; Validated
 1494-1965 6.16e-09

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 61.37  E-value: 6.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1494 IPQMLAAQVARIPEAEAV--CCGDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLP 1571
Cdd:PRK08315   18 IGQLLDRTAARYPDREALvyRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVT 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1572 IDPANPPPRVAF-----------------------MLGDAVPVAAVTTAG-LRS----------RLAGHDLPIIDVVDAL 1617
Cdd:PRK08315   98 INPAYRLSELEYalnqsgckaliaadgfkdsdyvaMLYELAPELATCEPGqLQSarlpelrrviFLGDEKHPGMLNFDEL 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1618 AAYPGTPPPMPAA-----------VNlayILYTSGTTGEPKGVGITHRNVtrlfaslparlsaaqvwsqchsygfdasaw 1686
Cdd:PRK08315  178 LALGRAVDDAELAarqatldpddpIN---IQYTSGTTGFPKGATLTHRNI------------------------------ 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1687 eiwgalLGGGRLviVPESVAASPND--------FH------GLLVAehvsvLTQTPAAVAML----PTQGLESV------ 1742
Cdd:PRK08315  225 ------LNNGYF--IGEAMKLTEEDrlcipvplYHcfgmvlGNLAC-----VTHGATMVYPGegfdPLATLAAVeeerct 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1743 AL---------------------------VVAGEACPAALVDrwapgRVM--LN------AYGPTETT--ICA-AISAPL 1784
Cdd:PRK08315  292 ALygvptmfiaeldhpdfarfdlsslrtgIMAGSPCPIEVMK-----RVIdkMHmsevtiAYGMTETSpvSTQtRTDDPL 366

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1785 RP-----GSGMPPIGV----PVSGaalfvldswlRPVPAGVAGELYIAGAGVGVGYWRRAGLTASRFVAcpfggsgARMY 1855
Cdd:PRK08315  367 EKrvttvGRALPHLEVkivdPETG----------ETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDA-------DGWM 429

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1856 RTGDLVCWRADGQLEFLGRTDDQVkIRG----YRIELGEV-----ATALAELAGV-----GQAV---VIAREDRPgdkrl 1918
Cdd:PRK08315  430 HTGDLAVMDEEGYVNIVGRIKDMI-IRGgeniYPREIEEFlythpKIQDVQVVGVpdekyGEEVcawIILRPGAT----- 503

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*..
gi 489495878 1919 vgyateiapgaVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGK 1965
Cdd:PRK08315  504 -----------LTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGK 539
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
 574-910 8.81e-09

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 59.82  E-value: 8.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  574 TAYIMPTSGTTGQPKLVRISHGSlavfcdAISRAYGWGAhdtvlqCAPLTSDISVEEI------FG-GAACGARLVRSAA 646
Cdd:cd17638     2 VSDIMFTSGTTGRSKGVMCAHRQ------TLRAAAAWAD------CADLTEDDRYLIInpffhtFGyKAGIVACLLTGAT 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  647 ---MKTGDLAALVDDLVARETTIVDLPTAVWQLLCADGDAIDAiGRSRLRQIVIGGEAIRCSAVDKWLESAASQGIslLS 723
Cdd:cd17638    70 vvpVAVFDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKF-DLSSLRAAVTGAATVPVELVRRMRSELGFETV--LT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  724 SYGPTEATVVATFLP---IVCDQTT----MDGALLRLGRPilpntvflafGEVVIVGDLVADGYL--------GIDGDGF 788
Cdd:cd17638   147 AYGLTEAGVATMCRPgddAETVATTcgraCPGFEVRIADD----------GEVLVRGYNVMQGYLddpeataeAIDADGW 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  789 gtvtaadgsrrraFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV----ELHSGSLGVWF 864
Cdd:cd17638   217 -------------LHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVigvpDERMGEVGKAF 283

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 489495878  865 KSQRTREG--EQDAAAATRIRLVLVSLgvsSFFVVGVPNIPRKPNGKI 910
Cdd:cd17638   284 VVARPGVTltEEDVIAWCRERLANYKV---PRFVRFLDELPRNASGKV 328
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
 537-853 9.93e-09

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 60.46  E-value: 9.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  537 VVDVAATQLAVVGHDELRKVVDERVTQVTHDALLATKTAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTV 616
Cdd:cd05959   128 VLIVSGGAGPEAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDV 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  617 LqcapltsdISVEEIF---G-GAAC------GARLVRSAAMKTgdlAALVDDLVARE--TTIVDLPTAVWQLLCADGdaI 684
Cdd:cd05959   208 C--------FSAAKLFfayGlGNSLtfplsvGATTVLMPERPT---PAAVFKRIRRYrpTVFFGVPTLYAAMLAAPN--L 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  685 DAIGRSRLRQIVIGGEAIRCSAVDKWlesAASQGISLLSSYGPTEAtvvatfLPIVCDQTTMDGALLRLGRPIlPNTvfl 764
Cdd:cd05959   275 PSRDLSSLRLCVSAGEALPAEVGERW---KARFGLDILDGIGSTEM------LHIFLSNRPGRVRYGTTGKPV-PGY--- 341

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  765 afgEVVIVGD---LVADGYLG---IDGDGFGTV--TAADGSRRRA----FATGDRVTVDAEGFPVFSGRKDAVVKISGKR 832
Cdd:cd05959   342 ---EVELRDEdggDVADGEPGelyVRGPSSATMywNNRDKTRDTFqgewTRTGDKYVRDDDGFYTYAGRADDMLKVSGIW 418

                         330       340
                  ....*....|....*....|.
gi 489495878  833 VDIAEVTRRIAEDPAVSDVAV 853
Cdd:cd05959   419 VSPFEVESALVQHPAVLEAAV 439
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
1632-1971 1.14e-08

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 60.45  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1632 NLAYILYTSGTTGEPKGVGITHRN-VTRLFASLPARLSAAQVWSQchsygFDASAWEIWG--AL---------LGGGRLV 1699
Cdd:PRK08974  207 DLAFLQYTGGTTGVAKGAMLTHRNmLANLEQAKAAYGPLLHPGKE-----LVVTALPLYHifALtvncllfieLGGQNLL 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1700 IVpesvaaSPNDFHGLlvaehVSVLTQTPAAV---------AMLPTQGLE-----SVALVVAG-EACPAALVDRW--APG 1762
Cdd:PRK08974  282 IT------NPRDIPGF-----VKELKKYPFTAitgvntlfnALLNNEEFQeldfsSLKLSVGGgMAVQQAVAERWvkLTG 350

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1763 RVMLNAYGPTETT-ICAAISAPLRPGSGmpPIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTAS- 1840
Cdd:PRK08974  351 QYLLEGYGLTECSpLVSVNPYDLDYYSG--SIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEv 428

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1841 ---RFVAcpfggsgarmyrTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAredRPGDkr 1917
Cdd:PRK08974  429 ikdGWLA------------TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVG---VPSE-- 491

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 489495878 1918 LVGYATEIAPGAVDPA----GLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:PRK08974  492 VSGEAVKIFVVKKDPSlteeELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
 1514-1656 1.15e-08

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 60.15  E-value: 1.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1514 GDASMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAYLPIDPANPPPRVAFMLGDAVPVAA 1593
Cdd:cd05914     4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489495878 1594 VTTaglrsrlaghdlpiiDVVDalaaypgtpppmpaavnLAYILYTSGTTGEPKGVGITHRNV 1656
Cdd:cd05914    84 FVS---------------DEDD-----------------VALINYTSGTTGNSKGVMLTYRNI 114
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
 580-853 1.66e-08

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 59.72  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  580 TSGTTGQPKLVRISHGS--LAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARLVRSAAMKTGdlaALVD 657
Cdd:PRK07008  184 TSGTTGNPKGALYSHRStvLHAYGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPLTGAKLVLPGPDLDG---KSLY 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  658 DLVARE--TTIVDLPTaVWQLLCadgDAIDAIGR--SRLRQIVIGGEAirC-SAVDKWLESAasQGISLLSSYGPTEATV 732
Cdd:PRK07008  261 ELIEAErvTFSAGVPT-VWLGLL---NHMREAGLrfSTLRRTVIGGSA--CpPAMIRTFEDE--YGVEVIHAWGMTEMSP 332

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  733 VATFLPIVCDQTTMDGA-----LLRLGRPI--------------LP-NTVflAFGEVVIVGDLVADGYLGIDGDGFgtvt 792
Cdd:PRK07008  333 LGTLCKLKWKHSQLPLDeqrklLEKQGRVIygvdmkivgddgreLPwDGK--AFGDLQVRGPWVIDRYFRGDASPL---- 406

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489495878  793 aadgsRRRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:PRK07008  407 -----VDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAAC 462
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
 1624-1663 2.97e-08

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 59.15  E-value: 2.97e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 489495878 1624 PPPMPAAVNLAYILYTSGTTGEPKGVGITHRNVTRLFASL 1663
Cdd:cd05927   107 PPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGV 146
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
 1629-1966 3.01e-08

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 59.04  E-value: 3.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1629 AAVNLAYILYTSGTTGEPKGVGITHRNVTrlFASLpARLSAAQVWSQ---------CHSYGFdASAWEIwgaLLGGGRLV 1699
Cdd:PLN02860  170 APDDAVLICFTSGTTGRPKGVTISHSALI--VQSL-AKIAIVGYGEDdvylhtaplCHIGGL-SSALAM---LMVGACHV 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1700 IVPEsvaaspndFHGLLVAE-----HVSVLTQTPAAVAMLPT--------QGLESV-ALVVAGEACPAALVD---RWAPG 1762
Cdd:PLN02860  243 LLPK--------FDAKAALQaikqhNVTSMITVPAMMADLISltrksmtwKVFPSVrKILNGGGSLSSRLLPdakKLFPN 314

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1763 RVMLNAYGPTETtiCAAIS-------------------APLRPGSGMPPIGVPVSGAALFVLDSWLRPVPAGVaGELYIA 1823
Cdd:PLN02860  315 AKLFSAYGMTEA--CSSLTfmtlhdptlespkqtlqtvNQTKSSSVHQPQGVCVGKPAPHVELKIGLDESSRV-GRILTR 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1824 GAGVGVGYWrraGLTASRFVACPFGGsgarMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQ 1903
Cdd:PLN02860  392 GPHVMLGYW---GQNSETASVLSNDG----WLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVAS 464

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489495878 1904 AVVIARED-RPGDK-----RL--------VGYATEIAPGAVDPAGLRAQL-AQRLPGYLVPAAVVVI-DALPLTVNGKL 1966
Cdd:PLN02860  465 VVVVGVPDsRLTEMvvacvRLrdgwiwsdNEKENAKKNLTLSSETLRHHCrEKNLSRFKIPKLFVQWrKPFPLTTTGKI 543
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
580-910 3.01e-08

long-chain-fatty acid--ACP ligase MbtM;


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 59.01  E-value: 3.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  580 TSGTTGQPKLVRISHGS-LAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARLVRSAamkTGDLAA---- 654
Cdd:PRK05851  160 TAGSTGTPRTAILSPGAvLSNLRGLNARVGLDAATDVGCSWLPLYHDMGLAFLLTAALAGAPLWLAP---TTAFSAspfr 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  655 LVDDLVARETTIVDLPTAVWQLLCADGDAIDAIGRSRLRQIVIGGEAIRCSAVDKWLESAASQGI---SLLSSYGPTEAT 731
Cdd:PRK05851  237 WLSWLSDSRATLTAAPNFAYNLIGKYARRVSDVDLGALRVALNGGEPVDCDGFERFATAMAPFGFdagAAAPSYGLAEST 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  732 VVATfLPI------VCDQTTMDGALLR----LGRPILPNTVFLA------------FGEVVIVGDLVADGYLGidgdgfg 789
Cdd:PRK05851  317 CAVT-VPVpgiglrVDEVTTDDGSGARrhavLGNPIPGMEVRISpgdgaagvagreIGEIEIRGASMMSGYLG------- 388

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  790 tvtAADGSRRRAFATGDRVTVDAEGFpVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSD---VAVELHSGSL--GVWF 864
Cdd:PRK05851  389 ---QAPIDPDDWFPTGDLGYLVDGGL-VVCGRAKELITVAGRNIFPTEIERVAAQVRGVREgavVAVGTGEGSArpGLVI 464

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 489495878  865 KSQrTREGEQDAAAATRIRLVLVSLGVSSFFVVGVP--NIPRKPNGKI 910
Cdd:PRK05851  465 AAE-FRGPDEAGARSEVVQRVASECGVVPSDVVFVApgSLPRTSSGKL 511
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
 574-910 3.82e-08

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 58.04  E-value: 3.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  574 TAYIMPTSGTTGQPKLVRISHGSL-AVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEI----FGGAAC---GARLVRSA 645
Cdd:cd17635     3 PLAVIFTSGTTGEPKAVLLANKTFfAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWIltclIHGGLCvtgGENTTYKS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  646 AMKTGDLAALvddlvareTTIVDLPTAVWQLLCADGDAIDAIgrSRLRQIVIGGEAIrcsAVDKWLESAASQGISLLSSY 725
Cdd:cd17635    83 LFKILTTNAV--------TTTCLVPTLLSKLVSELKSANATV--PSLRLIGYGGSRA---IAADVRFIEATGLTNTAQVY 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  726 GPTEaTVVATFLPIVCDQTTMDGallrLGRPILPNTVFLA-----------FGEVVIVGDLVADGYLGidgdgfGTVTAA 794
Cdd:cd17635   150 GLSE-TGTALCLPTDDDSIEINA----VGRPYPGVDVYLAatdgiagpsasFGTIWIKSPANMLGYWN------NPERTA 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  795 DGSRRRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV-ELHSGSLGVWFKSQRTREGE 873
Cdd:cd17635   219 EVLIDGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACyEISDEEFGELVGLAVVASAE 298

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 489495878  874 QDAAAATRIRL-VLVSLGVSSF--FVVGVPNIPRKPNGKI 910
Cdd:cd17635   299 LDENAIRALKHtIRRELEPYARpsTIVIVTDIPRTQSGKV 338
PRK07201 PRK07201
SDR family oxidoreductase;
2109-2316 3.82e-08

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 58.81  E-value: 3.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2109 TVLLTGATGFLGRYLVLELLRRlDVDGRLICLVRAESdedaRRRLEktfdsgdpellRHFKELAADRLEVVAGDKSEPDL 2188
Cdd:PRK07201    2 RYFVTGGTGFIGRRLVSRLLDR-RREATVHVLVRRQS----LSRLE-----------ALAAYWGADRVVPLVGDLTEPGL 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2189 GLDQPMWRR---------LAETVDLIVDSAAMVNAfpyhelfgpNVAGTAELIRIALTTKLKPFTYVSTADVgAAIEPSA 2259
Cdd:PRK07201   66 GLSEADIAElgdidhvvhLAAIYDLTADEEAQRAA---------NVDGTRNVVELAERLQAATFHHVSSIAV-AGDYEGV 135

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2260 FTE---DADIRVISPtrtvdggwaggYGTSKWAGEVLLREAndlCALPVAVFRCGMILAD 2316
Cdd:PRK07201  136 FREddfDEGQGLPTP-----------YHRTKFEAEKLVREE---CGLPWRVYRPAVVVGD 181
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 540-910 3.99e-08

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 58.79  E-value: 3.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  540 VAATQLAVVGHDELRKVVDERVT-----QVTHDALLATKTAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHD 614
Cdd:cd05931   112 VRAFAASRPAAGTPRLLVVDLLPdtsaaDWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGD 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  615 TVLQCAPLTSDIS-VEEIFGGAACGARLVRSAAM----KTGDLAALVDDLVAretTIVDLPTAVWQlLCAD---GDAIDA 686
Cdd:cd05931   192 VVVSWLPLYHDMGlIGGLLTPLYSGGPSVLMSPAaflrRPLRWLRLISRYRA---TISAAPNFAYD-LCVRrvrDEDLEG 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  687 IGRSRLRQIVIGGEAIRCSAVDKWLESAASQGI---SLLSSYGPTEATVVATFLPI----VCDQTTMDG----------- 748
Cdd:cd05931   268 LDLSSWRVALNGAEPVRPATLRRFAEAFAPFGFrpeAFRPSYGLAEATLFVSGGPPgtgpVVLRVDRDAlagravavaad 347

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  749 -----ALLRLGRPIL--------PNTVFLA----FGEVVIVGDLVADGYLGIDG---DGFGTVTAADGsrRRAFATGDRV 808
Cdd:cd05931   348 dpaarELVSCGRPLPdqevrivdPETGRELpdgeVGEIWVRGPSVASGYWGRPEataETFGALAATDE--GGWLRTGDLG 425

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  809 TVdAEGFPVFSGRKDAVVKISGKRV---DIAEVTRRIAEDPAVSDVAV----ELHSGSLGVWFKSQRTREGEQDAAAATR 881
Cdd:cd05931   426 FL-HDGELYITGRLKDLIIVRGRNHypqDIEATAEEAHPALRPGCVAAfsvpDDGEERLVVVAEVERGADPADLAAIAAA 504

                         410       420       430
                  ....*....|....*....|....*....|..
gi 489495878  882 IR-LVLVSLGVSSFFVVGVPN--IPRKPNGKI 910
Cdd:cd05931   505 IRaAVAREHGVAPADVVLVRPgsIPRTSSGKI 536
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
 1632-1904 4.53e-08

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 58.29  E-value: 4.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1632 NLAYILYTSGTTGEPKGVGITHRNvtrLFASLPARLSAAQVWSQ---------CHSYGFDASAweIWGALLGggrLVIVP 1702
Cdd:PRK06334  184 DVAVILFTSGTEKLPKGVPLTHAN---LLANQRACLKFFSPKEDdvmmsflppFHAYGFNSCT--LFPLLSG---VPVVF 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1703 ESVAASPNDFHGLLVAEHVSVLTQTPA------AVAMLPTQGLESVALVV-AGEACPAAL---VDRWAPGRVMLNAYGPT 1772
Cdd:PRK06334  256 AYNPLYPKKIVEMIDEAKVTFLGSTPVffdyilKTAKKQESCLPSLRFVViGGDAFKDSLyqeALKTFPHIQLRQGYGTT 335

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1773 ETTICAAISAPLRPGSGmPPIGVPVSGA-ALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWrrAGLTASRFVACpfggSG 1851
Cdd:PRK06334  336 ECSPVITINTVNSPKHE-SCVGMPIRGMdVLIVSEETKVPVSSGETGLVLTRGTSLFSGYL--GEDFGQGFVEL----GG 408

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 489495878 1852 ARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQA 1904
Cdd:PRK06334  409 ETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAA 461
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
 574-853 5.91e-08

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 58.23  E-value: 5.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  574 TAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARLV---RSAAmktg 650
Cdd:PRK06155  182 TAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVlepRFSA---- 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  651 dlAALVDDLVARETTIVDLPTAVWQLLCADgDAIDAIGRSRLRQIVIGGEAIRcsAVDKWLESAasqGISLLSSYGPTEA 730
Cdd:PRK06155  258 --SGFWPAVRRHGATVTYLLGAMVSILLSQ-PARESDRAHRVRVALGPGVPAA--LHAAFRERF---GVDLLDGYGSTET 329

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  731 TVVATFLPIVCDQTTM----DGALLRL----GRPILPNTVflafGEVVIVGD---LVADGYlgiDGDGFGTVTAAdgsRR 799
Cdd:PRK06155  330 NFVIAVTHGSQRPGSMgrlaPGFEARVvdehDQELPDGEP----GELLLRADepfAFATGY---FGMPEKTVEAW---RN 399

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 489495878  800 RAFATGDRVTVDAEGFPVFSGR-KDAvVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:PRK06155  400 LWFHTGDRVVRDADGWFRFVDRiKDA-IRRRGENISSFEVEQVLLSHPAVAAAAV 453
PRK06164 PRK06164
acyl-CoA synthetase; Validated
 580-853 5.96e-08

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 58.22  E-value: 5.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  580 TSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIFGGAACGARLVRSAAMKTGDLAALVDDl 659
Cdd:PRK06164  189 TSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPVFDAARTARALRR- 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  660 vARETTIVDLPTAVWQLLCADGDAIDAigrSRLRQIvigGEAIRCSAVDKWLESAASQGISLLSSYGPTEatVVATFLpi 739
Cdd:PRK06164  268 -HRVTHTFGNDEMLRRILDTAGERADF---PSARLF---GFASFAPALGELAALARARGVPLTGLYGSSE--VQALVA-- 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  740 vCDQTTMDGALLRL--GRPILPNTVFLAF-------------GEVVIVGDLVADGYLGiDGDGFGTVTAADGsrrrAFAT 804
Cdd:PRK06164  337 -LQPATDPVSVRIEggGRPASPEARVRARdpqdgallpdgesGEIEIRAPSLMRGYLD-NPDATARALTDDG----YFRT 410

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 489495878  805 GDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:PRK06164  411 GDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQV 459
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 574-853 6.67e-08

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 57.99  E-value: 6.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  574 TAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTsdisveEIFG-GAACGARLVRSAAM---KT 649
Cdd:PRK07656  168 VADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFF------HVFGyKAGVNAPLMRGATIlplPV 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  650 GDLAALVDDLVARETTIVDLPTAVWQLLCA--DGDAIDAigrSRLRQIVIGGEAIRCSAVDKwLESAASQGIsLLSSYGP 727
Cdd:PRK07656  242 FDPDEVFRLIETERITVLPGPPTMYNSLLQhpDRSAEDL---SSLRLAVTGAASMPVALLER-FESELGVDI-VLTGYGL 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  728 TEATVVATFLPIVCDQTT--------MDGALLR----LGRPILPNTVflafGEVVIVGDLVADGYLG--------IDGDG 787
Cdd:PRK07656  317 SEASGVTTFNRLDDDRKTvagtigtaIAGVENKivneLGEEVPVGEV----GELLVRGPNVMKGYYDdpeataaaIDADG 392

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489495878  788 FgtvtaadgsrrraFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:PRK07656  393 W-------------LHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAV 445
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
 552-853 6.70e-08

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 57.49  E-value: 6.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  552 ELRKVVDERVTQVTHDALLATktayimpTSGTTGQPKLVRISHGSLAVFCDaisrayGWGAHdtVLQCAPLTSDISVEEI 631
Cdd:cd05958    84 ITVALCAHALTASDDICILAF-------TSGTTGAPKATMHFHRDPLASAD------RYAVN--VLRLREDDRFVGSPPL 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  632 FGGAACGARLV------RSAAMKTGDLAALVDDLVARE--TTIVDLPTAvWQLLCADGDAIDAIGrSRLRQIVIGGEAIR 703
Cdd:cd05958   149 AFTFGLGGVLLfpfgvgASGVLLEEATPDLLLSAIARYkpTVLFTAPTA-YRAMLAHPDAAGPDL-SSLRKCVSAGEALP 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  704 CSAVDKWLESAasqGISLLSSYGPTEA------------------TVVATFLPIVCDQttmdgallrLGRPILPNTvfla 765
Cdd:cd05958   227 AALHRAWKEAT---GIPIIDGIGSTEMfhifisarpgdarpgatgKPVPGYEAKVVDD---------EGNPVPDGT---- 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  766 fgevviVGDLVADGYLGIDGDgfgtvtaADGSRRRAF-----ATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTR 840
Cdd:cd05958   291 ------IGRLAVRGPTGCRYL-------ADKRQRTYVqggwnITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVED 357

                         330
                  ....*....|...
gi 489495878  841 RIAEDPAVSDVAV 853
Cdd:cd05958   358 VLLQHPAVAECAV 370
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
 575-853 9.55e-08

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 57.50  E-value: 9.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  575 AYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTsdisveEIFGGAACGARLVRSAA---MKTGD 651
Cdd:PLN02860  175 VLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLC------HIGGLSSALAMLMVGAChvlLPKFD 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  652 LAALVDDLVARE-TTIVDLPTAVWQLLCADGDAIDAIGRSRLRQIVIGGEAIRC---SAVDKWLESAAsqgisLLSSYGP 727
Cdd:PLN02860  249 AKAALQAIKQHNvTSMITVPAMMADLISLTRKSMTWKVFPSVRKILNGGGSLSSrllPDAKKLFPNAK-----LFSAYGM 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  728 TEATVVATFLPIvcDQTTMDGALLRLGRPILPNTVFLAFGEVVIVGDLVADGYLGIDGDGFGTV---------------- 791
Cdd:PLN02860  324 TEACSSLTFMTL--HDPTLESPKQTLQTVNQTKSSSVHQPQGVCVGKPAPHVELKIGLDESSRVgriltrgphvmlgywg 401

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489495878  792 ----TAADGSRRRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:PLN02860  402 qnseTASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVV 467
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
 1486-1943 1.06e-07

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 57.36  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1486 APAPTPVSIPQMLAAQVARIPE----AEAVCCGDA--SMTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAM 1559
Cdd:PRK12582   43 PLGPYPRSIPHLLAKWAAEAPDrpwlAQREPGHGQwrKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMT 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1560 VAVLKTGAAYLPIDPANP----------------PPRVAFMlGDAVP----VAAVTTAGLRSRLAGHDLPIIDVVdALAA 1619
Cdd:PRK12582  123 LAAMQAGVPAAPVSPAYSlmshdhaklkhlfdlvKPRVVFA-QSGAPfaraLAALDLLDVTVVHVTGPGEGIASI-AFAD 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1620 YPGTPPPM----------PAAVnlAYILYTSGTTGEPKGVGITHRNVT-------RLFASLPARLSAAQV----WSqcHS 1678
Cdd:PRK12582  201 LAATPPTAavaaaiaaitPDTV--AKYLFTSGSTGMPKAVINTQRMMCaniamqeQLRPREPDPPPPVSLdwmpWN--HT 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1679 YGFDASaweIWGALLGGGRLVIVPESvaASPNDFHGLLVAEH-VS--VLTQTPAAVAMLPT-------------QGLESV 1742
Cdd:PRK12582  277 MGGNAN---FNGLLWGGGTLYIDDGK--PLPGMFEETIRNLReISptVYGNVPAGYAMLAEamekddalrrsffKNLRLM 351

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1743 ALvvAGEACPAALVDRW------APGR--VMLNAYGPTET--TICAAISAPLRPGSgmppIGVPVSGAALFVldswlrpV 1812
Cdd:PRK12582  352 AY--GGATLSDDLYERMqalavrTTGHriPFYTGYGATETapTTTGTHWDTERVGL----IGLPLPGVELKL-------A 418

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1813 PAGVAGELYIAGAGVGVGYWRRAGLTASRFVACPFggsgarmYRTGDLVCW----RADGQLEFLGRTDDQVKI-RGYRIE 1887
Cdd:PRK12582  419 PVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF-------YRLGDAARFvdpdDPEKGLIFDGRVAEDFKLsTGTWVS 491

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489495878 1888 LGEVAT-ALAELAGVGQAVVIAREDRP-----------GDKRLVGYATEIAPGAVDPAGLRAQLAQRL 1943
Cdd:PRK12582  492 VGTLRPdAVAACSPVIHDAVVAGQDRAfigllawpnpaACRQLAGDPDAAPEDVVKHPAVLAILREGL 559
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
 501-853 1.20e-07

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 57.09  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  501 IACHLAGCGYSVCDTADEISVRTNAITEHGDGILVTVVDVAATQLAVVGHDELRKVVDE--RVTQVTHDAllatkTAYIM 578
Cdd:PRK07786  106 IAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPahAPVDIPNDS-----PALIM 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  579 PTSGTTGQPKLVRISHGSLAvfCDAISRAYGWGA---HDTVLQCAPLTSDISVEEIFGGAACGARLVRSAaMKTGDLAAL 655
Cdd:PRK07786  181 YTSGTTGRPKGAVLTHANLT--GQAMTCLRTNGAdinSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYP-LGAFDPGQL 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  656 VDDLVARETTIVDLPTAVWQLLCADGDAIdaiGRS-RLRQIVIGGeairCSAVDKWLE--SAASQGISLLSSYGPTEATv 732
Cdd:PRK07786  258 LDVLEAEKVTGIFLVPAQWQAVCAEQQAR---PRDlALRVLSWGA----APASDTLLRqmAATFPEAQILAAFGQTEMS- 329

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  733 vatflPIVCdqtTMDG--ALLRLG---RPI---------------LPNTVflafGEVVIVGDLVADGYLGidgDGFGTVT 792
Cdd:PRK07786  330 -----PVTC---MLLGedAIRKLGsvgKVIptvaarvvdenmndvPVGEV----GEIVYRAPTLMSGYWN---NPEATAE 394

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489495878  793 AADGSrrrAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:PRK07786  395 AFAGG---WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAV 452
UDP_G4E_4_SDR_e cd05232
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
 2109-2331 1.23e-07

UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of bacterial proteins, and includes the Staphylococcus aureus capsular polysaccharide Cap5N, which may have a role in the synthesis of UDP-N-acetyl-d-fucosamine. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187543 [Multi-domain]  Cd Length: 303  Bit Score: 55.82  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2109 TVLLTGATGFLGRYLVLELLrrldvdgrliclvraesdedarrrlektfdsgdpelLRHFKELAADRLEVVAGDKSEPDL 2188
Cdd:cd05232     1 KVLVTGANGFIGRALVDKLL------------------------------------SRGEEVRIAVRNAENAEPSVVLAE 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2189 GLDqPMWR-RLAETVDLIVDSAAMVNAF------PYHELFGPNVAGTAELIRIALTTKLKPFTYVSTadVGAAIEPsafT 2261
Cdd:cd05232    45 LPD-IDSFtDLFLGVDAVVHLAARVHVMndqgadPLSDYRKVNTELTRRLARAAARQGVKRFVFLSS--VKVNGEG---T 118

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2262 EDADIRVISPTRTVDGgwaggYGTSKWAGEVLLREANDLCALPVAVFRCGMILADTSYAGQLNMSDWVTR 2331
Cdd:cd05232   119 VGAPFDETDPPAPQDA-----YGRSKLEAERALLELGASDGMEVVILRPPMVYGPGVRGNFARLMRLIDR 183
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
563-852 1.46e-07

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 56.81  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  563 QVTHDALlatktAYIMPTSGTTGQPKLVRISHGSLAVfcdAISRAYGWGA--------HDTVLQCAPLTsdisveEIFGG 634
Cdd:PRK08751  204 QIEPDDI-----AFLQYTGGTTGVAKGAMLTHRNLVA---NMQQAHQWLAgtgkleegCEVVITALPLY------HIFAL 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  635 AACGarLVrsaAMKTG----------DLAALVDDLV-ARETTIVDLPTAVWQLLCADGdaIDAIGRSRLRQIVIGGEAIR 703
Cdd:PRK08751  270 TANG--LV---FMKIGgcnhlisnprDMPGFVKELKkTRFTAFTGVNTLFNGLLNTPG--FDQIDFSSLKMTLGGGMAVQ 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  704 CSAVDKWLESAasqGISLLSSYGPTEATVVATFLPIVCDQttMDGALlrlGRPIlPNT---------VFLAFGEV---VI 771
Cdd:PRK08751  343 RSVAERWKQVT---GLTLVEAYGLTETSPAACINPLTLKE--YNGSI---GLPI-PSTdacikddagTVLAIGEIgelCI 413

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  772 VGDLVADGYLGiDGDGFGTVTAADGsrrrAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDV 851
Cdd:PRK08751  414 KGPQVMKGYWK-RPEETAKVMDADG----WLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEV 488


                  .
gi 489495878  852 A 852
Cdd:PRK08751  489 A 489
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 570-852 1.80e-07

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 56.31  E-value: 1.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  570 LATKTAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSdisveeIFG---GAACGARLVRSAA 646
Cdd:cd05910    83 KADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLFA------LFGpalGLTSVIPDMDPTR 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  647 MKTGDLAALVDDLVARETTIVDLPTAVWQLLCADGDAIDaIGRSRLRQIVIGGEAIRCSAVDKwLESAASQGISLLSSYG 726
Cdd:cd05910   157 PARADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHG-ITLPSLRRVLSAGAPVPIALAAR-LRKMLSDEAEILTPYG 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  727 PTEATVVATF----LPIVCDQTTMDGALLRLGRPILPNTVFL--------------------AFGEVVIVGDLVADGYLG 782
Cdd:cd05910   235 ATEALPVSSIgsreLLATTTAATSGGAGTCVGRPIPGVRVRIieiddepiaewddtlelprgEIGEITVTGPTVTPTYVN 314

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489495878  783 -IDGDGFGTVTaaDGSRRRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVA 852
Cdd:cd05910   315 rPVATALAKID--DNSEGFWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSA 383
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 561-853 1.98e-07

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 55.99  E-value: 1.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  561 VTQVTHDALLATKTAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCA-PLTSDISVEEIFGGAACGa 639
Cdd:cd05973    77 VTDAANRHKLDSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAAdPGWAYGLYYAITGPLALG- 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  640 rlVRSAAMKTGDLAALVDDLVARE--TTIVDLPTAvWQLLCADGDAIDAIGRSRLRQIVIGGEAIRcSAVDKWleSAASQ 717
Cdd:cd05973   156 --HPTILLEGGFSVESTWRVIERLgvTNLAGSPTA-YRLLMAAGAEVPARPKGRLRRVSSAGEPLT-PEVIRW--FDAAL 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  718 GISLLSSYGPTEATVVatflpiVCDQTTmdgallrLGRPILPNTVFLAF-GEVVIVGDLVAD-------GYLGIDGDG-- 787
Cdd:cd05973   230 GVPIHDHYGQTELGMV------LANHHA-------LEHPVHAGSAGRAMpGWRVAVLDDDGDelgpgepGRLAIDIANsp 296

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489495878  788 ---FGTVTAADGSR--RRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:cd05973   297 lmwFRGYQLPDTPAidGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAV 367
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 580-862 2.53e-07

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 55.56  E-value: 2.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  580 TSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTS-DISVEEIFGGAACGARLVRSAAMKTGDlAALVDD 658
Cdd:cd05944    10 TGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHvNGSVVTLLTPLASGAHVVLAGPAGYRN-PGLFDN 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  659 ---LVARE--TTIVDLPTAVWQLLCADGDAidaiGRSRLRQIVIGGEAIRCsAVDKWLESAAsqGISLLSSYGPTEATVV 733
Cdd:cd05944    89 fwkLVERYriTSLSTVPTVYAALLQVPVNA----DISSLRFAMSGAAPLPV-ELRARFEDAT--GLPVVEGYGLTEATCL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  734 ATF---------------LPIVCDQTTMDGALLRLGRPILPNTVflafGEVVIVGDLVADGYLgiDGDGFGTVTAADGsr 798
Cdd:cd05944   162 VAVnppdgpkrpgsvglrLPYARVRIKVLDGVGRLLRDCAPDEV----GEICVAGPGVFGGYL--YTEGNKNAFVADG-- 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489495878  799 rrAFATGDRVTVDAEGFPVFSGR-KDAVVKiSGKRVDIAEVTRRIAEDPAVSDVAV----ELHSGSLGV 862
Cdd:cd05944   234 --WLNTGDLGRLDADGYLFITGRaKDLIIR-GGHNIDPALIEEALLRHPAVAFAGAvgqpDAHAGELPV 299
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
 1604-1971 2.64e-07

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 56.30  E-value: 2.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1604 AGHDLPIIDVVDALAAYpGTPPPMPAAVNLaYILYTSGTTGEPKGV-----G------ITHRNV-----------Trlfa 1661
Cdd:PRK00174  220 EGRDLWWHELVAGASDE-CEPEPMDAEDPL-FILYTSGSTGKPKGVlhttgGylvyaaMTMKYVfdykdgdvywcT---- 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1662 slparlsaAQV-WSQCHSYGfdasaweIWGALLGGGRLVIVpESVAASPN-DFHGLLVAEH-VSVLTQTPAAVAMLPTQG 1738
Cdd:PRK00174  294 --------ADVgWVTGHSYI-------VYGPLANGATTLMF-EGVPNYPDpGRFWEVIDKHkVTIFYTAPTAIRALMKEG 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1739 --------LESVAL------------------VVAGEACPaaLVDRW---APGRVMLnaygpteTTICAAIsaPLRPGSG 1789
Cdd:PRK00174  358 dehpkkydLSSLRLlgsvgepinpeawewyykVVGGERCP--IVDTWwqtETGGIMI-------TPLPGAT--PLKPGSA 426

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1790 MPPI-----------GVPVSGAA---LFVLDSW---LRpvpaGVAG--ELYIAgagvgvGYWrragltaSRFVACPFGGS 1850
Cdd:PRK00174  427 TRPLpgiqpavvdeeGNPLEGGEggnLVIKDPWpgmMR----TIYGdhERFVK------TYF-------STFKGMYFTGD 489

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1851 GARMyrtgDlvcwrADGQLEFLGRTDDQVKIRGYRIELGEVATAL------AELAGV-------GQAV---VIAREDRPG 1914
Cdd:PRK00174  490 GARR----D-----EDGYYWITGRVDDVLNVSGHRLGTAEIESALvahpkvAEAAVVgrpddikGQGIyafVTLKGGEEP 560

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489495878 1915 DKRLvgyATEiapgavdpagLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:PRK00174  561 SDEL---RKE----------LRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRIL 604
PLN02996 PLN02996
fatty acyl-CoA reductase
 2108-2251 3.01e-07

fatty acyl-CoA reductase


Pssm-ID: 215538 [Multi-domain]  Cd Length: 491  Bit Score: 55.87  E-value: 3.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2108 RTVLLTGATGFLGRYLVLELLRRLDVDGRLICLVRAESDEDARRRLEKtfDSGDPELLRHFKE--------LAADRLEVV 2179
Cdd:PLN02996   12 KTILVTGATGFLAKIFVEKILRVQPNVKKLYLLLRASDAKSATQRLHD--EVIGKDLFKVLREklgenlnsLISEKVTPV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2180 AGDKSEPDLG-----LDQPMWRRlaetVDLIVDSAAMVNaFP--YHELFGPNVAGTAELIRIA-LTTKLKPFTYVSTADV 2251
Cdd:PLN02996   90 PGDISYDDLGvkdsnLREEMWKE----IDIVVNLAATTN-FDerYDVALGINTLGALNVLNFAkKCVKVKMLLHVSTAYV 164
PRK05850 PRK05850
acyl-CoA synthetase; Validated
 1580-1883 3.07e-07

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 55.72  E-value: 3.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1580 RVAFMLGDAVPVAAVTTAG----LRSRLAGHDL---PIIDVVDAL--AAYPGTPPPMPAAVNLAYILYTSGTTGEPKGVG 1650
Cdd:PRK05850  100 RVSAVLRDTSPSVVLTTSAvvddVTEYVAPQPGqsaPPVIEVDLLdlDSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVM 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1651 ITHRNVT----RLFAS-LPARLSAAQVWSQCHSygfdasaweiW-------GALLGggrlVIVP-----ESVAASPNDFh 1713
Cdd:PRK05850  180 VSHRNVIanfeQLMSDyFGDTGGVPPPDTTVVS----------WlpfyhdmGLVLG----VCAPilggcPAVLTSPVAF- 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1714 gL--------LVAEHVSVLTQTP-----AAV-----AMLPTQGLESVALVVAG--EACPAAL---VDRWAP----GRVML 1766
Cdd:PRK05850  245 -LqrparwmqLLASNPHAFSAAPnfafeLAVrktsdDDMAGLDLGGVLGIISGseRVHPATLkrfADRFAPfnlrETAIR 323

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1767 NAYGPTETTICAAISAPLRP---------------------GSGMPPI--GVPVSGAALFVLDSWLRPVPAGVAGELYIA 1823
Cdd:PRK05850  324 PSYGLAEATVYVATREPGQPpesvrfdyeklsaghakrcetGGGTPLVsyGSPRSPTVRIVDPDTCIECPAGTVGEIWVH 403

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489495878 1824 GAGVGVGYWRRAGLTASRF----VACPFGGSGARMYRTGDL-VCWraDGQLEFLGRTDDQVKIRG 1883
Cdd:PRK05850  404 GDNVAAGYWQKPEETERTFgatlVDPSPGTPEGPWLRTGDLgFIS--EGELFIVGRIKDLLIVDG 466
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
 577-853 3.26e-07

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 54.97  E-value: 3.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  577 IMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLtsdisveeiFGGAACGARLvrsAAMKTGDLAALV 656
Cdd:cd17637     5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPL---------FHIAGLNLAL---ATFHAGGANVVM 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  657 D--------DLVARE--TTIVDLPTAVWQLLcadgDAIDAIGR--SRLRqIVIGGEAIrcSAVDKWLESAASQgisLLSS 724
Cdd:cd17637    73 EkfdpaealELIEEEkvTLMGSFPPILSNLL----DAAEKSGVdlSSLR-HVLGLDAP--ETIQRFEETTGAT---FWSL 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  725 YGPTEATVVATFLPIvcdqTTMDGALlrlGRPILPNTVFL-----------AFGEVVIVGDLVADGYLGIDgdgfgTVTA 793
Cdd:cd17637   143 YGQTETSGLVTLSPY----RERPGSA---GRPGPLVRVRIvddndrpvpagETGEIVVRGPLVFQGYWNLP-----ELTA 210

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489495878  794 adgsrrRAFA-----TGDRVTVDAEGFPVFSGRKDA--VVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:cd17637   211 ------YTFRngwhhTGDLGRFDEDGYLWYAGRKPEkeLIKPGGENVYPAEVEKVILEHPAIAEVCV 271
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
 1514-1680 3.51e-07

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 55.38  E-value: 3.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1514 GDASMTYRELDEASNRLAHRL-AGCGAGPGECVALL------------------------------------FERCapav 1556
Cdd:cd05938     2 EGETYTYRDVDRRSNQAARALlAHAGLRPGDTVALLlgnepaflwiwlglaklgcpvaflntnirsksllhcFRCC---- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1557 vamvavlktGAAYLPIDPAnppprvafmLGDAV-PV-AAVTTAGLRSRLAGHDLP---IIDVVDALAAYPGTPPP--MPA 1629
Cdd:cd05938    78 ---------GAKVLVVAPE---------LQEAVeEVlPALRADGVSVWYLSHTSNtegVISLLDKVDAASDEPVPasLRA 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1630 AVNL----AYIlYTSGTTGEPKGVGITHRNVTR---------------LFASLP------------------------AR 1666
Cdd:cd05938   140 HVTIkspaLYI-YTSGTTGLPKAARISHLRVLQcsgflslcgvtaddvIYITLPlyhssgfllgiggcielgatcvlkPK 218

                         250
                  ....*....|....
gi 489495878 1667 LSAAQVWSQCHSYG 1680
Cdd:cd05938   219 FSASQFWDDCRKHN 232
PRK07788 PRK07788
acyl-CoA synthetase; Validated
 517-918 3.53e-07

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 55.70  E-value: 3.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  517 DEISVRTNAITEHGDGILVTVVDVAATQLAVVGHDELRKVVDERVTQVthdALLATKTA-YIMPTSGTTGQPKLVRISH- 594
Cdd:PRK07788  154 DEFTDLLSALPPDLGRLRAWGGNPDDDEPSGSTDETLDDLIAGSSTAP---LPKPPKPGgIVILTSGTTGTPKGAPRPEp 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  595 ---GSLAVFCDAISraygWGAHDTVLQCAPLTSDISVEEIFGGAACGARLVrsaAMKTGDLAALVDDLVA-RETTIVDLP 670
Cdd:PRK07788  231 splAPLAGLLSRVP----FRAGETTLLPAPMFHATGWAHLTLAMALGSTVV---LRRRFDPEATLEDIAKhKATALVVVP 303

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  671 TAVWQLLCADGDAIDAIGRSRLRQIVIGGeaircSAVDKWLESAASQ--GISLLSSYGPTEATV--VATFLPIVCDQTTM 746
Cdd:PRK07788  304 VMLSRILDLGPEVLAKYDTSSLKIIFVSG-----SALSPELATRALEafGPVLYNLYGSTEVAFatIATPEDLAEAPGTV 378

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  747 D----GALLRL----GRPILPNTVflafGEVVIVGDLVADGYLG------IDGdgfgtvtaadgsrrrAFATGDRVTVDA 812
Cdd:PRK07788  379 GrppkGVTVKIldenGNEVPRGVV----GRIFVGNGFPFEGYTDgrdkqiIDG---------------LLSSGDVGYFDE 439

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  813 EGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAVelhsgsLGV----WFKSQR----TREGEQDAAAATR--I 882
Cdd:PRK07788  440 DGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAV------IGVddeeFGQRLRafvvKAPGAALDEDAIKdyV 513

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 489495878  883 RLVLVSLGVSSfFVVGVPNIPRKPNGKIdsdnLPRL 918
Cdd:PRK07788  514 RDNLARYKVPR-DVVFLDELPRNPTGKV----LKRE 544
UDP_AE_SDR_e cd05256
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ...
 2110-2309 3.65e-07

UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains UDP-N-acetylglucosamine 4-epimerase of Pseudomonas aeruginosa, WbpP, an extended SDR, that catalyzes the NAD+ dependent conversion of UDP-GlcNAc and UDPGalNA to UDP-Glc and UDP-Gal. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187566 [Multi-domain]  Cd Length: 304  Bit Score: 54.53  E-value: 3.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2110 VLLTGATGFLGRYLVLELLRRldvDGRLICLvraesDEdarrrlektFDSGDPELLRHFKelaaDRLEVVAGDKSepdlg 2189
Cdd:cd05256     2 VLVTGGAGFIGSHLVERLLER---GHEVIVL-----DN---------LSTGKKENLPEVK----PNVKFIEGDIR----- 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2190 lDQPMWRRLAETVDLIVDSAAM-------VNAFPYHELfgpNVAGTAELIRIALTTKLKPFTYVSTADVGAAIEPSAFTE 2262
Cdd:cd05256    56 -DDELVEFAFEGVDYVFHQAAQasvprsiEDPIKDHEV---NVLGTLNLLEAARKAGVKRFVYASSSSVYGDPPYLPKDE 131

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 489495878 2263 DADIRVISPtrtvdggwaggYGTSKWAGEVLLREANDLCALPVAVFR 2309
Cdd:cd05256   132 DHPPNPLSP-----------YAVSKYAGELYCQVFARLYGLPTVSLR 167
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 667-1193 3.90e-07

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 56.03  E-value: 3.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  667 VDLPTAVWQ---LLCADGDAIDAIGRSRLRQIVIGGEAIRCSAVDKWLESAASQGISLLSSYGPTEATVVATFLPIVCDQ 743
Cdd:COG3321   861 VPLPTYPFQredAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAA 940

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  744 TTMDGALLRLGRPILPntvfLAFGEVVIVGDLVADGYLGIDGDGFGTVTAADGSRRRAFATGDRVTVDAEGFPVFSGRKD 823
Cdd:COG3321   941 ALLALAAAAAAAAAAL----AAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAA 1016

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  824 AVVKISGKRVDIAEVTRRIAEDPAVSDVAVELHSGSLGVWFKSQRTREGEQDAAAATRIRLVLVSLGVSSFFVVGVPNIP 903
Cdd:COG3321  1017 AAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALA 1096

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  904 RKPNGKIDSDNLPRLPQWSAAGLNTAETGQRAAGLSQIWSRQLGRAIGPDSSLLGEGIGSLDLIRILPETRRYLGWRLSL 983
Cdd:COG3321  1097 LALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLA 1176

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  984 LDLIGADTAANLADYAPTPDAPTGEDRFRPLVAAQRPAAIPLSFAQRRLWFLDQLQRPAPVYNMAVALRLRGYLDTEALG 1063
Cdd:COG3321  1177 LALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALL 1256

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1064 AAVADVVGRHESLRTVFPAVDGVPRQLVIEARRADLGCDIVDATAWPADRLQRAIEEAARHSFDLATEIPLRTWLFRIAD 1143
Cdd:COG3321  1257 AALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAA 1336

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 489495878 1144 DEHVLVAVAHHIAADGWSVAPLTADLSAAYASRCAGRAPDWAPLPVQYVD 1193
Cdd:COG3321  1337 VAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
 515-853 4.62e-07

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 54.93  E-value: 4.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  515 TADEISvrtNAITEHGDGILVTVVD----VAATQLAVVGHDELRKV---VDERVTQVTHDALLATK-----TAYIMPTSG 582
Cdd:cd05904    92 TPAEIA---KQVKDSGAKLAFTTAElaekLASLALPVVLLDSAEFDslsFSDLLFEADEAEPPVVVikqddVAALLYSSG 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  583 TTGQPKLVRISHGSLAVFCDAISRAYG-WGAHDTVLQCA-PLTsdisveEIFG-------GAACGARLVrsaAMKTGDLA 653
Cdd:cd05904   169 TTGRSKGVMLTHRNLIAMVAQFVAGEGsNSDSEDVFLCVlPMF------HIYGlssfalgLLRLGATVV---VMPRFDLE 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  654 ALVDDLVARETTIVDL-PTAVWQLlcADGDAIDAIGRSRLRQIVIGGeaircSAVDKWLESAASQ---GISLLSSYGPTE 729
Cdd:cd05904   240 ELLAAIERYKVTHLPVvPPIVLAL--VKSPIVDKYDLSSLRQIMSGA-----APLGKELIEAFRAkfpNVDLGQGYGMTE 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  730 ATVVATFLPIVCDQTTMDGALLRL-------------GRPILPNTVflafGEVVIVGDLVADGYLG--------IDGDGF 788
Cdd:cd05904   313 STGVVAMCFAPEKDRAKYGSVGRLvpnveakivdpetGESLPPNQT----GELWIRGPSIMKGYLNnpeataatIDKEGW 388

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489495878  789 gtvtaadgsrrraFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:cd05904   389 -------------LHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAV 440
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 570-910 5.23e-07

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 54.75  E-value: 5.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  570 LATKTAYIMPTSGTTGQPKLVRISHGSLAvfcdaisraygwgAHDTVLQ----CAPLTSDIsveeiFGGAA----CGARL 641
Cdd:cd05971    86 GSDDPALIIYTSGTTGPPKGALHAHRVLL-------------GHLPGVQfpfnLFPRDGDL-----YWTPAdwawIGGLL 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  642 ------------VRSAAMKTGDLAALVDDLVARETTIVDLPTAVWQLLCADGDAIDAIGRsRLRQIVIGGEaircSAVDK 709
Cdd:cd05971   148 dvllpslyfgvpVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQV-KLRAIATGGE----SLGEE 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  710 WLESAASQ-GISLLSSYGPTEATVVATFLPIVCDqtTMDGALlrlGRPILPNTVFL--AFGEVVIVGdlvADGYLGI--- 783
Cdd:cd05971   223 LLGWAREQfGVEVNEFYGQTECNLVIGNCSALFP--IKPGSM---GKPIPGHRVAIvdDNGTPLPPG---EVGEIAVelp 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  784 DGDGFGTVTAADGSRRRAFA-----TGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV----E 854
Cdd:cd05971   295 DPVAFLGYWNNPSATEKKMAgdwllTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVvgipD 374

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 489495878  855 LHSGSLGVWFKSQRTREGEQDAAAATRIRLVLVSLGVSSF--FVVGVPNIPRKPNGKI 910
Cdd:cd05971   375 PIRGEIVKAFVVLNPGETPSDALAREIQELVKTRLAAHEYprEIEFVNELPRTATGKI 432
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
1573-1971 6.21e-07

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 54.79  E-value: 6.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1573 DPANPPpRVAFMLGDAVPVAAVTTAGLRS--RLAGHDLPIIDVVDALAAYPGTPP----PMPAAVNLAYILYTSGTTGEP 1646
Cdd:PRK05620  118 DPRLAE-QLGEILKECPCVRAVVFIGPSDadSAAAHMPEGIKVYSYEALLDGRSTvydwPELDETTAAAICYSTGTTGAP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1647 KGVGITHRNVTRLFASLPARLSAA----QVWSQC----H--SYGFDASAWEIWGALLGGGRLViVPESVA-----ASPND 1711
Cdd:PRK05620  197 KGVVYSHRSLYLQSLSLRTTDSLAvthgESFLCCvpiyHvlSWGVPLAAFMSGTPLVFPGPDL-SAPTLAkiiatAMPRV 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1712 FHGLlvaehVSVLTQTPAAVAMLPTQGLESVALVVAGEACPAALVDRWAP--GRVMLNAYGPTETTICAAISaplRPGSG 1789
Cdd:PRK05620  276 AHGV-----PTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEEryGVDVVHVWGMTETSPVGTVA---RPPSG 347

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1790 mppigvpVSGAALFVLDSWLRPVPAGV-----------------AGELYIAGAGVGVGYWR----RAGLTASRFVACPFG 1848
Cdd:PRK05620  348 -------VSGEARWAYRVSQGRFPASLeyrivndgqvmestdrnEGEIQVRGNWVTASYYHspteEGGGAASTFRGEDVE 420

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1849 GSGARM-----YRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKR---LVG 1920
Cdd:PRK05620  421 DANDRFtadgwLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERplaVTV 500

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 489495878 1921 YATEIAPGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:PRK05620  501 LAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
PRK07638 PRK07638
acyl-CoA synthetase; Validated
 1506-1971 7.90e-07

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 54.40  E-value: 7.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1506 PEAEAVCCGDASMTYRELDEASNRLAHRLaGCGAGPGECVALLFERcapavVAMVAVLKTGAAYL-----PIDPANPPPR 1580
Cdd:PRK07638   15 PNKIAIKENDRVLTYKDWFESVCKVANWL-NEKESKNKTIAILLEN-----RIEFLQLFAGAAMAgwtcvPLDIKWKQDE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1581 VAFMLGDAVPVAAVTTAGLRSRLAGHDLPIID---VVDALAAYPGTPPPMPAAVNLA-YILYTSGTTGEPKGVGITHRNV 1656
Cdd:PRK07638   89 LKERLAISNADMIVTERYKLNDLPDEEGRVIEideWKRMIEKYLPTYAPIENVQNAPfYMGFTSGSTGKPKAFLRAQQSW 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1657 TRLFaslparlsaaqvwsQCHSYGFDASAWE---IWGALLG-------------GGRLVIVPEsvaASPNDFHGLLVAEH 1720
Cdd:PRK07638  169 LHSF--------------DCNVHDFHMKREDsvlIAGTLVHslflygaistlyvGQTVHLMRK---FIPNQVLDKLETEN 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1721 VSVLTQTPAAV-AMLPTQGL--ESVALVVAGEACPA----ALVDRWaPGRVMLNAYGPTETTICAAIS---APLRPGSgm 1790
Cdd:PRK07638  232 ISVMYTVPTMLeSLYKENRVieNKMKIISSGAKWEAeakeKIKNIF-PYAKLYEFYGASELSFVTALVdeeSERRPNS-- 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1791 ppIGVPVSGAALFVLDSWLRPVPAGVAGELYIAGAGVGVGYWRRAGLTASrfvacpfggSGARMYRT-GDLVCWRADGQL 1869
Cdd:PRK07638  309 --VGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARE---------LNADGWMTvRDVGYEDEEGFI 377

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1870 EFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRpgdkrlvgYATEIA----PGAVDPAGLRAQLAQRLPG 1945
Cdd:PRK07638  378 YIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDS--------YWGEKPvaiiKGSATKQQLKSFCLQRLSS 449

                         490       500
                  ....*....|....*....|....*.
gi 489495878 1946 YLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:PRK07638  450 FKIPKEWHFVDEIPYTNSGKIARMEA 475
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
 2110-2297 9.91e-07

uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, extended (e) SDRs; This subgroup contains proteins of unknown function related to aldehyde reductase and flavonoid reductase of the extended SDR-type. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187539 [Multi-domain]  Cd Length: 318  Bit Score: 53.44  E-value: 9.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2110 VLLTGATGFLGRYLVLELLRRldvDGRLICLVRAESDedarrrlektfdsgdpellrhFKELAADRLEVVAGDKSEPDLG 2189
Cdd:cd05228     1 ILVTGATGFLGSNLVRALLAQ---GYRVRALVRSGSD---------------------AVLLDGLPVEVVEGDLTDAASL 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2190 LDQPmwrrlaETVDLIVDSAAMVNAFPYH--ELFGPNVAGTAELIRIALTTKLKPFTYVSTADVGAAIEPSAFTEDADIR 2267
Cdd:cd05228    57 AAAM------KGCDRVFHLAAFTSLWAKDrkELYRTNVEGTRNVLDAALEAGVRRVVHTSSIAALGGPPDGRIDETTPWN 130

                         170       180       190
                  ....*....|....*....|....*....|
gi 489495878 2268 VISPtrtvdggwAGGYGTSKWAGEVLLREA 2297
Cdd:cd05228   131 ERPF--------PNDYYRSKLLAELEVLEA 152
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
 1623-1656 1.48e-06

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 53.58  E-value: 1.48e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 489495878 1623 TPPPMPAAVNLAYILYTSGTTGEPKGVGITHRNV 1656
Cdd:PLN02387  242 VDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNI 275
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
 538-853 1.77e-06

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 53.11  E-value: 1.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  538 VDVAATQLAVVGHDELRKVVDERVTQVTHDALLATKTAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVL 617
Cdd:PRK13388  116 LDLPGVRVLDVDTPAYAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCY 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  618 QCAPLTSDISVEEIFGGA-ACGARLVRSAAMKTGDLAALVDDLVARETTIVDLPTAVwqLLCADGDAIDAigRSRLRqIV 696
Cdd:PRK13388  196 VSMPLFHSNAVMAGWAPAvASGAAVALPAKFSASGFLDDVRRYGATYFNYVGKPLAY--ILATPERPDDA--DNPLR-VA 270

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  697 IGGEAircSAVDKwLESAASQGISLLSSYGPTEATVVatflpIVCDQTTMDGAllrLGRPIL------PNTV-------F 763
Cdd:PRK13388  271 FGNEA---SPRDI-AEFSRRFGCQVEDGYGSSEGAVI-----VVREPGTPPGS---IGRGAPgvaiynPETLtecavarF 338

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  764 LAFGEVV----IVGDLV----ADGYLGIDGDgfgtvTAADGSRRRA--FATGDRVTVDAEGFPVFSGRKDAVVKISGKRV 833
Cdd:PRK13388  339 DAHGALLnadeAIGELVntagAGFFEGYYNN-----PEATAERMRHgmYWSGDLAYRDADGWIYFAGRTADWMRVDGENL 413

                         330       340
                  ....*....|....*....|
gi 489495878  834 DIAEVTRRIAEDPAVSDVAV 853
Cdd:PRK13388  414 SAAPIERILLRHPAINRVAV 433
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
 569-910 2.01e-06

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 53.09  E-value: 2.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  569 LLATKTAYIMPTSGTTGQPK-LVRISHGSLAVFCDAISRAYGWGAHDtVLQCApltSDIS--VEE---IFGGAACGARLV 642
Cdd:cd05967   227 VAATDPLYILYTSGTTGKPKgVVRDNGGHAVALNWSMRNIYGIKPGD-VWWAA---SDVGwvVGHsyiVYGPLLHGATTV 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  643 RSAAMKTG--DLAA---LVDDlvARETTIVDLPTAVWQLLCAD--GDAIDAIGRSRLRQIVIGGEaiRC-SAVDKWLESA 714
Cdd:cd05967   303 LYEGKPVGtpDPGAfwrVIEK--YQVNALFTAPTAIRAIRKEDpdGKYIKKYDLSSLRTLFLAGE--RLdPPTLEWAENT 378

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  715 AsqGISLLSSYGPTEatvvaTFLPIVCDQTTMDGALLRLGRPILP----NTVFL----------AFGEVVIVGDLVADGY 780
Cdd:cd05967   379 L--GVPVIDHWWQTE-----TGWPITANPVGLEPLPIKAGSPGKPvpgyQVQVLdedgepvgpnELGNIVIKLPLPPGCL 451

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  781 LGIDGDGFGTVTAADGSRRRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAVelhsgsL 860
Cdd:cd05967   452 LTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAV------V 525

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489495878  861 GVW--FKSQRT------REGEQDAAAATR---IRLVLVSLG-VSSF-FVVGVPNIPRKPNGKI 910
Cdd:cd05967   526 GVRdeLKGQVPlglvvlKEGVKITAEELEkelVALVREQIGpVAAFrLVIFVKRLPKTRSGKI 588
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 1993-2057 2.05e-06

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 48.02  E-value: 2.05e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489495878   1993 VAGIFARVLGL---ERVGVDDSFFELGGDSLAAMRVIAAINTTLNADLPVRALLHASSTRGLSQLLGR 2057
Cdd:smart00823   17 VREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
 1638-1971 2.96e-06

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 52.45  E-value: 2.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1638 YTSGTTGEPKGVGITHR-NVTR-LFASLPARLSAAQVWSQCHSYG-FDASAWEI-WGALLGGGRLVIV-PESVAASpndF 1712
Cdd:PRK06018  184 YTSGTTGDPKGVLYSHRsNVLHaLMANNGDALGTSAADTMLPVVPlFHANSWGIaFSAPSMGTKLVMPgAKLDGAS---V 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1713 HGLLVAEHVSVLTQTPAAVAMLpTQGLESVAL--------VVAGEACPAALVDRWAPGRV-MLNAYGPTETTICAAISAp 1783
Cdd:PRK06018  261 YELLDTEKVTFTAGVPTVWLML-LQYMEKEGLklphlkmvVCGGSAMPRSMIKAFEDMGVeVRHAWGMTEMSPLGTLAA- 338

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1784 LRPG---------------SGMPPIGVPV-----SGAALfvldswlrPVPAGVAGELYIAGAGVGVGYWRRAG--LTASR 1841
Cdd:PRK06018  339 LKPPfsklpgdarldvlqkQGYPPFGVEMkitddAGKEL--------PWDGKTFGRLKVRGPAVAAAYYRVDGeiLDDDG 410

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1842 FvacpfggsgarmYRTGDLVCWRADGQLEFLGRTDDQVKIRG---YRIELGEVATALAELAgvgQAVVIAREDRPGDKRL 1918
Cdd:PRK06018  411 F------------FDTGDVATIDAYGYMRITDRSKDVIKSGGewiSSIDLENLAVGHPKVA---EAAVIGVYHPKWDERP 475

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489495878 1919 VgYATEIAPGaVDPAglRAQLAQRLPG----YLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:PRK06018  476 L-LIVQLKPG-ETAT--REEILKYMDGkiakWWMPDDVAFVDAIPHTATGKILKTAL 528
3b-HSD_HSDB1_like_SDR_e cd09811
human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, ...
 2111-2298 3.50e-06

human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, extended (e) SDRs; This extended-SDR subgroup includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7], and related proteins. These proteins have the characteristic active site tetrad and NAD(P)-binding motif of extended SDRs. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. C(27) 3beta-HSD is a membrane-bound enzyme of the endoplasmic reticulum, it catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187671 [Multi-domain]  Cd Length: 354  Bit Score: 51.74  E-value: 3.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2111 LLTGATGFLGRYLVLELLRRLDVDGRLiclvraesdedarRRLEKTFdsgDPELLRHF-KELAADRLEVVAGDKsepdlg 2189
Cdd:cd09811     3 LVTGGGGFLGQHIIRLLLERKEELKEI-------------RVLDKAF---GPELIEHFeKSQGKTYVTDIEGDI------ 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2190 LDQPMWRRLAETVDLIVDSAAMVNAF---PYHELFGPNVAGTAELIRIALTTKLKPFTYVSTADVGA--AIEPSAFTEDA 2264
Cdd:cd09811    61 KDLSFLFRACQGVSVVIHTAAIVDVFgppNYEELEEVNVNGTQAVLEACVQNNVKRLVYTSSIEVAGpnFKGRPIFNGVE 140

                         170       180       190
                  ....*....|....*....|....*....|....
gi 489495878 2265 DirviSPTRTVdggWAGGYGTSKWAGEVLLREAN 2298
Cdd:cd09811   141 D----TPYEDT---STPPYASSKLLAENIVLNAN 167
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
 472-853 3.80e-06

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 52.13  E-value: 3.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  472 VAWLVQRGAAPGDVLVFTDDDTDKTIDLLIACHLAGCGYSVCD---TADEISvrtnAITEHGDGILVTVVDVA----ATQ 544
Cdd:cd05923    42 AARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINprlKAAELA----ELIERGEMTAAVIAVDAqvmdAIF 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  545 LAVVGHDELRKVVDERVTQVTHDALLA-----TKTAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYG--WGAHDTVL 617
Cdd:cd05923   118 QSGVRVLALSDLVGLGEPESAGPLIEDpprepEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGlrHGRHNVVL 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  618 QCAPLTSDISVEEIFGGA-ACGARLVRSAAMKTGDLAALVDDLvaRETTIVDLPTAVWQLLCAdgdaIDAIGR--SRLRQ 694
Cdd:cd05923   198 GLMPLYHVIGFFAVLVAAlALDGTYVVVEEFDPADALKLIEQE--RVTSLFATPTHLDALAAA----AEFAGLklSSLRH 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  695 IVIGGEAIRCSAVDKwLESAASqgISLLSSYGPTEATvvaTFLpivCDQTTMDGALLRLGrpilpntvflAFGEVVIVGD 774
Cdd:cd05923   272 VTFAGATMPDAVLER-VNQHLP--GEKVNIYGTTEAM---NSL---YMRDARTGTEMRPG----------FFSEVRIVRI 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  775 LVADGYLGIDGDGFGTVTAADGS-----------------RRRAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAE 837
Cdd:cd05923   333 GGSPDEALANGEEGELIVAAAADaaftgylnqpeatakklQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSE 412

                         410
                  ....*....|....*.
gi 489495878  838 VTRRIAEDPAVSDVAV 853
Cdd:cd05923   413 IERVLSRHPGVTEVVV 428
PLN03051 PLN03051
acyl-activating enzyme; Provisional
 1618-1971 5.01e-06

acyl-activating enzyme; Provisional


Pssm-ID: 215552 [Multi-domain]  Cd Length: 499  Bit Score: 51.74  E-value: 5.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1618 AAYPGTPPPMP------AAVNLAYILYTSGTTGEPKGVGITH----RNVTRLFASLPARLSAAQVWSQchSYGFDASAWE 1687
Cdd:PLN03051  100 AAAQGSVGGNEyspvyaPVESVTNILFSSGTTGEPKAIPWTHlsplRCASDGWAHMDIQPGDVVCWPT--NLGWMMGPWL 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1688 IWGALLGGGRLVIVpeSVAASPNDFHGLLVAEHVSVLTQTPAAVAM------LPTQGLESVALVVAGEACPAALVDR--W 1759
Cdd:PLN03051  178 LYSAFLNGATLALY--GGAPLGRGFGKFVQDAGVTVLGLVPSIVKAwrhtgaFAMEGLDWSKLRVFASTGEASAVDDvlW 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1760 -----APGRVMLNAYGPTETTICAAISAPLRPgSGMPPIGVPVSGAALFVLDSWLRPVPAGVA--GELYIAGAGVGVG-Y 1831
Cdd:PLN03051  256 lssvrGYYKPVIEYCGGTELASGYISSTLLQP-QAPGAFSTASLGTRFVLLNDNGVPYPDDQPcvGEVALAPPMLGASdR 334

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1832 WRRAGLTASRFVACP-FGGSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYR---IELGEVATALAELAGVGQAVVI 1907
Cdd:PLN03051  335 LLNADHDKVYYKGMPmYGSKGMPLRRHGDIMKRTPGGYFCVQGRADDTMNLGGIKtssVEIERACDRAVAGIAETAAVGV 414

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489495878 1908 AREDrPGDKRLVGYAT----EIAPGAVDPAGLRAQLAQRLPGYLVP----AAVVVIDALPLTVNGKLDHRAL 1971
Cdd:PLN03051  415 APPD-GGPELLVIFLVlgeeKKGFDQARPEALQKKFQEAIQTNLNPlfkvSRVKIVPELPRNASNKLLRRVL 485
PRK13382 PRK13382
bile acid CoA ligase;
562-917 6.33e-06

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 51.68  E-value: 6.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  562 TQVTHDALLAT-----------KTAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEE 630
Cdd:PRK13382  175 HDLTVEVLIAAhagqrpeptgrKGRVILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGFSQ 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  631 IFGGAACGARLVRSAAMKTGDLAALVDDlvARETTIVDLPTAVWQLLCADGDAIDAIGRSRLRQIVIGGEAIRCSAVDKW 710
Cdd:PRK13382  255 LVLAASLACTIVTRRRFDPEATLDLIDR--HRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAF 332

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  711 LESAasqGISLLSSYGPTEATVVATFLPivCD-QTTMDGAllrlGRP-------IL-PNTVFLAFGEV---VIVGDLVAD 778
Cdd:PRK13382  333 MDQF---GDVIYNNYNATEAGMIATATP--ADlRAAPDTA----GRPaegteirILdQDFREVPTGEVgtiFVRNDTQFD 403

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  779 GYL-GIDGD---GFgtvtaadgsrrraFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV- 853
Cdd:PRK13382  404 GYTsGSTKDfhdGF-------------MASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVi 470

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489495878  854 ----ELHSGSLGVWF----KSQRTREgeqdaAAATRIRLVLVSLGVSSFFVVgVPNIPRKPNGKIDSDNLPR 917
Cdd:PRK13382  471 gvddEQYGQRLAAFVvlkpGASATPE-----TLKQHVRDNLANYKVPRDIVV-LDELPRGATGKILRRELQA 536
PRK09192 PRK09192
fatty acyl-AMP ligase;
1520-1654 9.01e-06

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 51.16  E-value: 9.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1520 YRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTG--AAYLPIdPANPPPRVAF------MLGDAVPV 1591
Cdd:PRK09192   52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGlvPVPLPL-PMGFGGRESYiaqlrgMLASAQPA 130

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1592 AAVTTAGLRSRLA----GHDLPII---DVVDALAAyPGTPPPMPAAVNLAYILYTSGTTGEPKGVGITHR 1654
Cdd:PRK09192  131 AIITPDELLPWVNeathGNPLLHVlshAWFKALPE-ADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHR 199
Arna_like_SDR_e cd05257
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme ...
 2109-2309 1.26e-05

Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme involved in the modification of outer membrane protein lipid A of gram-negative bacteria. It is a bifunctional enzyme that catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid and N-10-formyltetrahydrofolate-dependent formylation of UDP-4-amino-4-deoxy-l-arabinose; its NAD-dependent decaboxylating activity is in the C-terminal 360 residues. This subgroup belongs to the extended SDR family, however the NAD binding motif is not a perfect match and the upstream Asn of the canonical active site tetrad is not conserved. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187567 [Multi-domain]  Cd Length: 316  Bit Score: 49.61  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2109 TVLLTGATGFLGRYLVLELLRRldvdGrliCLVRAESDedarrrlektFDSGDPELLRHFKELaaDRLEVVAGDKSEPDL 2188
Cdd:cd05257     1 NVLVTGADGFIGSHLTERLLRE----G---HEVRALDI----------YNSFNSWGLLDNAVH--DRFHFISGDVRDASE 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2189 gldqpmWRRLAETVDLIVDSAAMVnAFPY-----HELFGPNVAGTAELIRIALTTKLKPFTYVSTADVGAAIEPSAFTED 2263
Cdd:cd05257    62 ------VEYLVKKCDVVFHLAALI-AIPYsytapLSYVETNVFGTLNVLEAACVLYRKRVVHTSTSEVYGTAQDVPIDED 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 489495878 2264 ADIRVISPTRtvdggWagGYGTSKWAGEvllREANDLCA---LPVAVFR 2309
Cdd:cd05257   135 HPLLYINKPR-----S--PYSASKQGAD---RLAYSYGRsfgLPVTIIR 173
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
1634-1971 2.97e-05

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 49.32  E-value: 2.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1634 AYILYTSGTTGEPKGVGITHR----NV--TRLFASLPAR---LSAAQVWsqcHSYGFDASaweIWGALLGGGRLVIVPes 1704
Cdd:PRK08043  368 ALILFTSGSEGHPKGVVHSHKsllaNVeqIKTIADFTPNdrfMSALPLF---HSFGLTVG---LFTPLLTGAEVFLYP-- 439

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1705 vaaSPndFHGLLVAEHV-----SVL--TQT----------PAAVAMLptqglesvALVVAG-----EACPAALVDRWapG 1762
Cdd:PRK08043  440 ---SP--LHYRIVPELVydrncTVLfgTSTflgnyarfanPYDFARL--------RYVVAGaeklqESTKQLWQDKF--G 504

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1763 RVMLNAYGPTETTICAAISAPL--RPGSgmppigvpvSGAALFVLDSWLRPVPaGVA--GELYIAGAGVGVGYWR--RAG 1836
Cdd:PRK08043  505 LRILEGYGVTECAPVVSINVPMaaKPGT---------VGRILPGMDARLLSVP-GIEqgGRLQLKGPNIMNGYLRveKPG 574

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1837 LTASRFVACPFGGSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDK 1916
Cdd:PRK08043  575 VLEVPTAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGE 654

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1917 RLVGYATeiapgavDPAGLRAQLAQR-----LPGYLVPAAVVVIDALPLTVNGKLDHRAL 1971
Cdd:PRK08043  655 ALVLFTT-------DSELTREKLQQYarehgVPELAVPRDIRYLKQLPLLGSGKPDFVTL 707
PLN02736 PLN02736
long-chain acyl-CoA synthetase
 1625-1655 3.55e-05

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 49.33  E-value: 3.55e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 489495878 1625 PPMPAAVnlAYILYTSGTTGEPKGVGITHRN 1655
Cdd:PLN02736  217 PPKPEDV--ATICYTSGTTGTPKGVVLTHGN 245
dTDP_GD_SDR_e cd05246
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4, ...
 2108-2310 3.86e-05

dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4,6-dehydratase and related proteins, members of the extended-SDR family, with the characteristic Rossmann fold core region, active site tetrad and NAD(P)-binding motif. dTDP-D-glucose 4,6-dehydratase is closely related to other sugar epimerases of the SDR family. dTDP-D-dlucose 4,6,-dehydratase catalyzes the second of four steps in the dTDP-L-rhamnose pathway (the dehydration of dTDP-D-glucose to dTDP-4-keto-6-deoxy-D-glucose) in the synthesis of L-rhamnose, a cell wall component of some pathogenic bacteria. In many gram negative bacteria, L-rhamnose is an important constituent of lipopoylsaccharide O-antigen. The larger N-terminal portion of dTDP-D-Glucose 4,6-dehydratase forms a Rossmann fold NAD-binding domain, while the C-terminus binds the sugar substrate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187557 [Multi-domain]  Cd Length: 315  Bit Score: 48.31  E-value: 3.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2108 RTVLLTGATGFLGRYLVLELLRRLDVDgRLICLvraesDedarrRLekTFdSGDPELLRHFKElaADRLEVVAGDKSepd 2187
Cdd:cd05246     1 MKILVTGGAGFIGSNFVRYLLNKYPDY-KIINL-----D-----KL--TY-AGNLENLEDVSS--SPRYRFVKGDIC--- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2188 lglDQPMWRRLAET--VDLIVDSAA-------MVNAFPYHELfgpNVAGTAELIRIALTTKLKPFTYVSTADV-GAAIEP 2257
Cdd:cd05246    62 ---DAELVDRLFEEekIDAVIHFAAeshvdrsISDPEPFIRT---NVLGTYTLLEAARKYGVKRFVHISTDEVyGDLLDD 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 489495878 2258 SAFTEDADIRVISPtrtvdggwaggYGTSKWAGEVLLREANDLCALPVAVFRC 2310
Cdd:cd05246   136 GEFTETSPLAPTSP-----------YSASKAAADLLVRAYHRTYGLPVVITRC 177
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
 1587-1668 4.48e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 48.82  E-value: 4.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1587 DAVPvAAVTTAGLRSrlaghdLPIIDVVD----ALAAYPGTPPPmpAAVNLAYILYTSGTTGEPKGVGITHRNVTRLFAS 1662
Cdd:PTZ00216  225 DSLP-ASVDTEGCRL------VAWTDVVAkghsAGSHHPLNIPE--NNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILA 295


                  ....*.
gi 489495878 1663 LPARLS 1668
Cdd:PTZ00216  296 LEDRLN 301
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
691-838 6.21e-05

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 48.55  E-value: 6.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  691 RLRQIVIGGEAIRCSAVDKWLESAasqGISLLSSYGPTE-ATVVATFLPIVCDQTTmdgallrLGRpILPN--TVFLAF- 766
Cdd:PRK08043  480 RLRYVVAGAEKLQESTKQLWQDKF---GLRILEGYGVTEcAPVVSINVPMAAKPGT-------VGR-ILPGmdARLLSVp 548

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  767 -----GEVVIVGDLVADGYLGIDGDGFGTVTAAD---GSRRRA-FATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAE 837
Cdd:PRK08043  549 gieqgGRLQLKGPNIMNGYLRVEKPGVLEVPTAEnarGEMERGwYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEM 628


                  .
gi 489495878  838 V 838
Cdd:PRK08043  629 V 629
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 2109-2313 8.09e-05

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 46.38  E-value: 8.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2109 TVLLTGATGFLGRYLVLELLRRldvDGRLICLVRaesdedarrrlektfdsgDPELLRHfkeLAADRLEVVAGDKSEPDl 2188
Cdd:COG0702     1 KILVTGATGFIGRRVVRALLAR---GHPVRALVR------------------DPEKAAA---LAAAGVEVVQGDLDDPE- 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2189 gldqpMWRRLAETVDLIVDsaamVNAFPYHELFGPNVAGTAELIRIALTTKLKPFTYVSTADvgaaiepsaftedadirv 2268
Cdd:COG0702    56 -----SLAAALAGVDAVFL----LVPSGPGGDFAVDVEGARNLADAAKAAGVKRIVYLSALG------------------ 108

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 489495878 2269 isptrtVDGGWAGGYGTSKWAGEVLLREAndlcALPVAVFRCGMI 2313
Cdd:COG0702   109 ------ADRDSPSPYLRAKAAVEEALRAS----GLPYTILRPGWF 143
3b-HSD-like_SDR_e cd05241
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family ...
 2109-2309 1.05e-04

3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family domains belonging to this subgroup have the characteristic active site tetrad and a fairly well-conserved NAD(P)-binding motif. 3b-HSD catalyzes the NAD-dependent conversion of various steroids, such as pregnenolone to progesterone, or androstenediol to testosterone. This subgroup includes an unusual bifunctional 3b-HSD/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. It also includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7]. C(27) 3beta-HSD/HSD3B7 is a membrane-bound enzyme of the endoplasmic reticulum, that catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human NSDHL (NAD(P)H steroid dehydrogenase-like protein) cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187552 [Multi-domain]  Cd Length: 331  Bit Score: 47.04  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2109 TVLLTGATGFLGRYLVLELLRRLDVDGRLiclvraesdedarrrlektFDSGDPELlrHFKELAADRLEVVAGDKSEPDl 2188
Cdd:cd05241     1 SVLVTGGSGFFGERLVKQLLERGGTYVRS-------------------FDIAPPGE--ALSAWQHPNIEFLKGDITDRN- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2189 gldqpMWRRLAETVDLIVDSAAMVNAFPYHELFGP-NVAGTAELIRIALTTKLKPFTYVSTADV---GAAIepsaFTEDA 2264
Cdd:cd05241    59 -----DVEQALSGADCVFHTAAIVPLAGPRDLYWEvNVGGTQNVLDACQRCGVQKFVYTSSSSVifgGQNI----HNGDE 129

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 489495878 2265 DIrvisPTRTVDggwAGGYGTSKWAGEVLLREANDLCALPVAVFR 2309
Cdd:cd05241   130 TL----PYPPLD---SDMYAETKAIAEIIVLEANGRDDLLTCALR 167
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
575-853 1.17e-04

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 47.57  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  575 AYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDIS-VEEIFGGAACGARLVRSAAMKTGDLA 653
Cdd:PRK05852  179 AMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGlIAALLATLASGGAVLLPARGRFSAHT 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  654 ALVDDLVARETTIVDLPTAVWQLLCADGDAIDAIGRSRLRQIViggeaiRCSAVdkwLESAASQ------GISLLSSYGP 727
Cdd:PRK05852  259 FWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIR------SCSAP---LTAETAQalqtefAAPVVCAFGM 329

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  728 TEATVVATFLPIVCDQTTMD------------GALLRL----GRPILPNTVflafGEVVIVGDLVADGYLGIDgdgfgTV 791
Cdd:PRK05852  330 TEATHQVTTTQIEGIGQTENpvvstglvgrstGAQIRIvgsdGLPLPAGAV----GEVWLRGTTVVRGYLGDP-----TI 400

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489495878  792 TAA---DGSRRrafaTGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:PRK05852  401 TAAnftDGWLR----TGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAV 461
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
2110-2299 1.40e-04

dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440708 [Multi-domain]  Cd Length: 279  Bit Score: 46.28  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2110 VLLTGATGFLGRYLVLELLRRldvDGRLICLVRAE---SDEDArrrLEKTFDSGDPELLRHfkeLAAdrleVVAGDK--S 2184
Cdd:COG1091     2 ILVTGANGQLGRALVRLLAER---GYEVVALDRSEldiTDPEA---VAALLEEVRPDVVIN---AAA----YTAVDKaeS 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2185 EPDLgldqpmwrrlAETVdlivdsaamvnafpyhelfgpNVAGTAELIRIALTTKLkPFTYVSTADV--GAAIEPsaFTE 2262
Cdd:COG1091    69 EPEL----------AYAV---------------------NATGPANLAEACAELGA-RLIHISTDYVfdGTKGTP--YTE 114

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 489495878 2263 DADIRVISPtrtvdggwaggYGTSKWAGEVLLREAND 2299
Cdd:COG1091   115 DDPPNPLNV-----------YGRSKLAGEQAVRAAGP 140
3Beta_HSD pfam01073
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid ...
 2111-2308 1.43e-04

3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase (3 beta-HSD) catalyzes the oxidation and isomerization of 5-ene-3 beta-hydroxypregnene and 5-ene-hydroxyandrostene steroid precursors into the corresponding 4-ene-ketosteroids necessary for the formation of all classes of steroid hormones.


Pssm-ID: 366449 [Multi-domain]  Cd Length: 279  Bit Score: 46.21  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2111 LLTGATGFLGRYLVLELLRRldvdGRLICLvraesdedarRRLEKTFdsgDPELLRHFKELaaDRLEVVAGD-KSEPDLg 2189
Cdd:pfam01073    1 VVTGGGGFLGRHIIKLLVRE----GELKEV----------RVFDLRE---SPELLEDFSKS--NVIKYIQGDvTDKDDL- 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2190 ldqpmwRRLAETVDLIVDSAAMVNAF---PYHELFGPNVAGTAELIRIALTTKLKPFTYVSTADVgaaIEPSAFTEdaDI 2266
Cdd:pfam01073   61 ------DNALEGVDVVIHTASAVDVFgkyTFDEIMKVNVKGTQNVLEACVKAGVRVLVYTSSAEV---VGPNSYGQ--PI 129

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 489495878  2267 RVISPTRTVDGGWAGGYGTSKWAGEVLLREANDL----------CAL-PVAVF 2308
Cdd:pfam01073  130 LNGDEETPYESTHQDAYPRSKAIAEKLVLKANGRplknggrlytCALrPAGIY 182
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
 573-853 1.47e-04

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 47.05  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  573 KTAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLtsdisvEEIFG-------GAACGARLVRSA 645
Cdd:cd05914    90 DVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPL------HHIYPltftlllPLLNGAHVVFLD 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  646 AMKTgdlaALVDDLVARETTIVDLPTAVWQLL-------------------------------CADGDAIDAIGrSRLRQ 694
Cdd:cd05914   164 KIPS----AKIIALAFAQVTPTLGVPVPLVIEkifkmdiipkltlkkfkfklakkinnrkirkLAFKKVHEAFG-GNIKE 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  695 IVIGGEAIRcSAVDKWLESAasqGISLLSSYGPTEATVVATFLP---IVCDQT--TMDGALLRLGRPIlPNTvflAFGEV 769
Cdd:cd05914   239 FVIGGAKIN-PDVEEFLRTI---GFPYTIGYGMTETAPIISYSPpnrIRLGSAgkVIDGVEVRIDSPD-PAT---GEGEI 310

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  770 VIVGDLVADGYLG--------IDGDGFgtvtaadgsrrraFATGDRVTVDAEGFPVFSGR-KDAVVKISGKRVDIAEVTR 840
Cdd:cd05914   311 IVRGPNVMKGYYKnpeataeaFDKDGW-------------FHTGDLGKIDAEGYLYIRGRkKEMIVLSSGKNIYPEEIEA 377

                         330
                  ....*....|....*
gi 489495878  841 RIAEDPAV--SDVAV 853
Cdd:cd05914   378 KINNMPFVleSLVVV 392
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
558-853 1.63e-04

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 46.58  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  558 DERVTQVTHDALLATK-----TAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYG----W-----GAHDTVLQcaplt 623
Cdd:PRK07824   16 DERRAALLRDALRVGEpidddVALVVATSGTTGTPKGAMLTAAALTASADATHDRLGgpgqWllalpAHHIAGLQ----- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  624 sdISVEEIFGGAACGARLVrSAAMKTGDLAALVDDLVA--RETTIVdlPTavwQLLCADGD--AIDAIgrSRLRQIVIGG 699
Cdd:PRK07824   91 --VLVRSVIAGSEPVELDV-SAGFDPTALPRAVAELGGgrRYTSLV--PM---QLAKALDDpaATAAL--AELDAVLVGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  700 EAIRCSAvdkwLESAASQGISLLSSYGPTEatvvaTFLPIVCDQTTMDGALLRLGRpilpntvflafGEVVIVGDLVADG 779
Cdd:PRK07824  161 GPAPAPV----LDAAAAAGINVVRTYGMSE-----TSGGCVYDGVPLDGVRVRVED-----------GRIALGGPTLAKG 220

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489495878  780 YLGIdgdgfgtVTAADGSRRRAFATGDRVTVDaEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:PRK07824  221 YRNP-------VDPDPFAEPGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAV 286
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
 576-853 1.78e-04

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 46.24  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  576 YIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVEEIF-----GGAACGarlvrsaaMKTG 650
Cdd:cd17633     4 YIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAIsalylGGTFIG--------QRKF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  651 DLAALVDDLVARETTIVDL-PTAVWQLLcadgdaidaigrsRLRQIVIGGEAIRCSAvDKWLESAASQ------GISLLS 723
Cdd:cd17633    76 NPKSWIRKINQYNATVIYLvPTMLQALA-------------RTLEPESKIKSIFSSG-QKLFESTKKKlknifpKANLIE 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  724 SYGPTEATVVaTFLpivCDQTTmdGALLRLGRPI------LPNTVFLAFGEVVIVGDLVADGYLgidgdgFGTVTAADGs 797
Cdd:cd17633   142 FYGTSELSFI-TYN---FNQES--RPPNSVGRPFpnveieIRNADGGEIGKIFVKSEMVFSGYV------RGGFSNPDG- 208

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 489495878  798 rrrAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:cd17633   209 ---WMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIV 261
PRK03584 PRK03584
acetoacetate--CoA ligase;
1517-1966 2.15e-04

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 46.71  E-value: 2.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1517 SMTYRELDEASNRLAHRLAGCGAGPGECVAllfercapavvamvavlktgaAYLPidpaNPPPRVAFMLG---------- 1586
Cdd:PRK03584  114 ELSWAELRRQVAALAAALRALGVGPGDRVA---------------------AYLP----NIPETVVAMLAtaslgaiwss 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1587 -------DAV--------PVAAVTTAG----------------LRSRL-------------AGHDLPIIDVV----DALA 1618
Cdd:PRK03584  169 cspdfgvQGVldrfgqiePKVLIAVDGyryggkafdrrakvaeLRAALpslehvvvvpylgPAAAAAALPGAllweDFLA 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1619 AYPGTPP---PMPAAVNLaYILYTSGTTGEPKGV-----GIT---------HRNVT---RLFaslparlsaaqvWsqchs 1678
Cdd:PRK03584  249 PAEAAELefePVPFDHPL-WILYSSGTTGLPKCIvhghgGILlehlkelglHCDLGpgdRFF------------W----- 310

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1679 ygFDASAWEIW----GALLGGGRLVIVPES-VAASPNDFHGLLVAEHVSVLTQTPAAVAMLPTQGLEsvalvvageacpa 1753
Cdd:PRK03584  311 --YTTCGWMMWnwlvSGLLVGATLVLYDGSpFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLV------------- 375

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1754 alvdrwaPGRVM----LNAYGPTetticaaisaplrpGSGMPPIG--------------VPVSG----AALFVLDSWLRP 1811
Cdd:PRK03584  376 -------PGETHdlsaLRTIGST--------------GSPLPPEGfdwvyehvkadvwlASISGgtdiCSCFVGGNPLLP 434

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1812 VpagVAGELYIAGAGVGVGYWRRAG-----------LTASrFVACPFG----GSGAR-------MY----RTGDLVCWRA 1865
Cdd:PRK03584  435 V---YRGEIQCRGLGMAVEAWDEDGrpvvgevgelvCTKP-FPSMPLGfwndPDGSRyrdayfdTFpgvwRHGDWIEITE 510

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1866 DGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAREDRPGDKRLVGYATeIAPGAVDPAGLRAQLAQRLPG 1945
Cdd:PRK03584  511 HGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVV-LAEGVTLDDALRARIRTTIRT 589

                         570       580
                  ....*....|....*....|....*
gi 489495878 1946 YL----VPAAVVVIDALPLTVNGKL 1966
Cdd:PRK03584  590 NLsprhVPDKIIAVPDIPRTLSGKK 614
PRK07867 PRK07867
acyl-CoA synthetase; Validated
 580-853 2.16e-04

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 46.60  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  580 TSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDISVeeIFG---GAACGARLVRSAAMKTGDLAALV 656
Cdd:PRK07867  160 TSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAV--MAGwavALAAGASIALRRKFSASGFLPDV 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  657 DDLVARETTIVDLPTAVwqLLCADGDAIDAigRSRLRqIVIGGEAircSAVDKwLESAASQGISLLSSYGPTEATVVATF 736
Cdd:PRK07867  238 RRYGATYANYVGKPLSY--VLATPERPDDA--DNPLR-IVYGNEG---APGDI-ARFARRFGCVVVDGFGSTEGGVAITR 308

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  737 LPivcdqTTMDGALLRLGRPI----------LPNTVFLAFGEV---VIVGDLVadgylGIDG----DGFGTVTAADGSRR 799
Cdd:PRK07867  309 TP-----DTPPGALGPLPPGVaivdpdtgteCPPAEDADGRLLnadEAIGELV-----NTAGpggfEGYYNDPEADAERM 378

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 489495878  800 RA--FATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:PRK07867  379 RGgvYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAV 434
PRK09088 PRK09088
acyl-CoA synthetase; Validated
 472-926 3.27e-04

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 45.95  E-value: 3.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  472 VAWLVQRGAAPGDVLVFTDDDTDKTIDLLIACHLAGCGYSVCD---TADEIsvrtNAITEHGD-GILVTVVDVAATQLAV 547
Cdd:PRK09088   36 AAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNwrlSASEL----DALLQDAEpRLLLGDDAVAAGRTDV 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  548 VGHDELRKVVDErVTQVTHDALLATKTAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDI- 626
Cdd:PRK09088  112 EDLAAFIASADA-LEPADTPSIPPERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIg 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  627 ---SVEEIFggAACGARLVRSAAMKTGDLAALVDDLVAReTTIVDLPTAVWQLlcADGDAIDAIGRSRLRQIVIGGEAIR 703
Cdd:PRK09088  191 litSVRPVL--AVGGSILVSNGFEPKRTLGRLGDPALGI-THYFCVPQMAQAF--RAQPGFDAAALRHLTALFTGGAPHA 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  704 CSAVDKWLEsaasQGISLLSSYGPTEAtvvATFLPIVCDQTTMDGallRLGRPILPN-TVFLAF-------------GEV 769
Cdd:PRK09088  266 AEDILGWLD----DGIPMVDGFGMSEA---GTVFGMSVDCDVIRA---KAGAAGIPTpTVQTRVvddqgndcpagvpGEL 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  770 VIVGDLVADGYLGiDGDGFGTVTAADGsrrrAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVS 849
Cdd:PRK09088  336 LLRGPNLSPGYWR-RPQATARAFTGDG----WFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIR 410

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  850 DVAV----ELHSGSLGVWFKSQRTREGEQDAAAATRIRLVLVSLGVSSFFVVgVPNIPRKPNGKIDSdnlPRLPQWSAAG 925
Cdd:PRK09088  411 ECAVvgmaDAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRL-VDALPRTASGKLQK---ARLRDALAAG 486


                  .
gi 489495878  926 L 926
Cdd:PRK09088  487 R 487
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
 577-853 3.40e-04

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 45.81  E-value: 3.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  577 IMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPLTSDIsveeifgGAACGARL--VRSAAMKTGDL-- 652
Cdd:PRK13295  202 LIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQT-------GFMYGLMMpvMLGATAVLQDIwd 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  653 AALVDDLVARE---------TTIVDLPTAVwqllcadgdAIDAIGRSRLRQIVIGGEAIRCSAVDKwleSAASQGISLLS 723
Cdd:PRK13295  275 PARAAELIRTEgvtftmastPFLTDLTRAV---------KESGRPVSSLRTFLCAGAPIPGALVER---ARAALGAKIVS 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  724 SYGPTEATVVATFLP-------IVCDQTTMDGALLRL----GRPILPNTVflafGEVVIVGDLVADGYLGIDGdgfGTVT 792
Cdd:PRK13295  343 AWGMTENGAVTLTKLddpderaSTTDGCPLPGVEVRVvdadGAPLPAGQI----GRLQVRGCSNFGGYLKRPQ---LNGT 415

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489495878  793 AADGsrrrAFATGDRVTVDAEGFPVFSGR-KDAVVKiSGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:PRK13295  416 DADG----WFDTGDLARIDADGYIRISGRsKDVIIR-GGENIPVVEIEALLYRHPAIAQVAI 472
PLN02430 PLN02430
long-chain-fatty-acid-CoA ligase
 1623-1657 3.74e-04

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178049 [Multi-domain]  Cd Length: 660  Bit Score: 45.96  E-value: 3.74e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 489495878 1623 TPPPMPaaVNLAYILYTSGTTGEPKGVGITHRNVT 1657
Cdd:PLN02430  214 TNPPKP--LDICTIMYTSGTSGDPKGVVLTHEAVA 246
PLN02246 PLN02246
4-coumarate--CoA ligase
 1503-1656 4.27e-04

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 45.74  E-value: 4.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1503 ARIPE-AEAVCCGDAS----MTYRELDEASNRLAHRLAGCGAGPGECVALLFERCAPAVVAMVAVLKTGAAylpIDPANP 1577
Cdd:PLN02246   31 ERLSEfSDRPCLIDGAtgrvYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAV---TTTANP 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1578 ---PPRVAFMLGDAVPVAAVTTAG----LRSRLAGHDLPIIDVVDA----------LAAYPGTPPPMP-AAVNLAYILYT 1639
Cdd:PLN02246  108 fytPAEIAKQAKASGAKLIITQSCyvdkLKGLAEDDGVTVVTIDDPpegclhfselTQADENELPEVEiSPDDVVALPYS 187

                         170
                  ....*....|....*..
gi 489495878 1640 SGTTGEPKGVGITHRNV 1656
Cdd:PLN02246  188 SGTTGLPKGVMLTHKGL 204
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
 1639-1954 5.33e-04

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 45.14  E-value: 5.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1639 TSGTTGEPKGVGIThRNVTRLFASLPAR-LSAA--------QVwsqCHSYGFDASAWeiwGALLGGGRL--VIVPESVaa 1707
Cdd:COG1541    91 SSGTTGKPTVVGYT-RKDLDRWAELFARsLRAAgvrpgdrvQN---AFGYGLFTGGL---GLHYGAERLgaTVIPAGG-- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1708 spndfhG-------LLVAEHVSVLTQTP--------AAVAM---LPTQGLEsvALVVAGEACP----AALVDRWapGRVM 1765
Cdd:COG1541   162 ------GnterqlrLMQDFGPTVLVGTPsyllylaeVAEEEgidPRDLSLK--KGIFGGEPWSeemrKEIEERW--GIKA 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1766 LNAYGPTETTICAAISAPLRPGSGMPPIGV------PVSGaalfvldswlRPVPAGVAGELYIagagvgvgywrraglTA 1839
Cdd:COG1541   232 YDIYGLTEVGPGVAYECEAQDGLHIWEDHFlveiidPETG----------EPVPEGEEGELVV---------------TT 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1840 SRFVACPfggsgarM--YRTGDLVCW------------RADGqleFLGRTDDQVKIRGYRIELGEVATALAELAGVGQA- 1904
Cdd:COG1541   287 LTKEAMP-------LirYRTGDLTRLlpepcpcgrthpRIGR---ILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEy 356

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489495878 1905 -VVIAREDRPgDKRLVgyATEIAPGAvDPAGLRAQLAQRLPGYL-VPAAVVV 1954
Cdd:COG1541   357 qIVVDREGGL-DELTV--RVELAPGA-SLEALAEAIAAALKAVLgLRAEVEL 404
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
 1597-1659 5.87e-04

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 45.14  E-value: 5.87e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489495878 1597 AGLRSRLAGHDLPIIdVVDALAAYPGTPPPMPAAVN------LAYILYTSGTTGEPKGVGITHRNVTRL 1659
Cdd:cd17632   184 ESARERLAAVGIPVT-TLTLIAVRGRDLPPAPLFRPepdddpLALLIYTSGSTGTPKGAMYTERLVATF 251
PLN02657 PLN02657
3,8-divinyl protochlorophyllide a 8-vinyl reductase
 2091-2186 9.11e-04

3,8-divinyl protochlorophyllide a 8-vinyl reductase


Pssm-ID: 178263 [Multi-domain]  Cd Length: 390  Bit Score: 44.37  E-value: 9.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2091 ADTLATAVNLPGPSPELRTVLLTGATGFLGRYLVLELLRRldvdG-RLICLVRAESDEDARRRLEKTFDSGDPELLRHFK 2169
Cdd:PLN02657   44 ATAAAAAQSFRSKEPKDVTVLVVGATGYIGKFVVRELVRR----GyNVVAVAREKSGIRGKNGKEDTKKELPGAEVVFGD 119

                          90
                  ....*....|....*..
gi 489495878 2170 ELAADRLEVVAGDKSEP 2186
Cdd:PLN02657  120 VTDADSLRKVLFSEGDP 136
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
 799-853 9.45e-04

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 44.50  E-value: 9.45e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  799 RRAFA-----TGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:PRK04319  426 ESYFAgdwyvSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGV 485
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
 580-844 9.58e-04

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 44.37  E-value: 9.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  580 TSGTTGQPKLVRISHGSLAVFCDAISRAY---GWGAHDTVLQCAPL---TSDISVEEifGGAACGARLVRSAAMKTGDLA 653
Cdd:COG1541    91 SSGTTGKPTVVGYTRKDLDRWAELFARSLraaGVRPGDRVQNAFGYglfTGGLGLHY--GAERLGATVIPAGGGNTERQL 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  654 ALVDDLvaRETTIVDLPTAVWQLlcadGDAIDAIG----RSRLRQIVIGGEAIRCSAVdKWLESAAsqGISLLSSYGPTE 729
Cdd:COG1541   169 RLMQDF--GPTVLVGTPSYLLYL----AEVAEEEGidprDLSLKKGIFGGEPWSEEMR-KEIEERW--GIKAYDIYGLTE 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  730 ATV-VAT--------------FLPIVCDQTTmdgallrlGRPilpntvfLAFGEvviVGDLVadgylgidgdgFGTVTaa 794
Cdd:COG1541   240 VGPgVAYeceaqdglhiwedhFLVEIIDPET--------GEP-------VPEGE---EGELV-----------VTTLT-- 288

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489495878  795 dgsrRRA-----FATGDRVTVDAE------GFPVFS---GRKDAVVKISGKRV---DIAEVTRRIAE 844
Cdd:COG1541   289 ----KEAmplirYRTGDLTRLLPEpcpcgrTHPRIGrilGRADDMLIIRGVNVfpsQIEEVLLRIPE 351
RmlD_sub_bind pfam04321
RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some ...
 2110-2298 1.15e-03

RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some bacteria. Its precursor, dTDP-L-rhamnose, is synthesized by four different enzymes the final one of which is RmlD. The RmlD substrate binding domain is responsible for binding a sugar nucleotide.


Pssm-ID: 427865 [Multi-domain]  Cd Length: 284  Bit Score: 43.42  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2110 VLLTGATGFLGRylvlELLRRLDVDGR-LICLVRAESDEDARRRLEKTFDSGDPELLRHfkeLAADRlevvAGDKSEPDl 2188
Cdd:pfam04321    1 ILITGANGQLGT----ELRRLLAERGIeVVALTRAELDLTDPEAVARLLREIKPDVVVN---AAAYT----AVDKAESE- 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  2189 gldqpmwRRLAETVdlivdsaamvnafpyhelfgpNVAGTAELIRIALTTKLkPFTYVSTADVGAAIEPSAFTEDAdirv 2268
Cdd:pfam04321   69 -------PDLAYAI---------------------NALAPANLAEACAAVGA-PLIHISTDYVFDGTKPRPYEEDD---- 115

                          170       180       190
                   ....*....|....*....|....*....|
gi 489495878  2269 isPTRTVdggwaGGYGTSKWAGEVLLREAN 2298
Cdd:pfam04321  116 --ETNPL-----NVYGRTKLAGEQAVRAAG 138
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
 473-622 1.66e-03

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 43.81  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  473 AWLVQRGAAPGDVLVFTDDDTDKTIDLLIACHLAG---CGYSVCDTADEISVRTNAItEH-----GDGILVT---VVDVA 541
Cdd:cd05906    54 AGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGfvpAPLTVPPTYDEPNARLRKL-RHiwqllGSPVVLTdaeLVAEF 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  542 ATQLAVVGHDELRKVVDERVTQVTHDALLATKT----AYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVL 617
Cdd:cd05906   133 AGLETLSGLPGIRVLSIEELLDTAADHDLPQSRpddlALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFL 212


                  ....*
gi 489495878  618 QCAPL 622
Cdd:cd05906   213 NWVPL 217
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
 805-852 3.11e-03

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 42.86  E-value: 3.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 489495878  805 GDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVA 852
Cdd:cd05968   476 GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESA 523
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
1768-1966 3.45e-03

long-chain-fatty acid--ACP ligase MbtM;


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 42.45  E-value: 3.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1768 AYGPTETTiCAaISAPlRPGSG-------MPPIGVP----VSGAALFVLDSWLRPV--PAGVA----GELYIAGAGVGVG 1830
Cdd:PRK05851  309 SYGLAEST-CA-VTVP-VPGIGlrvdevtTDDGSGArrhaVLGNPIPGMEVRISPGdgAAGVAgreiGEIEIRGASMMSG 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1831 YWRRAGLTASRFvacpfggsgarmYRTGDLvCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGV--GQAVVIA 1908
Cdd:PRK05851  386 YLGQAPIDPDDW------------FPTGDL-GYLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVreGAVVAVG 452

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489495878 1909 REDRPGDKRLVGYATEIAPgavDPAGLRAQLAQRLPGY--LVPAAVVVID--ALPLTVNGKL 1966
Cdd:PRK05851  453 TGEGSARPGLVIAAEFRGP---DEAGARSEVVQRVASEcgVVPSDVVFVApgSLPRTSSGKL 511
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
 2108-2248 4.31e-03

UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; UDP-Glcnac inverting 4,6-dehydratase was identified in Helicobacter pylori as the hexameric flaA1 gene product (FlaA1). FlaA1 is hexameric, possesses UDP-GlcNAc-inverting 4,6-dehydratase activity, and catalyzes the first step in the creation of a pseudaminic acid derivative in protein glycosylation. Although this subgroup has the NADP-binding motif characteristic of extended SDRs, its members tend to have a Met substituted for the active site Tyr found in most SDR families. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187548 [Multi-domain]  Cd Length: 287  Bit Score: 41.84  E-value: 4.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2108 RTVLLTGATGFLGRYLVLELLRRldVDGRLICLVRAESDEDarrrlektfdsgdpELLRHFKEL-AADRLEVVAGDKSEP 2186
Cdd:cd05237     3 KTILVTGGAGSIGSELVRQILKF--GPKKLIVFDRDENKLH--------------ELVRELRSRfPHDKLRFIIGDVRDK 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489495878 2187 DLgldQPMWRRLAEtVDLIVDSAAM--VNA--FPYHELFGPNVAGTAELIRIALTTKLKPFTYVST 2248
Cdd:cd05237    67 ER---LRRAFKERG-PDIVFHAAALkhVPSmeDNPEEAIKTNVLGTKNVIDAAIENGVEKFVCIST 128
PRK09192 PRK09192
fatty acyl-AMP ligase;
505-739 4.52e-03

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 42.30  E-value: 4.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  505 LAGCGYSVCDTADEISVRTNAITEHGDGilvtVVDVAATQLAvvghdeLRKVVDERVTQVTHDALlatktAYIMPTSGTT 584
Cdd:PRK09192  124 LASAQPAAIITPDELLPWVNEATHGNPL----LHVLSHAWFK------ALPEADVALPRPTPDDI-----AYLQYSSGST 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  585 GQPKLVRISHGSLAVFCDAIS----------RAYGWGA--HDTVLQ---CAPLTSDISVEeifggaacgarlvrsaAMKT 649
Cdd:PRK09192  189 RFPRGVIITHRALMANLRAIShdglkvrpgdRCVSWLPfyHDMGLVgflLTPVATQLSVD----------------YLPT 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  650 GD-----LAALvdDLVAR-ETTIVDLPTAVWQlLCA---DGDAIDAIGRSRLRQIVIGGEAIRCSAVDKWLESAASQGIS 720
Cdd:PRK09192  253 RDfarrpLQWL--DLISRnRGTISYSPPFGYE-LCArrvNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAFAPAGFD 329

                         250       260
                  ....*....|....*....|..
gi 489495878  721 ---LLSSYGPTEATVVATFLPI 739
Cdd:PRK09192  330 dkaFMPSYGLAEATLAVSFSPL 351
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
 575-667 4.60e-03

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 42.20  E-value: 4.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  575 AYIMPTSGTTGQPKLVRISHGSL----AVFCDAISRAYGWGAHDTVLQCAPLtsdisveeifggAACGARLVRSAAMK-- 648
Cdd:cd05927   117 ATICYTSGTTGNPKGVMLTHGNIvsnvAGVFKILEILNKINPTDVYISYLPL------------AHIFERVVEALFLYhg 184

                          90       100
                  ....*....|....*....|....*
gi 489495878  649 ------TGDLAALVDDLVARETTIV 667
Cdd:cd05927   185 akigfySGDIRLLLDDIKALKPTVF 209
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
 690-853 5.06e-03

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 42.12  E-value: 5.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  690 SRLRQIVIGGEAIRCSAVDKWlesAASQGISLLSSYGPTEATVVATFLPIvcdqttmdGALLRLGR---PIlPNTVF--- 763
Cdd:PRK12492  333 SALKLTNSGGTALVKATAERW---EQLTGCTIVEGYGLTETSPVASTNPY--------GELARLGTvgiPV-PGTALkvi 400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878  764 ------LAFGE---VVIVGDLVADGYLGiDGDGFGTVTAADGsrrrAFATGDRVTVDAEGFPVFSGRKDAVVKISGKRVD 834
Cdd:PRK12492  401 dddgneLPLGErgeLCIKGPQVMKGYWQ-QPEATAEALDAEG----WFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVY 475

                         170
                  ....*....|....*....
gi 489495878  835 IAEVTRRIAEDPAVSDVAV 853
Cdd:PRK12492  476 PNEIEDVVMAHPKVANCAA 494
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
 574-605 5.31e-03

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 42.27  E-value: 5.31e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 489495878  574 TAYIMPTSGTTGQPKLVRISHGSLAVFCDAIS 605
Cdd:PTZ00216  266 LALIMYTSGTTGDPKGVMHTHGSLTAGILALE 297
ArgR-Cyc_NRPS-like cd20480
Cyc (heterocyclization)-like domain of Vibrio anguillarum AngR and similar proteins; belongs ...
 1217-1360 5.74e-03

Cyc (heterocyclization)-like domain of Vibrio anguillarum AngR and similar proteins; belongs to the Condensation-domain family; Vibrio anguillarum AngR plays a role in regulating the expression of iron transport genes as well as in the production of the siderophore anguibactin. Cyc-domains are a type of Condensation (C) domain. Cyc-domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have a alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. Members of this subfamily have an SxxxD motif at the active site. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to Cyc-domains there are various other subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380470 [Multi-domain]  Cd Length: 406  Bit Score: 41.72  E-value: 5.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1217 AYWENALAGMPERLRLPTARPyPPVADQRGASL-VVDWPASVQQQVRRIARQHNATSFMVVAAGLAVLLSKLSGSPDVAV 1295
Cdd:cd20480   182 AFWNEQILQLPSSANLPTVCE-PEKLRETGITRrTLTLSSDKWQQLVTISKQHNVTPELTLASIFSAVLSLWGNQKDMML 260

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489495878 1296 GFPIAGRSDPAldNLVGFFVNTLVlrVNLAG-DPSFAELLGQVRARSLAAYENQDVPFEVLVDRLK 1360
Cdd:cd20480   261 RFDLNKKNDVA--GVIGQFTQPLL--VGLSGfGQSFLSLVKENQKHFEQAYPFRQIPIFDLVRQLA 322
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
 2109-2437 5.88e-03

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187579 [Multi-domain]  Cd Length: 273  Bit Score: 41.08  E-value: 5.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2109 TVLLTGATGFLGRYLVLELLRRldvdG-RLICLVRaesDEDARRRLEKTFDSGdpellrhfkelaadRLEVVAGDKSEPD 2187
Cdd:cd05271     2 VVTVFGATGFIGRYVVNRLAKR----GsQVIVPYR---CEAYARRLLVMGDLG--------------QVLFVEFDLRDDE 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2188 lgldqpMWRRLAETVDLIVDSAAMVNAFPYHELFGPNVAGTAELIRIALTTKLKPFTYVSTAdvGAaiepsafteDADir 2267
Cdd:cd05271    61 ------SIRKALEGSDVVINLVGRLYETKNFSFEDVHVEGPERLAKAAKEAGVERLIHISAL--GA---------DAN-- 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2268 viSPTRtvdggwaggYGTSKWAGEVLLREandlcALPVAV-FRCGMILADTSYagqlnmsdWVTRMVLSLMATGIAPRsf 2346
Cdd:cd05271   122 --SPSK---------YLRSKAEGEEAVRE-----AFPEATiVRPSVVFGREDR--------FLNRFAKLLAFLPFPPL-- 175

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2347 yePDSEGNRQRahfdglPVTF--VAEAIAVLgarVAGSSLAGfATYHVMNPHddGIGLDEYVDWLIEAGYPIRRIDDFAE 2424
Cdd:cd05271   176 --IGGGQTKFQ------PVYVgdVAEAIARA---LKDPETEG-KTYELVGPK--VYTLAELVELLRRLGGRKRRVLPLPL 241

                         330
                  ....*....|...
gi 489495878 2425 WLQRFEASLGALP 2437
Cdd:cd05271   242 WLARLIARVKLLL 254
3b-HSD-NSDHL-like_SDR_e cd09813
human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This ...
 2109-2308 5.88e-03

human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This subgroup includes human NSDHL and related proteins. These proteins have the characteristic active site tetrad of extended SDRs, and also have a close match to their NAD(P)-binding motif. Human NSDHL is a 3beta-hydroxysteroid dehydrogenase (3 beta-HSD) which functions in the cholesterol biosynthetic pathway. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. Mutations in the gene encoding NSDHL cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. This subgroup also includes an unusual bifunctional [3beta-hydroxysteroid dehydrogenase (3b-HSD)/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187673 [Multi-domain]  Cd Length: 335  Bit Score: 41.58  E-value: 5.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2109 TVLLTGATGFLGRYLVLELLRRLdvdgrlICLVRAesdedarrrlektFDSGDPELLRHFKElaaDRLEVVAGDKSEPDl 2188
Cdd:cd09813     1 SCLVVGGSGFLGRHLVEQLLRRG------NPTVHV-------------FDIRPTFELDPSSS---GRVQFHTGDLTDPQ- 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2189 gldQPMWRRLAETVDLIVDSAAMVNAFPYHELFGPNVAGTAELIRIALTTKLKPFTYVSTADVgaaIEPSAFTEDADIRV 2268
Cdd:cd09813    58 ---DLEKAFNEKGPNVVFHTASPDHGSNDDLYYKVNVQGTRNVIEACRKCGVKKLVYTSSASV---VFNGQDIINGDESL 131

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 489495878 2269 ISPTRTVDggwagGYGTSKWAGEVLLREAND------LCAL-PVAVF 2308
Cdd:cd09813   132 PYPDKHQD-----AYNETKALAEKLVLKANDpesgllTCALrPAGIF 173
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
 551-622 6.05e-03

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 41.89  E-value: 6.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489495878  551 DELRKVVDERVTQVTHDALLATKTAYIMPTSGTTGQPKLVRISHGSLaVFCDAISRAYGWGAHDTVLQCAPL 622
Cdd:cd05938   123 DKVDAASDEPVPASLRAHVTIKSPALYIYTSGTTGLPKAARISHLRV-LQCSGFLSLCGVTADDVIYITLPL 193
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
 1689-1972 6.07e-03

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 41.52  E-value: 6.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1689 WGALLGGGRLVIVP-------ESVAASPNDFHGLLVAEHVSVLTQtpaavamLPTQGLESVALVVAGEAcPA--ALVD-- 1757
Cdd:PRK07445  179 MRSFLTGGKLVILPykrlksgQELPPNPSDFFLSLVPTQLQRLLQ-------LRPQWLAQFRTILLGGA-PAwpSLLEqa 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1758 -----RWAPgrvmlnAYGPTETticAAISAPLRPG---SGMPPIGVPVSGAALfvldswlrPVPAGVAGELYIAGAGVGV 1829
Cdd:PRK07445  251 rqlqlRLAP------TYGMTET---ASQIATLKPDdflAGNNSSGQVLPHAQI--------TIPANQTGNITIQAQSLAL 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 1830 GYWrragltasrfvacPFGGSGARMYRTGDLVCWRADGQLEFLGRTDDQVKIRGYRIELGEVATALAELAGVGQAVVIAR 1909
Cdd:PRK07445  314 GYY-------------PQILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGL 380

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489495878 1910 EDRPGDKRLVgyATEI-APGAVDPAGLRAQLAQRLPGYLVPAAVVVIDALPLTVNGKLDHRALP 1972
Cdd:PRK07445  381 PDPHWGEVVT--AIYVpKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
 575-622 6.83e-03

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 41.43  E-value: 6.83e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 489495878  575 AYIMPTSGTTGQPKLVRISHGSLAVFCDAIS-RAYGW-GAHDTVLQCAPL 622
Cdd:cd17639    91 ACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGdRVPELlGPDDRYLAYLPL 140
AR_SDR_e cd05227
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ...
 2109-2257 6.83e-03

aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the extended SDR-type and related proteins. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187538 [Multi-domain]  Cd Length: 301  Bit Score: 41.10  E-value: 6.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2109 TVLLTGATGFLGRYLVLELLRRldvdgrlICLVRAE-SDEDARRRLEKTFDSGDPEllrhfkelaaDRLEVVAgdksepd 2187
Cdd:cd05227     1 LVLVTGATGFIASHIVEQLLKA-------GYKVRGTvRSLSKSAKLKALLKAAGYN----------DRLEFVI------- 56

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495878 2188 lgldqpmwrrlaetVDLIVDSAAmvnafpyhelFGPNVAGTAELIRIAlttklKPFTYVSTADVGAAIEP 2257
Cdd:cd05227    57 --------------VDDLTAPNA----------WDEALKGVDYVIHVA-----SPFPFTGPDAEDDVIDP 97
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
 802-853 7.48e-03

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 41.39  E-value: 7.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489495878  802 FATGDRVTVDAEGFPVFSGRKDAVVKISGKRVDIAEVTRRIAEDPAVSDVAV 853
Cdd:cd05966   471 YFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAV 522
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
 568-622 7.94e-03

bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341296 [Multi-domain]  Cd Length: 569  Bit Score: 41.64  E-value: 7.94e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 489495878  568 ALLATK---TAYIMPTSGTTGQPKLVRISHGSLAVFCDAISRAYGWGAHDTVLQCAPL 622
Cdd:cd17641   151 EVAAGKgedVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPL 208
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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