NCBI Conserved Domain Search

Conserved domains on [gi|602182148|gb|AHN91582|]

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mixed NRPS/PKS [Cylindrospermopsis raciborskii CHAB3438]

Protein Classification

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

PksD

COG3321

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...

673-2008

0e+00

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];

Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 1312.56 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  673 DSNDIAIISVAGRFPGAETIEQFWHNLCNGVESITLFSDDKLEQTL----PELFNNPAYVKAGAVLEGVELFDATFFGYS 748
Cdd:COG3321     2 ADEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWDADAyydpDPDAPGKTYVRWGGFLDDVDEFDALFFGIS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  749 PKEAAVTDPQQRILLECAWEAFERAGYNPETYP-EPVGVYAGSSLSTYLLNNIGSALGIiteqpfietdmeQFQAKIGND 827
Cdd:COG3321    82 PREAEAMDPQQRLLLEVAWEALEDAGYDPESLAgSRTGVFVGASSNDYALLLLADPEAI------------DAYALTGNA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  828 RSYLATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQKGGYLYEEGMVRSQDGHCRAFD 907
Cdd:COG3321   150 KSVLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFD 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  908 AEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGAIKmGYTAPSVDGQADVISEAIAIADIDASTIGYVEA 987
Cdd:COG3321   230 ADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSN-GLTAPNGPAQAAVIRRALADAGVDPATVDYVEA 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  988 HGTATQLGDPIEVAGLARAFQRSTDsvlGKQQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPRID 1067
Cdd:COG3321   309 HGTGTPLGDPIEAAALTAAFGQGRP---ADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHID 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1068 FDATPFFVNTELREWSRNGYPRRAGVSSFGVGGTNSHIVLEESPVKQPTlfSSLPERSHHLLTLSAHTQEALHELVQRYI 1147
Cdd:COG3321   386 FENSPFYVNTELRPWPAGGGPRRAGVSSFGFGGTNAHVVLEEAPAAAPA--AAAAARPPQLLVLSAKTEEALRALAARLA 463

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1148 QHNETHLDIDLGDLCFTANTGRKHFEHRLAVVAESIPGLQAQLETAQTAISAQ-----KKNAPPTIAFLFTGQGSQYINM 1222
Cdd:COG3321   464 AFLEAHPDLDLADVAYTLATGRAHFEHRLAVVASSREELAAKLRALAAGEAAPgvvtgAAAAAPKVAFLFPGQGSQYVGM 543

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1223 GRTLYDTESTFRAALDRCETILQNLGIESIISVIFGSSEHGLsLDDTAYTQPALFAIEYALYQLWKSWGIQPSVVIGHSV 1302
Cdd:COG3321   544 GRELYETEPVFRAALDECDALLRPHLGWSLREVLFPDEEESR-LDRTEVAQPALFAVEYALARLWRSWGVRPDAVIGHSV 622

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1303 GEYVSACVAGVFSLEDGLKLIAERGRLIQALPRDGSMVSVMASEKRIADIILPYGGqVGIAAINGPQSVVISGQQQAIDA 1382
Cdd:COG3321   623 GEYAAACVAGVLSLEDALRLVAARGRLMQALPGGGAMLAVGLSEEEVEALLAGYDG-VSIAAVNGPRSTVVSGPAEAVEA 701

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1383 ICAILETEGIKSKKLNVSHAFHSPLVEAMLDSFLQVAQEVTYSQPQIKLISNVTGTLASHEscpdelpITTAEYWVRHVR 1462
Cdd:COG3321   702 LAARLEARGIRARRLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIPLISNVTGTWLTGE-------ALDADYWVRHLR 774

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1463 QPVRFAAGMESLEGQGVNVFIEIGPKPVLLGMGRDCLPEQE-GLWLPSLRPKQDDWQQVLSSLRDLYLVGVTIDWSSFDQ 1541
Cdd:COG3321   775 QPVRFADAVEALLADGVRVFLEVGPGPVLTGLVRQCLAAAGdAVVLPSLRRGEDELAQLLTALAQLWVAGVPVDWSALYP 854

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1542 GYARRRVPLPTYPWQRERHWVEPIIRHRQSVLQATNTTKLTRNASVAQHPLLGQRLHLSRTQEIYFQTFIHSDFPIWVAD 1621
Cdd:COG3321   855 GRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVA 934

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1622 HKVFGNVIIPGVAYFEMALAAGKALKPDSIFWLEDVSIAQALIIPDEGQTVQIVLSPQEESAyffeILSLEKENSWVLHA 1701
Cdd:COG3321   935 LAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAAL----AAAAALALLAAAAL 1010

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1702 SGKLVAQEQVLETEPIDLIALQAHCCEEVSVDVLYQEEMARRLDMGPMMRGVKQLWRYPLSFAKSHDAIALAKVSLPEIL 1781
Cdd:COG3321  1011 LLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAAL 1090

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1782 LHESNAYQFHPVILDAGLQMITVSYPEANQGQTYVPVGIEGLQVYGRPSSELWCRAQYRPPLDTDQRQGIDLLPKKLIAD 1861
Cdd:COG3321  1091 AAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAA 1170

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1862 LHLFDTQGRVVAIMFGVQSVLVGREAMLRSQDTWRNWLYQVLWKPQACFGLLPNYLPTPDKIRKRLETKLATLIIEANLA 1941
Cdd:COG3321  1171 AALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAA 1250

                        1290      1300      1310      1320      1330      1340
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 602182148 1942 TYAIAYTQLERLSLAYVVAAFRQMGWLFQPGERFSTAQKVSALGIVDQHRQLFARLLDILAEADILR 2008
Cdd:COG3321  1251 AAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAA 1317

EntF

COG1020

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...

3-663

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: 603.77 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    3 ERESPQILFDGNGTQSEFP-DSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIE 81
Cdd:COG1020   455 AAERQQLLAEWNATAAPYPaDATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLE 534

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   82 RSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLTSTDVAKKLaltiPALQeCQTVYLDQEifeydfhfl 161
Cdd:COG1020   535 RSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARL----PELG-VPVLALDAL--------- 600

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  162 aiakllhnqylrllhfyfytLIQQCQATSVSQGIQtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSV 241
Cdd:COG1020   601 --------------------ALAAEPATNPPVPVT----PDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLG 656

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  242 QGVRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNgnkSTSLAL 321
Cdd:COG1020   657 PGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAP---EALPSL 733

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  322 CEVITTGEQmqITPAVANLFQKT--GAMLHNHYGATEFQ-DATTHTLKGNPEGWPTlVPVGRPLHNVQVYILDEAQQPVP 398
Cdd:COG1020   734 RLVLVGGEA--LPPELVRRWRARlpGARLVNLYGPTETTvDSTYYEVTPPDADGGS-VPIGRPIANTRVYVLDAHLQPVP 810

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  399 LGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGtnENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEI 478
Cdd:COG1020   811 VGVPGELYIGGAGLARGYLNRPELTAERFVADPFG--FPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEI 888

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  479 ESVLASHQAVRECAVVAREIA-GHTQLVGYIIAKDTLnlsfDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLD 557
Cdd:COG1020   889 EAALLQHPGVREAVVVAREDApGDKRLVAYVVPEAGA----AAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLD 964

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  558 RRALPDPkgDRPALSTPLVKPRTQTEKRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKFLCETFNINLSAVSLFQ 637
Cdd:COG1020   965 RLALPAP--AAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLA 1042

                         650       660
                  ....*....|....*....|....*.
gi 602182148  638 YPTIQTLAQYIDCQGDTTSSNTASRH 663
Cdd:COG1020  1043 AAAAAAAAAAAAAAAAAAAPLAAAAA 1068

KR_2_FAS_SDR_x

cd08955

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...

2353-2747

1.26e-127

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); Ketoreductase, a module of the multidomain polyketide synthase, has 2 subdomains, each corresponding to a short-chain dehydrogenases/reductase (SDR) family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerizes but is composed of 2 subdomains, each resembling an SDR monomer. In some instances, as in porcine FAS, an enoyl reductase (a Rossman fold NAD binding domain of the MDR family) module is inserted between the sub-domains. The active site resembles that of typical SDRs, except that the usual positions of the catalytic asparagine and tyrosine are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular polyketide synthases are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) fatty acid synthase. In some instances, such as porcine FAS , an enoyl reductase module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER). Polyketide syntheses also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes the KR domain of the Lyngbya majuscule Jam J, -K, and #L which are encoded on the jam gene cluster and are involved in the synthesis of the Jamaicamides (neurotoxins); Lyngbya majuscule Jam P belongs to a different KR_FAS_SDR_x subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, 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 KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187658 [Multi-domain] Cd Length: 376 Bit Score: 407.06 E-value: 1.26e-127

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2353 LLNRVPNIQEIVHCWSM----VSTDLDRATIFSCSSTLHLVQAL--ANYPKNPRLSLVTLGAQAVN-EHHVQNVVGAALW 2425
Cdd:cd08955     1 ALLGSAPLAGVVHLWSLdaprEEPADAASQELGCASALHLVQALskAGLRRAPRLWLVTRGAQSVLaDGEPVSPAQAPLW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2426 GMGKVIALEHPELQVAQMDLDPNGKVKAQVEVLRDELLARKDpasamsvpdlqtrphEKQIAFREQTRYVARLSPLDRPN 2505
Cdd:cd08955    81 GLGRVIALEHPELRCGLVDLDPEATAAEEAEALLAELLAADA---------------EDQVALRGGARYVARLVRAPARP 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2506 prekgtqealtFRDDGSYLIAGGLGGLGLVVARFLVTNGARYLVLVGRRGAREEQQAQLSELEQLGASVKVLQADIADAE 2585
Cdd:cd08955   146 -----------LRPDATYLITGGLGGLGLLVAEWLVERGARHLVLTGRRAPSAAARQAIAALEEAGAEVVVLAADVSDRD 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2586 QLAQALSAV--TYPPLRGVIHAAGTLNDGILQQQSWQAFKEVMNPKVAGAWNLHILTKNQPLDFFVLFSSATSLLGNAGQ 2663
Cdd:cd08955   215 ALAAALAQIraSLPPLRGVIHAAGVLDDGVLANQDWERFRKVLAPKVQGAWNLHQLTQDLPLDFFVLFSSVASLLGSPGQ 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2664 ANHAAANAFLDGLASYRRHLGLPSLSINWGTWSEVGIAARLGLDKLSSKQGEGTITLGQGLQILEQLLKDENGvyQVGVM 2743
Cdd:cd08955   295 ANYAAANAFLDALAHYRRARGLPALSINWGPWAEVGMAASLARQARLEARGVGAISPAAGLQALGQLLRTGST--QVGVA 372


                  ....
gi 602182148 2744 PINW 2747
Cdd:cd08955   373 PVDW 376

Methyltransf_12

pfam08242

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.

2113-2213

7.14e-25

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.

Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 100.91 E-value: 7.14e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  2113 LEIGAGTGGTTAYLLPHLPGdqTKYVFTDISAFFLAKAEERFKDYPFVRYQVLDIEQAPQAQGFEPQiYDLIVAADVLHA 2192
Cdd:pfam08242    1 LEIGCGTGTLLRALLEALPG--LEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPGS-FDVVVASNVLHH 77

                           90       100
                   ....*....|....*....|.
gi 602182148  2193 TSDLRQTLVHIRQLLAPGGML 2213
Cdd:pfam08242   78 LADPRAVLRNIRRLLKPGGVL 98

PKS_PP

smart00823

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...

2795-2881

9.49e-25

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: 100.02 E-value: 9.49e-25

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   2795 LENAPPKEGLTLLQAHVREQVSQVLGIDTKTLLaEQDVGFFTLGMDSLTSVELRNRLQASLGCSLSSTLAFDYPTQQALV 2874
Cdd:smart00823    1 LAALPPAERRRLLLDLVREQVAAVLGHAAAEAI-DPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALA 79


                    ....*..
gi 602182148   2875 NYLANEL 2881
Cdd:smart00823   80 EHLAAEL 86

Name

Accession

Description

Interval

E-value

PksD

COG3321

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...

673-2008

0e+00

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];

Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 1312.56 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  673 DSNDIAIISVAGRFPGAETIEQFWHNLCNGVESITLFSDDKLEQTL----PELFNNPAYVKAGAVLEGVELFDATFFGYS 748
Cdd:COG3321     2 ADEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWDADAyydpDPDAPGKTYVRWGGFLDDVDEFDALFFGIS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  749 PKEAAVTDPQQRILLECAWEAFERAGYNPETYP-EPVGVYAGSSLSTYLLNNIGSALGIiteqpfietdmeQFQAKIGND 827
Cdd:COG3321    82 PREAEAMDPQQRLLLEVAWEALEDAGYDPESLAgSRTGVFVGASSNDYALLLLADPEAI------------DAYALTGNA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  828 RSYLATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQKGGYLYEEGMVRSQDGHCRAFD 907
Cdd:COG3321   150 KSVLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFD 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  908 AEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGAIKmGYTAPSVDGQADVISEAIAIADIDASTIGYVEA 987
Cdd:COG3321   230 ADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSN-GLTAPNGPAQAAVIRRALADAGVDPATVDYVEA 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  988 HGTATQLGDPIEVAGLARAFQRSTDsvlGKQQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPRID 1067
Cdd:COG3321   309 HGTGTPLGDPIEAAALTAAFGQGRP---ADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHID 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1068 FDATPFFVNTELREWSRNGYPRRAGVSSFGVGGTNSHIVLEESPVKQPTlfSSLPERSHHLLTLSAHTQEALHELVQRYI 1147
Cdd:COG3321   386 FENSPFYVNTELRPWPAGGGPRRAGVSSFGFGGTNAHVVLEEAPAAAPA--AAAAARPPQLLVLSAKTEEALRALAARLA 463

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1148 QHNETHLDIDLGDLCFTANTGRKHFEHRLAVVAESIPGLQAQLETAQTAISAQ-----KKNAPPTIAFLFTGQGSQYINM 1222
Cdd:COG3321   464 AFLEAHPDLDLADVAYTLATGRAHFEHRLAVVASSREELAAKLRALAAGEAAPgvvtgAAAAAPKVAFLFPGQGSQYVGM 543

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1223 GRTLYDTESTFRAALDRCETILQNLGIESIISVIFGSSEHGLsLDDTAYTQPALFAIEYALYQLWKSWGIQPSVVIGHSV 1302
Cdd:COG3321   544 GRELYETEPVFRAALDECDALLRPHLGWSLREVLFPDEEESR-LDRTEVAQPALFAVEYALARLWRSWGVRPDAVIGHSV 622

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1303 GEYVSACVAGVFSLEDGLKLIAERGRLIQALPRDGSMVSVMASEKRIADIILPYGGqVGIAAINGPQSVVISGQQQAIDA 1382
Cdd:COG3321   623 GEYAAACVAGVLSLEDALRLVAARGRLMQALPGGGAMLAVGLSEEEVEALLAGYDG-VSIAAVNGPRSTVVSGPAEAVEA 701

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1383 ICAILETEGIKSKKLNVSHAFHSPLVEAMLDSFLQVAQEVTYSQPQIKLISNVTGTLASHEscpdelpITTAEYWVRHVR 1462
Cdd:COG3321   702 LAARLEARGIRARRLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIPLISNVTGTWLTGE-------ALDADYWVRHLR 774

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1463 QPVRFAAGMESLEGQGVNVFIEIGPKPVLLGMGRDCLPEQE-GLWLPSLRPKQDDWQQVLSSLRDLYLVGVTIDWSSFDQ 1541
Cdd:COG3321   775 QPVRFADAVEALLADGVRVFLEVGPGPVLTGLVRQCLAAAGdAVVLPSLRRGEDELAQLLTALAQLWVAGVPVDWSALYP 854

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1542 GYARRRVPLPTYPWQRERHWVEPIIRHRQSVLQATNTTKLTRNASVAQHPLLGQRLHLSRTQEIYFQTFIHSDFPIWVAD 1621
Cdd:COG3321   855 GRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVA 934

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1622 HKVFGNVIIPGVAYFEMALAAGKALKPDSIFWLEDVSIAQALIIPDEGQTVQIVLSPQEESAyffeILSLEKENSWVLHA 1701
Cdd:COG3321   935 LAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAAL----AAAAALALLAAAAL 1010

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1702 SGKLVAQEQVLETEPIDLIALQAHCCEEVSVDVLYQEEMARRLDMGPMMRGVKQLWRYPLSFAKSHDAIALAKVSLPEIL 1781
Cdd:COG3321  1011 LLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAAL 1090

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1782 LHESNAYQFHPVILDAGLQMITVSYPEANQGQTYVPVGIEGLQVYGRPSSELWCRAQYRPPLDTDQRQGIDLLPKKLIAD 1861
Cdd:COG3321  1091 AAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAA 1170

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1862 LHLFDTQGRVVAIMFGVQSVLVGREAMLRSQDTWRNWLYQVLWKPQACFGLLPNYLPTPDKIRKRLETKLATLIIEANLA 1941
Cdd:COG3321  1171 AALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAA 1250

                        1290      1300      1310      1320      1330      1340
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 602182148 1942 TYAIAYTQLERLSLAYVVAAFRQMGWLFQPGERFSTAQKVSALGIVDQHRQLFARLLDILAEADILR 2008
Cdd:COG3321  1251 AAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAA 1317

PKS

cd00833

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...

675-1107

0e+00

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.

Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 610.33 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  675 NDIAIISVAGRFPGAETIEQFWHNLCNGVESITLFSDDKLEQTL---PELFNNPAYVKAGAVLEGVELFDATFFGYSPKE 751
Cdd:cd00833     1 EPIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGyypDPGKPGKTYTRRGGFLDDVDAFDAAFFGISPRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  752 AAVTDPQQRILLECAWEAFERAGYNPET-YPEPVGVYAGSSLSTYLLNNIGSALGIiteqpfietdmEQFQAkIGNDRSY 830
Cdd:cd00833    81 AEAMDPQQRLLLEVAWEALEDAGYSPESlAGSRTGVFVGASSSDYLELLARDPDEI-----------DAYAA-TGTSRAF 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  831 LATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQKGGYLYEEGMVRSQDGHCRAFDAEA 910
Cdd:cd00833   149 LANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADA 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  911 QGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGAIKmGYTAPSVDGQADVISEAIAIADIDASTIGYVEAHGT 990
Cdd:cd00833   229 DGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTK-GITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGT 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  991 ATQLGDPIEVAGLARAFQRSTDsvlGKQQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPRIDFDA 1070
Cdd:cd00833   308 GTPLGDPIEVEALAKVFGGSRS---ADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEE 384

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 602182148 1071 TPFFVNTELREWSRNGYPRRAGVSSFGVGGTNSHIVL 1107
Cdd:cd00833   385 SPLRVPTEARPWPAPAGPRRAGVSSFGFGGTNAHVIL 421

EntF

COG1020

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...

3-663

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: 603.77 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    3 ERESPQILFDGNGTQSEFP-DSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIE 81
Cdd:COG1020   455 AAERQQLLAEWNATAAPYPaDATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLE 534

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   82 RSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLTSTDVAKKLaltiPALQeCQTVYLDQEifeydfhfl 161
Cdd:COG1020   535 RSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARL----PELG-VPVLALDAL--------- 600

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  162 aiakllhnqylrllhfyfytLIQQCQATSVSQGIQtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSV 241
Cdd:COG1020   601 --------------------ALAAEPATNPPVPVT----PDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLG 656

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  242 QGVRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNgnkSTSLAL 321
Cdd:COG1020   657 PGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAP---EALPSL 733

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  322 CEVITTGEQmqITPAVANLFQKT--GAMLHNHYGATEFQ-DATTHTLKGNPEGWPTlVPVGRPLHNVQVYILDEAQQPVP 398
Cdd:COG1020   734 RLVLVGGEA--LPPELVRRWRARlpGARLVNLYGPTETTvDSTYYEVTPPDADGGS-VPIGRPIANTRVYVLDAHLQPVP 810

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  399 LGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGtnENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEI 478
Cdd:COG1020   811 VGVPGELYIGGAGLARGYLNRPELTAERFVADPFG--FPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEI 888

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  479 ESVLASHQAVRECAVVAREIA-GHTQLVGYIIAKDTLnlsfDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLD 557
Cdd:COG1020   889 EAALLQHPGVREAVVVAREDApGDKRLVAYVVPEAGA----AAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLD 964

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  558 RRALPDPkgDRPALSTPLVKPRTQTEKRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKFLCETFNINLSAVSLFQ 637
Cdd:COG1020   965 RLALPAP--AAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLA 1042

                         650       660
                  ....*....|....*....|....*.
gi 602182148  638 YPTIQTLAQYIDCQGDTTSSNTASRH 663
Cdd:COG1020  1043 AAAAAAAAAAAAAAAAAAAPLAAAAA 1068

A_NRPS_VisG_like

cd17651

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...

29-562

0e+00

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: 578.91 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   29 FEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYP 108
Cdd:cd17651     1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  109 ADRIEYMLRDSDARILLTSTDVAKKLALTIPALqecqtVYLDQEifeydfhflaiakllhnqylrllhfyfytliQQCQA 188
Cdd:cd17651    81 AERLAFMLADAGPVLVLTHPALAGELAVELVAV-----TLLDQP-------------------------------GAAAG 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  189 TSVSQGIQTQvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTLCLG 268
Cdd:cd17651   125 ADAEPDPALD--ADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAG 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  269 GILVLVPEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALCEVITTGEQMQITPAVANLFQK-TGAM 347
Cdd:cd17651   203 ATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLVLTEDLREFCAGlPGLR 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  348 LHNHYGATEFQDATTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKF 427
Cdd:cd17651   283 LHNHYGPTETHVVTALSLPGDPAAWPAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERF 362

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  428 IPNPFGTNEnakKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVARE-IAGHTQLVG 506
Cdd:cd17651   363 VPDPFVPGA---RMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREdRPGEKRLVA 439

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 602182148  507 YIIAKDTLNLSFDKlepiLRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALP 562
Cdd:cd17651   440 YVVGDPEAPVDAAE----LRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491

mycolic_Pks13

NF040607

polyketide synthase Pks13;

628-1563

4.38e-169

polyketide synthase Pks13;

Pssm-ID: 468580 [Multi-domain] Cd Length: 1671 Bit Score: 570.33 E-value: 4.38e-169

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  628 INLSAVSLFQYPTIQTLAQYIdCQGDTTSSNTASRHKKVRKKQSGDSNDIAIISVAGRFPGA-ETIEQFWHNLCNGVESI 706
Cdd:NF040607   54 VTLTATVAYQHPTIASLATRI-IEGEPEVAADDDDDADWSRRPRSDAHDIAIVGLATRFPGAgNTPEEMWEALIEGRDGI 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  707 TLFSDDKLEqtlpELFNNPAYVKA-------GAVLEGVELFDATFFGYSPKEAAVTDPQQRILLECAWEAFERAGYNPET 779
Cdd:NF040607  133 TDLPEGRWS----EFAADPRIAERvakantrGGYLDDIKGFDAEFFALSPLEAENVDPQQRLALELTWEALEHARIPASS 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  780 YP-EPVGVYAGSSLSTY-LLnnigSALGIITEQPFietdmeqfqAKIGNDRSYLATRISYKLNLKGPSVNVQTACSTSLV 857
Cdd:NF040607  209 LRgEPVGVFIGSSNNDYqML----AVADPAEAHPY---------ALTGTSSSIIANRVSYFFDFRGPSVAVDTACSSSLV 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  858 AVHMACQSLISGECQMALAGGISVVVPQKGGYLYEE-GMVRSQDGHCRAFDAEAQGTIFGNGGGLVLLKRLQDALDDNDN 936
Cdd:NF040607  276 AVHQAVRALRSGEADVAVAGGVNMLLTPAVTLGFDElGGVLAPDGRIKAFSSDADGMVRSEGGGVVVLKRLADARRDGDT 355

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  937 IMAVIKATAINNDGAiKMGYTAPSVDGQADVISEAIAIADIDASTIGYVEAHGTATQLGDPIEVAGLARafqrstdsVLG 1016
Cdd:NF040607  356 ILAVIAGSAVNSDGR-SNGLTAPNPDAQVDVLRRAYADAGIDPRTVDYVEAHGTGTILGDPIEADALGR--------VVG 426

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1017 KQQCA-----IGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPRIDFDATPFFVNTELREWSR-NGYPrR 1090
Cdd:NF040607  427 RGRDAdkpalLGSAKTNFGHLESAAGAAGLAKVVLAMQHDKLPPSLNYAGPNPYIDFDAEHLKVVDEPTEWPRySGHA-V 505

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1091 AGVSSFGVGGTNSHIVLEE--SPVKQPTLFSSLPERSHHLLTLSAHTQEALHELVQRYIQHNETH--------------- 1153
Cdd:NF040607  506 AGVSGFGFGGTNAHVVVREvlPADLVEPEAQPDEDTEAELAGLTAEAKRLLAEAELAAEFAPAAPegpvvplpvsgflps 585

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1154 ------------LDIDLG---DLCFTANT--GRKHFEHRLAVVA----ESIPGLQAQLE--TAQTAISAqkkNAPPTI-- 1208
Cdd:NF040607  586 rrraaaadladwLESEEGratPLADVARAlaRRNHGRSRAVVLAhtheEAIKGLRAVAEgkPGPGVFSA---DAPAANgp 662

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1209 AFLFTGQGSQYINMGRTLYDTESTFRAALDRCETILQNLGIESIISVIfgssehglsLDD-----TAYTQPALFAIEYAL 1283
Cdd:NF040607  663 VWVLSGFGSQHRKMAKQLYLENPVFAARIDEVDELVQDESGYSIVELI---------LDDeqtydIETAQVGIFAIQIAL 733

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1284 YQLWKSWGIQPSVVIGHSVGEYVSACVAGVFSLEDGLKLIAERGRLI----QALPRD--GSMVSVMASEKRIADIILPYG 1357
Cdd:NF040607  734 ADLLRHHGAKPAAVVGHSMGEAAAAYAAGGLSLEDAVRVICHRSRLMgegeAMLPGDdiRLMALVEYSAEEIETVLADFP 813

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1358 GqVGIAAINGPQSVVISGQQQAIDAICAILETEGIKSKKLNVSHAFHSplveAMLDSFL-QVAQEVTYSQPQ---IKLIS 1433
Cdd:NF040607  814 D-LEVCVYAAPTHTVIGGPREQVDAIVARAEAEGKFARKLQTKGASHT----SQMDPLLgELAAELAGIEPQpltVGLYS 888

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1434 NV-TGTL--ASHEscpdelPITTAEYWVRHVRQPVRFAAGMESLEGQGVNVFIEIGPKPV-LLGMGRDC----LPEQEgl 1505
Cdd:NF040607  889 SVdRGTFyrPGHE------PIHDVDYWVKGLRHSVWFTQAVRKAVDAGHTTFLELAPNPVaLMSVAATTfaagLHDAQ-- 960

                         970       980       990      1000      1010      1020
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1506 WLPSLRPKQDDWQQVLSSLRDLYLVGVTIDWSS-FDQG-YArrrvPLPTYPWQRERHWVE 1563
Cdd:NF040607  961 LIPTLKRKEDESESVLNALAQLYVHGHDVDLRSlFGAGdYA----DIPRTRFKRKPYWLD 1016

PKS_KS

smart00825

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...

677-1109

1.29e-151

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.

Pssm-ID: 214836 [Multi-domain] Cd Length: 298 Bit Score: 472.20 E-value: 1.29e-151

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    677 IAIISVAGRFPGAETIEQFWHNLCNGvesitlfsddkleqtlpelfnnpayvkagavLEGVELFDATFFGYSPKEAAVTD 756
Cdd:smart00825    1 IAIVGMSCRFPGADDPEEFWDLLLAG-------------------------------LDDVDLFDAAFFGISPREAEAMD 49

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    757 PQQRILLECAWEAFERAGYNPETYPE-PVGVYAGSSLSTYllnnigsalgiiteqpfietdmeqfqakigndrsylatri 835
Cdd:smart00825   50 PQQRLLLEVAWEALEDAGIDPESLRGsRTGVFVGVSSSDY---------------------------------------- 89

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    836 syklnlkgpSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQKGGYLYEEGMVRSQDGHCRAFDAEAQGTIF 915
Cdd:smart00825   90 ---------SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVR 160

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    916 GNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGAiKMGYTAPSVDGqadviseaiaiadidastigyveahgtatqlg 995
Cdd:smart00825  161 GEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGR-SNGITAPSGPA-------------------------------- 207

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    996 dpievaglarafqrstdsvlgkqQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPRIDFDATPFFV 1075
Cdd:smart00825  208 -----------------------QLLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRV 264

                           410       420       430
                    ....*....|....*....|....*....|....
gi 602182148   1076 NTELREWSRNGYPRRAGVSSFGVGGTNSHIVLEE 1109
Cdd:smart00825  265 PTELTPWPPPGRPRRAGVSSFGFGGTNAHVILEE 298

PRK12467

peptide synthase; Provisional

3-645

1.39e-148

peptide synthase; Provisional

Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 522.03 E-value: 1.39e-148

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    3 ERESPQILFDGNGTQSEFP-DSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIE 81
Cdd:PRK12467 1553 EAERRQILEGWNATHTGYPlARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVE 1632

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   82 RSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLTSTDVAKKLaltiPALQECQTVYLDQEifeydfhfl 161
Cdd:PRK12467 1633 RSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARL----PLPDGLRSLVLDQE--------- 1699

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  162 aiakllhnqylrllhfyfytliQQCQATSVSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSV 241
Cdd:PRK12467 1700 ----------------------DDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLS 1757

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  242 QGVRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRQNPFALAEFISQQKIEKL-FLPVI--ALLQLAEAVNGnkstS 318
Cdd:PRK12467 1758 AADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLhFVPSMlqQLLQMDEQVEH----P 1833

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  319 LALCEVITTGEQMQITPAVANLFQKTGAMLHNHYGATEFQDATTHTL--KGNPEGWPTlVPVGRPLHNVQVYILDEAQQP 396
Cdd:PRK12467 1834 LSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTcrRKDLEGRDS-VPIGQPIANLSTYILDASLNP 1912

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  397 VPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGTNenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELG 476
Cdd:PRK12467 1913 VPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGTV--GSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELG 1990

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  477 EIESVLASHQAVRECAVVAREIAGHTQLVGYIIAKDTLNLSFDK----LEPILRQYSEAVLPEYMIPTRFINISNMPLTP 552
Cdd:PRK12467 1991 EIEARLREQGGVREAVVIAQDGANGKQLVAYVVPTDPGLVDDDEaqvaLRAILKNHLKASLPEYMVPAHLVFLARMPLTP 2070

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  553 SGKLDRRALPDPkgDRPALSTPLVKPRTQTEKRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKfLCETFNINLSA 632
Cdd:PRK12467 2071 NGKLDRKALPAP--DASELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVS-RARQAGIRFTP 2147

                         650
                  ....*....|...
gi 602182148  633 VSLFQYPTIQTLA 645
Cdd:PRK12467 2148 KDLFQHQTVQSLA 2160

AA-adenyl-dom

TIGR01733

amino acid adenylation domain; This model represents a domain responsible for the specific ...

50-493

2.14e-141

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: 447.87 E-value: 2.14e-141

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    50 TYGELNVRANHLAQHLLSLGC-QPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLTST 128
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAGGvGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   129 DVAKKLAltipalqecqtvYLDQEIFEYDFHFLAIAkllhnqylrllhfyfytliqqcQATSVSQGIQTQVLPNNLAYCI 208
Cdd:TIGR01733   81 ALASRLA------------GLVLPVILLDPLELAAL----------------------DDAPAPPPPDAPSGPDDLAYVI 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   209 YTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRQNPFAL-AE 287
Cdd:TIGR01733  127 YTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALlAA 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   288 FISQQKIEKLFLPVIALLQLAEAVNGNKSTslaLCEVITTGEQmqITPAVANLFQKT--GAMLHNHYGATEFQ-DATTHT 364
Cdd:TIGR01733  207 LIAEHPVTVLNLTPSLLALLAAALPPALAS---LRLVILGGEA--LTPALVDRWRARgpGARLINLYGPTETTvWSTATL 281

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   365 LKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGTNENAKkLYRT 444
Cdd:TIGR01733  282 VDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAGGDGAR-LYRT 360

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 602182148   445 GDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAV 493
Cdd:TIGR01733  361 GDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409

KR_2_FAS_SDR_x

cd08955

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...

2353-2747

1.26e-127

Pssm-ID: 187658 [Multi-domain] Cd Length: 376 Bit Score: 407.06 E-value: 1.26e-127

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2353 LLNRVPNIQEIVHCWSM----VSTDLDRATIFSCSSTLHLVQAL--ANYPKNPRLSLVTLGAQAVN-EHHVQNVVGAALW 2425
Cdd:cd08955     1 ALLGSAPLAGVVHLWSLdaprEEPADAASQELGCASALHLVQALskAGLRRAPRLWLVTRGAQSVLaDGEPVSPAQAPLW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2426 GMGKVIALEHPELQVAQMDLDPNGKVKAQVEVLRDELLARKDpasamsvpdlqtrphEKQIAFREQTRYVARLSPLDRPN 2505
Cdd:cd08955    81 GLGRVIALEHPELRCGLVDLDPEATAAEEAEALLAELLAADA---------------EDQVALRGGARYVARLVRAPARP 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2506 prekgtqealtFRDDGSYLIAGGLGGLGLVVARFLVTNGARYLVLVGRRGAREEQQAQLSELEQLGASVKVLQADIADAE 2585
Cdd:cd08955   146 -----------LRPDATYLITGGLGGLGLLVAEWLVERGARHLVLTGRRAPSAAARQAIAALEEAGAEVVVLAADVSDRD 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2586 QLAQALSAV--TYPPLRGVIHAAGTLNDGILQQQSWQAFKEVMNPKVAGAWNLHILTKNQPLDFFVLFSSATSLLGNAGQ 2663
Cdd:cd08955   215 ALAAALAQIraSLPPLRGVIHAAGVLDDGVLANQDWERFRKVLAPKVQGAWNLHQLTQDLPLDFFVLFSSVASLLGSPGQ 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2664 ANHAAANAFLDGLASYRRHLGLPSLSINWGTWSEVGIAARLGLDKLSSKQGEGTITLGQGLQILEQLLKDENGvyQVGVM 2743
Cdd:cd08955   295 ANYAAANAFLDALAHYRRARGLPALSINWGPWAEVGMAASLARQARLEARGVGAISPAAGLQALGQLLRTGST--QVGVA 372


                  ....
gi 602182148 2744 PINW 2747
Cdd:cd08955   373 PVDW 376

omega_3_PfaA

TIGR02813

polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...

677-1554

1.61e-115

polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.

Pssm-ID: 274311 [Multi-domain] Cd Length: 2582 Bit Score: 412.86 E-value: 1.61e-115

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   677 IAIISVAGRFPGAETIEQFWHNLCNGVESIT-----------LFSDDKLEQtlpelfnNPAYVKAGAVLEGVElFDATFF 745
Cdd:TIGR02813    9 IAIVGMASIFANSRYLNKFWDLIFEKIDAITdvpsdhwakddYYDSDKSEA-------DKSYCKRGGFLPEVD-FNPMEF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   746 GYSPKEAAVTDPQQRILLECAWEAFERAGYnPETYPE-----PVGVYAGSSLSTYL--------LNNIGSALGIITE--- 809
Cdd:TIGR02813   81 GLPPNILELTDISQLLSLVVAKEVLNDAGL-PDGYDRdkigiTLGVGGGQKQSSSLnarlqypvLKKVFKASGVEDEdse 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   810 -------QPFIETDMEQFQAKIGNdrsYLATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGisvV 882
Cdd:TIGR02813  160 mlikkfqDQYIHWEENSFPGSLGN---VISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGG---V 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   883 VPQKGGYLYeegMVRSQ------DGHCRAFDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGAIKMGY 956
Cdd:TIGR02813  234 CTDNSPFMY---MSFSKtpafttNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIY 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   957 tAPSVDGQADVISEAIAIADIDASTIGYVEAHGTATQLGDPIEVAGLARAFQRSTDSvlgKQQCAIGSVKTNIGHLDEAA 1036
Cdd:TIGR02813  311 -APRPEGQAKALKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQ---KQHIALGSVKSQIGHTKSTA 386

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  1037 GIAGLIKAALALQYGQIPPSLHYANPNPRIDFDATPFFVNTELREWSR--NGYPRRAGVSSFGVGGTNSHIVLEE-SP-- 1111
Cdd:TIGR02813  387 GTAGMIKAVLALHHKVLPPTINVDQPNPKLDIENSPFYLNTETRPWMQreDGTPRRAGISSFGFGGTNFHMVLEEySPkh 466

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  1112 ----------VKQPTLFSS------LPERSHHLLTLSAHTQEALHELVQRYIQHNETHLDIDLGDLCFTANTGrkhfEHR 1175
Cdd:TIGR02813  467 qrddqyrqraVAQTLLFTAanekalVSSLKDWKNKLSAKADDQPYAFNALAVENTLRTIAVALARLGFVAKNA----DEL 542

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  1176 LAVVAESIPGLQAQ-LETAQ--TAISAQKK---NAPPTIAFLFTGQGSQYINMGRTLYDTESTFRAALDRCETILQNLGI 1249
Cdd:TIGR02813  543 ITMLEQAITQLEAKsCEEWQlpSGISYRKSalvVESGKVAALFAGQGSQYLNMGRELACNFPEVRQAAADMDSVFTQAGK 622

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  1250 ESIISVIF--------GSSEHGLSLDDTAYTQPALFAIEYALYQLWKSWGIQPSVVIGHSVGEYVSACVAGVFSLEDGLK 1321
Cdd:TIGR02813  623 GALSPVLYpipvfndeSRKAQEEALTNTQHAQSAIGTLSMGQYKLFTQAGFKADMTAGHSFGELSALCAAGVISDDDYMM 702

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  1322 LIAERGRLIQALPRD---GSMVSVMASEKRIADIILPYGGQ---VGIAAINGPQSVVISG----QQQAIDAicaiLETEG 1391
Cdd:TIGR02813  703 LAFSRGQAMAAPTGEadiGFMYAVILAVVGSPTVIANCIKDfegVSIANYNSPTQLVIAGvstqIQIAAKA----LKEKG 778

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  1392 IKSKKLNVSHAFHSPLVEAMLDSFLQVAQEVTYSQPQIKLISNVTGTLASHescpDELPITTAeyWVRHVRQPVRFAAGM 1471
Cdd:TIGR02813  779 FKAIPLPVSGAFHTPLVAHAQKPFSAAIDKAKFNTPLVPLYSNGTGKLHSN----DAAAIKKA--LKNHMLQSVHFSEQL 852

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  1472 ESLEGQGVNVFIEIGPKPVLLGMGRDCLPEQEG-LWLPSL--RPKQDDWQQVLSSLRDLYLVGVTIDwsSFDQGYARRRV 1548
Cdd:TIGR02813  853 EAMYAAGARVFVEFGPKNILQKLVENTLKDKENeLCAISInpNPKGDSDMQLRQAAVQLAVLGLELT--EIDPYQAEKRP 930


                   ....*.
gi 602182148  1549 PLPTYP 1554
Cdd:TIGR02813  931 PAATSP 936

AMP-binding

pfam00501

AMP-binding enzyme;

29-469

1.37e-98

AMP-binding enzyme;

Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 325.04 E-value: 1.37e-98

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    29 FEDQAAKRPDAIALIDGE-QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGY 107
Cdd:pfam00501    1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   108 PADRIEYMLRDSDARILLTstDVAKKLALTIPALQECQTVYldqeifeydfHFLAIAKLLHNQYLRLLHFYFYTLIQQCQ 187
Cdd:pfam00501   81 PAEELAYILEDSGAKVLIT--DDALKLEELLEALGKLEVVK----------LVLVLDRDPVLKEEPLPEEAKPADVPPPP 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   188 ATSVSqgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGV----RTLQFCAVSFDFS-CHEIF 262
Cdd:pfam00501  149 PPPPD--------PDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLgpddRVLSTLPLFHDFGlSLGLL 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   263 STLCLGGILVLVPEAVRQNPFALAEFISQQKIEKLFLP---VIALLQlAEAVNGNKSTSLalcEVITTGeQMQITPAVAN 339
Cdd:pfam00501  221 GPLLAGATVVLPPGFPALDPAALLELIERYKVTVLYGVptlLNMLLE-AGAPKRALLSSL---RLVLSG-GAPLPPELAR 295

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   340 -LFQKTGAMLHNHYGATEfqdATTHTLKGNPEGWPTLVP--VGRPLHNVQVYILDEA-QQPVPLGGEGEFCIGGIGLARG 415
Cdd:pfam00501  296 rFRELFGGALVNGYGLTE---TTGVVTTPLPLDEDLRSLgsVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKG 372

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 602182148   416 YHNLPDLTNEKFIPNPFgtnenakklYRTGDLARYLPDGTIEHLGRIDHQVKIR 469
Cdd:pfam00501  373 YLNDPELTAEAFDEDGW---------YRTGDLGRRDEDGYLEIVGRKKDQIKLG 417

ketoacyl-synt

pfam00109

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...

675-930

3.11e-79

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.

Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 262.96 E-value: 3.11e-79

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   675 NDIAIISVAGRFPGAETIEQFWHNLCNGVESITLFSDDKLE----QTLPELFNNPAYVKAGAvLEGVELFDATFFGYSPK 750
Cdd:pfam00109    1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRWDpdklYDPPSRIAGKIYTKWGG-LDDIFDFDPLFFGISPR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   751 EAAVTDPQQRILLECAWEAFERAGYNPETYPEP-VGVYAGSSLSTY----LLNNIGSALGIiteQPFIetdmeqfqakIG 825
Cdd:pfam00109   80 EAERMDPQQRLLLEAAWEALEDAGITPDSLDGSrTGVFIGSGIGDYaallLLDEDGGPRRG---SPFA----------VG 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   826 NDRSYLATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQKGGYLYEEGMVRSQDGHCRA 905
Cdd:pfam00109  147 TMPSVIAGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKA 226

                          250       260
                   ....*....|....*....|....*
gi 602182148   906 FDAEAQGTIFGNGGGLVLLKRLQDA 930
Cdd:pfam00109  227 FDPFADGFVRGEGVGAVVLKRLSDA 251

PKS_KR

smart00822

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...

2535-2697

2.11e-74

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.

Pssm-ID: 214833 [Multi-domain] Cd Length: 180 Bit Score: 245.85 E-value: 2.11e-74

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   2535 VVARFLVTNGARYLVLVGRRGAREEQQAQL-SELEQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVIHAAGTLND 2611
Cdd:smart00822   15 ALARWLAERGARRLVLLSRSGPDAPGAAALlAELEAAGARVTVVACDVADRDALAAVLAAIpaVEGPLTGVIHAAGVLDD 94

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   2612 GILQQQSWQAFKEVMNPKVAGAWNLHILTKNQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGLASYRRHLGLPSLSIN 2691
Cdd:smart00822   95 GVLASLTPERFAAVLAPKAAGAWNLHELTADLPLDFFVLFSSIAGVLGSPGQANYAAANAFLDALAEYRRARGLPALSIA 174


                    ....*.
gi 602182148   2692 WGTWSE 2697
Cdd:smart00822  175 WGAWAE 180

pfam08659

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...

2521-2697

2.17e-71

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.

Pssm-ID: 430138 [Multi-domain] Cd Length: 180 Bit Score: 237.46 E-value: 2.17e-71

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  2521 GSYLIAGGLGGLGLVVARFLVTNGARYLVLVGRRGA-REEQQAQLSELEQLGASVKVLQADIADAEQLAQALSAV--TYP 2597
Cdd:pfam08659    1 GTYLITGGLGGLGRELARWLAERGARHLVLLSRSAApRPDAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIkaEGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  2598 PLRGVIHAAGTLNDGILQQQSWQAFKEVMNPKVAGAWNLHILTKNQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGLA 2677
Cdd:pfam08659   81 PIRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPDEPLDFFVLFSSIAGLLGSPGQANYAAANAFLDALA 160

                          170       180
                   ....*....|....*....|
gi 602182148  2678 SYRRHLGLPSLSINWGTWSE 2697
Cdd:pfam08659  161 EYRRSQGLPATSINWGPWAE 180

PLN02752

[acyl-carrier protein] S-malonyltransferase

1206-1494

1.33e-36

[acyl-carrier protein] S-malonyltransferase

Pssm-ID: 215401 [Multi-domain] Cd Length: 343 Bit Score: 143.36 E-value: 1.33e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1206 PTIAFLFTGQGSQYINMGRTLYDTEstfrAALDRCETILQNLGIESIISVIFGSSEhglSLDDTAYTQPALFAIEYALYQ 1285
Cdd:PLN02752   38 PTTAFLFPGQGAQAVGMGKEAAEVP----AAKALFDKASEILGYDLLDVCVNGPKE---KLDSTVVSQPAIYVASLAAVE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1286 LWKSWGIQPSVV------IGHSVGEYVSACVAGVFSLEDGLKLIAERGRLIQAL--PRDGSMVSV--MASEKrIADIILP 1355
Cdd:PLN02752  111 KLRARDGGQAVIdsvdvcAGLSLGEYTALVFAGALSFEDGLKLVKLRGEAMQAAadAGPSGMVSVigLDSDK-VQELCAA 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1356 YGGQVG------IAAINGPQSVVISGQQQAIDAICAILETEG-IKSKKLNVSHAFHSPLVEAMLDSFLQVAQEVTYSQPQ 1428
Cdd:PLN02752  190 ANEEVGeddvvqIANYLCPGNYAVSGGKKGIDAVEAKAKSFKaRMTVRLAVAGAFHTSFMEPAVDALEAALAAVEIRTPR 269

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 602182148 1429 IKLISNVTGtlASHeSCPDELPITTAeywvRHVRQPVRFAAGMESLEGQGVNVFIEIGPKPVLLGM 1494
Cdd:PLN02752  270 IPVISNVDA--QPH-SDPATIKKILA----RQVTSPVQWETTVKTLLEKGLEKSYELGPGKVIAGI 328

Methyltransf_12

pfam08242

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.

2113-2213

7.14e-25

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.

Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 100.91 E-value: 7.14e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  2113 LEIGAGTGGTTAYLLPHLPGdqTKYVFTDISAFFLAKAEERFKDYPFVRYQVLDIEQAPQAQGFEPQiYDLIVAADVLHA 2192
Cdd:pfam08242    1 LEIGCGTGTLLRALLEALPG--LEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPGS-FDVVVASNVLHH 77

                           90       100
                   ....*....|....*....|.
gi 602182148  2193 TSDLRQTLVHIRQLLAPGGML 2213
Cdd:pfam08242   78 LADPRAVLRNIRRLLKPGGVL 98

PKS_PP

smart00823

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...

2795-2881

9.49e-25

Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 100.02 E-value: 9.49e-25

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   2795 LENAPPKEGLTLLQAHVREQVSQVLGIDTKTLLaEQDVGFFTLGMDSLTSVELRNRLQASLGCSLSSTLAFDYPTQQALV 2874
Cdd:smart00823    1 LAALPPAERRRLLLDLVREQVAAVLGHAAAEAI-DPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALA 79


                    ....*..
gi 602182148   2875 NYLANEL 2881
Cdd:smart00823   80 EHLAAEL 86

UbiE

COG2226

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...

2100-2224

1.08e-23

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis

Pssm-ID: 441828 [Multi-domain] Cd Length: 143 Bit Score: 99.30 E-value: 1.08e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2100 ALEQLPPERGWRILEIGAGTGGTTAYLLPHlpgdQTKYVFTDISAFFLAKAEERFKDYPF-VRYQVLDIEQAPqaqgFEP 2178
Cdd:COG2226    14 LLAALGLRPGARVLDLGCGTGRLALALAER----GARVTGVDISPEMLELARERAAEAGLnVEFVVGDAEDLP----FPD 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 602182148 2179 QIYDLIVAADVLHATSDLRQTLVHIRQLLAPGGMLILMEDSEPARW 2224
Cdd:COG2226    86 GSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLA 131

YqjQ

COG0300

Short-chain dehydrogenase [General function prediction only];

2536-2693

6.32e-20

Short-chain dehydrogenase [General function prediction only];

Pssm-ID: 440069 [Multi-domain] Cd Length: 252 Bit Score: 91.85 E-value: 6.32e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2536 VARFLVTNGARyLVLVGRRGAREEQQAQlsELEQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVIHAAGTLNDGI 2613
Cdd:COG0300    21 LARALAARGAR-VVLVARDAERLEALAA--ELRAAGARVEVVALDVTDPDAVAALAEAVlaRFGPIDVLVNNAGVGGGGP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2614 LQQQSWQAFKEVMNPKVAGAWNLHILT----KNQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGLA-SYR---RHLGL 2685
Cdd:COG0300    98 FEELDLEDLRRVFEVNVFGPVRLTRALlplmRARGRGRIVNVSSVAGLRGLPGMAAYAASKAALEGFSeSLRaelAPTGV 177


                  ....*...
gi 602182148 2686 PSLSINWG 2693
Cdd:COG0300   178 RVTAVCPG 185

BioC

TIGR02072

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...

2097-2215

1.79e-13

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]

Pssm-ID: 273953 [Multi-domain] Cd Length: 240 Bit Score: 72.70 E-value: 1.79e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  2097 LLSALEQLPPERGWRILEIGAGTGGTTAYLLPHLPgdQTKYVFTDISAFFLAKAEERFKdyPFVRYQVLDIEQAPqaqgF 2176
Cdd:TIGR02072   23 LLALLKEKGIFIPASVLDIGCGTGYLTRALLKRFP--QAEFIALDISAGMLAQAKTKLS--ENVQFICGDAEKLP----L 94

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 602182148  2177 EPQIYDLIVAADVLHATSDLRQTLVHIRQLLAPGGMLIL 2215
Cdd:TIGR02072   95 EDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAF 133

AcpP

COG0236

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...

2805-2881

2.07e-13

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: 67.57 E-value: 2.07e-13

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 602182148 2805 TLLQAHVREQVSQVLGIDTKTLLAEQDvgFFT-LGMDSLTSVELRNRLQASLGCSLSSTLAFDYPTQQALVNYLANEL 2881
Cdd:COG0236     4 EELEERLAEIIAEVLGVDPEEITPDDS--FFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKL 79

fabG

PRK12825

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

2536-2677

5.84e-12

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

Pssm-ID: 237218 [Multi-domain] Cd Length: 249 Bit Score: 68.36 E-value: 5.84e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2536 VARFLVTNGARylVLVGRRGAREEQQAQLSELEQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVIHAAGTLNDGI 2613
Cdd:PRK12825   22 IALRLARAGAD--VVVHYRSDEEAAEELVEAVEALGRRAQAVQADVTDKAALEAAVAAAveRFGRIDILVNNAGIFEDKP 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 602182148 2614 LQQQSWQAFKEVMNPKVAGAWNL-----HILTKNQpldF--FVLFSSATSLLGNAGQANHAAANAFLDGLA 2677
Cdd:PRK12825  100 LADMSDDEWDEVIDVNLSGVFHLlravvPPMRKQR---GgrIVNISSVAGLPGWPGRSNYAAAKAGLVGLT 167

PP-binding

pfam00550

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...

2811-2869

1.57e-09

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: 56.03 E-value: 1.57e-09

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 602182148  2811 VREQVSQVLGIDTKTLLAEQDvgFFTLGMDSLTSVELRNRLQASLGCSLSSTLAFDYPT 2869
Cdd:pfam00550    3 LRELLAEVLGVPAEEIDPDTD--LFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPT 59

AdoMet_MTases

cd02440

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...

2111-2216

4.97e-09

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).

Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 56.28 E-value: 4.97e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2111 RILEIGAGTGGTTAYLLPHLPGdqtKYVFTDISAFFLAKAEERFKDYPFVRYQVL--DIEQAPQaqgFEPQIYDLIVAAD 2188
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGA---RVTGVDISPVALELARKAAAALLADNVEVLkgDAEELPP---EADESFDVIISDP 74

                          90       100
                  ....*....|....*....|....*....
gi 602182148 2189 VLHATSDLRQTLVH-IRQLLAPGGMLILM 2216
Cdd:cd02440    75 PLHHLVEDLARFLEeARRLLKPGGVLVLT 103

PRK06060

p-hydroxybenzoic acid--AMP ligase FadD22;

2801-2893

1.35e-06

p-hydroxybenzoic acid--AMP ligase FadD22;

Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 54.27 E-value: 1.35e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2801 KEGLTLLQAHVREQVSQVLGIDTKTLLAE-------QDVGFFTLGMDSLTSVELRNRLQASLGCSLSSTLAFDYPTQQAL 2873
Cdd:PRK06060  532 RERLVALRQERQRLVVDAVCAEAAKMLGEpdpwsvdQDLAFSELGFDSQMTVTLCKRLAAVTGLRLPETVGWDYGSISGL 611

                          90       100
                  ....*....|....*....|
gi 602182148 2874 VNYLANELLGTPEQLQEPES 2893
Cdd:PRK06060  612 AQYLEAELAGGHGRLKSAGP 631

PKS_PP

smart00823

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...

595-648

6.46e-06

Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 46.47 E-value: 6.46e-06

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 602182148    595 AVDIVGTHDNFFDLGGTSLLLTQAHKFLCETFNINLSAVSLFQYPTIQTLAQYI 648
Cdd:smart00823   29 AAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82

PRK08317

hypothetical protein; Provisional

2100-2217

6.14e-05

hypothetical protein; Provisional

Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 47.24 E-value: 6.14e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2100 ALEQLPPERGWRILEIGAGTGGTTAYlLPHLPGDQTKYVFTDISAFFLAKAEERFK-DYPFVRYQVLDIEQAPqaqgFEP 2178
Cdd:PRK08317   11 TFELLAVQPGDRVLDVGCGPGNDARE-LARRVGPEGRVVGIDRSEAMLALAKERAAgLGPNVEFVRGDADGLP----FPD 85

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 602182148 2179 QIYDLIVAADVLHATSDLRQTLVHIRQLLAPGGMLILME 2217
Cdd:PRK08317   86 GSFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVLD 124

Name

Accession

Description

Interval

E-value

PksD

COG3321

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...

673-2008

0e+00

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];

Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 1312.56 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  673 DSNDIAIISVAGRFPGAETIEQFWHNLCNGVESITLFSDDKLEQTL----PELFNNPAYVKAGAVLEGVELFDATFFGYS 748
Cdd:COG3321     2 ADEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWDADAyydpDPDAPGKTYVRWGGFLDDVDEFDALFFGIS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  749 PKEAAVTDPQQRILLECAWEAFERAGYNPETYP-EPVGVYAGSSLSTYLLNNIGSALGIiteqpfietdmeQFQAKIGND 827
Cdd:COG3321    82 PREAEAMDPQQRLLLEVAWEALEDAGYDPESLAgSRTGVFVGASSNDYALLLLADPEAI------------DAYALTGNA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  828 RSYLATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQKGGYLYEEGMVRSQDGHCRAFD 907
Cdd:COG3321   150 KSVLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFD 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  908 AEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGAIKmGYTAPSVDGQADVISEAIAIADIDASTIGYVEA 987
Cdd:COG3321   230 ADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSN-GLTAPNGPAQAAVIRRALADAGVDPATVDYVEA 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  988 HGTATQLGDPIEVAGLARAFQRSTDsvlGKQQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPRID 1067
Cdd:COG3321   309 HGTGTPLGDPIEAAALTAAFGQGRP---ADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHID 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1068 FDATPFFVNTELREWSRNGYPRRAGVSSFGVGGTNSHIVLEESPVKQPTlfSSLPERSHHLLTLSAHTQEALHELVQRYI 1147
Cdd:COG3321   386 FENSPFYVNTELRPWPAGGGPRRAGVSSFGFGGTNAHVVLEEAPAAAPA--AAAAARPPQLLVLSAKTEEALRALAARLA 463

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1148 QHNETHLDIDLGDLCFTANTGRKHFEHRLAVVAESIPGLQAQLETAQTAISAQ-----KKNAPPTIAFLFTGQGSQYINM 1222
Cdd:COG3321   464 AFLEAHPDLDLADVAYTLATGRAHFEHRLAVVASSREELAAKLRALAAGEAAPgvvtgAAAAAPKVAFLFPGQGSQYVGM 543

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1223 GRTLYDTESTFRAALDRCETILQNLGIESIISVIFGSSEHGLsLDDTAYTQPALFAIEYALYQLWKSWGIQPSVVIGHSV 1302
Cdd:COG3321   544 GRELYETEPVFRAALDECDALLRPHLGWSLREVLFPDEEESR-LDRTEVAQPALFAVEYALARLWRSWGVRPDAVIGHSV 622

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1303 GEYVSACVAGVFSLEDGLKLIAERGRLIQALPRDGSMVSVMASEKRIADIILPYGGqVGIAAINGPQSVVISGQQQAIDA 1382
Cdd:COG3321   623 GEYAAACVAGVLSLEDALRLVAARGRLMQALPGGGAMLAVGLSEEEVEALLAGYDG-VSIAAVNGPRSTVVSGPAEAVEA 701

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1383 ICAILETEGIKSKKLNVSHAFHSPLVEAMLDSFLQVAQEVTYSQPQIKLISNVTGTLASHEscpdelpITTAEYWVRHVR 1462
Cdd:COG3321   702 LAARLEARGIRARRLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIPLISNVTGTWLTGE-------ALDADYWVRHLR 774

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1463 QPVRFAAGMESLEGQGVNVFIEIGPKPVLLGMGRDCLPEQE-GLWLPSLRPKQDDWQQVLSSLRDLYLVGVTIDWSSFDQ 1541
Cdd:COG3321   775 QPVRFADAVEALLADGVRVFLEVGPGPVLTGLVRQCLAAAGdAVVLPSLRRGEDELAQLLTALAQLWVAGVPVDWSALYP 854

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1542 GYARRRVPLPTYPWQRERHWVEPIIRHRQSVLQATNTTKLTRNASVAQHPLLGQRLHLSRTQEIYFQTFIHSDFPIWVAD 1621
Cdd:COG3321   855 GRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVA 934

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1622 HKVFGNVIIPGVAYFEMALAAGKALKPDSIFWLEDVSIAQALIIPDEGQTVQIVLSPQEESAyffeILSLEKENSWVLHA 1701
Cdd:COG3321   935 LAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAAL----AAAAALALLAAAAL 1010

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1702 SGKLVAQEQVLETEPIDLIALQAHCCEEVSVDVLYQEEMARRLDMGPMMRGVKQLWRYPLSFAKSHDAIALAKVSLPEIL 1781
Cdd:COG3321  1011 LLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAAL 1090

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1782 LHESNAYQFHPVILDAGLQMITVSYPEANQGQTYVPVGIEGLQVYGRPSSELWCRAQYRPPLDTDQRQGIDLLPKKLIAD 1861
Cdd:COG3321  1091 AAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAA 1170

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1862 LHLFDTQGRVVAIMFGVQSVLVGREAMLRSQDTWRNWLYQVLWKPQACFGLLPNYLPTPDKIRKRLETKLATLIIEANLA 1941
Cdd:COG3321  1171 AALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAA 1250

                        1290      1300      1310      1320      1330      1340
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 602182148 1942 TYAIAYTQLERLSLAYVVAAFRQMGWLFQPGERFSTAQKVSALGIVDQHRQLFARLLDILAEADILR 2008
Cdd:COG3321  1251 AAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAA 1317

PKS

cd00833

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...

675-1107

0e+00

Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 610.33 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  675 NDIAIISVAGRFPGAETIEQFWHNLCNGVESITLFSDDKLEQTL---PELFNNPAYVKAGAVLEGVELFDATFFGYSPKE 751
Cdd:cd00833     1 EPIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGyypDPGKPGKTYTRRGGFLDDVDAFDAAFFGISPRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  752 AAVTDPQQRILLECAWEAFERAGYNPET-YPEPVGVYAGSSLSTYLLNNIGSALGIiteqpfietdmEQFQAkIGNDRSY 830
Cdd:cd00833    81 AEAMDPQQRLLLEVAWEALEDAGYSPESlAGSRTGVFVGASSSDYLELLARDPDEI-----------DAYAA-TGTSRAF 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  831 LATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQKGGYLYEEGMVRSQDGHCRAFDAEA 910
Cdd:cd00833   149 LANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADA 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  911 QGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGAIKmGYTAPSVDGQADVISEAIAIADIDASTIGYVEAHGT 990
Cdd:cd00833   229 DGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTK-GITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGT 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  991 ATQLGDPIEVAGLARAFQRSTDsvlGKQQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPRIDFDA 1070
Cdd:cd00833   308 GTPLGDPIEVEALAKVFGGSRS---ADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEE 384

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 602182148 1071 TPFFVNTELREWSRNGYPRRAGVSSFGVGGTNSHIVL 1107
Cdd:cd00833   385 SPLRVPTEARPWPAPAGPRRAGVSSFGFGGTNAHVIL 421

EntF

COG1020

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...

3-663

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: 603.77 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    3 ERESPQILFDGNGTQSEFP-DSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIE 81
Cdd:COG1020   455 AAERQQLLAEWNATAAPYPaDATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLE 534

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   82 RSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLTSTDVAKKLaltiPALQeCQTVYLDQEifeydfhfl 161
Cdd:COG1020   535 RSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARL----PELG-VPVLALDAL--------- 600

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  162 aiakllhnqylrllhfyfytLIQQCQATSVSQGIQtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSV 241
Cdd:COG1020   601 --------------------ALAAEPATNPPVPVT----PDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLG 656

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  242 QGVRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNgnkSTSLAL 321
Cdd:COG1020   657 PGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAP---EALPSL 733

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  322 CEVITTGEQmqITPAVANLFQKT--GAMLHNHYGATEFQ-DATTHTLKGNPEGWPTlVPVGRPLHNVQVYILDEAQQPVP 398
Cdd:COG1020   734 RLVLVGGEA--LPPELVRRWRARlpGARLVNLYGPTETTvDSTYYEVTPPDADGGS-VPIGRPIANTRVYVLDAHLQPVP 810

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  399 LGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGtnENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEI 478
Cdd:COG1020   811 VGVPGELYIGGAGLARGYLNRPELTAERFVADPFG--FPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEI 888

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  479 ESVLASHQAVRECAVVAREIA-GHTQLVGYIIAKDTLnlsfDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLD 557
Cdd:COG1020   889 EAALLQHPGVREAVVVAREDApGDKRLVAYVVPEAGA----AAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLD 964

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  558 RRALPDPkgDRPALSTPLVKPRTQTEKRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKFLCETFNINLSAVSLFQ 637
Cdd:COG1020   965 RLALPAP--AAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLA 1042

                         650       660
                  ....*....|....*....|....*.
gi 602182148  638 YPTIQTLAQYIDCQGDTTSSNTASRH 663
Cdd:COG1020  1043 AAAAAAAAAAAAAAAAAAAPLAAAAA 1068

A_NRPS_VisG_like

cd17651

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...

29-562

0e+00

Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 578.91 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   29 FEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYP 108
Cdd:cd17651     1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  109 ADRIEYMLRDSDARILLTSTDVAKKLALTIPALqecqtVYLDQEifeydfhflaiakllhnqylrllhfyfytliQQCQA 188
Cdd:cd17651    81 AERLAFMLADAGPVLVLTHPALAGELAVELVAV-----TLLDQP-------------------------------GAAAG 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  189 TSVSQGIQTQvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTLCLG 268
Cdd:cd17651   125 ADAEPDPALD--ADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAG 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  269 GILVLVPEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALCEVITTGEQMQITPAVANLFQK-TGAM 347
Cdd:cd17651   203 ATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLVLTEDLREFCAGlPGLR 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  348 LHNHYGATEFQDATTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKF 427
Cdd:cd17651   283 LHNHYGPTETHVVTALSLPGDPAAWPAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERF 362

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  428 IPNPFGTNEnakKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVARE-IAGHTQLVG 506
Cdd:cd17651   363 VPDPFVPGA---RMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREdRPGEKRLVA 439

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 602182148  507 YIIAKDTLNLSFDKlepiLRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALP 562
Cdd:cd17651   440 YVVGDPEAPVDAAE----LRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491

A_NRPS

cd05930

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...

37-561

3.09e-177

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: 552.13 E-value: 3.09e-177

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   37 PDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYML 116
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  117 RDSDARILLTStdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiq 196
Cdd:cd05930    81 EDSGAKLVLTD--------------------------------------------------------------------- 91

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  197 tqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPE 276
Cdd:cd05930    92 ----PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPE 167

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  277 AVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALceVITTGEQMqiTPAVANLFQKT--GAMLHNHYGA 354
Cdd:cd05930   168 EVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSLRL--VLVGGEAL--PPDLVRRWRELlpGARLVNLYGP 243

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  355 TEFQ-DATTHTLKGNPEGwPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFG 433
Cdd:cd05930   244 TEATvDATYYRVPPDDEE-DGRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFG 322

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  434 TNEnakKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVARE-IAGHTQLVGYIIAKD 512
Cdd:cd05930   323 PGE---RMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREdGDGEKRLVAYVVPDE 399

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 602182148  513 TLNLSFDKlepiLRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05930   400 GGELDEEE----LRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444

mycolic_Pks13

NF040607

polyketide synthase Pks13;

628-1563

4.38e-169

polyketide synthase Pks13;

Pssm-ID: 468580 [Multi-domain] Cd Length: 1671 Bit Score: 570.33 E-value: 4.38e-169

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  628 INLSAVSLFQYPTIQTLAQYIdCQGDTTSSNTASRHKKVRKKQSGDSNDIAIISVAGRFPGA-ETIEQFWHNLCNGVESI 706
Cdd:NF040607   54 VTLTATVAYQHPTIASLATRI-IEGEPEVAADDDDDADWSRRPRSDAHDIAIVGLATRFPGAgNTPEEMWEALIEGRDGI 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  707 TLFSDDKLEqtlpELFNNPAYVKA-------GAVLEGVELFDATFFGYSPKEAAVTDPQQRILLECAWEAFERAGYNPET 779
Cdd:NF040607  133 TDLPEGRWS----EFAADPRIAERvakantrGGYLDDIKGFDAEFFALSPLEAENVDPQQRLALELTWEALEHARIPASS 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  780 YP-EPVGVYAGSSLSTY-LLnnigSALGIITEQPFietdmeqfqAKIGNDRSYLATRISYKLNLKGPSVNVQTACSTSLV 857
Cdd:NF040607  209 LRgEPVGVFIGSSNNDYqML----AVADPAEAHPY---------ALTGTSSSIIANRVSYFFDFRGPSVAVDTACSSSLV 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  858 AVHMACQSLISGECQMALAGGISVVVPQKGGYLYEE-GMVRSQDGHCRAFDAEAQGTIFGNGGGLVLLKRLQDALDDNDN 936
Cdd:NF040607  276 AVHQAVRALRSGEADVAVAGGVNMLLTPAVTLGFDElGGVLAPDGRIKAFSSDADGMVRSEGGGVVVLKRLADARRDGDT 355

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  937 IMAVIKATAINNDGAiKMGYTAPSVDGQADVISEAIAIADIDASTIGYVEAHGTATQLGDPIEVAGLARafqrstdsVLG 1016
Cdd:NF040607  356 ILAVIAGSAVNSDGR-SNGLTAPNPDAQVDVLRRAYADAGIDPRTVDYVEAHGTGTILGDPIEADALGR--------VVG 426

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1017 KQQCA-----IGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPRIDFDATPFFVNTELREWSR-NGYPrR 1090
Cdd:NF040607  427 RGRDAdkpalLGSAKTNFGHLESAAGAAGLAKVVLAMQHDKLPPSLNYAGPNPYIDFDAEHLKVVDEPTEWPRySGHA-V 505

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1091 AGVSSFGVGGTNSHIVLEE--SPVKQPTLFSSLPERSHHLLTLSAHTQEALHELVQRYIQHNETH--------------- 1153
Cdd:NF040607  506 AGVSGFGFGGTNAHVVVREvlPADLVEPEAQPDEDTEAELAGLTAEAKRLLAEAELAAEFAPAAPegpvvplpvsgflps 585

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1154 ------------LDIDLG---DLCFTANT--GRKHFEHRLAVVA----ESIPGLQAQLE--TAQTAISAqkkNAPPTI-- 1208
Cdd:NF040607  586 rrraaaadladwLESEEGratPLADVARAlaRRNHGRSRAVVLAhtheEAIKGLRAVAEgkPGPGVFSA---DAPAANgp 662

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1209 AFLFTGQGSQYINMGRTLYDTESTFRAALDRCETILQNLGIESIISVIfgssehglsLDD-----TAYTQPALFAIEYAL 1283
Cdd:NF040607  663 VWVLSGFGSQHRKMAKQLYLENPVFAARIDEVDELVQDESGYSIVELI---------LDDeqtydIETAQVGIFAIQIAL 733

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1284 YQLWKSWGIQPSVVIGHSVGEYVSACVAGVFSLEDGLKLIAERGRLI----QALPRD--GSMVSVMASEKRIADIILPYG 1357
Cdd:NF040607  734 ADLLRHHGAKPAAVVGHSMGEAAAAYAAGGLSLEDAVRVICHRSRLMgegeAMLPGDdiRLMALVEYSAEEIETVLADFP 813

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1358 GqVGIAAINGPQSVVISGQQQAIDAICAILETEGIKSKKLNVSHAFHSplveAMLDSFL-QVAQEVTYSQPQ---IKLIS 1433
Cdd:NF040607  814 D-LEVCVYAAPTHTVIGGPREQVDAIVARAEAEGKFARKLQTKGASHT----SQMDPLLgELAAELAGIEPQpltVGLYS 888

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1434 NV-TGTL--ASHEscpdelPITTAEYWVRHVRQPVRFAAGMESLEGQGVNVFIEIGPKPV-LLGMGRDC----LPEQEgl 1505
Cdd:NF040607  889 SVdRGTFyrPGHE------PIHDVDYWVKGLRHSVWFTQAVRKAVDAGHTTFLELAPNPVaLMSVAATTfaagLHDAQ-- 960

                         970       980       990      1000      1010      1020
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1506 WLPSLRPKQDDWQQVLSSLRDLYLVGVTIDWSS-FDQG-YArrrvPLPTYPWQRERHWVE 1563
Cdd:NF040607  961 LIPTLKRKEDESESVLNALAQLYVHGHDVDLRSlFGAGdYA----DIPRTRFKRKPYWLD 1016

A_NRPS_Bac

cd17655

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...

28-564

4.92e-161

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: 508.02 E-value: 4.92e-161

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   28 LFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGY 107
Cdd:cd17655     2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  108 PADRIEYMLRDSDARILLTSTDVAKKLALTipalqecQTVYL--DQEIFEYDFHFLAIakllhnqylrllhfyfytliqq 185
Cdd:cd17655    82 PEERIQYILEDSGADILLTQSHLQPPIAFI-------GLIDLldEDTIYHEESENLEP---------------------- 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  186 cqatsVSQgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTL 265
Cdd:cd17655   133 -----VSK-------SDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASL 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  266 CLGGILVLVPEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAvngNKSTSLALCEVITTGEQMqiTPAVANLFQK-- 343
Cdd:cd17655   201 LSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLKLLDAA---DDSEGLSLKHLIVGGEAL--STELAKKIIElf 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  344 -TGAMLHNHYGATEFQ-DATTHTLKGNPEGWPTlVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPD 421
Cdd:cd17655   276 gTNPTITNAYGPTETTvDASIYQYEPETDQQVS-VPIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPE 354

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  422 LTNEKFIPNPFGTNEnakKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIA-G 500
Cdd:cd17655   355 LTAEKFVDDPFVPGE---RMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEqG 431

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 602182148  501 HTQLVGYIIAKDTLNLSfdklepILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALPDP 564
Cdd:cd17655   432 QNYLCAYIVSEKELPVA------QLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPEP 489

A_NRPS_ApnA-like

cd17644

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...

24-562

9.30e-156

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: 491.56 E-value: 9.30e-156

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   24 CIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPL 103
Cdd:cd17644     1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  104 DVGYPADRIEYMLRDSDARILLTStdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytli 183
Cdd:cd17644    81 DPNYPQERLTYILEDAQISVLLTQ-------------------------------------------------------- 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  184 qqcqatsvsqgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFS 263
Cdd:cd17644   105 -----------------PENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYV 167

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  264 TLCLGGILVLVPEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSL-ALCEVITTGEQMQitPAVANLFQ 342
Cdd:cd17644   168 TLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLPsSLRLVIVGGEAVQ--PELVRQWQ 245

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  343 KTGA---MLHNHYGATEFQ-DATTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHN 418
Cdd:cd17644   246 KNVGnfiQLINVYGPTEATiAATVCRLTQLTERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLN 325

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  419 LPDLTNEKFIPNPFGTNEnAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVARE- 497
Cdd:cd17644   326 RPELTAEKFISHPFNSSE-SERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREd 404

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 602182148  498 IAGHTQLVGYIIAKDTLNLSFDKlepiLRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALP 562
Cdd:cd17644   405 QPGNKRLVAYIVPHYEESPSTVE----LRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRALP 465

PKS_KS

smart00825

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...

677-1109

1.29e-151

Pssm-ID: 214836 [Multi-domain] Cd Length: 298 Bit Score: 472.20 E-value: 1.29e-151

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    677 IAIISVAGRFPGAETIEQFWHNLCNGvesitlfsddkleqtlpelfnnpayvkagavLEGVELFDATFFGYSPKEAAVTD 756
Cdd:smart00825    1 IAIVGMSCRFPGADDPEEFWDLLLAG-------------------------------LDDVDLFDAAFFGISPREAEAMD 49

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    757 PQQRILLECAWEAFERAGYNPETYPE-PVGVYAGSSLSTYllnnigsalgiiteqpfietdmeqfqakigndrsylatri 835
Cdd:smart00825   50 PQQRLLLEVAWEALEDAGIDPESLRGsRTGVFVGVSSSDY---------------------------------------- 89

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    836 syklnlkgpSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQKGGYLYEEGMVRSQDGHCRAFDAEAQGTIF 915
Cdd:smart00825   90 ---------SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVR 160

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    916 GNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGAiKMGYTAPSVDGqadviseaiaiadidastigyveahgtatqlg 995
Cdd:smart00825  161 GEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGR-SNGITAPSGPA-------------------------------- 207

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    996 dpievaglarafqrstdsvlgkqQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPRIDFDATPFFV 1075
Cdd:smart00825  208 -----------------------QLLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRV 264

                           410       420       430
                    ....*....|....*....|....*....|....
gi 602182148   1076 NTELREWSRNGYPRRAGVSSFGVGGTNSHIVLEE 1109
Cdd:smart00825  265 PTELTPWPPPGRPRRAGVSSFGFGGTNAHVILEE 298

A_NRPS_Srf_like

cd12117

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...

28-561

1.30e-150

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: 477.85 E-value: 1.30e-150

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   28 LFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGY 107
Cdd:cd12117     2 LFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  108 PADRIEYMLRDSDARILLTSTDVAKKLALTIPALqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytLIQQCQ 187
Cdd:cd12117    82 PAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAV----------------------------------------VIDEAL 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  188 ATSVSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNmLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTLCL 267
Cdd:cd12117   122 DAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVR-LVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLN 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  268 GGILVLVPEAVRQNPFALAEFISQQKIEKLFLpvIALL--QLAEAVNGnkstSLA-LCEVITTGEQMQItPAVANLFQKT 344
Cdd:cd12117   201 GARLVLAPKGTLLDPDALGALIAEEGVTVLWL--TAALfnQLADEDPE----CFAgLRELLTGGEVVSP-PHVRRVLAAC 273

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  345 GAM-LHNHYGATE---FqdATTHTLkGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLP 420
Cdd:cd12117   274 PGLrLVNGYGPTEnttF--TTSHVV-TELDEVAGSIPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRP 350

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  421 DLTNEKFIPNPFGTNEnakKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIA- 499
Cdd:cd12117   351 ALTAERFVADPFGPGE---RLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAg 427

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 602182148  500 GHTQLVGYIIAKDTLNlsfdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd12117   428 GDKRLVAYVVAEGALD------AAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483

A_NRPS_ProA

cd17656

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...

37-562

1.14e-148

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: 471.96 E-value: 1.14e-148

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   37 PDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYML 116
Cdd:cd17656     2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  117 RDSDARILLTSTDVAKKLAltipalqecqtvyldqeiFEYDFHFLAiakllhnqylrllhfyfYTLIQQCQAtsvsQGIQ 196
Cdd:cd17656    82 LDSGVRVVLTQRHLKSKLS------------------FNKSTILLE-----------------DPSISQEDT----SNID 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  197 TQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPE 276
Cdd:cd17656   123 YINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIRE 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  277 AVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALCEVITTGEQMQITPAVANLFQKTGAMLHNHYGATE 356
Cdd:cd17656   203 ETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFINRFPTCVKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSE 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  357 FQDATTHTLKGNPEgWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGTNe 436
Cdd:cd17656   283 THVVTTYTINPEAE-IPELPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPN- 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  437 naKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAR-EIAGHTQLVGYIIAKDTLN 515
Cdd:cd17656   361 --ERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKaDDKGEKYLCAYFVMEQELN 438

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 602182148  516 LSfdklepILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALP 562
Cdd:cd17656   439 IS------QLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKALP 479

PRK12467

peptide synthase; Provisional

3-645

1.39e-148

peptide synthase; Provisional

Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 522.03 E-value: 1.39e-148

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    3 ERESPQILFDGNGTQSEFP-DSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIE 81
Cdd:PRK12467 1553 EAERRQILEGWNATHTGYPlARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVE 1632

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   82 RSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLTSTDVAKKLaltiPALQECQTVYLDQEifeydfhfl 161
Cdd:PRK12467 1633 RSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARL----PLPDGLRSLVLDQE--------- 1699

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  162 aiakllhnqylrllhfyfytliQQCQATSVSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSV 241
Cdd:PRK12467 1700 ----------------------DDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLS 1757

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  242 QGVRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRQNPFALAEFISQQKIEKL-FLPVI--ALLQLAEAVNGnkstS 318
Cdd:PRK12467 1758 AADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLhFVPSMlqQLLQMDEQVEH----P 1833

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  319 LALCEVITTGEQMQITPAVANLFQKTGAMLHNHYGATEFQDATTHTL--KGNPEGWPTlVPVGRPLHNVQVYILDEAQQP 396
Cdd:PRK12467 1834 LSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTcrRKDLEGRDS-VPIGQPIANLSTYILDASLNP 1912

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  397 VPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGTNenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELG 476
Cdd:PRK12467 1913 VPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGTV--GSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELG 1990

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  477 EIESVLASHQAVRECAVVAREIAGHTQLVGYIIAKDTLNLSFDK----LEPILRQYSEAVLPEYMIPTRFINISNMPLTP 552
Cdd:PRK12467 1991 EIEARLREQGGVREAVVIAQDGANGKQLVAYVVPTDPGLVDDDEaqvaLRAILKNHLKASLPEYMVPAHLVFLARMPLTP 2070

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  553 SGKLDRRALPDPkgDRPALSTPLVKPRTQTEKRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKfLCETFNINLSA 632
Cdd:PRK12467 2071 NGKLDRKALPAP--DASELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVS-RARQAGIRFTP 2147

                         650
                  ....*....|...
gi 602182148  633 VSLFQYPTIQTLA 645
Cdd:PRK12467 2148 KDLFQHQTVQSLA 2160

A_NRPS_AB3403-like

cd17646

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...

26-561

8.65e-147

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: 466.75 E-value: 8.65e-147

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   26 HHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDV 105
Cdd:cd17646     1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  106 GYPADRIEYMLRDSDARILLTSTDVAKKLALTIPALQECQTVYldqeifeydfhflaiakllhnqylrllhfyfytliqq 185
Cdd:cd17646    81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEAL------------------------------------- 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  186 cqATSVSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTL 265
Cdd:cd17646   124 --AAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPL 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  266 CLGGILVLVPEAVRQNPFALAEFISQQKIEKL-FLPVI--ALLQLAEAvngnkSTSLALCEVITTGEQMqiTPAVANLF- 341
Cdd:cd17646   202 VAGARLVVARPGGHRDPAYLAALIREHGVTTChFVPSMlrVFLAEPAA-----GSCASLRRVFCSGEAL--PPELAARFl 274

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  342 QKTGAMLHNHYGATEFQ-DATTHTLKGNPEGWPtlVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLP 420
Cdd:cd17646   275 ALPGAELHNLYGPTEAAiDVTHWPVRGPAETPS--VPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRP 352

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  421 DLTNEKFIPNPFGTNEnakKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREI-A 499
Cdd:cd17646   353 ALTAERFVPDPFGPGS---RMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAApA 429

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 602182148  500 GHTQLVGYIIAKDTlnlSFDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd17646   430 GAARLVGYVVPAAG---AAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488

PRK12316

peptide synthase; Provisional

1-652

4.03e-146

peptide synthase; Provisional

Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 514.51 E-value: 4.03e-146

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    1 MQERESPQILFDGNGTQSEFPDS-CIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAIC 79
Cdd:PRK12316 4528 LEKAEQQRIVALWNRTDAGYPATrCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIA 4607

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   80 IERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLTSTDVAKKLaltiPALQECQTVYLDQEIFEYDFH 159
Cdd:PRK12316 4608 MERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRL----PIPDGLASLALDRDEDWEGFP 4683

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  160 FLAIAKLLHnqylrllhfyfytliqqcqatsvsqgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRP 239
Cdd:PRK12316 4684 AHDPAVRLH--------------------------------PDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYE 4731

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  240 SVQGVRTLQFCAVSFDFSCHEIFSTLCLGGiLVLVPEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAE--AVNGNkst 317
Cdd:PRK12316 4732 LTPDDRVLQFMSFSFDGSHEGLYHPLINGA-SVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEhaERDGE--- 4807

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  318 SLALCEVITTGEQMQITPAVANLFQKTGAMLHNHYGATEFQDATTH--TLKGNPEGwPTLVPVGRPLHNVQVYILDEAQQ 395
Cdd:PRK12316 4808 PPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLwkARDGDACG-AAYMPIGTPLGNRSGYVLDGQLN 4886

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  396 PVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGtnENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVEL 475
Cdd:PRK12316 4887 PLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFG--APGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIEL 4964

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  476 GEIESVLASHQAVRECAVVAREIAGHTQLVGYIIAKDTLNLSFDKLEPILRQYSEA----VLPEYMIPTRFINISNMPLT 551
Cdd:PRK12316 4965 GEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALADADEAQAELRDELKAalreRLPEYMVPAHLVFLARMPLT 5044

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  552 PSGKLDRRALPDPkgDRPALSTPLVKPRTQTEKRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKFLCETFNINLS 631
Cdd:PRK12316 5045 PNGKLDRKALPQP--DASLLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELP 5122

                         650       660
                  ....*....|....*....|.
gi 602182148  632 AVSLFQYPTIQTLAQYIDCQG 652
Cdd:PRK12316 5123 LRELFQTPTLAAFVELAAAAG 5143

PRK12467

peptide synthase; Provisional

8-648

1.81e-145

peptide synthase; Provisional

Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 512.01 E-value: 1.81e-145

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    8 QILFDGNGTQSEFP-DSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAEL 86
Cdd:PRK12467 3079 QVLHAWNATAAAYPsERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEM 3158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   87 FIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLTSTDVAKKLaltiPALQECQTVYLDQEIFEydfhflaiAKL 166
Cdd:PRK12467 3159 IVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQL----PAPAGDTALTLDRLDLN--------GYS 3226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  167 LHNqylrllhfyfytliqqcqatsvsqgIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRT 246
Cdd:PRK12467 3227 ENN-------------------------PSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRV 3281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  247 LQFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRqNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLAlcEVIT 326
Cdd:PRK12467 3282 LLFMSFSFDGAQERFLWTLICGGCLVVRDNDLW-DPEELWQAIHAHRISIACFPPAYLQQFAEDAGGADCASLD--IYVF 3358

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  327 TGEQMQITpAVANLFQKTG-AMLHNHYGATEFQDATTH-TLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGE 404
Cdd:PRK12467 3359 GGEAVPPA-AFEQVKRKLKpRGLTNGYGPTEAVVTVTLwKCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGE 3437

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  405 FCIGGIGLARGYHNLPDLTNEKFIPNPFGTNenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLAS 484
Cdd:PRK12467 3438 LYIGGVGLARGYHQRPSLTAERFVADPFSGS--GGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQ 3515

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  485 HQAVRECAVVAREIAGHTQLVGYIIAKDtlnLSFDKLEpILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALPDP 564
Cdd:PRK12467 3516 HPSVREAVVLARDGAGGKQLVAYVVPAD---PQGDWRE-TLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDP 3591

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  565 KGDrpaLSTPLVKPRTQTEKRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKFLCETFNINLSAVSLFQYPTIQTL 644
Cdd:PRK12467 3592 DAK---GSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAEL 3668


                  ....
gi 602182148  645 AQYI 648
Cdd:PRK12467 3669 AGYS 3672

PRK12467

peptide synthase; Provisional

5-657

1.51e-143

peptide synthase; Provisional

Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 505.85 E-value: 1.51e-143

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    5 ESPQILFDGNGTQSEFPDSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSA 84
Cdd:PRK12467  494 ERARELVRWNAPATEYAPDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSI 573

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   85 ELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLTSTDVAKKLALtiPAlqecqtvyldqeifeydfhflAIA 164
Cdd:PRK12467  574 EMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPV--PA---------------------GLR 630

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  165 KLLHNQYLRLLhfyfytliQQCQATSVSqgiqTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGV 244
Cdd:PRK12467  631 SLCLDEPADLL--------CGYSGHNPE----VALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADD 698

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  245 RTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAvnGNKSTSLALCEV 324
Cdd:PRK12467  699 SMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQA--SRVALPRPQRAL 776

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  325 ITTGEQMQITpAVANLFQKT-GAMLHNHYGATEFQ-DATTHTLKGNPEGWPTlVPVGRPLHNVQVYILDEAQQPVPLGGE 402
Cdd:PRK12467  777 VCGGEALQVD-LLARVRALGpGARLINHYGPTETTvGVSTYELSDEERDFGN-VPIGQPLANLGLYILDHYLNPVPVGVV 854

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  403 GEFCIGGIGLARGYHNLPDLTNEKFIPNPFGTNenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVL 482
Cdd:PRK12467  855 GELYIGGAGLARGYHRRPALTAERFVPDPFGAD--GGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARL 932

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  483 ASHQAVRECAVVAREIAGHTQLVGYII----AKDTLNLSF-DKLEPILRQyseaVLPEYMIPTRFINISNMPLTPSGKLD 557
Cdd:PRK12467  933 LAQPGVREAVVLAQPGDAGLQLVAYLVpaavADGAEHQATrDELKAQLRQ----VLPDYMVPAHLLLLDSLPLTPNGKLD 1008

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  558 RRALPDPkgDRPALSTPLVKPRTQTEKRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKFLCETFNINLSAVSLFQ 637
Cdd:PRK12467 1009 RKALPKP--DASAVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFE 1086

                         650       660
                  ....*....|....*....|
gi 602182148  638 YPTIQTLAQYIDCQGDTTSS 657
Cdd:PRK12467 1087 HQTLAGFAQAVAAQQQGAQP 1106

PRK12316

peptide synthase; Provisional

5-646

1.62e-141

peptide synthase; Provisional

Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 499.48 E-value: 1.62e-141

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    5 ESPQILFDGNGTQSEFP-DSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERS 83
Cdd:PRK12316  492 ERGQLVEGWNATAAEYPlQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERS 571

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   84 AELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLTSTDVAKKLaltiPALQECQTVYLDQEIFEYDFHFlai 163
Cdd:PRK12316  572 IEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKL----PLAAGVQVLDLDRPAAWLEGYS--- 644

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  164 akllhnqylrllhfyfytliqqcqatsvSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQG 243
Cdd:PRK12316  645 ----------------------------EENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVG 696

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  244 VRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALce 323
Cdd:PRK12316  697 DTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRR-- 774

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  324 VITTGEQMQITpAVANLFQK-TGAMLHNHYGATEFQDATTHTLKGNpEGWPTlVPVGRPLHNVQVYILDEAQQPVPLGGE 402
Cdd:PRK12316  775 IVCSGEALPAD-AQEQVFAKlPQAGLYNLYGPTEAAIDVTHWTCVE-EGGDS-VPIGRPIANLACYILDANLEPVPVGVL 851

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  403 GEFCIGGIGLARGYHNLPDLTNEKFIPNPFGTNEnakKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVL 482
Cdd:PRK12316  852 GELYLAGRGLARGYHGRPGLTAERFVPSPFVAGE---RMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARL 928

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  483 ASHQAVRECAVVAreiAGHTQLVGYIIAKDTLNlsfdKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALP 562
Cdd:PRK12316  929 LEHPWVREAAVLA---VDGKQLVGYVVLESEGG----DWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALP 1001

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  563 DPKGDRPALStpLVKPRTQTEKRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKfLCETFNINLSAVSLFQYPTIQ 642
Cdd:PRK12316 1002 APEASVAQQG--YVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVS-RARQAGIQLSPRDLFQHQTIR 1078


                  ....
gi 602182148  643 TLAQ 646
Cdd:PRK12316 1079 SLAL 1082

AA-adenyl-dom

TIGR01733

amino acid adenylation domain; This model represents a domain responsible for the specific ...

50-493

2.14e-141

Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 447.87 E-value: 2.14e-141

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    50 TYGELNVRANHLAQHLLSLGC-QPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLTST 128
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAGGvGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   129 DVAKKLAltipalqecqtvYLDQEIFEYDFHFLAIAkllhnqylrllhfyfytliqqcQATSVSQGIQTQVLPNNLAYCI 208
Cdd:TIGR01733   81 ALASRLA------------GLVLPVILLDPLELAAL----------------------DDAPAPPPPDAPSGPDDLAYVI 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   209 YTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRQNPFAL-AE 287
Cdd:TIGR01733  127 YTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALlAA 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   288 FISQQKIEKLFLPVIALLQLAEAVNGNKSTslaLCEVITTGEQmqITPAVANLFQKT--GAMLHNHYGATEFQ-DATTHT 364
Cdd:TIGR01733  207 LIAEHPVTVLNLTPSLLALLAAALPPALAS---LRLVILGGEA--LTPALVDRWRARgpGARLINLYGPTETTvWSTATL 281

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   365 LKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGTNENAKkLYRT 444
Cdd:TIGR01733  282 VDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAGGDGAR-LYRT 360

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 602182148   445 GDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAV 493
Cdd:TIGR01733  361 GDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409

PKS_AT

smart00827

Acyl transferase domain in polyketide synthase (PKS) enzymes;

1211-1513

2.86e-139

Acyl transferase domain in polyketide synthase (PKS) enzymes;

Pssm-ID: 214838 [Multi-domain] Cd Length: 298 Bit Score: 436.83 E-value: 2.86e-139

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   1211 LFTGQGSQYINMGRTLYDTESTFRAALDRCETILQNLGIESIISVIFGSSEHGlSLDDTAYTQPALFAIEYALYQLWKSW 1290
Cdd:smart00827    1 VFTGQGSQWAGMGRELYETEPVFREALDECDAALQPLLGWSLLDVLLGEDGAA-SLLDTEVAQPALFAVQVALARLLRSW 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   1291 GIQPSVVIGHSVGEYVSACVAGVFSLEDGLKLIAERGRLIQALPRDGSMVSVMASEKRIADIILPYGGQVGIAAINGPQS 1370
Cdd:smart00827   80 GVRPDAVVGHSSGEIAAAYVAGVLSLEDAARLVAARGRLMQALPGGGAMLAVGLSEEEVEPLLAGVPDRVSVAAVNSPSS 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   1371 VVISGQQQAIDAICAILETEGIKSKKLNVSHAFHSPLVEAMLDSFLQVAQEVTYSQPQIKLISNVTGTLASHEScpdelp 1450
Cdd:smart00827  160 VVLSGDEDAVDELAARLEAEGIFARRLKVDHAFHSPHMEPILDEFRAALAGLTPRPPRIPFVSTVTGTLIDGAE------ 233

                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 602182148   1451 ITTAEYWVRHVRQPVRFAAGMESL-EGQGVNVFIEIGPKPVLLGMGRDCLPEQEG-LWLPSLRPK 1513
Cdd:smart00827  234 LDDADYWVRNLREPVRFADAVRALlAEGGVTVFLEVGPHPVLTGPIKQTLAAAGSaVVLPSLRRG 298

A_NRPS_CmdD_like

cd17652

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...

37-562

6.94e-138

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: 439.00 E-value: 6.94e-138

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   37 PDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYML 116
Cdd:cd17652     1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  117 RDSDARILLTStdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiq 196
Cdd:cd17652    81 ADARPALLLTT--------------------------------------------------------------------- 91

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  197 tqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNM---LWWHQQTRPsvqGVRTLQFCAVSFDFSCHEIFSTLCLGGILVL 273
Cdd:cd17652    92 ----PDNLAYVIYTSGSTGRPKGVVVTHRGLANLaaaQIAAFDVGP---GSRVLQFASPSFDASVWELLMALLAGATLVL 164

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  274 VPEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAvngnksTSLALCEVITTGEQmqITPAVANLFQKTGAMLhNHYG 353
Cdd:cd17652   165 APAEELLPGEPLADLLREHRITHVTLPPAALAALPPD------DLPDLRTLVVAGEA--CPAELVDRWAPGRRMI-NAYG 235

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  354 ATEfqdATTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFG 433
Cdd:cd17652   236 PTE---TTVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFG 312

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  434 TNenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREI-AGHTQLVGYIIAKD 512
Cdd:cd17652   313 AP--GSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDrPGDKRLVAYVVPAP 390

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 602182148  513 TLNLSFDKlepiLRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALP 562
Cdd:cd17652   391 GAAPTAAE----LRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436

A_NRPS_Ta1_like

cd12116

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...

37-561

2.85e-137

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: 438.65 E-value: 2.85e-137

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   37 PDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYML 116
Cdd:cd12116     1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  117 RDSDARILLTSTDVAKKLALTIPALqecqtvyldqeifeydfhflaiakLLHNQYLRLLHfyfytliqqcqatsvsQGIQ 196
Cdd:cd12116    81 EDAEPALVLTDDALPDRLPAGLPVL------------------------LLALAAAAAAP----------------AAPR 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  197 TQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQtRPSVQ-GVRTLQFCAVSFDFSCHEIFSTLCLGGILVLVP 275
Cdd:cd12116   121 TPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRE-RLGLGpGDRLLAVTTYAFDISLLELLLPLLAGARVVIAP 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  276 EAVRQNPFALAEFISQQKIeKLFLPVIALLQLAEAVNGNKSTSL-ALCevitTGEQMQitPAVANLFQKTGAMLHNHYGA 354
Cdd:cd12116   200 RETQRDPEALARLIEAHSI-TVMQATPATWRMLLDAGWQGRAGLtALC----GGEALP--PDLAARLLSRVGSLWNLYGP 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  355 TEfqdATTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGt 434
Cdd:cd12116   273 TE---TTIWSTAARVTAAAGPIPIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFA- 348

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  435 nENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLVGYIIAKDTl 514
Cdd:cd12116   349 -GPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAG- 426

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 602182148  515 nLSFDKLEpiLRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd12116   427 -AAPDAAA--LRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470

A_NRPS_PvdJ-like

cd17649

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...

37-562

3.38e-136

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: 434.87 E-value: 3.38e-136

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   37 PDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYML 116
Cdd:cd17649     1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  117 RDSDARILLTSTdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiq 196
Cdd:cd17649    81 EDSGAGLLLTHH-------------------------------------------------------------------- 92

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  197 tqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNmlwwHQQTRPSVQGV----RTLQFCAVSFDFSCHEIFSTLCLGGILV 272
Cdd:cd17649    93 ----PRQLAYVIYTSGSTGTPKGVAVSHGPLAA----HCQATAERYGLtpgdRELQFASFNFDGAHEQLLPPLICGACVV 164

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  273 LVPEAVRQNPFALAEFISQQKIEKLFLPVIALLQLA-EAVNGNKSTSLALCEVITTGEQMqiTPAVANLFQKTGAMLHNH 351
Cdd:cd17649   165 LRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAeEADRTGDGRPPSLRLYIFGGEAL--SPELLRRWLKAPVRLFNA 242

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  352 YGATEfqdAT-THTL----KGNPEGWPTlVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEK 426
Cdd:cd17649   243 YGPTE---ATvTPLVwkceAGAARAGAS-MPIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAER 318

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  427 FIPNPFGtnENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLVG 506
Cdd:cd17649   319 FVPDPFG--APGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVA 396

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 602182148  507 YIIAKDTLNLSFDKLEpiLRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALP 562
Cdd:cd17649   397 YVVLRAAAAQPELRAQ--LRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450

A_NRPS_Cytc1-like

cd17643

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...

37-561

3.42e-136

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: 434.81 E-value: 3.42e-136

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   37 PDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYML 116
Cdd:cd17643     1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  117 RDSDARILLTStdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiq 196
Cdd:cd17643    81 ADSGPSLLLTD--------------------------------------------------------------------- 91

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  197 tqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPE 276
Cdd:cd17643    92 ----PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPY 167

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  277 AVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALCEVITTGEQMQItPAVANLFQKTGAM---LHNHYG 353
Cdd:cd17643   168 EVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEA-AMLRPWAGRFGLDrpqLVNMYG 246

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  354 ATEFQDATTHTLKGNPEGWP-TLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPF 432
Cdd:cd17643   247 ITETTVHVTFRPLDAADLPAaAASPIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPF 326

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  433 GtnENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVARE-IAGHTQLVGYIIAK 511
Cdd:cd17643   327 G--GPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREdEPGDTRLVAYVVAD 404

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 602182148  512 DtlnlSFDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd17643   405 D----GAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450

A_NRPS_Sfm_like

cd12115

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...

25-561

1.21e-135

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: 433.28 E-value: 1.21e-135

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   25 IHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLD 104
Cdd:cd12115     1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  105 VGYPADRIEYMLRDSDARILLTStdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliq 184
Cdd:cd12115    81 PAYPPERLRFILEDAQARLVLTD--------------------------------------------------------- 103

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  185 qcqatsvsqgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFST 264
Cdd:cd12115   104 ----------------PDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGP 167

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  265 LCLGGILVLVpeavrQNPFALAEFISQQK---IEKLFLPVIALLQLAEAVNGNKSTSLAlcevittGEQMQITpAVANLF 341
Cdd:cd12115   168 LATGGKVVLA-----DNVLALPDLPAAAEvtlINTVPSAAAELLRHDALPASVRVVNLA-------GEPLPRD-LVQRLY 234

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  342 QK-TGAMLHNHYGATEfqDATTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLP 420
Cdd:cd12115   235 ARlQVERVVNLYGPSE--DTTYSTVAPVPPGASGEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRP 312

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  421 DLTNEKFIPNPFGTNEnakKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVARE-IA 499
Cdd:cd12115   313 GLTAERFLPDPFGPGA---RLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGdAA 389

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 602182148  500 GHTQLVGYIIAKDTLNLSFDKLEPILRQyseaVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd12115   390 GERRLVAYIVAEPGAAGLVEDLRRHLGT----RLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447

A_NRPS_PpsD_like

cd17650

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...

37-561

2.99e-134

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: 429.19 E-value: 2.99e-134

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   37 PDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYML 116
Cdd:cd17650     1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  117 RDSDARILLTstdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiq 196
Cdd:cd17650    81 EDSGAKLLLT---------------------------------------------------------------------- 90

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  197 tqvLPNNLAYCIYTSGSTGNPKGILMEHRSLVNM-LWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTLCLGGILVLVP 275
Cdd:cd17650    91 ---QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAaHAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICP 167

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  276 EAVRQNPFALAEFISQQKIEKL-FLPVIALLQLAE-AVNGNKSTSLalcEVITTGEQMQITPAVANLFQKTGA--MLHNH 351
Cdd:cd17650   168 DEVKLDPAALYDLILKSRITLMeSTPALIRPVMAYvYRNGLDLSAM---RLLIVGSDGCKAQDFKTLAARFGQgmRIINS 244

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  352 YGATEFQ-DATTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPN 430
Cdd:cd17650   245 YGVTEATiDSTYYEEGRDPLGDSANVPIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVEN 324

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  431 PFGTNENakkLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIA-GHTQLVGYII 509
Cdd:cd17650   325 PFAPGER---MYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKgGEARLCAYVV 401

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 602182148  510 AKDTLNLSfdklepILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd17650   402 AAATLNTA------ELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447

entF

PRK10252

enterobactin non-ribosomal peptide synthetase EntF;

8-653

1.04e-131

enterobactin non-ribosomal peptide synthetase EntF;

Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 449.88 E-value: 1.04e-131

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    8 QILFDGNGTQSEFPDSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELF 87
Cdd:PRK10252  443 AQLAQVNATAVEIPETTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLT 522

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   88 IGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLTSTDVAKKLAlTIPalqecqtvylDQEIFEYDFHFLAiakll 167
Cdd:PRK10252  523 LALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFA-DVP----------DLTSLCYNAPLAP----- 586

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  168 hnqylrllhfyfytliQQCQATSVSQgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTL 247
Cdd:PRK10252  587 ----------------QGAAPLQLSQ-------PHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVL 643

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  248 QFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRQNPFALAEFISQQKIEKL-FLP-VIALLQLAEAVNGNKSTSLALCEVI 325
Cdd:PRK10252  644 QKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTThFVPsMLAAFVASLTPEGARQSCASLRQVF 723

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  326 TTGEQMqiTPAVANLFQK-TGAMLHNHYGATE----------FQDATTHTlKGNPegwptlVPVGRPLHNVQVYILDEAQ 394
Cdd:PRK10252  724 CSGEAL--PADLCREWQQlTGAPLHNLYGPTEaavdvswypaFGEELAAV-RGSS------VPIGYPVWNTGLRILDARM 794

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  395 QPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGTNEnakKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVE 474
Cdd:PRK10252  795 RPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGE---RMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIE 871

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  475 LGEIESVLASHQAVRECAVVAREI-------AGHTQLVGYIIAKDTLNLSFDKLEPILRqyseAVLPEYMIPTRFINISN 547
Cdd:PRK10252  872 LGEIDRAMQALPDVEQAVTHACVInqaaatgGDARQLVGYLVSQSGLPLDTSALQAQLR----ERLPPHMVPVVLLQLDQ 947

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  548 MPLTPSGKLDRRALPDPKgdrPALSTPLVKPRTQTEKRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKFLCETFN 627
Cdd:PRK10252  948 LPLSANGKLDRKALPLPE---LKAQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQFA 1024

                         650       660
                  ....*....|....*....|....*.
gi 602182148  628 INLSAVSLFQYPTIQTLAQYIDCQGD 653
Cdd:PRK10252 1025 RQVTPGQVMVASTVAKLATLLDAEED 1050

PRK12316

peptide synthase; Provisional

5-645

4.38e-130

peptide synthase; Provisional

Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 462.12 E-value: 4.38e-130

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    5 ESPQILFDGNGTQSEFP-DSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERS 83
Cdd:PRK12316 1984 ERQRILADWDRTPEAYPrGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERS 2063

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   84 AELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLTSTDVAKKLALtiPALQECQTVYLDQEIFEYDfhflai 163
Cdd:PRK12316 2064 FELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPL--PAGVARLPLDRDAEWADYP------ 2135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  164 akllhnqylrllhfyfytliqqcqatsvSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQG 243
Cdd:PRK12316 2136 ----------------------------DTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPA 2187

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  244 VRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRqNPFALAEFISQQKIEKLFLPVIALLQLAE--AVNGNKstsLAL 321
Cdd:PRK12316 2188 DCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELW-DPEQLYDEMERHGVTILDFPPVYLQQLAEhaERDGRP---PAV 2263

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  322 CEVITTGEQMQITPAVANLFQKTGAMLHNHYGATE-FQDATTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLG 400
Cdd:PRK12316 2264 RVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEaVVTPLLWKCRPQDPCGAAYVPIGRALGNRRAYILDADLNLLAPG 2343

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  401 GEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGTNenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIES 480
Cdd:PRK12316 2344 MAGELYLGGEGLARGYLNRPGLTAERFVPDPFSAS--GERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEA 2421

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  481 VLASHQAVRECAVVAREIAGHTQLVGYIIAKDTLNLsfdkLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRA 560
Cdd:PRK12316 2422 RLQAHPAVREAVVVAQDGASGKQLVAYVVPDDAAED----LLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKA 2497

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  561 LPDPkgDRPALSTPLVKPRTQTEKRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKFLCETFNINLSAVSLFQYPT 640
Cdd:PRK12316 2498 LPKP--DVSQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPT 2575


                  ....*
gi 602182148  641 IQTLA 645
Cdd:PRK12316 2576 LAAFA 2580

A_NRPS_SidN3_like

cd05918

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...

25-561

2.95e-128

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: 413.09 E-value: 2.95e-128

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   25 IHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLD 104
Cdd:cd05918     1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  105 VGYPADRIEYMLRDSDARILLTSTdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliq 184
Cdd:cd05918    81 PSHPLQRLQEILQDTGAKVVLTSS-------------------------------------------------------- 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  185 qcqatsvsqgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFST 264
Cdd:cd05918   105 ----------------PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTT 168

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  265 LCLGGILVLVPEAVRQNpfALAEFISQQKIEKLFLP--VIALLQLAEAVNgnkstslaLCEVITTGEQMqiTPAVANLFQ 342
Cdd:cd05918   169 LAAGGCLCIPSEEDRLN--DLAGFINRLRVTWAFLTpsVARLLDPEDVPS--------LRTLVLGGEAL--TQSDVDTWA 236

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  343 KtGAMLHNHYGATEfqdATTHTLKGNPEGWPTLVPVGRPLhNVQVYILDEA--QQPVPLGGEGEFCIGGIGLARGYHNLP 420
Cdd:cd05918   237 D-RVRLINAYGPAE---CTIAATVSPVVPSTDPRNIGRPL-GATCWVVDPDnhDRLVPIGAVGELLIEGPILARGYLNDP 311

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  421 DLTNEKFIPNP-FGTNENAK---KLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVA- 495
Cdd:cd05918   312 EKTAAAFIEDPaWLKQEGSGrgrRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEv 391

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  496 ---REIAGHTQLVGYIIAKDT-------------LNLSFDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRR 559
Cdd:cd05918   392 vkpKDGSSSPQLVAFVVLDGSssgsgdgdslflePSDEFRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRR 471


                  ..
gi 602182148  560 AL 561
Cdd:cd05918   472 AL 473

KR_2_FAS_SDR_x

cd08955

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...

2353-2747

1.26e-127

Pssm-ID: 187658 [Multi-domain] Cd Length: 376 Bit Score: 407.06 E-value: 1.26e-127

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2353 LLNRVPNIQEIVHCWSM----VSTDLDRATIFSCSSTLHLVQAL--ANYPKNPRLSLVTLGAQAVN-EHHVQNVVGAALW 2425
Cdd:cd08955     1 ALLGSAPLAGVVHLWSLdaprEEPADAASQELGCASALHLVQALskAGLRRAPRLWLVTRGAQSVLaDGEPVSPAQAPLW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2426 GMGKVIALEHPELQVAQMDLDPNGKVKAQVEVLRDELLARKDpasamsvpdlqtrphEKQIAFREQTRYVARLSPLDRPN 2505
Cdd:cd08955    81 GLGRVIALEHPELRCGLVDLDPEATAAEEAEALLAELLAADA---------------EDQVALRGGARYVARLVRAPARP 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2506 prekgtqealtFRDDGSYLIAGGLGGLGLVVARFLVTNGARYLVLVGRRGAREEQQAQLSELEQLGASVKVLQADIADAE 2585
Cdd:cd08955   146 -----------LRPDATYLITGGLGGLGLLVAEWLVERGARHLVLTGRRAPSAAARQAIAALEEAGAEVVVLAADVSDRD 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2586 QLAQALSAV--TYPPLRGVIHAAGTLNDGILQQQSWQAFKEVMNPKVAGAWNLHILTKNQPLDFFVLFSSATSLLGNAGQ 2663
Cdd:cd08955   215 ALAAALAQIraSLPPLRGVIHAAGVLDDGVLANQDWERFRKVLAPKVQGAWNLHQLTQDLPLDFFVLFSSVASLLGSPGQ 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2664 ANHAAANAFLDGLASYRRHLGLPSLSINWGTWSEVGIAARLGLDKLSSKQGEGTITLGQGLQILEQLLKDENGvyQVGVM 2743
Cdd:cd08955   295 ANYAAANAFLDALAHYRRARGLPALSINWGPWAEVGMAASLARQARLEARGVGAISPAAGLQALGQLLRTGST--QVGVA 372


                  ....
gi 602182148 2744 PINW 2747
Cdd:cd08955   373 PVDW 376

PRK12316

peptide synthase; Provisional

5-646

2.13e-122

peptide synthase; Provisional

Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 436.70 E-value: 2.13e-122

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    5 ESPQILFDGNGTQSEFP-DSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERS 83
Cdd:PRK12316 3038 ERGQLLEAWNATAAEYPlERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERS 3117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   84 AELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLTSTDvakklaLTIPALQECQTVYLDQEIFEYDFHFLAI 163
Cdd:PRK12316 3118 LEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSH------LRLPLAQGVQVLDLDRGDENYAEANPAI 3191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  164 akllhnqylrllhfyfytliqqcqatsvsqgiqtQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQG 243
Cdd:PRK12316 3192 ----------------------------------RTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVG 3237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  244 VRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALCe 323
Cdd:PRK12316 3238 DRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRI- 3316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  324 vITTGEQMqitPAVANLFQKTGAMLHNHYGATEFQ-DATTHTLKGNPEGWPtlvPVGRPLHNVQVYILDEAQQPVPLGGE 402
Cdd:PRK12316 3317 -VCGGEAL---PADLQQQVFAGLPLYNLYGPTEATiTVTHWQCVEEGKDAV---PIGRPIANRACYILDGSLEPVPVGAL 3389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  403 GEFCIGGIGLARGYHNLPDLTNEKFIPNPFGTNEnakKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVL 482
Cdd:PRK12316 3390 GELYLGGEGLARGYHNRPGLTAERFVPDPFVPGE---RLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARL 3466

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  483 ASHQAVRECAVVAREiagHTQLVGYIIAKDtlnlSFDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALP 562
Cdd:PRK12316 3467 LEHPWVREAVVLAVD---GRQLVAYVVPED----EAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALP 3539

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  563 DPkgDRPALSTPLVKPRTQTEKRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKfLCETFNINLSAVSLFQYPTIQ 642
Cdd:PRK12316 3540 RP--DAALLQQDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVS-RARQAGIRFTPKDLFQHQTIQ 3616


                  ....
gi 602182148  643 TLAQ 646
Cdd:PRK12316 3617 GLAR 3620

A_NRPS_LgrA-like

cd17645

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...

26-562

2.45e-122

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: 394.61 E-value: 2.45e-122

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   26 HHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDV 105
Cdd:cd17645     1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  106 GYPADRIEYMLRDSDARILLTStdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqq 185
Cdd:cd17645    81 DYPGERIAYMLADSSAKILLTN---------------------------------------------------------- 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  186 cqatsvsqgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTL 265
Cdd:cd17645   103 ---------------PDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHL 167

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  266 CLGGILVLVPEAVRQNPFALAEFISQQKIEKLFLPViallQLAEAVNGNKSTSLALceVITTGEQMqitpavaNLFQKTG 345
Cdd:cd17645   168 TAGAALHVVPSERRLDLDALNDYFNQEGITISFLPT----GAAEQFMQLDNQSLRV--LLTGGDKL-------KKIERKG 234

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  346 AMLHNHYGATEFQDATTHTLKGNPEGwptLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNE 425
Cdd:cd17645   235 YKLVNNYGPTENTVVATSFEIDKPYA---NIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAE 311

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  426 KFIPNPFGTNEnakKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGH-TQL 504
Cdd:cd17645   312 KFIVHPFVPGE---RMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGrKYL 388

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 602182148  505 VGYIIAKDTLNLSfdklepILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALP 562
Cdd:cd17645   389 VAYVTAPEEIPHE------ELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKALP 440

omega_3_PfaA

TIGR02813

polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...

677-1554

1.61e-115

Pssm-ID: 274311 [Multi-domain] Cd Length: 2582 Bit Score: 412.86 E-value: 1.61e-115

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   677 IAIISVAGRFPGAETIEQFWHNLCNGVESIT-----------LFSDDKLEQtlpelfnNPAYVKAGAVLEGVElFDATFF 745
Cdd:TIGR02813    9 IAIVGMASIFANSRYLNKFWDLIFEKIDAITdvpsdhwakddYYDSDKSEA-------DKSYCKRGGFLPEVD-FNPMEF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   746 GYSPKEAAVTDPQQRILLECAWEAFERAGYnPETYPE-----PVGVYAGSSLSTYL--------LNNIGSALGIITE--- 809
Cdd:TIGR02813   81 GLPPNILELTDISQLLSLVVAKEVLNDAGL-PDGYDRdkigiTLGVGGGQKQSSSLnarlqypvLKKVFKASGVEDEdse 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   810 -------QPFIETDMEQFQAKIGNdrsYLATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGisvV 882
Cdd:TIGR02813  160 mlikkfqDQYIHWEENSFPGSLGN---VISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGG---V 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   883 VPQKGGYLYeegMVRSQ------DGHCRAFDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGAIKMGY 956
Cdd:TIGR02813  234 CTDNSPFMY---MSFSKtpafttNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIY 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   957 tAPSVDGQADVISEAIAIADIDASTIGYVEAHGTATQLGDPIEVAGLARAFQRSTDSvlgKQQCAIGSVKTNIGHLDEAA 1036
Cdd:TIGR02813  311 -APRPEGQAKALKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQ---KQHIALGSVKSQIGHTKSTA 386

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  1037 GIAGLIKAALALQYGQIPPSLHYANPNPRIDFDATPFFVNTELREWSR--NGYPRRAGVSSFGVGGTNSHIVLEE-SP-- 1111
Cdd:TIGR02813  387 GTAGMIKAVLALHHKVLPPTINVDQPNPKLDIENSPFYLNTETRPWMQreDGTPRRAGISSFGFGGTNFHMVLEEySPkh 466

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  1112 ----------VKQPTLFSS------LPERSHHLLTLSAHTQEALHELVQRYIQHNETHLDIDLGDLCFTANTGrkhfEHR 1175
Cdd:TIGR02813  467 qrddqyrqraVAQTLLFTAanekalVSSLKDWKNKLSAKADDQPYAFNALAVENTLRTIAVALARLGFVAKNA----DEL 542

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  1176 LAVVAESIPGLQAQ-LETAQ--TAISAQKK---NAPPTIAFLFTGQGSQYINMGRTLYDTESTFRAALDRCETILQNLGI 1249
Cdd:TIGR02813  543 ITMLEQAITQLEAKsCEEWQlpSGISYRKSalvVESGKVAALFAGQGSQYLNMGRELACNFPEVRQAAADMDSVFTQAGK 622

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  1250 ESIISVIF--------GSSEHGLSLDDTAYTQPALFAIEYALYQLWKSWGIQPSVVIGHSVGEYVSACVAGVFSLEDGLK 1321
Cdd:TIGR02813  623 GALSPVLYpipvfndeSRKAQEEALTNTQHAQSAIGTLSMGQYKLFTQAGFKADMTAGHSFGELSALCAAGVISDDDYMM 702

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  1322 LIAERGRLIQALPRD---GSMVSVMASEKRIADIILPYGGQ---VGIAAINGPQSVVISG----QQQAIDAicaiLETEG 1391
Cdd:TIGR02813  703 LAFSRGQAMAAPTGEadiGFMYAVILAVVGSPTVIANCIKDfegVSIANYNSPTQLVIAGvstqIQIAAKA----LKEKG 778

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  1392 IKSKKLNVSHAFHSPLVEAMLDSFLQVAQEVTYSQPQIKLISNVTGTLASHescpDELPITTAeyWVRHVRQPVRFAAGM 1471
Cdd:TIGR02813  779 FKAIPLPVSGAFHTPLVAHAQKPFSAAIDKAKFNTPLVPLYSNGTGKLHSN----DAAAIKKA--LKNHMLQSVHFSEQL 852

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  1472 ESLEGQGVNVFIEIGPKPVLLGMGRDCLPEQEG-LWLPSL--RPKQDDWQQVLSSLRDLYLVGVTIDwsSFDQGYARRRV 1548
Cdd:TIGR02813  853 EAMYAAGARVFVEFGPKNILQKLVENTLKDKENeLCAISInpNPKGDSDMQLRQAAVQLAVLGLELT--EIDPYQAEKRP 930


                   ....*.
gi 602182148  1549 PLPTYP 1554
Cdd:TIGR02813  931 PAATSP 936

PRK05691

peptide synthase; Validated

28-637

1.55e-114

peptide synthase; Validated

Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 410.71 E-value: 1.55e-114

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   28 LFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGY 107
Cdd:PRK05691 1136 LLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDY 1215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  108 PADRIEYMLRDSDARILLTSTDVAKKLaltiPALQECQTVYLDQeifeydfhflaiakllhnqylrlLHFYFYTliqqcq 187
Cdd:PRK05691 1216 PAERLAYMLADSGVELLLTQSHLLERL----PQAEGVSAIALDS-----------------------LHLDSWP------ 1262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  188 atsvSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTLCL 267
Cdd:PRK05691 1263 ----SQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLIT 1338

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  268 GGILVLVPEAVRQNPFALAEFISQQKIEKL-FLPviALLQL-AEAVNGNKSTSLALceVITTGEQMqiTPAVAN--LFQK 343
Cdd:PRK05691 1339 GCRLVLAGPGEHRDPQRIAELVQQYGVTTLhFVP--PLLQLfIDEPLAAACTSLRR--LFSGGEAL--PAELRNrvLQRL 1412

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  344 TGAMLHNHYGATEFQDATTHTLKGNPEGwpTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLT 423
Cdd:PRK05691 1413 PQVQLHNRYGPTETAINVTHWQCQAEDG--ERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALT 1490

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  424 NEKFIPNPFGtnENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQ 503
Cdd:PRK05691 1491 AERFVPDPLG--EDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQ 1568

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  504 LVGYIIAKDTLNLSFDKLEPILrqysEAVLPEYMIPTRFINISNMPLTPSGKLDRRALPDPKGDRpalsTPLVKPRTQTE 583
Cdd:PRK05691 1569 LVGYYTGEAGQEAEAERLKAAL----AAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQ----REHVEPRTELQ 1640

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 602182148  584 KRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKFLCETFNINLSAVSLFQ 637
Cdd:PRK05691 1641 QQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFE 1694

A_NRPS_ACVS-like

cd17648

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...

37-562

3.46e-114

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: 371.73 E-value: 3.46e-114

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   37 PDAIALIDGEQSLTYGELNVRANHLAQHLLSLGC-QPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYM 115
Cdd:cd17648     1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEiRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  116 LRDSDARILLTStdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgi 195
Cdd:cd17648    81 LEDTGARVVITN-------------------------------------------------------------------- 92

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  196 qtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMlwwHQQTRPSVQGVRT-----LQFCAVSFDFSCHEIFSTLCLGGI 270
Cdd:cd17648    93 -----STDLAYAIYTSGTTGKPKGVLVEHGSVVNL---RTSLSERYFGRDNgdeavLFFSNYVFDFFVEQMTLALLNGQK 164

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  271 LVLVPEAVRQNPFALAEFISQQKIEKLF-LP-VIALLQLAEAvngnksTSLALceVITTGEQMQiTPAVANLFQKTGAML 348
Cdd:cd17648   165 LVVPPDEMRFDPDRFYAYINREKVTYLSgTPsVLQQYDLARL------PHLKR--VDAAGEEFT-APVFEKLRSRFAGLI 235

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  349 HNHYGATEFqdATTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFI 428
Cdd:cd17648   236 INAYGPTET--TVTNHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFL 313

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  429 PNPFGTNENAK-----KLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQ 503
Cdd:cd17648   314 PNPFQTEQERArgrnaRLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQ 393

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 602182148  504 ------LVGYIIAkDTLNLSfdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALP 562
Cdd:cd17648   394 sriqkyLVGYYLP-EPGHVP----ESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRALP 453

PRK05691

peptide synthase; Validated

1-672

4.72e-113

peptide synthase; Validated

Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 406.09 E-value: 4.72e-113

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    1 MQERESPQILFDGNGTQSEFP-DSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAIC 79
Cdd:PRK05691 2165 LAAAEQQQLLDSLAGEAGEARlDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLA 2244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   80 IERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLTSTDVAKKLAlTIPA------LQECQTVYLDQEI 153
Cdd:PRK05691 2245 LERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALG-ELPAgvarwcLEDDAAALAAYSD 2323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  154 FEYDFhflaiakllhnqylrllhfyfytliqqcqatsvsqgiqtQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVnmlwW 233
Cdd:PRK05691 2324 APLPF---------------------------------------LSLPQHQAYLIYTSGSTGKPKGVVVSHGEIA----M 2360

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  234 HQQTRPSVQGVRT----LQFCAVSFDFSCHEIFSTLCLGGILVLVpeavRQNPFA---LAEFISQQKIEKL-FLPVIALl 305
Cdd:PRK05691 2361 HCQAVIERFGMRAddceLHFYSINFDAASERLLVPLLCGARVVLR----AQGQWGaeeICQLIREQQVSILgFTPSYGS- 2435

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  306 QLAEAVNG-NKSTSLALCevIT-----TGEQMQitpAVANLFQKtgAMLHNHYGATEFQDATTHTLKGN--PEGWPTlVP 377
Cdd:PRK05691 2436 QLAQWLAGqGEQLPVRMC--ITggealTGEHLQ---RIRQAFAP--QLFFNAYGPTETVVMPLACLAPEqlEEGAAS-VP 2507

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  378 VGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGTNenAKKLYRTGDLARYLPDGTIE 457
Cdd:PRK05691 2508 IGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAD--GGRLYRTGDLVRLRADGLVE 2585

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  458 HLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLVGYIIAK--DTLNLSFDKLEPILRQYSEAVLPE 535
Cdd:PRK05691 2586 YVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVSAvaGQDDEAQAALREALKAHLKQQLPD 2665

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  536 YMIPTRFINISNMPLTPSGKLDRRAL--PDPKGDRPAlstpLVKPRTQTEKRLAEIWGSYLAVDIVGTHDNFFDLGGTSL 613
Cdd:PRK05691 2666 YMVPAHLILLDSLPLTANGKLDRRALpaPDPELNRQA----YQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSI 2741

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 602182148  614 LLTQAHKfLCETFNINLSAVSLFQYPTIQTLAQYIdcqgdtTSSNTASRHKKVRKKQSG 672
Cdd:PRK05691 2742 LSIQVVS-RARQLGIHFSPRDLFQHQTVQTLAAVA------THSEAAQAEQGPLQGASG 2793

A_NRPS_GliP_like

cd17653

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...

27-561

1.40e-109

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: 357.39 E-value: 1.40e-109

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   27 HLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVG 106
Cdd:cd17653     1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  107 YPADRIEYMLRDSDARILLTSTDvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqc 186
Cdd:cd17653    81 LPSARIQAILRTSGATLLLTTDS--------------------------------------------------------- 103

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  187 qatsvsqgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTLC 266
Cdd:cd17653   104 --------------PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLC 169

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  267 LGGILVLVPEAvrqNPFA-LAEFISqqkieklFLP----VIALLQLAEAVNgnkstslaLCEVITTGEQmqITPAVANLF 341
Cdd:cd17653   170 NGGTLVLADPS---DPFAhVARTVD-------ALMstpsILSTLSPQDFPN--------LKTIFLGGEA--VPPSLLDRW 229

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  342 QKtGAMLHNHYGATE--FQDATTHTLKGNPegwptlVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNL 419
Cdd:cd17653   230 SP-GRRLYNAYGPTEctISSTMTELLPGQP------VTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGN 302

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  420 PDLTNEKFIPNPFgtnENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQA-VRECAVVAREi 498
Cdd:cd17653   303 PALTASKFVPDPF---WPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPeVTQAAAIVVN- 378

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 602182148  499 aghTQLVGYiIAKDTLNLSfdklepILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd17653   379 ---GRLVAF-VTPETVDVD------GLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKAL 431

A_NRPS_TlmIV_like

cd12114

The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...

37-561

2.17e-104

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: 344.25 E-value: 2.17e-104

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   37 PDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYML 116
Cdd:cd12114     1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  117 RDSDARILLTSTDVAKKLALTIPALqecqtvyldqeifeydfhflaiakllhnqylrllhfyfyTLIQQCQATSvSQGIQ 196
Cdd:cd12114    81 ADAGARLVLTDGPDAQLDVAVFDVL---------------------------------------ILDLDALAAP-APPPP 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  197 TQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQtRPSVQGV-RTLQFCAVSFDFSCHEIFSTLCLGGILVLVP 275
Cdd:cd12114   121 VDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINR-RFAVGPDdRVLALSSLSFDLSVYDIFGALSAGATLVLPD 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  276 EAVRQNPFALAEFISQQKIeKLFLPVIALLQL----AEAVNGNKStSLALceVITTGE--QMQITPAVANLFqkTGAMLH 349
Cdd:cd12114   200 EARRRDPAHWAELIERHGV-TLWNSVPALLEMlldvLEAAQALLP-SLRL--VLLSGDwiPLDLPARLRALA--PDARLI 273

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  350 NHYGATEfqdAT----THTLKGNPEGWPTlVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNE 425
Cdd:cd12114   274 SLGGATE---ASiwsiYHPIDEVPPDWRS-IPYGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAA 349

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  426 KFIPNPFGtnenaKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLV 505
Cdd:cd12114   350 RFVTHPDG-----ERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLA 424

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 602182148  506 GYIIAKDTLNLSFdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd12114   425 AFVVPDNDGTPIA---PDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477

AMP-binding

pfam00501

AMP-binding enzyme;

29-469

1.37e-98

AMP-binding enzyme;

Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 325.04 E-value: 1.37e-98

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    29 FEDQAAKRPDAIALIDGE-QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGY 107
Cdd:pfam00501    1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   108 PADRIEYMLRDSDARILLTstDVAKKLALTIPALQECQTVYldqeifeydfHFLAIAKLLHNQYLRLLHFYFYTLIQQCQ 187
Cdd:pfam00501   81 PAEELAYILEDSGAKVLIT--DDALKLEELLEALGKLEVVK----------LVLVLDRDPVLKEEPLPEEAKPADVPPPP 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   188 ATSVSqgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGV----RTLQFCAVSFDFS-CHEIF 262
Cdd:pfam00501  149 PPPPD--------PDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLgpddRVLSTLPLFHDFGlSLGLL 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   263 STLCLGGILVLVPEAVRQNPFALAEFISQQKIEKLFLP---VIALLQlAEAVNGNKSTSLalcEVITTGeQMQITPAVAN 339
Cdd:pfam00501  221 GPLLAGATVVLPPGFPALDPAALLELIERYKVTVLYGVptlLNMLLE-AGAPKRALLSSL---RLVLSG-GAPLPPELAR 295

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   340 -LFQKTGAMLHNHYGATEfqdATTHTLKGNPEGWPTLVP--VGRPLHNVQVYILDEA-QQPVPLGGEGEFCIGGIGLARG 415
Cdd:pfam00501  296 rFRELFGGALVNGYGLTE---TTGVVTTPLPLDEDLRSLgsVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKG 372

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 602182148   416 YHNLPDLTNEKFIPNPFgtnenakklYRTGDLARYLPDGTIEHLGRIDHQVKIR 469
Cdd:pfam00501  373 YLNDPELTAEAFDEDGW---------YRTGDLGRRDEDGYLEIVGRKKDQIKLG 417

PRK05691

peptide synthase; Validated

2-662

1.51e-97

peptide synthase; Validated

Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 354.86 E-value: 1.51e-97

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    2 QEREspqILFDG-NGTQSEFP-DSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAIC 79
Cdd:PRK05691 3700 QERD---FLLDGcNRSERDYPlEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALL 3776

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   80 IERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLTStdvAKKLALTIPALQECQTVyldqeifeydfh 159
Cdd:PRK05691 3777 AERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCS---AACREQARALLDELGCA------------ 3841

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  160 flAIAKLLhnqylrllhfyFYTLIQQCQATSVSQGIQTQvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNmlwwHQQTR- 238
Cdd:PRK05691 3842 --NRPRLL-----------VWEEVQAGEVASHNPGIYSG--PDNLAYVIYTSGSTGLPKGVMVEQRGMLN----NQLSKv 3902

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  239 P----SVQGVrTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRQNPFALAEFISQQKIEKLfLPVIALLQ--LAEavn 312
Cdd:PRK05691 3903 PylalSEADV-IAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITVL-ESVPSLIQgmLAE--- 3977

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  313 gNKSTSLALCEVITTGEQMQITPAVANLFQKTGAMLHNHYGATEFQD--ATTHTLKGNPEGwpTLVPVGRPLHNVQVYIL 390
Cdd:PRK05691 3978 -DRQALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDdvAFFRVDLASTRG--SYLPIGSPTDNNRLYLL 4054

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  391 DEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGtnENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRG 470
Cdd:PRK05691 4055 DEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFG--APGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRG 4132

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  471 FRVELGEIESVLASHQAVRECAVVAREIAGHTQLVGYIIAKDTLNLSFDKLEPIlRQYSEAVLPEYMIPTRFINISNMPL 550
Cdd:PRK05691 4133 YRIELGEIEARLHEQAEVREAAVAVQEGVNGKHLVGYLVPHQTVLAQGALLERI-KQRLRAELPDYMVPLHWLWLDRLPL 4211

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  551 TPSGKLDRRALPDPkgDRPAL-STPLVKPRTQTEKRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKFLCETFNIN 629
Cdd:PRK05691 4212 NANGKLDRKALPAL--DIGQLqSQAYLAPRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRN 4289

                         650       660       670
                  ....*....|....*....|....*....|....
gi 602182148  630 LSAVSLFQYPTIQTLAQYID-CQGDTTSSNTASR 662
Cdd:PRK05691 4290 VPLRAMFECSTVEELAEYIEgLAGSAIDEQKVDR 4323

DltA

cd05945

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...

33-561

5.41e-97

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: 321.89 E-value: 5.41e-97

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   33 AAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRI 112
Cdd:cd05945     1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  113 EYMLRDSDARILLTStdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvs 192
Cdd:cd05945    81 REILDAAKPALLIAD----------------------------------------------------------------- 95

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  193 qgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTLCLGGILV 272
Cdd:cd05945    96 --------GDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLV 167

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  273 LVPEAVRQNPFALAEFISQQKIEKLF-LP-VIALLQLAEAVNGNKSTSLALceVITTGEQMQItPAVANLFQKT-GAMLH 349
Cdd:cd05945   168 PVPRDATADPKQLFRFLAEHGITVWVsTPsFAAMCLLSPTFTPESLPSLRH--FLFCGEVLPH-KTARALQQRFpDARIY 244

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  350 NHYGATEFQDATT------HTLKGNPEgwptlVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLT 423
Cdd:cd05945   245 NTYGPTEATVAVTyievtpEVLDGYDR-----LPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKT 319

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  424 NEKFIPNPfgtnenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAR-EIAGHT 502
Cdd:cd05945   320 AAAFFPDE------GQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKyKGEKVT 393

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 602182148  503 QLVGYIIAKDTLNlsfDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05945   394 ELIAFVVPKPGAE---AGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449

KR_FAS_SDR_x

cd05274

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...

2381-2746

1.78e-94

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, 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 KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187582 [Multi-domain] Cd Length: 375 Bit Score: 311.63 E-value: 1.78e-94

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2381 SCSSTLHLVQALAN--YPKNPRLSLVTLGAQAVNEHHVQNVVGAALWGMGKVIALEHPELQVAQMDLDPNgkvkaqvevl 2458
Cdd:cd05274    29 ALAALLALVAALLAayASTGPPLWLVTRGAEAVSADDVAALAQAALWGLLRVLALEHPELWGGLVDLDAA---------- 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2459 rdellaRKDPASAMSVPDLQTRPHEKQIAFREQTRYVARLSPLDRPNPRekgtQEALTFRDDGSYLIAGGLGGLGLVVAR 2538
Cdd:cd05274    99 ------DAADEAAALAALLAGAPGEDELALRGGQRLVPRLVRAPAAALE----LAAAPGGLDGTYLITGGLGGLGLLVAR 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2539 FLVTNGARYLVLVGRRGAREEQQAQLSELEQLGASVKVLQADIADAEQLAQALSAV-TYPPLRGVIHAAGTLNDGILQQQ 2617
Cdd:cd05274   169 WLAARGARHLVLLSRRGPAPRAAARAALLRAGGARVSVVRCDVTDPAALAALLAELaAGGPLAGVIHAAGVLRDALLAEL 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2618 SWQAFKEVMNPKVAGAWNLHILTKNQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGLASYRRHLGLPSLSINWGTWSE 2697
Cdd:cd05274   249 TPAAFAAVLAAKVAGALNLHELTPDLPLDFFVLFSSVAALLGGAGQAAYAAANAFLDALAAQRRRRGLPATSVQWGAWAG 328

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 602182148 2698 VGIAARLGLDKLSSKQGEGTITLGQGLQILEQLLKDENGvyQVGVMPIN 2746
Cdd:cd05274   329 GGMAAAAALRARLARSGLGPLAPAEALEALEALLASDAP--QAVVASVD 375

MenE/FadK

COG0318

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...

25-563

2.08e-94

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: 314.44 E-value: 2.08e-94

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   25 IHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLD 104
Cdd:COG0318     1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  105 VGYPADRIEYMLRDSDARILLTstdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliq 184
Cdd:COG0318    81 PRLTAEELAYILEDSGARALVT---------------------------------------------------------- 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  185 qcqatsvsqgiqtqvlpnnlAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFS-CHEIFS 263
Cdd:COG0318   103 --------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLA 162

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  264 TLCLGGILVLVPeavRQNPFALAEFISQQKIEKLFLP---VIALLQLAEAvNGNKSTSLALceVITTGEQMqiTPAVANL 340
Cdd:COG0318   163 PLLAGATLVLLP---RFDPERVLELIERERVTVLFGVptmLARLLRHPEF-ARYDLSSLRL--VVSGGAPL--PPELLER 234

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  341 FQK-TGAMLHNHYGATEfqdaTTHTLKGNPE--GWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYH 417
Cdd:COG0318   235 FEErFGVRIVEGYGLTE----TSPVVTVNPEdpGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYW 310

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  418 NLPDLTNEKFiPNPFgtnenakklYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVARE 497
Cdd:COG0318   311 NDPEATAEAF-RDGW---------LRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVP 380

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 602182148  498 IAGHTQ-LVGYIIAKDTLNLSfdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALPD 563
Cdd:COG0318   381 DEKWGErVVAFVVLRPGAELD----AEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRE 443

ketoacyl-synt

pfam00109

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...

675-930

3.11e-79

Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 262.96 E-value: 3.11e-79

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   675 NDIAIISVAGRFPGAETIEQFWHNLCNGVESITLFSDDKLE----QTLPELFNNPAYVKAGAvLEGVELFDATFFGYSPK 750
Cdd:pfam00109    1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRWDpdklYDPPSRIAGKIYTKWGG-LDDIFDFDPLFFGISPR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   751 EAAVTDPQQRILLECAWEAFERAGYNPETYPEP-VGVYAGSSLSTY----LLNNIGSALGIiteQPFIetdmeqfqakIG 825
Cdd:pfam00109   80 EAERMDPQQRLLLEAAWEALEDAGITPDSLDGSrTGVFIGSGIGDYaallLLDEDGGPRRG---SPFA----------VG 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   826 NDRSYLATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQKGGYLYEEGMVRSQDGHCRA 905
Cdd:pfam00109  147 TMPSVIAGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKA 226

                          250       260
                   ....*....|....*....|....*
gi 602182148   906 FDAEAQGTIFGNGGGLVLLKRLQDA 930
Cdd:pfam00109  227 FDPFADGFVRGEGVGAVVLKRLSDA 251

FabD

COG0331

Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ...

1207-1505

1.58e-76

Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl CoA-acyl carrier protein transacylase is part of the Pathway/BioSystem: Fatty acid biosynthesis

Pssm-ID: 440100 [Multi-domain] Cd Length: 306 Bit Score: 257.36 E-value: 1.58e-76

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1207 TIAFLFTGQGSQYINMGRTLYDTESTFRAALDRCETILQnlgiESIISVIFGSSEHglSLDDTAYTQPALFAIEYALYQL 1286
Cdd:COG0331     2 KLAFLFPGQGSQYVGMGKDLYENFPVAREVFEEASEALG----YDLSALCFEGPEE--ELNLTENTQPAILAASVAAYRA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1287 WKSWGIQPSVVIGHSVGEYVSACVAGVFSLEDGLKLIAERGRLIQAL--PRDGSMVSVM-ASEKRIADII--LPYGGQVG 1361
Cdd:COG0331    76 LEEEGIRPDAVAGHSLGEYSALVAAGALSFEDALRLVRLRGRLMQEAvpAGPGGMAAVLgLDDEEVEALCaeAAQGEVVE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1362 IAAINGPQSVVISGQQQAIDAICAILETEGIK-SKKLNVSHAFHSPLVEAMLDSFLQVAQEVTYSQPQIKLISNVTGTla 1440
Cdd:COG0331   156 IANYNSPGQIVISGEKEAVEAAAELAKEAGAKrAVPLPVSGPFHTPLMAPAAEKLAEALAAVTFADPKIPVVSNVDAA-- 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 602182148 1441 shescpdelPITTAEYW----VRHVRQPVRFAAGMESLEGQGVNVFIEIGPKPVLLGMGRDCLPEQEGL 1505
Cdd:COG0331   234 ---------PVTDPEEIrellVRQLTSPVRWDESVEALAEAGVTTFVELGPGKVLSGLVKRIDPGVEVL 293

PKS_KR

smart00822

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...

2535-2697

2.11e-74

Pssm-ID: 214833 [Multi-domain] Cd Length: 180 Bit Score: 245.85 E-value: 2.11e-74

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   2535 VVARFLVTNGARYLVLVGRRGAREEQQAQL-SELEQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVIHAAGTLND 2611
Cdd:smart00822   15 ALARWLAERGARRLVLLSRSGPDAPGAAALlAELEAAGARVTVVACDVADRDALAAVLAAIpaVEGPLTGVIHAAGVLDD 94

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   2612 GILQQQSWQAFKEVMNPKVAGAWNLHILTKNQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGLASYRRHLGLPSLSIN 2691
Cdd:smart00822   95 GVLASLTPERFAAVLAPKAAGAWNLHELTADLPLDFFVLFSSIAGVLGSPGQANYAAANAFLDALAEYRRARGLPALSIA 174


                    ....*.
gi 602182148   2692 WGTWSE 2697
Cdd:smart00822  175 WGAWAE 180

pfam08659

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...

2521-2697

2.17e-71

Pssm-ID: 430138 [Multi-domain] Cd Length: 180 Bit Score: 237.46 E-value: 2.17e-71

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  2521 GSYLIAGGLGGLGLVVARFLVTNGARYLVLVGRRGA-REEQQAQLSELEQLGASVKVLQADIADAEQLAQALSAV--TYP 2597
Cdd:pfam08659    1 GTYLITGGLGGLGRELARWLAERGARHLVLLSRSAApRPDAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIkaEGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  2598 PLRGVIHAAGTLNDGILQQQSWQAFKEVMNPKVAGAWNLHILTKNQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGLA 2677
Cdd:pfam08659   81 PIRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPDEPLDFFVLFSSIAGLLGSPGQANYAAANAFLDALA 160

                          170       180
                   ....*....|....*....|
gi 602182148  2678 SYRRHLGLPSLSINWGTWSE 2697
Cdd:pfam08659  161 EYRRSQGLPATSINWGPWAE 180

alpha_am_amid

TIGR03443

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...

24-690

3.05e-70

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: 262.31 E-value: 3.05e-70

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    24 CIHHLFEDQAAKRPDAIALI---------DGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGIL 94
Cdd:TIGR03443  237 AIHDIFADNAEKHPDRTCVVetpsfldpsSKTRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVL 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    95 KAGCAYVPLDVGYPADRIEYMLRDSDARIL-----------LTSTDVAKKLAL--TIPAL--QECQTV---YLDQEifEY 156
Cdd:TIGR03443  317 KAGATFSVIDPAYPPARQTIYLSVAKPRALiviekagtldqLVRDYIDKELELrtEIPALalQDDGSLvggSLEGG--ET 394

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   157 DFhfLAiakllhnQYLRLlhfyfytliqQCQATSVSQGiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQ 236
Cdd:TIGR03443  395 DV--LA-------PYQAL----------KDTPTGVVVG------PDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAK 449

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   237 TRPSVQGVRTLQFCAVSFDFSCHEIFSTLCLGGILvLVPEAVR-QNPFALAEFISQQKIEKLFL-PVIALLQLAEAVNGN 314
Cdd:TIGR03443  450 RFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQL-LVPTADDiGTPGRLAEWMAKYGATVTHLtPAMGQLLSAQATTPI 528

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   315 KSTSLA--LCEVITTGEQMQITPAVANLFqktgamLHNHYGATEFQDATTH----TLKGNPEGWPTL---VPVGRPLHNV 385
Cdd:TIGR03443  529 PSLHHAffVGDILTKRDCLRLQTLAENVC------IVNMYGTTETQRAVSYfeipSRSSDSTFLKNLkdvMPAGKGMKNV 602

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   386 QVYILD--EAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGTN--------ENAK-----------KLYRT 444
Cdd:TIGR03443  603 QLLVVNrnDRTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDPshwidldkENNKperefwlgprdRLYRT 682

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   445 GDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRE-CAVVAREIAGHTQLVGYIIAKDTLNlSFDKL-- 521
Cdd:TIGR03443  683 GDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVREnVTLVRRDKDEEPTLVSYIVPQDKSD-ELEEFks 761

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   522 --------EPI---LRQYSEAV----------LPEYMIPTRFINISNMPLTPSGKLDRRALPDPKGDRPALSTPLVKPR- 579
Cdd:TIGR03443  762 evddeessDPVvkgLIKYRKLIkdireylkkkLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTAQLAAVAKNRSASa 841

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   580 -----TQTEKRLAEIWGSYL--AVDIVGTHDNFFDLGGTSLLLTQAHKFLCETFNINLSAVSLFQYPTIQTLAQYID--C 650
Cdd:TIGR03443  842 adeefTETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFAKEVDrlK 921

                          730       740       750       760
                   ....*....|....*....|....*....|....*....|...
gi 602182148   651 QGDTTSSNTASRHKKVRKKQSGD-SNDIA--IISVAGRFPGAE 690
Cdd:TIGR03443  922 KGEELADEGDSEIEEEETVLELDyAKDAKtlVDSLPKSYPSRK 964

PRK04813

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

29-561

8.36e-70

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

Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 245.19 E-value: 8.36e-70

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   29 FEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLgcQPDDLLAICI--ERSAELFIGLLGILKAGCAYVPLDVG 106
Cdd:PRK04813    8 IEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSL--KLPDKSPIIVfgHMSPEMLATFLGAVKAGHAYIPVDVS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  107 YPADRIEYMLRDSDARILLTSTDvakkLALTIpalQECQTVYLD--QEIFEYDFHFlaiakllhnqylrllhfyfytliq 184
Cdd:PRK04813   86 SPAERIEMIIEVAKPSLIIATEE----LPLEI---LGIPVITLDelKDIFATGNPY------------------------ 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  185 qcQATSvsqgiqtQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFST 264
Cdd:PRK04813  135 --DFDH-------AVKGDDNYYIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPT 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  265 LCLGGILVLVPEAVRQNPFALAEFISQQKIEklflpV---------IALLqlAEAVNGNKSTSLA---LCevittGEQMq 332
Cdd:PRK04813  206 LASGGTLVALPKDMTANFKQLFETLPQLPIN-----VwvstpsfadMCLL--DPSFNEEHLPNLThflFC-----GEEL- 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  333 iTPAVA-NLFQK-TGAMLHNHYGATEFQDATThTLKGNPE---GWPTLvPVGRPLHNVQVYILDEAQQPVPLGGEGEFCI 407
Cdd:PRK04813  273 -PHKTAkKLLERfPSATIYNTYGPTEATVAVT-SIEITDEmldQYKRL-PIGYAKPDSPLLIIDEEGTKLPDGEQGEIVI 349

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  408 GGIGLARGYHNLPDLTNEKFIPnpfgtnENAKKLYRTGDLArYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQA 487
Cdd:PRK04813  350 SGPSVSKGYLNNPEKTAEAFFT------FDGQPAYHTGDAG-YLEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSY 422

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 602182148  488 VRECAVVAREIAGH-TQLVGYIIAKDTlnlSFDK---LEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:PRK04813  423 VESAVVVPYNKDHKvQYLIAYVVPKEE---DFERefeLTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497

KR_3_FAS_SDR_x

cd08956

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); ...

2364-2714

2.69e-69

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta- ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the second KR domains of SpiE,-G, I, and -J, both KR domains of SpiD, and the third KR domain of SpiH. The single KR domain of SpiF, the first and second KR domains of SpiH, the first KR domains of SpiE,-G,- I, and -J, and the third KR domain of SpiG, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, 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 KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187659 [Multi-domain] Cd Length: 448 Bit Score: 241.79 E-value: 2.69e-69

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2364 VHCWSMVSTDLDRATIFSCSSTLHLVQA-LANyPK--NPRLSLVTLGAQAVN-EHHVQNVVGAALWGMGKVIALEHPeLQ 2439
Cdd:cd08956    58 VPCPAAAGGDLAAAAHAAAARALALLQAwLAD-PRlaDSRLVVVTRGAVAAGpDEDVPDLAAAAVWGLVRSAQAEHP-GR 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2440 VAQMDLDPngkvkaqvevlrDELLARKDPASAMSVpdlqtrphEKQIAFREQTRYVARLSpldRPNPREKGTQEALTFRD 2519
Cdd:cd08956   136 FVLVDLDD------------DAASAAALPAALASG--------EPQLALRDGRLLVPRLA---RVAPAATLPPVPRPLDP 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2520 DGSYLIAGGLGGLGLVVARFLVTN-GARYLVLVGRRGAREEQQAQL-SELEQLGASVKVLQADIADAEQLAQALSAVTY- 2596
Cdd:cd08956   193 DGTVLITGGTGTLGALLARHLVTEhGVRHLLLVSRRGPDAPGAAELvAELAALGAEVTVAACDVADRAALAALLAAVPAd 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2597 PPLRGVIHAAGTLNDGILQQQSWQAFKEVMNPKVAGAWNLHILTKNQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGL 2676
Cdd:cd08956   273 HPLTAVVHAAGVLDDGVLTSLTPERLDAVLRPKVDAAWHLHELTRDLDLAAFVLFSSAAGVLGSPGQANYAAANAFLDAL 352

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 602182148 2677 ASYRRHLGLPSLSINWGTWSEVGIA------------ARLGLDKLSSKQG 2714
Cdd:cd08956   353 AQHRRARGLPATSLAWGLWAQASGMtahlsdadlarlARGGLRPLSAEEG 402

D-ala-DACP-lig

TIGR01734

D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...

25-561

7.98e-69

D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]

Pssm-ID: 273780 [Multi-domain] Cd Length: 502 Bit Score: 242.36 E-value: 7.98e-69

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    25 IHHLFEdQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLD 104
Cdd:TIGR01734    3 IEAIQA-FAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVD 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   105 VGYPADRIEYMLRDSDARILLTSTDvakkLALTIPAlQECQTVYLDQEIFEydfhflaiakllhnqylrllhfyfytliq 184
Cdd:TIGR01734   82 TSIPSERIEMIIEAAGPELVIHTAE----LSIDAVG-TQIITLSALEQAET----------------------------- 127

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   185 qcQATSVSQgiQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFST 264
Cdd:TIGR01734  128 --SGGPVSF--DHAVKGDDNYYIIYTSGSTGNPKGVQISHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPC 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   265 LCLGGILVLVPEAVRQNPFALAEFISQQKI-EKLFLPVIA-LLQLAEAVNGNKSTSLAlcEVITTGEQMQITPAVANLFQ 342
Cdd:TIGR01734  204 LASGGTLHCLDKDITNNFKLLFEELPKTGLnVWVSTPSFVdMCLLDPNFNQENYPHLT--HFLFCGEELPVKTAKALLER 281

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   343 KTGAMLHNHYGATEFQDA------TTHTLKGNPEgwptlVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGY 416
Cdd:TIGR01734  282 FPKATIYNTYGPTEATVAvtsvkiTQEILDQYPR-----LPIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGY 356

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   417 HNLPDLTNEKFIpnpfgTNENaKKLYRTGDLArYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAR 496
Cdd:TIGR01734  357 LNNPEKTAEAFF-----SHEG-QPAYRTGDAG-TITDGQLFYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPK 429

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   497 EIAGH--TQLVGYIIAKDTlnlSFDKLEPILRQYSE---AVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:TIGR01734  430 YNKDHkvEYLIAAIVPETE---DFEKEFQLTKAIKKelkKSLPAYMIPRKFIYRDQLPLTANGKIDRKAL 496

KR_2_SDR_x

cd08953

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...

2344-2731

3.94e-67

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, 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 KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187656 [Multi-domain] Cd Length: 436 Bit Score: 234.95 E-value: 3.94e-67

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2344 PGDIEEwqqLLNRVPNIQEIVHCWSMVSTDLDRATIFSCSSTLHLVQALA--------NYPKNPRLSL-VTLGAQAVNEH 2414
Cdd:cd08953    42 PAALAS---AFLALAYEAALLGLAAAEAALLDALSALDPAAALQLLESLQrllkagllAARASGRALLqVVTGLPGALGL 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2415 HVQNVVGAALWGMGKVIALEHPELQVAQMDLDPngkvkaqvEVLRDELLARKdpasamsVPDLQTRPHEKQIAFREQTRY 2494
Cdd:cd08953   119 DALDPAGAGLAGLLRTLAQEYPGLTCRLIDLDA--------GEASAEALARE-------LAAELAAPGAAEVRYRDGLRY 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2495 VARLspldRPNPREKGTQEALTFRDDGSYLIAGGLGGLGLVVARFLVTNGARYLVLVGRRGAREEQQAQLS---ELEQLG 2571
Cdd:cd08953   184 VQTL----EPLPLPAGAAASAPLKPGGVYLVTGGAGGIGRALARALARRYGARLVLLGRSPLPPEEEWKAQtlaALEALG 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2572 ASVKVLQADIADAEQLAQALSAV--TYPPLRGVIHAAGTLNDGILQQQSWQAFKEVMNPKVAGAWNLHILTKNQPLDFFV 2649
Cdd:cd08953   260 ARVLYISADVTDAAAVRRLLEKVreRYGAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQALADEPLDFFV 339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2650 LFSSATSLLGNAGQANHAAANAFLDGLASYRR--HLGLPSLSINWGTWSEVGIAARLGLDKLSSKQGEGTITLGQGLQIL 2727
Cdd:cd08953   340 LFSSVSAFFGGAGQADYAAANAFLDAFAAYLRqrGPQGRVLSINWPAWREGGMAADLGARELLARAGLLPIEPEEGLQAL 419


                  ....
gi 602182148 2728 EQLL 2731
Cdd:cd08953   420 EQAL 423

KR_1_SDR_x

cd08952

ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ...

2385-2710

8.66e-67

ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the single KR domain of SpiF, the first KR domains of SpiE,-G,H,-I,and #J, the third KR domain of SpiG, and the second KR domain of SpiH. The second KR domains of SpiE,-G, I, and #J, and the KR domains of SpiD, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, 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 KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187655 [Multi-domain] Cd Length: 480 Bit Score: 235.53 E-value: 8.66e-67

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2385 TLHLVQALANYPKNPRLSLVTLGAQAVNEH-HVQNVVGAALWGMGKVIALEHPELQVAQMDLdPngkvkaqvEVLRDELL 2463
Cdd:cd08952   116 TLALVQALGDAGVDAPLWCVTRGAVAVGPDdPLPDPAQAAVWGLGRVAALEHPDRWGGLVDL-P--------ADLDARAL 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2464 ARKdpASAmsvpdLQTRPHEKQIAFREQTRYVARLSPLDRPNPREKgtqealTFRDDGSYLIAGGLGGLGLVVARFLVTN 2543
Cdd:cd08952   187 RRL--AAV-----LAGAGGEDQVAVRASGVFARRLVRAPAPAPAAR------PWRPRGTVLVTGGTGALGAHVARWLARR 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2544 GARYLVLVGRRGAREEQQAQL-SELEQLGASVKVLQADIADAEQLAQALSAVTY-PPLRGVIHAAGTLNDGILQQQSWQA 2621
Cdd:cd08952   254 GAEHLVLTSRRGPDAPGAAELvAELTALGARVTVAACDVADRDALAALLAALPAgHPLTAVVHAAGVLDDGPLDDLTPER 333

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2622 FKEVMNPKVAGAWNLHILTKNQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGLASYRRHLGLPSLSINWGTWSEVGIA 2701
Cdd:cd08952   334 LAEVLRAKVAGARHLDELTRDRDLDAFVLFSSIAGVWGSGGQGAYAAANAYLDALAERRRARGLPATSVAWGPWAGGGMA 413


                  ....*....
gi 602182148 2702 ARLGLDKLS 2710
Cdd:cd08952   414 AGAAAERLR 422

PS-DH

pfam14765

Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. ...

1590-1890

4.20e-63

Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. Structural analysis shows these DH domains are double hotdogs in which the active site contains a histidine from the N-terminal hotdog and an aspartate from the C-terminal hotdog. Studies have uncovered that a substrate tunnel formed between the DH domains may be essential for loading substrates and unloading products.

Pssm-ID: 434191 Cd Length: 296 Bit Score: 218.40 E-value: 4.20e-63

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  1590 HPLLGQRLHLSRTQEIYFQTFIHSDFPIWVADHKVFGNVIIPGVAYFEMALAAGKALKPDSIFW-LEDVSIAQALIIP-D 1667
Cdd:pfam14765    1 HPLLGSRVPSPSDLEPVWRNRLRLADLPWLRDHRVGGTVVLPGAGYLEMALEAARQLFGGSGAVaLRDVSILKALVLPeD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  1668 EGQTVQIVLSPQEESAYF---FEILSLEKE-NSWVLHASGKLVAqEQVLETEPIDLIALQAHCCEE-----VSVDVLYQE 1738
Cdd:pfam14765   81 DPVEVQTSLTPEEDGADSwweFEIFSRAGGgWEWTLHATGTVRL-APGEPAAPVDLESLPARCAQPadprsVSSAEFYER 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  1739 EMARRLDMGPMMRGVKQLWRYPLSfakshdaiALAKVSLPEILLHESNAYQFHPVILDAGLQMITVSYPEA--NQGQTYV 1816
Cdd:pfam14765  160 LAARGLFYGPAFQGLRRIWRGDGE--------ALAEARLPEAAAGGESPYLLHPALLDAALQLLGAALPAEaeHADQAYL 231

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 602182148  1817 PVGIEGLQVYG--RPSSELWCRAQYRPPLDTDqrqgidllpkkLIADLHLFDTQGRVVAIMFGVQSVLVGREAMLR 1890
Cdd:pfam14765  232 PVGIERLRIYRslPPGEPLWVHARLERRGGRT-----------IVGDLTLVDEDGRVVARIEGLRLRRVEREALLR 296

Acs

COG0365

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

26-576

5.94e-61

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

Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 221.14 E-value: 5.94e-61

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   26 HHLFEDQAAKRPDAIALI----DGE-QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAY 100
Cdd:COG0365    12 YNCLDRHAEGRGDKVALIwegeDGEeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  101 VPLDVGYPADRIEYMLRDSDARILLTST---------DVAKKLAltiPALQECQTV-------YLDQEIF---EYDFH-F 160
Cdd:COG0365    92 SPVFPGFGAEALADRIEDAEAKVLITADgglrggkviDLKEKVD---EALEELPSLehvivvgRTGADVPmegDLDWDeL 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  161 LAIAKllhnqylrllhfyfytliQQCQATSVSqgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRS-LVNMLWWHQQtrp 239
Cdd:COG0365   169 LAAAS------------------AEFEPEPTD--------ADDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKY--- 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  240 sVQGVR---TLqFCAVSFDF-SCH--EIFSTLCLGGILVLVPEA-VRQNPFALAEFISQQKIEKLFLP--VIALLQLAEA 310
Cdd:COG0365   220 -VLDLKpgdVF-WCTADIGWaTGHsyIVYGPLLNGATVVLYEGRpDFPDPGRLWELIEKYGVTVFFTAptAIRALMKAGD 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  311 VNGNKS--TSLALCevITTGEQmqITPAVAN-LFQKTGAMLHNHYGATEfqdaTTHTLKGNPEGWPtLVP--VGRPLHNV 385
Cdd:COG0365   298 EPLKKYdlSSLRLL--GSAGEP--LNPEVWEwWYEAVGVPIVDGWGQTE----TGGIFISNLPGLP-VKPgsMGKPVPGY 368

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  386 QVYILDEAQQPVPLGGEGEFCIGG--IGLARGYHNLPDLTNEKFipnpFGTNENakkLYRTGDLARYLPDGTIEHLGRID 463
Cdd:COG0365   369 DVAVVDEDGNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETY----FGRFPG---WYRTGDGARRDEDGYFWILGRSD 441

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  464 HQVKIRGFRVELGEIESVLASHQAVRECAVVAR--EIAGhTQLVGYIIAKDTLNLSfDKLEPILRQYSEAVLPEYMIPTR 541
Cdd:COG0365   442 DVINVSGHRIGTAEIESALVSHPAVAEAAVVGVpdEIRG-QVVKAFVVLKPGVEPS-DELAKELQAHVREELGPYAYPRE 519

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|
gi 602182148  542 FINISNMPLTPSGKLDRRALPD-----PKGDRPALSTPLV 576
Cdd:COG0365   520 IEFVDELPKTRSGKIMRRLLRKiaegrPLGDTSTLEDPEA 559

KAS_I_II

cd00834

Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...

677-1107

2.85e-58

Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.

Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 208.16 E-value: 2.85e-58

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  677 IAIISvagrfPGAETIEQFWHNLCNGVESItlfsddkleQTLPELFNNPAYVKAGAVlegVELFDATFFGySPKEAAVTD 756
Cdd:cd00834     8 LGAVT-----PLGNGVEEFWEALLAGRSGI---------RPITRFDASGFPSRIAGE---VPDFDPEDYL-DRKELRRMD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  757 PQQRILLECAWEAFERAGYNPETY-PEPVGVYAGSSLSTylLNNIGSALGIITEQPFIETDMEQFQAKIGNDrsyLATRI 835
Cdd:cd00834    70 RFAQFALAAAEEALADAGLDPEELdPERIGVVIGSGIGG--LATIEEAYRALLEKGPRRVSPFFVPMALPNM---AAGQV 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  836 SYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVpqkggylyEEGMV-----------RSQD--GH 902
Cdd:cd00834   145 AIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALI--------TPLTLagfaalralstRNDDpeKA 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  903 CRAFDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDgAIKMgyTAPSVD--GQADVISEAIAIADIDAS 980
Cdd:cd00834   217 SRPFDKDRDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASSD-AYHI--TAPDPDgeGAARAMRAALADAGLSPE 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  981 TIGYVEAHGTATQLGDPIEVAGLARAFQRSTDSVlgkqqcAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYA 1060
Cdd:cd00834   294 DIDYINAHGTSTPLNDAAESKAIKRVFGEHAKKV------PVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLE 367

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 602182148 1061 NPNPRIDFDatpfFVNTELREWsrngyPRRAGVS-SFGVGGTNSHIVL 1107
Cdd:cd00834   368 EPDPECDLD----YVPNEAREA-----PIRYALSnSFGFGGHNASLVF 406

FC-FACS_FadD_like

cd05936

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...

27-561

1.10e-57

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: 208.57 E-value: 1.10e-57

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   27 HLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVG 106
Cdd:cd05936     3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  107 YPADRIEYMLRDSDARILLTSTDVAKKLALTIPALQECQTVyldqeifeydfhflaiakllhnqylrllhfyfytliqqc 186
Cdd:cd05936    83 YTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERVALT--------------------------------------- 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  187 qatsvsqgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLV-NMlwwhQQTRPSVQGVRTLQ---FCAV----SFDFSC 258
Cdd:cd05936   124 --------------PEDVAVLQYTSGTTGVPKGAMLTHRNLVaNA----LQIKAWLEDLLEGDdvvLAALplfhVFGLTV 185

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  259 HeIFSTLCLGGILVLVPeavRQNPFALAEFISQQKIEkLFLPV----IALLQLAEAVNGNKStSLALCevITTGeqMQIT 334
Cdd:cd05936   186 A-LLLPLALGATIVLIP---RFRPIGVLKEIRKHRVT-IFPGVptmyIALLNAPEFKKRDFS-SLRLC--ISGG--APLP 255

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  335 PAVANLF-QKTGAMLHNHYGATEFQDATThtlkGNPEGWPTlVP--VGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIG 411
Cdd:cd05936   256 VEVAERFeELTGVPIVEGYGLTETSPVVA----VNPLDGPR-KPgsIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQ 330

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  412 LARGYHNLPDLTNEKFIPNPFgtnenakklyRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVREC 491
Cdd:cd05936   331 VMKGYWNRPEETAEAFVDGWL----------RTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEA 400

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 602182148  492 AVVA--REIAGHTqLVGYIIAKDTLNLSfdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05936   401 AVVGvpDPYSGEA-VKAFVVLKEGASLT----EEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467

decarbox_cond_enzymes

cd00825

decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...

758-1107

3.09e-56

decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).

Pssm-ID: 238421 [Multi-domain] Cd Length: 332 Bit Score: 199.78 E-value: 3.09e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  758 QQRILLECAWEAFERAGYNPETYPEP-VGVYAGSSLSTYLLNNIGSAlGIITEQPFIETdmeqfqakiGNDRSYLATRIS 836
Cdd:cd00825    11 VSILGFEAAERAIADAGLSREYQKNPiVGVVVGTGGGSPRFQVFGAD-AMRAVGPYVVT---------KAMFPGASGQIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  837 YKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQKGGYLYEEGMVRSQDGHCRAFDAEAQGTIFG 916
Cdd:cd00825    81 TPLGIHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALSTPEKASRTFDAAADGFVFG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  917 NGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGAiKMGYTAPSVDGQADVISEAIAIADIDASTIGYVEAHGTATQLGD 996
Cdd:cd00825   161 DGAGALVVEELEHALARGAHIYAEIVGTAATIDGA-GMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  997 PIEvaglarafQRSTDSVLGKQQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPRIDFDATPffvn 1076
Cdd:cd00825   240 VKE--------LKLLRSEFGDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLNIVTE---- 307

                         330       340       350
                  ....*....|....*....|....*....|.
gi 602182148 1077 telrewSRNGYPRRAGVSSFGVGGTNSHIVL 1107
Cdd:cd00825   308 ------TTPRELRTALLNGFGLGGTNATLVL 332

Acyl_transf_1

pfam00698

Acyl transferase domain;

1210-1518

2.31e-55

Acyl transferase domain;

Pssm-ID: 395567 Cd Length: 319 Bit Score: 196.92 E-value: 2.31e-55

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  1210 FLFTGQGSQYINMGRTLYDTESTFRAALDRCETILQNLGIESIISVIFgSSEHGLsLDDTAYTQPALFAIEYALYQLWKS 1289
Cdd:pfam00698    2 FVFSGQGSQWAGMGMQLLKTSPAFAAVIDRADEAFKPQYGFSVSDVLR-NNPEGT-LDGTQFVQPALFAMQIALAALLQS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  1290 WGIQPSVVIGHSVGEYVSACVAGVFSLEDGLKLIAERGRLIQALPRDGSMVSVMASEKRIADIILPyggQVGIAAINGPQ 1369
Cdd:pfam00698   80 YGVRPDAVVGHSLGEYAAAVVAGALSPEEALLAAVLRSRLMMQLAGPGGMAAVELSAEEVEQRWPD---DVVGAVVNSPR 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  1370 SVVISGQQQAIDAICAILETEGIKSKKLNVSHAFHSPLVEAMLDSFLQVAQEVTYSQPQIKLISnvtgtlaSHESCPDEL 1449
Cdd:pfam00698  157 SVVISGPQEAVRELVERVSKEGVGALVENVNYAVHSPQMDAIAPALLSALADIAPRTPRVPFIS-------STSIDPSDQ 229

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 602182148  1450 PITTAEYWVRHVRQPVRFAAGMESLEGQGVNVFIEIGPKPVLLGMGRDCLPEQEGL----WLPSLRPKQDDWQ 1518
Cdd:pfam00698  230 RTLSAEYWVRNLRSPVRFAEAILSAAEPGPLVFIEISPHPLLLAALIDTLKSASDGkvatLVGTLIRDQTDFL 302

fabD

TIGR00128

malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ...

1208-1494

2.41e-55

malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis transfers the malonyl moeity from coenzyme A to acyl-carrier protein. The seed alignment for this family of proteins contains a single member each from a number of bacterial species but also an additional pair of closely related, uncharacterized proteins from B. subtilis, one of which has a long C-terminal extension. [Fatty acid and phospholipid metabolism, Biosynthesis]

Pssm-ID: 272922 [Multi-domain] Cd Length: 290 Bit Score: 195.76 E-value: 2.41e-55

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  1208 IAFLFTGQGSQYINMGRTLYDTESTFRAALDRCETILQNlgieSIISVIFGSSEhgLSLDDTAYTQPALFAIEYALYQLW 1287
Cdd:TIGR00128    3 IAYVFPGQGSQTVGMGKDLYEQYPIAKELFDQASEALGY----DLKKLCQEGPA--EELNKTQYTQPALYVVSAILYLKL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  1288 K-SWGIQPSVVIGHSVGEYVSACVAGVFSLEDGLKLIAERGRLIQ-ALP-RDGSMVSVMA-SEKRIADIILPYGGQ-VGI 1362
Cdd:TIGR00128   77 KeQGGLKPDFAAGHSLGEYSALVAAGALDFETALKLVKKRGELMQeAVPeGGGAMAAVIGlDEEQLAQACEEATENdVDL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  1363 AAINGPQSVVISGQQQAIDAICAILETEGIK-SKKLNVSHAFHSPLVEAMLDSFLQVAQEVTYSQPQIKLISNVTgtlAS 1441
Cdd:TIGR00128  157 ANFNSPGQVVISGTKDGVEAAAALFKEMGAKrAVPLEVSGAFHSRFMKPAAEKFAETLEACQFNDPTVPVISNVD---AK 233

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 602182148  1442 HESCPDELpittAEYWVRHVRQPVRFAAGMESLEGQGVNVFIEIGPKPVLLGM 1494
Cdd:TIGR00128  234 PYTNGDRI----KEKLSEQLTSPVRWTDSVEKLMARGVTEFAEVGPGKVLTGL 282

FabB

COG0304

3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...

687-1107

7.05e-55

3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis

Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 198.40 E-value: 7.05e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  687 PGAETIEQFWHNLCNG---VESITLFSDDKLEQTLpelfnnpayvkAGAVLEgvelFDATFFgYSPKEAAVTDPQQRILL 763
Cdd:COG0304    13 PLGNGVEEFWEALLAGrsgIRPITRFDASGLPVRI-----------AGEVKD----FDPEEY-LDRKELRRMDRFTQYAL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  764 ECAWEAFERAGYNPETY-PEPVGVYAGSSLSTylLNNIGSALGIITEQ------PFIETDMeqfqakIGNDrsyLATRIS 836
Cdd:COG0304    77 AAAREALADAGLDLDEVdPDRTGVIIGSGIGG--LDTLEEAYRALLEKgprrvsPFFVPMM------MPNM---AAGHVS 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  837 YKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISvvvpqkgGYLYEEGM----------VRSQD--GHCR 904
Cdd:COG0304   146 IRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAE-------AAITPLGLagfdalgalsTRNDDpeKASR 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  905 AFDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGAiKMGYTAPSVDGQADVISEAIAIADIDASTIGY 984
Cdd:COG0304   219 PFDKDRDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDAY-HITAPAPDGEGAARAMRAALKDAGLSPEDIDY 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  985 VEAHGTATQLGDPIEVAGLARAFQRSTDSVlgkqqcAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNP 1064
Cdd:COG0304   298 INAHGTSTPLGDAAETKAIKRVFGDHAYKV------PVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDP 371

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 602182148 1065 RIDFDatpfFVNTELREWsrngyPRRAGVS-SFGVGGTNSHIVL 1107
Cdd:COG0304   372 ECDLD----YVPNEAREA-----KIDYALSnSFGFGGHNASLVF 406

AFD_class_I

cd04433

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...

204-557

1.09e-53

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: 192.50 E-value: 1.09e-53

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  204 LAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLqfCAVSFDFSCH--EIFSTLCLGGILVLVPeavRQN 281
Cdd:cd04433     2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFL--STLPLFHIGGlfGLLGALLAGGTVVLLP---KFD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  282 PFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALCEVITTGEQMqiTPAVANLF-QKTGAMLHNHYGATEFQDA 360
Cdd:cd04433    77 PEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPL--PPELLERFeEAPGIKLVNGYGLTETGGT 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  361 TTHTLKGNPEGWPTlvPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNpfgtnenakk 440
Cdd:cd04433   155 VATGPPDDDARKPG--SVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDG---------- 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  441 LYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLVG-YIIAKDTLNLSFD 519
Cdd:cd04433   223 WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVaVVVLRPGADLDAE 302

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 602182148  520 KlepiLRQYSEAVLPEYMIPTRFINISNMPLTPSGKLD 557
Cdd:cd04433   303 E----LRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336

PRK06187

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

25-564

7.91e-52

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

Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 192.71 E-value: 7.91e-52

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   25 IHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLD 104
Cdd:PRK06187    8 IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPIN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  105 VGYPADRIEYMLRDSDARILLTSTDVAKKLALTIPALQECQTVyldqeIFEYDFHFLAIAKLLHNqylrllhfyFYTLIq 184
Cdd:PRK06187   88 IRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTV-----IVEGDGPAAPLAPEVGE---------YEELL- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  185 qcqATSVSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMlwwhqqtrpsvqgvrTLQFCAVsFDFSCHEIF-- 262
Cdd:PRK06187  153 ---AAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLH---------------SLAVCAW-LKLSRDDVYlv 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  263 ---------STLCLGGILV----LVPEavRQNPFALAEFISQQKIEKLFL-PVI--ALLQLAEAvNGNKSTSLALceVIT 326
Cdd:PRK06187  214 ivpmfhvhaWGLPYLALMAgakqVIPR--RFDPENLLDLIETERVTFFFAvPTIwqMLLKAPRA-YFVDFSSLRL--VIY 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  327 TGEQMqiTPAVANLFQ-KTGAMLHNHYGATEfqdaTTHTL------KGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPL 399
Cdd:PRK06187  289 GGAAL--PPALLREFKeKFGIDLVQGYGMTE----TSPVVsvlppeDQLPGQWTKRRSAGRPLPGVEARIVDDDGDELPP 362

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  400 GGE--GEFCIGGIGLARGYHNLPDLTNEKFipnpfgtnenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGE 477
Cdd:PRK06187  363 DGGevGEIIVRGPWLMQGYWNRPEATAETI----------DGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRE 432

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  478 IESVLASHQAVRECAVVAR--EIAGHTQLVgYIIAKDTLNLSFDKLepilRQYSEAVLPEYMIPTRFINISNMPLTPSGK 555
Cdd:PRK06187  433 LEDALYGHPAVAEVAVIGVpdEKWGERPVA-VVVLKPGATLDAKEL----RAFLRGRLAKFKLPKRIAFVDELPRTSVGK 507


                  ....*....
gi 602182148  556 LDRRALPDP 564
Cdd:PRK06187  508 ILKRVLREQ 516

Ketoacyl-synt_C

pfam02801

Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...

938-1059

2.28e-49

Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.

Pssm-ID: 426989 Cd Length: 118 Bit Score: 171.60 E-value: 2.28e-49

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   938 MAVIKATAINNDGAiKMGYTAPSVDGQADVISEAIAIADIDASTIGYVEAHGTATQLGDPIEVAGLARAFQRSTDsvlgK 1017
Cdd:pfam02801    1 YAVIKGSAVNHDGR-HNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGAR----K 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 602182148  1018 QQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHY 1059
Cdd:pfam02801   76 QPLAIGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNL 117

A_NRPS_alphaAR

cd17647

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...

47-564

3.32e-49

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: 185.03 E-value: 3.32e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   47 QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRieymlrdsdarillt 126
Cdd:cd17647    19 RSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPAR--------------- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  127 stdvakklaltipalqecQTVYLDqeifeydfhflaIAKllhnqylrllhfyfytliqqCQATSVSQGIQTQVLPNNLAY 206
Cdd:cd17647    84 ------------------QNIYLG------------VAK--------------------PRGLIVIRAAGVVVGPDSNPT 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  207 CIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTLCLGGILvLVPEAVRQ-NPFAL 285
Cdd:cd17647   114 LSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQL-LVPTQDDIgTPGRL 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  286 AEFISQQKIEKLFL-PVIALLQLAEAVNGNKSTSLA--LCEVITTGEQMQITPAVANLfqktgaMLHNHYGATEFQDATT 362
Cdd:cd17647   193 AEWMAKYGATVTHLtPAMGQLLTAQATTPFPKLHHAffVGDILTKRDCLRLQTLAENV------RIVNMYGTTETQRAVS 266

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  363 H----TLKGNP---EGWPTLVPVGRPLHNVQVYILD--EAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPF- 432
Cdd:cd17647   267 YfevpSRSSDPtflKNLKDVMPAGRGMLNVQLLVVNrnDRTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFv 346

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  433 ----------GTNENAK--------KLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRE-CAV 493
Cdd:cd17647   347 epdhwnyldkDNNEPWRqfwlgprdRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVREnITL 426

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  494 VAREIAGHTQLVGYIIAKDTLNLSFDKL----------EPI-------------LRQYSEAVLPEYMIPTRFINISNMPL 550
Cdd:cd17647   427 VRRDKDEEPTLVSYIVPRFDKPDDESFAqedvpkevstDPIvkgligyrklikdIREFLKKRLASYAIPSLIVVLDKLPL 506

                         570
                  ....*....|....
gi 602182148  551 TPSGKLDRRALPDP 564
Cdd:cd17647   507 NPNGKVDKPKLQFP 520

Firefly_Luc_like

cd05911

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...

41-556

1.47e-47

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: 179.33 E-value: 1.47e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   41 ALIDGE--QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRD 118
Cdd:cd05911     1 AQIDADtgKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  119 SDARILLTSTDVAKKLaltIPALQECQTVY----LDQEIFEYdfhfLAIAKLLHNQYLRLLHFYFytliqqcqatsvsqg 194
Cdd:cd05911    81 SKPKVIFTDPDGLEKV---KEAAKELGPKDkiivLDDKPDGV----LSIEDLLSPTLGEEDEDLP--------------- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  195 IQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFD-----FSCHeiFSTLClGG 269
Cdd:cd05911   139 PPLKDGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYhiyglFTTL--ASLLN-GA 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  270 ILVLVPeavRQNPFALAEFISQQKIEKLFL--PVIALLQLAEAVNGNKSTSLalcEVITTG-----EQMQitPAVANLFQ 342
Cdd:cd05911   216 TVIIMP---KFDSELFLDLIEKYKITFLYLvpPIAAALAKSPLLDKYDLSSL---RVILSGgaplsKELQ--ELLAKRFP 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  343 KtgAMLHNHYGATEFQDATTHtlkgNPEGWPTLVPVGRPLHNVQVYILDEA-QQPVPLGGEGEFCIGGIGLARGYHNLPD 421
Cdd:cd05911   288 N--ATIKQGYGMTETGGILTV----NPDGDDKPGSVGRLLPNVEAKIVDDDgKDSLGPNEPGEICVRGPQVMKGYYNNPE 361

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  422 LTNEKFIPNPFgtnenakklYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGH 501
Cdd:cd05911   362 ATKETFDEDGW---------LHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVS 432

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  502 TQL-VGYIIAKDTLNLSFDKlepiLRQYSEAVLPEYmipTRFIN----ISNMPLTPSGKL 556
Cdd:cd05911   433 GELpRAYVVRKPGEKLTEKE----VKDYVAKKVASY---KQLRGgvvfVDEIPKSASGKI 485

elong_cond_enzymes

cd00828

"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...

688-1107

9.54e-47

"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.

Pssm-ID: 238424 [Multi-domain] Cd Length: 407 Bit Score: 174.93 E-value: 9.54e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  688 GAETIEQFWHNLCNGVESITLFSDDKLEqtlpelfnnpayvKAGAVLEGVELFDatFFGYSPKEAAVTDPQQRILLECAW 767
Cdd:cd00828    17 GCDEVEEFWEALREGRSGIAPVARLKSR-------------FDRGVAGQIPTGD--IPGWDAKRTGIVDRTTLLALVATE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  768 EAFERAGYNPETY--PEPVGVYAGSSLSTYllnnigSALGIITEQPFIETDMEQFQAKIGNDRSYLATRISYKLNLKGPS 845
Cdd:cd00828    82 EALADAGITDPYEvhPSEVGVVVGSGMGGL------RFLRRGGKLDARAVNPYVSPKWMLSPNTVAGWVNILLLSSHGPI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  846 VNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQKGGYLYEEGMV----RSQDGHCRAFDAEAQGTIFGNGGGL 921
Cdd:cd00828   156 KTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSGFANMGALstaeEEPEEMSRPFDETRDGFVEAEGAGV 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  922 VLLKRLQDALDDNDNIMAVIKATAINNDGAiKMGYTAPsVDGQADVISEAIAIADIDASTIGYVEAHGTATQLGDPIEVA 1001
Cdd:cd00828   236 LVLERAELALARGAPIYGRVAGTASTTDGA-GRSVPAG-GKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAESR 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1002 GLARAFQRSTDSVlgkqqcAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPRIDFDATPffvnTELRe 1081
Cdd:cd00828   314 AIAEVAGALGAPL------PVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVV----GLSR- 382

                         410       420
                  ....*....|....*....|....*.
gi 602182148 1082 wSRNGYPRRAGVSSFGVGGTNSHIVL 1107
Cdd:cd00828   383 -DLNLKVRAALVNAFGFGGSNAALVL 407

ligase_PEP_1

TIGR03098

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...

25-561

3.62e-45

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: 173.04 E-value: 3.62e-45

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148    25 IHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLD 104
Cdd:TIGR03098    2 LHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   105 VGYPADRIEYMLRDSDARILLTStdvAKKLALTIPALQECqtvyldqeifeYDFHFLAIAKLLHNqyLRLLHFYFYTLIQ 184
Cdd:TIGR03098   82 PLLKAEQVAHILADCNVRLLVTS---SERLDLLHPALPGC-----------HDLRTLIIVGDPAH--ASEGHPGEEPASW 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   185 QCQATSVSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVN---MLWWHQQTRPsvqGVRTLQFCAVSFDFSCHEI 261
Cdd:TIGR03098  146 PKLLALGDADPPHPVIDSDMAAILYTSGSTGRPKGVVLSHRNLVAgaqSVATYLENRP---DDRLLAVLPLSFDYGFNQL 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   262 FSTLCLGGILVLVPEAVrqnPFALAEFISQQKIEKLF-LPVIaLLQLAEaVNGNKSTSLALCEVITTGEQM--QITPAVA 338
Cdd:TIGR03098  223 TTAFYVGATVVLHDYLL---PRDVLKALEKHGITGLAaVPPL-WAQLAQ-LDWPESAAPSLRYLTNSGGAMprATLSRLR 297

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   339 NLFQKtgAMLHNHYGATEFQDATTHTlkgnpegwPTLV-----PVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLA 413
Cdd:TIGR03098  298 SFLPN--ARLFLMYGLTEAFRSTYLP--------PEEVdrrpdSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVA 367

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   414 RGYHNLPDLTNEKFIPNPfgTNENAKKLYRT----GDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVR 489
Cdd:TIGR03098  368 MGYWNDPEKTAERFRPLP--PFPGELHLPELavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVA 445

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 602182148   490 ECAV--VAREIAGHtQLVGYIIAKDTLNLSFDKLEPILRQYseavLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:TIGR03098  446 EAVAfgVPDPTLGQ-AIVLVVTPPGGEELDRAALLAECRAR----LPNYMVPALIHVRQALPRNANGKIDRKAL 514

BCL_4HBCL

cd05959

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...

36-561

3.92e-45

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: 172.94 E-value: 3.92e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   36 RPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYM 115
Cdd:cd05959    17 RGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYY 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  116 LRDSDARILLTSTDVAKKLALTIPALQECQTVYLDQEIFEYDFHFLAIAKLLhnqylrllhfyfytliqqcqATSVSQGI 195
Cdd:cd05959    97 LEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPEAGALLLAELV--------------------AAEAEQLK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  196 QTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQtrpSVQGVRTLQFCavsfdFSCHEIF-------STLC-- 266
Cdd:cd05959   157 PAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYAR---NVLGIREDDVC-----FSAAKLFfayglgnSLTFpl 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  267 -LGGILVLVPEavRQNPFALAEFISQQKIEKLF-LPVI--ALLQLAEAVNGNKStSLALCevITTGEQMqitPA-VANLF 341
Cdd:cd05959   229 sVGATTVLMPE--RPTPAAVFKRIRRYRPTVFFgVPTLyaAMLAAPNLPSRDLS-SLRLC--VSAGEAL---PAeVGERW 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  342 QK-TGAMLHNHYGATE----FQDATTHTLKGNPEGWPtlVPvgrplhNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGY 416
Cdd:cd05959   301 KArFGLDILDGIGSTEmlhiFLSNRPGRVRYGTTGKP--VP------GYEVELRDEDGGDVADGEPGELYVRGPSSATMY 372

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  417 HNLPDLTNEKFIpnpfgtnenaKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAR 496
Cdd:cd05959   373 WNNRDKTRDTFQ----------GEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGV 442

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 602182148  497 EIA-GHTQLVGYIIAKDTLNLSfDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05959   443 EDEdGLTKPKAFVVLRPGYEDS-EALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507

FACL_FadD13-like

cd17631

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...

33-558

1.30e-44

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: 169.33 E-value: 1.30e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   33 AAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRI 112
Cdd:cd17631     5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  113 EYMLRDSDARILLtstdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvs 192
Cdd:cd17631    85 AYILADSGAKVLF------------------------------------------------------------------- 97

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  193 qgiqtqvlpNNLAYCIYTSGSTGNPKGILMEHRSLVnmlwWHQQTRPSVQGVRTLQFCAVSFD-FSCHE----IFSTLCL 267
Cdd:cd17631    98 ---------DDLALLMYTSGTTGRPKGAMLTHRNLL----WNAVNALAALDLGPDDVLLVVAPlFHIGGlgvfTLPTLLR 164

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  268 GGILVLVPEAvrqNPFALAEFISQQKIEKLFLP---VIALLQLAEAVNGNKSTslaLCEVITTGEQMQitPAVANLFQKT 344
Cdd:cd17631   165 GGTVVILRKF---DPETVLDLIERHRVTSFFLVptmIQALLQHPRFATTDLSS---LRAVIYGGAPMP--ERLLRALQAR 236

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  345 GAMLHNHYGATE------FQDATTHTLKgnpegwptLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHN 418
Cdd:cd17631   237 GVKFVQGYGMTEtspgvtFLSPEDHRRK--------LGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWN 308

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  419 LPDLTNEKFipnpfgtnenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAR-- 496
Cdd:cd17631   309 RPEATAAAF----------RDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVpd 378

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 602182148  497 ----EIAghtqlVGYIIAKDTLNLSfdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDR 558
Cdd:cd17631   379 ekwgEAV-----VAVVVPRPGAELD----EDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435

FACL_fum10p_like

cd05926

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...

37-563

1.07e-41

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: 162.10 E-value: 1.07e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   37 PDAIALI--DGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEY 114
Cdd:cd05926     1 PDAPALVvpGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  115 MLRDSDARILLTSTDV-------AKKLALTIpalqecQTVYLDQEIFEydfhflaiaklLHNQYLRLlhfyfytliQQCQ 187
Cdd:cd05926    81 YLADLGSKLVLTPKGElgpasraASKLGLAI------LELALDVGVLI-----------RAPSAESL---------SNLL 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  188 ATSVSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNmlwwhqqtrpSVQGV----------RTLqfcAVSFDFS 257
Cdd:cd05926   135 ADKKNAKSEGVPLPDDLALILHTSGTTGRPKGVPLTHRNLAA----------SATNItntykltpddRTL---VVMPLFH 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  258 CHEI----FSTLCLGGILVLVPEavrqnpFALAEFISQqkIEKL------FLPVI--ALLQLAEAVNGNK--------ST 317
Cdd:cd05926   202 VHGLvaslLSTLAAGGSVVLPPR------FSASTFWPD--VRDYnatwytAVPTIhqILLNRPEPNPESPppklrfirSC 273

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  318 SLALcevittgeqmqiTPAVANLFQKT-GAMLHNHYGATEfqdaTTHTLKGNPegWPTLVP----VGRPlHNVQVYILDE 392
Cdd:cd05926   274 SASL------------PPAVLEALEATfGAPVLEAYGMTE----AAHQMTSNP--LPPGPRkpgsVGKP-VGVEVRILDE 334

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  393 AQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFgtnenakklYRTGDLARYLPDGTIEHLGRIDHQVKIRGFR 472
Cdd:cd05926   335 DGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW---------FRTGDLGYLDADGYLFLTGRIKELINRGGEK 405

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  473 VELGEIESVLASHQAVRECAVVA--REIAGhtQLVG-YIIAKdtLNLSFDKLEpiLRQYSEAVLPEYMIPTRFINISNMP 549
Cdd:cd05926   406 ISPLEVDGVLLSHPAVLEAVAFGvpDEKYG--EEVAaAVVLR--EGASVTEEE--LRAFCRKHLAAFKVPKKVYFVDELP 479

                         570
                  ....*....|....
gi 602182148  550 LTPSGKLDRRALPD 563
Cdd:cd05926   480 KTATGKIQRRKVAE 493

KR_1_FAS_SDR_x

cd08954

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ...

2537-2735

5.04e-41

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; NADP-dependent KR domain of the multidomain type I FAS, a complex SDR family. This subfamily also includes proteins identified as polyketide synthase (PKS), a protein with related modular protein architecture and similar function. It includes the KR domains of mammalian and chicken FAS, and Dictyostelium discoideum putative polyketide synthases (PKSs). These KR domains contain two subdomains, each of which is related to SDR Rossmann fold domains. However, while the C-terminal subdomain has an active site similar to the other SDRs and a NADP-binding capability, the N-terminal SDR-like subdomain is truncated and lacks these functions, serving a supportive structural role. In some instances, such as porcine FAS, an enoyl reductase (a Rossman fold NAD-binding domain of the medium-chain dehydrogenase/reductase, MDR family) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER); this KR and ER are members of the SDR family. This KR subfamily has an active site tetrad with a similar 3D orientation compared to archetypical SDRs, but the active site Lys and Asn residue positions are swapped. The characteristic NADP-binding is typical of the multidomain complex SDRs, with a GGXGXXG NADP binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, 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 KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187657 [Multi-domain] Cd Length: 452 Bit Score: 159.15 E-value: 5.04e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2537 ARFLVTNGAR-YLVLVGRRGAREEQQAQLSELEQLGASVKVLQADIADAEQLA----QALSAVTYPPLRGVIHAAGTLND 2611
Cdd:cd08954   235 LKWLVKRGAVeNIIILSRSGMKWELELLIREWKSQNIKFHFVSVDVSDVSSLEkainLILNAPKIGPIGGIFHLAFVLID 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2612 GILQQQSWQAFKEVMNPKVAGAWNLHILT--KNQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGLASYRRHLGLPSLS 2689
Cdd:cd08954   315 KVLEIDTESLFISVNKAKVMGAINLHNQSikRCWKLDYFVLFSSVSSIRGSAGQCNYVCANSVLDSLSRYRKSIGLPSIA 394

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 602182148 2690 INWGTWSEVGIAARLG-LDKLSSKQGEGTITLGQGLQILEQLLKDEN 2735
Cdd:cd08954   395 INWGAIGDVGFVSRNEsVDTLLGGQGLLPQSINSCLGTLDLFLQNPS 441

MCS

cd05941

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...

38-561

1.88e-40

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: 157.07 E-value: 1.88e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   38 DAIALIDGEQSLTYGELNVRANHLAQHLLSLGC-QPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYML 116
Cdd:cd05941     1 DRIAIVDDGDSITYADLVARAARLANRLLALGKdLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  117 RDSDARILLtstdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiq 196
Cdd:cd05941    81 TDSEPSLVL----------------------------------------------------------------------- 89

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  197 tqvlpnNLAYCIYTSGSTGNPKGILMEHRSLVNML------W-------------WHQqtrpsVQGVRTLQFCAV----- 252
Cdd:cd05941    90 ------DPALILYTSGTTGRPKGVVLTHANLAANVralvdaWrwteddvllhvlpLHH-----VHGLVNALLCPLfagas 158

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  253 ---SFDFSCHEIFSTLCLGGILVL--VP-------EAVRQNpFALAEFISQQKIEKLFLPViallqlaeavngnkSTSLA 320
Cdd:cd05941   159 vefLPKFDPKEVAISRLMPSITVFmgVPtiytrllQYYEAH-FTDPQFARAAAAERLRLMV--------------SGSAA 223

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  321 LcevittgeqmqITPAVANLFQKTGAMLHNHYGATEFQDATTHTLKGNPE-GWptlvpVGRPLHNVQVYILD-EAQQPVP 398
Cdd:cd05941   224 L-----------PVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGERRpGT-----VGMPLPGVQARIVDeETGEPLP 287

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  399 LGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFgtnenakklYRTGDLARYLPDGTIEHLGRI-DHQVKIRGFRVELGE 477
Cdd:cd05941   288 RGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW---------FKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALE 358

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  478 IESVLASHQAVRECAVVAREIAGHTQLVGYIIA--KDTLNLSFDKLEPILRQyseaVLPEYMIPTRFINISNMPLTPSGK 555
Cdd:cd05941   359 IERVLLAHPGVSECAVIGVPDPDWGERVVAVVVlrAGAAALSLEELKEWAKQ----RLAPYKRPRRLILVDELPRNAMGK 434


                  ....*.
gi 602182148  556 LDRRAL 561
Cdd:cd05941   435 VNKKEL 440

PRK07656

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

31-561

3.59e-40

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

Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 158.14 E-value: 3.59e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   31 DQAAKR-PDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPA 109
Cdd:PRK07656   12 ARAARRfGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  110 DRIEYMLRDSDARILLTSTD---VAKKLALTIPALqECQTVYLDQEIFEYDFHFLAIAKLLhnqylrllhfyfytliqqc 186
Cdd:PRK07656   92 DEAAYILARGDAKALFVLGLflgVDYSATTRLPAL-EHVVICETEEDDPHTEKMKTFTDFL------------------- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  187 qATSVSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSL-------VNMLwwhqQTRPsvqGVRTLqfCAVSFdfsch 259
Cdd:PRK07656  152 -AAGDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLlsnaadwAEYL----GLTE---GDRYL--AANPF----- 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  260 eiFSTLCL----------GGILVLVPeavRQNPFALAEFISQQKIEKLF-LPVI--ALLQLAEAVNGNKStSLALCevIT 326
Cdd:PRK07656  217 --FHVFGYkagvnaplmrGATILPLP---VFDPDEVFRLIETERITVLPgPPTMynSLLQHPDRSAEDLS-SLRLA--VT 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  327 TGEQMqitpAVANL--FQK--------TGamlhnhYGATEFQDATTHTlkgNPEGWPTLVP--VGRPLHNVQVYILDEAQ 394
Cdd:PRK07656  289 GAASM----PVALLerFESelgvdivlTG------YGLSEASGVTTFN---RLDDDRKTVAgtIGTAIAGVENKIVNELG 355

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  395 QPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFgtnenakkLYrTGDLARYLPDGTIEHLGRIDHQVKIRGFRVE 474
Cdd:PRK07656  356 EEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGW--------LH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVY 426

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  475 LGEIESVLASHQAVRECAVV----AR--EiAGHtqlvGYIIAKDTLNLSfdklEPILRQYSEAVLPEYMIPTRFINISNM 548
Cdd:PRK07656  427 PAEVEEVLYEHPAVAEAAVIgvpdERlgE-VGK----AYVVLKPGAELT----EEELIAYCREHLAKYKVPRSIEFLDEL 497

                         570
                  ....*....|...
gi 602182148  549 PLTPSGKLDRRAL 561
Cdd:PRK07656  498 PKNATGKVLKRAL 510

MACS_like_3

cd05971

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...

50-561

1.87e-38

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: 151.43 E-value: 1.87e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   50 TYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLTStd 129
Cdd:cd05971     8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTD-- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  130 vakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiqtqvLPNNLAYCIY 209
Cdd:cd05971    86 ----------------------------------------------------------------------GSDDPALIIY 95

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  210 TSGSTGNPKGILMEHRSLVNMLwwhqqtrPSVQgvrtlqfcavsfdfSCHEIFSTL-----------CLGGIL-VLVPE- 276
Cdd:cd05971    96 TSGTTGPPKGALHAHRVLLGHL-------PGVQ--------------FPFNLFPRDgdlywtpadwaWIGGLLdVLLPSl 154

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  277 -------AVRQNPF---ALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALCEVITTGEqmqitPAVANLFQ---- 342
Cdd:cd05971   155 yfgvpvlAHRMTKFdpkAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGE-----SLGEELLGware 229

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  343 KTGAMLHNHYGATEfqdatTHTLKGNPEGWPTLVP--VGRPLHNVQVYILDEAQQPVPLGGEGEfciggIGLAR------ 414
Cdd:cd05971   230 QFGVEVNEFYGQTE-----CNLVIGNCSALFPIKPgsMGKPIPGHRVAIVDDNGTPLPPGEVGE-----IAVELpdpvaf 299

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  415 -GYHNLPDLTNEKFipnpfgtnenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAV 493
Cdd:cd05971   300 lGYWNNPSATEKKM----------AGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAV 369

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 602182148  494 VAREIAGHTQLV-GYIIakdtLNLSFDKLEPI---LRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05971   370 VGIPDPIRGEIVkAFVV----LNPGETPSDALareIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRREL 437

BCL_like

cd05919

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...

41-561

2.68e-38

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: 150.69 E-value: 2.68e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   41 ALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSD 120
Cdd:cd05919     3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  121 ARILLTSTDvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiqtqvl 200
Cdd:cd05919    83 ARLVVTSAD----------------------------------------------------------------------- 91

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  201 pnNLAYCIYTSGSTGNPKGILMEHRslvNMLWWHQQTRPSVQGV----RTLQFCAVSFDFSC-HEIFSTLCLGGILVLVP 275
Cdd:cd05919    92 --DIAYLLYSSGTTGPPKGVMHAHR---DPLLFADAMAREALGLtpgdRVFSSAKMFFGYGLgNSLWFPLAVGASAVLNP 166

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  276 EAVrqNPFALAEFISQQKIEKLF-LPVIALLQLAEAVNGNKS-TSLALCevITTGEQMQitpavANLFQK----TGAMLH 349
Cdd:cd05919   167 GWP--TAERVLATLARFRPTVLYgVPTFYANLLDSCAGSPDAlRSLRLC--VSAGEALP-----RGLGERwmehFGGPIL 237

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  350 NHYGATEfqdaTTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFip 429
Cdd:cd05919   238 DGIGATE----VGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-- 311

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  430 npfgtnenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVA-REIAGHTQLVGYI 508
Cdd:cd05919   312 --------NGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAvPESTGLSRLTAFV 383

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 602182148  509 IAKDTLNLSFDKLEPILRQYSEAvLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05919   384 VLKSPAAPQESLARDIHRHLLER-LSAHKVPRRIAFVDELPRTATGKLQRFKL 435

MACS_like

cd05972

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...

49-563

4.99e-38

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: 149.79 E-value: 4.99e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   49 LTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLTST 128
Cdd:cd05972     1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  129 DvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiqtqvlpnNLAYCI 208
Cdd:cd05972    81 E-------------------------------------------------------------------------DPALIY 87

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  209 YTSGSTGNPKGILMEHRSLVNmlwwHQQTRPSVQGVRT--LQFC--------AVSFDFscheiFSTLCLGgILVLVPEAV 278
Cdd:cd05972    88 FTSGTTGLPKGVLHTHSYPLG----HIPTAAYWLGLRPddIHWNiadpgwakGAWSSF-----FGPWLLG-ATVFVYEGP 157

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  279 RQNPFALAEFISQQKIEKLFLPVIALLQLAEA--VNGNKSTslaLCEVITTGEQMqiTPAVANLFQ-KTGAMLHNHYGAT 355
Cdd:cd05972   158 RFDAERILELLERYGVTSFCGPPTAYRMLIKQdlSSYKFSH---LRLVVSAGEPL--NPEVIEWWRaATGLPIRDGYGQT 232

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  356 E--FQDATTHTLKGNPEGwptlvpVGRPLHNVQVYILDEAQQPVPLGGEGEFCI--GGIGLARGYHNLPDLTNEKFIPNp 431
Cdd:cd05972   233 EtgLTVGNFPDMPVKPGS------MGRPTPGYDVAIIDDDGRELPPGEEGDIAIklPPPGLFLGYVGDPEKTEASIRGD- 305

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  432 fgtnenakkLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLV-GYIIA 510
Cdd:cd05972   306 ---------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVkAFVVL 376

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 602182148  511 KDTLNLSfDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALPD 563
Cdd:cd05972   377 TSGYEPS-EELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428

A_NRPS_acs4

cd17654

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...

37-561

5.32e-38

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: 150.32 E-value: 5.32e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   37 PDAIALIDGEQ----SLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRI 112
Cdd:cd17654     1 PDRPALIIDQTtsdtTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  113 EYMLRDSDarilltstdvakklaltipalqecqtvyldqeifeyDFHFLAiAKLLHNQYLRLLHFYFYTLIQQcqatsvs 192
Cdd:cd17654    81 LTVMKKCH------------------------------------VSYLLQ-NKELDNAPLSFTPEHRHFNIRT------- 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  193 qgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLV-NMLWWHQQTRPSVQgvRTLQFCAV-SFDFSCHEIFSTLCLGGI 270
Cdd:cd17654   117 --------DECLAYVIHTSGTTGTPKIVAVPHKCILpNIQHFRSLFNITSE--DILFLTSPlTFDPSVVEIFLSLSSGAT 186

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  271 LVLVPEAVRQNPFALAEFI-SQQKIEKLFLPViALL-----QLAEAVNGNKSTSLalcEVITTGEQMQITPAVANLFQKT 344
Cdd:cd17654   187 LLIVPTSVKVLPSKLADILfKRHRITVLQATP-TLFrrfgsQSIKSTVLSATSSL---RVLALGGEPFPSLVILSSWRGK 262

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  345 GAMLH--NHYGATEFQD-ATTHTLKGNPEGwptlVPVGRPLHNVQVYILDEAQQPvplgGEGEFCIGGI---GLARGYHN 418
Cdd:cd17654   263 GNRTRifNIYGITEVSCwALAYKVPEEDSP----VQLGSPLLGTVIEVRDQNGSE----GTGQVFLGGLnrvCILDDEVT 334

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  419 LPdltnekfipnpFGTNenakklYRTGDLARyLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVareI 498
Cdd:cd17654   335 VP-----------KGTM------RATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVT---L 393

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 602182148  499 AGHTQLVGYIIAKDTLNLSFDKLEPILrqyseavLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd17654   394 SDQQRLIAFIVGESSSSRIHKELQLTL-------LSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449

PKS_DH

smart00826

Dehydratase domain in polyketide synthase (PKS) enzymes;

1590-1753

8.83e-38

Dehydratase domain in polyketide synthase (PKS) enzymes;

Pssm-ID: 214837 Cd Length: 167 Bit Score: 140.44 E-value: 8.83e-38

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   1590 HPLLGQRLHLSRTQEIYFQTFIHSDFPIWVADHKVFGNVIIPGVAYFEMALAAGKALKPDSIFWLEDVSIAQALIIPDEG 1669
Cdd:smart00826    1 HPLLGARVELADGGGVVLTGRLSLRTHPWLADHRVGGTVVLPGAAYVELALAAADEVGGGAPARLEELTLEAPLVLPEDG 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   1670 -QTVQIVLS-PQEESAYFFEILSL-EKENSWVLHASGKLVAQEQVLETEPIDLIALQAHCCEEVSVDVLYQEEMARRLDM 1746
Cdd:smart00826   81 aVRVQVVVGaPDEDGRRTFTVYSRpDGDGPWTRHATGTLRPAAAAPAAPAADLAAWPPAGAEPVDVDDLYERLAARGLEY 160


                    ....*..
gi 602182148   1747 GPMMRGV 1753
Cdd:smart00826  161 GPAFQGL 167

EntE

COG1021

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...

25-561

1.31e-36

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: 147.98 E-value: 1.31e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   25 IHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCayVPLD 104
Cdd:COG1021    27 LGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPVF 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  105 VgYPADR---IEYMLRDSDARILLTSTDVAKklaltipalqecqtvyldqeifeydFHFLAIAKLLHNQYLRLLHF---- 177
Cdd:COG1021   105 A-LPAHRraeISHFAEQSEAVAYIIPDRHRG-------------------------FDYRALARELQAEVPSLRHVlvvg 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  178 ---YFYTLiQQCQATSVSqGIQTQVLPNNLAYCIYTSGSTGNPKGILMEH-------RSLVNMLWWHQQTRpsvqgvrtl 247
Cdd:COG1021   159 dagEFTSL-DALLAAPAD-LSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHddylysvRASAEICGLDADTV--------- 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  248 QFCAV----SFDFSCHEIFSTLCLGGILVLVPEAVRQNPFALaefISQQKIEKLFL-PVIALLQLaEAVNGNKST--SLa 320
Cdd:COG1021   228 YLAALpaahNFPLSSPGVLGVLYAGGTVVLAPDPSPDTAFPL---IERERVTVTALvPPLALLWL-DAAERSRYDlsSL- 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  321 lcEVITTGEQmQITPAVANLFQKT-GAMLHNHYGATEF----------QDATTHTlkgnpegwptlvpVGRPL--HNvQV 387
Cdd:COG1021   303 --RVLQVGGA-KLSPELARRVRPAlGCTLQQVFGMAEGlvnytrlddpEEVILTT-------------QGRPIspDD-EV 365

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  388 YILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFgtnenakklYRTGDLARYLPDGTIEHLGRIDHQVk 467
Cdd:COG1021   366 RIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGF---------YRTGDLVRRTPDGYLVVEGRAKDQI- 435

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  468 IRGfrvelGE------IESVLASHQAVRECAVVAREiaghTQLVG-----YIIAKDTlNLSFDKLEPILRqysEAVLPEY 536
Cdd:COG1021   436 NRG-----GEkiaaeeVENLLLAHPAVHDAAVVAMP----DEYLGerscaFVVPRGE-PLTLAELRRFLR---ERGLAAF 502

                         570       580
                  ....*....|....*....|....*
gi 602182148  537 MIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:COG1021   503 KLPDRLEFVDALPLTAVGKIDKKAL 527

PLN02752

[acyl-carrier protein] S-malonyltransferase

1206-1494

1.33e-36

[acyl-carrier protein] S-malonyltransferase

Pssm-ID: 215401 [Multi-domain] Cd Length: 343 Bit Score: 143.36 E-value: 1.33e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1206 PTIAFLFTGQGSQYINMGRTLYDTEstfrAALDRCETILQNLGIESIISVIFGSSEhglSLDDTAYTQPALFAIEYALYQ 1285
Cdd:PLN02752   38 PTTAFLFPGQGAQAVGMGKEAAEVP----AAKALFDKASEILGYDLLDVCVNGPKE---KLDSTVVSQPAIYVASLAAVE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1286 LWKSWGIQPSVV------IGHSVGEYVSACVAGVFSLEDGLKLIAERGRLIQAL--PRDGSMVSV--MASEKrIADIILP 1355
Cdd:PLN02752  111 KLRARDGGQAVIdsvdvcAGLSLGEYTALVFAGALSFEDGLKLVKLRGEAMQAAadAGPSGMVSVigLDSDK-VQELCAA 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1356 YGGQVG------IAAINGPQSVVISGQQQAIDAICAILETEG-IKSKKLNVSHAFHSPLVEAMLDSFLQVAQEVTYSQPQ 1428
Cdd:PLN02752  190 ANEEVGeddvvqIANYLCPGNYAVSGGKKGIDAVEAKAKSFKaRMTVRLAVAGAFHTSFMEPAVDALEAALAAVEIRTPR 269

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 602182148 1429 IKLISNVTGtlASHeSCPDELPITTAeywvRHVRQPVRFAAGMESLEGQGVNVFIEIGPKPVLLGM 1494
Cdd:PLN02752  270 IPVISNVDA--QPH-SDPATIKKILA----RQVTSPVQWETTVKTLLEKGLEKSYELGPGKVIAGI 328

23DHB-AMP_lg

cd05920

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...

27-561

5.58e-34

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: 139.00 E-value: 5.58e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   27 HLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVpldVG 106
Cdd:cd05920    19 DLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPV---LA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  107 YPADRieymLRDSDARIlltstDVAKKLALTIPalqecqtvyldQEIFEYDFHFLAIaKLLHNQylrllhfyfytliqqc 186
Cdd:cd05920    96 LPSHR----RSELSAFC-----AHAEAVAYIVP-----------DRHAGFDHRALAR-ELAESI---------------- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  187 qatsvsqgiqtqvlpNNLAYCIYTSGSTGNPKGILMEHRSLVNMLwwhqqtRPSVQ----GVRTLQFCAVS----FDFSC 258
Cdd:cd05920   139 ---------------PEVALFLLSGGTTGTPKLIPRTHNDYAYNV------RASAEvcglDQDTVYLAVLPaahnFPLAC 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  259 HEIFSTLCLGGILVLVPEAVRQNPFALaefISQQKIEKLFL-PVIALLQLAEAVNGNKS-TSLALCEVitTGEQMQITPA 336
Cdd:cd05920   198 PGVLGTLLAGGRVVLAPDPSPDAAFPL---IEREGVTVTALvPALVSLWLDAAASRRADlSSLRLLQV--GGARLSPALA 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  337 vANLFQKTGAMLHNHYGATEfqDATTHTLKGNPEGwPTLVPVGRPLH-NVQVYILDEAQQPVPLGGEGEFCIGGIGLARG 415
Cdd:cd05920   273 -RRVPPVLGCTLQQVFGMAE--GLLNYTRLDDPDE-VIIHTQGRPMSpDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRG 348

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  416 YHNLPDLTNEKFIPNPFgtnenakklYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVA 495
Cdd:cd05920   349 YYRAPEHNARAFTPDGF---------YRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVA 419

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 602182148  496 --REIAGHTQLVgYIIAKDTlNLSFDKLEPILRqysEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05920   420 mpDELLGERSCA-FVVLRDP-PPSAAQLRRFLR---ERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482

PRK07314

beta-ketoacyl-ACP synthase II;

687-1107

4.06e-33

beta-ketoacyl-ACP synthase II;

Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 134.92 E-value: 4.06e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  687 PGAETIEQFWHNLC---NGVESITLFSDDKLEqtlpelfnnpayVKAGAVLEGvelFDATFFgYSPKEAAVTDPQQRILL 763
Cdd:PRK07314   14 PLGNDVESTWKNLLagkSGIGPITHFDTSDLA------------VKIAGEVKD---FNPDDY-MSRKEARRMDRFIQYGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  764 ECAWEAFERAGYNPETY-PEPVGVYAGSSlstyllnnIGsALGIITEQ-------------PFietdmeqF-QAKIGNdr 828
Cdd:PRK07314   78 AAAKQAVEDAGLEITEEnADRIGVIIGSG--------IG-GLETIEEQhitllekgprrvsPF-------FvPMAIIN-- 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  829 sYLATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGG-------ISVvvpqkGGYLYEEGMVRSQD- 900
Cdd:PRK07314  140 -MAAGHVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGaeaaitpLGI-----AGFAAARALSTRNDd 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  901 --GHCRAFDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDgAIKMgyTAPSVDGQ--ADVISEAIAIAD 976
Cdd:PRK07314  214 peRASRPFDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGD-AYHM--TAPAPDGEgaARAMKLALKDAG 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  977 IDASTIGYVEAHGTATQLGDPIEVAGLARAFQRSTDSVlgkqqcAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPS 1056
Cdd:PRK07314  291 INPEDIDYINAHGTSTPAGDKAETQAIKRVFGEHAYKV------AVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPT 364

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 602182148 1057 LHYANPNPRIDFDATPffvntelrewsrnGYPRRAGV-----SSFGVGGTNSHIVL 1107
Cdd:PRK07314  365 INLDNPDEECDLDYVP-------------NEARERKIdyalsNSFGFGGTNASLVF 407

cond_enzymes

cd00327

Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...

758-1107

8.71e-33

Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.

Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 129.49 E-value: 8.71e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  758 QQRILLECAWEAFERAGYnpeTYPEPVGVYAGSSLSTYLLnnigsalgiiteqpfietdmeqfqakigndrSYLATRISY 837
Cdd:cd00327     7 ASELGFEAAEQAIADAGL---SKGPIVGVIVGTTGGSGEF-------------------------------SGAAGQLAY 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  838 KLNLK-GPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVpqkggylyeegmvrsqdghcrafdaeaqgtiFG 916
Cdd:cd00327    53 HLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEEFV-------------------------------FG 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  917 NGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGAikMGYTAPSVDGQADVISEAIAIADIDASTIGYVEAHGTATQLGD 996
Cdd:cd00327   102 DGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGA--SMVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGD 179

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  997 PIEVAGLarafqrstDSVLGKQQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPslhyanpnpridfdatpffvn 1076
Cdd:cd00327   180 AVELALG--------LDPDGVRSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPP--------------------- 230

                         330       340       350
                  ....*....|....*....|....*....|.
gi 602182148 1077 telrewsRNGYPRRAGVSSFGVGGTNSHIVL 1107
Cdd:cd00327   231 -------TPREPRTVLLLGFGLGGTNAAVVL 254

PTZ00050

3-oxoacyl-acyl carrier protein synthase; Provisional

691-1103

8.76e-33

3-oxoacyl-acyl carrier protein synthase; Provisional

Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 134.05 E-value: 8.76e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  691 TIEQFWHNLCNGVESITLFS--DDKLEQTLPELFNNPAYVkaGAVLEGV------ELFDATFFGYSPKEaavtDPQQRIL 762
Cdd:PTZ00050    8 GAESTWEALIAGKSGIRKLTefPKFLPDCIPEQKALENLV--AAMPCQIaaevdqSEFDPSDFAPTKRE----SRATHFA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  763 LECAWEAFERAG--YNPETYPEPVGVyagsslstyllnNIGSALGIITEqpfIETDMEQFQAK-------------IGND 827
Cdd:PTZ00050   82 MAAAREALADAKldILSEKDQERIGV------------NIGSGIGSLAD---LTDEMKTLYEKghsrvspyfipkiLGNM 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  828 RSYLatrISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGG-------ISVV--------------VPQK 886
Cdd:PTZ00050  147 AAGL---VAIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGteasitpVSFAgfsrmralctkyndDPQR 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  887 GgylyeegmvrsqdghCRAFDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGaikMGYTAPSVDGQAD 966
Cdd:PTZ00050  224 A---------------SRPFDKDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDA---HHITAPHPDGRGA 285

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  967 VISEAIAI---ADIDASTIGYVEAHGTATQLGDPIEVAGLARAFQRSTDsvlgkQQCAIGSVKTNIGHLDEAAGIAGLIK 1043
Cdd:PTZ00050  286 RRCMENALkdgANININDVDYVNAHATSTPIGDKIELKAIKKVFGDSGA-----PKLYVSSTKGGLGHLLGAAGAVESIV 360

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 602182148 1044 AALALQYGQIPPSLHYANPNPRIDFDATPFFVNTELRewsrngyPRRAGVS-SFGVGGTNS 1103
Cdd:PTZ00050  361 TILSLYEQIIPPTINLENPDAECDLNLVQGKTAHPLQ-------SIDAVLStSFGFGGVNT 414

PRK06178

acyl-CoA synthetase; Validated

33-561

1.82e-32

acyl-CoA synthetase; Validated

Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 135.94 E-value: 1.82e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   33 AAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRI 112
Cdd:PRK06178   43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  113 EYMLRDSDARILLTSTDVAKklaLTIPALQECQTvyldQEIFEYDFH-------------FLAIAKLLHNQYLRLLhfyf 179
Cdd:PRK06178  123 SYELNDAGAEVLLALDQLAP---VVEQVRAETSL----RHVIVTSLAdvlpaeptlplpdSLRAPRLAAAGAIDLL---- 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  180 ytliqQCQATSVSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNM-----LWWHQQTRPSVQGVRTLQFCAVSF 254
Cdd:PRK06178  192 -----PALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTaaaayAVAVVGGEDSVFLSFLPEFWIAGE 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  255 DFSCheIFSTLClGGILVLVpeaVRQNPFALAEFISQQKIEKLFLPV---IALLQLAEAVNGNKSTslaLCEVITTGEQM 331
Cdd:PRK06178  267 NFGL--LFPLFS-GATLVLL---ARWDAVAFMAAVERYRVTRTVMLVdnaVELMDHPRFAEYDLSS---LRQVRVVSFVK 337

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  332 QITPAVANLFQK-TGAML-HNHYGATEFQDATTHT---------LKGNPegwptlVPVGRPLHNVQVYILD-EAQQPVPL 399
Cdd:PRK06178  338 KLNPDYRQRWRAlTGSVLaEAAWGMTETHTCDTFTagfqdddfdLLSQP------VFVGLPVPGTEFKICDfETGELLPL 411

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  400 GGEGEFCIGGIGLARGYHNLPDLTNEKFIPNpfgtnenakkLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIE 479
Cdd:PRK06178  412 GAEGEIVVRTPSLLKGYWNKPEATAEALRDG----------WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVE 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  480 SVLASHQAVRECAVVAREIAGHTQL-VGYIIAKDTLNLSfdklEPILRQYSEAVLPEYMIPTRFInISNMPLTPSGKLDR 558
Cdd:PRK06178  482 ALLGQHPAVLGSAVVGRPDPDKGQVpVAFVQLKPGADLT----AAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRK 556


                  ...
gi 602182148  559 RAL 561
Cdd:PRK06178  557 QDL 559

PRK07798

acyl-CoA synthetase; Validated

28-559

2.01e-32

acyl-CoA synthetase; Validated

Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 135.01 E-value: 2.01e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   28 LFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGY 107
Cdd:PRK07798    8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  108 PADRIEYMLRDSDARILLTSTDVAKKLALTIPALQECQtvyldqeifeydfHFLAIAKLLHNQYLRLLHFYfytliqqcq 187
Cdd:PRK07798   88 VEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLPKLR-------------TLVVVEDGSGNDLLPGAVDY--------- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  188 ATSVSQGIQTQVL----PNNLaYCIYTSGSTGNPKGILMEH----RSLVNMLWW---------HQQTRPSVQGVRTLQFC 250
Cdd:PRK07798  146 EDALAAGSPERDFgersPDDL-YLLYTGGTTGMPKGVMWRQedifRVLLGGRDFatgepiedeEELAKRAAAGPGMRRFP 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  251 AVSFdfsCH-----EIFSTLCLGGILVLVPEaVRQNPFALAEFISQQKIEKLFL-------PVIALLQLAEAVNGnksTS 318
Cdd:PRK07798  225 APPL---MHgagqwAAFAALFSGQTVVLLPD-VRFDADEVWRTIEREKVNVITIvgdamarPLLDALEARGPYDL---SS 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  319 LALceVITTGEQMqiTPAVANLFQ--KTGAMLHNHYGATE--FQdATTHTLKGNPEGWPTLVPVGRplhnvQVYILDEAQ 394
Cdd:PRK07798  298 LFA--IASGGALF--SPSVKEALLelLPNVVLTDSIGSSEtgFG-GSGTVAKGAVHTGGPRFTIGP-----RTVVLDEDG 367

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  395 QPVPLGGegefciGGIG-LAR------GYHNLPDLTNEKF---------IPnpfgtnenakklyrtGDLARYLPDGTIEH 458
Cdd:PRK07798  368 NPVEPGS------GEIGwIARrghiplGYYKDPEKTAETFptidgvryaIP---------------GDRARVEADGTITL 426

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  459 LGRiDHQV------KIrgFrVElgEIESVLASHQAVRECAVVAR--EIAGhtQLVGYIIAKDTlNLSFDKLEpiLRQYSE 530
Cdd:PRK07798  427 LGR-GSVCintggeKV--F-PE--EVEEALKAHPDVADALVVGVpdERWG--QEVVAVVQLRE-GARPDLAE--LRAHCR 495

                         570       580
                  ....*....|....*....|....*....
gi 602182148  531 AVLPEYMIPTRFINISNMPLTPSGKLDRR 559
Cdd:PRK07798  496 SSLAGYKVPRAIWFVDEVQRSPAGKADYR 524

FACL_DitJ_like

cd05934

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...

50-562

3.79e-32

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: 132.03 E-value: 3.79e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   50 TYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLTStd 129
Cdd:cd05934     5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD-- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  130 vakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiqtqvlpnnLAYCIY 209
Cdd:cd05934    83 --------------------------------------------------------------------------PASILY 88

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  210 TSGSTGNPKGILMEHRslvNMLWWHQQTRpSVQGVRTLQFCAVSFDFS-----CHEIFSTLCLGGILVLVPEavrqnpFA 284
Cdd:cd05934    89 TSGTTGPPKGVVITHA---NLTFAGYYSA-RRFGLGEDDVYLTVLPLFhinaqAVSVLAALSVGATLVLLPR------FS 158

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  285 LAEFISQqkIEKL------FLPVIALLQLAEAVNGNKSTS---LALCEVITTGEqmqitpaVANLFQKTGAMLHNHYGAT 355
Cdd:cd05934   159 ASRFWSD--VRRYgatvtnYLGAMLSYLLAQPPSPDDRAHrlrAAYGAPNPPEL-------HEEFEERFGVRLLEGYGMT 229

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  356 EfqdaTTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCI---GGIGLARGYHNLPDLTNEKFiPNPF 432
Cdd:cd05934   230 E----TIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIrglRGWGFFKGYYNMPEATAEAM-RNGW 304

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  433 gtnenakklYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVA-REIAGHTQLVGYIIAK 511
Cdd:cd05934   305 ---------FHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAvPDEVGEDEVKAVVVLR 375

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 602182148  512 DTLNLSFDKlepiLRQYSEAVLPEYMIPtRFINI-SNMPLTPSGKLDRRALP 562
Cdd:cd05934   376 PGETLDPEE----LFAFCEGQLAYFKVP-RYIRFvDDLPKTPTEKVAKAQLR 422

PRK06333

beta-ketoacyl-ACP synthase;

692-1107

3.96e-32

beta-ketoacyl-ACP synthase;

Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 132.04 E-value: 3.96e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  692 IEQFWHNLCNGVESITLFSDDKLEQTlpelfnnPAYVkAGAVLEGVELFDAtffGYSPkEAAVTDPQQR-----IL--LE 764
Cdd:PRK06333   21 VETFWQRLLAGQSGIRTLTDFPVGDL-------ATKI-GGQVPDLAEDAEA---GFDP-DRYLDPKDQRkmdrfILfaMA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  765 CAWEAFERAGYNPETYPEPV--GVYAGSSlstyllnnIGsALGIITEQpfIETDMEQfqakiGNDR-------SYL---- 831
Cdd:PRK06333   89 AAKEALAQAGWDPDTLEDRErtATIIGSG--------VG-GFPAIAEA--VRTLDSR-----GPRRlspftipSFLtnma 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  832 ATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQ--KGGYL----YEEGMVRSQDGHCRA 905
Cdd:PRK06333  153 AGHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRvsLAGFAaaraLSTRFNDAPEQASRP 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  906 FDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDgAIKMgyTAPSVDGQ--ADVISEAIAIADIDASTIG 983
Cdd:PRK06333  233 FDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSAD-AYHM--TAGPEDGEgaRRAMLIALRQAGIPPEEVQ 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  984 YVEAHGTATQLGDPIEVAGLARAFqrSTDSVLgkqqcAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPN 1063
Cdd:PRK06333  310 HLNAHATSTPVGDLGEVAAIKKVF--GHVSGL-----AVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPD 382

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 602182148 1064 PRID-FDatpfFVNTELREWSRngypRRAGVSSFGVGGTNSHIVL 1107
Cdd:PRK06333  383 PAAEgLD----VVANKARPMDM----DYALSNGFGFGGVNASILF 419

PRK06188

acyl-CoA synthetase; Validated

34-561

3.35e-31

acyl-CoA synthetase; Validated

Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 131.26 E-value: 3.35e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   34 AKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLD-VGYPADRI 112
Cdd:PRK06188   23 KRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHpLGSLDDHA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  113 eYMLRDSDARILLTS----TDVAKKLALTIPALQECQTVyldqEIFEYDFHFLAIAkllhnqylrllhfyfytliqqcqA 188
Cdd:PRK06188  103 -YVLEDAGISTLIVDpapfVERALALLARVPSLKHVLTL----GPVPDGVDLLAAA-----------------------A 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  189 TSVSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNML------W-WHQQTRPSVqgVRTLQFCAVSFdfscheI 261
Cdd:PRK06188  155 KFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAqiqlaeWeWPADPRFLM--CTPLSHAGGAF------F 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  262 FSTLCLGGILVLVPEAvrqNPFALAEFISQQKIEKLFL-P--VIALLQLAEAVNGNKStSLalcEVITTGEQmQITPA-V 337
Cdd:PRK06188  227 LPTLLRGGTVIVLAKF---DPAEVLRAIEEQRITATFLvPtmIYALLDHPDLRTRDLS-SL---ETVYYGAS-PMSPVrL 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  338 ANLFQKTGAMLHNHYGATEFQDATTHTLKG-----NPEgwpTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGL 412
Cdd:PRK06188  299 AEAIERFGPIFAQYYGQTEAPMVITYLRKRdhdpdDPK---RLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLV 375

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  413 ARGYHNLPDLTNEKFipnpfgtnenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECA 492
Cdd:PRK06188  376 MDGYWNRPEETAEAF----------RDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVA 445

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 602182148  493 V--VAREIAGHTqLVGYIIAKDTLNLSFDKLEPILRQYSEAVlpeyMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:PRK06188  446 VigVPDEKWGEA-VTAVVVLRPGAAVDAAELQAHVKERKGSV----HAPKQVDFVDSLPLTALGKPDKKAL 511

PRK08316

acyl-CoA synthetase; Validated

33-561

3.47e-31

acyl-CoA synthetase; Validated

Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 131.21 E-value: 3.47e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   33 AAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRI 112
Cdd:PRK08316   21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEEL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  113 EYMLRDSDARILLTSTDVAkklALTIPALQECQTVYLDQEIF----EYDFHFLAIAKLLhnqylrllhfyfytliqqcQA 188
Cdd:PRK08316  101 AYILDHSGARAFLVDPALA---PTAEAALALLPVDTLILSLVlggrEAPGGWLDFADWA-------------------EA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  189 TSVSQGiQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVnmlwwHQQTRpsvqgvrtlqfCAVSFDFSCHEIF------ 262
Cdd:PRK08316  159 GSVAEP-DVELADDDLAQILYTSGTESLPKGAMLTHRALI-----AEYVS-----------CIVAGDMSADDIPlhalpl 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  263 -----------STLCLGGILVLVPEAVRQNPFALaefISQQKIEKLFLP--V-IALLQLAEaVNGNKSTSLALC------ 322
Cdd:PRK08316  222 yhcaqldvflgPYLYVGATNVILDAPDPELILRT---IEAERITSFFAPptVwISLLRHPD-FDTRDLSSLRKGyygasi 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  323 ---EVITtgEQMQITPAVAnlfqktgamLHNHYGATEFqdATTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPL 399
Cdd:PRK08316  298 mpvEVLK--ELRERLPGLR---------FYNCYGQTEI--APLATVLGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAP 364

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  400 GGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFgtnenakklyRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIE 479
Cdd:PRK08316  365 GEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWF----------HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVE 434

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  480 SVLASHQAVRECAVVA----REIAGHTQLVgyiIAKDTLNLSFDKLEPILRQYseavLPEYMIPTRFINISNMPLTPSGK 555
Cdd:PRK08316  435 EALYTHPAVAEVAVIGlpdpKWIEAVTAVV---VPKAGATVTEDELIAHCRAR----LAGFKVPKRVIFVDELPRNPSGK 507


                  ....*.
gi 602182148  556 LDRRAL 561
Cdd:PRK08316  508 ILKREL 513

LC_FACS_like

cd05935

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...

48-561

8.22e-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: 128.37 E-value: 8.22e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   48 SLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLTS 127
Cdd:cd05935     1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  128 TDVakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiqtqvlpNNLAYC 207
Cdd:cd05935    81 SEL-----------------------------------------------------------------------DDLALI 89

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  208 IYTSGSTGNPKGILMEHRSL----VNMLWWHQQTrPSVQGVRTLQFCAVSfDFScHEIFSTLCLGGILVLVpeaVRQNPF 283
Cdd:cd05935    90 PYTSGTTGLPKGCMHTHFSAaanaLQSAVWTGLT-PSDVILACLPLFHVT-GFV-GSLNTAVYVGGTYVLM---ARWDRE 163

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  284 ALAEFISQQKIEKLFLPVIALLQLAEAVNgNKSTSLALCEVITTGeQMQITPAVANLFQKTGAMLHNH-YGATEFQdATT 362
Cdd:cd05935   164 TALELIEKYKVTFWTNIPTMLVDLLATPE-FKTRDLSSLKVLTGG-GAPMPPAVAEKLLKLTGLRFVEgYGLTETM-SQT 240

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  363 HTlkgNPEGWPTLVPVGRPLHNVQVYILD-EAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIpnpfgtNENAKKL 441
Cdd:cd05935   241 HT---NPPLRPKLQCLGIP*FGVDARVIDiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFI------EIKGRRF 311

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  442 YRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAR--EIAGHTqLVGYIIAKDTLNLSFD 519
Cdd:cd05935   312 FRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVpdERVGEE-VKAFIVLRPEYRGKVT 390

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 602182148  520 KLEPIlrQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05935   391 EEDII--EWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430

FAA1

COG1022

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];

25-494

8.39e-30

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];

Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 128.29 E-value: 8.39e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   25 IHHLFEDQAAKRPDAIALI----DGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAY 100
Cdd:COG1022    13 LPDLLRRRAARFPDRVALRekedGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVT 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  101 VPLDVGYPADRIEYMLRDSDARILLTST----DVAKKLALTIPALQecQTVYLDQEIFEYDFHFLAIAKLLHNQYLRLLH 176
Cdd:COG1022    93 VPIYPTSSAEEVAYILNDSGAKVLFVEDqeqlDKLLEVRDELPSLR--HIVVLDPRGLRDDPRLLSLDELLALGREVADP 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  177 FYFYTLIQQCQatsvsqgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLqfcavSFDF 256
Cdd:COG1022   171 AELEARRAAVK-------------PDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTL-----SFLP 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  257 SCH--E-IFSTLCL-GGILVLVPEAVRQNPFALAE-----FIS------------QQKIE-------KLFLPVIAL-LQL 307
Cdd:COG1022   233 LAHvfErTVSYYALaAGATVAFAESPDTLAEDLREvkptfMLAvprvwekvyagiQAKAEeagglkrKLFRWALAVgRRY 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  308 AEAVNGNKSTSLAL----------------------CEV-ITTGEQMQitPAVANLFQKTGAMLHNHYGATEfqdaTTHT 364
Cdd:COG1022   313 ARARLAGKSPSLLLrlkhaladklvfsklrealggrLRFaVSGGAALG--PELARFFRALGIPVLEGYGLTE----TSPV 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  365 LKGNPEGWPTLVPVGRPLHNVQVYIldeaqqpvplGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFgtnenakklYRT 444
Cdd:COG1022   387 ITVNRPGDNRIGTVGPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAEAFDADGW---------LHT 447

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 602182148  445 GDLARYLPDGTIEHLGRIDHQVKIR-GFRVELGEIESVLASHQAVRECAVV 494
Cdd:COG1022   448 GDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVV 498

PRK06087

medium-chain fatty-acid--CoA ligase;

31-561

1.02e-29

medium-chain fatty-acid--CoA ligase;

Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 127.17 E-value: 1.02e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   31 DQAAKRPDAIALIDGE-QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPA 109
Cdd:PRK06087   31 QTARAMPDKIAVVDNHgASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWRE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  110 DRIEYMLRDSDARILLTSTDVAK----KLALTI----PALQecQTVYLDQEIFEYDfhFLAIAKLLHNqylrllhfyFYT 181
Cdd:PRK06087  111 AELVWVLNKCQAKMFFAPTLFKQtrpvDLILPLqnqlPQLQ--QIVGVDKLAPATS--SLSLSQIIAD---------YEP 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  182 LIQQCQATSvsqgiqtqvlpNNLAYCIYTSGSTGNPKGILMEHRSLV----------NMLWWHQQTRPSVQGVRTLQFca 251
Cdd:PRK06087  178 LTTAITTHG-----------DELAAVLFTSGTEGLPKGVMLTHNNILaseraycarlNLTWQDVFMMPAPLGHATGFL-- 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  252 vsfdfscHEIFSTLCLGGILVLVPeavRQNPFALAEFISQQKIEKLF--LPVIA-LLQLAEAVNGNKST-SLALCEVITt 327
Cdd:PRK06087  245 -------HGVTAPFLIGARSVLLD---IFTPDACLALLEQQRCTCMLgaTPFIYdLLNLLEKQPADLSAlRFFLCGGTT- 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  328 geqmqITPAVANLFQKTGAMLHNHYGATEfqdATTHTL--KGNPEGWpTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEF 405
Cdd:PRK06087  314 -----IPKKVARECQQRGIKLLSVYGSTE---SSPHAVvnLDDPLSR-FMHTDGYAAAGVEIKVVDEARKTLPPGCEGEE 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  406 CIGGIGLARGYHNLPDLTNEKFipnpfgtneNAKKLYRTGDLARYLPDGTIEHLGRiDHQVKIRGFR-VELGEIESVLAS 484
Cdd:PRK06087  385 ASRGPNVFMGYLDEPELTARAL---------DEEGWYYSGDLCRMDEAGYIKITGR-KKDIIVRGGEnISSREVEDILLQ 454

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 602182148  485 HQAVRECAVVAR--EIAGHtQLVGYIIAKDTLNLSfdKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:PRK06087  455 HPKIHDACVVAMpdERLGE-RSCAYVVLKAPHHSL--TLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530

FACL_like_6

cd05922

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...

57-561

4.95e-29

Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 123.70 E-value: 4.95e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   57 RANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCA----YVPLDVGYPADRIEYMLRDSDARILLTSTDVAK 132
Cdd:cd05922     2 GVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAAD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  133 KLALTIPALQECQTVYLDQEIfeydfhflaiaklLHNQYLRLLHfyfytliqqcqatsvsqgiqtQVLPNNLAYCIYTSG 212
Cdd:cd05922    82 RLRDALPASPDPGTVLDADGI-------------RAARASAPAH---------------------EVSHEDLALLLYTSG 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  213 STGNPKGILMEHRSLVnmlwWHQQTRPSVQGV----RTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRqnPFALAEF 288
Cdd:cd05922   128 STGSPKLVRLSHQNLL----ANARSIAEYLGItaddRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVL--DDAFWED 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  289 ISQQKIEKlFLPVIALLQLAEAVnGNKSTSLALCEVIT-TGEQMqitPAV-----ANLFQktGAMLHNHYGATE-FQDAT 361
Cdd:cd05922   202 LREHGATG-LAGVPSTYAMLTRL-GFDPAKLPSLRYLTqAGGRL---PQEtiarlRELLP--GAQVYVMYGQTEaTRRMT 274

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  362 T---HTLKGNPEGwptlvpVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPdltneKFIPNPFGTNEna 438
Cdd:cd05922   275 YlppERILEKPGS------IGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDP-----PYRRKEGRGGG-- 341

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  439 kkLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLVGYIIAKDTLNLSf 518
Cdd:cd05922   342 --VLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLALFVTAPDKIDPK- 418

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 602182148  519 dklePILRQYSEaVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05922   419 ----DVLRSLAE-RLPPYKVPATVRVVDELPLTASGKVDYAAL 456

PRK07910

beta-ketoacyl-ACP synthase;

676-1107

1.07e-28

beta-ketoacyl-ACP synthase;

Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 121.76 E-value: 1.07e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  676 DIAIISVAGRFPGAETIEQFWHNLCNGVESITLFSDDKLEQtlpelFNNPayVKAGAVLegVELFDAtffGYSPKEAAVT 755
Cdd:PRK07910   13 NVVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDDPFVEE-----FDLP--VRIGGHL--LEEFDH---QLTRVELRRM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  756 DPQQRILLECAWEAFERAGyNPETYPEPVGVyagsslstyllnNIGSALGIITEQPFIETDMEQFQAKIGNDRS---YL- 831
Cdd:PRK07910   81 SYLQRMSTVLGRRVWENAG-SPEVDTNRLMV------------SIGTGLGSAEELVFAYDDMRARGLRAVSPLAvqmYMp 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  832 ---ATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISV---VVPQKGGYLYEEGMVRSQD---GH 902
Cdd:PRK07910  148 ngpAAAVGLERHAKAGVITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETrieAVPIAGFAQMRIVMSTNNDdpaGA 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  903 CRAFDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGaikMGYTAPSVDGQ--ADVISEAIAIADIDAS 980
Cdd:PRK07910  228 CRPFDKDRDGFVFGEGGALMVIETEEHAKARGANILARIMGASITSDG---FHMVAPDPNGEraGHAMTRAIELAGLTPG 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  981 TIGYVEAHGTATQLGDPIEvaglARAFQRStdsvLGKQQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYA 1060
Cdd:PRK07910  305 DIDHVNAHATGTSVGDVAE----GKAINNA----LGGHRPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLE 376

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 602182148 1061 NPNPRIDFDAtpffVNTElrewSRNGYPRRAGVSSFGVGGTNSHIVL 1107
Cdd:PRK07910  377 NLDPEIDLDV----VAGE----PRPGNYRYAINNSFGFGGHNVALAF 415

MACS_like_2

cd05973

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...

49-561

1.64e-28

Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 121.47 E-value: 1.64e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   49 LTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLTst 128
Cdd:cd05973     1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  129 DVAKKlaltipalqecqtvyldqeifeydfHFLAIAKLLHnqylrllhfyfytliqqcqatsvsqgiqtqvlpnnlaycI 208
Cdd:cd05973    79 DAANR-------------------------HKLDSDPFVM---------------------------------------M 94

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  209 YTSGSTGNPKGILMEHRSLvnmLWWHQQTRPSVqGVR--TLQFCAVSFDFSC---HEIFSTLCLGgilvlVPEAVRQNPF 283
Cdd:cd05973    95 FTSGTTGLPKGVPVPLRAL---AAFGAYLRDAV-DLRpeDSFWNAADPGWAYglyYAITGPLALG-----HPTILLEGGF 165

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  284 ALAefISQQKIEKLFL------PVIALLQLAEAVNGNKSTSLALCEVITTGEQMqiTPAVANLFQKT-GAMLHNHYGATE 356
Cdd:cd05973   166 SVE--STWRVIERLGVtnlagsPTAYRLLMAAGAEVPARPKGRLRRVSSAGEPL--TPEVIRWFDAAlGVPIHDHYGQTE 241

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  357 F------QDATTHTLKgnpEGwptlvPVGRPLHNVQVYILDEAQQPVplgGEGEFCIGGIGLAR-------GYHNLPDlt 423
Cdd:cd05973   242 LgmvlanHHALEHPVH---AG-----SAGRAMPGWRVAVLDDDGDEL---GPGEPGRLAIDIANsplmwfrGYQLPDT-- 308

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  424 nekfiPNPFGtnenakKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQ 503
Cdd:cd05973   309 -----PAIDG------GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTE 377

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 602182148  504 LV-GYIIAKDTLNLSFDkLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05973   378 VVkAFVVLRGGHEGTPA-LADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLL 435

4CL

cd05904

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...

33-500

4.47e-28

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: 121.57 E-value: 4.47e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   33 AAKRPDAIALIDGE--QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPAD 110
Cdd:cd05904    15 ASAHPSRPALIDAAtgRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  111 RIEYMLRDSDARILLTSTDVAKKLA-LTIPalqecqTVYLDqeifEYDFHFLAiakllhnqylrllhfyFYTLIQQCQAT 189
Cdd:cd05904    95 EIAKQVKDSGAKLAFTTAELAEKLAsLALP------VVLLD----SAEFDSLS----------------FSDLLFEADEA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  190 SVSQgiqTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLwwhQQTRPSVQGVRTLQ---FCAVSFdfsCHeIFS--- 263
Cdd:cd05904   149 EPPV---VVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMV---AQFVAGEGSNSDSEdvfLCVLPM---FH-IYGlss 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  264 ----TLCLGGILVLVPEavrqnpFALAEFISQ-QKIEKLFLPVIA--LLQLAEAVNGNKSTSLALcEVITTGE---QMQI 333
Cdd:cd05904   219 falgLLRLGATVVVMPR------FDLEELLAAiERYKVTHLPVVPpiVLALVKSPIVDKYDLSSL-RQIMSGAaplGKEL 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  334 TPAVANLFQKtgAMLHNHYGATEFQDATTHTLkgNPEGWPT-LVPVGRPLHNVQVYILD-EAQQPVPLGGEGEFCIGGIG 411
Cdd:cd05904   292 IEAFRAKFPN--VDLGQGYGMTESTGVVAMCF--APEKDRAkYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPS 367

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  412 LARGYHNLPDLTNEKFIPNPFgtnenakklYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVREC 491
Cdd:cd05904   368 IMKGYLNNPEATAATIDKEGW---------LHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDA 438

                         490
                  ....*....|.
gi 602182148  492 AVVAR--EIAG 500
Cdd:cd05904   439 AVIPYpdEEAG 449

PRK06164

acyl-CoA synthetase; Validated

28-554

6.62e-28

acyl-CoA synthetase; Validated

Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 121.39 E-value: 6.62e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   28 LFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGY 107
Cdd:PRK06164   15 LLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRY 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  108 PADRIEYMLRDSDARILLT-----STDVAKKLALTIPAlqECQTVyldQEIFEYDFHFLAIAKllhnqylRLLHFYFYTL 182
Cdd:PRK06164   95 RSHEVAHILGRGRARWLVVwpgfkGIDFAAILAAVPPD--ALPPL---RAIAVVDDAADATPA-------PAPGARVQLF 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  183 IQQCQATSVSQGIQTQVlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTL---QFCAVsFDFSch 259
Cdd:PRK06164  163 ALPDPAPPAAAGERAAD-PDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLaalPFCGV-FGFS-- 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  260 EIFSTLCLGGILVLVP--EAVRQnpfalAEFISQQKIEKLFLPVIALLQLAEAVNGNKS-TSLALCEVITtgeqmqITPA 336
Cdd:PRK06164  239 TLLGALAGGAPLVCEPvfDAART-----ARALRRHRVTHTFGNDEMLRRILDTAGERADfPSARLFGFAS------FAPA 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  337 VANLFQKT---GAMLHNHYGATEFQDATThtlkgnpeGWPTLVPV-------GRPLH-NVQVYILDEAQQPV-PLGGEGE 404
Cdd:PRK06164  308 LGELAALArarGVPLTGLYGSSEVQALVA--------LQPATDPVsvrieggGRPASpEARVRARDPQDGALlPDGESGE 379

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  405 FCIGGIGLARGYHNLPDLTNEKFIPNPFgtnenakklYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLAS 484
Cdd:PRK06164  380 IEIRAPSLMRGYLDNPDATARALTDDGY---------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEA 450

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  485 HQAVRECAVVAREIAGHTQLVGYIIAKDTLNLSfdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPSG 554
Cdd:PRK06164  451 LPGVAAAQVVGATRDGKTVPVAFVIPTDGASPD----EAGLMAACREALAGFKVPARVQVVEAFPVTESA 516

PRK06839

o-succinylbenzoate--CoA ligase;

25-568

6.86e-28

o-succinylbenzoate--CoA ligase;

Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 120.74 E-value: 6.86e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   25 IHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLL-SLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPL 103
Cdd:PRK06839    4 IAYWIEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  104 DVGYPADRIEYMLRDSDARILLtstdVAKKLALTIPALQECQTVYldqeifeydfHFLAIAKLlhnqylrllhfyfytli 183
Cdd:PRK06839   84 NIRLTENELIFQLKDSGTTVLF----VEKTFQNMALSMQKVSYVQ----------RVISITSL----------------- 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  184 qqcqATSVSQGIQTQVLPNNLAYCI--YTSGSTGNPKGILMEHrslVNMLWwhqqtrPSVQGVRTLqfcavsfDFSCHEI 261
Cdd:PRK06839  133 ----KEIEDRKIDNFVEKNESASFIicYTSGTTGKPKGAVLTQ---ENMFW------NALNNTFAI-------DLTMHDR 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  262 -----------------FSTLCLGGILVlVPEavRQNPFALAEFISQQKIEKLF-LPVI--ALLQLAEAVngnkSTSLAL 321
Cdd:PRK06839  193 sivllplfhiggiglfaFPTLFAGGVII-VPR--KFEPTKALSMIEKHKVTVVMgVPTIhqALINCSKFE----TTNLQS 265

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  322 CEVITTGEQMQITPAVANlFQKTGAMLHNHYGATEFQDATTHTLKGNPEGWPTlvPVGRPLHNVQVYILDEAQQPVPLGG 401
Cdd:PRK06839  266 VRWFYNGGAPCPEELMRE-FIDRGFLFGQGFGMTETSPTVFMLSEEDARRKVG--SIGKPVLFCDYELIDENKNKVEVGE 342

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  402 EGEFCIGGIGLARGYHNLPDLTNEKfIPNPFgtnenakklYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESV 481
Cdd:PRK06839  343 VGELLIRGPNVMKEYWNRPDATEET-IQDGW---------LCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQV 412

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  482 LASHQAVRECAVVAR------EIAghtqlVGYIIAKDTLNLSfdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGK 555
Cdd:PRK06839  413 INKLSDVYEVAVVGRqhvkwgEIP-----IAFIVKKSSSVLI----EKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGK 483

                         570
                  ....*....|...
gi 602182148  556 LDRRALPDPKGDR 568
Cdd:PRK06839  484 IQKAQLVNQLKSR 496

AAS_C

cd05909

C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...

48-561

7.51e-28

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: 120.51 E-value: 7.51e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   48 SLTYGELNVRANHLAQhLLSLGCQPDDLLAICIERSAELFIGLLGILKAGcaYVPLDVGYPA--DRIEYMLRDSDARILL 125
Cdd:cd05909     7 SLTYRKLLTGAIALAR-KLAKMTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTAglRELRACIKLAGIKTVL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  126 TSTDVAKKLALT--IPALQECQTVYLDQ---EIFEYDFHFLAIAKLLHNQYLRLLHFyfytliqqcqatsvsqgiQTQVL 200
Cdd:cd05909    84 TSKQFIEKLKLHhlFDVEYDARIVYLEDlraKISKADKCKAFLAGKFPPKWLLRIFG------------------VAPVQ 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  201 PNNLAYCIYTSGSTGNPKGILMEHRSLVNMLwwhQQTRPSVQGVRTLQFCAV-----SFDF-SCheIFSTLCLGGILVLV 274
Cdd:cd05909   146 PDDPAVILFTSGSEGLPKGVVLSHKNLLANV---EQITAIFDPNPEDVVFGAlpffhSFGLtGC--LWLPLLSGIKVVFH 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  275 PEAVrqNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALceVITTGEQMQitPAVANLFQKT-GAMLHNHYG 353
Cdd:cd05909   221 PNPL--DYKKIPELIYDKKATILLGTPTFLRGYARAAHPEDFSSLRL--VVAGAEKLK--DTLRQEFQEKfGIRILEGYG 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  354 ATEFQDATTHTLK--GNPEGwptlvPVGRPLHNVQVYILD-EAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFipn 430
Cdd:cd05909   295 TTECSPVISVNTPqsPNKEG-----TVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF--- 366

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  431 pfgtnenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAV-RECAVVAREIAGHTQLVgyII 509
Cdd:cd05909   367 -------GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEdNEVAVVSVPDGRKGEKI--VL 437

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 602182148  510 AKDTLNLSFDKLEPILRqysEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05909   438 LTTTTDTDPSSLNDILK---NAGISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486

PRK08314

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

21-495

7.82e-28

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

Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 121.22 E-value: 7.82e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   21 PDSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLS-LGCQPDDLLAICIERSAELFIGLLGILKAGCA 99
Cdd:PRK08314    8 PETSLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  100 YVPLDVGYPADRIEYMLRDSDARILLTSTDVAKKLAltiPALQECQ---------TVYLDQEiFEYDFH-FLAIAKLLHN 169
Cdd:PRK08314   88 VVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVA---PAVGNLRlrhvivaqySDYLPAE-PEIAVPaWLRAEPPLQA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  170 QYLRLLHFYFYTLIQQCQATSVSQGiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSL----VNMLWWHQQTRPSVqGVR 245
Cdd:PRK08314  164 LAPGGVVAWKEALAAGLAPPPHTAG------PDDLAVLPYTSGTTGVPKGCMHTHRTVmanaVGSVLWSNSTPESV-VLA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  246 TLQFCAVS-FDFSCHeifSTLCLGGILVLVPEAVRQnpfALAEFISQQK-----------IEKLFLPVIALLQLAeavng 313
Cdd:PRK08314  237 VLPLFHVTgMVHSMN---APIYAGATVVLMPRWDRE---AAARLIERYRvthwtniptmvVDFLASPGLAERDLS----- 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  314 nkstSLALceviTTGEQMQITPAVAN-LFQKTGAMLHNHYGATEfQDATTHTlkgNPEGWPTLVPVGRPLHNVQVYILD- 391
Cdd:PRK08314  306 ----SLRY----IGGGGAAMPEAVAErLKELTGLDYVEGYGLTE-TMAQTHS---NPPDRPKLQCLGIPTFGVDARVIDp 373

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  392 EAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIpnpfgtnE-NAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRG 470
Cdd:PRK08314  374 ETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFI-------EiDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASG 446

                         490       500
                  ....*....|....*....|....*
gi 602182148  471 FRVELGEIESVLASHQAVRECAVVA 495
Cdd:PRK08314  447 FKVWPAEVENLLYKHPAIQEACVIA 471

PRK07103

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated

829-1108

4.63e-27

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated

Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 116.67 E-value: 4.63e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  829 SYLATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALA-GGISVVVPQKGGYLYEEGMVRSQ------DG 901
Cdd:PRK07103  144 TDLVGLCSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAvGALMDLSYWECQALRSLGAMGSDrfadepEA 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  902 HCRAFDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGAikmGYTAPSVDGQADVISEAIAIADIDAST 981
Cdd:PRK07103  224 ACRPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDAN---RGPDPSLEGEMRVIRAALRRAGLGPED 300

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  982 IGYVEAHGTATQLGDPIEVAGLARAfqrstdsvlGKQQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYAN 1061
Cdd:PRK07103  301 IDYVNPHGTGSPLGDETELAALFAS---------GLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDE 371

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 602182148 1062 P-NPRIDFdatpffvnteLREWSRNGYPRRAGVSSFGVGGTNSHIVLE 1108
Cdd:PRK07103  372 PiDERFRW----------VGSTAESARIRYALSLSFGFGGINTALVLE 409

PRK05677

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

19-563

5.90e-27

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

Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 118.71 E-value: 5.90e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   19 EFPDscIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSL-GCQPDDLLAICIERSAELFIGLLGILKAG 97
Cdd:PRK05677   22 EYPN--IQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   98 CAYVPLDVGYPADRIEYMLRDSDARILLTSTDVAKKLALTIPALQECQTVYldQEIfeYDFHfLAIAKLLHNQYLRLLHF 177
Cdd:PRK05677  100 LIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAEKVLPKTGVKHVIV--TEV--ADML-PPLKRLLINAVVKHVKK 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  178 YF--YTLIQQCQATSV-SQGIQTQVLP-----NNLAYCIYTSGSTGNPKGILMEHRSLV-NMLwwhqQTRPSVqGVRTLQ 248
Cdd:PRK05677  175 MVpaYHLPQAVKFNDAlAKGAGQPVTEanpqaDDVAVLQYTGGTTGVAKGAMLTHRNLVaNML----QCRALM-GSNLNE 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  249 FCAV-----------SFDFSCheiFSTLCLGGILVLVPeavrqNPFALAEFISQQKIEKlFLPVIALLQLAEAVNGNKS- 316
Cdd:PRK05677  250 GCEIliaplplyhiyAFTFHC---MAMMLIGNHNILIS-----NPRDLPAMVKELGKWK-FSGFVGLNTLFVALCNNEAf 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  317 -----TSLALceviTTGEQMQITPAVANLFQK-TGAMLHNHYGATEfqdaTTHTLKGNPEGWPTLVPVGRPLHNVQVYIL 390
Cdd:PRK05677  321 rkldfSALKL----TLSGGMALQLATAERWKEvTGCAICEGYGMTE----TSPVVSVNPSQAIQVGTIGIPVPSTLCKVI 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  391 DEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFipnpfgtneNAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRG 470
Cdd:PRK05677  393 DDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEIL---------DSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSG 463

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  471 FRVELGEIESVLASHQAVRECAV--VAREIAGHTQLVgYIIAKDTLNLSFDKlepiLRQYSEAVLPEYMIPTRFINISNM 548
Cdd:PRK05677  464 FNVYPNELEDVLAALPGVLQCAAigVPDEKSGEAIKV-FVVVKPGETLTKEQ----VMEHMRANLTGYKVPKAVEFRDEL 538

                         570
                  ....*....|....*
gi 602182148  549 PLTPSGKLDRRALPD 563
Cdd:PRK05677  539 PTTNVGKILRRELRD 553

CHC_CoA_lg

cd05903

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...

48-556

7.07e-27

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: 116.71 E-value: 7.07e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   48 SLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLTs 127
Cdd:cd05903     1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  128 tdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqaTSVSQGIQTQVLPNNLAYC 207
Cdd:cd05903    80 -------------------------------------------------------------PERFRQFDPAAMPDAVALL 98

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  208 IYTSGSTGNPKGILMEHRSLVNMLwwHQQTRPSVQGVRTLQFCAVS---FDFSCHEIFSTLCLGGILVLVPeavRQNPFA 284
Cdd:cd05903    99 LFTSGTTGEPKGVMHSHNTLSASI--RQYAERLGLGPGDVFLVASPmahQTGFVYGFTLPLLLGAPVVLQD---IWDPDK 173

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  285 LAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALCEVITTGEQmqITPAVA-NLFQKTGAMLHNHYGATEFQDATTH 363
Cdd:cd05903   174 ALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGAT--VPRSLArRAAELLGAKVCSAYGSTECPGAVTS 251

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  364 TLKGNPEgwPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFipnPFGtnenakkLYR 443
Cdd:cd05903   252 ITPAPED--RRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAA---PEG-------WFR 319

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  444 TGDLARYLPDGTIEHLGRiDHQVKIR-GFRVELGEIESVLASHQAVRECAVVA--REIAGHtQLVGYIIAKDTLNLSFDK 520
Cdd:cd05903   320 TGDLARLDEDGYLRITGR-SKDIIIRgGENIPVLEVEDLLLGHPGVIEAAVVAlpDERLGE-RACAVVVTKSGALLTFDE 397

                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 602182148  521 lepiLRQYSEAV-LPEYMIPTRFINISNMPLTPSGKL 556
Cdd:cd05903   398 ----LVAYLDRQgVAKQYWPERLVHVDDLPRTPSGKV 430

VL_LC_FACS_like

cd05907

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...

44-561

8.45e-27

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: 116.93 E-value: 8.45e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   44 DGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLdvgYP---ADRIEYMLRDSD 120
Cdd:cd05907     1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPI---YPtssAEQIAYILNDSE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  121 ARILLTSTdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiqtqvl 200
Cdd:cd05907    78 AKALFVED------------------------------------------------------------------------ 85

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  201 PNNLAYCIYTSGSTGNPKGILMEHRslvNMLWwhqQTRPSVQGVRTLQFCA-VSFDFSCH--E----IFSTLCLGGILVL 273
Cdd:cd05907    86 PDDLATIIYTSGTTGRPKGVMLSHR---NILS---NALALAERLPATEGDRhLSFLPLAHvfErragLYVPLLAGARIYF 159

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  274 VP--EAVRQNpfaLAEFISQQKI------EKLFLPViallqLAEAVNGNKSTSLAL-----CEVITTGEQmQITPAVANL 340
Cdd:cd05907   160 ASsaETLLDD---LSEVRPTVFLavprvwEKVYAAI-----KVKAVPGLKRKLFDLavggrLRFAASGGA-PLPAELLHF 230

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  341 FQKTGAMLHNHYGATEfqdaTTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEaqqpvplggeGEFCIGGIGLARGYHNLP 420
Cdd:cd05907   231 FRALGIPVYEGYGLTE----TSAVVTLNPPGDNRIGTVGKPLPGVEVRIADD----------GEILVRGPNVMLGYYKNP 296

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  421 DLTNEKFIPNPFgtnenakklYRTGDLARYLPDGTIEHLGRI-DHQVKIRGFRVELGEIESVLASHQAVRECAVVAR--- 496
Cdd:cd05907   297 EATAEALDADGW---------LHTGDLGEIDEDGFLHITGRKkDLIITSGGKNISPEPIENALKASPLISQAVVIGDgrp 367

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  497 ----------EIAGHTQLVGYIIAKDTLNLSFDK-LEPILRQYSEAV---LPEYMIPTRFI------NISNMPLTPSGKL 556
Cdd:cd05907   368 flvalivpdpEALEAWAEEHGIAYTDVAELAANPaVRAEIEAAVEAAnarLSRYEQIKKFLllpepfTIENGELTPTLKL 447


                  ....*
gi 602182148  557 DRRAL 561
Cdd:cd05907   448 KRPVI 452

MACS_like_4

cd05969

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...

49-561

8.61e-27

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: 116.45 E-value: 8.61e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   49 LTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLTST 128
Cdd:cd05969     1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  129 DVAKKLAltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiqtqvlPNNLAYCI 208
Cdd:cd05969    81 ELYERTD-----------------------------------------------------------------PEDPTLLH 95

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  209 YTSGSTGNPKGILMEHRSLVNmlwwHQQTRPSVQGVRT--LQFCAVSFDF---SCHEIFSTLcLGGILVLVPEAvRQNPF 283
Cdd:cd05969    96 YTSGTTGTPKGVLHVHDAMIF----YYFTGKYVLDLHPddIYWCTADPGWvtgTVYGIWAPW-LNGVTNVVYEG-RFDAE 169

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  284 ALAEFISQQKIEKLFLPVIALLQL----AEAVNGNKSTSLALceVITTGEQMQiTPAVANLFQKTGAMLHNHYGATEfqd 359
Cdd:cd05969   170 SWYGIIERVKVTVWYTAPTAIRMLmkegDELARKYDLSSLRF--IHSVGEPLN-PEAIRWGMEVFGVPIHDTWWQTE--- 243

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  360 aTTHTLKGNPEGWPTLV-PVGRPLHNVQVYILDEAQQPVPLGGEGEFCI--GGIGLARGYHNLPDLTNEKFIPNpfgtne 436
Cdd:cd05969   244 -TGSIMIANYPCMPIKPgSMGKPLPGVKAAVVDENGNELPPGTKGILALkpGWPSMFRGIWNDEERYKNSFIDG------ 316

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  437 nakkLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREiaghTQLVGYII-AKDTLN 515
Cdd:cd05969   317 ----WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKP----DPLRGEIIkAFISLK 388

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 602182148  516 LSF---DKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05969   389 EGFepsDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVL 437

CBAL

cd05923

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...

33-561

1.05e-26

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: 117.22 E-value: 1.05e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   33 AAKRPDAIALIDGEQS--LTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPAD 110
Cdd:cd05923    11 ASRAPDACAIADPARGlrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  111 RIEYMLRDSDARILLTSTDvakklALTIPALqecqtvyldqeifeydfhFLAIAKLLhnqylrllhfYFYTLIQQCQATS 190
Cdd:cd05923    91 ELAELIERGEMTAAVIAVD-----AQVMDAI------------------FQSGVRVL----------ALSDLVGLGEPES 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  191 VSQGIQT-QVLPNNLAYCIYTSGSTGNPKGILMEHRslvnmlwwHQQTR----PSVQGVR---------------TLQFC 250
Cdd:cd05923   138 AGPLIEDpPREPEQPAFVFYTSGTTGLPKGAVIPQR--------AAESRvlfmSTQAGLRhgrhnvvlglmplyhVIGFF 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  251 AVsfdfscheIFSTLCLGGILVLVPEAVRQNPFALaefISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALCEVITTGEQ 330
Cdd:cd05923   210 AV--------LVAALALDGTYVVVEEFDPADALKL---IEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGAT 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  331 MQiTPAVANLFQKTGAMLHNHYGATEfqdATTHTLKGNP-EGwptlvPVGRPLHNVQVY---ILDEAQQPVPLGGEGEFC 406
Cdd:cd05923   279 MP-DAVLERVNQHLPGEKVNIYGTTE---AMNSLYMRDArTG-----TEMRPGFFSEVRivrIGGSPDEALANGEEGELI 349

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  407 IGGIGLA--RGYHNLPDLTnekfipnpfgtnenAKKL----YRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIES 480
Cdd:cd05923   350 VAAAADAafTGYLNQPEAT--------------AKKLqdgwYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIER 415

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  481 VLASHQAVRECAV--VAREIAGhtQLVGYIIAKDTLNLSFDKLEPILRQySEavLPEYMIPTRFINISNMPLTPSGKLDR 558
Cdd:cd05923   416 VLSRHPGVTEVVVigVADERWG--QSVTACVVPREGTLSADELDQFCRA-SE--LADFKRPRRYFFLDELPKNAMNKVLR 490


                  ...
gi 602182148  559 RAL 561
Cdd:cd05923   491 RQL 493

PRK07059

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

27-565

1.12e-26

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

Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 117.81 E-value: 1.12e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   27 HLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVG 106
Cdd:PRK07059   27 DLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  107 YPADRIEYMLRDSDARILLTSTDVAKKLALTIPALQECQTVYLDQEifeydfHFLAIAKLLHNQYLRLL----------- 175
Cdd:PRK07059  107 YTPRELEHQLKDSGAEAIVVLENFATTVQQVLAKTAVKHVVVASMG------DLLGFKGHIVNFVVRRVkkmvpawslpg 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  176 HFYFYTLIQQCQATSVSQgiqTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLV-NMLW---WHQ---QTRPSVQGVRTLq 248
Cdd:PRK07059  181 HVRFNDALAEGARQTFKP---VKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVaNVLQmeaWLQpafEKKPRPDQLNFV- 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  249 fCAVSFdfscHEIFS-TLC------LGGILVLVPeavrqNPFALAEFISQQKIEKlFLPVIALLQLAEAV-NGNKSTSLA 320
Cdd:PRK07059  257 -CALPL----YHIFAlTVCgllgmrTGGRNILIP-----NPRDIPGFIKELKKYQ-VHIFPAVNTLYNALlNNPDFDKLD 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  321 LCEVITT-GEQMQITPAVAN-LFQKTGAMLHNHYGATEfqdaTTHTLKGNPEGWPTLV-PVGRPLHNVQVYILDEAQQPV 397
Cdd:PRK07059  326 FSKLIVAnGGGMAVQRPVAErWLEMTGCPITEGYGLSE----TSPVATCNPVDATEFSgTIGLPLPSTEVSIRDDDGNDL 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  398 PLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFgtnenakklYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGE 477
Cdd:PRK07059  402 PLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF---------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNE 472

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  478 IESVLASHQAVRECAVVAREIAGHTQLVGYIIAKDTLNLSfdklEPILRQYSEAVLPEYMIPtRFINISN-MPLTPSGKL 556
Cdd:PRK07059  473 IEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKDPALT----EEDVKAFCKERLTNYKRP-KFVEFRTeLPKTNVGKI 547


                  ....*....
gi 602182148  557 DRRALPDPK 565
Cdd:PRK07059  548 LRRELRDGK 556

FAAL

cd05931

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...

31-560

4.88e-26

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: 115.80 E-value: 4.88e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   31 DQAAKRPDAIALI------DGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICiERSAELFIGLLGILKAGCAYVPLd 104
Cdd:cd05931     1 RRAAARPDRPAYTflddegGREETLTYAELDRRARAIAARLQAVGKPGDRVLLLA-PPGLDFVAAFLGCLYAGAIAVPL- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  105 vgYP------ADRIEYMLRDSDARILLTSTDVAKKLAltipalqecqtvyldqEIFEYDFHFLAIAKLLHNQYLrllhfy 178
Cdd:cd05931    79 --PPptpgrhAERLAAILADAGPRVVLTTAAALAAVR----------------AFAASRPAAGTPRLLVVDLLP------ 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  179 fytliqqcqATSVSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWwhqqtrpsvQGVRTLQFCA----VSF 254
Cdd:cd05931   135 ---------DTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVR---------QIRRAYGLDPgdvvVSW 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  255 -----DFSCHE-IFSTLCLGGILVLV-PEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLAL--CEVI 325
Cdd:cd05931   197 lplyhDMGLIGgLLTPLYSGGPSVLMsPAAFLRRPLRWLRLISRYRATISAAPNFAYDLCVRRVRDEDLEGLDLssWRVA 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  326 TTGEQMqITPAVANLFQKTGA-------MLHNHYG---ATEF-------QDATTHTL------------KGNPEGWPTLV 376
Cdd:cd05931   277 LNGAEP-VRPATLRRFAEAFApfgfrpeAFRPSYGlaeATLFvsggppgTGPVVLRVdrdalagravavAADDPAARELV 355

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  377 PVGRPLHNVQVYILDEA-QQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNpfgTNENAKKLYRTGDLArYLPDGT 455
Cdd:cd05931   356 SCGRPLPDQEVRIVDPEtGRELPDGEVGEIWVRGPSVASGYWGRPEATAETFGAL---AATDEGGWLRTGDLG-FLHDGE 431

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  456 IEHLGRIDHQVKIRGFRVELGEIE-SVLASHQAVRECAVVAREIAGHTQLVGYIIAKDTLNLSFDKLEPILRQYSEAVLP 534
Cdd:cd05931   432 LYITGRLKDLIIVRGRNHYPQDIEaTAEEAHPALRPGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAR 511

                         570       580
                  ....*....|....*....|....*....
gi 602182148  535 EYMIPTR---FINISNMPLTPSGKLDRRA 560
Cdd:cd05931   512 EHGVAPAdvvLVRPGSIPRTSSGKIQRRA 540

PRK12583

acyl-CoA synthetase; Provisional

22-558

5.93e-26

acyl-CoA synthetase; Provisional

Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 115.64 E-value: 5.93e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   22 DSCIHHLFEDQAAKRPDAIALIDGEQSL--TYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCA 99
Cdd:PRK12583   17 TQTIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  100 YVPLDVGYPADRIEYMLRDSDARILLT-----STDVAKKLALTIPALQECQTVYLdqeifeydfhflAIAKLLHNQYLRL 174
Cdd:PRK12583   97 LVNINPAYRASELEYALGQSGVRWVICadafkTSDYHAMLQELLPGLAEGQPGAL------------ACERLPELRGVVS 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  175 L------HFYFYTLIQQcQATSVSQG----IQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQtrpSVQGV 244
Cdd:PRK12583  165 LapapppGFLAWHELQA-RGETVSREalaeRQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAE---SLGLT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  245 RTLQFCA-VSFdFSCH-EIFSTL-CL--GGILVLVPEAVrqNPFALAEFISQQKIEKLF-LPVIALLQLAEAVNGNKSTS 318
Cdd:PRK12583  241 EHDRLCVpVPL-YHCFgMVLANLgCMtvGACLVYPNEAF--DPLATLQAVEEERCTALYgVPTMFIAELDHPQRGNFDLS 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  319 lalceVITTGeQMQITPAVANLFQKTGAMLHNH-----YGATE-----FQDATTHTLKGNPEgwptlvPVGRPLHNVQVY 388
Cdd:PRK12583  318 -----SLRTG-IMAGAPCPIEVMRRVMDEMHMAevqiaYGMTEtspvsLQTTAADDLERRVE------TVGRTQPHLEVK 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  389 ILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFipnpfgtneNAKKLYRTGDLARYLPDGTIEHLGRIDHQVkI 468
Cdd:PRK12583  386 VVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESI---------DEDGWMHTGDLATMDEQGYVRIVGRSKDMI-I 455

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  469 RGFR-VELGEIESVLASHQAVRECAV--VAREIAGHtQLVGYIIAKDTLNLSFDKlepiLRQYSEAVLPEYMIPTRFINI 545
Cdd:PRK12583  456 RGGEnIYPREIEEFLFTHPAVADVQVfgVPDEKYGE-EIVAWVRLHPGHAASEEE----LREFCKARIAHFKVPRYFRFV 530

                         570
                  ....*....|...
gi 602182148  546 SNMPLTPSGKLDR 558
Cdd:PRK12583  531 DEFPMTVTGKVQK 543

PRK08722

beta-ketoacyl-ACP synthase II;

831-1109

1.15e-25

beta-ketoacyl-ACP synthase II;

Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 112.79 E-value: 1.15e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  831 LATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQKG--GYLYEEGMVRSQD---GHCRA 905
Cdd:PRK08722  143 IAGNLSIMRGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGmaGFGAAKALSTRNDepqKASRP 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  906 FDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDgAIKMgyTAPSVDGQADVISEAIAIAD--IDASTIG 983
Cdd:PRK08722  223 WDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGMSGD-AYHM--TSPSEDGSGGALAMEAAMRDagVTGEQIG 299

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  984 YVEAHGTATQLGDPIEVAGLARAFQRStdsvlGKQQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPN 1063
Cdd:PRK08722  300 YVNAHGTSTPAGDVAEIKGIKRALGEA-----GSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPE 374

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 602182148 1064 PRIDFDATPFfvntELREWSRNGYprrAGVSSFGVGGTNSHIVLEE 1109
Cdd:PRK08722  375 EGLDIDLVPH----TARKVESMEY---AICNSFGFGGTNGSLIFKK 413

PLN02836

3-oxoacyl-[acyl-carrier-protein] synthase

832-1111

1.84e-25

3-oxoacyl-[acyl-carrier-protein] synthase

Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 112.58 E-value: 1.84e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  832 ATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQkggyLYEEGMVRSQ----------DG 901
Cdd:PLN02836  164 AGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDA----LSIAGFSRSRalstkfnscpTE 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  902 HCRAFDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGaikMGYTAPSVDGQADV--ISEAIAIADIDA 979
Cdd:PLN02836  240 ASRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDA---HHITQPHEDGRGAVlaMTRALQQSGLHP 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  980 STIGYVEAHGTATQLGDPIEVAGLARAF-QRSTDSVLgkqqcAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLH 1058
Cdd:PLN02836  317 NQVDYVNAHATSTPLGDAVEARAIKTVFsEHATSGGL-----AFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLN 391

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 602182148 1059 YANPNPRIDFDATPFfvnTELREwsrngYPRRAGVS-SFGVGGTNSHIVLEESP 1111
Cdd:PLN02836  392 LERPDPIFDDGFVPL---TASKA-----MLIRAALSnSFGFGGTNASLLFTSPP 437

PRK08276

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

39-564

2.33e-25

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

Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 113.07 E-value: 2.33e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   39 AIALIDGE-QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLR 117
Cdd:PRK08276    1 PAVIMAPSgEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  118 DSDARILLTST---DVAKKLALTIPA-LQECQTVYLDQEIFE-YDfhflaiakllhnqylrllhfyfytliqQCQATSVS 192
Cdd:PRK08276   81 DSGAKVLIVSAalaDTAAELAAELPAgVPLLLVVAGPVPGFRsYE---------------------------EALAAQPD 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  193 QGIQTQVLPNNLAyciYTSGSTGNPKGILME------HRSLVNMLWWHQQTRPSVQGVRTL-----------QFCAvsfd 255
Cdd:PRK08276  134 TPIADETAGADML---YSSGTTGRPKGIKRPlpgldpDEAPGMMLALLGFGMYGGPDSVYLspaplyhtaplRFGM---- 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  256 fscheifSTLCLGGILVLVPeavRQNPFALAEFISQQKIEKL-FLPV--IALLQLAEAVNGNKSTSlALCEVITTG---- 328
Cdd:PRK08276  207 -------SALALGGTVVVME---KFDAEEALALIERYRVTHSqLVPTmfVRMLKLPEEVRARYDVS-SLRVAIHAAapcp 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  329 ----EQMqitpavanlFQKTGAMLHNHYGATEFQDATTHTlkgnPEGWPTLvP--VGRPLHNVqVYILDEAQQPVPLGGE 402
Cdd:PRK08276  276 vevkRAM---------IDWWGPIIHEYYASSEGGGVTVIT----SEDWLAH-PgsVGKAVLGE-VRILDEDGNELPPGEI 340

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  403 GE--FCIGGIGLArgYHNLPDLTNEKFIPNPFGTnenakklyrTGDLArYL-PDGTIEHLGRIDHQVKIRGFRVELGEIE 479
Cdd:PRK08276  341 GTvyFEMDGYPFE--YHNDPEKTAAARNPHGWVT---------VGDVG-YLdEDGYLYLTDRKSDMIISGGVNIYPQEIE 408

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  480 SVLASHQAVRECAV--VAREIAGHtQLVGYIIAKDTLNLSfDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLD 557
Cdd:PRK08276  409 NLLVTHPKVADVAVfgVPDEEMGE-RVKAVVQPADGADAG-DALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLY 486


                  ....*..
gi 602182148  558 RRALPDP 564
Cdd:PRK08276  487 KRRLRDR 493

PRK08439

3-oxoacyl-(acyl carrier protein) synthase II; Reviewed

732-1106

2.44e-25

3-oxoacyl-(acyl carrier protein) synthase II; Reviewed

Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 111.36 E-value: 2.44e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  732 AVLEG------VELFDATFF---------GYSPKEaaVTDPQQ--------RILLECAWEAFERAGYNPETY-PEPVGVY 787
Cdd:PRK08439   25 AICNGecgikkITLFDASDFpvqiageitDFDPTE--VMDPKEvkkadrfiQLGLKAAREAMKDAGFLPEELdAERFGVS 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  788 AGSSLSTylLNNIGSALGIITEQ------PFIetdmeqFQAKIGNdrsYLATRISYKLNLKGPSVNVQTACSTSLVAVHM 861
Cdd:PRK08439  103 SASGIGG--LPNIEKNSIICFEKgprkisPFF------IPSALVN---MLGGFISIEHGLKGPNLSSVTACAAGTHAIIE 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  862 ACQSLISGEC-QMALAGGISVVVPQK-GGYLYEEGM-VRSQDGH--CRAFDAEAQGTIFGNGGGLVLLKRLQDALDDNDN 936
Cdd:PRK08439  172 AVKTIMLGGAdKMLVVGAESAICPVGiGGFAAMKALsTRNDDPKkaSRPFDKDRDGFVMGEGAGALVLEEYESAKKRGAK 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  937 IMAVIKATAINNDGAikmGYTAPSVDGQADVISEAIAIADIDasTIGYVEAHGTATQLGDPIEVAGLARAFQrstdsvlG 1016
Cdd:PRK08439  252 IYAEIIGFGESGDAN---HITSPAPEGPLRAMKAALEMAGNP--KIDYINAHGTSTPYNDKNETAALKELFG-------S 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1017 KQQCA-IGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPRIDFDATPffvNTelrewsrngyPRRAGV-- 1093
Cdd:PRK08439  320 KEKVPpVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIP---NV----------ARKAELnv 386

                         410
                  ....*....|....*.
gi 602182148 1094 ---SSFGVGGTNSHIV 1106
Cdd:PRK08439  387 vmsNSFGFGGTNGVVI 402

ttLC_FACS_AlkK_like

cd12119

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...

50-561

5.87e-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: 111.95 E-value: 5.87e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   50 TYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLTSTD 129
Cdd:cd12119    27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRD 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  130 VAKKLAltiPALQECQTVYLDQEIFEYDFHFLAIAKLLHNqYLRLLHfyfytliqqcqatSVSQGIQTQVLPNNLAYCI- 208
Cdd:cd12119   107 FLPLLE---AIAPRLPTVEHVVVMTDDAAMPEPAGVGVLA-YEELLA-------------AESPEYDWPDFDENTAAAIc 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  209 YTSGSTGNPKGILMEHRSLVnmlwwhqqtrpsvqgVRTLQFCAVSFdFSCHEI------------------FSTLCLGGI 270
Cdd:cd12119   170 YTSGTTGNPKGVVYSHRSLV---------------LHAMAALLTDG-LGLSESdvvlpvvpmfhvnawglpYAAAMVGAK 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  271 LVLvPeAVRQNPFALAEFISQQKIE-KLFLPVIaLLQLAEAVNGNKSTSLALCEVITTGEQMqiTPAVANLFQKTGAMLH 349
Cdd:cd12119   234 LVL-P-GPYLDPASLAELIEREGVTfAAGVPTV-WQGLLDHLEANGRDLSSLRRVVIGGSAV--PRSLIEAFEERGVRVI 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  350 NHYGATE------FQDATTHTLKGNP-EGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGE--GEFCIGGIGLARGYHNLP 420
Cdd:cd12119   309 HAWGMTEtsplgtVARPPSEHSNLSEdEQLALRAKQGRPVPGVELRIVDDDGRELPWDGKavGELQVRGPWVTKSYYKND 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  421 DlTNEKFIPNPFgtnenakklYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVA----- 495
Cdd:cd12119   389 E-ESEALTEDGW---------LRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGvphpk 458

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 602182148  496 ---REIAghtqlvgYIIAKDTLNLSFDKlepiLRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd12119   459 wgeRPLA-------VVVLKEGATVTAEE----LLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516

ABCL

cd05958

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...

209-561

6.72e-25

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: 110.65 E-value: 6.72e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  209 YTSGSTGNPKGILMEHRSLVNM--LWWHQQTRPSVQGVrtlqFCAVSfdfschEIFSTLCLGGIL----------VLVPE 276
Cdd:cd05958   104 FTSGTTGAPKATMHFHRDPLASadRYAVNVLRLREDDR----FVGSP------PLAFTFGLGGVLlfpfgvgasgVLLEE 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  277 AVRQNPFALaefISQQKIEKLF-LPVI--ALLQLAEAvNGNKSTSLALCevITTGEQMqiTPAVANLFQK-TGAMLHNHY 352
Cdd:cd05958   174 ATPDLLLSA---IARYKPTVLFtAPTAyrAMLAHPDA-AGPDLSSLRKC--VSAGEAL--PAALHRAWKEaTGIPIIDGI 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  353 GATEfqdaTTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGiglARGYHNLPDLTNEKFIPNpf 432
Cdd:cd05958   246 GSTE----MFHIFISARPGDARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRG---PTGCRYLADKRQRTYVQG-- 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  433 GTNEnakklyrTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLV-GYIIAK 511
Cdd:cd05958   317 GWNI-------TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVkAFVVLR 389

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 602182148  512 DTLNLSFDKLEPiLRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05958   390 PGVIPGPVLARE-LQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438

Methyltransf_12

pfam08242

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.

2113-2213

7.14e-25

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.

Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 100.91 E-value: 7.14e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  2113 LEIGAGTGGTTAYLLPHLPGdqTKYVFTDISAFFLAKAEERFKDYPFVRYQVLDIEQAPQAQGFEPQiYDLIVAADVLHA 2192
Cdd:pfam08242    1 LEIGCGTGTLLRALLEALPG--LEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPGS-FDVVVASNVLHH 77

                           90       100
                   ....*....|....*....|.
gi 602182148  2193 TSDLRQTLVHIRQLLAPGGML 2213
Cdd:pfam08242   78 LADPRAVLRNIRRLLKPGGVL 98

PRK05605

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

19-563

8.76e-25

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

Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 112.02 E-value: 8.76e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   19 EFPDSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGC 98
Cdd:PRK05605   28 DYGDTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGA 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   99 AYV---PLdvgYPADRIEYMLRDSDARILL---TSTDVAKKLALTIPAlqecqtvyldQEIFEYDfhfLAIAKLLHNQY- 171
Cdd:PRK05605  108 VVVehnPL---YTAHELEHPFEDHGARVAIvwdKVAPTVERLRRTTPL----------ETIVSVN---MIAAMPLLQRLa 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  172 LRL-----------LH------FYFYTLIQqcqATSVSQGIQTQ---VLPNNLAYCIYTSGSTGNPKGILMEHRSLV-NM 230
Cdd:PRK05605  172 LRLpipalrkaraaLTgpapgtVPWETLVD---AAIGGDGSDVShprPTPDDVALILYTSGTTGKPKGAQLTHRNLFaNA 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  231 LwwhqQTRPSVQGVRTLQ--FCAVSFDFscHEIFSTLCL------GGILVLVP--------EAVRQNPfalaefisqqki 294
Cdd:PRK05605  249 A----QGKAWVPGLGDGPerVLAALPMF--HAYGLTLCLtlavsiGGELVLLPapdidlilDAMKKHP------------ 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  295 eKLFLPVI-----ALLQLAEAvngnKSTSLALCEVITTGeQMQITPAVANLFQK-TGAMLHNHYGATEfqdaTTHTLKGN 368
Cdd:PRK05605  311 -PTWLPGVpplyeKIAEAAEE----RGVDLSGVRNAFSG-AMALPVSTVELWEKlTGGLLVEGYGLTE----TSPIIVGN 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  369 PEGwPTLVP--VGRPLHNVQVYILD--EAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNpfgtnenakkLYRT 444
Cdd:PRK05605  381 PMS-DDRRPgyVGVPFPDTEVRIVDpeDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG----------WFRT 449

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  445 GDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVV--AREiAGHTQLVGYIIAKDTLNLSFDKle 522
Cdd:PRK05605  450 GDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVglPRE-DGSEEVVAAVVLEPGAALDPEG-- 526

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|.
gi 602182148  523 piLRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALPD 563
Cdd:PRK05605  527 --LRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565

PKS_PP

smart00823

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...

2795-2881

9.49e-25

Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 100.02 E-value: 9.49e-25

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   2795 LENAPPKEGLTLLQAHVREQVSQVLGIDTKTLLaEQDVGFFTLGMDSLTSVELRNRLQASLGCSLSSTLAFDYPTQQALV 2874
Cdd:smart00823    1 LAALPPAERRRLLLDLVREQVAAVLGHAAAEAI-DPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALA 79


                    ....*..
gi 602182148   2875 NYLANEL 2881
Cdd:smart00823   80 EHLAAEL 86

ACS-like

cd17634

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...

20-556

1.08e-24

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: 111.90 E-value: 1.08e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   20 FPDSCI---HHLFEDQAAKRPDAIALI----DGEQS--LTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGL 90
Cdd:cd17634    47 FEDATLnlaANALDRHLRENGDRTAIIyegdDTSQSrtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAM 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   91 LGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLTSTD-------------VAKKLALTIPALQecQTVYLDQEIFEYD 157
Cdd:cd17634   127 LACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGgvragrsvplkknVDDALNPNVTSVE--HVIVLKRTGSDID 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  158 FHFLAiakllhnqylrllHFYFYTLIQQCQATSVSQgiqtQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQT 237
Cdd:cd17634   205 WQEGR-------------DLWWRDLIAKASPEHQPE----AMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKY 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  238 RPSVqGVRTLQFCAVSFDF-SCHE--IFSTLCLGGILVLVPEA-VRQNPFALAEFISQQKIEKLFLPVIALLQLA----E 309
Cdd:cd17634   268 VFDY-GPGDIYWCTADVGWvTGHSylLYGPLACGATTLLYEGVpNWPTPARMWQVVDKHGVNILYTAPTAIRALMaagdD 346

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  310 AVNGNKSTSLALceVITTGEQMQITP---AVANLFQKTGAMLhNHYGATEFQDATTHTLKGNPE---GWPTlvpvgRPLH 383
Cdd:cd17634   347 AIEGTDRSSLRI--LGSVGEPINPEAyewYWKKIGKEKCPVV-DTWWQTETGGFMITPLPGAIElkaGSAT-----RPVF 418

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  384 NVQVYILDEAQQPVPLGGEGEFCIGGI--GLARGYHNLPDltneKFIPNPFGTNENakkLYRTGDLARYLPDGTIEHLGR 461
Cdd:cd17634   419 GVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHE----RFEQTYFSTFKG---MYFSGDGARRDEDGYYWITGR 491

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  462 IDHQVKIRGFRVELGEIESVLASHQAVRECAVVA--REIAGhTQLVGYIIAKDTLNLSfDKLEPILRQYSEAVLPEYMIP 539
Cdd:cd17634   492 SDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGipHAIKG-QAPYAYVVLNHGVEPS-PELYAELRNWVRKEIGPLATP 569

                         570
                  ....*....|....*..
gi 602182148  540 TRFINISNMPLTPSGKL 556
Cdd:cd17634   570 DVVHWVDSLPKTRSGKI 586

PRK12492

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

28-564

4.55e-24

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

Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 109.91 E-value: 4.55e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   28 LFEDQAAKRPDAIALIDGEQSLTYGELN----VRANHLAQHLlslGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPL 103
Cdd:PRK12492   29 VFERSCKKFADRPAFSNLGVTLSYAELErhsaAFAAYLQQHT---DLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNT 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  104 DVGYPADRIEYMLRDSDARILLTSTDVAKKLaltipalqecQTVYLDQEIfEYDFH-----FLAIAK-LLHNQYLRLLHF 177
Cdd:PRK12492  106 NPLYTAREMRHQFKDSGARALVYLNMFGKLV----------QEVLPDTGI-EYLIEakmgdLLPAAKgWLVNTVVDKVKK 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  178 YF--YTLIQQC---QATSVSQGIQTQVLPNNL---AYCIYTSGSTGNPKGILMEHRSLV-NMLWWH---QQTRPSVQGV- 244
Cdd:PRK12492  175 MVpaYHLPQAVpfkQALRQGRGLSLKPVPVGLddiAVLQYTGGTTGLAKGAMLTHGNLVaNMLQVRaclSQLGPDGQPLm 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  245 RTLQFCAVS---------FDFSCheifstLCL---GGILVLVpeavrQNPFALAEFISQQKIEKlFLPVIALLQLAEAVN 312
Cdd:PRK12492  255 KEGQEVMIAplplyhiyaFTANC------MCMmvsGNHNVLI-----TNPRDIPGFIKELGKWR-FSALLGLNTLFVALM 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  313 GN---KSTSLALCEVITTGEQMQITPAVANLFQKTGAMLHNHYGATEfqdaTTHTLKGNPEG-WPTLVPVGRPLHNVQVY 388
Cdd:PRK12492  323 DHpgfKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTE----TSPVASTNPYGeLARLGTVGIPVPGTALK 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  389 ILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFipnpfgtneNAKKLYRTGDLARYLPDGTIEHLGRIDHQVKI 468
Cdd:PRK12492  399 VIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEAL---------DAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIV 469

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  469 RGFRVELGEIESVLASHQAVRECAV--VAREIAGHTQLVgYIIAKDTlNLSFDKlepiLRQYSEAVLPEYMIPTRFINIS 546
Cdd:PRK12492  470 SGFNVYPNEIEDVVMAHPKVANCAAigVPDERSGEAVKL-FVVARDP-GLSVEE----LKAYCKENFTGYKVPKHIVLRD 543

                         570
                  ....*....|....*...
gi 602182148  547 NMPLTPSGKLDRRALPDP 564
Cdd:PRK12492  544 SLPMTPVGKILRRELRDI 561

PRK07638

acyl-CoA synthetase; Validated

25-561

7.72e-24

acyl-CoA synthetase; Validated

Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 108.33 E-value: 7.72e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   25 IHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLlAICIERSAELFIGLLGILKAGCAYVPLD 104
Cdd:PRK07638    3 ITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKTI-AILLENRIEFLQLFAGAAMAGWTCVPLD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  105 VGYPADRIEYMLRDSDARILLTSTDVAKKLALtipalQECQTVYLDQeifeydfhflaiakllhnqYLRLLHFYfytliq 184
Cdd:PRK07638   82 IKWKQDELKERLAISNADMIVTERYKLNDLPD-----EEGRVIEIDE-------------------WKRMIEKY------ 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  185 qcqATSVSQGIQTQVLPnnlAYCIYTSGSTGNPKGILMEHRSLV-----NMLWWHQQTRPSVQGVRTLqfcavsfdFSCH 259
Cdd:PRK07638  132 ---LPTYAPIENVQNAP---FYMGFTSGSTGKPKAFLRAQQSWLhsfdcNVHDFHMKREDSVLIAGTL--------VHSL 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  260 EIF---STLCLGGILVLVPeavRQNPFALAEFISQQKIEKLF-LPVI--ALLQlAEAVNGNKSTslalceVITTGEQMQI 333
Cdd:PRK07638  198 FLYgaiSTLYVGQTVHLMR---KFIPNQVLDKLETENISVMYtVPTMleSLYK-ENRVIENKMK------IISSGAKWEA 267

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  334 TP--AVANLFQKtgAMLHNHYGATE--FQDATTH---TLKGNPegwptlvpVGRPLHNVQVYILDEAQQPVPLGGEGEFC 406
Cdd:PRK07638  268 EAkeKIKNIFPY--AKLYEFYGASElsFVTALVDeesERRPNS--------VGRPFHNVQVRICNEAGEEVQKGEIGTVY 337

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  407 IGGIGLARGYHNLPDLTNEKfipnpfgtneNAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQ 486
Cdd:PRK07638  338 VKSPQFFMGYIIGGVLAREL----------NADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHP 407

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 602182148  487 AVRECAVV--AREIAGhTQLVGYIIAKDTlnlsfdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:PRK07638  408 AVDEIVVIgvPDSYWG-EKPVAIIKGSAT--------KQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475

UbiE

COG2226

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...

2100-2224

1.08e-23

Pssm-ID: 441828 [Multi-domain] Cd Length: 143 Bit Score: 99.30 E-value: 1.08e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2100 ALEQLPPERGWRILEIGAGTGGTTAYLLPHlpgdQTKYVFTDISAFFLAKAEERFKDYPF-VRYQVLDIEQAPqaqgFEP 2178
Cdd:COG2226    14 LLAALGLRPGARVLDLGCGTGRLALALAER----GARVTGVDISPEMLELARERAAEAGLnVEFVVGDAEDLP----FPD 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 602182148 2179 QIYDLIVAADVLHATSDLRQTLVHIRQLLAPGGMLILMEDSEPARW 2224
Cdd:COG2226    86 GSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLA 131

entE

PRK10946

(2,3-dihydroxybenzoyl)adenylate synthase;

27-561

3.06e-23

(2,3-dihydroxybenzoyl)adenylate synthase;

Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 107.00 E-value: 3.06e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   27 HLFEDQAAkrPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYV----- 101
Cdd:PRK10946   29 DILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVAPVnalfs 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  102 --PLDVGYPADRIEYMLRDSDAR-ILLTSTDVAKKLALTIPALQecqtvyldqeifeydfhflaIAKLLHNQYLRLLHfy 178
Cdd:PRK10946  107 hqRSELNAYASQIEPALLIADRQhALFSDDDFLNTLVAEHSSLR--------------------VVLLLNDDGEHSLD-- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  179 fyTLIQQCQATSVSqgiqTQVLPNNLAYCIYTSGSTGNPKGILMEHRSlvnmlwWHQQTRPSVQ----GVRTLQFCAV-- 252
Cdd:PRK10946  165 --DAINHPAEDFTA----TPSPADEVAFFQLSGGSTGTPKLIPRTHND------YYYSVRRSVEicgfTPQTRYLCALpa 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  253 --SFDFSCHEIFSTLCLGGILVLVPeavrqNPFALAEF--ISQQKIE--KLFLPVIAL-LQLAEAVNGNKS-TSLALCEV 324
Cdd:PRK10946  233 ahNYPMSSPGALGVFLAGGTVVLAP-----DPSATLCFplIEKHQVNvtALVPPAVSLwLQAIAEGGSRAQlASLKLLQV 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  325 --ITTGEQM--QITPAVANLFQKTGAM---LHNHygaTEFQDATTHTLKGNpegwptlvpvGRPLH-NVQVYILDEAQQP 396
Cdd:PRK10946  308 ggARLSETLarRIPAELGCQLQQVFGMaegLVNY---TRLDDSDERIFTTQ----------GRPMSpDDEVWVADADGNP 374

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  397 VPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFgtnenakklYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELG 476
Cdd:PRK10946  375 LPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF---------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAE 445

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  477 EIESVLASHQAVRECAVVAREiaghTQLVG-----YIIAKDTLNlsfdklEPILRQY-SEAVLPEYMIPTRFINISNMPL 550
Cdd:PRK10946  446 EIENLLLRHPAVIHAALVSME----DELMGekscaFLVVKEPLK------AVQLRRFlREQGIAEFKLPDRVECVDSLPL 515

                         570
                  ....*....|.
gi 602182148  551 TPSGKLDRRAL 561
Cdd:PRK10946  516 TAVGKVDKKQL 526

PRK07788

acyl-CoA synthetase; Validated

33-563

4.20e-23

acyl-CoA synthetase; Validated

Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 106.55 E-value: 4.20e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   33 AAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGcayvpldvgypadri 112
Cdd:PRK07788   59 ARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVG--------------- 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  113 eymlrdsdARILLTSTDVAKklaltiPALQEC------QTVYLDQEifeydfhFLAIAKLLHNQYLRLLHFYFYTLIQQC 186
Cdd:PRK07788  124 --------ARIILLNTGFSG------PQLAEVaaregvKALVYDDE-------FTDLLSALPPDLGRLRAWGGNPDDDEP 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  187 QATSVS------QGIQTQVLP---NNLAYCIYTSGSTGNPKGILMEH----RSLVNMLwwhqqTRPSVQGVRTLQFCAVS 253
Cdd:PRK07788  183 SGSTDEtlddliAGSSTAPLPkppKPGGIVILTSGTTGTPKGAPRPEpsplAPLAGLL-----SRVPFRAGETTLLPAPM 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  254 FD---FSCHEIfsTLCLGGILVLvpeAVRQNPFALAEFISQQKIEKLFL-PVI--ALLQLAEAVNGNKSTSlALCEVITT 327
Cdd:PRK07788  258 FHatgWAHLTL--AMALGSTVVL---RRRFDPEATLEDIAKHKATALVVvPVMlsRILDLGPEVLAKYDTS-SLKIIFVS 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  328 GEQMqiTPAVANLFQKT-GAMLHNHYGATEFQDATTHTlkgnPEGW---PTLVpvGRPLHNVQVYILDEAQQPVPLGGEG 403
Cdd:PRK07788  332 GSAL--SPELATRALEAfGPVLYNLYGSTEVAFATIAT----PEDLaeaPGTV--GRPPKGVTVKILDENGNEVPRGVVG 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  404 E-FCIGGIGLaRGYhnlpdltnekfipnpfgTNENAKK----LYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEI 478
Cdd:PRK07788  404 RiFVGNGFPF-EGY-----------------TDGRDKQiidgLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEV 465

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  479 ESVLASHQAVRECAVVAREIA--GHtQLVGYIIAKDTLNLSFDKlepiLRQYSEAVLPEYMIPTRFINISNMPLTPSGKL 556
Cdd:PRK07788  466 EDLLAGHPDVVEAAVIGVDDEefGQ-RLRAFVVKAPGAALDEDA----IKDYVRDNLARYKVPRDVVFLDELPRNPTGKV 540


                  ....*..
gi 602182148  557 DRRALPD 563
Cdd:PRK07788  541 LKRELRE 547

PRK06710

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

25-561

6.25e-23

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

Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 106.27 E-value: 6.25e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   25 IHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLD 104
Cdd:PRK06710   26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  105 VGYPADRIEYMLRDSDARILLTstdvakkLALTIPALQECQ-TVYLDQEIFEYDFHFLAIAKLLHNQYLRLLHFYFYTLI 183
Cdd:PRK06710  106 PLYTERELEYQLHDSGAKVILC-------LDLVFPRVTNVQsATKIEHVIVTRIADFLPFPKNLLYPFVQKKQSNLVVKV 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  184 QQCQA----TSVSQGIQTQV-LP----NNLAYCIYTSGSTGNPKGILMEHRSLV-NMLWWHQQTRPSVQGVRTLqFCAVS 253
Cdd:PRK06710  179 SESETihlwNSVEKEVNTGVeVPcdpeNDLALLQYTGGTTGFPKGVMLTHKNLVsNTLMGVQWLYNCKEGEEVV-LGVLP 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  254 FdFSCHEIFSTLCL----GGILVLVPEAVRQNPFalaEFISQQKIeKLF--LPV--IALLQlAEAVNGNKSTSLALCevI 325
Cdd:PRK06710  258 F-FHVYGMTAVMNLsimqGYKMVLIPKFDMKMVF---EAIKKHKV-TLFpgAPTiyIALLN-SPLLKEYDISSIRAC--I 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  326 TTGEQMQItpAVANLFQK-TGAMLHNHYGATEFQDATTHTLKgnpegWPTLVP--VGRPLHNVQVYILD-EAQQPVPLGG 401
Cdd:PRK06710  330 SGSAPLPV--EVQEKFETvTGGKLVEGYGLTESSPVTHSNFL-----WEKRVPgsIGVPWPDTEAMIMSlETGEALPPGE 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  402 EGEFCIGGIGLARGYHNLPDltnekfipnpfgtnENAKKL----YRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGE 477
Cdd:PRK06710  403 IGEIVVKGPQIMKGYWNKPE--------------ETAAVLqdgwLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPRE 468

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  478 IESVLASHQAVRECAVVAREIAGHTQLV-GYIIAKDTLNLSFDKLEPILRQYseavLPEYMIPTRFINISNMPLTPSGKL 556
Cdd:PRK06710  469 VEEVLYEHEKVQEVVTIGVPDPYRGETVkAFVVLKEGTECSEEELNQFARKY----LAAYKVPKVYEFRDELPKTTVGKI 544


                  ....*
gi 602182148  557 DRRAL 561
Cdd:PRK06710  545 LRRVL 549

Firefly_Luc

cd17642

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...

31-561

9.28e-23

insect luciferase, similar to plant 4-coumarate: CoA ligases; 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: 341297 [Multi-domain] Cd Length: 532 Bit Score: 105.30 E-value: 9.28e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   31 DQAAKRPDAIALIDG--EQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYP 108
Cdd:cd17642    25 KRYASVPGTIAFTDAhtGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYN 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  109 ADRIEYMLRDSDARILLTSTDVAKKLALTIPALQECQTVYLDQEIFEYDfHFLAIAKLLHNQYLRLLHFYFYTliqqcqa 188
Cdd:cd17642   105 ERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIIKTIIILDSKEDYK-GYQCLYTFITQNLPPGFNEYDFK------- 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  189 tSVSQGIQTQVlpnnlAYCIYTSGSTGNPKGILMEHRSLVNMLwwHQQTRPSV-----QGVRTLQFCAVSFDFSCHEIFS 263
Cdd:cd17642   177 -PPSFDRDEQV-----ALIMNSSGSTGLPKGVQLTHKNIVARF--SHARDPIFgnqiiPDTAILTVIPFHHGFGMFTTLG 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  264 TLCLGGILVLVPEavrqnpFALAEFIS---QQKIEKLFL--PVIALLQLAEAVNGNKSTSLAlcEVITTGEQM--QITPA 336
Cdd:cd17642   249 YLICGFRVVLMYK------FEEELFLRslqDYKVQSALLvpTLFAFFAKSTLVDKYDLSNLH--EIASGGAPLskEVGEA 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  337 VANLFQKTGamLHNHYGATEfqdaTTHTLKGNPEGW--PTLVPVGRPLHNVQVYILDEAQQpvpLGGE--GEFCIGGIGL 412
Cdd:cd17642   321 VAKRFKLPG--IRQGYGLTE----TTSAILITPEGDdkPGAVGKVVPFFYAKVVDLDTGKT---LGPNerGELCVKGPMI 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  413 ARGYHNLPDLTNEKFIPNPFgtnenakklYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECA 492
Cdd:cd17642   392 MKGYVNNPEATKALIDKDGW---------LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAG 462

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 602182148  493 VVAR--EIAGHTQLVGYII-AKDTLNlsfdklEPILRQY-SEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd17642   463 VAGIpdEDAGELPAAVVVLeAGKTMT------EKEVMDYvASQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKI 529

PRK07529

AMP-binding domain protein; Validated

21-561

3.99e-22

AMP-binding domain protein; Validated

Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 104.27 E-value: 3.99e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   21 PDScIHHLFEDQAAKRPDAIALI--------DGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLG 92
Cdd:PRK07529   24 PAS-TYELLSRAAARHPDAPALSflldadplDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   93 ILKAGCAyVPLDVGYPADRIEYMLRDSDARILLT-----STDVAKKLALTIPALQECQTVYL----DQEIFEYDFHFLAI 163
Cdd:PRK07529  103 GEAAGIA-NPINPLLEPEQIAELLRAAGAKVLVTlgpfpGTDIWQKVAEVLAALPELRTVVEvdlaRYLPGPKRLAVPLI 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  164 AKLLHNQYLRllhfyFYTLIQQCQATSVSQGiqTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQG 243
Cdd:PRK07529  182 RRKAHARILD-----FDAELARQPGDRLFSG--RPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPG 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  244 vRTLqFCAVS-FD-FSCHEI-FSTLCLGGILVLVPEAVRQNPFALAEF---ISQQKIEKLF-LPVI--ALLQLAeaVNGN 314
Cdd:PRK07529  255 -DTV-FCGLPlFHvNALLVTgLAPLARGAHVVLATPQGYRGPGVIANFwkiVERYRINFLSgVPTVyaALLQVP--VDGH 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  315 KSTSLALceVITTGEQMqiTPAVANLFQ-KTGAMLHNHYGATEfqdATTHTLKGNPEGWPTLVPVGRPL--HNVQVYILD 391
Cdd:PRK07529  331 DISSLRY--ALCGAAPL--PVEVFRRFEaATGVRIVEGYGLTE---ATCVSSVNPPDGERRIGSVGLRLpyQRVRVVILD 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  392 EA---QQPVPLGGEGEFCIGGIGLARGYhnlpdlTNEkfipnpfgtnENAKKLY------RTGDLARYLPDGTIEHLGRi 462
Cdd:PRK07529  404 DAgryLRDCAVDEVGVLCIAGPNVFSGY------LEA----------AHNKGLWledgwlNTGDLGRIDADGYFWLTGR- 466

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  463 dhqVK---IR-GFRVELGEIESVLASHQAVRECAVVAREIAGHTQL-VGYIIAKDTLNLSfdklEPILRQYSEAVLPE-Y 536
Cdd:PRK07529  467 ---AKdliIRgGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELpVAYVQLKPGASAT----EAELLAFARDHIAErA 539

                         570       580
                  ....*....|....*....|....*
gi 602182148  537 MIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:PRK07529  540 AVPKHVRILDALPKTAVGKIFKPAL 564

PRK13295

cyclohexanecarboxylate-CoA ligase; Reviewed

21-561

4.48e-22

cyclohexanecarboxylate-CoA ligase; Reviewed

Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 103.59 E-value: 4.48e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   21 PDSCIHHLFEDQAAKRPDAIALID-----GE-QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGIL 94
Cdd:PRK13295   22 HDRTINDDLDACVASCPDKTAVTAvrlgtGApRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACS 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   95 KAGCAYVPLDVGYPADRIEYMLRDSDARILLtstdvakklaltIPALqecqtvyldqeiFEyDFHFLAIAKLLHNQYLRL 174
Cdd:PRK13295  102 RIGAVLNPLMPIFRERELSFMLKHAESKVLV------------VPKT------------FR-GFDHAAMARRLRPELPAL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  175 LHFY---------FYTLI------QQCQATSVSQGIQTQvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLwwhqqtRP 239
Cdd:PRK13295  157 RHVVvvggdgadsFEALLitpaweQEPDAPAILARLRPG--PDDVTQLIYTSGTTGEPKGVMHTANTLMANI------VP 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  240 SVQGVRtlqfcaVSFDFSCHeIFSTLC-LGGIL--VLVP-----EAVRQ---NPFALAEFISQQKIEKLFLPVIALLQLA 308
Cdd:PRK13295  229 YAERLG------LGADDVIL-MASPMAhQTGFMygLMMPvmlgaTAVLQdiwDPARAAELIRTEGVTFTMASTPFLTDLT 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  309 EAVNGNKSTSLALCEVITTGEQmqITPAVANLFQKT-GAMLHNHYGATEFQDATTHTLKGNPEgwPTLVPVGRPLHNVQV 387
Cdd:PRK13295  302 RAVKESGRPVSSLRTFLCAGAP--IPGALVERARAAlGAKIVSAWGMTENGAVTLTKLDDPDE--RASTTDGCPLPGVEV 377

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  388 YILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLtnekfipnpfgTNENAKKLYRTGDLARYLPDGTIEHLGRiDHQVK 467
Cdd:PRK13295  378 RVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQL-----------NGTDADGWFDTGDLARIDADGYIRISGR-SKDVI 445

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  468 IRGFR-VELGEIESVLASHQAVRECAVVA--------REIAghtqlvgYIIAKDTLNLSFDKLEPILRqySEAVLPEYmI 538
Cdd:PRK13295  446 IRGGEnIPVVEIEALLYRHPAIAQVAIVAypderlgeRACA-------FVVPRPGQSLDFEEMVEFLK--AQKVAKQY-I 515

                         570       580
                  ....*....|....*....|...
gi 602182148  539 PTRFINISNMPLTPSGKLDRRAL 561
Cdd:PRK13295  516 PERLVVRDALPRTPSGKIQKFRL 538

PRK08751

long-chain fatty acid--CoA ligase;

25-563

4.88e-22

long-chain fatty acid--CoA ligase;

Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 103.42 E-value: 4.88e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   25 IHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLS-LGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPL 103
Cdd:PRK08751   27 VAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGeLQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNV 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  104 DVGYPADRIEYMLRDSDARILLT----STDVAKKLALTiPALQECQTVYLDQEIFE----YDFHFLAIAKLLHNQYL-RL 174
Cdd:PRK08751  107 NPLYTPRELKHQLIDSGASVLVVidnfGTTVQQVIADT-PVKQVITTGLGDMLGFPkaalVNFVVKYVKKLVPEYRInGA 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  175 LHFyfytliQQCQATSVSQGIQT-QVLPNNLAYCIYTSGSTGNPKGILMEHRSLV-NMLWWHQ--QTRPSVQGVRTLQFC 250
Cdd:PRK08751  186 IRF------REALALGRKHSMPTlQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVaNMQQAHQwlAGTGKLEEGCEVVIT 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  251 AVSFdfscHEIFSTLCLGGILVLVP--EAVRQNPFALAEFISQQKIeklfLPVIALLQLAEAVNGNKST----SLALCEV 324
Cdd:PRK08751  260 ALPL----YHIFALTANGLVFMKIGgcNHLISNPRDMPGFVKELKK----TRFTAFTGVNTLFNGLLNTpgfdQIDFSSL 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  325 -ITTGEQMQITPAVANLFQK-TGAMLHNHYGATEFQDATTHtlkgNPEGWPTLV-PVGRPLHNVQVYILDEAQQPVPLGG 401
Cdd:PRK08751  332 kMTLGGGMAVQRSVAERWKQvTGLTLVEAYGLTETSPAACI----NPLTLKEYNgSIGLPIPSTDACIKDDAGTVLAIGE 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  402 EGEFCIGGIGLARGYHNLPDLTNEKFipnpfgtneNAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESV 481
Cdd:PRK08751  408 IGELCIKGPQVMKGYWKRPEETAKVM---------DADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDV 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  482 LASHQAVRECAVVAREIAGHTQLVGYIIAKDTLNLSFDKlepiLRQYSEAVLPEYMIPtRFINI-SNMPLTPSGKLDRRA 560
Cdd:PRK08751  479 IAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKDPALTAED----VKAHARANLTGYKQP-RIIEFrKELPKTNVGKILRRE 553


                  ...
gi 602182148  561 LPD 563
Cdd:PRK08751  554 LRD 556

PRK06155

crotonobetaine/carnitine-CoA ligase; Provisional

28-561

5.85e-22

crotonobetaine/carnitine-CoA ligase; Provisional

Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 102.91 E-value: 5.85e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   28 LFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGY 107
Cdd:PRK06155   26 MLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTAL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  108 PADRIEYMLRDSDARILLTSTDVAKKLALTIPALqecqtvyldqeifeydfhfLAIAKLLhnqylrllhfyfytLIQQCQ 187
Cdd:PRK06155  106 RGPQLEHILRNSGARLLVVEAALLAALEAADPGD-------------------LPLPAVW--------------LLDAPA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  188 ATSVSQGIQT-------------QVLPNNLAYCIYTSGSTGNPKGILMEHrslVNMLWWhqqtrpSVQGVRTLQFCAVSF 254
Cdd:PRK06155  153 SVSVPAGWSTaplppldapapaaAVQPGDTAAILYTSGTTGPSKGVCCPH---AQFYWW------GRNSAEDLEIGADDV 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  255 DFSCHEIFST---------LCLGGILVLVP--------EAVRQN----PFALAEFISqqkieklflpvIALLQLAEAVNG 313
Cdd:PRK06155  224 LYTTLPLFHTnalnaffqaLLAGATYVLEPrfsasgfwPAVRRHgatvTYLLGAMVS-----------ILLSQPARESDR 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  314 NKSTSLALcevittgeqmqiTPAV-----ANLFQKTGAMLHNHYGATEFQDATTHTLKGNPEGWptlvpVGRPLHNVQVY 388
Cdd:PRK06155  293 AHRVRVAL------------GPGVpaalhAAFRERFGVDLLDGYGSTETNFVIAVTHGSQRPGS-----MGRLAPGFEAR 355

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  389 ILDEAQQPVPLGGEGEFCIGG---IGLARGYHNLPDLTNEKFipnpfgtnenaKKL-YRTGDLARYLPDGTIEHLGRIDH 464
Cdd:PRK06155  356 VVDEHDQELPDGEPGELLLRAdepFAFATGYFGMPEKTVEAW-----------RNLwFHTGDRVVRDADGWFRFVDRIKD 424

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  465 QVKIRGFRVELGEIESVLASHQAVRECAV--VAREIAGHTQLVGyIIAKDTLNLSFDKLEpilrQYSEAVLPEYMIPtRF 542
Cdd:PRK06155  425 AIRRRGENISSFEVEQVLLSHPAVAAAAVfpVPSELGEDEVMAA-VVLRDGTALEPVALV----RHCEPRLAYFAVP-RY 498

                         570       580
                  ....*....|....*....|
gi 602182148  543 INI-SNMPLTPSGKLDRRAL 561
Cdd:PRK06155  499 VEFvAALPKTENGKVQKFVL 518

A_NRPS_TubE_like

cd05906

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...

32-561

8.61e-22

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: 102.36 E-value: 8.61e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   32 QAAKRPDAIALI----DG-EQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVG 106
Cdd:cd05906    18 RAAERGPTKGITyidaDGsEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  107 yPADRIEymlRDSDARILLTSTDVAKKLALTIPALQEcqtvyldqeifeydfHFLAIAKLLHNQYLRLLhfyfyTLIQQC 186
Cdd:cd05906    98 -PTYDEP---NARLRKLRHIWQLLGSPVVLTDAELVA---------------EFAGLETLSGLPGIRVL-----SIEELL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  187 QATSVSQGIQTQvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLW---WHQQTRPsvqgvRTLQFCAVSFD-----FSC 258
Cdd:cd05906   154 DTAADHDLPQSR--PDDLALLMLTSGSTGFPKAVPLTHRNILARSAgkiQHNGLTP-----QDVFLNWVPLDhvgglVEL 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  259 HeIFStLCLGGILVLVP-EAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALCEV---ITTGEQMqIT 334
Cdd:cd05906   227 H-LRA-VYLGCQQVHVPtEEILADPLRWLDLIDRYRVTITWAPNFAFALLNDLLEEIEDGTWDLSSLrylVNAGEAV-VA 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  335 PAVANLFQ---KTGA---MLHNHYGATEFQDATT---HTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEF 405
Cdd:cd05906   304 KTIRRLLRllePYGLppdAIRPAFGMTETCSGVIysrSFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRL 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  406 CIGGIGLARGYHNLPDLTNEKFipnpfgTNENakkLYRTGDLArYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASH 485
Cdd:cd05906   384 QVRGPVVTKGYYNNPEANAEAF------TEDG---WFRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEV 453

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  486 QAVRE---CAVVAREIAGHT-QLVgyIIAKDTLNLSfDKLEPILRQYSEAVL------PEYMIPtrfINISNMPLTPSGK 555
Cdd:cd05906   454 PGVEPsftAAFAVRDPGAETeELA--IFFVPEYDLQ-DALSETLRAIRSVVSrevgvsPAYLIP---LPKEEIPKTSLGK 527


                  ....*.
gi 602182148  556 LDRRAL 561
Cdd:cd05906   528 IQRSKL 533

OSB_MenE-like

cd17630

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...

204-561

8.80e-22

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: 99.33 E-value: 8.80e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  204 LAYCIYTSGSTGNPKGILMEHRSLVNmlwwhqqtrpSVQGVRTLqfcaVSFDFSCHEIfstLCL-----GGILVLV---- 274
Cdd:cd17630     2 LATVILTSGSTGTPKAVVHTAANLLA----------SAAGLHSR----LGFGGGDSWL---LSLplyhvGGLAILVrsll 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  275 ---PEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEavNGNKSTSLALCEVITTGEQmQITPAVANLFQKTGAMLHNH 351
Cdd:cd17630    65 agaELVLLERNQALAEDLAPPGVTHVSLVPTQLQRLLD--SGQGPAALKSLRAVLLGGA-PIPPELLERAADRGIPLYTT 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  352 YGATEFQDATThtlkgnpeGWPTLVP----VGRPLHNVQVYILDEaqqpvplggeGEFCIGGIGLARGYHNLPdltnekf 427
Cdd:cd17630   142 YGMTETASQVA--------TKRPDGFgrggVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQ------- 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  428 IPNPFgtneNAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVV--AREIAGHtQLV 505
Cdd:cd17630   197 LVPEF----NEDGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVgvPDEELGQ-RPV 271

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 602182148  506 GYIIAKDTLNLSfdklepILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd17630   272 AVIVGRGPADPA------ELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321

ttLC_FACS_AEE21_like

cd12118

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...

28-555

1.31e-21

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: 101.22 E-value: 1.31e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   28 LFEDQAAK-RPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVG 106
Cdd:cd12118     8 SFLERAAAvYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  107 YPADRIEYMLRDSDARILLTstdvakklaltipalqecqtvylDQEiFEYDfHFLAIAKllhnqylrllhfYFYTLIQ-- 184
Cdd:cd12118    88 LDAEEIAFILRHSEAKVLFV-----------------------DRE-FEYE-DLLAEGD------------PDFEWIPpa 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  185 -QCQATSVSqgiqtqvlpnnlayciYTSGSTGNPKGILMEHR-----SLVNMLWWHQQTRPSVqgVRTLQfcavsfDFSC 258
Cdd:cd12118   131 dEWDPIALN----------------YTSGTTGRPKGVVYHHRgaylnALANILEWEMKQHPVY--LWTLP------MFHC 186

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  259 HE---IFSTLCLGGILVLVPEAvrqNPFALAEFISQQKIEKLFLPVIALLQLAeavNGNKSTSLAL---CEVITTGEqmq 332
Cdd:cd12118   187 NGwcfPWTVAAVGGTNVCLRKV---DAKAIYDLIEKHKVTHFCGAPTVLNMLA---NAPPSDARPLphrVHVMTAGA--- 257

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  333 iTPAVANLFQKTGAMLH-NH-YGATE-FQDATTHTLKgnPEgWPTLVP-----------VGRPLHNvQVYILD-EAQQPV 397
Cdd:cd12118   258 -PPPAAVLAKMEELGFDvTHvYGLTEtYGPATVCAWK--PE-WDELPTeerarlkarqgVRYVGLE-EVDVLDpETMKPV 332

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  398 PLGGE--GEFCIGGIGLARGYHNLPDLTNEKFipnpfgtnenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVEL 475
Cdd:cd12118   333 PRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF----------RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISS 402

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  476 GEIESVLASHQAVRECAVVAR--EIAGHTqLVGYIIAKDTLNLSFDKlepiLRQYSEAVLPEYMIPtRFINISNMPLTPS 553
Cdd:cd12118   403 VEVEGVLYKHPAVLEAAVVARpdEKWGEV-PCAFVELKEGAKVTEEE----IIAFCREHLAGFMVP-KTVVFGELPKTST 476


                  ..
gi 602182148  554 GK 555
Cdd:cd12118   477 GK 478

KAsynt_C_assoc

pfam16197

Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ...

1062-1175

1.34e-21

Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human.

Pssm-ID: 465059 [Multi-domain] Cd Length: 111 Bit Score: 92.22 E-value: 1.34e-21

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  1062 PNPRID-FDATPFFVNTELREWSRNgyprRAGVSSFGVGGTNSHIVLEESPVKQPTlfSSLPERSHHLLTLSAHTQEALH 1140
Cdd:pfam16197    1 PNPDIPaLLDGRLKVVTEPTPWPGG----IVGVNSFGFGGANAHVILKSNPKPKIP--PESPDNLPRLVLLSGRTEEAVK 74

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 602182148  1141 ELVQRYIQHNETHLDIDLGDLCFTANtgRKHFEHR 1175
Cdd:pfam16197   75 ALLEKLENHLDDAEFLSLLNDIHSLP--ISGHPYR 107

MACS_AAE_MA_like

cd05970

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...

33-558

1.93e-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: 101.42 E-value: 1.93e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   33 AAKRPDAIALI-----DGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGY 107
Cdd:cd05970    27 AKEYPDKLALVwcddaGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  108 PADRIEYMLRDSDARILLTS-----TDVAKKlaltipALQECQTVYL-------DQEIFEyDFHflaiaKLLHNQYlrll 175
Cdd:cd05970   107 TAKDIVYRIESADIKMIVAIaedniPEEIEK------AAPECPSKPKlvwvgdpVPEGWI-DFR-----KLIKNAS---- 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  176 hfyfyTLIQQCQATSVSQGiqtqvlpNNLAYCIYTSGSTGNPKgiLMEHR------SLVNMLWWHQqTRPsvqGVRTLQF 249
Cdd:cd05970   171 -----PDFERPTANSYPCG-------EDILLVYFSSGTTGMPK--MVEHDftyplgHIVTAKYWQN-VRE---GGLHLTV 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  250 CAVSFDFSCHEIFSTLCLGGILVLVPEAVRQNPFALAEFISQQKIEKLFLP-VIALLQLAEAVNGNKSTSLALCevITTG 328
Cdd:cd05970   233 ADTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPpTIYRFLIREDLSRYDLSSLRYC--TTAG 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  329 EQMqiTPAVANLF-QKTGAMLHNHYGATEfqdaTTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCI 407
Cdd:cd05970   311 EAL--NPEVFNTFkEKTGIKLMEGFGQTE----TTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVI 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  408 G-----GIGLARGYHNLPDLTNEKFipnpfgtnenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVL 482
Cdd:cd05970   385 RtskgkPVGLFGGYYKDAEKTAEVW----------HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESAL 454

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 602182148  483 ASHQAVRECAV--VAREIAGHTQLVGYIIAKDTlnLSFDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDR 558
Cdd:cd05970   455 IQHPAVLECAVtgVPDPIRGQVVKATIVLAKGY--EPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRR 530

ACS

cd05966

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...

32-561

7.39e-21

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: 99.94 E-value: 7.39e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   32 QAAKRPDAIALI----DGEQS--LTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDV 105
Cdd:cd05966    62 HLKERGDKVAIIwegdEPDQSrtITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFA 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  106 GYPA----DRIEymlrDSDARILLTsTDVAKKLALTIP-------ALQECQTVYldqeifeydfHFLaIAKLLHNQ--YL 172
Cdd:cd05966   142 GFSAeslaDRIN----DAQCKLVIT-ADGGYRGGKVIPlkeivdeALEKCPSVE----------KVL-VVKRTGGEvpMT 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  173 RLLHFYFYTLIQQ----CQATSVSqgiqtqvlPNNLAYCIYTSGSTGNPKGILmeHRSLVNMLWWHqqtrpsvqgvRTLQ 248
Cdd:cd05966   206 EGRDLWWHDLMAKqspeCEPEWMD--------SEDPLFILYTSGSTGKPKGVV--HTTGGYLLYAA----------TTFK 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  249 FcavSFDFSCHEIF------------STLCLG----GILVLVPEAVRQNPFA--LAEFISQQKIEKLFL-P-VIALLQLA 308
Cdd:cd05966   266 Y---VFDYHPDDIYwctadigwitghSYIVYGplanGATTVMFEGTPTYPDPgrYWDIVEKHKVTIFYTaPtAIRALMKF 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  309 --EAVNGNKSTSLalcEVITT-GEQmqITPAVANLFqktgamlHNHYGA-------TEFQDAT-THTLKGNPEGWPTlVP 377
Cdd:cd05966   343 gdEWVKKHDLSSL---RVLGSvGEP--INPEAWMWY-------YEVIGKercpivdTWWQTETgGIMITPLPGATPL-KP 409

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  378 --VGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGI--GLARGYHNLPdltnEKFIP---NPFgtnenaKKLYRTGDLARY 450
Cdd:cd05966   410 gsATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDH----ERYEDtyfSKF------PGYYFTGDGARR 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  451 LPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAR--EIAGHTqLVGYIIAKDTLNLSfDKLEPILRQY 528
Cdd:cd05966   480 DEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRphDIKGEA-IYAFVTLKDGEEPS-DELRKELRKH 557

                         570       580       590
                  ....*....|....*....|....*....|...
gi 602182148  529 SEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05966   558 VRKEIGPIATPDKIQFVPGLPKTRSGKIMRRIL 590

PLN02787

3-oxoacyl-[acyl-carrier-protein] synthase II

800-1107

8.00e-21

3-oxoacyl-[acyl-carrier-protein] synthase II

Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 99.28 E-value: 8.00e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  800 IGSALGIIteqpfietdmeqfqaKIGNDrSYLATRISYK----------------------LNLKGPSVNVQTACSTSLV 857
Cdd:PLN02787  233 IGSAMGGM---------------KVFND-AIEALRISYRkmnpfcvpfattnmgsamlamdLGWMGPNYSISTACATSNF 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  858 AVHMACQSLISGECQMALAGGI-SVVVP-QKGGYLYEEGMVRSQDGHCRA---FDAEAQGTIFGNGGGLVLLKRLQDALD 932
Cdd:PLN02787  297 CILNAANHIIRGEADVMLCGGSdAAIIPiGLGGFVACRALSQRNDDPTKAsrpWDMNRDGFVMGEGAGVLLLEELEHAKK 376

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  933 DNDNIMAVIKATAINNDgAIKMgyTAPSVDGQADV--ISEAIAIADIDASTIGYVEAHGTATQLGDPIEVAGLARAFQRS 1010
Cdd:PLN02787  377 RGANIYAEFLGGSFTCD-AYHM--TEPHPEGAGVIlcIEKALAQSGVSKEDVNYINAHATSTKAGDLKEYQALMRCFGQN 453

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 1011 TdsvlgkqQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPRIDfdaTPFFVNTELREWSrngyPRR 1090
Cdd:PLN02787  454 P-------ELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVD---TKVLVGPKKERLD----IKV 519

                         330
                  ....*....|....*..
gi 602182148 1091 AGVSSFGVGGTNSHIVL 1107
Cdd:PLN02787  520 ALSNSFGFGGHNSSILF 536

PRK07786

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

33-556

1.07e-20

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

Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 99.08 E-value: 1.07e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   33 AAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRI 112
Cdd:PRK07786   27 ALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  113 EYMLRDSDARILLTS---TDVAKKLALTIPALQECQTV--YLDQEIFEYDfhflaiakllhnqylrllhfyfyTLIQQCQ 187
Cdd:PRK07786  107 AFLVSDCGAHVVVTEaalAPVATAVRDIVPLLSTVVVAggSSDDSVLGYE-----------------------DLLAEAG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  188 ATSVSQGIqtqvlPNNLAYCI-YTSGSTGNPKGILMEHRSLVN-----MLWWHQQTRPSVqgvrtlQFCAVSFdFSCHEI 261
Cdd:PRK07786  164 PAHAPVDI-----PNDSPALImYTSGTTGRPKGAVLTHANLTGqamtcLRTNGADINSDV------GFVGVPL-FHIAGI 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  262 FST---LCLGGILVLVPEAVRqNPFALAEFISQQKIEKLFLpVIALLQLAEAVNGNKSTSLALcEVITTGEqmqiTPAVA 338
Cdd:PRK07786  232 GSMlpgLLLGAPTVIYPLGAF-DPGQLLDVLEAEKVTGIFL-VPAQWQAVCAEQQARPRDLAL-RVLSWGA----APASD 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  339 NLFQKTGAMLHNH-----YGATEFQDATThTLKGNpEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLA 413
Cdd:PRK07786  305 TLLRQMAATFPEAqilaaFGQTEMSPVTC-MLLGE-DAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLM 382

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  414 RGYHNLPDLTNEKFipnpfgtnenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAV 493
Cdd:PRK07786  383 SGYWNNPEATAEAF----------AGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAV 452

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 602182148  494 VAR--EIAGHTQLVGYIIAKDTLNLSFDKLEPILRQYseavLPEYMIPTRFINISNMPLTPSGKL 556
Cdd:PRK07786  453 IGRadEKWGEVPVAVAAVRNDDAALTLEDLAEFLTDR----LARYKHPKALEIVDALPRNPAGKV 513

PRK13391

acyl-CoA synthetase; Provisional

33-564

1.17e-20

acyl-CoA synthetase; Provisional

Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 98.61 E-value: 1.17e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   33 AAKRPDAIALI---DGEqSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPA 109
Cdd:PRK13391    7 AQTTPDKPAVImasTGE-VVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  110 DRIEYMLRDSDARILLTST---DVAKKLALTIPALQECQTVYLDQEIFEYDFHFLAIAkllhnqylrllhfyfytliqQC 186
Cdd:PRK13391   86 AEAAYIVDDSGARALITSAaklDVARALLKQCPGVRHRLVLDGDGELEGFVGYAEAVA--------------------GL 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  187 QATSvsqgIQTQVLPNNLaycIYTSGSTGNPKGILMEHRSLvnmlwwhqqtrPSVQGVRTLQFCAVSFDFSCHEIF---- 262
Cdd:PRK13391  146 PATP----IADESLGTDM---LYSSGTTGRPKGIKRPLPEQ-----------PPDTPLPLTAFLQRLWGFRSDMVYlspa 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  263 ------------STLCLGGILVLVPeavRQNPFALAEFISQQKI-EKLFLPV--IALLQLAEAVNGNKSTS--------L 319
Cdd:PRK13391  208 plyhsapqravmLVIRLGGTVIVME---HFDAEQYLALIEEYGVtHTQLVPTmfSRMLKLPEEVRDKYDLSslevaihaA 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  320 ALCEViTTGEQMqitpavanlFQKTGAMLHNHYGATEFQDATThtlkGNPEGWptLV---PVGRPLHNVqVYILDEAQQP 396
Cdd:PRK13391  285 APCPP-QVKEQM---------IDWWGPIIHEYYAATEGLGFTA----CDSEEW--LAhpgTVGRAMFGD-LHILDDDGAE 347

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  397 VPLGGEGEFCIGGiGLARGYHNLPDLTNEKFIPNPFGTNenakklyrTGDLArYLPDGTIEHL-GRIDHQVKIRGFRVEL 475
Cdd:PRK13391  348 LPPGEPGTIWFEG-GRPFEYLNDPAKTAEARHPDGTWST--------VGDIG-YVDEDGYLYLtDRAAFMIISGGVNIYP 417

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  476 GEIESVLASHQAVRECAVV-------AREIAGHTQLVGYIIAKdtlnlsfDKLEPILRQYSEAVLPEYMIPTRFINISNM 548
Cdd:PRK13391  418 QEAENLLITHPKVADAAVFgvpnedlGEEVKAVVQPVDGVDPG-------PALAAELIAFCRQRLSRQKCPRSIDFEDEL 490

                         570
                  ....*....|....*.
gi 602182148  549 PLTPSGKLDRRALPDP 564
Cdd:PRK13391  491 PRLPTGKLYKRLLRDR 506

PRK06501

beta-ketoacyl-ACP synthase;

832-1112

1.96e-20

beta-ketoacyl-ACP synthase;

Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 97.01 E-value: 1.96e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  832 ATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISvvvpqkgGYLYEEGMVR--------SQD--- 900
Cdd:PRK06501  155 ADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATD-------GSVSAEALIRfsllsalsTQNdpp 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  901 -GHCRAFDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGAIKmgyTAPSVDGQADV--ISEAIAIADI 977
Cdd:PRK06501  228 eKASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHR---TRSSPDGSPAIgaIRAALADAGL 304

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  978 DASTIGYVEAHGTATQLGDPIEVAGLArafqrstdSVLGKQ--QCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPP 1055
Cdd:PRK06501  305 TPEQIDYINAHGTSTPENDKMEYLGLS--------AVFGERlaSIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPP 376

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 602182148 1056 SLHYANPNPRIDFDATPffvNTelrewSRNGYPRRAGVSSFGVGGTNSHIVLEESPV 1112
Cdd:PRK06501  377 TINYDNPDPAIPLDVVP---NV-----ARDARVTAVLSNSFGFGGQNASLVLTAEPA 425

PRK05952

beta-ketoacyl-ACP synthase;

842-1107

2.11e-20

beta-ketoacyl-ACP synthase;

Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 96.27 E-value: 2.11e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  842 KGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGI-SVVVP------QKGGYLYEEGmvrsqdghCRAFDAEAQGTI 914
Cdd:PRK05952  136 QGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVeAPITPltlagfQQMGALAKTG--------AYPFDRQREGLV 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  915 FGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDgAIKMgyTAPSVDGQADV--ISEAIAIADIDASTIGYVEAHGTAT 992
Cdd:PRK05952  208 LGEGGAILVLESAELAQKRGAKIYGQILGFGLTCD-AYHM--SAPEPDGKSAIaaIQQCLARSGLTPEDIDYIHAHGTAT 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  993 QLGDPIEVAGLARAFqrstdsvlgKQQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPRIDFDATP 1072
Cdd:PRK05952  285 RLNDQREANLIQALF---------PHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPEFDLNFVRQA 355

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 602182148 1073 ffVNTELREwsrngyprrAGVSSFGVGGTNSHIVL 1107
Cdd:PRK05952  356 --QQSPLQN---------VLCLSFGFGGQNAAIAL 379

PRK07470

acyl-CoA synthetase; Validated

32-574

2.15e-20

acyl-CoA synthetase; Validated

Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 98.19 E-value: 2.15e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   32 QAAKR-PDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPAD 110
Cdd:PRK07470   15 QAARRfPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  111 RIEYMLRDSDARILLTSTDVAKKL-ALTIPALQECQTVYLDQEIFEYDFHflaiakllhnqylrllhfyfyTLIQQCQAT 189
Cdd:PRK07470   95 EVAYLAEASGARAMICHADFPEHAaAVRAASPDLTHVVAIGGARAGLDYE---------------------ALVARHLGA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  190 SVSQgiqTQVLPNNLAYCIYTSGSTGNPKGILMEH----------------------RSLVnmlwwhqqTRPSVQGVRTL 247
Cdd:PRK07470  154 RVAN---AAVDHDDPCWFFFTSGTTGRPKAAVLTHgqmafvitnhladlmpgtteqdASLV--------VAPLSHGAGIH 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  248 QFCAVSfdfscheifstlcLGGILVLVPeavrQNPFALAEF---ISQQKIEKLF-LPVI-ALLQLAEAVNGNKSTSLAlc 322
Cdd:PRK07470  223 QLCQVA-------------RGAATVLLP----SERFDPAEVwalVERHRVTNLFtVPTIlKMLVEHPAVDRYDHSSLR-- 283

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  323 EVITTGEQMQITPAVANLfQKTGAMLHNHYGATEFQDATT------HTLKGNPEgwPTLVPVGRPLHNVQVYILDEAQQP 396
Cdd:PRK07470  284 YVIYAGAPMYRADQKRAL-AKLGKVLVQYFGLGEVTGNITvlppalHDAEDGPD--ARIGTCGFERTGMEVQIQDDEGRE 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  397 VPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFgtnenakklyRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELG 476
Cdd:PRK07470  361 LPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF----------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPR 430

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  477 EIESVLASHQAVRECAVVA------REIAghtqlVGYIIAKDTLNLSfdklEPILRQYSEAVLPEYMIPTRFINISNMPL 550
Cdd:PRK07470  431 EIEEKLLTHPAVSEVAVLGvpdpvwGEVG-----VAVCVARDGAPVD----EAELLAWLDGKVARYKLPKRFFFWDALPK 501

                         570       580
                  ....*....|....*....|....*..
gi 602182148  551 TPSGKLDRRALPDP---KGDRPALSTP 574
Cdd:PRK07470  502 SGYGKITKKMVREEleeRGLLDLERAP 528

AACS_like

cd05968

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...

25-574

3.81e-20

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: 97.95 E-value: 3.81e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   25 IHHLFEDQAAKRPDAIALI----DGE-QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCA 99
Cdd:cd05968    63 VEQLLDKWLADTRTRPALRwegeDGTsRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  100 YVPLDVGYPADRIEYMLRDSDARILLTSTDVAKK------LALTIPALQECQTVYldqeifeydfHFLAIAKLLHNQYLR 173
Cdd:cd05968   143 VVPIFSGFGKEAAATRLQDAEAKALITADGFTRRgrevnlKEEADKACAQCPTVE----------KVVVVRHLGNDFTPA 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  174 LLHFYFYTLIQQCQATSVSQgiqtqVLPNNLAYCIYTSGSTGNPKGILMEH-----RSLVNMlwWHQ-QTRPsvqGVRTL 247
Cdd:cd05968   213 KGRDLSYDEEKETAGDGAER-----TESEDPLMIIYTSGTTGKPKGTVHVHagfplKAAQDM--YFQfDLKP---GDLLT 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  248 QFCAVSFDFSCHEIFSTLCLGGILVLVpEAVRQNPFA--LAEFISQQKIEKLFLP---VIALLQLAEA-VNGNKSTSLal 321
Cdd:cd05968   283 WFTDLGWMMGPWLIFGGLILGATMVLY-DGAPDHPKAdrLWRMVEDHEITHLGLSptlIRALKPRGDApVNAHDLSSL-- 359

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  322 cEVI-TTGEQmqITPAVANLFQKTGAMLH----NHYGATEFQDAtthtLKGN-------PEGWPTLVPvgrplhNVQVYI 389
Cdd:cd05968   360 -RVLgSTGEP--WNPEPWNWLFETVGKGRnpiiNYSGGTEISGG----ILGNvlikpikPSSFNGPVP------GMKADV 426

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  390 LDEAQQPVPlGGEGEFCIGG--IGLARGYHNLPDLTNEKFipnpFGTNENakkLYRTGDLARYLPDGTIEHLGRIDHQVK 467
Cdd:cd05968   427 LDESGKPAR-PEVGELVLLApwPGMTRGFWRDEDRYLETY----WSRFDN---VWVHGDFAYYDEEGYFYILGRSDDTIN 498

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  468 IRGFRVELGEIESVLASHQAVRECAV--VAREIAGhTQLVGYIIAKDTLNLSfDKLEPILRQYSEAVLPEYMIPTRFINI 545
Cdd:cd05968   499 VAGKRVGPAEIESVLNAHPAVLESAAigVPHPVKG-EAIVCFVVLKPGVTPT-EALAEELMERVADELGKPLSPERILFV 576

                         570       580       590
                  ....*....|....*....|....*....|....
gi 602182148  546 SNMPLTPSGKLDRRA-----LPDPKGDRPALSTP 574
Cdd:cd05968   577 KDLPKTRNAKVMRRViraayLGKELGDLSSLENP 610

PRK07787

acyl-CoA synthetase; Validated

33-494

3.85e-20

acyl-CoA synthetase; Validated

Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 96.60 E-value: 3.85e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   33 AAKRPDAIALidGEQSLTYGELNVRANHLAQHLLSLgcqpdDLLAICIERSAELFIGLLGILKAGCAYVPL--DVGyPAD 110
Cdd:PRK07787   12 AADIADAVRI--GGRVLSRSDLAGAATAVAERVAGA-----RRVAVLATPTLATVLAVVGALIAGVPVVPVppDSG-VAE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  111 RiEYMLRDSDARILLTSTDvakklaltiPALQECQTVYLDqeifeydfhflaiaklLHNqylRLLHFYfytliqqcqats 190
Cdd:PRK07787   84 R-RHILADSGAQAWLGPAP---------DDPAGLPHVPVR----------------LHA---RSWHRY------------ 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  191 vsqgiqTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNML------WwhQQTRPSVQgVRTLQFcavsfdFSCHE---- 260
Cdd:PRK07787  123 ------PEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLdalaeaW--QWTADDVL-VHGLPL------FHVHGlvlg 187

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  261 IFSTLCLGGILVLVpeaVRQNPFALAEFISQQKIEKLFLP-----VIALLQLAEAVNGNK---STSLALCevittgeqmq 332
Cdd:PRK07787  188 VLGPLRIGNRFVHT---GRPTPEAYAQALSEGGTLYFGVPtvwsrIAADPEAARALRGARllvSGSAALP---------- 254

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  333 iTPAVANLFQKTGAMLHNHYGATEfqdaTTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGE--GEFCIGGI 410
Cdd:PRK07787  255 -VPVFDRLAALTGHRPVERYGMTE----TLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGP 329

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  411 GLARGYHNLPDLTNEKFIPNPFgtnenakklYRTGDLARYLPDGTIEHLGR--IDhQVKIRGFRVELGEIESVLASHQAV 488
Cdd:PRK07787  330 TLFDGYLNRPDATAAAFTADGW---------FRTGDVAVVDPDGMHRIVGResTD-LIKSGGYRIGAGEIETALLGHPGV 399


                  ....*.
gi 602182148  489 RECAVV 494
Cdd:PRK07787  400 REAAVV 405

PRK12406

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

41-564

3.91e-20

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

Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 97.08 E-value: 3.91e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   41 ALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSD 120
Cdd:PRK12406    4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  121 ARILLTSTDVAKKLALTIPALQECQTVYLDQEIfeydfhfLAIAKL-LHNQYLRLLHFYFYTLIQQCQATSVSQGIQTQV 199
Cdd:PRK12406   84 ARVLIAHADLLHGLASALPAGVTVLSVPTPPEI-------AAAYRIsPALLTPPAGAIDWEGWLAQQEPYDGPPVPQPQS 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  200 LpnnlaycIYTSGSTGNPKGI-----LMEH------------------RSLVNMLWWHqqTRPSVQGVRTLQfcavsfdf 256
Cdd:PRK12406  157 M-------IYTSGTTGHPKGVrraapTPEQaaaaeqmraliyglkpgiRALLTGPLYH--SAPNAYGLRAGR-------- 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  257 scheifstlcLGGILVLVPeavRQNPFALAEFISQQKIEKLFL-PV--IALLQLAEAVNGNKSTSlALCEVITTGeqmqi 333
Cdd:PRK12406  220 ----------LGGVLVLQP---RFDPEELLQLIERHRITHMHMvPTmfIRLLKLPEEVRAKYDVS-SLRHVIHAA----- 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  334 TPAVANLFQKT----GAMLHNHYGATEFQDATTHTlkgnPEGW---PTlvPVGRPLHNVQVYILDEAQQPVPLGGEGEFC 406
Cdd:PRK12406  281 APCPADVKRAMiewwGPVIYEYYGSTESGAVTFAT----SEDAlshPG--TVGKAAPGAELRFVDEDGRPLPQGEIGEIY 354

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  407 IGGIGLAR-GYHNLPD----LTNEKFIPnpfgtnenakklyrTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESV 481
Cdd:PRK12406  355 SRIAGNPDfTYHNKPEkraeIDRGGFIT--------------SGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAV 420

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  482 LASHQAVRECAV--VAREIAGHTqLVGYIIAKDTLNLSfdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRR 559
Cdd:PRK12406  421 LHAVPGVHDCAVfgIPDAEFGEA-LMAVVEPQPGATLD----EADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKR 495


                  ....*
gi 602182148  560 ALPDP 564
Cdd:PRK12406  496 RLRDP 500

LC_FACS_like

cd17640

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...

44-482

5.52e-20

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: 96.27 E-value: 5.52e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   44 DGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARI 123
Cdd:cd17640     1 KPPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  124 LLTSTDvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiqtqvlPNN 203
Cdd:cd17640    81 LVVEND-----------------------------------------------------------------------SDD 89

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  204 LAYCIYTSGSTGNPKGILMEHRSL---VNMLWWHQQTRPsvqGVRTLQFCAV--SFDFSChEIFSTLCLGGI-------- 270
Cdd:cd17640    90 LATIIYTSGTTGNPKGVMLTHANLlhqIRSLSDIVPPQP---GDRFLSILPIwhSYERSA-EYFIFACGCSQaytsirtl 165

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  271 -----------LVLVP---EAVRQN---PFALAEFISQqkieKLFLPVIALLQLAEAVNGNKStslalcevittgeqmqI 333
Cdd:cd17640   166 kddlkrvkphyIVSVPrlwESLYSGiqkQVSKSSPIKQ----FLFLFFLSGGIFKFGISGGGA----------------L 225

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  334 TPAVANLFQKTGAMLHNHYGATEfqdaTTHTLKGNPEGWPTLVPVGRPLHNVQVYILD-EAQQPVPLGGEGEFCIGGIGL 412
Cdd:cd17640   226 PPHVDTFFEAIGIEVLNGYGLTE----TSPVVSARRLKCNVRGSVGRPLPGTEIKIVDpEGNVVLPPGEKGIVWVRGPQV 301

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 602182148  413 ARGYHNLPDLTnEKFIpnpfgtneNAKKLYRTGDLARYLPDGTIEHLGRI-DHQVKIRGFRVELGEIESVL 482
Cdd:cd17640   302 MKGYYKNPEAT-SKVL--------DSDGWFNTGDLGWLTCGGELVLTGRAkDTIVLSNGENVEPQPIEEAL 363

YqjQ

COG0300

Short-chain dehydrogenase [General function prediction only];

2536-2693

6.32e-20

Short-chain dehydrogenase [General function prediction only];

Pssm-ID: 440069 [Multi-domain] Cd Length: 252 Bit Score: 91.85 E-value: 6.32e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2536 VARFLVTNGARyLVLVGRRGAREEQQAQlsELEQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVIHAAGTLNDGI 2613
Cdd:COG0300    21 LARALAARGAR-VVLVARDAERLEALAA--ELRAAGARVEVVALDVTDPDAVAALAEAVlaRFGPIDVLVNNAGVGGGGP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2614 LQQQSWQAFKEVMNPKVAGAWNLHILT----KNQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGLA-SYR---RHLGL 2685
Cdd:COG0300    98 FEELDLEDLRRVFEVNVFGPVRLTRALlplmRARGRGRIVNVSSVAGLRGLPGMAAYAASKAALEGFSeSLRaelAPTGV 177


                  ....*...
gi 602182148 2686 PSLSINWG 2693
Cdd:COG0300   178 RVTAVCPG 185

LC_FACL_like

cd05914

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...

42-558

1.08e-19

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: 95.20 E-value: 1.08e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   42 LIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDA 121
Cdd:cd05914     1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  122 RILLTSTdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiqtqvlP 201
Cdd:cd05914    81 KAIFVSD------------------------------------------------------------------------E 88

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  202 NNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCheifstlCLGGILVLVPEA---- 277
Cdd:cd05914    89 DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPL-------TFTLLLPLLNGAhvvf 161

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  278 VRQNPFALAEFISQQK------------IEKLF----LPVIAL----LQLAEAVNGNKSTSLA-----------LCEVIT 326
Cdd:cd05914   162 LDKIPSAKIIALAFAQvtptlgvpvplvIEKIFkmdiIPKLTLkkfkFKLAKKINNRKIRKLAfkkvheafggnIKEFVI 241

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  327 TGEQMQitPAVANLFQKTGAMLHNHYGATEfqdaTTHTLKGNPEGWPTLVPVGRPLHNVQVYILDeaqqPVPLGGEGEFC 406
Cdd:cd05914   242 GGAKIN--PDVEEFLRTIGFPYTIGYGMTE----TAPIISYSPPNRIRLGSAGKVIDGVEVRIDS----PDPATGEGEII 311

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  407 IGGIGLARGYHNLPDLTNEKFIPNPFgtnenakklYRTGDLARYLPDGTIEHLGRIDHQ-VKIRGFRVELGEIESVLASH 485
Cdd:cd05914   312 VRGPNVMKGYYKNPEATAEAFDKDGW---------FHTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNM 382

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  486 QAVRECAVVAREiaGHTQLVGYIIAkDTLNLSFDKLEPILRQYSEAV-------LPEY-------MIPTRFinisnmPLT 551
Cdd:cd05914   383 PFVLESLVVVQE--KKLVALAYIDP-DFLDVKALKQRNIIDAIKWEVrdkvnqkVPNYkkiskvkIVKEEF------EKT 453


                  ....*..
gi 602182148  552 PSGKLDR 558
Cdd:cd05914   454 PKGKIKR 460

PRK05852

fatty acid--CoA ligase family protein;

28-561

1.25e-19

fatty acid--CoA ligase family protein;

Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 95.72 E-value: 1.25e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   28 LFEDQAAKRPDAIALIDGEQ--SLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDV 105
Cdd:PRK05852   21 LVEVAATRLPEAPALVVTADriAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDP 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  106 GYPADRIEYMLRDSDAR-ILLTSTDVAKKLALTIPALQECQTVYLDQEIFE--YDFHFLAIAKLLHnqylrllhfyfytl 182
Cdd:PRK05852  101 ALPIAEQRVRSQAAGARvVLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGgtLSVHLDAATEPTP-------------- 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  183 iqqcqATSVSQGiqtqvLPNNLAYCIYTSGSTGNPKgilmehrslvnML-WWHQQTRPSVQGVRTL-------QFCAVSF 254
Cdd:PRK05852  167 -----ATSTPEG-----LRPDDAMIMFTGGTTGLPK-----------MVpWTHANIASSVRAIITGyrlsprdATVAVMP 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  255 DFSCH----EIFSTLCLGGIlVLVPEAVRqnpFALAEFISQQKIEK----LFLPVI--ALLQLA-EAVNGNKSTSLALCE 323
Cdd:PRK05852  226 LYHGHgliaALLATLASGGA-VLLPARGR---FSAHTFWDDIKAVGatwyTAVPTIhqILLERAaTEPSGRKPAALRFIR 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  324 VITTgeqmQITPAVANLFQKT-GAMLHNHYGATE--FQDATTHTLKGNPEGWPTLV--PVGRPLhNVQVYILDEAQQPVP 398
Cdd:PRK05852  302 SCSA----PLTAETAQALQTEfAAPVVCAFGMTEatHQVTTTQIEGIGQTENPVVStgLVGRST-GAQIRIVGSDGLPLP 376

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  399 LGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFgtnenakklyRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEI 478
Cdd:PRK05852  377 AGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWL----------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERV 446

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  479 ESVLASHQAVRECAVVAREIAGHTQLVG-YIIAKDTLNLSFDKLEPILRQYseavLPEYMIPTRFINISNMPLTPSGKLD 557
Cdd:PRK05852  447 EGVLASHPNVMEAAVFGVPDQLYGEAVAaVIVPRESAPPTAEELVQFCRER----LAAFEIPASFQEASGLPHTAKGSLD 522


                  ....
gi 602182148  558 RRAL 561
Cdd:PRK05852  523 RRAV 526

PRK06145

acyl-CoA synthetase; Validated

33-563

1.57e-19

acyl-CoA synthetase; Validated

Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 94.95 E-value: 1.57e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   33 AAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRI 112
Cdd:PRK06145   12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  113 EYMLRDSDARILLtstdvakklaltipalqecqtvyLDQEifeydfhFLAIAKLLHNQYLRLLHfyfytliQQCQATSVS 192
Cdd:PRK06145   92 AYILGDAGAKLLL-----------------------VDEE-------FDAIVALETPKIVIDAA-------AQADSRRLA 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  193 QG-----IQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLvnmlWWHQQTRPSVQGVRTLQFCAV--------SFDFSCh 259
Cdd:PRK06145  135 QGgleipPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNL----HWKSIDHVIALGLTASERLLVvgplyhvgAFDLPG- 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  260 eiFSTLCLGGILVLVPEAvrqNPFALAEFISQQKIE-KLFLPVI--ALLQLAEAVNGNKSTslaLCEVITTGEQmqiTP- 335
Cdd:PRK06145  210 --IAVLWVGGTLRIHREF---DPEAVLAAIERHRLTcAWMAPVMlsRVLTVPDRDRFDLDS---LAWCIGGGEK---TPe 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  336 ----AVANLFqkTGAMLHNHYGATEFQDATTHTLKGNPegWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIG 411
Cdd:PRK06145  279 srirDFTRVF--TRARYIDAYGLTETCSGDTLMEAGRE--IEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPK 354

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  412 LARGYHNLPDLTNEKFIPNPFgtnenakklyRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVREC 491
Cdd:PRK06145  355 VTKGYWKDPEKTAEAFYGDWF----------RSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEA 424

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 602182148  492 AVV-AREIAGHTQLVGYIIAKDTLNLSFDKlepiLRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALPD 563
Cdd:PRK06145  425 AVIgVHDDRWGERITAVVVLNPGATLTLEA----LDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRD 493

caiC

PRK08008

putative crotonobetaine/carnitine-CoA ligase; Validated

28-561

2.10e-19

putative crotonobetaine/carnitine-CoA ligase; Validated

Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 94.75 E-value: 2.10e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   28 LFEDQAAKRPDAIALI----DGE-QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVP 102
Cdd:PRK08008   12 MWDDLADVYGHKTALIfessGGVvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  103 LDVGYPADRIEYMLRDSDARILLTStdvAKKLALTIPALQECQTVYldQEIFEYDFHFLAIAKLLHnqylrllhfyFYTL 182
Cdd:PRK08008   92 INARLLREESAWILQNSQASLLVTS---AQFYPMYRQIQQEDATPL--RHICLTRVALPADDGVSS----------FTQL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  183 IQQcQATSVSQgiQTQVLPNNLAYCIYTSGSTGNPKGILMEHrslVNMLW------WHQQTRPSVQGVRTLQFCAVsfDF 256
Cdd:PRK08008  157 KAQ-QPATLCY--APPLSTDDTAEILFTSGTTSRPKGVVITH---YNLRFagyysaWQCALRDDDVYLTVMPAFHI--DC 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  257 SCHEIFSTLCLGGILVLVPEavrqnpFALAEFISQQKIEKLFL----PVIA---LLQLAEAVNGNKstslALCEVITTge 329
Cdd:PRK08008  229 QCTAAMAAFSAGATFVLLEK------YSARAFWGQVCKYRATIteciPMMIrtlMVQPPSANDRQH----CLREVMFY-- 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  330 qMQITPAVANLF-QKTGAMLHNHYGATEfqdaTTHTLKGNPEG----WPTlvpVGRPLHNVQVYILDEAQQPVPLGGEGE 404
Cdd:PRK08008  297 -LNLSDQEKDAFeERFGVRLLTSYGMTE----TIVGIIGDRPGdkrrWPS---IGRPGFCYEAEIRDDHNRPLPAGEIGE 368

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  405 FCIGGI---GLARGYHNLPDLTNEKFIPNPFgtnenakkLYrTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESV 481
Cdd:PRK08008  369 ICIKGVpgkTIFKEYYLDPKATAKVLEADGW--------LH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENI 439

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  482 LASHQAVRECAVVAREIAGHTQLV-GYIIAKDTLNLSfdkLEPILrQYSEAVLPEYMIPTrFINI-SNMPLTPSGKLDRR 559
Cdd:PRK08008  440 IATHPKIQDIVVVGIKDSIRDEAIkAFVVLNEGETLS---EEEFF-AFCEQNMAKFKVPS-YLEIrKDLPRNCSGKIIKK 514


                  ..
gi 602182148  560 AL 561
Cdd:PRK08008  515 NL 516

AFD_YhfT-like

cd17633

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...

203-558

2.74e-19

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: 91.70 E-value: 2.74e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  203 NLAYCIYTSGSTGNPKGILMEHRSL-------VNMLWWHQQTRPSVQGvrtlqfcAVSFDFSCHEIFSTLCLGGILVLVP 275
Cdd:cd17633     1 NPFYIGFTSGTTGLPKAYYRSERSWiesfvcnEDLFNISGEDAILAPG-------PLSHSLFLYGAISALYLGGTFIGQR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  276 EAvrqNPFALAEFISQQKIEKLFLpVIALLQLAEAVNGNKSTslalCEVITTGEQM---QITPAVANLFQKtgAMLHNHY 352
Cdd:cd17633    74 KF---NPKSWIRKINQYNATVIYL-VPTMLQALARTLEPESK----IKSIFSSGQKlfeSTKKKLKNIFPK--ANLIEFY 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  353 GATEfqdATTHTLKGNPEGWPTLvPVGRPLHNVQVYILDEAQqpvplGGEGEFCIGgiglargyhnlpdlTNEKFIPNPF 432
Cdd:cd17633   144 GTSE---LSFITYNFNQESRPPN-SVGRPFPNVEIEIRNADG-----GEIGKIFVK--------------SEMVFSGYVR 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  433 GTNENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLVGYIIAKD 512
Cdd:cd17633   201 GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD 280

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 602182148  513 TLNlsfdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDR 558
Cdd:cd17633   281 KLT------YKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320

FACL_like_2

cd05917

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...

209-558

4.18e-19

Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 91.57 E-value: 4.18e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  209 YTSGSTGNPKGILMEHRSLVN-------MLWWHQQTRPSvqgvrtlqfCAVSFdFSCH----EIFSTLCLGGILVLVPEA 277
Cdd:cd05917     9 FTSGTTGSPKGATLTHHNIVNngyfigeRLGLTEQDRLC---------IPVPL-FHCFgsvlGVLACLTHGATMVFPSPS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  278 VrqNPFALAEFISQQKIEKLF-LPV--IALLQLAEAVNGNKSTslaLCEVITTG-----EQMQitpavaNLFQKTGAM-L 348
Cdd:cd05917    79 F--DPLAVLEAIEKEKCTALHgVPTmfIAELEHPDFDKFDLSS---LRTGIMAGapcppELMK------RVIEVMNMKdV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  349 HNHYGATEFQDATTHTLKGNPEGwPTLVPVGRPLHNVQVYILDEAQQPVP-LGGEGEFCIGGIGLARGYHNLPDLTNEKf 427
Cdd:cd05917   148 TIAYGMTETSPVSTQTRTDDSIE-KRVNTVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEKTAEA- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  428 ipnpfgtnENAKKLYRTGDLARYLPDGTIEHLGRIDHQVkIRGfrvelG------EIESVLASHQAVRECAVVAreIAGH 501
Cdd:cd05917   226 --------IDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRG-----GeniyprEIEEFLHTHPKVSDVQVVG--VPDE 289

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  502 T---QLVGYIIAKDTLNLSfdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDR 558
Cdd:cd05917   290 RygeEVCAWIRLKEGAELT----EEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345

Tam

COG4106

Trans-aconitate methyltransferase [Energy production and conversion];

2108-2215

4.18e-19

Trans-aconitate methyltransferase [Energy production and conversion];

Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 84.49 E-value: 4.18e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2108 RGWRILEIGAGTGGTTAYLLPHLPGDQtkYVFTDISAFFLAKAEERFKDypfVRYQVLDIEQAPqaqgFEPQiYDLIVAA 2187
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERFPGAR--VTGVDLSPEMLARARARLPN---VRFVVADLRDLD----PPEP-FDLVVSN 70

                          90       100
                  ....*....|....*....|....*...
gi 602182148 2188 DVLHATSDLRQTLVHIRQLLAPGGMLIL 2215
Cdd:COG4106    71 AALHWLPDHAALLARLAAALAPGGVLAV 98

COG4976

Predicted methyltransferase, contains TPR repeat [General function prediction only];

2094-2221

4.66e-19

Predicted methyltransferase, contains TPR repeat [General function prediction only];

Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 87.36 E-value: 4.66e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2094 QEALLSALEQLPPERGWRILEIGAGTGGTTAYLLPHlpGDqtKYVFTDISAFFLAKAEERFKDypfVRYQVLDIEQAPQa 2173
Cdd:COG4976    32 ALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPR--GY--RLTGVDLSEEMLAKAREKGVY---DRLLVADLADLAE- 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 602182148 2174 qgfEPQIYDLIVAADVLHATSDLRQTLVHIRQLLAPGGMLIL-MEDSEP 2221
Cdd:COG4976   104 ---PDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFsVEDADG 149

PrpE

cd05967

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...

199-561

5.44e-19

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: 93.92 E-value: 5.44e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  199 VLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLqFCA------VSFDFSCheiFSTLCLG---- 268
Cdd:cd05967   227 VAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVW-WAAsdvgwvVGHSYIV---YGPLLHGattv 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  269 ---GILVLVPEavrqnPFALAEFISQQKIEKLFLPVIALLQL----AEAVNGNKSTSLALCEVITTGEQMQItPAVANLF 341
Cdd:cd05967   303 lyeGKPVGTPD-----PGAFWRVIEKYQVNALFTAPTAIRAIrkedPDGKYIKKYDLSSLRTLFLAGERLDP-PTLEWAE 376

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  342 QKTGAMLHNHYGATEfqdaTTHTLKGNPEGWPTLVP----VGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGiGLARGyh 417
Cdd:cd05967   377 NTLGVPVIDHWWQTE----TGWPITANPVGLEPLPIkagsPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKL-PLPPG-- 449

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  418 NLPDL--TNEKFIPNPFGtneNAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVA 495
Cdd:cd05967   450 CLLTLwkNDERFKKLYLS---KFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVG 526

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 602182148  496 R--EIAGHTQLvGYIIAKDTLNLSFDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05967   527 VrdELKGQVPL-GLVVLKEGVKITAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTL 593

PRK03640

o-succinylbenzoate--CoA ligase;

32-561

6.02e-19

o-succinylbenzoate--CoA ligase;

Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 93.10 E-value: 6.02e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   32 QAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADR 111
Cdd:PRK03640   11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  112 IEYMLRDSDARILLTSTDVAKKLALTIPAL-QECQTVYLDQEIFEYDFHFLAIAKLlhnqylrllhfyfytliqqcqats 190
Cdd:PRK03640   91 LLWQLDDAEVKCLITDDDFEAKLIPGISVKfAELMNGPKEEAEIQEEFDLDEVATI------------------------ 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  191 vsqgiqtqvlpnnlaycIYTSGSTGNPKGILM---EHrslvnmlWWHqqtrpsvqgvrtlqfcAVS--FDFSCHEIFSTL 265
Cdd:PRK03640  147 -----------------MYTSGTTGKPKGVIQtygNH-------WWS----------------AVGsaLNLGLTEDDCWL 186

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  266 C------LGGILVLVPEAVRQNPFALAEFISQQKIEKLFLP--------VIALLQ--LAEAVNGNKSTSLAlCEVITTGe 329
Cdd:PRK03640  187 AavpifhISGLSILMRSVIYGMRVVLVEKFDAEKINKLLQTggvtiisvVSTMLQrlLERLGEGTYPSSFR-CMLLGGG- 264

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  330 qmqitPAVANLFQKtgAMLHN-----HYGATE---------FQDATThtlkgnpegwpTLVPVGRPLHNVQVYILDEAQq 395
Cdd:PRK03640  265 -----PAPKPLLEQ--CKEKGipvyqSYGMTEtasqivtlsPEDALT-----------KLGSAGKPLFPCELKIEKDGV- 325

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  396 PVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFgtnenakklyRTGDLArYL-PDGTIEHLGRIDHQVKIRGFRVE 474
Cdd:PRK03640  326 VVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF----------KTGDIG-YLdEEGFLYVLDRRSDLIISGGENIY 394

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  475 LGEIESVLASHQAVRECAVVAREIAGHTQL-VGYIIAKDTLNlsfdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPS 553
Cdd:PRK03640  395 PAEIEEVLLSHPGVAEAGVVGVPDDKWGQVpVAFVVKSGEVT------EEELRHFCEEKLAKYKVPKRFYFVEELPRNAS 468


                  ....*...
gi 602182148  554 GKLDRRAL 561
Cdd:PRK03640  469 GKLLRHEL 476

UbiG

COG2227

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...

2095-2216

8.11e-19

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis

Pssm-ID: 441829 [Multi-domain] Cd Length: 126 Bit Score: 84.68 E-value: 8.11e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2095 EALLSALEQLPPeRGWRILEIGAGTGGTTAYLLPHlpGDQtkYVFTDISAFFLAKAEERFKDYPfVRYQVLDIEQAPqaq 2174
Cdd:COG2227    12 RRLAALLARLLP-AGGRVLDVGCGTGRLALALARR--GAD--VTGVDISPEALEIARERAAELN-VDFVQGDLEDLP--- 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 602182148 2175 gFEPQIYDLIVAADVLHATSDLRQTLVHIRQLLAPGGMLILM 2216
Cdd:COG2227    83 -LEDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLS 123

PRK08974

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

27-563

1.12e-18

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

Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 92.81 E-value: 1.12e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   27 HLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLS-LGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDV 105
Cdd:PRK08974   27 DMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNgLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNP 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  106 GYPADRIEYMLRDSDAR-ILLTS------------TDVaKKLALT-----IPA----LQECQTVYLDQEIFEYDF-HFLA 162
Cdd:PRK08974  107 LYTPRELEHQLNDSGAKaIVIVSnfahtlekvvfkTPV-KHVILTrmgdqLSTakgtLVNFVVKYIKRLVPKYHLpDAIS 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  163 IAKLLHNQYLRllhfyfytliqqcqatsvsQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLV-NMLWWHQQTRPSV 241
Cdd:PRK08974  186 FRSALHKGRRM-------------------QYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLaNLEQAKAAYGPLL 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  242 QGVRTLQFCAVSFdfscHEIF--STLCL-----GGILVLVpeavrQNPFALAEFISQQKIEKlFLPVIALLQLAEAVNGN 314
Cdd:PRK08974  247 HPGKELVVTALPL----YHIFalTVNCLlfielGGQNLLI-----TNPRDIPGFVKELKKYP-FTAITGVNTLFNALLNN 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  315 KS------TSLALceviTTGEQMQITPAVANLFQK-TGAMLHNHYGATE---FQDATTHTLKGNpEGwptlvPVGRPLHN 384
Cdd:PRK08974  317 EEfqeldfSSLKL----SVGGGMAVQQAVAERWVKlTGQYLLEGYGLTEcspLVSVNPYDLDYY-SG-----SIGLPVPS 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  385 VQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEkFIPNPFgtnenakklYRTGDLARYLPDGTIEHLGRIDH 464
Cdd:PRK08974  387 TEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDE-VIKDGW---------LATGDIAVMDEEGFLRIVDRKKD 456

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  465 QVKIRGFRVELGEIESVLASHQAVRECAV--VAREIAGHTQLVgYIIAKDTlNLSFDKLEPILRQYseavLPEYMIPtRF 542
Cdd:PRK08974  457 MILVSGFNVYPNEIEDVVMLHPKVLEVAAvgVPSEVSGEAVKI-FVVKKDP-SLTEEELITHCRRH----LTGYKVP-KL 529

                         570       580
                  ....*....|....*....|..
gi 602182148  543 INISN-MPLTPSGKLDRRALPD 563
Cdd:PRK08974  530 VEFRDeLPKSNVGKILRRELRD 551

FADD10

cd17635

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...

208-558

1.23e-18

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: 90.01 E-value: 1.23e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  208 IYTSGSTGNPKGILMEHRSLV---NMLWWHQQTrpSVQGVRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEavRQNPFA 284
Cdd:cd17635     7 IFTSGTTGEPKAVLLANKTFFavpDILQKEGLN--WVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGE--NTTYKS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  285 LAEFISQQKIEKLFLPVIALLQLaeaVNGNKSTsLALCE---VITTGEQMQITPAVANLFQKTGAMLHNHYGATEfqdAT 361
Cdd:cd17635    83 LFKILTTNAVTTTCLVPTLLSKL---VSELKSA-NATVPslrLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSE---TG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  362 THTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFgtnenakkl 441
Cdd:cd17635   156 TALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV--------- 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  442 yRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLVGYIIAK---DTLNLSF 518
Cdd:cd17635   227 -NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAsaeLDENAIR 305

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 602182148  519 DKLEPILRQyseavLPEYMIPTRFINISNMPLTPSGKLDR 558
Cdd:cd17635   306 ALKHTIRRE-----LEPYARPSTIVIVTDIPRTQSGKVKR 340

PLN02330

4-coumarate--CoA ligase-like 1

38-563

1.32e-18

4-coumarate--CoA ligase-like 1

Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 92.35 E-value: 1.32e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   38 DAIALIDGE--QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYM 115
Cdd:PLN02330   43 DKVAFVEAVtgKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQ 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  116 LRDSDARILLTS-TDVAKKLALTIPalqecqTVYLDQEIFEYDFHFlaiAKLLHNQylrllhfyfytliQQCQATSVSQg 194
Cdd:PLN02330  123 AEAAGAKLIVTNdTNYGKVKGLGLP------VIVLGEEKIEGAVNW---KELLEAA-------------DRAGDTSDNE- 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  195 iqtQVLPNNLAYCIYTSGSTGNPKGILMEHRSLV-NMLWWHQQTRPSVQG-VRTLQFcaVSFdFSCHEI----FSTLCLG 268
Cdd:PLN02330  180 ---EILQTDLCALPFSSGTTGISKGVMLTHRNLVaNLCSSLFSVGPEMIGqVVTLGL--IPF-FHIYGItgicCATLRNK 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  269 GILVLVpeavrqNPFALAEF----ISQQ-KIEKLFLPVIALLQLAEAVNGNKSTSLALCEVITTGEQMqiTPAVANLFQK 343
Cdd:PLN02330  254 GKVVVM------SRFELRTFlnalITQEvSFAPIVPPIILNLVKNPIVEEFDLSKLKLQAIMTAAAPL--APELLTAFEA 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  344 T--GAMLHNHYGATEFQDAT-THtlkGNPE---GWPTLVPVGRPLHNVQVYILD-EAQQPVPLGGEGEFCIGGIGLARGY 416
Cdd:PLN02330  326 KfpGVQVQEAYGLTEHSCITlTH---GDPEkghGIAKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGY 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  417 HNLPDLTNEKFipnpfgtneNAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVV-- 494
Cdd:PLN02330  403 YNNKEETDRTI---------DEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVpl 473

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  495 AREIAGHTQLVGYIIAKDtlnlSFDKLEPILrQYSEAVLPEYMiPTRFIN-ISNMPLTPSGKLDRRALPD 563
Cdd:PLN02330  474 PDEEAGEIPAACVVINPK----AKESEEDIL-NFVAANVAHYK-KVRVVQfVDSIPKSLSGKIMRRLLKE 537

PtmA

cd17636

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...

208-494

1.58e-18

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: 89.67 E-value: 1.58e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  208 IYTSGSTGNPKGILMEHRSL----VNMLWWHQQTRPSV---QG----VRTLQFCavsfdfscheiFSTLCLGGILVLVPe 276
Cdd:cd17636     6 IYTAAFSGRPNGALLSHQALlaqaLVLAVLQAIDEGTVflnSGplfhIGTLMFT-----------LATFHAGGTNVFVR- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  277 avRQNPFALAEFISQQKIEKLFLPVIALLQLAEAvNGNKSTSLALCEVITT--GEQMQITPAVANLFQKTGAmlhnhYGA 354
Cdd:cd17636    74 --RVDAEEVLELIEAERCTHAFLLPPTIDQIVEL-NADGLYDLSSLRSSPAapEWNDMATVDTSPWGRKPGG-----YGQ 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  355 TE-FQDATTHTLKGNPEGwptlvPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFipnpfg 433
Cdd:cd17636   146 TEvMGLATFAALGGGAIG-----GAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT------ 214

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 602182148  434 tnenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVV 494
Cdd:cd17636   215 ----RGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVI 271

PRK04319

acetyl-CoA synthetase; Provisional

36-573

3.02e-18

acetyl-CoA synthetase; Provisional

Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 91.50 E-value: 3.02e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   36 RPDAIALI----DGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADR 111
Cdd:PRK04319   57 RKDKVALRyldaSRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEA 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  112 IEYMLRDSDARILLTSTDV-AKKLALTIPALqecQTVYLDQEIFEYDFHFLAIAKLLhnqylrllhfyfytliqqcQATS 190
Cdd:PRK04319  137 VRDRLEDSEAKVLITTPALlERKPADDLPSL---KHVLLVGEDVEEGPGTLDFNALM-------------------EQAS 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  191 VSQGIqTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNmlwwHQQTRPSVQgvrtlqfcavsfDFscHE---------- 260
Cdd:PRK04319  195 DEFDI-EWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQ----HYQTGKYVL------------DL--HEddvywctadp 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  261 ---------IFSTLCLGGILVLVpeAVRQNPFALAEFISQQKIEKLFLPVIALLQL----AEAVNGNKSTSLALC----- 322
Cdd:PRK04319  256 gwvtgtsygIFAPWLNGATNVID--GGRFSPERWYRILEDYKVTVWYTAPTAIRMLmgagDDLVKKYDLSSLRHIlsvge 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  323 ----EVITTGEQMQITPAVANLFQ-KTGAMLHNHYGATEFQDATthtlkgnpegwptlvpVGRPLHNVQVYILDEAQQPV 397
Cdd:PRK04319  334 plnpEVVRWGMKVFGLPIHDNWWMtETGGIMIANYPAMDIKPGS----------------MGKPLPGIEAAIVDDQGNEL 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  398 PLGGEGEFCI--GGIGLARGYHNLPDLTNEKFIPNpfgtnenakkLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVEL 475
Cdd:PRK04319  398 PPNRMGNLAIkkGWPSMMRGIWNNPEKYESYFAGD----------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGP 467

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  476 GEIESVLASHQAVRECAVvareIAGHTQLVGYII-AKDTLNLSF---DKLEPILRQYSEAVLPEYMIPTRFINISNMPLT 551
Cdd:PRK04319  468 FEVESKLMEHPAVAEAGV----IGKPDPVRGEIIkAFVALRPGYepsEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKT 543

                         570       580
                  ....*....|....*....|....*..
gi 602182148  552 PSGKLDRRALPD-----PKGDrpaLST 573
Cdd:PRK04319  544 RSGKIMRRVLKAwelglPEGD---LST 567

OSB_CoA_lg

cd05912

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...

48-561

5.32e-18

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: 89.33 E-value: 5.32e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   48 SLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDarillts 127
Cdd:cd05912     1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSD------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  128 tdVAKKLALTIpalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiqtqvlpnnlayc 207
Cdd:cd05912    74 --VKLDDIATI--------------------------------------------------------------------- 82

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  208 IYTSGSTGNPKGILMEHRslvnMLWWHqqtrpSVQGVRTLQF-------CAVS-FDFSCHEI-FSTLCLGGILVLVPeav 278
Cdd:cd05912    83 MYTSGTTGKPKGVQQTFG----NHWWS-----AIGSALNLGLteddnwlCALPlFHISGLSIlMRSVIYGMTVYLVD--- 150

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  279 RQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALceVITTGEqmqitPAVANLF---QKTGAMLHNHYGAT 355
Cdd:cd05912   151 KFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRC--ILLGGG-----PAPKPLLeqcKEKGIPVYQSYGMT 223

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  356 EfqdATTHTLKGNPEGWPT-LVPVGRPLHNVQVYILDEAQQPvplGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFgt 434
Cdd:cd05912   224 E---TCSQIVTLSPEDALNkIGSAGKPLFPVELKIEDDGQPP---YEVGEILLKGPNVTKGYLNRPDATEESFENGWF-- 295

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  435 nenakklyRTGDLArYL-PDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQL-VGYIIAKD 512
Cdd:cd05912   296 --------KTGDIG-YLdEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVpVAFVVSER 366

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 602182148  513 TlnLSFDKLEPILRQYseavLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05912   367 P--ISEEELIAYCSEK----LAKYKVPKKIYFVDELPRTASGKLLRHEL 409

PRK09185

beta-ketoacyl-ACP synthase;

839-1107

8.70e-18

beta-ketoacyl-ACP synthase;

Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 88.36 E-value: 8.70e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  839 LNLKGPSVNVQTACSTSlVAVHMACQSLI-SGECQMALAGGI---------------SVvvpqkggylyeegmvrsQDGH 902
Cdd:PRK09185  147 LGLSGPAYTISTACSSS-AKVFASARRLLeAGLCDAAIVGGVdslcrltlngfnsleSL-----------------SPQP 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  903 CRAFDAEAQGTIFGNGGGLVLLKRLQDAlddndnimAVIKATAINNDGAIKMGYTAPSVDGQADVISEAIAIADIDASTI 982
Cdd:PRK09185  209 CRPFSANRDGINIGEAAAFFLLEREDDA--------AVALLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADI 280

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  983 GYVEAHGTATQLGDPIEVAGLARAFQRSTdsvlgkqqcAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANP 1062
Cdd:PRK09185  281 GYINLHGTATPLNDAMESRAVAAVFGDGV---------PCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQP 351

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 602182148 1063 NPriDFDATPFFVNTELREwsrngyPRRAGVSSFGVGGTNSHIVL 1107
Cdd:PRK09185  352 DP--ALPPLYLVENAQALA------IRYVLSNSFAFGGNNCSLIF 388

AcpA

COG3433

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...

369-656

1.27e-17

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];

Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 86.34 E-value: 1.27e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  369 PEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEfcIGGIGLARGYHNLPDLTNEKFIPNPFGTNENAKKLYRTGDLA 448
Cdd:COG3433    11 PTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGE--GGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLRLL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  449 RYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLVGYIIAKDTLNLSFdklepILRQY 528
Cdd:COG3433    89 LRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAA-----AAALA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  529 SEAVLPEYMIPTRFINISNMPLTPSGKLDRRALPDPKGDRPALSTPLVKPRT---QTEKRLAEIWGSYLAVDI--VGTHD 603
Cdd:COG3433   164 ALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALetaLTEEELRADVAELLGVDPeeIDPDD 243

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 602182148  604 NFFDLGGTSLLLTQahkfLCETFN---INLSAVSLFQYPTIQTLAQYIDCQGDTTS 656
Cdd:COG3433   244 NLFDLGLDSIRLMQ----LVERWRkagLDVSFADLAEHPTLAAWWALLAAAQAAAA 295

Methyltransf_25

pfam13649

Methyltransferase domain; This family appears to be a methyltransferase domain.

2112-2211

1.39e-17

Methyltransferase domain; This family appears to be a methyltransferase domain.

Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 79.92 E-value: 1.39e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  2112 ILEIGAGTGGTTAYLLPHLPGdqtKYVFTDISAFFLAKAEERFKDYPF-VRYQVLDIEQAPqaqgFEPQIYDLIVAADVL 2190
Cdd:pfam13649    1 VLDLGCGTGRLTLALARRGGA---RVTGVDLSPEMLERARERAAEAGLnVEFVQGDAEDLP----FPDGSFDLVVSSGVL 73

                           90       100
                   ....*....|....*....|...
gi 602182148  2191 HATS--DLRQTLVHIRQLLAPGG 2211
Cdd:pfam13649   74 HHLPdpDLEAALREIARVLKPGG 96

PRK09274

peptide synthase; Provisional

26-505

1.97e-17

peptide synthase; Provisional

Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 88.80 E-value: 1.97e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   26 HHLfEDQAAKRPDAIALIDGE----------QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILK 95
Cdd:PRK09274   10 RHL-PRAAQERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFK 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   96 AGCAYVPLDVGYPADRIEYMLRDSDARILLTstdvakklaltIPALQecqtvyLDQEIFEYDF----HFLAIAKllhnqy 171
Cdd:PRK09274   89 AGAVPVLVDPGMGIKNLKQCLAEAQPDAFIG-----------IPKAH------LARRLFGWGKpsvrRLVTVGG------ 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  172 lRLLHF-YFYTLIQQCQATSVSQGIQTQvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRtlqfc 250
Cdd:PRK09274  146 -RLLWGgTTLATLLRDGAAAPFPMADLA--PDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEI----- 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  251 avsfDFSCHEIFS--TLCLGGILVlVPEA-----VRQNPFALAEFISQQKIEKLFL-PviALLQ-LAEAVNGNKSTSLAL 321
Cdd:PRK09274  218 ----DLPTFPLFAlfGPALGMTSV-IPDMdptrpATVDPAKLFAAIERYGVTNLFGsP--ALLErLGRYGEANGIKLPSL 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  322 CEVITTGEqmQITPAVANLFQKT---GAMLHNHYGATE------------FQDATTHTLKGnpEGwptlVPVGRPLHNVQ 386
Cdd:PRK09274  291 RRVISAGA--PVPIAVIERFRAMlppDAEILTPYGATEalpissiesreiLFATRAATDNG--AG----ICVGRPVDGVE 362

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  387 VYILD---------EAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPfgtneNAKKLYRTGDLARYLPDGTIE 457
Cdd:PRK09274  363 VRIIAisdapipewDDALRLATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDG-----QGDVWHRMGDLGYLDAQGRLW 437

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 602182148  458 HLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLV 505
Cdd:PRK09274  438 FCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVPGAQRPV 485

PLN02574

4-coumarate--CoA ligase-like

23-563

7.88e-17

4-coumarate--CoA ligase-like

Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 86.82 E-value: 7.88e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   23 SCIHHLFedQAAKRPDAIALIDGEQ--SLTYGELNVRANHLAQHLL-SLGCQPDDLLAICIERSAELFIGLLGILKAGCA 99
Cdd:PLN02574   41 DAVSFIF--SHHNHNGDTALIDSSTgfSISYSELQPLVKSMAAGLYhVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGI 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  100 YVPLDVGYPADRIEYMLRDSDARILLTSTDVAKKL-ALTIPALQECQTVYLDQEIFEYDfhflaiakllhnqylrllhfY 178
Cdd:PLN02574  119 VTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLsPLGVPVIGVPENYDFDSKRIEFP--------------------K 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  179 FYTLIQQ----CQATSVSQgiqtqvlpNNLAYCIYTSGSTGNPKGILMEHRSLVNMlwwhqqtrpsvqgVRT-LQFCAVS 253
Cdd:PLN02574  179 FYELIKEdfdfVPKPVIKQ--------DDVAAIMYSSGTTGASKGVVLTHRNLIAM-------------VELfVRFEASQ 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  254 FDFS------------CHEIFSTLCLGGILVLVPEAVRQNPFALAEFIsqQKIEKL---FLPVI-----ALLQLAEAVNG 313
Cdd:PLN02574  238 YEYPgsdnvylaalpmFHIYGLSLFVVGLLSLGSTIVVMRRFDASDMV--KVIDRFkvtHFPVVppilmALTKKAKGVCG 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  314 NKSTSLAlcevittgeqmQITPAVANLFQKT-----GAMLH----NHYGATEFQDATTHTLkgNPEGWPTLVPVGRPLHN 384
Cdd:PLN02574  316 EVLKSLK-----------QVSCGAAPLSGKFiqdfvQTLPHvdfiQGYGMTESTAVGTRGF--NTEKLSKYSSVGLLAPN 382

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  385 VQVYILD-EAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFgtnenakklYRTGDLARYLPDGTIEHLGRID 463
Cdd:PLN02574  383 MQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW---------LRTGDIAYFDEDGYLYIVDRLK 453

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  464 HQVKIRGFRVELGEIESVLASHQAVRECAV--VAREIAGHTQlVGYIIAKDTLNLSfdkLEPILRQYSEAVLPeYMIPTR 541
Cdd:PLN02574  454 EIIKYKGFQIAPADLEAVLISHPEIIDAAVtaVPDKECGEIP-VAFVVRRQGSTLS---QEAVINYVAKQVAP-YKKVRK 528

                         570       580
                  ....*....|....*....|..
gi 602182148  542 FINISNMPLTPSGKLDRRALPD 563
Cdd:PLN02574  529 VVFVQSIPKSPAGKILRRELKR 550

PRK09088

acyl-CoA synthetase; Validated

32-563

1.49e-16

acyl-CoA synthetase; Validated

Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 85.63 E-value: 1.49e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   32 QAAKRPDAIALID--GEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPA 109
Cdd:PRK09088    4 HARLQPQRLAAVDlaLGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  110 DRIEYMLRDSDARILLTSTDVAkklALTipalqeCQTVYLDQEIFEYDFHFLAIAKLLHnqylrllhfyfytliqqcqat 189
Cdd:PRK09088   84 SELDALLQDAEPRLLLGDDAVA---AGR------TDVEDLAAFIASADALEPADTPSIP--------------------- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  190 svsqgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSL----VNMLWWHQQTRPSVQGVRTLQFCAVSFDFScheIFSTL 265
Cdd:PRK09088  134 -----------PERVSLILFTSGTSGQPKGVMLSERNLqqtaHNFGVLGRVDAHSSFLCDAPMFHIIGLITS---VRPVL 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  266 CLGGILVLVP--EAVRqnpfALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLA-LCEVITTGEQMQITPAVANLFQ 342
Cdd:PRK09088  200 AVGGSILVSNgfEPKR----TLGRLGDPALGITHYFCVPQMAQAFRAQPGFDAAALRhLTALFTGGAPHAAEDILGWLDD 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  343 ktGAMLHNHYGATE----FQDATTHTLKGNPEGwptlvPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHN 418
Cdd:PRK09088  276 --GIPMVDGFGMSEagtvFGMSVDCDVIRAKAG-----AAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWR 348

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  419 LPDLTNEKFipnpfgtneNAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREI 498
Cdd:PRK09088  349 RPQATARAF---------TGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMAD 419

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 602182148  499 AGHTQlVGYIIAKDTLNLSFDkLEPIlRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALPD 563
Cdd:PRK09088  420 AQWGE-VGYLAIVPADGAPLD-LERI-RSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRD 481

MACS_like_1

cd05974

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...

209-561

2.51e-16

Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 84.54 E-value: 2.51e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  209 YTSGSTGNPKGILMEHRS-----LVNMLWWHQQTRPSVQGVRTLQFCAVSFdfSCheIFSTLCLGGILVLVPEAvRQNPF 283
Cdd:cd05974    92 FTSGTTSKPKLVEHTHRSypvghLSTMYWIGLKPGDVHWNISSPGWAKHAW--SC--FFAPWNAGATVFLFNYA-RFDAK 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  284 ALAEFISQQKIEKLFLPVIALLQLAEAvnGNKSTSLALCEVITTGEQMQitPAVANLFQKT-GAMLHNHYGATEfqdatT 362
Cdd:cd05974   167 RVLAALVRYGVTTLCAPPTVWRMLIQQ--DLASFDVKLREVVGAGEPLN--PEVIEQVRRAwGLTIRDGYGQTE-----T 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  363 HTLKGNPEGWPTLV-PVGRPLHNVQVYILDEAQQPVplgGEGEFCIG-----GIGLARGYHNLPDLTNEKFipnpfgtne 436
Cdd:cd05974   238 TALVGNSPGQPVKAgSMGRPLPGYRVALLDPDGAPA---TEGEVALDlgdtrPVGLMKGYAGDPDKTAHAM--------- 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  437 nAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAreiaghtqlvgyiiAKDTLNL 516
Cdd:cd05974   306 -RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVP--------------SPDPVRL 370

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 602182148  517 SFDKLEPILRQYSEAV----------LPEYMIP---TRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05974   371 SVPKAFIVLRAGYEPSpetaleifrfSRERLAPykrIRRLEFAELPKTISGKIRRVEL 428

PRK14691

3-oxoacyl-(acyl carrier protein) synthase II; Provisional

832-1108

2.74e-16

3-oxoacyl-(acyl carrier protein) synthase II; Provisional

Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 83.24 E-value: 2.74e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  832 ATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVP--QKGGYLYEEGMV----RSQDGHCRA 905
Cdd:PRK14691   71 AGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDtvSLAGFAAARALSthfnSTPEKASRP 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  906 FDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDgAIKMGYTAPSVDGQADVISEAIAIADIDASTIGYV 985
Cdd:PRK14691  151 FDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSAD-AYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHL 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  986 EAHGTATQLGDPIEVAGLARAFQRStdsvlgkQQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPR 1065
Cdd:PRK14691  230 NAHATSTPVGDLGEINAIKHLFGES-------NALAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPA 302

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 602182148 1066 ------IDFDATPFFVNTELrewsRNGyprragvssFGVGGTNSHIVLE 1108
Cdd:PRK14691  303 akglniIAGNAQPHDMTYAL----SNG---------FGFAGVNASILLK 338

PRK08279

long-chain-acyl-CoA synthetase; Validated

29-233

3.08e-16

long-chain-acyl-CoA synthetase; Validated

Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 85.31 E-value: 3.08e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   29 FEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYP 108
Cdd:PRK08279   43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQR 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  109 ADRIEYMLRDSDARILLTSTDVAKKLALTIPALQECQTVYLDQEIFEYDFH-FLAIAKLLHNqylrllhfyfytliqQCQ 187
Cdd:PRK08279  123 GAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDDPEgYEDLAAAAAG---------------APT 187

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 602182148  188 ATSVSQGiqtQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWW 233
Cdd:PRK08279  188 TNPASRS---GVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGG 230

FACL_like_5

cd05924

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...

206-559

6.86e-16

Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 82.04 E-value: 6.86e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  206 YCIYTSGSTGNPKGILMEHRSLVNML--------------WWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTLCLGGIL 271
Cdd:cd05924     7 YILYTGGTTGMPKGVMWRQEDIFRMLmggadfgtgeftpsEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  272 VLVpeAVRQNPFALAEFISQQKIEKLFLPVIALLQ-LAEAVNGNKSTSL-ALCEVITTGEQMqiTPAVANLFQ--KTGAM 347
Cdd:cd05924    87 VLP--DDRFDPEEVWRTIEKHKVTSMTIVGDAMARpLIDALRDAGPYDLsSLFAISSGGALL--SPEVKQGLLelVPNIT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  348 LHNHYGATEFQDATTHTLKGNPEGWPTLVPVGrplHNVQVyiLDEAQQPVPLGGEGEFCIGGIGL-ARGYHNLPDLTNEK 426
Cdd:cd05924   163 LVDAFGSSETGFTGSGHSAGSGPETGPFTRAN---PDTVV--LDDDGRVVPPGSGGVGWIARRGHiPLGYYGDEAKTAET 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  427 FIpnpfgTNENAKKLYrTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLVG 506
Cdd:cd05924   238 FP-----EVDGVRYAV-PGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVV 311

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 602182148  507 YIIAKDT-LNLSFDKLEPILRQyseaVLPEYMIPTRFINISNMPLTPSGKLDRR 559
Cdd:cd05924   312 AVVQLREgAGVDLEELREHCRT----RIARYKLPKQVVFVDEIERSPAGKADYR 361

PRK08315

AMP-binding domain protein; Validated

16-555

1.36e-15

AMP-binding domain protein; Validated

Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 82.94 E-value: 1.36e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   16 TQSEFPDSCIHHLFEDQAAKRPDAIALIDGEQSL--TYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGI 93
Cdd:PRK08315    9 TDVPLLEQTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFAT 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   94 LKAGCAYVPLDVGYPADRIEYMLRDSDARILLT-----STDVAKKLALTIPALQECQ--------------TVYLDQEIF 154
Cdd:PRK08315   89 AKIGAILVTINPAYRLSELEYALNQSGCKALIAadgfkDSDYVAMLYELAPELATCEpgqlqsarlpelrrVIFLGDEKH 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  155 EYDFHFLAIAKLLHNQYLRLLhfyfytliQQCQAT-SVSQGIQTQvlpnnlayciYTSGSTGNPKGILMEHRSLVNMLWW 233
Cdd:PRK08315  169 PGMLNFDELLALGRAVDDAEL--------AARQATlDPDDPINIQ----------YTSGTTGFPKGATLTHRNILNNGYF 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  234 hqqtrpsvqgV-RTLQF-------CAVSFdFSCheiF----STL-CL--GGILVLVPEAVrqNPFALAEFISQQKIEKLF 298
Cdd:PRK08315  231 ----------IgEAMKLteedrlcIPVPL-YHC---FgmvlGNLaCVthGATMVYPGEGF--DPLATLAAVEEERCTALY 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  299 -LPV--IALLQLAEAVNGNKStSL-------ALC------EVIttgEQM---QITPAvanlfqktgamlhnhYGATE--- 356
Cdd:PRK08315  295 gVPTmfIAELDHPDFARFDLS-SLrtgimagSPCpievmkRVI---DKMhmsEVTIA---------------YGMTEtsp 355

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  357 --FQDATTHTLKGNPEgwpTlvpVGRPLHNVQVYILD-EAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFg 433
Cdd:PRK08315  356 vsTQTRTDDPLEKRVT---T---VGRALPHLEVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGW- 428

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  434 tnenakklYRTGDLARYLPDGTIEHLGRIDHQVkIRGfrvelG------EIESVLASHQAVRECAV--VAREIAGHtQLV 505
Cdd:PRK08315  429 --------MHTGDLAVMDEEGYVNIVGRIKDMI-IRG-----GeniyprEIEEFLYTHPKIQDVQVvgVPDEKYGE-EVC 493

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|
gi 602182148  506 GYIIAKDTLNLSFDKlepiLRQYSEAVLPEYMIPTRFINISNMPLTPSGK 555
Cdd:PRK08315  494 AWIILRPGATLTEED----VRDFCRGKIAHYKIPRYIRFVDEFPMTVTGK 539

PRK13383

acyl-CoA synthetase; Provisional

33-562

1.91e-15

acyl-CoA synthetase; Provisional

Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 82.35 E-value: 1.91e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   33 AAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRI 112
Cdd:PRK13383   45 AARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDAL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  113 EYMLRDSDARILLTSTDVAKKLALTIPALqecqtvyldqeifeydfhflaiakllhnqylrllhfyfyTLIQQCQATSVS 192
Cdd:PRK13383  125 AAALRAHHISTVVADNEFAERIAGADDAV---------------------------------------AVIDPATAGAEE 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  193 QGIQTQVLPNNlAYCIYTSGSTGNPKGILMEHRSLVNMLWW---HQQTR---PSVQGVRTLQFCAVSFDFscheIFSTLC 266
Cdd:PRK13383  166 SGGRPAVAAPG-RIVLLTSGTTGKPKGVPRAPQLRSAVGVWvtiLDRTRlrtGSRISVAMPMFHGLGLGM----LMLTIA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  267 LGGILVLVPEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSlALCEVITTGEQMQitPAVANLFQKT-G 345
Cdd:PRK13383  241 LGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVLARILELPPRVRARNPLP-QLRVVMSSGDRLD--PTLGQRFMDTyG 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  346 AMLHNHYGATEF---QDATTHTLKGNPEgwptlvPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNlpdl 422
Cdd:PRK13383  318 DILYNGYGSTEVgigALATPADLRDAPE------TVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTD---- 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  423 tnekfipnpFGTNENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAV--VAREIAG 500
Cdd:PRK13383  388 ---------GGGKAVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVigVPDERFG 458

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 602182148  501 HtQLVGYIIAKDTLNLSFDKlepiLRQYSEAVLPEYMIPtRFINI-SNMPLTPSGKLDRRALP 562
Cdd:PRK13383  459 H-RLAAFVVLHPGSGVDAAQ----LRDYLKDRVSRFEQP-RDINIvSSIPRNPTGKVLRKELP 515

FabG

COG1028

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...

2536-2677

1.99e-15

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis

Pssm-ID: 440651 [Multi-domain] Cd Length: 249 Bit Score: 78.67 E-value: 1.99e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2536 VARFLVTNGARyLVLVGRRGAREEQQAQlsELEQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVIHAAGTLNDGI 2613
Cdd:COG1028    22 IARALAAEGAR-VVITDRDAEALEAAAA--ELRAAGGRALAVAADVTDEAAVEALVAAAvaAFGRLDILVNNAGITPPGP 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2614 LQQQSWQAFKEVMNPKVAGAWNL------HILTKNQPLdfFVLFSSATSLLGNAGQANHAAANAFLDGLA 2677
Cdd:COG1028    99 LEELTEEDWDRVLDVNLKGPFLLtraalpHMRERGGGR--IVNISSIAGLRGSPGQAAYAASKAAVVGLT 166

PRK07967

beta-ketoacyl-ACP synthase I;

904-1107

8.34e-15

beta-ketoacyl-ACP synthase I;

Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 79.33 E-value: 8.34e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  904 RAFDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGAiKMgyTAPSvdGQADVISEAIAIADIDAStIG 983
Cdd:PRK07967  219 RAYDANRDGFVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGY-DM--VAPS--GEGAVRCMQMALATVDTP-ID 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  984 YVEAHGTATQLGDPIEVAGLARAFqrstdsvlGKQQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPN 1063
Cdd:PRK07967  293 YINTHGTSTPVGDVKELGAIREVF--------GDKSPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELD 364

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 602182148 1064 PriDFDATPFfvnteLREWSRNGYPRRAGVSSFGVGGTNSHIVL 1107
Cdd:PRK07967  365 P--QAAGMPI-----VTETTDNAELTTVMSNSFGFGGTNATLVF 401

MACS_euk

cd05928

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...

31-563

1.01e-14

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: 80.20 E-value: 1.01e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   31 DQAAKRPDAIAL--IDG---EQSLTYGELNVRANHLAqHLLSLGC--QPDDLLAICIERSAELFIGLLGILKAGCAYVPL 103
Cdd:cd05928    19 EKAGKRPPNPALwwVNGkgdEVKWSFRELGSLSRKAA-NVLSGACglQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  104 DVGYPADRIEYMLRDSDARILLTSTDVAKKL---ALTIPALQecqtvyldqeifeydfhflaiAKLLHNQYLRLLHFYFY 180
Cdd:cd05928    98 TIQLTAKDILYRLQASKAKCIVTSDELAPEVdsvASECPSLK---------------------TKLLVSEKSRDGWLNFK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  181 TLIQQcqATSVSQGIQTQVLPNNLAYciYTSGSTGNPKGILMEHRSL-----VNMLWWHQQTRPSVQGVRTLQFCAVSFD 255
Cdd:cd05928   157 ELLNE--ASTEHHCVETGSQEPMAIY--FTSGTTGSPKMAEHSHSSLglglkVNGRYWLDLTASDIMWNTSDTGWIKSAW 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  256 FScheIFSTLCLGGIlVLVPEAVRQNPFALAEFISQQKIEKLF-LPVIALLQLAEAVNGNKSTSLALCevITTGEQmqIT 334
Cdd:cd05928   233 SS---LFEPWIQGAC-VFVHHLPRFDPLVILKTLSSYPITTFCgAPTVYRMLVQQDLSSYKFPSLQHC--VTGGEP--LN 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  335 PAVANLFQ-KTGAMLHNHYGATEfqdatTHTLKGNPEGW---PTLVPVGRPLHNVQvyILDEAQQPVPLGGEGEFCIggi 410
Cdd:cd05928   305 PEVLEKWKaQTGLDIYEGYGQTE-----TGLICANFKGMkikPGSMGKASPPYDVQ--IIDDNGNVLPPGTEGDIGI--- 374

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  411 glaRGYHNLPDLTNEKFIPNPFGTNENAK-KLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVR 489
Cdd:cd05928   375 ---RVKPIRPFGLFSGYVDNPEKTAATIRgDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVV 451

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 602182148  490 ECAVVAR--EIAGHTQLVGYIIAKDTLNLSFDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALPD 563
Cdd:cd05928   452 ESAVVSSpdPIRGEVVKAFVVLAPQFLSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527

PRK09116

beta-ketoacyl-ACP synthase;

832-1065

1.31e-14

beta-ketoacyl-ACP synthase;

Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 78.88 E-value: 1.31e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  832 ATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQkggylyeEGMV---------RSQDGH 902
Cdd:PRK09116  144 AVNVGLFFGLKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPT-------EAAVfdtlfatstRNDAPE 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  903 C--RAFDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGAikmGYTAPSVDGQADVISEAIAIADIDAS 980
Cdd:PRK09116  217 LtpRPFDANRDGLVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGA---HVTQPQAETMQIAMELALKDAGLAPE 293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  981 TIGYVEAHGTATQLGDPIEvaglarafQRSTDSVLGKQQcAIGSVKTNIGHldeAAGIAGLIKAALALQY---GQIPPSL 1057
Cdd:PRK09116  294 DIGYVNAHGTATDRGDIAE--------SQATAAVFGARM-PISSLKSYFGH---TLGACGALEAWMSIEMmneGWFAPTL 361


                  ....*...
gi 602182148 1058 HYANPNPR 1065
Cdd:PRK09116  362 NLTQVDPA 369

FACL_like_1

cd05910

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...

205-531

1.37e-14

Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 79.04 E-value: 1.37e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  205 AYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRtlqfcavsfDFSCHEIFSTL-CLGGILVLVPE-----AV 278
Cdd:cd05910    88 AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEV---------DLATFPLFALFgPALGLTSVIPDmdptrPA 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  279 RQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALCEVITTGeqmqiTPAVANLFQKTGAMLH------NHY 352
Cdd:cd05910   159 RADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAG-----APVPIALAARLRKMLSdeaeilTPY 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  353 GATEFQD----------ATTHTLKGNPEGwptlVPVGRPLHNVQVYILDEAQQP---------VPLGGEGEFCIGGIGLA 413
Cdd:cd05910   234 GATEALPvssigsrellATTTAATSGGAG----TCVGRPIPGVRVRIIEIDDEPiaewddtleLPRGEIGEITVTGPTVT 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  414 RGYHNLPDLTNEKFIPNPFGTnenakKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAV 493
Cdd:cd05910   310 PTYVNRPVATALAKIDDNSEG-----FWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSAL 384

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 602182148  494 VAREIAGHTQLVGYIIAKDTLNLSFDKLEPILRQYSEA 531
Cdd:cd05910   385 VGVGKPGCQLPVLCVEPLPGTITPRARLEQELRALAKD 422

PRK07514

malonyl-CoA synthase; Validated

26-494

1.74e-14

malonyl-CoA synthase; Validated

Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 79.15 E-value: 1.74e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   26 HHLFE--DQAAKRPDAIAL-IDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVP 102
Cdd:PRK07514    3 NNLFDalRAAFADRDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  103 LDVGYPADRIEYMLRDSDARILLTST---DVAKKLALTIPAlqecQTVY-LDQEifeydfhflAIAKLLHnqylrllhfy 178
Cdd:PRK07514   83 LNTAYTLAELDYFIGDAEPALVVCDPanfAWLSKIAAAAGA----PHVEtLDAD---------GTGSLLE---------- 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  179 fytliqqcQATSVSQGIQT-QVLPNNLAYCIYTSGSTGNPKGILMEHRSLV-NMLWWHQQTRPSVQGV--RTLQFcavsf 254
Cdd:PRK07514  140 --------AAAAAPDDFETvPRGADDLAAILYTSGTTGRSKGAMLSHGNLLsNALTLVDYWRFTPDDVliHALPI----- 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  255 dFSCHEIF----STLCLGGILVLVPEavrqnpFALAEFISQQKIEKLFLPV----IALLQLA----EAVNGNK---STSL 319
Cdd:PRK07514  207 -FHTHGLFvatnVALLAGASMIFLPK------FDPDAVLALMPRATVMMGVptfyTRLLQEPrltrEAAAHMRlfiSGSA 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  320 ALceVITTGEQMQitpavanlfQKTGAMLHNHYGATEfqdatTHTLKGNP-EGwpTLVP--VGRPLHNVQVYILD-EAQQ 395
Cdd:PRK07514  280 PL--LAETHREFQ---------ERTGHAILERYGMTE-----TNMNTSNPyDG--ERRAgtVGFPLPGVSLRVTDpETGA 341

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  396 PVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFgtnenakklYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVEL 475
Cdd:PRK07514  342 ELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF---------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYP 412

                         490
                  ....*....|....*....
gi 602182148  476 GEIESVLASHQAVRECAVV 494
Cdd:PRK07514  413 KEVEGEIDELPGVVESAVI 431

SmtA

COG0500

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...

2094-2215

2.37e-14

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];

Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 74.18 E-value: 2.37e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2094 QEALLSALEQLPPERgwRILEIGAGTGGTTAYLLPHLPGdqtKYVFTDISAFFLAKAEERFKDYPF--VRYQVLDIEQAP 2171
Cdd:COG0500    14 LAALLALLERLPKGG--RVLDLGCGTGRNLLALAARFGG---RVIGIDLSPEAIALARARAAKAGLgnVEFLVADLAELD 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 602182148 2172 QaqgFEPQIYDLIVAADVLHATS--DLRQTLVHIRQLLAPGGMLIL 2215
Cdd:COG0500    89 P---LPAESFDLVVAFGVLHHLPpeEREALLRELARALKPGGVLLL 131

PRK13382

bile acid CoA ligase;

28-564

3.12e-14

bile acid CoA ligase;

Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 78.65 E-value: 3.12e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   28 LFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAIcIERSAELFIGLLgilkagCAyvpldvgy 107
Cdd:PRK13382   48 GFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGI-MCRNHRGFVEAL------LA-------- 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  108 pADRIeymlrdsDARILLTSTDVAKKLALTIPALQECQTVYLDQEifeydfhFLA-IAKLLHN--QYLRLLHF---YFYT 181
Cdd:PRK13382  113 -ANRI-------GADILLLNTSFAGPALAEVVTREGVDTVIYDEE-------FSAtVDRALADcpQATRIVAWtdeDHDL 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  182 LIQQCQATSVSQGIQTQvlPNNLAYCIYTSGSTGNPKGI-------LMEHRSLVNMLWWHQQtRPSV--------QGVRT 246
Cdd:PRK13382  178 TVEVLIAAHAGQRPEPT--GRKGRVILLTSGTTGTPKGArrsgpggIGTLKAILDRTPWRAE-EPTVivapmfhaWGFSQ 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  247 LQFCAVsfdFSCHEI----FStlclggilvlvPEAV-----RQNPFALAefisqqkieklFLPVI--ALLQLAEAVNgNK 315
Cdd:PRK13382  255 LVLAAS---LACTIVtrrrFD-----------PEATldlidRHRATGLA-----------VVPVMfdRIMDLPAEVR-NR 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  316 STSLALCEVITTGEQMQitPAVANLFQ-KTGAMLHNHYGATEFQDATTHT---LKGNPEgwptlvPVGRPLHNVQVYILD 391
Cdd:PRK13382  309 YSGRSLRFAAASGSRMR--PDVVIAFMdQFGDVIYNNYNATEAGMIATATpadLRAAPD------TAGRPAEGTEIRILD 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  392 EAQQPVPLGGEGEFCIGGIGLARGYhnlpdltnekfipNPFGTNENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGF 471
Cdd:PRK13382  381 QDFREVPTGEVGTIFVRNDTQFDGY-------------TSGSTKDFHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGE 447

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  472 RVELGEIESVLASHQAVRECAVVAREIAGHTQ-LVGYIIAKDTLNLSFDKlepiLRQYSEAVLPEYMIPTRFINISNMPL 550
Cdd:PRK13382  448 NVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQrLAAFVVLKPGASATPET----LKQHVRDNLANYKVPRDIVVLDELPR 523

                         570
                  ....*....|....
gi 602182148  551 TPSGKLDRRALPDP 564
Cdd:PRK13382  524 GATGKILRRELQAR 537

PRK08633

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated

201-561

7.90e-14

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated

Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 78.04 E-value: 7.90e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  201 PNNLAYCIYTSGSTGNPKGILMEHRslvNMLWWHQQTRPSVQGVRTLQFCAV-----SFDFSChEIFSTLCLGGILVLVP 275
Cdd:PRK08633  781 PDDTATIIFSSGSEGEPKGVMLSHH---NILSNIEQISDVFNLRNDDVILSSlpffhSFGLTV-TLWLPLLEGIKVVYHP 856

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  276 eavrqNP---FALAEFISQQKIEKLF-----------LPVIALLQLAeavngnkstSLALceVITTGEQMqiTPAVANLF 341
Cdd:PRK08633  857 -----DPtdaLGIAKLVAKHRATILLgtptflrlylrNKKLHPLMFA---------SLRL--VVAGAEKL--KPEVADAF 918

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  342 Q-KTGAMLHNHYGATE-----------FQDATTHTLKGNPEGwptlvPVGRPLHNVQVYILD-EAQQPVPLGGEGEFCIG 408
Cdd:PRK08633  919 EeKFGIRILEGYGATEtspvasvnlpdVLAADFKRQTGSKEG-----SVGMPLPGVAVRIVDpETFEELPPGEDGLILIG 993

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  409 GIGLARGYHNLPDLTNEKFipnpfgTNENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLA--SHQ 486
Cdd:PRK08633  994 GPQVMKGYLGDPEKTAEVI------KDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAkaLGG 1067

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  487 AVRECAVVA--------REIAGHTQLvgyiiAKDTlnlsfdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDR 558
Cdd:PRK08633 1068 EEVVFAVTAvpdekkgeKLVVLHTCG-----AEDV--------EELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDL 1134


                  ...
gi 602182148  559 RAL 561
Cdd:PRK08633 1135 KGL 1137

BioC

TIGR02072

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...

2097-2215

1.79e-13

Pssm-ID: 273953 [Multi-domain] Cd Length: 240 Bit Score: 72.70 E-value: 1.79e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  2097 LLSALEQLPPERGWRILEIGAGTGGTTAYLLPHLPgdQTKYVFTDISAFFLAKAEERFKdyPFVRYQVLDIEQAPqaqgF 2176
Cdd:TIGR02072   23 LLALLKEKGIFIPASVLDIGCGTGYLTRALLKRFP--QAEFIALDISAGMLAQAKTKLS--ENVQFICGDAEKLP----L 94

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 602182148  2177 EPQIYDLIVAADVLHATSDLRQTLVHIRQLLAPGGMLIL 2215
Cdd:TIGR02072   95 EDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAF 133

PRK12582

acyl-CoA synthetase; Provisional

25-495

1.99e-13

acyl-CoA synthetase; Provisional

Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 76.24 E-value: 1.99e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   25 IHHLFEDQAAKRPDAIALIDGEQ------SLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGC 98
Cdd:PRK12582   51 IPHLLAKWAAEAPDRPWLAQREPghgqwrKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGV 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   99 AYVPLDVGYPA-----DRIEYMLRDSDARILLTSTDVAKKLALTIPALQECQTVYLDQEIfeYDFHFLAIAKLLhnqylr 173
Cdd:PRK12582  131 PAAPVSPAYSLmshdhAKLKHLFDLVKPRVVFAQSGAPFARALAALDLLDVTVVHVTGPG--EGIASIAFADLA------ 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  174 llhfyfytliqqcqATSVSQGIQ---TQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTlqfc 250
Cdd:PRK12582  203 --------------ATPPTAAVAaaiAAITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPP---- 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  251 AVSFDF-SCHEIFS-------TLCLGGILVL-----VPEAVRQNPFALAEfISqqkieklflPV------IALLQLAEAV 311
Cdd:PRK12582  265 PVSLDWmPWNHTMGgnanfngLLWGGGTLYIddgkpLPGMFEETIRNLRE-IS---------PTvygnvpAGYAMLAEAM 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  312 NGNKstslALCE----------------------------VITTGEQMQITpavanlfqkTGamlhnhYGATEFQDATTH 363
Cdd:PRK12582  335 EKDD----ALRRsffknlrlmayggatlsddlyermqalaVRTTGHRIPFY---------TG------YGATETAPTTTG 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  364 TlkgnpeGWPTLVP--VGRPLHNVQVYIldeaqqpVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFgtnenakkl 441
Cdd:PRK12582  396 T------HWDTERVglIGLPLPGVELKL-------APVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF--------- 453

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  442 YRTGDLARYL-PDGTIEHL---GRIDHQVKI-RGFRVELGEIE-SVLASHQAVRECAVVA 495
Cdd:PRK12582  454 YRLGDAARFVdPDDPEKGLifdGRVAEDFKLsTGTWVSVGTLRpDAVAACSPVIHDAVVA 513

AcpP

COG0236

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...

2805-2881

2.07e-13

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: 67.57 E-value: 2.07e-13

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 602182148 2805 TLLQAHVREQVSQVLGIDTKTLLAEQDvgFFT-LGMDSLTSVELRNRLQASLGCSLSSTLAFDYPTQQALVNYLANEL 2881
Cdd:COG0236     4 EELEERLAEIIAEVLGVDPEEITPDDS--FFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKL 79

PLN03102

acyl-activating enzyme; Provisional

37-563

3.14e-13

acyl-activating enzyme; Provisional

Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 75.44 E-value: 3.14e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   37 PDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYML 116
Cdd:PLN03102   28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  117 RDSDARILLTSTDVAkklaltiPALQECQTVYLDQE---------IFEYDFHFLAIAKLLHnqylrllhfyFYTLIQQCQ 187
Cdd:PLN03102  108 RHAKPKILFVDRSFE-------PLAREVLHLLSSEDsnlnlpvifIHEIDFPKRPSSEELD----------YECLIQRGE 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  188 ATSVSQG----IQTQVLPNNLAYciyTSGSTGNPKGILMEHR-----SLVNMLWWHQQTRPSVqgVRTLQFcavsfdFSC 258
Cdd:PLN03102  171 PTPSLVArmfrIQDEHDPISLNY---TSGTTADPKGVVISHRgaylsTLSAIIGWEMGTCPVY--LWTLPM------FHC 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  259 H---EIFSTLCLGGILVLV-----PEAVRQnpfalaefISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALCEVITTGEQ 330
Cdd:PLN03102  240 NgwtFTWGTAARGGTSVCMrhvtaPEIYKN--------IEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSP 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  331 mqiTPAV-ANLFQKTGAMLHNHYGATE---------FQDATTHTlkgnPEGWPTLVPVGRPLHNVQVYILD----EAQQP 396
Cdd:PLN03102  312 ---PPAAlVKKVQRLGFQVMHAYGLTEatgpvlfceWQDEWNRL----PENQQMELKARQGVSILGLADVDvknkETQES 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  397 VPLGGE--GEFCIGGIGLARGYhnlpdltnekfIPNPFGTNENAKKLY-RTGDLARYLPDGTIEHLGRIDHQVKIRGFRV 473
Cdd:PLN03102  385 VPRDGKtmGEIVIKGSSIMKGY-----------LKNPKATSEAFKHGWlNTGDVGVIHPDGHVEIKDRSKDIIISGGENI 453

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  474 ELGEIESVLASHQAVRECAVVA--REIAGHTQLVGYIIAK--DTLNLSFDKL---EPILRQYSEAVLPEYMIPTRFINIS 546
Cdd:PLN03102  454 SSVEVENVLYKYPKVLETAVVAmpHPTWGETPCAFVVLEKgeTTKEDRVDKLvtrERDLIEYCRENLPHFMCPRKVVFLQ 533

                         570
                  ....*....|....*..
gi 602182148  547 NMPLTPSGKLDRRALPD 563
Cdd:PLN03102  534 ELPKNGNGKILKPKLRD 550

PRK07824

o-succinylbenzoate--CoA ligase;

379-561

4.56e-13

o-succinylbenzoate--CoA ligase;

Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 73.54 E-value: 4.56e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  379 GRPLHNVQVYILDeaqqpvplggeGEFCIGGIGLARGYHNLPDltnekfiPNPFGTnenaKKLYRTGDLARyLPDGTIEH 458
Cdd:PRK07824  195 GVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPVD-------PDPFAE----PGWFRTDDLGA-LDDGVLTV 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  459 LGRIDHQVKIRGFRVELGEIESVLASHQAVRECAV--VAREIAGH---TQLVGYIIAKDTLNlsfdklepILRQYSEAVL 533
Cdd:PRK07824  252 LGRADDAISTGGLTVLPQVVEAALATHPAVADCAVfgLPDDRLGQrvvAAVVGDGGPAPTLE--------ALRAHVARTL 323

                         170       180
                  ....*....|....*....|....*...
gi 602182148  534 PEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:PRK07824  324 DRTAAPRELHVVDELPRRGIGKVDRRAL 351

ACLS-CaiC

cd17637

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...

205-494

5.79e-13

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: 72.69 E-value: 5.79e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  205 AYCI-YTSGSTGNPKGILMEHRSLV--NMlwwhqqtrpsvQGVRTLQFCAVSFDFSCHEIF---------STLCLGGILV 272
Cdd:cd17637     2 PFVIiHTAAVAGRPRGAVLSHGNLIaaNL-----------QLIHAMGLTEADVYLNMLPLFhiaglnlalATFHAGGANV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  273 LVPeavRQNPFALAEFISQQKIEKL--FLPVIALLQLAEAVNGNKSTSLalcEVITTGEqmqiTPAVANLFQK-TGAMLH 349
Cdd:cd17637    71 VME---KFDPAEALELIEEEKVTLMgsFPPILSNLLDAAEKSGVDLSSL---RHVLGLD----APETIQRFEEtTGATFW 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  350 NHYGATEfqdatTHtlkgnpeGWPTLVP-------VGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDL 422
Cdd:cd17637   141 SLYGQTE-----TS-------GLVTLSPyrerpgsAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPEL 208

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 602182148  423 TNEKFipnpfgtnenAKKLYRTGDLARYLPDGTIEHLGRIDHQ--VKIRGFRVELGEIESVLASHQAVRECAVV 494
Cdd:cd17637   209 TAYTF----------RNGWHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVI 272

PRK05691

peptide synthase; Validated

19-645

1.15e-12

peptide synthase; Validated

Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 74.82 E-value: 1.15e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   19 EFPDSCIHHLfEDQAAKRPDAIALI----DGEQS--LTYGELNVRANHLAQHLLSLGcQPDDLLAICIERSAELFIGLLG 92
Cdd:PRK05691    6 ELPLTLVQAL-QRRAAQTPDRLALRfladDPGEGvvLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   93 ILKAGCAYVPldvGYPAdriEYMLRDSDARILLTSTDVAKKLALTIPALQECqtvyldqeifeydfhFLAIAKLLHNQYL 172
Cdd:PRK05691   84 CLYAGVIAVP---AYPP---ESARRHHQERLLSIIADAEPRLLLTVADLRDS---------------LLQMEELAAANAP 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  173 RLLhfyfytLIQQCQATSVSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWwhqqtrpsvqgvrtLQFCAV 252
Cdd:PRK05691  143 ELL------CVDTLDPALAEAWQEPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQ--------------LIRHGF 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  253 SFDFSCHE-IFSTLCL-------GGIL----------VLVPEAVRQNPFALAEFISQ-----------------QKIEKL 297
Cdd:PRK05691  203 GIDLNPDDvIVSWLPLyhdmgliGGLLqpifsgvpcvLMSPAYFLERPLRWLEAISEyggtisggpdfayrlcsERVSES 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  298 FLPVIALLQLAEAVNGnkSTSLALCEVITTGEQMQ---ITP---------AVANLFQkTGAMLHNHYGATEFQDATTHTL 365
Cdd:PRK05691  283 ALERLDLSRWRVAYSG--SEPIRQDSLERFAEKFAacgFDPdsffasyglAEATLFV-SGGRRGQGIPALELDAEALARN 359

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  366 KGNPEGWPTLVPVGRPLHNVQVYILDEAQQPV-PLGGEGEFCIGGIGLARGYHNLPDLTNEKFIpnpfgtNENAKKLYRT 444
Cdd:PRK05691  360 RAEPGTGSVLMSCGRSQPGHAVLIVDPQSLEVlGDNRVGEIWASGPSIAHGYWRNPEASAKTFV------EHDGRTWLRT 433

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  445 GDLArYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAV---------------RECAVVAREIAGHTQLVgyii 509
Cdd:PRK05691  434 GDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVvrkgrvaafavnhqgEEGIGIAAEISRSVQKI---- 508

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  510 akdtlnLSFDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRA----LPDPKGDRPAL--STPLVKPRTQT- 582
Cdd:PRK05691  509 ------LPPQALIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSAcrlrLADGSLDSYALfpALQAVEAAQTAa 582

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 602182148  583 -----EKRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKFLCETFNINLSAVSLFQYPTIQTLA 645
Cdd:PRK05691  583 sgdelQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFS 650

Methyltransf_11

pfam08241

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.

2113-2215

1.60e-12

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.

Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 65.76 E-value: 1.60e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  2113 LEIGAGTGGTTAYLLPHLPgdqtKYVFTDISAFFLAKAEERFKDYPfVRYQVLDIEQAPqaqgFEPQIYDLIVAADVLHA 2192
Cdd:pfam08241    1 LDVGCGTGLLTELLARLGA----RVTGVDISPEMLELAREKAPREG-LTFVVGDAEDLP----FPDNSFDLVLSSEVLHH 71

                           90       100
                   ....*....|....*....|...
gi 602182148  2193 TSDLRQTLVHIRQLLAPGGMLIL 2215
Cdd:pfam08241   72 VEDPERALREIARVLKPGGILII 94

Methyltransf_31

pfam13847

Methyltransferase domain; This family appears to have methyltransferase activity.

2111-2227

1.89e-12

Methyltransferase domain; This family appears to have methyltransferase activity.

Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 67.44 E-value: 1.89e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  2111 RILEIGAGTGgTTAYLLPHLPGDQTKYVFTDISAFFLAKAEERFKDYPF--VRYQVLDIEQAPQAqgFEPQIYDLIVAAD 2188
Cdd:pfam13847    6 RVLDLGCGTG-HLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLGFdnVEFEQGDIEELPEL--LEDDKFDVVISNC 82

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 602182148  2189 VLHATSDLRQTLVHIRQLLAPGGMLILmedSEPARWADL 2227
Cdd:pfam13847   83 VLNHIPDPDKVLQEILRVLKPGGRLII---SDPDSLAEL 118

AMP-binding_C

pfam13193

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...

477-555

2.92e-12

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: 64.10 E-value: 2.92e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   477 EIESVLASHQAVRECAVVAR--EIAGHTqLVGYIIAKDtlnlSFDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSG 554
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVpdELKGEA-PVAFVVLKP----GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSG 75


                   .
gi 602182148   555 K 555
Cdd:pfam13193   76 K 76

Methyltransf_23

pfam13489

Methyltransferase domain; This family appears to be a methyltransferase domain.

2093-2264

3.01e-12

Methyltransferase domain; This family appears to be a methyltransferase domain.

Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 67.07 E-value: 3.01e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  2093 VQEALLSALEQLPP--ERGWRILEIGAGTGgttaYLLPHLPGDQTKYVFTDISAfflakaEERFKDYPFVRYQVLDIEQA 2170
Cdd:pfam13489    5 RERLLADLLLRLLPklPSPGRVLDFGCGTG----IFLRLLRAQGFSVTGVDPSP------IAIERALLNVRFDQFDEQEA 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  2171 PQAQGfepqIYDLIVAADVLHATSDLRQTLVHIRQLLAPGGMLILMEDSEPARWADLtfgLTEGWWKFTDHDLrpnHPLL 2250
Cdd:pfam13489   75 AVPAG----KFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRL---LLEWPYLRPRNGH---ISLF 144

                          170
                   ....*....|....
gi 602182148  2251 SPEQWQILLSEMGF 2264
Cdd:pfam13489  145 SARSLKRLLEEAGF 158

BACL_like

cd05929

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...

208-563

3.15e-12

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: 71.64 E-value: 3.15e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  208 IYTSGSTGNPKGILMEH----------RSLVNMLWWHQqtrpsvqGVRTLQ----FCAVSFDFScheiFSTLCLGGILVL 273
Cdd:cd05929   131 LYSGGTTGRPKGIKRGLpggppdndtlMAAALGFGPGA-------DSVYLSpaplYHAAPFRWS----MTALFMGGTLVL 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  274 VPeavRQNPFALAEFISQQKIEKL-FLPVI--ALLQLAEAVNGNKSTSlALCEVITTGEQMqiTPAV-ANLFQKTGAMLH 349
Cdd:cd05929   200 ME---KFDPEEFLRLIERYRVTFAqFVPTMfvRLLKLPEAVRNAYDLS-SLKRVIHAAAPC--PPWVkEQWIDWGGPIIW 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  350 NHYGATEFQDAT--------THtlKGNpegwptlvpVGRPLHNVqVYILDEAQQPVPLGGEGEFCIGGiGLARGYHNLPD 421
Cdd:cd05929   274 EYYGGTEGQGLTiingeewlTH--PGS---------VGRAVLGK-VHILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPE 340

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  422 LTNEKFipnpfgtneNAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGH 501
Cdd:cd05929   341 KTAAAR---------NEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEEL 411

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 602182148  502 TQLVGYIIAKDTLNLSFDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALPD 563
Cdd:cd05929   412 GQRVHAVVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473

fabG

PRK12825

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

2536-2677

5.84e-12

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

Pssm-ID: 237218 [Multi-domain] Cd Length: 249 Bit Score: 68.36 E-value: 5.84e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2536 VARFLVTNGARylVLVGRRGAREEQQAQLSELEQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVIHAAGTLNDGI 2613
Cdd:PRK12825   22 IALRLARAGAD--VVVHYRSDEEAAEELVEAVEALGRRAQAVQADVTDKAALEAAVAAAveRFGRIDILVNNAGIFEDKP 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 602182148 2614 LQQQSWQAFKEVMNPKVAGAWNL-----HILTKNQpldF--FVLFSSATSLLGNAGQANHAAANAFLDGLA 2677
Cdd:PRK12825  100 LADMSDDEWDEVIDVNLSGVFHLlravvPPMRKQR---GgrIVNISSVAGLPGWPGRSNYAAAKAGLVGLT 167

PLN02479

acetate-CoA ligase

209-561

8.58e-12

acetate-CoA ligase

Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 70.64 E-value: 8.58e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  209 YTSGSTGNPKGILMEHR-----SLVNMLWWHQQtrpsvQGVRTLQFCAVsfdFSCHE-----IFSTLCLGGIlvlvpeAV 278
Cdd:PLN02479  202 YTSGTTASPKGVVLHHRgaylmALSNALIWGMN-----EGAVYLWTLPM---FHCNGwcftwTLAALCGTNI------CL 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  279 RQ-NPFALAEFISQQKIEKLF-LPVIallqLAEAVNGNKS-TSLAL---CEVITTGEQMqiTPAVANLFQKTGAMLHNHY 352
Cdd:PLN02479  268 RQvTAKAIYSAIANYGVTHFCaAPVV----LNTIVNAPKSeTILPLprvVHVMTAGAAP--PPSVLFAMSEKGFRVTHTY 341

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  353 GATE-FQDATTHTLKgnPEgWPTLVPVGRP-LHNVQ--VYI----LD----EAQQPVPLGGE--GEFCIGGIGLARGYHN 418
Cdd:PLN02479  342 GLSEtYGPSTVCAWK--PE-WDSLPPEEQArLNARQgvRYIglegLDvvdtKTMKPVPADGKtmGEIVMRGNMVMKGYLK 418

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  419 LPDLTNEKFipnpfgtnenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAR-- 496
Cdd:PLN02479  419 NPKANEEAF----------ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARpd 488

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 602182148  497 EIAGHTQlVGYIIAKDTLNLSFD-KLEPILRQYSEAVLPEYMIPtRFINISNMPLTPSGKLDRRAL 561
Cdd:PLN02479  489 ERWGESP-CAFVTLKPGVDKSDEaALAEDIMKFCRERLPAYWVP-KSVVFGPLPKTATGKIQKHVL 552

AcpP

COG0236

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...

578-649

1.68e-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: 1.68e-11

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 602182148  578 PRTQTEKRLAEIWGSYLAVDI--VGTHDNFF-DLGGTSLLLTQAHKFLCETFNINLSAVSLFQYPTIQTLAQYID 649
Cdd:COG0236     2 PREELEERLAEIIAEVLGVDPeeITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLE 76

Dip2

cd05905

Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...

48-493

2.32e-11

Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.

Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 69.30 E-value: 2.32e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   48 SLTYGELNVRANHLAQHLL-SLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLT 126
Cdd:cd05905    14 TLTWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALT 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  127 STDVAKKLALTIPA-LQECQTVYldqeifeydfhFLAIAKLlhnqylrllhFYFYTLIQQCQATSVSQGIQTQVLPNNLA 205
Cdd:cd05905    94 VEACLKGLPKKLLKsKTAAEIAK-----------KKGWPKI----------LDFVKIPKSKRSKLKKWGPHPPTRDGDTA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  206 YCIYTSGSTGNPKGILMEHRSLVNMLWWHQ---QTRPSvqgvRTLqfcAVSFDFSC-----HEIFSTLCLGGILVLVPEA 277
Cdd:cd05905   153 YIEYSFSSDGSLSGVAVSHSSLLAHCRALKeacELYES----RPL---VTVLDFKSglglwHGCLLSVYSGHHTILIPPE 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  278 -VRQNPFALAEFISQQKIEKLFLP---VIALLQLAEAVNGNKST------SLALCEVITTGE-QMQITPAVANLFQKTGa 346
Cdd:cd05905   226 lMKTNPLLWLQTLSQYKVRDAYVKlrtLHWCLKDLSSTLASLKNrdvnlsSLRMCMVPCENRpRISSCDSFLKLFQTLG- 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  347 mLHNHYGATEF-----------QDATTHTLKG--------------NPEGWP---TLVPVGRPLHNVQVYILDEAQQPVP 398
Cdd:cd05905   305 -LSPRAVSTEFgtrvnpficwqGTSGPEPSRVyldmralrhgvvrlDERDKPnslPLQDSGKVLPGAQVAIVNPETKGLC 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  399 LGGE-GEFCIGGIGLARGYHNLPDLTN---EKFIPNPFGTNENAKKLYRTGDLA-----RYLPDGTIEH-----LGRIDH 464
Cdd:cd05905   384 KDGEiGEIWVNSPANASGYFLLDGETNdtfKVFPSTRLSTGITNNSYARTGLLGflrptKCTDLNVEEHdllfvVGSIDE 463

                         490       500       510
                  ....*....|....*....|....*....|
gi 602182148  465 QVKIRGFRVELGEIE-SVLASHQAVRECAV 493
Cdd:cd05905   464 TLEVRGLRHHPSDIEaTVMRVHPYRGRCAV 493

PRK12476

putative fatty-acid--CoA ligase; Provisional

49-560

2.37e-11

putative fatty-acid--CoA ligase; Provisional

Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 69.38 E-value: 2.37e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   49 LTYGELNVRANHLAQHLLSLgCQPDDLLAICIERSAELFIGLLGILKAGCAYVPL---DVGYPADRIEYMLRDSDARILL 125
Cdd:PRK12476   69 LTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfapELPGHAERLDTALRDAEPTVVL 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  126 TSTDVAkklaltiPALQEcqtvyldqeifeydfhFLAiaKLLHNQYLRLLhfyfytLIQQCQATSVSQGIQTQVLPNNLA 205
Cdd:PRK12476  148 TTTAAA-------EAVEG----------------FLR--NLPRLRRPRVI------AIDAIPDSAGESFVPVELDTDDVS 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  206 YCIYTSGSTGNPKGILMEHRS----LVNMLWWHQQTRPSVQGVRTLqfcAVSFDFSCHEI-FSTLCLGGILVLVPEAVRQ 280
Cdd:PRK12476  197 HLQYTSGSTRPPVGVEITHRAvgtnLVQMILSIDLLDRNTHGVSWL---PLYHDMGLSMIgFPAVYGGHSTLMSPTAFVR 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  281 NPFalaEFISQQKIEKLFLPVIAL--------------------LQLAEAV--NGNKSTSLALCEVITTG------EQMQ 332
Cdd:PRK12476  274 RPQ---RWIKALSEGSRTGRVVTAapnfayewaaqrglpaegddIDLSNVVliIGSEPVSIDAVTTFNKAfapyglPRTA 350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  333 ITP----AVANLFQKTGAMlHNHYGATEF---QDATTHTLKgNPEGWPTLVP---VGRPLHNVQVYILDE-AQQPVPLGG 401
Cdd:PRK12476  351 FKPsygiAEATLFVATIAP-DAEPSVVYLdreQLGAGRAVR-VAADAPNAVAhvsCGQVARSQWAVIVDPdTGAELPDGE 428

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  402 EGEFCIGGIGLARGYHNLPDLTNEKF-----IPNPFGTN-----ENAKKLyRTGDLARYLpDGTIEHLGRIDHQVKIRGF 471
Cdd:PRK12476  429 VGEIWLHGDNIGRGYWGRPEETERTFgaklqSRLAEGSHadgaaDDGTWL-RTGDLGVYL-DGELYITGRIADLIVIDGR 506

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  472 RVELGEIE-SVLASHQAVRECAVVAREIAGHTQLVGYIIAKDTLNLSFDKLEPILRQYSEAVLPEYMIPT---RFINISN 547
Cdd:PRK12476  507 NHYPQDIEaTVAEASPMVRRGYVTAFTVPAEDNERLVIVAERAAGTSRADPAPAIDAIRAAVSRRHGLAVadvRLVPAGA 586

                         570
                  ....*....|...
gi 602182148  548 MPLTPSGKLDRRA 560
Cdd:PRK12476  587 IPRTTSGKLARRA 599

PLN02246

4-coumarate--CoA ligase

18-561

3.96e-11

4-coumarate--CoA ligase

Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 68.47 E-value: 3.96e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   18 SEFPDSCI-HHL------FEdQAAKRPDAIALIDGE--QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFI 88
Cdd:PLN02246   12 SKLPDIYIpNHLplhdycFE-RLSEFSDRPCLIDGAtgRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   89 GLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLTSTDVAKKLAltipALQECQTVYldqeIFEYDFHFlaiAKLLH 168
Cdd:PLN02246   91 AFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYVDKLK----GLAEDDGVT----VVTIDDPP---EGCLH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  169 nqylrllhfyFYTLIQQCQATSVSQGIQtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLwwHQQtrpsVQG-VRTL 247
Cdd:PLN02246  160 ----------FSELTQADENELPEVEIS----PDDVVALPYSSGTTGLPKGVMLTHKGLVTSV--AQQ----VDGeNPNL 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  248 QF-------CAVS-FD-FSCHEIFstLC---LGGILVLVPEavrqnpF---ALAEFISQQKIE-KLFLPVIaLLQLAE-- 309
Cdd:PLN02246  220 YFhsddvilCVLPmFHiYSLNSVL--LCglrVGAAILIMPK------FeigALLELIQRHKVTiAPFVPPI-VLAIAKsp 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  310 AVNGNKSTSLALceVITTGEQM--QITPAVANLFqkTGAMLHNHYGATEFQDATTHTLKGNPEGWP-------TLVpvgr 380
Cdd:PLN02246  291 VVEKYDLSSIRM--VLSGAAPLgkELEDAFRAKL--PNAVLGQGYGMTEAGPVLAMCLAFAKEPFPvksgscgTVV---- 362

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  381 plHNVQVYILD-EAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEkfipnpfgTNENAKKLYrTGDLARYLPDGTIEHL 459
Cdd:PLN02246  363 --RNAELKIVDpETGASLPRNQPGEICIRGPQIMKGYLNDPEATAN--------TIDKDGWLH-TGDIGYIDDDDELFIV 431

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  460 GRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAR--EIAGHTQlVGYIIAKDTLNLSFDKlepiLRQYSEAVLPEYM 537
Cdd:PLN02246  432 DRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMkdEVAGEVP-VAFVVRSNGSEITEDE----IKQFVAKQVVFYK 506

                         570       580
                  ....*....|....*....|....
gi 602182148  538 IPTRFINISNMPLTPSGKLDRRAL 561
Cdd:PLN02246  507 RIHKVFFVDSIPKAPSGKILRKDL 530

PRK00174

acetyl-CoA synthetase; Provisional

379-561

7.02e-11

acetyl-CoA synthetase; Provisional

Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 67.86 E-value: 7.02e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  379 GRPLHNVQVYILDEAQQPVPLGGEGEFCIGGI--GLARGYHNLPdltnEKFIPNPFGTnenAKKLYRTGDLARYLPDGTI 456
Cdd:PRK00174  427 TRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDPwpGMMRTIYGDH----ERFVKTYFST---FKGMYFTGDGARRDEDGYY 499

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  457 EHLGRIDHQVKIRGFRveLG--EIESVLASHQAVRECAVVAR--EIAGHtQLVGYIIAKDTLNLSfDKLEPILRQY-SEA 531
Cdd:PRK00174  500 WITGRVDDVLNVSGHR--LGtaEIESALVAHPKVAEAAVVGRpdDIKGQ-GIYAFVTLKGGEEPS-DELRKELRNWvRKE 575

                         170       180       190
                  ....*....|....*....|....*....|....
gi 602182148  532 VLPeymIPT----RFinISNMPLTPSGKLDRRAL 561
Cdd:PRK00174  576 IGP---IAKpdviQF--APGLPKTRSGKIMRRIL 604

Cfa

COG2230

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...

2094-2215

7.82e-11

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];

Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 63.02 E-value: 7.82e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2094 QEALLSA-LEQLPPERGWRILEIGAGTGGTTAYLLPHLpgdQTKYVFTDISAFFLAKAEERFKDYPF---VRYQVLDIEQ 2169
Cdd:COG2230    36 QEAKLDLiLRKLGLKPGMRVLDIGCGWGGLALYLARRY---GVRVTGVTLSPEQLEYARERAAEAGLadrVEVRLADYRD 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 602182148 2170 APQAQGFepqiyDLIVAADVLHA--TSDLRQTLVHIRQLLAPGGMLIL 2215
Cdd:COG2230   113 LPADGQF-----DAIVSIGMFEHvgPENYPAYFAKVARLLKPGGRLLL 155

SDR

cd02266

Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...

2602-2722

1.71e-10

Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase (KR) domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187535 [Multi-domain] Cd Length: 186 Bit Score: 62.53 E-value: 1.71e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2602 VIHAAGTLNDGILQQQSWQAFKEVMNPKVAGAWNLHILTKNQ----PLDFFVLFSSATSLLGNAGQANHAAANAFLDGLA 2677
Cdd:cd02266    35 VVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELmkakRLGRFILISSVAGLFGAPGLGGYAASKAALDGLA 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 602182148 2678 SYRRHL----GLPSLSINWGTWSEVGIAARLGLD-KLSSKQGEGTITLGQ 2722
Cdd:cd02266   115 QQWASEgwgnGLPATAVACGTWAGSGMAKGPVAPeEILGNRRHGVRTMPP 164

fabG

PRK05653

3-oxoacyl-ACP reductase FabG;

2536-2671

3.31e-10

3-oxoacyl-ACP reductase FabG;

Pssm-ID: 235546 [Multi-domain] Cd Length: 246 Bit Score: 63.26 E-value: 3.31e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2536 VARFLVTNGARylVLVGRRGaREEQQAQLSELEQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVIHAAGTLNDGI 2613
Cdd:PRK05653   21 IALRLAADGAK--VVIYDSN-EEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAveAFGALDILVNNAGITRDAL 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 602182148 2614 LQQQSWQAFKEVMNPKVAGAWN-----LHILTKNQpldfF---VLFSSATSLLGNAGQANHAAANA 2671
Cdd:PRK05653   98 LPRMSEEDWDRVIDVNLTGTFNvvraaLPPMIKAR----YgriVNISSVSGVTGNPGQTNYSAAKA 159

fabG

PRK05557

3-ketoacyl-(acyl-carrier-protein) reductase; Validated

2536-2676

3.43e-10

3-ketoacyl-(acyl-carrier-protein) reductase; Validated

Pssm-ID: 235500 [Multi-domain] Cd Length: 248 Bit Score: 63.29 E-value: 3.43e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2536 VARFLVTNGARylVLVGRRGAREEQQAQLSELEQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVIHAAGTLNDGI 2613
Cdd:PRK05557   21 IAERLAAQGAN--VVINYASSEAGAEALVAEIGALGGKALAVQGDVSDAESVERAVDEAkaEFGGVDILVNNAGITRDNL 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 602182148 2614 LQQQSWQAFKEVMNPKVAGAWNL-----HILTKnQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGL 2676
Cdd:PRK05557   99 LMRMKEEDWDRVIDTNLTGVFNLtkavaRPMMK-QRSGRIINISSVVGLMGNPGQANYAASKAGVIGF 165

LC-FACS_euk

cd05927

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...

49-493

4.81e-10

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: 64.93 E-value: 4.81e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   49 LTYGELNVRANHLAQHLLSLGC--QPDDLLAICIERSAELFIGLLGILKAGCAYVPLdvgYP---ADRIEYMLRDSDARI 123
Cdd:cd05927     6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPL---YDtlgPEAIEYILNHAEISI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  124 LLTSTDVakklaltipalqecqTVYLDQEifeydfhFLAIAKllhnqylrllhfyfytliqqcqatsvsQGIQTQVL--P 201
Cdd:cd05927    83 VFCDAGV---------------KVYSLEE-------FEKLGK---------------------------KNKVPPPPpkP 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  202 NNLAYCIYTSGSTGNPKGILMEHRSLVN----MLWWHQQTRPsvqgvRTLQFCAVSFDFSCHeIF------STLCLGG-- 269
Cdd:cd05927   114 EDLATICYTSGTTGNPKGVMLTHGNIVSnvagVFKILEILNK-----INPTDVYISYLPLAH-IFervveaLFLYHGAki 187

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  270 --------------------ILVLVP------------EAVRQNPFA--LAEFISQQKIEKL---------FLPVIALLQ 306
Cdd:cd05927   188 gfysgdirlllddikalkptVFPGVPrvlnriydkifnKVQAKGPLKrkLFNFALNYKLAELrsgvvraspFWDKLVFNK 267

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  307 LAEAVNGNkstslalCEVITTGEQmQITPAVANLFQKT-GAMLHNHYGATEFQDATTHTLKGNpegwPTLVPVGRPLHNV 385
Cdd:cd05927   268 IKQALGGN-------VRLMLTGSA-PLSPEVLEFLRVAlGCPVLEGYGQTECTAGATLTLPGD----TSVGHVGGPLPCA 335

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  386 QVYILDeaqqpVP-LG-------GEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFgtnenakklYRTGDLARYLPDGTIE 457
Cdd:cd05927   336 EVKLVD-----VPeMNydakdpnPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGW---------LHTGDIGEWLPNGTLK 401

                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 602182148  458 HLGRIDHQVKI-RGFRVELGEIESVLASHQAVRECAV 493
Cdd:cd05927   402 IIDRKKNIFKLsQGEYVAPEKIENIYARSPFVAQIFV 438

PRK05850

acyl-CoA synthetase; Validated

28-228

5.19e-10

acyl-CoA synthetase; Validated

Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 64.96 E-value: 5.19e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   28 LFEDQAAKRPDAIAL--IDGEQ-------SLTYGELNVRANHLAQHLLSLGcQPDDLLAICIERSAELFIGLLGILKAGC 98
Cdd:PRK05850    6 LLRERASLQPDDAAFtfIDYEQdpagvaeTLTWSQLYRRTLNVAEELRRHG-STGDRAVILAPQGLEYIVAFLGALQAGL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   99 AYVPLDVGYPA---DRIEYMLRDSDARILLTS----TDVAKKLAL----TIPALQECQTVYLDQEifeydfhflaiakll 167
Cdd:PRK05850   85 IAVPLSVPQGGahdERVSAVLRDTSPSVVLTTsavvDDVTEYVAPqpgqSAPPVIEVDLLDLDSP--------------- 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 602182148  168 hnqylrllhfyfytliQQCQATSVSqgiqtqvLPnNLAYCIYTSGSTGNPKGILMEHRSLV 228
Cdd:PRK05850  150 ----------------RGSDARPRD-------LP-STAYLQYTSGSTRTPAGVMVSHRNVI 186

SDR_c

cd05233

classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...

2530-2684

5.37e-10

classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, 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. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 212491 [Multi-domain] Cd Length: 234 Bit Score: 62.30 E-value: 5.37e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2530 GGLGLVVARFLVTNGARyLVLVGRrgaREEQQAQLSELEQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVIHAAG 2607
Cdd:cd05233     8 SGIGRAIARRLAREGAK-VVLADR---NEEALAELAAIEALGGNAVAVQADVSDEEDVEALVEEAleEFGRLDILVNNAG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2608 TLNDGILQQQSWQAFKEVMNPKVAGAWNL------HILTKNQPLdfFVLFSSATSLLGNAGQANHAAANAFLDGLA-SYR 2680
Cdd:cd05233    84 IARPGPLEELTDEDWDRVLDVNLTGVFLLtraalpHMKKQGGGR--IVNISSVAGLRPLPGQAAYAASKAALEGLTrSLA 161


                  ....
gi 602182148 2681 RHLG 2684
Cdd:cd05233   162 LELA 165

AFD_CAR-like

cd17632

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...

48-556

5.46e-10

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: 65.17 E-value: 5.46e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   48 SLTYGELNVRANHLA-QHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLT 126
Cdd:cd17632    67 TITYAELWERVGAVAaAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAV 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  127 ST---DVAKKLALTIPALQecQTVYLDQEIfEYDFHFLAiaklLHNQYLRLLHF-----YFYTLIQQCQATSVSQGIQTQ 198
Cdd:cd17632   147 SAehlDLAVEAVLEGGTPP--RLVVFDHRP-EVDAHRAA----LESARERLAAVgipvtTLTLIAVRGRDLPPAPLFRPE 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  199 VLPNNLAYCIYTSGSTGNPKGILMEHRsLVNMLWwhqQTRPSVQGVR-----TLQFCAVSFDFSCHEIFSTLCLGGI--- 270
Cdd:cd17632   220 PDDDPLALLIYTSGSTGTPKGAMYTER-LVATFW---LKVSSIQDIRppasiTLNFMPMSHIAGRISLYGTLARGGTayf 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  271 --------------------LVLVP---EAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSlALCEVITT 327
Cdd:cd17632   296 aaasdmstlfddlalvrpteLFLVPrvcDMLFQRYQAELDRRSVAGADAETLAERVKAELRERVLGGRLLA-AVCGSAPL 374

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  328 GEQMQitpavANLFQKTGAMLHNHYGATEfqdATTHTLKGNpegwptlvpVGRPlhnvqvYILDEAQQPVP-LG------ 400
Cdd:cd17632   375 SAEMK-----AFMESLLDLDLHDGYGSTE---AGAVILDGV---------IVRP------PVLDYKLVDVPeLGyfrtdr 431

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  401 --GEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFgtnenakklYRTGD-LARYLPDgTIEHLGRIDHQVKI-RGFRVELG 476
Cdd:cd17632   432 phPRGELLVKTDTLFPGYYKRPEVTAEVFDEDGF---------YRTGDvMAELGPD-RLVYVDRRNNVLKLsQGEFVTVA 501

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  477 EIESVLASHQAVRECAVVAReiAGHTQLVGYII-------AKDTLNLSFDKLEPILRQYSEAVLPEYMIPTRFInISNMP 549
Cdd:cd17632   502 RLEAVFAASPLVRQIFVYGN--SERAYLLAVVVptqdalaGEDTARLRAALAESLQRIAREAGLQSYEIPRDFL-IETEP 578


                  ....*..
gi 602182148  550 LTPSGKL 556
Cdd:cd17632   579 FTIANGL 585

PRK13390

acyl-CoA synthetase; Provisional

33-556

6.52e-10

acyl-CoA synthetase; Provisional

Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 64.64 E-value: 6.52e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   33 AAKRPDAIALIDGEQsLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRI 112
Cdd:PRK13390   10 APDRPAVIVAETGEQ-VSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  113 EYMLRDSDARILLTSTDvakklaltipalqecqtvyLDQeifeydfhflAIAKLLHNQYLRLLHFYFYTLIQQCQATSVS 192
Cdd:PRK13390   89 DYIVGDSGARVLVASAA-------------------LDG----------LAAKVGADLPLRLSFGGEIDGFGSFEAALAG 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  193 QGIQTQVLPNNlAYCIYTSGSTGNPKGIL--MEHRSLvnmlwwHQQTRPSVQGVRTLqFCAVSFD--FSCHEIFSTL--- 265
Cdd:PRK13390  140 AGPRLTEQPCG-AVMLYSSGTTGFPKGIQpdLPGRDV------DAPGDPIVAIARAF-YDISESDiyYSSAPIYHAAplr 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  266 ------CLGGILVLVPEAVRQNPFALAE---FISQQKIEKLFlpvIALLQLAEAVNGNKSTSlALCEVITTGEQMQITPA 336
Cdd:PRK13390  212 wcsmvhALGGTVVLAKRFDAQATLGHVEryrITVTQMVPTMF---VRLLKLDADVRTRYDVS-SLRAVIHAAAPCPVDVK 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  337 VAnLFQKTGAMLHNHYGATEfqdATTHTLKGNPEGWPTLVPVGRPLHNvQVYILDEAQQPVPLGGEGEFCIGGIGLARGY 416
Cdd:PRK13390  288 HA-MIDWLGPIVYEYYSSTE---AHGMTFIDSPDWLAHPGSVGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRY 362

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  417 HNLPDLTNEKFIP-NPFGTNenakklyrTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVA 495
Cdd:PRK13390  363 LNDPEKTAAAQHPaHPFWTT--------VGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIG 434

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 602182148  496 -------REIAGHTQLVGYIIAKDTLNLSfdklepiLRQYSEAVLPEYMIPTRFINISNMPLTPSGKL 556
Cdd:PRK13390  435 vpdpemgEQVKAVIQLVEGIRGSDELARE-------LIDYTRSRIAHYKAPRSVEFVDELPRTPTGKL 495

A_NRPS_MycA_like

cd05908

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...

200-558

8.78e-10

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that 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: 341234 [Multi-domain] Cd Length: 499 Bit Score: 64.05 E-value: 8.78e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  200 LPNNLAYCIYTSGSTGNPKGILMEHRSLV-NMLWWHQQTRPSVQGvRTLQFCAVSFDF---SCHeifstlclggiLVLVP 275
Cdd:cd05908   104 LADELAFIQFSSGSTGDPKGVMLTHENLVhNMFAILNSTEWKTKD-RILSWMPLTHDMgliAFH-----------LAPLI 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  276 EAVRQNPFALAEFI----------SQQKIE---------KLFL----PVIA----LLQLAEAVNGNKSTSLALCEVITTg 328
Cdd:cd05908   172 AGMNQYLMPTRLFIrrpilwlkkaSEHKATivsspnfgyKYFLktlkPEKAndwdLSSIRMILNGAEPIDYELCHEFLD- 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  329 eQMqitpAVANLfqKTGAMLhNHYGATE------FQDATTHTL-------------------KGNPEGWpTLVPVGRPLH 383
Cdd:cd05908   251 -HM----SKYGL--KRNAIL-PVYGLAEasvgasLPKAQSPFKtitlgrrhvthgepepevdKKDSECL-TFVEVGKPID 321

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  384 NVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFgtnenakklYRTGDLArYLPDGTIEHLGRID 463
Cdd:cd05908   322 ETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGW---------LKTGDLG-FIRNGRLVITGREK 391

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  464 HQVKIRGFRVELGEIESVLASHQAVRECAVVA----REIAGHTQLVGYIIAKDTLN----LSfDKLEPILRQYS----EA 531
Cdd:cd05908   392 DIIFVNGQNVYPHDIERIAEELEGVELGRVVAcgvnNSNTRNEEIFCFIEHRKSEDdfypLG-KKIKKHLNKRGgwqiNE 470

                         410       420
                  ....*....|....*....|....*..
gi 602182148  532 VLPeymiptrfinISNMPLTPSGKLDR 558
Cdd:cd05908   471 VLP----------IRRIPKTTSGKVKR 487

PP-binding

pfam00550

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...

2811-2869

1.57e-09

Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 56.03 E-value: 1.57e-09

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 602182148  2811 VREQVSQVLGIDTKTLLAEQDvgFFTLGMDSLTSVELRNRLQASLGCSLSSTLAFDYPT 2869
Cdd:pfam00550    3 LRELLAEVLGVPAEEIDPDTD--LFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPT 59

PRK08162

acyl-CoA synthetase; Validated

37-572

1.58e-09

acyl-CoA synthetase; Validated

Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 63.43 E-value: 1.58e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   37 PDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYML 116
Cdd:PRK08162   32 PDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFML 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  117 RDSDARILLTST---DVAKKLALTIPALQECQTVYLDQEIFEYDFhflaIAKLLHNQYLRLLHFYF-YTLIQ-QCQATSV 191
Cdd:PRK08162  112 RHGEAKVLIVDTefaEVAREALALLPGPKPLVIDVDDPEYPGGRF----IGALDYEAFLASGDPDFaWTLPAdEWDAIAL 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  192 SqgiqtqvlpnnlayciYTSGSTGNPKGILMEHR-----SLVNMLWWHQQTRPSVqgVRTLQFcavsfdFSCHE---IFS 263
Cdd:PRK08162  188 N----------------YTSGTTGNPKGVVYHHRgaylnALSNILAWGMPKHPVY--LWTLPM------FHCNGwcfPWT 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  264 TLCLGGILVLVPeavRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALCEVITTGEqmqiTPAVANLfQK 343
Cdd:PRK08162  244 VAARAGTNVCLR---KVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAGA----APPAAVI-AK 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  344 TGAM---LHNHYGATEFQDATTHTLKgnPEGWPTLVPVGRPLHNV----------QVYILD-EAQQPVPLGGE--GEFCI 407
Cdd:PRK08162  316 MEEIgfdLTHVYGLTETYGPATVCAW--QPEWDALPLDERAQLKArqgvryplqeGVTVLDpDTMQPVPADGEtiGEIMF 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  408 GGIGLARGYHNLPDLTNEKFipnpfgtnenAKKLYRTGDLARYLPDGTIehlgridhQVKIR--------GFRVELGEIE 479
Cdd:PRK08162  394 RGNIVMKGYLKNPKATEEAF----------AGGWFHTGDLAVLHPDGYI--------KIKDRskdiiisgGENISSIEVE 455

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  480 SVLASHQAVRECAVVAR--EIAGHTQlVGYIIAKDTLNLSfdklEPILRQYSEAVLPEYMIPTRFInISNMPLTPSGKLD 557
Cdd:PRK08162  456 DVLYRHPAVLVAAVVAKpdPKWGEVP-CAFVELKDGASAT----EEEIIAHCREHLAGFKVPKAVV-FGELPKTSTGKIQ 529

                         570
                  ....*....|....*
gi 602182148  558 RRALPDPKGDRPALS 572
Cdd:PRK08162  530 KFVLREQAKSLKAID 544

AdoMet_MTases

cd02440

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...

2111-2216

4.97e-09

Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 56.28 E-value: 4.97e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2111 RILEIGAGTGGTTAYLLPHLPGdqtKYVFTDISAFFLAKAEERFKDYPFVRYQVL--DIEQAPQaqgFEPQIYDLIVAAD 2188
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGA---RVTGVDISPVALELARKAAAALLADNVEVLkgDAEELPP---EADESFDVIISDP 74

                          90       100
                  ....*....|....*....|....*....
gi 602182148 2189 VLHATSDLRQTLVH-IRQLLAPGGMLILM 2216
Cdd:cd02440    75 PLHHLVEDLARFLEeARRLLKPGGVLVLT 103

PRK06060

p-hydroxybenzoic acid--AMP ligase FadD22;

49-586

4.97e-09

p-hydroxybenzoic acid--AMP ligase FadD22;

Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 61.97 E-value: 4.97e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   49 LTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLTST 128
Cdd:PRK06060   31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSD 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  129 DVAKKLALTipalqecqTVYLDQEIFEydfhflaiakllhnqylrllhfyfytliqqcQATSVSQGIQTQVLPNNLAYCI 208
Cdd:PRK06060  111 ALRDRFQPS--------RVAEAAELMS-------------------------------EAARVAPGGYEPMGGDALAYAT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  209 YTSGSTGNPKGILmeHRSLVNMLWWHQQTRPSVQGV-RTLQFCAVSFDFSC---HEIFSTLCLGGILVLVPEAVRQNPFA 284
Cdd:PRK06060  152 YTSGTTGPPKAAI--HRHADPLTFVDAMCRKALRLTpEDTGLCSARMYFAYglgNSVWFPLATGGSAVINSAPVTPEAAA 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  285 LaefisqqkIEKLFLPVIA------LLQLAEAVNGNKSTSLAlCeVITTGEQMQitPAVANLFQK--TGAMLHNHYGATE 356
Cdd:PRK06060  230 I--------LSARFGPSVLygvpnfFARVIDSCSPDSFRSLR-C-VVSAGEALE--LGLAERLMEffGGIPILDGIGSTE 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  357 F-QDATTHTLkgnpEGWpTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPD--LTNEKFIpnpfg 433
Cdd:PRK06060  298 VgQTFVSNRV----DEW-RLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDspVANEGWL----- 367

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  434 tnenakklyRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVA-REIAGHTQLVGYIIAKD 512
Cdd:PRK06060  368 ---------DTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAvRESTGASTLQAFLVATS 438

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 602182148  513 TLNLSfdklEPILRQYSEAVLPE---YMIPTRFINISNMPLTPSGKLDRRALPDPKGDRPALSTPLVKPRTQTEKRL 586
Cdd:PRK06060  439 GATID----GSVMRDLHRGLLNRlsaFKVPHRFAVVDRLPRTPNGKLVRGALRKQSPTKPIWELSLTEPGSGVRAQR 511

CLF

cd00832

Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...

755-1107

6.05e-09

Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic antibiotic-producing polyketide synthases (PKSs) of filamentous bacteria. CLFs have been shown to have decarboxylase activity towards malonyl-acyl carrier protein (ACP). CLFs are similar to other elongation ketosynthase domains, but their active site cysteine is replaced by a conserved glutamine.

Pssm-ID: 238428 [Multi-domain] Cd Length: 399 Bit Score: 60.84 E-value: 6.05e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  755 TDPQQRILLECAWEAFERAGYNPETYPE-PVGVYAGSSLStyllnniGSALGiiteQPFIETDMEQFQAKIGNDRS---- 829
Cdd:cd00832    68 TDRMTRLALAAADWALADAGVDPAALPPyDMGVVTASAAG-------GFEFG----QRELQKLWSKGPRHVSAYQSfawf 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  830 YLAT--RISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMaLAGGISV------VVPQKGGylyeeGMVRSQDG 901
Cdd:cd00832   137 YAVNtgQISIRHGMRGPSGVVVAEQAGGLDALAQARRLVRRGTPLV-VSGGVDSalcpwgWVAQLSS-----GRLSTSDD 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  902 HCRA---FDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGAIKMGYTApsvdGQADVISEAIAIADID 978
Cdd:cd00832   211 PARAylpFDAAAAGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAATFDPPPGSGRPP----GLARAIRLALADAGLT 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  979 ASTIGYVEAHGTATQLGDPIEVAGLARAFqrstdsvlGKQQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLH 1058
Cdd:cd00832   287 PEDVDVVFADAAGVPELDRAEAAALAAVF--------GPRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVN 358

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 602182148 1059 YANPNPRIDFDAtpffVNTELREWSrngyPRRAGVSSFGVGGTNSHIVL 1107
Cdd:cd00832   359 VTDVPPAYGLDL----VTGRPRPAA----LRTALVLARGRGGFNSALVV 399

PRK05857

fatty acid--CoA ligase;

18-561

8.42e-09

fatty acid--CoA ligase;

Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 61.18 E-value: 8.42e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   18 SEFPDSCIHHLFEdQAAKRPDAIAL--IDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILK 95
Cdd:PRK05857   10 PQLPSTVLDRVFE-QARQQPEAIALrrCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAK 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   96 AGCAYVPLDVGYPADRIEYMLRDSDARILLT-------STDVAKKLAlTIPALQECQTVYLDqeifeYDFHFLAIAKLlh 168
Cdd:PRK05857   89 LGAIAVMADGNLPIAAIERFCQITDPAAALVapgskmaSSAVPEALH-SIPVIAVDIAAVTR-----ESEHSLDAASL-- 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  169 nqylrllhfyfytliqqcqATSVSQGIQtqvlpNNLAYcIYTSGSTGNPKGILMEHRSLVNMlwwhqqtrPSV---QGVR 245
Cdd:PRK05857  161 -------------------AGNADQGSE-----DPLAM-IFTSGTTGEPKAVLLANRTFFAV--------PDIlqkEGLN 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  246 TLQFCAVSFDFS----CH-----EIFSTLCLGGILVLVPEavrqNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKS 316
Cdd:PRK05857  208 WVTWVVGETTYSplpaTHigglwWILTCLMHGGLCVTGGE----NTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANA 283

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  317 TSLALcEVITTGEQMQITPAVaNLFQKTGAMLHNHYGATEfQDATTHTLKGNPEGWPTLV--PVGRPLHNVQVYILDE-- 392
Cdd:PRK05857  284 TVPSL-RLVGYGGSRAIAADV-RFIEATGVRTAQVYGLSE-TGCTALCLPTDDGSIVKIEagAVGRPYPGVDVYLAATdg 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  393 AQQPVPLGGE----GEFCIGGIGLARGYHNLPDLTNEKFIpnpfgtnenaKKLYRTGDLARYLPDGTIEHLGRIDHQVKI 468
Cdd:PRK05857  361 IGPTAPGAGPsasfGTLWIKSPANMLGYWNNPERTAEVLI----------DGWVNTGDLLERREDGFFYIKGRSSEMIIC 430

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  469 RGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLVGY-IIAKDTLNLSF-----DKLEPILRQYSEAVLPeymiPTRF 542
Cdd:PRK05857  431 GGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLaVVASAELDESAaralkHTIAARFRRESEPMAR----PSTI 506

                         570
                  ....*....|....*....
gi 602182148  543 INISNMPLTPSGKLDRRAL 561
Cdd:PRK05857  507 VIVTDIPRTQSGKVMRASL 525

LC_FACS_euk1

cd17639

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...

49-488

9.78e-09

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: 60.69 E-value: 9.78e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   49 LTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGcayVPLDVGYP---ADRIEYMLRDSDARILL 125
Cdd:cd17639     6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYAtlgEDALIHSLNETECSAIF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  126 TSTDvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiqtqvlPNNLA 205
Cdd:cd17639    83 TDGK-----------------------------------------------------------------------PDDLA 91

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  206 YCIYTSGSTGNPKGILMEHRSLVNMLwwHQQTRPSVQGVRT-------------LQFCA--VSFDFSCHEIFS---TL-- 265
Cdd:cd17639    92 CIMYTSGSTGNPKGVMLTHGNLVAGI--AGLGDRVPELLGPddrylaylplahiFELAAenVCLYRGGTIGYGsprTLtd 169

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  266 -----CLGGILVL-------VPE-----------------AVRQNPFALAEFISQQKI----------EKLFLPVIALL- 305
Cdd:cd17639   170 kskrgCKGDLTEFkptlmvgVPAiwdtirkgvlaklnpmgGLKRTLFWTAYQSKLKALkegpgtplldELVFKKVRAALg 249

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  306 -QLAEAVNG----NKST----SLALCEVITtgeqmqitpavanlfqktGamlhnhYGATEFQDATTHTlkgNPEGWPTLV 376
Cdd:cd17639   250 gRLRYMLSGgaplSADTqeflNIVLCPVIQ------------------G------YGLTETCAGGTVQ---DPGDLETGR 302

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  377 pVGRPLHNVQVYILDeaqqpVPLGG--------EGEFCIGGIGLARGYHNLPDLTNEKFipnpfgtneNAKKLYRTGDLA 448
Cdd:cd17639   303 -VGPPLPCCEIKLVD-----WEEGGystdkpppRGEILIRGPNVFKGYYKNPEKTKEAF---------DGDGWFHTGDIG 367

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 602182148  449 RYLPDGTIEHLGRIDHQVKIR-GFRVELGEIESVLASHQAV 488
Cdd:cd17639   368 EFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLV 408

PRK08308

acyl-CoA synthetase; Validated

420-562

1.08e-08

acyl-CoA synthetase; Validated

Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 60.44 E-value: 1.08e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  420 PDLTNEKFIPNPF-------GTNENA---------KKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLA 483
Cdd:PRK08308  255 PDMKSHLDLGNPLphvsvsaGSDENApeeivvkmgDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVML 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  484 SHQAVREcAVVAReiaGHTQLVGYIIAkdTLNLSFDKLEPI-LRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALP 562
Cdd:PRK08308  335 RLPGVQE-AVVYR---GKDPVAGERVK--AKVISHEEIDPVqLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408

PRK07769

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

11-560

1.41e-08

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

Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 60.51 E-value: 1.41e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   11 FDGNGTQSEFPDSCIHHLFEDQAAKRPDAIAL--------IDGE-QSLTYGELNVRANHLAQHLLSLGcQPDDLLAICIE 81
Cdd:PRK07769    9 FDVNGKIRFPPNTNLVRHVERWAKVRGDKLAYrfldfsteRDGVaRDLTWSQFGARNRAVGARLQQVT-KPGDRVAILAP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   82 RSAELFIGLLGILKAGCAYVPL-DVGYP--ADRIEYMLRDSDARILLTSTDVA---KKLALTIPALQECQTVYLDqeife 155
Cdd:PRK07769   88 QNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAILTTTDSAegvRKFFRARPAKERPRVIAVD----- 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  156 ydfhflAIAkllhnqylrllhfyfytliQQCQATSVSQGIQTqvlpNNLAYCIYTSGSTGNPKGILMEHRSL-VNMLwwh 234
Cdd:PRK07769  163 ------AVP-------------------DEVGATWVPPEANE----DTIAYLQYTSGSTRIPAGVQITHLNLpTNVL--- 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  235 qQTRPSVQ---GVRTLQFCAVSFDFS-CHEIFSTLCLGGILVLVPEAVRQNP-----------------FALA-----EF 288
Cdd:PRK07769  211 -QVIDALEgqeGDRGVSWLPFFHDMGlITVLLPALLGHYITFMSPAAFVRRPgrwirelarkpggtggtFSAApnfafEH 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  289 ISQQKIEKLFLPVIALLQLAEAVNGNkstslalcEVITTGEQMQITPAVANL-FQKTGamLHNHYG---ATEFQDATTHt 364
Cdd:PRK07769  290 AAARGLPKDGEPPLDLSNVKGLLNGS--------EPVSPASMRKFNEAFAPYgLPPTA--IKPSYGmaeATLFVSTTPM- 358

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  365 lkgnpEGWPTLVPVGRPLHN----VQV----------------------YILD-EAQQPVPLGGEGEFCIGGIGLARGYH 417
Cdd:PRK07769  359 -----DEEPTVIYVDRDELNagrfVEVpadapnavaqvsagkvgvsewaVIVDpETASELPDGQIGEIWLHGNNIGTGYW 433

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  418 NLPDLTNEKF-------IPNPF--GTNENAKKLyRTGDLARYLpDGTIEHLGRIDHQVKIRGFRVELGEIE-SVLASHQA 487
Cdd:PRK07769  434 GKPEETAATFqnilksrLSESHaeGAPDDALWV-RTGDYGVYF-DGELYITGRVKDLVIIDGRNHYPQDLEyTAQEATKA 511

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  488 VRECAVVAREIAGHtQLVGYIIAKDTLNLSFDK---------------------LEPILRQYSEAVLPEYMIPTRFINI- 545
Cdd:PRK07769  512 LRTGYVAAFSVPAN-QLPQVVFDDSHAGLKFDPedtseqlvivaerapgahkldPQPIADDIRAAIAVRHGVTVRDVLLv 590

                         650
                  ....*....|....*..
gi 602182148  546 --SNMPLTPSGKLDRRA 560
Cdd:PRK07769  591 paGSIPRTSSGKIARRA 607

FadD3

cd17638

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...

208-556

2.53e-08

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: 58.67 E-value: 2.53e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  208 IYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFScheiFSTLCLGGIL---VLVPEAVRqNPFA 284
Cdd:cd17638     6 MFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFG----YKAGIVACLLtgaTVVPVAVF-DVDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  285 LAEFISQQKIEklFLP-VIALLQLAEAVNGNKSTSLALCEVITTGEQMQITPAVANLFQKTGAM-LHNHYGATEfqdATT 362
Cdd:cd17638    81 ILEAIERERIT--VLPgPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTE---AGV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  363 HTLkGNPEGWPTLVP--VGRPLHNVQVYILDEaqqpvplggeGEFCIGGIGLARGYHNLPDLTNEKFipnpfgtneNAKK 440
Cdd:cd17638   156 ATM-CRPGDDAETVAttCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAI---------DADG 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  441 LYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAV--VAREIAGHtqlVG--YIIAKDTLNL 516
Cdd:cd17638   216 WLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVigVPDERMGE---VGkaFVVARPGVTL 292

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 602182148  517 SfdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKL 556
Cdd:cd17638   293 T----EEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328

FACL_like_4

cd05944

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...

201-561

3.09e-08

Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 58.65 E-value: 3.09e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  201 PNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQqtRPSVQGVRTLQFCAVSFdFSCHEIFSTLCL----GGILVLVPE 276
Cdd:cd05944     1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLA--LNSLFDPDDVLLCGLPL-FHVNGSVVTLLTplasGAHVVLAGP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  277 AVRQNPFALAEF---ISQQKIEKLF-LPVI--ALLQlaeaVNGNKSTSlALCEVITTGEQMQItpAVANLFQ-KTGAMLH 349
Cdd:cd05944    78 AGYRNPGLFDNFwklVERYRITSLStVPTVyaALLQ----VPVNADIS-SLRFAMSGAAPLPV--ELRARFEdATGLPVV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  350 NHYGATEfqdATTHTLKGNPEGWPTLVPVGRPLHNVQVYILDE-----AQQPVPLGGEGEFCIGGIGLARGYhnlpdlTN 424
Cdd:cd05944   151 EGYGLTE---ATCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLdgvgrLLRDCAPDEVGEICVAGPGVFGGY------LY 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  425 EKFIPNPFGtnenAKKLYRTGDLARYLPDGTIEHLGRIDHQVkIR-GFRVELGEIESVLASHQAVRECAVVAREIAGHTQ 503
Cdd:cd05944   222 TEGNKNAFV----ADGWLNTGDLGRLDADGYLFITGRAKDLI-IRgGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGE 296

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 602182148  504 L-VGYIIAKDTLNLSFDKLEPILRQY--SEAVLPEYMIPtrfinISNMPLTPSGKLDRRAL 561
Cdd:cd05944   297 LpVAYVQLKPGAVVEEEELLAWARDHvpERAAVPKHIEV-----LEELPVTAVGKVFKPAL 352

PLN02387

long-chain-fatty-acid-CoA ligase family protein

49-488

5.83e-08

long-chain-fatty-acid-CoA ligase family protein

Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 58.59 E-value: 5.83e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   49 LTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILLTST 128
Cdd:PLN02387  107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  129 DVAKKLALTIPALQECQTV-YLDQEIFEYDFhflaiaKLLHNQYLRLLHFyfyTLIQQCQATSVSQGIQTqvLPNNLAYC 207
Cdd:PLN02387  187 KQLKKLIDISSQLETVKRViYMDDEGVDSDS------SLSGSSNWTVSSF---SEVEKLGKENPVDPDLP--SPNDIAVI 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  208 IYTSGSTGNPKGILMEHRSLVnmlwwhqqtrPSVQGVRTlqfcaVSFDFSCHEIF-STLCLGGILVLVPEAVRQ------ 280
Cdd:PLN02387  256 MYTSGSTGLPKGVMMTHGNIV----------ATVAGVMT-----VVPKLGKNDVYlAYLPLAHILELAAESVMAavgaai 320

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  281 ---NPFALAEfiSQQKIEK------------LFLPVIALL----------------------QLA-----EAVNGNKSTS 318
Cdd:PLN02387  321 gygSPLTLTD--TSNKIKKgtkgdasalkptLMTAVPAILdrvrdgvrkkvdakgglakklfDIAykrrlAAIEGSWFGA 398

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  319 LALcevittgEQMQITPAVanlFQKTGAMLHNH------------------------------YGATEFQDATTHTlkgn 368
Cdd:PLN02387  399 WGL-------EKLLWDALV---FKKIRAVLGGRirfmlsggaplsgdtqrfiniclgapigqgYGLTETCAGATFS---- 464

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  369 peGW--PTLVPVGRPLHNVQVYILD-------EAQQPVPlggEGEFCIGGIGLARGYHNLPDLTNEKFipnpfGTNENAK 439
Cdd:PLN02387  465 --EWddTSVGRVGPPLPCCYVKLVSweeggylISDKPMP---RGEIVIGGPSVTLGYFKNQEKTDEVY-----KVDERGM 534

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 602182148  440 KLYRTGDLARYLPDGTIEHLGRIDHQVKIR-GFRVELGEIESVLASHQAV 488
Cdd:PLN02387  535 RWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALSVSPYV 584

PP-binding

pfam00550

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...

584-642

6.78e-08

Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 51.41 E-value: 6.78e-08

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 602182148   584 KRLAEIWGSYLAVDI--VGTHDNFFDLGGTSLLLTQAHKFLCETFNINLSAVSLFQYPTIQ 642
Cdd:pfam00550    1 ERLRELLAEVLGVPAeeIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61

FATP_FACS

cd05940

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...

46-546

1.19e-07

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: 56.98 E-value: 1.19e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   46 EQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCayvpldvgyPADRIEYMLRdsdARILL 125
Cdd:cd05940     1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGA---------VAALINYNLR---GESLA 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  126 TSTDVAKKLALTIPALqecqtvyldqeifeydfhflaiakllhnqylrllhfyFYtliqqcqatsvsqgiqtqvlpnnla 205
Cdd:cd05940    69 HCLNVSSAKHLVVDAA-------------------------------------LY------------------------- 86

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  206 ycIYTSGSTGNPKGILMEHRSLVNMLWWHQQtrpSVQGVRTLQFcavsfdFSC----HEIFSTLCLGGILVLVPEAVRQN 281
Cdd:cd05940    87 --IYTSGTTGLPKAAIISHRRAWRGGAFFAG---SGGALPSDVL------YTClplyHSTALIVGWSACLASGATLVIRK 155

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  282 PFALAEFISQ-QKIEKLFLPVIA-----LLQLAEAVNGNKSTSLALCevittGEQMQitPAVANLFQKTGAMLH--NHYG 353
Cdd:cd05940   156 KFSASNFWDDiRKYQATIFQYIGelcryLLNQPPKPTERKHKVRMIF-----GNGLR--PDIWEEFKERFGVPRiaEFYA 228

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  354 ATEFQDATTHtLKGNPEGW---PTLVPVGRPLHNVQVYIldEAQQP----------VPLGGEGEfCIGGIG-LAR--GYH 417
Cdd:cd05940   229 ATEGNSGFIN-FFGKPGAIgrnPSLLRKVAPLALVKYDL--ESGEPirdaegrcikVPRGEPGL-LISRINpLEPfdGYT 304

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  418 NlPDLTNEKFIPNPFgtnENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVARE 497
Cdd:cd05940   305 D-PAATEKKILRDVF---KKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQ 380

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 602182148  498 IAGHTQLVGYIIAKDTLNLSFDkLEPiLRQYSEAVLPEYMIPtRFINIS 546
Cdd:cd05940   381 VPGTDGRAGMAAIVLQPNEEFD-LSA-LAAHLEKNLPGYARP-LFLRLQ 426

DUF938

pfam06080

Protein of unknown function (DUF938); This family consists of several hypothetical proteins ...

2095-2215

1.22e-07

Protein of unknown function (DUF938); This family consists of several hypothetical proteins from both prokaryotes and eukaryotes. The function of this family is unknown.

Pssm-ID: 253548 Cd Length: 201 Bit Score: 54.77 E-value: 1.22e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  2095 EALLSALEQLPPERGWRILEIGAGTGGTTAYLLPHLP------GDQTKYVFTDISAFFLAKAEERFKdYPFvryqVLDIE 2168
Cdd:pfam06080   12 EPILSVLQSYFAKTTERVLEIASGTGQHAVFFAPLLPnltwqpSDPDPNLRGSIAAWADQQGLRNLR-PPL----HLDVT 86

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 602182148  2169 QAP-QAQGFEPQIYDLIVAADVLHaTSDLRQTLVHIR---QLLAPGGMLIL 2215
Cdd:pfam06080   87 RPPwPVEAPAPASYDAIFSINMIH-ISPWSCVEGLFRgagRLLPPGGVLYI 136

prpE

PRK10524

propionyl-CoA synthetase; Provisional

439-574

1.51e-07

propionyl-CoA synthetase; Provisional

Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 57.27 E-value: 1.51e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  439 KKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVV--AREIAGhtQL-VGYIIAKDTLN 515
Cdd:PRK10524  472 RQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVgvKDALKG--QVaVAFVVPKDSDS 549

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 602182148  516 LS----FDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALP------DPkGDRPALSTP 574
Cdd:PRK10524  550 LAdreaRLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQaiaegrDP-GDLTTIEDP 617

HSD10-like_SDR_c

cd05371

17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...

2536-2668

2.29e-07

17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, 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. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187629 [Multi-domain] Cd Length: 252 Bit Score: 54.60 E-value: 2.29e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2536 VARFLVTNGARyLVLVGRRGAREEQQAqlseleQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVIHAAG------ 2607
Cdd:cd05371    18 TVERLLAQGAK-VVILDLPNSPGETVA------KLGDNCRFVPVDVTSEKDVKAALALAkaKFGRLDIVVNCAGiavaak 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 602182148 2608 TLNDGILQQQSWQAFKEVMNPKVAGAWNL-----HILTKNQPLDF-----FVLFSSATSLLGNAGQANHAA 2668
Cdd:cd05371    91 TYNKKGQQPHSLELFQRVINVNLIGTFNVirlaaGAMGKNEPDQGgergvIINTASVAAFEGQIGQAAYSA 161

Gcd14

COG2519

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...

2109-2214

2.75e-07

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification

Pssm-ID: 442009 [Multi-domain] Cd Length: 249 Bit Score: 54.40 E-value: 2.75e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2109 GWRILEIGAGTGGTTAYLLPHLpGDQTKYVFTDISAFFLAKAE---ERFKDYPFVRYQVLDIEqapqaQGFEPQIYDLIV 2185
Cdd:COG2519    92 GARVLEAGTGSGALTLALARAV-GPEGKVYSYERREDFAEIARknlERFGLPDNVELKLGDIR-----EGIDEGDVDAVF 165

                          90       100       110
                  ....*....|....*....|....*....|..
gi 602182148 2186 AadvlhatsDLRQ---TLVHIRQLLAPGGMLI 2214
Cdd:COG2519   166 L--------DMPDpweALEAVAKALKPGGVLV 189

HTH_51

pfam18558

Helix-turn-helix domain; This is helix turn helix domain found in polyketide synthases (PKSs) ...

1928-2011

3.38e-07

Helix-turn-helix domain; This is helix turn helix domain found in polyketide synthases (PKSs) in fungi. They are multidomain enzymes that biosynthesize a wide range of natural products. Family members include citrinin polyketide synthases which contain a C-methyltransferase (CMeT) domain pfam08242 that adds one or more S-adenosylmethionine (SAM)-derived methyl groups to the carbon framework.

Pssm-ID: 465801 Cd Length: 90 Bit Score: 50.16 E-value: 3.38e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  1928 ETKLAT--LIIEANLATYA-IAYTQLERLSLAYVVAAFRQMGW---LFQPGerfstaQKVSALGIVDQHRQLFARLLDIL 2001
Cdd:pfam18558    3 ETKKLTdqFIEEYGFAGYWdEVYPRQTRLCLALIVEAFEKLGCdlrSAKPG------QKLPRIPHLPKHQRLVDYLYEIL 76

                           90
                   ....*....|
gi 602182148  2002 AEADILRSEN 2011
Cdd:pfam18558   77 EDARLVDIDG 86

PRK13388

acyl-CoA synthetase; Provisional

345-561

4.42e-07

acyl-CoA synthetase; Provisional

Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 55.42 E-value: 4.42e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  345 GAMLHNHYGATEFQDATTHTlKGNPEGwptlvPVGRPLHNVQVYILDEAQQ-PVPLGGE------GEFCIG------GIG 411
Cdd:PRK13388  288 GCQVEDGYGSSEGAVIVVRE-PGTPPG-----SIGRGAPGVAIYNPETLTEcAVARFDAhgallnADEAIGelvntaGAG 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  412 LARGYHNLPDLTNEKFipnpfgtnenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVREC 491
Cdd:PRK13388  362 FFEGYYNNPEATAERM----------RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRV 431

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 602182148  492 AV--VAREIAGhTQLVGYIIAKDTLNLSFDKLEPILRqySEAVLPEYMIPtRFINIS-NMPLTPSGKLDRRAL 561
Cdd:PRK13388  432 AVyaVPDERVG-DQVMAALVLRDGATFDPDAFAAFLA--AQPDLGTKAWP-RYVRIAaDLPSTATNKVLKREL 500

hsFATP2a_ACSVL_like

cd05938

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...

45-230

6.23e-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: 54.99 E-value: 6.23e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   45 GEQSLTYGELNVRANHLAQHLLS-LGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARI 123
Cdd:cd05938     2 EGETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  124 LLTSTDVAKKLALTIPALQecqtvyldqeifEYDFHFLAIAKLLHNQYLRllhfyfyTLIQQCQATS---VSQGIQTQVL 200
Cdd:cd05938    82 LVVAPELQEAVEEVLPALR------------ADGVSVWYLSHTSNTEGVI-------SLLDKVDAASdepVPASLRAHVT 142

                         170       180       190
                  ....*....|....*....|....*....|
gi 602182148  201 PNNLAYCIYTSGSTGNPKGILMEHRSLVNM 230
Cdd:cd05938   143 IKSPALYIYTSGTTGLPKAARISHLRVLQC 172

KDSR-like_SDR_c

cd08939

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...

2536-2677

8.49e-07

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, 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. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187643 [Multi-domain] Cd Length: 239 Bit Score: 52.64 E-value: 8.49e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2536 VARFLVTNGARyLVLVGRRGAREEQQAQLSELEQLGASVKVL--QADIADAEQLAQALSAVTYP--PLRGVIHAAGTLND 2611
Cdd:cd08939    17 LAKELVKEGAN-VIIVARSESKLEEAVEEIEAEANASGQKVSyiSADLSDYEEVEQAFAQAVEKggPPDLVVNCAGISIP 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2612 GILQQQSWQAFKEVMNPKVAGAWNL-H---ILTKNQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGLA 2677
Cdd:cd08939    96 GLFEDLTAEEFERGMDVNYFGSLNVaHavlPLMKEQRPGHIVFVSSQAALVGIYGYSAYCPSKFALRGLA 165

PRK06060

p-hydroxybenzoic acid--AMP ligase FadD22;

2801-2893

1.35e-06

p-hydroxybenzoic acid--AMP ligase FadD22;

Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 54.27 E-value: 1.35e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2801 KEGLTLLQAHVREQVSQVLGIDTKTLLAE-------QDVGFFTLGMDSLTSVELRNRLQASLGCSLSSTLAFDYPTQQAL 2873
Cdd:PRK06060  532 RERLVALRQERQRLVVDAVCAEAAKMLGEpdpwsvdQDLAFSELGFDSQMTVTLCKRLAAVTGLRLPETVGWDYGSISGL 611

                          90       100
                  ....*....|....*....|
gi 602182148 2874 VNYLANELLGTPEQLQEPES 2893
Cdd:PRK06060  612 AQYLEAELAGGHGRLKSAGP 631

PRK06198

short chain dehydrogenase; Provisional

2536-2627

1.52e-06

short chain dehydrogenase; Provisional

Pssm-ID: 180462 [Multi-domain] Cd Length: 260 Bit Score: 52.31 E-value: 1.52e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2536 VARFLVTNGARYLVLVGRRGAREEQQAqlSELEQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVIHAAGTLNDGI 2613
Cdd:PRK06198   22 IARAFAERGAAGLVICGRNAEKGEAQA--AELEALGAKAVFVQADLSDVEDCRRVVAAAdeAFGRLDALVNAAGLTDRGT 99

                          90
                  ....*....|....
gi 602182148 2614 LQQQSWQAFKEVMN 2627
Cdd:PRK06198  100 ILDTSPELFDRHFA 113

BKR_SDR_c

cd05333

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...

2536-2677

1.81e-06

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, 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 type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187594 [Multi-domain] Cd Length: 240 Bit Score: 51.78 E-value: 1.81e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2536 VARFLVTNGARyLVLVGRRgaREEQQAQLSELEQLGASVKVLQADIADAEQLAQALSAVT--YPPLRGVIHAAGTLNDGI 2613
Cdd:cd05333    16 IALRLAAEGAK-VAVTDRS--EEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEaeFGPVDILVNNAGITRDNL 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 602182148 2614 LQQQSWQAFKEVMNPKVAGAWNL-----HILTKNQPLDFfVLFSSATSLLGNAGQANHAAANAFLDGLA 2677
Cdd:cd05333    93 LMRMSEEDWDAVINVNLTGVFNVtqaviRAMIKRRSGRI-INISSVVGLIGNPGQANYAASKAGVIGFT 160

PRK08180

feruloyl-CoA synthase; Reviewed

24-227

1.91e-06

feruloyl-CoA synthase; Reviewed

Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 53.34 E-value: 1.91e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   24 CIHHLFEDQAAKRPDAIALI-----DGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGC 98
Cdd:PRK08180   40 RLTDRLVHWAQEAPDRVFLAergadGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGV 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   99 AYVPLDVGY---PAD--RIEYMLRdsdariLLTSTDV-AKKLALTIPALQECqtVYLDQEIFeydfhflaiakLLHNQYL 172
Cdd:PRK08180  120 PYAPVSPAYslvSQDfgKLRHVLE------LLTPGLVfADDGAAFARALAAV--VPADVEVV-----------AVRGAVP 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 602182148  173 RLLHFYFYTLIQQCQATSVSQGIQtQVLPNNLAYCIYTSGSTGNPKGILMEHRSL 227
Cdd:PRK08180  181 GRAATPFAALLATPPTAAVDAAHA-AVGPDTIAKFLFTSGSTGLPKAVINTHRML 234

PRK07768

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

375-560

2.65e-06

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

Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 53.08 E-value: 2.65e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  375 LVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYhnlpdLTNEKFIPnpfgtNENAKKLYRTGDLARYLPDG 454
Cdd:PRK07768  359 LATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY-----LTMDGFIP-----AQDADGWLDTGDLGYLTEEG 428

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  455 TIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRE-CAVVAREIAGHTQlVGYIIAKDTlNLSFD--KLEPILRQYSEA 531
Cdd:PRK07768  429 EVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPgNAVAVRLDAGHSR-EGFAVAVES-NAFEDpaEVRRIRHQVAHE 506

                         170       180       190
                  ....*....|....*....|....*....|..
gi 602182148  532 VLPEYMIPTRFINI---SNMPLTPSGKLDRRA 560
Cdd:PRK07768  507 VVAEVGVRPRNVVVlgpGSIPKTPSGKLRRAN 538

PRK12827

short chain dehydrogenase; Provisional

2536-2676

3.40e-06

short chain dehydrogenase; Provisional

Pssm-ID: 237219 [Multi-domain] Cd Length: 249 Bit Score: 51.26 E-value: 3.40e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2536 VARFLVTNGARYLVLVG--RRGaREEQQAQLSELEQLGASVKVLQADIADAEQLAQALSAVT--YPPLRGVIHAAGTLND 2611
Cdd:PRK12827   22 IAVRLAADGADVIVLDIhpMRG-RAEADAVAAGIEAAGGKALGLAFDVRDFAATRAALDAGVeeFGRLDILVNNAGIATD 100

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2612 GILQQQSWQAFKEVMNPKVAGAWNL-HILT----KNQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGL 2676
Cdd:PRK12827  101 AAFAELSIEEWDDVIDVNLDGFFNVtQAALppmiRARRGGRIVNIASVAGVRGNRGQVNYAASKAGLIGL 170

PKS_PP

smart00823

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...

595-648

6.46e-06

Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 46.47 E-value: 6.46e-06

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 602182148    595 AVDIVGTHDNFFDLGGTSLLLTQAHKFLCETFNINLSAVSLFQYPTIQTLAQYI 648
Cdd:smart00823   29 AAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82

AACS

cd05943

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...

27-555

7.75e-06

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: 51.50 E-value: 7.75e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   27 HLFEDQAAkrPDAIALIDGE----QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLL-----GILKAG 97
Cdd:cd05943    75 NLLRHADA--DDPAAIYAAEdgerTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLatasiGAIWSS 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   98 CAyvPlDVGYPA--DRieymLRDSDARILLT---------STDVAKKLALTIPALQEC-QTVYLDQEIFEYDFHFLAIAK 165
Cdd:cd05943   153 CS--P-DFGVPGvlDR----FGQIEPKVLFAvdaytyngkRHDVREKVAELVKGLPSLlAVVVVPYTVAAGQPDLSKIAK 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  166 LlhnqylrllHFYFYTLiqqcQATSVSQGIQTQVLPNNLAYCIYTSGSTGNPK-------GILMEHRSLVnMLwwHQQTR 238
Cdd:cd05943   226 A---------LTLEDFL----ATGAAGELEFEPLPFDHPLYILYSSGTTGLPKcivhgagGTLLQHLKEH-IL--HCDLR 289

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  239 PsvqGVRtlqFCAVSfdfSC-----HEIFSTLCLGGILVLVPEavrqNPF-----ALAEFISQQKIEklFLPVIA--LLQ 306
Cdd:cd05943   290 P---GDR---LFYYT---TCgwmmwNWLVSGLAVGATIVLYDG----SPFypdtnALWDLADEEGIT--VFGTSAkyLDA 354

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  307 LAEA-VNGNKSTSL-ALCEVITTGeqmqiTPAVANLFQ------KTGAMLHNHYGATefqDATTHTLKGNPegwptLVPV 378
Cdd:cd05943   355 LEKAgLKPAETHDLsSLRTILSTG-----SPLKPESFDyvydhiKPDVLLASISGGT---DIISCFVGGNP-----LLPV 421

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  379 GR-----PLHNVQVYILDEAQQPVPlGGEGEF-CIGGI-GLARGYHNLPDltNEKFIPNPFGTNENakkLYRTGDLARYL 451
Cdd:cd05943   422 YRgeiqcRGLGMAVEAFDEEGKPVW-GEKGELvCTKPFpSMPVGFWNDPD--GSRYRAAYFAKYPG---VWAHGDWIEIT 495

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  452 PDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREI-AGHTQLVGYIIAKDTLNLSFDKLEPILRQYSE 530
Cdd:cd05943   496 PRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWkDGDERVILFVKLREGVELDDELRKRIRSTIRS 575

                         570       580
                  ....*....|....*....|....*
gi 602182148  531 AVLPEYmIPTRFINISNMPLTPSGK 555
Cdd:cd05943   576 ALSPRH-VPAKIIAVPDIPRTLSGK 599

PRK12826

SDR family oxidoreductase;

2524-2684

8.66e-06

SDR family oxidoreductase;

Pssm-ID: 183775 [Multi-domain] Cd Length: 251 Bit Score: 49.91 E-value: 8.66e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2524 LIAGGLGGLGLVVARFLVTNGARYLVlVGRRGAREEQQAQLseLEQLGASVKVLQADIADAEQLAQALSAVT--YPPLRG 2601
Cdd:PRK12826   10 LVTGAARGIGRAIAVRLAADGAEVIV-VDICGDDAAATAEL--VEAAGGKARARQVDVRDRAALKAAVAAGVedFGRLDI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2602 VIHAAGTLNDGILQQQSWQAFKEVMNPKVAGAWNL------HILTKNQPLdfFVLFSSATSL-LGNAGQANHAAANAFLD 2674
Cdd:PRK12826   87 LVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLtqaalpALIRAGGGR--IVLTSSVAGPrVGYPGLAHYAASKAGLV 164

                         170
                  ....*....|.
gi 602182148 2675 GLA-SYRRHLG 2684
Cdd:PRK12826  165 GFTrALALELA 175

PTZ00237

acetyl-CoA synthetase; Provisional

206-558

8.98e-06

acetyl-CoA synthetase; Provisional

Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 51.28 E-value: 8.98e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  206 YCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRpSVQGVRTLQFCAVSFDF-SCHE-IFSTLCLGGILVLVPEAVRQNPF 283
Cdd:PTZ00237  258 YILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSI-IEKDIPTVVFSHSSIGWvSFHGfLYGSLSLGNTFVMFEGGIIKNKH 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  284 A---LAEFISQQKIEKLFLPVIALLQL------AEAVNGNKSTSlALCEVITTGEQmqITPAVANLF-QKTGAMLHNHYG 353
Cdd:PTZ00237  337 IeddLWNTIEKHKVTHTLTLPKTIRYLiktdpeATIIRSKYDLS-NLKEIWCGGEV--IEESIPEYIeNKLKIKSSRGYG 413

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  354 ATE-----FQDATTHTLKGNPEGWPTlvPVGRPLhnvqvyILDEAQQPVPLGGEGEFCIggiglargyhNLPdltnekfI 428
Cdd:PTZ00237  414 QTEigityLYCYGHINIPYNATGVPS--IFIKPS------ILSEDGKELNVNEIGEVAF----------KLP-------M 468

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  429 PNPFGT-----NENAKKL-------YRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAR 496
Cdd:PTZ00237  469 PPSFATtfyknDEKFKQLfskfpgyYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGI 548

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 602182148  497 E-IAGHTQLVGYIIAK---DTLNLSFDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDR 558
Cdd:PTZ00237  549 YdPDCYNVPIGLLVLKqdqSNQSIDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614

adh_short

pfam00106

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.

2530-2677

1.17e-05

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.

Pssm-ID: 395056 [Multi-domain] Cd Length: 195 Bit Score: 48.76 E-value: 1.17e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  2530 GGLGLVVARFLVTNGARyLVLVGRRGAREEQQAQlsELEQLGASVKVLQADIADAEQLAQALSAVT--YPPLRGVIHAAG 2607
Cdd:pfam00106   10 SGIGRAIAKRLAKEGAK-VVLVDRSEEKLEAVAK--ELGALGGKALFIQGDVTDRAQVKALVEQAVerLGRLDILVNNAG 86

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 602182148  2608 TLNDGILQQQSWQAFKEVMNPKVAGAWNL------HILTKNQPLDFFVlfSSATSLLGNAGQANHAAANAFLDGLA 2677
Cdd:pfam00106   87 ITGLGPFSELSDEDWERVIDVNLTGVFNLtravlpAMIKGSGGRIVNI--SSVAGLVPYPGGSAYSASKAAVIGFT 160

YdfG

COG4221

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...

2530-2684

1.41e-05

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation

Pssm-ID: 443365 [Multi-domain] Cd Length: 240 Bit Score: 49.02 E-value: 1.41e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2530 GGLGLVVARFLVTNGARyLVLVGRRGAReeqqaqLSEL-EQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVIHAA 2606
Cdd:COG4221    15 SGIGAATARALAAAGAR-VVLAARRAER------LEALaAELGGRALAVPLDVTDEAAVEAAVAAAvaEFGRLDVLVNNA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2607 GTLNDGILQQQSWQAFKEVMNPKVAGAWNL--------------HILTknqpldffvlFSSATSLLGNAGQANHAAANAF 2672
Cdd:COG4221    88 GVALLGPLEELDPEDWDRMIDVNVKGVLYVtraalpamrargsgHIVN----------ISSIAGLRPYPGGAVYAATKAA 157

                         170
                  ....*....|...
gi 602182148 2673 LDGLA-SYRRHLG 2684
Cdd:COG4221   158 VRGLSeSLRAELR 170

FATP_chFAT1_like

cd05937

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...

45-545

2.46e-05

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: 49.74 E-value: 2.46e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   45 GEQSLTYGELNVRANHLAQHLLS-LGCQPDDLLAICIERSAELFIGLLGILKAGCAyvpldvgyPAdRIEYMLRDsdari 123
Cdd:cd05937     2 EGKTWTYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA--------PA-FINYNLSG----- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  124 lltstdvakklaltipalqecqtvyldqeifeydfhflaiAKLLHnqylrllhfyfytliqqCQATSVSqgiqTQVL--P 201
Cdd:cd05937    68 ----------------------------------------DPLIH-----------------CLKLSGS----RFVIvdP 86

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  202 NNLAYCIYTSGSTGNPKGILMEHRslvnMLWWHQQTRPSVQGVR---TLQFCAVSFDFSCHEIFSTLCL--GGILVLVPE 276
Cdd:cd05937    87 DDPAILIYTSGTTGLPKAAAISWR----RTLVTSNLLSHDLNLKngdRTYTCMPLYHGTAAFLGACNCLmsGGTLALSRK 162

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  277 avrqnpFALAEFISQQKIEK--LFLPVIALLQLAEAVNGNKSTSLALCEVITtGEQMQitPAVANLFQKTGAM--LHNHY 352
Cdd:cd05937   163 ------FSASQFWKDVRDSGatIIQYVGELCRYLLSTPPSPYDRDHKVRVAW-GNGLR--PDIWERFRERFNVpeIGEFY 233

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  353 GATEfqdATTHTLKGNPEGWpTLVPVGR-------PLHNVQVYI-LD-EAQQP-----------VPLGGEGEFcIGGI-- 410
Cdd:cd05937   234 AATE---GVFALTNHNVGDF-GAGAIGHhglirrwKFENQVVLVkMDpETDDPirdpktgfcvrAPVGEPGEM-LGRVpf 308

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  411 ---GLARGYHNLPDLTNEKFIPNPFgtnENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQA 487
Cdd:cd05937   309 knrEAFQGYLHNEDATESKLVRDVF---RKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPD 385

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  488 VRECAVVAREIAGHTQLVGY--IIAKDTLNLSFDKLEPILRQYSEAVLPEYMIPtRFINI 545
Cdd:cd05937   386 IAEANVYGVKVPGHDGRAGCaaITLEESSAVPTEFTKSLLASLARKNLPSYAVP-LFLRL 444

PLN02654

acetate-CoA ligase

46-576

3.10e-05

acetate-CoA ligase

Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 49.51 E-value: 3.10e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   46 EQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDARILL 125
Cdd:PLN02654  118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  126 TSTDVaKKLALTIPaLQECQTVYLDQEifEYDFHFLAIAKLLHNQylrllhfyfytLIQQCQATSVSQGIQT---QVLPN 202
Cdd:PLN02654  198 TCNAV-KRGPKTIN-LKDIVDAALDES--AKNGVSVGICLTYENQ-----------LAMKREDTKWQEGRDVwwqDVVPN 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  203 NLAYC-------------IYTSGSTGNPKGILmehrslvnmlwwHQQTRPSVQGVRTLQFcavSFDFSCHEIF--STLC- 266
Cdd:PLN02654  263 YPTKCevewvdaedplflLYTSGSTGKPKGVL------------HTTGGYMVYTATTFKY---AFDYKPTDVYwcTADCg 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  267 -------------LGGILVLVPEAVRQNPFA--LAEFISQQKIEKLFLPVIALLQLA----EAVNGNKSTSLALceVITT 327
Cdd:PLN02654  328 witghsyvtygpmLNGATVLVFEGAPNYPDSgrCWDIVDKYKVTIFYTAPTLVRSLMrdgdEYVTRHSRKSLRV--LGSV 405

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  328 GEQmqITPAVANLFqktgamlHNHYGATE--FQDATTHTLKGN------PEGWPtLVP--VGRPLHNVQVYILDEAQQPV 397
Cdd:PLN02654  406 GEP--INPSAWRWF-------FNVVGDSRcpISDTWWQTETGGfmitplPGAWP-QKPgsATFPFFGVQPVIVDEKGKEI 475

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  398 PLGGEGEFCI-----GGIGLARGYHNLPDLTNEKfipnPFgtnenaKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFR 472
Cdd:PLN02654  476 EGECSGYLCVkkswpGAFRTLYGDHERYETTYFK----PF------AGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHR 545

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  473 VELGEIESVLASHQAVRECAVVA--REIAGHTqLVGYIIAKDTLNLSfDKLEPILRQYSEAVLPEYMIPTRFINISNMPL 550
Cdd:PLN02654  546 IGTAEVESALVSHPQCAEAAVVGieHEVKGQG-IYAFVTLVEGVPYS-EELRKSLILTVRNQIGAFAAPDKIHWAPGLPK 623

                         570       580       590
                  ....*....|....*....|....*....|...
gi 602182148  551 TPSGKLDRRALP-------DPKGDRPALSTPLV 576
Cdd:PLN02654  624 TRSGKIMRRILRkiasrqlDELGDTSTLADPGV 656

PRK05851

long-chain-fatty acid--ACP ligase MbtM;

378-558

5.72e-05

long-chain-fatty acid--ACP ligase MbtM;

Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 48.61 E-value: 5.72e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  378 VGRPLHNVQVYIlDEAQQPVPLGGE--GEFCIGGIGLARGYHNLPDLTNEKFIPnpfgtnenakklyrTGDLArYLPDGT 455
Cdd:PRK05851  347 LGNPIPGMEVRI-SPGDGAAGVAGReiGEIEIRGASMMSGYLGQAPIDPDDWFP--------------TGDLG-YLVDGG 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  456 IEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLVGYIIAKDTL--NLSFDKLEPILRQYSE-AV 532
Cdd:PRK05851  411 LVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSARPGLVIAAEFRgpDEAGARSEVVQRVASEcGV 490

                         170       180
                  ....*....|....*....|....*.
gi 602182148  533 LPEYMIptrFINISNMPLTPSGKLDR 558
Cdd:PRK05851  491 VPSDVV---FVAPGSLPRTSSGKLRR 513

PRK08317

hypothetical protein; Provisional

2100-2217

6.14e-05

hypothetical protein; Provisional

Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 47.24 E-value: 6.14e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2100 ALEQLPPERGWRILEIGAGTGGTTAYlLPHLPGDQTKYVFTDISAFFLAKAEERFK-DYPFVRYQVLDIEQAPqaqgFEP 2178
Cdd:PRK08317   11 TFELLAVQPGDRVLDVGCGPGNDARE-LARRVGPEGRVVGIDRSEAMLALAKERAAgLGPNVEFVRGDADGLP----FPD 85

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 602182148 2179 QIYDLIVAADVLHATSDLRQTLVHIRQLLAPGGMLILME 2217
Cdd:PRK08317   86 GSFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVLD 124

SCP-x_thiolase

cd00829

Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...

761-879

9.09e-05

Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.

Pssm-ID: 238425 [Multi-domain] Cd Length: 375 Bit Score: 47.64 E-value: 9.09e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  761 ILLECAWEAFERAGynpETYPEPVGVYAGSSLStyllnnigsalgiiteqpfietdmeqfqakiGNDRSYLATRISYKLN 840
Cdd:cd00829    19 LAAEAARAALDDAG---LEPADIDAVVVGNAAG-------------------------------GRFQSFPGALIAEYLG 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 602182148  841 LKG-PSVNVQTACSTSLVAVHMACQSLISGECQMALAGGI 879
Cdd:cd00829    65 LLGkPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGA 104

COG3963

Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];

2101-2214

9.49e-05

Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];

Pssm-ID: 443163 Cd Length: 193 Bit Score: 45.97 E-value: 9.49e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2101 LEQLPPERGWRILEIGAGTGGTTAYLLPHLPGDQTKYVFtDISAFFLAKAEERFKDYPFVRYQVLDIEQAPQAQGFEPqi 2180
Cdd:COG3963    38 ASEVDWSGAGPVVELGPGTGVFTRAILARGVPDARLLAV-EINPEFAEHLRRRFPRVTVVNGDAEDLAELLAEHGIGK-- 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 602182148 2181 YDLIVaadvlhatS---------DLRQTLVH-IRQLLAPGGMLI 2214
Cdd:COG3963   115 VDAVV--------SglpllsfppELRRAILDaAFRVLAPGGVFV 150

PRK05620

long-chain fatty-acid--CoA ligase;

44-227

1.01e-04

long-chain fatty-acid--CoA ligase;

Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 47.86 E-value: 1.01e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   44 DGEQSLTYGELNVRANHLAqHLL--SLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPADRIEYMLRDSDA 121
Cdd:PRK05620   34 AEQEQTTFAAIGARAAALA-HALhdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAED 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  122 RILLTSTDVAKKLAltiPALQECQTVYLDQEIFEYDFHFLAIAKLLHnqylrlLHFYFYTLIQQCQATSVSQgiqtQVLP 201
Cdd:PRK05620  113 EVIVADPRLAEQLG---EILKECPCVRAVVFIGPSDADSAAAHMPEG------IKVYSYEALLDGRSTVYDW----PELD 179

                         170       180
                  ....*....|....*....|....*..
gi 602182148  202 NNLAYCI-YTSGSTGNPKGILMEHRSL 227
Cdd:PRK05620  180 ETTAAAIcYSTGTTGAPKGVVYSHRSL 206

PLN02614

long-chain acyl-CoA synthetase

201-488

1.86e-04

long-chain acyl-CoA synthetase

Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 46.94 E-value: 1.86e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  201 PNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVS-------FDFSCHEIF----------- 262
Cdd:PLN02614  222 KSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANAALTVKDVYLSylplahiFDRVIEECFiqhgaaigfwr 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  263 --STLCLGGILVLVPEAVRQNPFALAEFIS--QQKI------EKLFLPVIALLQLAEAVNGNKSTSLA-LCEVITTGEQM 331
Cdd:PLN02614  302 gdVKLLIEDLGELKPTIFCAVPRVLDRVYSglQKKLsdggflKKFVFDSAFSYKFGNMKKGQSHVEASpLCDKLVFNKVK 381

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  332 QITPAVANLFQKTGAMLHNH----------------YGATEFQDATTHTLkgnPEGWPTLVPVGRPLHNVQVYIldeaqQ 395
Cdd:PLN02614  382 QGLGGNVRIILSGAAPLASHvesflrvvacchvlqgYGLTESCAGTFVSL---PDELDMLGTVGPPVPNVDIRL-----E 453

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  396 PVP------LGG--EGEFCIGGIGLARGYHNLPDLTNEKFIPNpfgtnenakkLYRTGDLARYLPDGTIEHLGRIDHQVK 467
Cdd:PLN02614  454 SVPemeydaLAStpRGEICIRGKTLFSGYYKREDLTKEVLIDG----------WLHTGDVGEWQPNGSMKIIDRKKNIFK 523

                         330       340
                  ....*....|....*....|..
gi 602182148  468 I-RGFRVELGEIESVLASHQAV 488
Cdd:PLN02614  524 LsQGEYVAVENIENIYGEVQAV 545

Thiolase_N

pfam00108

Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...

844-878

4.35e-04

Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.

Pssm-ID: 459676 [Multi-domain] Cd Length: 260 Bit Score: 44.60 E-value: 4.35e-04

                           10        20        30
                   ....*....|....*....|....*....|....*
gi 602182148   844 PSVNVQTACSTSLVAVHMACQSLISGECQMALAGG 878
Cdd:pfam00108   77 PAVTINKVCGSGLKAVYLAAQSIASGDADVVLAGG 111

PRK07867

acyl-CoA synthetase; Validated

352-564

4.49e-04

acyl-CoA synthetase; Validated

Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 45.83 E-value: 4.49e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  352 YGATEFQDATTHTlKGNPEGwptlvPVGRPLHNVQvyILD-EAQQPVPLG-------GEGEFCIG------GIGLARGYH 417
Cdd:PRK07867  297 FGSTEGGVAITRT-PDTPPG-----ALGPLPPGVA--IVDpDTGTECPPAedadgrlLNADEAIGelvntaGPGGFEGYY 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  418 NLPDLTNEKFipnpfgtnenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAR- 496
Cdd:PRK07867  369 NDPEADAERM----------RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVp 438

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 602182148  497 -EIAGhTQLVGYIIAKDTLNLSFDKLEPILRQYSEavLPEYMIPtRFINISN-MPLTPSGKLDRRAL-------PDP 564
Cdd:PRK07867  439 dPVVG-DQVMAALVLAPGAKFDPDAFAEFLAAQPD--LGPKQWP-SYVRVCAeLPRTATFKVLKRQLsaegvdcADP 511

PRK12939

short chain dehydrogenase; Provisional

2536-2691

6.71e-04

short chain dehydrogenase; Provisional

Pssm-ID: 183833 [Multi-domain] Cd Length: 250 Bit Score: 44.19 E-value: 6.71e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2536 VARFLVTNGARylVLVGrRGAREEQQAQLSELEQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVIHAAGTLNDGI 2613
Cdd:PRK12939   23 FAEALAEAGAT--VAFN-DGLAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAAaaALGGLDGLVNNAGITNSKS 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2614 LQQQSWQAFKEVMNPKVAGAWNL------HIltKNQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGL-ASYRRHLGLP 2686
Cdd:PRK12939  100 ATELDIDTWDAVMNVNVRGTFLMlraalpHL--RDSGRGRIVNLASDTALWGAPKLGAYVASKGAVIGMtRSLARELGGR 177


                  ....*
gi 602182148 2687 SLSIN 2691
Cdd:PRK12939  178 GITVN 182

PRK07008

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

50-228

7.75e-04

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

Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 45.08 E-value: 7.75e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148   50 TYGELNVRANHLAQHLLSLGCQPDD---LLAICIERSAELFIGLLGiLKAGCAYVPLDVgYPaDRIEYMLRDSDARILLt 126
Cdd:PRK07008   41 TYRDCERRAKQLAQALAALGVEPGDrvgTLAWNGYRHLEAYYGVSG-SGAVCHTINPRL-FP-EQIAYIVNHAEDRYVL- 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  127 stdvakklaltipalqecqtvyldqeifeYDFHFLAIAKLLHNQYLRLLHFYFYTLIQQCQATSV------------SQG 194
Cdd:PRK07008  117 -----------------------------FDLTFLPLVDALAPQCPNVKGWVAMTDAAHLPAGSTpllcyetlvgaqDGD 167

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 602182148  195 IQTQVLPNNLA-YCIYTSGSTGNPKGILMEHRSLV 228
Cdd:PRK07008  168 YDWPRFDENQAsSLCYTSGTTGNPKGALYSHRSTV 202

PaaJ

COG0183

Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...

844-878

9.04e-04

Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis

Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 44.29 E-value: 9.04e-04

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 602182148  844 PSVNVQTACSTSLVAVHMACQSLISGECQMALAGG 878
Cdd:COG0183    80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGG 114

ubiE

PRK00216

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...

2100-2221

9.16e-04

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;

Pssm-ID: 234689 [Multi-domain] Cd Length: 239 Bit Score: 43.60 E-value: 9.16e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2100 ALEQLPPERGWRILEIGAGTgGTTAYLLPHLPGDQTKYVFTDISAFFLAKAEERFKDY---PFVRYQVLDIEQAPqaqgF 2176
Cdd:PRK00216   43 TIKWLGVRPGDKVLDLACGT-GDLAIALAKAVGKTGEVVGLDFSEGMLAVGREKLRDLglsGNVEFVQGDAEALP----F 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 602182148 2177 EPQIYDLIVAADVLHATSDLRQTLVHIRQLLAPGGMLILMEDSEP 2221
Cdd:PRK00216  118 PDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVILEFSKP 162

Pcm

COG2518

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...

2101-2214

9.64e-04

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];

Pssm-ID: 442008 [Multi-domain] Cd Length: 197 Bit Score: 42.77 E-value: 9.64e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2101 LEQLPPERGWRILEIGAGTGGTTAyLLPHLpgdqTKYVFT-DISAFFLAKAEERFKD--YPFVRYQVLD-----IEQAPq 2172
Cdd:COG2518    59 LEALDLKPGDRVLEIGTGSGYQAA-VLARL----AGRVYSvERDPELAERARERLAAlgYDNVTVRVGDgalgwPEHAP- 132

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 602182148 2173 aqgfepqiYDLI-VAAdvlhATSDLRQTLVhirQLLAPGGMLI 2214
Cdd:COG2518   133 --------FDRIiVTA----AAPEVPEALL---EQLAPGGRLV 160

AcpA

COG3433

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...

2751-2878

1.11e-03

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];

Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 43.97 E-value: 1.11e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2751 LARQLTPQPFFGDAMKSIDTSVGKLTLQERDSCPQGYGHNIREQLENAPPKEGL--TLLQAHVREQVSQVLGIDTKTLLA 2828
Cdd:COG3433   162 LAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALetALTEEELRADVAELLGVDPEEIDP 241

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 602182148 2829 EQDvgFFTLGMDSLTSVELRNRLQAsLGCSLSSTLAFDYPTQQALVNYLA 2878
Cdd:COG3433   242 DDN--LFDLGLDSIRLMQLVERWRK-AGLDVSFADLAEHPTLAAWWALLA 288

thiolase

cd00751

Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...

844-879

1.13e-03

Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.

Pssm-ID: 238383 [Multi-domain] Cd Length: 386 Bit Score: 44.01 E-value: 1.13e-03

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 602182148  844 PSVNVQTACSTSLVAVHMACQSLISGECQMALAGGI 879
Cdd:cd00751    76 PATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGV 111

PRK12936

3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed

2536-2716

1.22e-03

3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed

Pssm-ID: 171820 [Multi-domain] Cd Length: 245 Bit Score: 43.37 E-value: 1.22e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2536 VARFLVTNGArylvLVGRRGAREEQQAQLSEleQLGASVKVLQADIADAEQLaQALSAVTYPPLRGV---IHAAGTLNDG 2612
Cdd:PRK12936   22 IARLLHAQGA----IVGLHGTRVEKLEALAA--ELGERVKIFPANLSDRDEV-KALGQKAEADLEGVdilVNNAGITKDG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2613 ILQQQSWQAFKEVMNPKVAGAWNL-----HILTKNQpLDFFVLFSSATSLLGNAGQANHAAANAFLDGLA-SYRRHLGLP 2686
Cdd:PRK12936   95 LFVRMSDEDWDSVLEVNLTATFRLtreltHPMMRRR-YGRIINITSVVGVTGNPGQANYCASKAGMIGFSkSLAQEIATR 173

                         170       180       190
                  ....*....|....*....|....*....|
gi 602182148 2687 SLSINwgtWSEVGIAARLGLDKLSSKQGEG 2716
Cdd:PRK12936  174 NVTVN---CVAPGFIESAMTGKLNDKQKEA 200

hydroxyacyl-CoA-like_DH_SDR_c-like

cd05353

(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...

2578-2677

1.37e-03

(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids in eukaryotes occurs by a four-reaction cycle, that may take place in mitochondria or in peroxisomes. (3R)-hydroxyacyl-CoA dehydrogenase is part of rat peroxisomal multifunctional MFE-2, it is a member of the NAD-dependent SDRs, but contains an additional small C-terminal domain that completes the active site pocket and participates in dimerization. The atypical, additional C-terminal extension allows for more extensive dimerization contact than other SDRs. MFE-2 catalyzes the second and third reactions of the peroxisomal beta oxidation cycle. Proteins in this subgroup have a typical catalytic triad, but have a His in place of the usual upstream Asn. This subgroup also contains members identified as 17-beta-hydroxysteroid dehydrogenases, including human peroxisomal 17-beta-hydroxysteroid dehydrogenase type 4 (17beta-HSD type 4, aka MFE-2, encoded by HSD17B4 gene) which is involved in fatty acid beta-oxidation and steroid metabolism. This subgroup also includes two SDR domains of the Neurospora crassa and Saccharomyces cerevisiae multifunctional beta-oxidation protein (MFP, aka Fox2). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187611 [Multi-domain] Cd Length: 250 Bit Score: 43.08 E-value: 1.37e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2578 QADIADAEQLAQ-ALSAvtYPPLRGVIHAAGTLNDGILQQQSWQAFKEVMNPKVAG-------AWNlHIltKNQPLDFFV 2649
Cdd:cd05353    69 YDSVEDGEKIVKtAIDA--FGRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGsfkvtraAWP-YM--RKQKFGRII 143

                          90       100
                  ....*....|....*....|....*...
gi 602182148 2650 LFSSATSLLGNAGQANHAAANAFLDGLA 2677
Cdd:cd05353   144 NTSSAAGLYGNFGQANYSAAKLGLLGLS 171

TrmR

COG4122

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...

2111-2215

1.87e-03

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification

Pssm-ID: 443298 Cd Length: 173 Bit Score: 41.71 E-value: 1.87e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2111 RILEIGAGTGGTTAYLLPHLPGDqTKYVFTDISAFFLAKAEERFKDYPF---VRYQVLD-IEQAPQaqgFEPQIYDLIVA 2186
Cdd:COG4122    19 RILEIGTGTGYSTLWLARALPDD-GRLTTIEIDPERAAIARENFARAGLadrIRLILGDaLEVLPR---LADGPFDLVFI 94

                          90       100       110
                  ....*....|....*....|....*....|
gi 602182148 2187 -ADVLHATSDLRqtlvHIRQLLAPGGMLIL 2215
Cdd:COG4122    95 dADKSNYPDYLE----LALPLLRPGGLIVA 120

PLN03052

acetate--CoA ligase; Provisional

387-561

1.92e-03

acetate--CoA ligase; Provisional

Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 43.91 E-value: 1.92e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  387 VYILDEAQQPVPlggEGEFCIGGIGLarGYHNL--------PDLTNEKFIPNPFgtnENAKKLYRTGDLARYLPDGTIEH 458
Cdd:PLN03052  536 LFILDDSGNPYP---DDAPCTGELAL--FPLMFgasstllnADHYKVYFKGMPV---FNGKILRRHGDIFERTSGGYYRA 607

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  459 LGRIDHQVKIRGFRVELGEIESVL-ASHQAVRECAVVAREIA--GHTQLV---------GYIIAKDTLNLSF-----DKL 521
Cdd:PLN03052  608 HGRADDTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPPggGPEQLViaavlkdppGSNPDLNELKKIFnsaiqKKL 687

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 602182148  522 EPILRQYSEAVLPEYmiptrfinisnmPLTPSGKLDRRAL 561
Cdd:PLN03052  688 NPLFKVSAVVIVPSF------------PRTASNKVMRRVL 715

Methyltransf_24

pfam13578

Methyltransferase domain; This family appears to be a methyltransferase domain.

2113-2215

2.72e-03

Methyltransferase domain; This family appears to be a methyltransferase domain.

Pssm-ID: 433324 [Multi-domain] Cd Length: 106 Bit Score: 39.60 E-value: 2.72e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  2113 LEIGAGTGGTTAYLLPHLP-GDQTKYVFTDI------SAFFLAKAEERfkdyPFVRYQVLDIEQApqAQGFEPQIYDLIV 2185
Cdd:pfam13578    1 VEIGTYSGVSTLWLAAALRdNGLGRLTAVDPdpgaeeAGALLRKAGLD----DRVRLIVGDSREA--LPSLADGPIDLLF 74

                           90       100       110
                   ....*....|....*....|....*....|
gi 602182148  2186 AaDVLHATSDLRQTLVHIRQLLAPGGMLIL 2215
Cdd:pfam13578   75 I-DGDHTYEAVLNDLELWLPRLAPGGVILF 103

PLN02430

long-chain-fatty-acid-CoA ligase

398-481

2.77e-03

long-chain-fatty-acid-CoA ligase

Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 43.27 E-value: 2.77e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  398 PLGG--EGEFCIGGIGLARGYHNLPDLTNEKFipnpfgtnenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKI-RGFRVE 474
Cdd:PLN02430  459 PLGEppRGEICVRGKCLFSGYYKNPELTEEVM----------KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLsQGEYVA 528


                  ....*..
gi 602182148  475 LGEIESV 481
Cdd:PLN02430  529 LEYLENV 535

PaaK

COG1541

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...

442-497

4.22e-03

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];

Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 42.44 E-value: 4.22e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 602182148  442 YRTGDLARYLPD----GT----IE-HLGRIDHQVKIRGFRVELGEIESVLASHQAVREC--AVVARE 497
Cdd:COG1541   297 YRTGDLTRLLPEpcpcGRthprIGrILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEyqIVVDRE 363

PLN02861

long-chain-fatty-acid-CoA ligase

403-495

4.30e-03

long-chain-fatty-acid-CoA ligase

Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 42.52 E-value: 4.30e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  403 GEFCIGGIGLARGYHNLPDLTNEKFIPNPFgtnenakklyRTGDLARYLPDGTIEhlgRIDHQVKIrgFRVELGEIESVL 482
Cdd:PLN02861  466 GEICLRGNTLFSGYHKRQDLTEEVLIDGWF----------HTGDIGEWQPNGAMK---IIDRKKNI--FKLSQGEYVAVE 530

                          90
                  ....*....|...
gi 602182148  483 ASHQAVRECAVVA 495
Cdd:PLN02861  531 NLENTYSRCPLIA 543

PRK12316

peptide synthase; Provisional

2798-2899

4.61e-03

peptide synthase; Provisional

Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 43.02 E-value: 4.61e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2798 APPKEGLTLLQ----AHVREQVSQVLGIDTKTLLAEQdVG----FFTLGMDSLTSVELRNRLQASLGCSLSSTLAFDYPT 2869
Cdd:PRK12316 5053 ALPQPDASLLQqayvAPRSELEQQVAAIWAEVLQLER-VGlddnFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPT 5131

                          90       100       110
                  ....*....|....*....|....*....|..
gi 602182148 2870 QQALVNYLANELLGTPEQLQEPES--DEEDEI 2899
Cdd:PRK12316 5132 LAAFVELAAAAGSGDDEKFDDLEEllSELEEI 5163

PRK06814

acyl-[ACP]--phospholipid O-acyltransferase;

442-557

5.25e-03

acyl-[ACP]--phospholipid O-acyltransferase;

Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 42.65 E-value: 5.25e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148  442 YRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGH-TQLVGYIIAKDTlnlsfdK 520
Cdd:PRK06814 1012 YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKgERIILLTTASDA------T 1085

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 602182148  521 LEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLD 557
Cdd:PRK06814 1086 RAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122

PRK12824

3-oxoacyl-ACP reductase;

2536-2676

6.25e-03

3-oxoacyl-ACP reductase;

Pssm-ID: 183773 [Multi-domain] Cd Length: 245 Bit Score: 40.90 E-value: 6.25e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2536 VARFLVTNGarYLVLVGRRGAREEQQAQLSELEQLGASVKVLQADIADAEQLAQALSAVT--YPPLRGVIHAAGTLNDGI 2613
Cdd:PRK12824   18 IARELLNDG--YRVIATYFSGNDCAKDWFEEYGFTEDQVRLKELDVTDTEECAEALAEIEeeEGPVDILVNNAGITRDSV 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 602182148 2614 LQQQSWQAFKEVMNPKVAGAWNLHILT----KNQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGL 2676
Cdd:PRK12824   96 FKRMSHQEWNDVINTNLNSVFNVTQPLfaamCEQGYGRIINISSVNGLKGQFGQTNYSAAKAGMIGF 162

PRK01683

trans-aconitate 2-methyltransferase; Provisional

2101-2263

7.51e-03

trans-aconitate 2-methyltransferase; Provisional

Pssm-ID: 234970 Cd Length: 258 Bit Score: 41.08 E-value: 7.51e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2101 LEQLPPERGWRILEIGAGTGGTTAYLLPHLPGDQTkyVFTDISAFFLAKAEERFKDYPFVRyqvLDIEQ-APqaqgfePQ 2179
Cdd:PRK01683   24 LARVPLENPRYVVDLGCGPGNSTELLVERWPAARI--TGIDSSPAMLAEARSRLPDCQFVE---ADIASwQP------PQ 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2180 IYDLIVAADVLHATSDLRQTLVHIRQLLAPGGML-------------ILMED-SEPARWADltfgltegwwKFTDHDLRP 2245
Cdd:PRK01683   93 ALDLIFANASLQWLPDHLELFPRLVSLLAPGGVLavqmpdnldepshVLMREvAENGPWEQ----------NLPDRGARR 162

                         170
                  ....*....|....*...
gi 602182148 2246 NhPLLSPEQWQILLSEMG 2263
Cdd:PRK01683  163 A-PLPPPHAYYDALAPAA 179

PRK05875

short chain dehydrogenase; Provisional

2519-2607

7.92e-03

short chain dehydrogenase; Provisional

Pssm-ID: 180300 [Multi-domain] Cd Length: 276 Bit Score: 40.94 E-value: 7.92e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2519 DDGSYLIAGGLGGLGLVVARFLVTNGARyLVLVGRRGAREEQQAQlsELEQLGA--SVKVLQADIADAEQLAQALSAVT- 2595
Cdd:PRK05875    6 QDRTYLVTGGGSGIGKGVAAGLVAAGAA-VMIVGRNPDKLAAAAE--EIEALKGagAVRYEPADVTDEDQVARAVDAATa 82

                          90
                  ....*....|...
gi 602182148 2596 -YPPLRGVIHAAG 2607
Cdd:PRK05875   83 wHGRLHGVVHCAG 95

ChcA_like_SDR_c

cd05359

1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...

2540-2679

8.11e-03

1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup contains classical SDR proteins, including members identified as 1-cyclohexenylcarbonyl coenzyme A reductase. ChcA of Streptomyces collinus is implicated in the final reduction step of shikimic acid to ansatrienin. ChcA shows sequence similarity to the SDR family of NAD-binding proteins, but it lacks the conserved Tyr of the characteristic catalytic site. This subgroup also contains the NADH-dependent enoyl-[acyl-carrier-protein(ACP)] reductase FabL from Bacillus subtilis. This enzyme participates in bacterial fatty acid synthesis, in type II fatty-acid synthases and catalyzes the last step in each elongation cycle. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187617 [Multi-domain] Cd Length: 242 Bit Score: 40.80 E-value: 8.11e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2540 LVTNGAR--------------YLVLVGRRGAREEQQAQLSELEQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVI 2603
Cdd:cd05359     2 LVTGGSRgigkaialrlaergADVVINYRKSKDAAAEVAAEIEELGGKAVVVRADVSQPQDVEEMFAAVkeRFGRLDVLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2604 H--AAGTLNDgiLQQQSWQAFKEVMNPKVAGAwnLHILTKNQPL------DFFVLFSSATSLLGNAGQANHAAANAFLDG 2675
Cdd:cd05359    82 SnaAAGAFRP--LSELTPAHWDAKMNTNLKAL--VHCAQQAAKLmrerggGRIVAISSLGSIRALPNYLAVGTAKAALEA 157


                  ....
gi 602182148 2676 LASY 2679
Cdd:cd05359   158 LVRY 161

SPR-like_SDR_c

cd05367

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...

2536-2626

9.73e-03

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, 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. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187625 [Multi-domain] Cd Length: 241 Bit Score: 40.35 E-value: 9.73e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 602182148 2536 VARFLVTNGARY-LVLVGRrgaREEQQAQLSELEQLGASVKVLQADIADAEQLAQALSAVtyPPLRG----VIHAAGTLN 2610
Cdd:cd05367    15 LAEELLKRGSPSvVVLLAR---SEEPLQELKEELRPGLRVTTVKADLSDAAGVEQLLEAI--RKLDGerdlLINNAGSLG 89

                          90
                  ....*....|....*..
gi 602182148 2611 D-GILQQQSWQAFKEVM 2626
Cdd:cd05367    90 PvSKIEFIDLDELQKYF 106

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