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Conserved domains on  [gi|22327387|ref|NP_198442|]
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AMP-dependent synthetase and ligase family protein [Arabidopsis thaliana]

Protein Classification

non-ribosomal peptide synthetase( domain architecture ID 10147962)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 3-472 1.10e-130

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: 403.45  E-value: 1.10e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    3 KVVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVlslisssnislviacglssveSHWLveRNVCPVLLFSMDEK 82
Cdd:cd05930   38 DLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERL---------------------AYIL--EDSGAKLVLTDPDD 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   83 LsvetgcssfvwpckkerqrkfCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFIDHIQEFL 162
Cdd:cd05930   95 L---------------------AYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIF 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  163 GAILSSTALVIPPFTLLKeNMISIIDFLEEYSISRLLAVPSMIRAILPTLQHRGHNNklqscLKLVVLSGEPFPVSLWDS 242
Cdd:cd05930  154 GALLAGATLVVLPEEVRK-DPEALADLLAEEGITVLHLTPSLLRLLLQELELAALPS-----LRLVLVGGEALPPDLVRR 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  243 LHSLLPETCFLNLYGSTEVSGDCTYFDCSELPrllktEEIGSVPIGKSISNCKVVLLGDEDKP----YEGEICVSGLCLS 318
Cdd:cd05930  228 WRELLPGARLVNLYGPTEATVDATYYRVPPDD-----EEDGRVPIGRPIPNTRVYVLDENLRPvppgVPGELYIGGAGLA 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  319 QGYmhssiesegyvklHNNSlcnHLTND-------CGSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIET 391
Cdd:cd05930  303 RGY-------------LNRP---ELTAErfvpnpfGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEA 366

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  392 TLELNPDIAEAVVLLSRDETELASLKAFVVLNKEsnsSDGIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEA 471
Cdd:cd05930  367 ALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEG---GELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKA 443


                 .
gi 22327387  472 L 472
Cdd:cd05930  444 L 444
PQQ_DH_like super family cl11493
PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases ...
 677-1028 7.84e-14

PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases with pyrroloquinoline quinone (PQQ) as a cofactor, such as ethanol, methanol, and membrane-bound glucose dehydrogenases. The alignment model contains an 8-bladed beta-propeller, and the family also includes distantly related proteins which are not enzymatically active and do not bind PQQ.


The actual alignment was detected with superfamily member TIGR03300:

Pssm-ID: 472205 [Multi-domain]  Cd Length: 377  Bit Score: 74.58  E-value: 7.84e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    677 VSMQEIWKVHMESCVDASPL----VVLKDSktyLFIGSHSRKFSCIDAKSGSMYWETILEGRIegSAMVVGDFSQVVIGC 752
Cdd:TIGR03300   38 VKVDQVWSASVGDGVGHYYLrlqpAVAGGK---VYAADADGTVAALDAETGKRLWRVDLDERL--SGGVGADGGLVFVGT 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    753 YKGKLYFLDFSTGSLCWKFQACGEIKCQPVVDtsSQLIWCGSHDHTLYALD---------YRSQccVYKLQCGGSifASP 823
Cdd:TIGR03300  113 EKGEVIALDAEDGKELWRAKLSSEVLSPPLVA--NGLVVVRTNDGRLTALDaatgerlwtYSRV--TPPLTLRGS--ASP 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    824 AIDEGhsSLYVASTSGRVIAVSIKDSpfHTLWlfelEAPIF---GSLCI--------TPSTQNVICCLV--DGQVIAMSP 890
Cdd:TIGR03300  187 VIADG--GVLVGFAGGKLVALDLQTG--QPLW----EQRVAlpkGRTELerlvdvdgDPVVDGGQVYAVsyQGRVAALDL 258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    891 -SGTIIWRYRTGGPifAGPCMSHvlpSQVLVCCRNGCVYSLEPESGCLVWednigdpitasayidENLHFESHEL---LA 966
Cdd:TIGR03300  259 rSGRVLWKRDASSY--QGPAVDD---NRLYVTDADGVVVALDRRSGSELW---------------KNDELKYRQLtapAV 318

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22327387    967 SDRLVTVCSSSGRVHVL-RVRPSILSRDSHDSkvgeitrmelqADIFSSPVMIGGRIFVGCRD 1028
Cdd:TIGR03300  319 LGGYLVVGDFEGYLHWLdRDDGSFVARLKTDG-----------SGIASPPVVVGDGLLVQTRD 370
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 498-548 5.68e-06

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: 44.86  E-value: 5.68e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 22327387    498 IKKAVCDALLV--KEVSDDDDFFAIGGDSLAAAHLSHSL------GIDMRLIYQFRSPS 548
Cdd:pfam00550    3 LRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLeeefgvEIPPSDLFEHPTLA 61
 
Name Accession Description Interval E-value
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 3-472 1.10e-130

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: 403.45  E-value: 1.10e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    3 KVVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVlslisssnislviacglssveSHWLveRNVCPVLLFSMDEK 82
Cdd:cd05930   38 DLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERL---------------------AYIL--EDSGAKLVLTDPDD 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   83 LsvetgcssfvwpckkerqrkfCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFIDHIQEFL 162
Cdd:cd05930   95 L---------------------AYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIF 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  163 GAILSSTALVIPPFTLLKeNMISIIDFLEEYSISRLLAVPSMIRAILPTLQHRGHNNklqscLKLVVLSGEPFPVSLWDS 242
Cdd:cd05930  154 GALLAGATLVVLPEEVRK-DPEALADLLAEEGITVLHLTPSLLRLLLQELELAALPS-----LRLVLVGGEALPPDLVRR 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  243 LHSLLPETCFLNLYGSTEVSGDCTYFDCSELPrllktEEIGSVPIGKSISNCKVVLLGDEDKP----YEGEICVSGLCLS 318
Cdd:cd05930  228 WRELLPGARLVNLYGPTEATVDATYYRVPPDD-----EEDGRVPIGRPIPNTRVYVLDENLRPvppgVPGELYIGGAGLA 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  319 QGYmhssiesegyvklHNNSlcnHLTND-------CGSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIET 391
Cdd:cd05930  303 RGY-------------LNRP---ELTAErfvpnpfGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEA 366

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  392 TLELNPDIAEAVVLLSRDETELASLKAFVVLNKEsnsSDGIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEA 471
Cdd:cd05930  367 ALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEG---GELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKA 443


                 .
gi 22327387  472 L 472
Cdd:cd05930  444 L 444
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 4-531 3.40e-79

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: 283.29  E-value: 3.40e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    4 VVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSlisssnislVIA-CGLSSV--ESHWLVERNVCPVLLFSMD 80
Cdd:COG1020  528 LVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAY---------MLEdAGARLVltQSALAARLPELGVPVLALD 598

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   81 EKLSVETGCSSFVWPCKKERQrkfCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFIDHIQE 160
Cdd:COG1020  599 ALALAAEPATNPPVPVTPDDL---AYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWE 675

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  161 FLGAILSSTALVIPPFTLLKeNMISIIDFLEEYSISRLLAVPSMIRAILPTLQHRGHNnklqscLKLVVLSGEPFPVSLW 240
Cdd:COG1020  676 IFGALLSGATLVLAPPEARR-DPAALAELLARHRVTVLNLTPSLLRALLDAAPEALPS------LRLVLVGGEALPPELV 748

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  241 DSLHSLLPETCFLNLYGSTEVSGDCTYFDCSELPrllktEEIGSVPIGKSISNCKVVLLGDEDKP----YEGEICVSGLC 316
Cdd:COG1020  749 RRWRARLPGARLVNLYGPTETTVDSTYYEVTPPD-----ADGGSVPIGRPIANTRVYVLDAHLQPvpvgVPGELYIGGAG 823

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  317 LSQGYmhssiesegyvklHNNSlcnHLT---------NDCGSQLyYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALE 387
Cdd:COG1020  824 LARGY-------------LNRP---ELTaerfvadpfGFPGARL-YRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELG 886

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  388 EIETTLELNPDIAEAVVLLSRDETELASLKAFVVLNKESNSSDGIIFSIRNWMggkLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:COG1020  887 EIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALL---LPPYMVPAAVVLLLPLPLTGNGKL 963

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327387  468 DYEALARlkcPTTGAQDMMQSNGTNSLLQNIKKAVCDALLVKEVSDDDDFFAIGGDSLAAAHLS 531
Cdd:COG1020  964 DRLALPA---PAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALA 1024
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 4-404 4.97e-76

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: 256.04  E-value: 4.97e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387      4 VVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSLISSSNISLVIACglssveSHW--LVERNVCPVLLFSMDE 81
Cdd:TIGR01733   27 RVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTD------SALasRLAGLVLPVILLDPLE 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387     82 KLSVETGCSSFvWPCKKERQRKFCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFiDH-IQE 160
Cdd:TIGR01733  101 LAALDDAPAPP-PPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSF-DAsVEE 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    161 FLGAILSSTALVIPPFTLLKENMISIIDFLEEYSISRLLAVPSMIRAILPtlqhrgHNNKLQSCLKLVVLSGEPFPVSLW 240
Cdd:TIGR01733  179 IFGALLAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALLAA------ALPPALASLRLVILGGEALTPALV 252

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    241 DSLHSLLPETCFLNLYGSTEVSGDCTYFDCSELPrllkTEEIGSVPIGKSISNCKVVLLGDEDKPY----EGEICVSGLC 316
Cdd:TIGR01733  253 DRWRARGPGARLINLYGPTETTVWSTATLVDPDD----APRESPVPIGRPLANTRLYVLDDDLRPVpvgvVGELYIGGPG 328

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    317 LSQGYMH-SSIESEGYVklhnnslcNHLTNDCGSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLEL 395
Cdd:TIGR01733  329 VARGYLNrPELTAERFV--------PDPFAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400


                   ....*....
gi 22327387    396 NPDIAEAVV 404
Cdd:TIGR01733  401 HPGVREAVV 409
PRK12467 PRK12467
peptide synthase; Provisional
 5-548 6.65e-65

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 241.22  E-value: 6.65e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387     5 VALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSLISSSNISLVIAcglssvESHWLVERNVC---PVLLfsMDE 81
Cdd:PRK12467  565 VGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLT------QSHLLAQLPVPaglRSLC--LDE 636

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    82 KLSVETGCSSfVWPCKKERQRKFCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFIDHIQEF 161
Cdd:PRK12467  637 PADLLCGYSG-HNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTEL 715

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   162 LGAILS-STALVIPPFTLLKENmiSIIDFLEEYSISRLLAVPSMIRAILPTLQhrghnNKLQSCLKLVVLSGEPFPVSLW 240
Cdd:PRK12467  716 FGALASgATLHLLPPDCARDAE--AFAALMADQGVTVLKIVPSHLQALLQASR-----VALPRPQRALVCGGEALQVDLL 788

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   241 DSLHSLLPETCFLNLYGSTEVSGDCTYFDCSELPRllkteEIGSVPIGKSISNCKVVLLGDEDKPYE----GEICVSGLC 316
Cdd:PRK12467  789 ARVRALGPGARLINHYGPTETTVGVSTYELSDEER-----DFGNVPIGQPLANLGLYILDHYLNPVPvgvvGELYIGGAG 863

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   317 LSQGYM-HSSIESEGYVKlhnnslcNHLTNDcGSQLyYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLEL 395
Cdd:PRK12467  864 LARGYHrRPALTAERFVP-------DPFGAD-GGRL-YRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLA 934

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   396 NPDIAEAVVlLSRDETELASLKAFVVLNKESNSSDGIIFS--IRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEALA 473
Cdd:PRK12467  935 QPGVREAVV-LAQPGDAGLQLVAYLVPAAVADGAEHQATRdeLKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALP 1013

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   474 rlKCPTTGAQDMMQSNGTNslLQNIKKAV-CDALLVKEVSDDDDFFAIGGDSLAA----AHLSHSLGIDMRLIYQFRSPS 548
Cdd:PRK12467 1014 --KPDASAVQATFVAPQTE--LEKRLAAIwADVLKVERVGLTDNFFELGGHSLLAtqviSRVRQRLGIQVPLRTLFEHQT 1089
AMP-binding pfam00501
AMP-binding enzyme;
4-379 2.88e-50

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 183.67  E-value: 2.88e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387      4 VVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSLISSSNISLVI---ACGLSSVESHWLVERNVCPVLLFSMD 80
Cdd:pfam00501   48 RVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLItddALKLEELLEALGKLEVVKLVLVLDRD 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387     81 ----EKLSVETGCSSFVWPCKKERQRKF--CYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYP----VVGEQRFAFKT 150
Cdd:pfam00501  128 pvlkEEPLPEEAKPADVPPPPPPPPDPDdlAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTL 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    151 SVGFI-DHIQEFLGAILSSTALVI-PPFTLLkeNMISIIDFLEEYSISRLLAVPSMIRAILptlQHRGHNNKLQSCLKLV 228
Cdd:pfam00501  208 PLFHDfGLSLGLLGPLLAGATVVLpPGFPAL--DPAALLELIERYKVTVLYGVPTLLNMLL---EAGAPKRALLSSLRLV 282

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    229 VLSGEPFPVSLWDSLHSLLPETcFLNLYGSTEVSGDCTYfdcsELPRLLKTEEIGSvpIGKSISNCKVVLLGDEDKPY-- 306
Cdd:pfam00501  283 LSGGAPLPPELARRFRELFGGA-LVNGYGLTETTGVVTT----PLPLDEDLRSLGS--VGRPLPGTEVKIVDDETGEPvp 355

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22327387    307 ---EGEICVSGLCLSQGYmhssiesegyvklHNNSlcnHLTNDC-GSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKL 379
Cdd:pfam00501  356 pgePGELCVRGPGVMKGY-------------LNDP---ELTAEAfDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKL 416
assembly_YfgL TIGR03300
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ...
 677-1028 7.84e-14

outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274511 [Multi-domain]  Cd Length: 377  Bit Score: 74.58  E-value: 7.84e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    677 VSMQEIWKVHMESCVDASPL----VVLKDSktyLFIGSHSRKFSCIDAKSGSMYWETILEGRIegSAMVVGDFSQVVIGC 752
Cdd:TIGR03300   38 VKVDQVWSASVGDGVGHYYLrlqpAVAGGK---VYAADADGTVAALDAETGKRLWRVDLDERL--SGGVGADGGLVFVGT 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    753 YKGKLYFLDFSTGSLCWKFQACGEIKCQPVVDtsSQLIWCGSHDHTLYALD---------YRSQccVYKLQCGGSifASP 823
Cdd:TIGR03300  113 EKGEVIALDAEDGKELWRAKLSSEVLSPPLVA--NGLVVVRTNDGRLTALDaatgerlwtYSRV--TPPLTLRGS--ASP 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    824 AIDEGhsSLYVASTSGRVIAVSIKDSpfHTLWlfelEAPIF---GSLCI--------TPSTQNVICCLV--DGQVIAMSP 890
Cdd:TIGR03300  187 VIADG--GVLVGFAGGKLVALDLQTG--QPLW----EQRVAlpkGRTELerlvdvdgDPVVDGGQVYAVsyQGRVAALDL 258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    891 -SGTIIWRYRTGGPifAGPCMSHvlpSQVLVCCRNGCVYSLEPESGCLVWednigdpitasayidENLHFESHEL---LA 966
Cdd:TIGR03300  259 rSGRVLWKRDASSY--QGPAVDD---NRLYVTDADGVVVALDRRSGSELW---------------KNDELKYRQLtapAV 318

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22327387    967 SDRLVTVCSSSGRVHVL-RVRPSILSRDSHDSkvgeitrmelqADIFSSPVMIGGRIFVGCRD 1028
Cdd:TIGR03300  319 LGGYLVVGDFEGYLHWLdRDDGSFVARLKTDG-----------SGIASPPVVVGDGLLVQTRD 370
PQQ_2 pfam13360
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
 680-898 1.89e-12

PQQ-like domain; This domain contains several repeats of the PQQ repeat.


Pssm-ID: 433144 [Multi-domain]  Cd Length: 233  Bit Score: 68.20  E-value: 1.89e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    680 QEIWKVHMESCVDASPLVvlkdSKTYLFIGSHSRKFSCIDAKSGSMYWETILEGRIEGSAMVVGDfsQVVIGCYKGKLYF 759
Cdd:pfam13360   14 AELWRVDLETGLGGGVAV----DGGRLFVATGGGQLVALDAATGKLLWRQTLSGEVLGAPLVAGG--RVFVVAGDGSLIA 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    760 LDFSTGSLCWKFQACGEikcQPVVDTSSQLIWcgsHDHTLYALDYRSQCCVYKLQCG--------------------GSI 819
Cdd:pfam13360   88 LDAADGRRLWSYQRSGE---PLALRSSGSPAV---VGDTVVAGFSSGKLVALDPATGkvrweaplaaprgtnelerlVDI 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    820 FASPAIDEGhsSLYVASTSGRVIAVSIKDSpfHTLWlfelEAPIFGSLCITPSTQNVICCLVDGQVIAMSP-SGTIIWRY 898
Cdd:pfam13360  162 TGTPVVAGG--RVFASAYQGRLVAFDAATG--RRLW----TREISGPNGPILDGDLLYVVSDDGELYALDRaTGAVVWKT 233
PQQ COG1520
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ...
 677-1038 2.98e-12

Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441129 [Multi-domain]  Cd Length: 370  Bit Score: 69.46  E-value: 2.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  677 VSMQEIWKVHMESCVDA--SPLV-VLKDSKtyLFIGSHSRKFSCIDAKSGSMYWETILEGRIegSAMVVGDFSQVVIGCY 753
Cdd:COG1520   30 VKVKQLWSASVGDGVGKgySRLApAVAGDR--VYAADADGRVAALDAATGKELWRVDLGEPL--SGGVGADGGLVVVGTE 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  754 KGKLYFLDFSTGSLCWKfqacgeikcqpvvdtsSQLiwcgshdhtlyaldyrsqccvyklqcGGSIFASPAIDEGHssLY 833
Cdd:COG1520  106 DGEVIALDADDGEELWR----------------ARL--------------------------SSEVLAAPAVAGGR--VV 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  834 VASTSGRVIAVSIKDSpfHTLWLFELEAPIF-----GSLCITPSTqnVICCLVDGQVIAMSP-SGTIIWRYR-------- 899
Cdd:COG1520  142 VRTGDGRVYALDAATG--ERLWSYQRPVPALtlrgtSSPVIVGGA--VLVGFANGKLVALDLaNGQPLWEQRvaqprgrt 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  900 --------TGGPIFAGPcmshvlpsqvLVCCR--NGCVYSLEPESGCLVWEDNIgdpitaSAYidenlhfesHELLASDR 969
Cdd:COG1520  218 elerlvdvDGTPVVDGG----------VVYAVayQGRLAALDLRSGRVLWSRDL------SSY---------TGLAVDGN 272

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327387  970 LVTVCSSSGRVHVLRvrpsilsRDShdskvGEI--TRMELQADIFSSPVMIGGRIFVGCRDDYVHCLSLES 1038
Cdd:COG1520  273 NLYVTDDDGRVWALD-------RRN-----GAElwKQDALLYRGLTAPVVLGDYVVVGDFEGYLHWLSRDD 331
BamB_YfgL cd10276
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ...
 706-1036 2.05e-07

Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is a non-essential component of the beta-barrel assembly machinery (Bam), a multi-subunit complex that inserts proteins with beta-barrel topology into the outer membrane. BamB has been found to interact with BamA, which in turn binds and stabilizes pre-folded beta-barrel proteins; it has been suggested that BamB participates in the stabilization.


Pssm-ID: 199834 [Multi-domain]  Cd Length: 358  Bit Score: 54.26  E-value: 2.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  706 LFIGSHSRKFSCIDAKSGSMYWETILeGRIEGSAMVVGDFSQVVIGCYKGKLYFLDFSTGSLCWKfqacgeikcqpvvdt 785
Cdd:cd10276   83 IFVGTESGYLYALDAKDGSELWRTEV-SDSQLLSPPTYADGKIYVGTGDGRLYYCNAETGKVVWN--------------- 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  786 ssqliwcgsHDHTLYALDYRSqccvyklqcggsiFASPAIDEGhsSLYVASTSGRVIAVSIKDspFHTLWLFELEAPIF- 864
Cdd:cd10276  147 ---------RTSTAPELSLRG-------------GAAPVGAYD--VVFVGDGNGTVVALNTGT--GVDIWEFSVSEPRGr 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  865 GSLC------ITPSTQNVICCLVDGQ--VIAM-SPSGTIIWRYRTGGpifaGPCMSHVLPSQVLVCCRNGCVYSLEPESG 935
Cdd:cd10276  201 TELPrmidssVTYVVVGGYLYSTSYQgyLVALdFESGQFLWSRKASG----GTSTSTDANGRVYVGDGEGSLYCLDASTG 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  936 CLVWEDNIGDP--ITASAYIDEnlhfeshellasDRLVTVCSSSGRVHVLRVRP-SILSRDSHDSKVGeitrmelqadIF 1012
Cdd:cd10276  277 DELWSQTVLLGrvLSSPAIYVG------------VYIYVTDNAEGYLYCLKDNDgLTVARVEVDYSQY----------IL 334

                        330       340
                 ....*....|....*....|....
gi 22327387 1013 SSPVMIGGRIFVGCRDDYVHCLSL 1036
Cdd:cd10276  335 QGPAVSDGWLYYGTDDGYLYALTR 358
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 498-548 5.68e-06

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: 44.86  E-value: 5.68e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 22327387    498 IKKAVCDALLV--KEVSDDDDFFAIGGDSLAAAHLSHSL------GIDMRLIYQFRSPS 548
Cdd:pfam00550    3 LRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLeeefgvEIPPSDLFEHPTLA 61
PRK11138 PRK11138
outer membrane biogenesis protein BamB; Provisional
 719-1038 6.42e-05

outer membrane biogenesis protein BamB; Provisional


Pssm-ID: 236857 [Multi-domain]  Cd Length: 394  Bit Score: 46.46  E-value: 6.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   719 DAKSGSMYWETILEGRI-----EGSAMVVG----DFSQVVIGCYKGKLYFLDFSTGSLCWKFQACGEIKCQPVVDTSSQL 789
Cdd:PRK11138   85 DADTGKEIWSVDLSEKDgwfskNKSALLSGgvtvAGGKVYIGSEKGQVYALNAEDGEVAWQTKVAGEALSRPVVSDGLVL 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   790 IwcgshdHT----LYALDYRS--QCCVYKLQC------GGSifaSPAIDEGhsSLYVASTSGRVIAVsIKDSPfHTLWlf 857
Cdd:PRK11138  165 V------HTsngmLQALNESDgaVKWTVNLDVpsltlrGES---APATAFG--GAIVGGDNGRVSAV-LMEQG-QLIW-- 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   858 elEAPIFgslciTPSTQNVICCLVDgqvIAMSPsgtIIwryrTGGPIFAgpcMSHvlpsqvlvccrNGCVYSLEPESGCL 937
Cdd:PRK11138  230 --QQRIS-----QPTGATEIDRLVD---VDTTP---VV----VGGVVYA---LAY-----------NGNLVALDLRSGQI 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   938 VWEDNIG---DPITASAYI---DENlhfeshellasDRLVTVCSSSGrvhvlrvrpSILSRDShdskvgeitrmELQADI 1011
Cdd:PRK11138  279 VWKREYGsvnDFAVDGGRIylvDQN-----------DRVYALDTRGG---------VELWSQS-----------DLLHRL 327

                         330       340
                  ....*....|....*....|....*..
gi 22327387  1012 FSSPVMIGGRIFVGCRDDYVHCLSLES 1038
Cdd:PRK11138  328 LTAPVLYNGYLVVGDSEGYLHWINRED 354
 
Name Accession Description Interval E-value
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 3-472 1.10e-130

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: 403.45  E-value: 1.10e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    3 KVVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVlslisssnislviacglssveSHWLveRNVCPVLLFSMDEK 82
Cdd:cd05930   38 DLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERL---------------------AYIL--EDSGAKLVLTDPDD 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   83 LsvetgcssfvwpckkerqrkfCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFIDHIQEFL 162
Cdd:cd05930   95 L---------------------AYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIF 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  163 GAILSSTALVIPPFTLLKeNMISIIDFLEEYSISRLLAVPSMIRAILPTLQHRGHNNklqscLKLVVLSGEPFPVSLWDS 242
Cdd:cd05930  154 GALLAGATLVVLPEEVRK-DPEALADLLAEEGITVLHLTPSLLRLLLQELELAALPS-----LRLVLVGGEALPPDLVRR 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  243 LHSLLPETCFLNLYGSTEVSGDCTYFDCSELPrllktEEIGSVPIGKSISNCKVVLLGDEDKP----YEGEICVSGLCLS 318
Cdd:cd05930  228 WRELLPGARLVNLYGPTEATVDATYYRVPPDD-----EEDGRVPIGRPIPNTRVYVLDENLRPvppgVPGELYIGGAGLA 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  319 QGYmhssiesegyvklHNNSlcnHLTND-------CGSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIET 391
Cdd:cd05930  303 RGY-------------LNRP---ELTAErfvpnpfGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEA 366

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  392 TLELNPDIAEAVVLLSRDETELASLKAFVVLNKEsnsSDGIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEA 471
Cdd:cd05930  367 ALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEG---GELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKA 443


                 .
gi 22327387  472 L 472
Cdd:cd05930  444 L 444
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 4-531 3.40e-79

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: 283.29  E-value: 3.40e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    4 VVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSlisssnislVIA-CGLSSV--ESHWLVERNVCPVLLFSMD 80
Cdd:COG1020  528 LVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAY---------MLEdAGARLVltQSALAARLPELGVPVLALD 598

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   81 EKLSVETGCSSFVWPCKKERQrkfCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFIDHIQE 160
Cdd:COG1020  599 ALALAAEPATNPPVPVTPDDL---AYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWE 675

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  161 FLGAILSSTALVIPPFTLLKeNMISIIDFLEEYSISRLLAVPSMIRAILPTLQHRGHNnklqscLKLVVLSGEPFPVSLW 240
Cdd:COG1020  676 IFGALLSGATLVLAPPEARR-DPAALAELLARHRVTVLNLTPSLLRALLDAAPEALPS------LRLVLVGGEALPPELV 748

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  241 DSLHSLLPETCFLNLYGSTEVSGDCTYFDCSELPrllktEEIGSVPIGKSISNCKVVLLGDEDKP----YEGEICVSGLC 316
Cdd:COG1020  749 RRWRARLPGARLVNLYGPTETTVDSTYYEVTPPD-----ADGGSVPIGRPIANTRVYVLDAHLQPvpvgVPGELYIGGAG 823

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  317 LSQGYmhssiesegyvklHNNSlcnHLT---------NDCGSQLyYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALE 387
Cdd:COG1020  824 LARGY-------------LNRP---ELTaerfvadpfGFPGARL-YRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELG 886

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  388 EIETTLELNPDIAEAVVLLSRDETELASLKAFVVLNKESNSSDGIIFSIRNWMggkLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:COG1020  887 EIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALL---LPPYMVPAAVVLLLPLPLTGNGKL 963

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327387  468 DYEALARlkcPTTGAQDMMQSNGTNSLLQNIKKAVCDALLVKEVSDDDDFFAIGGDSLAAAHLS 531
Cdd:COG1020  964 DRLALPA---PAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALA 1024
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 4-472 7.96e-77

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: 261.06  E-value: 7.96e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    4 VVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSLISSSNISLVIAcglSSVESHWLVERNVCPVLLfsmDEKL 83
Cdd:cd17646   50 RVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLT---TADLAARLPAGGDVALLG---DEAL 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   84 SVETGcssfVWPCKKERQRKFCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFIDHIQEFLG 163
Cdd:cd17646  124 AAPPA----TPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFW 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  164 AILSSTALVIPPFTLLKEnMISIIDFLEEYSISRLLAVPSMIRAILPTLQHRGHNNklqscLKLVVLSGEPFPVSLWDSL 243
Cdd:cd17646  200 PLVAGARLVVARPGGHRD-PAYLAALIREHGVTTCHFVPSMLRVFLAEPAAGSCAS-----LRRVFCSGEALPPELAARF 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  244 HSLLPETcFLNLYGSTEVSGDCTYFDCSElprllkTEEIGSVPIGKSISNCKVVLLGDEDKP----YEGEICVSGLCLSQ 319
Cdd:cd17646  274 LALPGAE-LHNLYGPTEAAIDVTHWPVRG------PAETPSVPIGRPVPNTRLYVLDDALRPvpvgVPGELYLGGVQLAR 346

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  320 GYMH-SSIESEGYVKLHNNSlcnhltndcGSQLyYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPD 398
Cdd:cd17646  347 GYLGrPALTAERFVPDPFGP---------GSRM-YRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPA 416

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327387  399 IAEAVVLLSRDETELASLKAFVVLnkESNSSDGIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEAL 472
Cdd:cd17646  417 VTHAVVVARAAPAGAARLVGYVVP--AAGAAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 4-404 4.97e-76

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: 256.04  E-value: 4.97e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387      4 VVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSLISSSNISLVIACglssveSHW--LVERNVCPVLLFSMDE 81
Cdd:TIGR01733   27 RVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTD------SALasRLAGLVLPVILLDPLE 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387     82 KLSVETGCSSFvWPCKKERQRKFCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFiDH-IQE 160
Cdd:TIGR01733  101 LAALDDAPAPP-PPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSF-DAsVEE 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    161 FLGAILSSTALVIPPFTLLKENMISIIDFLEEYSISRLLAVPSMIRAILPtlqhrgHNNKLQSCLKLVVLSGEPFPVSLW 240
Cdd:TIGR01733  179 IFGALLAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALLAA------ALPPALASLRLVILGGEALTPALV 252

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    241 DSLHSLLPETCFLNLYGSTEVSGDCTYFDCSELPrllkTEEIGSVPIGKSISNCKVVLLGDEDKPY----EGEICVSGLC 316
Cdd:TIGR01733  253 DRWRARGPGARLINLYGPTETTVWSTATLVDPDD----APRESPVPIGRPLANTRLYVLDDDLRPVpvgvVGELYIGGPG 328

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    317 LSQGYMH-SSIESEGYVklhnnslcNHLTNDCGSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLEL 395
Cdd:TIGR01733  329 VARGYLNrPELTAERFV--------PDPFAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400


                   ....*....
gi 22327387    396 NPDIAEAVV 404
Cdd:TIGR01733  401 HPGVREAVV 409
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 5-472 2.42e-65

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: 227.52  E-value: 2.42e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    5 VALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSlisssnislviacglssveshwlVERNVCPVLLFSMDEKLS 84
Cdd:cd05945   44 VVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIRE-----------------------ILDAAKPALLIADGDDNA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   85 vetgcssfvwpckkerqrkfcYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFA------FKTSVGFIdhi 158
Cdd:cd05945  101 ---------------------YIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLnqapfsFDLSVMDL--- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  159 qefLGAILSSTALVIPPFTLLKeNMISIIDFLEEYSISRLLAVPSMIRailPTLQHRGHNNKLQSCLKLVVLSGEPFPVS 238
Cdd:cd05945  157 ---YPALASGATLVPVPRDATA-DPKQLFRFLAEHGITVWVSTPSFAA---MCLLSPTFTPESLPSLRHFLFCGEVLPHK 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  239 LWDSLHSLLPETCFLNLYGSTEVSGDCTYFDCSELPrllkTEEIGSVPIGKSISNCKVVLLgDED-----KPYEGEICVS 313
Cdd:cd05945  230 TARALQQRFPDARIYNTYGPTEATVAVTYIEVTPEV----LDGYDRLPIGYAKPGAKLVIL-DEDgrpvpPGEKGELVIS 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  314 GLCLSQGYMHssiesegyVKLHNNSLCNHLTNdcgsQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTL 393
Cdd:cd05945  305 GPSVSKGYLN--------NPEKTAAAFFPDEG----QRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAAL 372

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  394 ELNPDIAEAVVL---LSRDETELAslkAFVVLNKESNSSDGIIfsIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYE 470
Cdd:cd05945  373 RQVPGVKEAVVVpkyKGEKVTELI---AFVVPKPGAEAGLTKA--IKAELAERLPPYMIPRRFVYLDELPLNANGKIDRK 447


                 ..
gi 22327387  471 AL 472
Cdd:cd05945  448 AL 449
PRK12467 PRK12467
peptide synthase; Provisional
 5-548 6.65e-65

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 241.22  E-value: 6.65e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387     5 VALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSLISSSNISLVIAcglssvESHWLVERNVC---PVLLfsMDE 81
Cdd:PRK12467  565 VGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLT------QSHLLAQLPVPaglRSLC--LDE 636

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    82 KLSVETGCSSfVWPCKKERQRKFCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFIDHIQEF 161
Cdd:PRK12467  637 PADLLCGYSG-HNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTEL 715

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   162 LGAILS-STALVIPPFTLLKENmiSIIDFLEEYSISRLLAVPSMIRAILPTLQhrghnNKLQSCLKLVVLSGEPFPVSLW 240
Cdd:PRK12467  716 FGALASgATLHLLPPDCARDAE--AFAALMADQGVTVLKIVPSHLQALLQASR-----VALPRPQRALVCGGEALQVDLL 788

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   241 DSLHSLLPETCFLNLYGSTEVSGDCTYFDCSELPRllkteEIGSVPIGKSISNCKVVLLGDEDKPYE----GEICVSGLC 316
Cdd:PRK12467  789 ARVRALGPGARLINHYGPTETTVGVSTYELSDEER-----DFGNVPIGQPLANLGLYILDHYLNPVPvgvvGELYIGGAG 863

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   317 LSQGYM-HSSIESEGYVKlhnnslcNHLTNDcGSQLyYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLEL 395
Cdd:PRK12467  864 LARGYHrRPALTAERFVP-------DPFGAD-GGRL-YRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLA 934

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   396 NPDIAEAVVlLSRDETELASLKAFVVLNKESNSSDGIIFS--IRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEALA 473
Cdd:PRK12467  935 QPGVREAVV-LAQPGDAGLQLVAYLVPAAVADGAEHQATRdeLKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALP 1013

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   474 rlKCPTTGAQDMMQSNGTNslLQNIKKAV-CDALLVKEVSDDDDFFAIGGDSLAA----AHLSHSLGIDMRLIYQFRSPS 548
Cdd:PRK12467 1014 --KPDASAVQATFVAPQTE--LEKRLAAIwADVLKVERVGLTDNFFELGGHSLLAtqviSRVRQRLGIQVPLRTLFEHQT 1089
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 4-472 2.05e-64

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: 226.44  E-value: 2.05e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    4 VVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSLISSsnislviaCGLSSVeshwLVERNVCPVLLFS----- 78
Cdd:cd17655   49 IVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILED--------SGADIL----LTQSHLQPPIAFIglidl 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   79 MDEKLSVETGCSSFVWPCKKerqRKFCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFIDHI 158
Cdd:cd17655  117 LDEDTIYHEESENLEPVSKS---DDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASV 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  159 QEFLGAILSSTALVIPPftllKENMIS---IIDFLEEYSISrllaVPSMIRAILPTLQHRGHnnKLQSCLKLVVLSGEPF 235
Cdd:cd17655  194 TEIFASLLSGNTLYIVR----KETVLDgqaLTQYIRQNRIT----IIDLTPAHLKLLDAADD--SEGLSLKHLIVGGEAL 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  236 PVSLWDSLHSLLPETC-FLNLYGSTEVSGDCTYFDCSElprllKTEEIGSVPIGKSISNCKVVLLGDEDKPY----EGEI 310
Cdd:cd17655  264 STELAKKIIELFGTNPtITNAYGPTETTVDASIYQYEP-----ETDQQVSVPIGKPLGNTRIYILDQYGRPQpvgvAGEL 338

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  311 CVSGLCLSQGYMH-SSIESEGYVklhNNSLCNhltndcGSQLYyRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEI 389
Cdd:cd17655  339 YIGGEGVARGYLNrPELTAEKFV---DDPFVP------GERMY-RTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEI 408

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  390 ETTLELNPDIAEAVVLLSRDETELASLKAFVVLNKESNSSDgiifsIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDY 469
Cdd:cd17655  409 EARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQ-----LREFLARELPDYMIPSYFIKLDEIPLTPNGKVDR 483


                 ...
gi 22327387  470 EAL 472
Cdd:cd17655  484 KAL 486
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 4-472 2.35e-63

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: 223.37  E-value: 2.35e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    4 VVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSLISSSNISLVIA----CGLSSVESHWLVERNVCPVLLFSM 79
Cdd:cd17651   47 LVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLThpalAGELAVELVAVTLLDQPGAAAGAD 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   80 DEkLSVETGCSSFVwpckkerqrkfcYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFIDHIQ 159
Cdd:cd17651  127 AE-PDPALDADDLA------------YVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQ 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  160 EFLGAILSSTALVIPPfTLLKENMISIIDFLEEYSISRLLAVPSMIRAILptlQHRGHNNKLQSCLKLVVLSGEPFPVsl 239
Cdd:cd17651  194 EIFSTLCAGATLVLPP-EEVRTDPPALAAWLDEQRISRVFLPTVALRALA---EHGRPLGVRLAALRYLLTGGEQLVL-- 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  240 wdslHSLLPETC-------FLNLYGSTEVsgdcTYFDCSELPRLLKTEEiGSVPIGKSISNCKVVLLGDEDKP----YEG 308
Cdd:cd17651  268 ----TEDLREFCaglpglrLHNHYGPTET----HVVTALSLPGDPAAWP-APPPIGRPIDNTRVYVLDAALRPvppgVPG 338

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  309 EICVSGLCLSQGYMHS-SIESEGYVKlhnnslcnhltnD--CGSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMA 385
Cdd:cd17651  339 ELYIGGAGLARGYLNRpELTAERFVP------------DpfVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIE 406

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  386 LEEIETTLELNPDIAEAVVLLSRDETELASLKAFVVLNKESNSSDGiifSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSG 465
Cdd:cd17651  407 LGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAA---ELRAALATHLPEYMVPSAFVLLDALPLTPNG 483


                 ....*..
gi 22327387  466 KVDYEAL 472
Cdd:cd17651  484 KLDRRAL 490
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 3-472 3.65e-63

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: 220.97  E-value: 3.65e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    3 KVVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVlslisssnislviacglssveSHWLveRNVCPVLLFSMDEK 82
Cdd:cd17652   38 RLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERI---------------------AYML--ADARPALLLTTPDN 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   83 LSvetgcssfvwpckkerqrkfcYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFIDHIQEFL 162
Cdd:cd17652   95 LA---------------------YVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQFASPSFDASVWELL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  163 GAILSSTALVIPPftllKENMIS---IIDFLEEYSISRLLAVPSMIRAI----LPTLQHrghnnklqsclklVVLSGEPF 235
Cdd:cd17652  154 MALLAGATLVLAP----AEELLPgepLADLLREHRITHVTLPPAALAALppddLPDLRT-------------LVVAGEAC 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  236 PVSL---WDslhsllPETCFLNLYGSTEVSGDCTYFDCSELPrllkteeiGSVPIGKSISNCKVVLLGDEDKP----YEG 308
Cdd:cd17652  217 PAELvdrWA------PGRRMINAYGPTETTVCATMAGPLPGG--------GVPPIGRPVPGTRVYVLDARLRPvppgVPG 282

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  309 EICVSGLCLSQGYMH-SSIESEGYVKlhnnslcnHLTNDCGSQLYyRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALE 387
Cdd:cd17652  283 ELYIAGAGLARGYLNrPGLTAERFVA--------DPFGAPGSRMY-RTGDLARWRADGQLEFLGRADDQVKIRGFRIELG 353

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  388 EIETTLELNPDIAEAVVLLSRDETELASLKAFVVLNKESNSSDGiifSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:cd17652  354 EVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAA---ELRAHLAERLPGYMVPAAFVVLDALPLTPNGKL 430


                 ....*
gi 22327387  468 DYEAL 472
Cdd:cd17652  431 DRRAL 435
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 4-472 3.70e-63

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: 222.46  E-value: 3.70e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    4 VVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSLISSSNISLVIACGLSSVeshWLVERNVCPVLLFSMDEKl 83
Cdd:cd12117   49 VVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLTDRSLAG---RAGGLEVAVVIDEALDAG- 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   84 svetGCSSFVWPCKKERqrkFCYLMYTSGSTGKPKGVCGTEQGLLnRFLWMQELYPVVGEQRFAFKTSVGFIDHIQEFLG 163
Cdd:cd12117  125 ----PAGNPAVPVSPDD---LAYVMYTSGSTGRPKGVAVTHRGVV-RLVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWG 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  164 AILSSTALVI-PPFTLLkeNMISIIDFLEEYSISRLLAVPSMIRAI-------LPTLQHrghnnklqsclklVVLSGEPF 235
Cdd:cd12117  197 ALLNGARLVLaPKGTLL--DPDALGALIAEEGVTVLWLTAALFNQLadedpecFAGLRE-------------LLTGGEVV 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  236 PVSLWDSLHSLLPETCFLNLYGSTEvsgdCTYFDCS-ELPRLlkTEEIGSVPIGKSISNCKVVLLGDEDKPYE----GEI 310
Cdd:cd12117  262 SPPHVRRVLAACPGLRLVNGYGPTE----NTTFTTShVVTEL--DEVAGSIPIGRPIANTRVYVLDEDGRPVPpgvpGEL 335

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  311 CVSGLCLSQGYMHSSIES-EGYVKLHNNSlcnhltndcGSQLYyRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEI 389
Cdd:cd12117  336 YVGGDGLALGYLNRPALTaERFVADPFGP---------GERLY-RTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEI 405

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  390 ETTLELNPDIAEAVVLLSRDETELASLKAFVVLNKESNSSDgiifsIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDY 469
Cdd:cd12117  406 EAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAAE-----LRAFLRERLPAYMVPAAFVVLDELPLTANGKVDR 480


                 ...
gi 22327387  470 EAL 472
Cdd:cd12117  481 RAL 483
PRK12316 PRK12316
peptide synthase; Provisional
 5-525 6.73e-63

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 235.24  E-value: 6.73e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387     5 VALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLslisssnislviacglssveshWLVERNVCPVLLFS--MDEK 82
Cdd:PRK12316  564 VGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLA----------------------YMLEDSGVQLLLSQshLGRK 621

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    83 LSVETGCSSF------VW-PCKKERQRKFC-------YLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAF 148
Cdd:PRK12316  622 LPLAAGVQVLdldrpaAWlEGYSEENPGTElnpenlaYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQ 701

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   149 KTSVGFIDHIQEFLGAILSSTALVIPPFTLLKeNMISIIDFLEEYSISRLLAVPSMIRAILptlqhrgHNNKLQSC--LK 226
Cdd:PRK12316  702 KTPFSFDVSVWEFFWPLMSGARLVVAAPGDHR-DPAKLVELINREGVDTLHFVPSMLQAFL-------QDEDVASCtsLR 773

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   227 LVVLSGEPFPVSLWDSLHSLLPETCFLNLYGSTEVSGDCTYFDCSElprllktEEIGSVPIGKSISNCKVVLLGDEDKPY 306
Cdd:PRK12316  774 RIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVE-------EGGDSVPIGRPIANLACYILDANLEPV 846

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   307 ----EGEICVSGLCLSQGYM-HSSIESEGYVKlhnNSLCNhltndcGSQLyYRTGDYGRQLSSGDLIFIGRRDRTVKLNG 381
Cdd:PRK12316  847 pvgvLGELYLAGRGLARGYHgRPGLTAERFVP---SPFVA------GERM-YRTGDLARYRADGVIEYAGRIDHQVKLRG 916

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   382 KRMALEEIETTLELNPDIAEAVVLLsrdeTELASLKAFVVLNKESNSsdgIIFSIRNWMGGKLPPVMIPNHFVLVEKLPL 461
Cdd:PRK12316  917 LRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLESEGGD---WREALKAHLAASLPEYMVPAQWLALERLPL 989

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327387   462 TSSGKVDYEALARlkcPTTGAQDMMQSNGTNSLLQNIKKAVCDALLVKEVSDDDDFFAIGGDSL 525
Cdd:PRK12316  990 TPNGKLDRKALPA---PEASVAQQGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSI 1050
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 5-472 3.90e-62

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: 218.73  E-value: 3.90e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    5 VALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSlisssnislviacglssveshwLVERNVCPVLLFSMDEKls 84
Cdd:cd12115   52 VGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRF----------------------ILEDAQARLVLTDPDDL-- 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   85 vetgcssfvwpckkerqrkfCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPvvGEQRFAF--KTSVGFIDHIQEFL 162
Cdd:cd12115  108 --------------------AYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFS--AEELAGVlaSTSICFDLSVFELF 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  163 GAiLSSTALVIppftlLKENMISIIDFLEEYSISRLLAVPSMIRAILptlQHrghnNKLQSCLKLVVLSGEPFPVSLWDS 242
Cdd:cd12115  166 GP-LATGGKVV-----LADNVLALPDLPAAAEVTLINTVPSAAAELL---RH----DALPASVRVVNLAGEPLPRDLVQR 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  243 LHSLLPETCFLNLYGSTEvsgDCTYFDCSELPRllktEEIGSVPIGKSISNCKVVLLGDEDKPYE----GEICVSGLCLS 318
Cdd:cd12115  233 LYARLQVERVVNLYGPSE---DTTYSTVAPVPP----GASGEVSIGRPLANTQAYVLDRALQPVPlgvpGELYIGGAGVA 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  319 QGYM-HSSIESEGYvklhnnslcnhLTNDCGSQLY-YRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELN 396
Cdd:cd12115  306 RGYLgRPGLTAERF-----------LPDPFGPGARlYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSI 374

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22327387  397 PDIAEAVVLLSRDETELASLKAFVVLnkeSNSSDGIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEAL 472
Cdd:cd12115  375 PGVREAVVVAIGDAAGERRLVAYIVA---EPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
PRK12467 PRK12467
peptide synthase; Provisional
 5-547 1.16e-60

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 228.12  E-value: 1.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387     5 VALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLslisssnislviacglssveshWLVERNVCPVLLF--SMDEK 82
Cdd:PRK12467 3148 VGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLA----------------------YMIEDSGVKLLLTqaHLLEQ 3205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    83 LSVETGCSSFVW------------PCKKERQRKFCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKT 150
Cdd:PRK12467 3206 LPAPAGDTALTLdrldlngysennPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFM 3285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   151 SVGFIDHIQEFLGAILSSTALVIPP---------FTLLKENMISIIDFleeysisrllaVPSMirailptLQHRGHNNKL 221
Cdd:PRK12467 3286 SFSFDGAQERFLWTLICGGCLVVRDndlwdpeelWQAIHAHRISIACF-----------PPAY-------LQQFAEDAGG 3347

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   222 QSC--LKLVVLSGEPFPVSLWDSLHSLLPETCFLNLYGSTEVSGDCTYFDCSELPRllktEEIGSVPIGKSISNCKVVLL 299
Cdd:PRK12467 3348 ADCasLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAV----CEAPYAPIGRPVAGRSIYVL 3423

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   300 GDEDKPYE----GEICVSGLCLSQGYMHS-SIESEGYVKlhnnslcnHLTNDCGSQLyYRTGDYGRQLSSGDLIFIGRRD 374
Cdd:PRK12467 3424 DGQLNPVPvgvaGELYIGGVGLARGYHQRpSLTAERFVA--------DPFSGSGGRL-YRTGDLARYRADGVIEYLGRID 3494

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   375 RTVKLNGKRMALEEIETTLELNPDIAEAVVlLSRDETELASLKAFVVLNKEsnsSDGIIFSIRNWMGGKLPPVMIPNHFV 454
Cdd:PRK12467 3495 HQVKIRGFRIELGEIEARLLQHPSVREAVV-LARDGAGGKQLVAYVVPADP---QGDWRETLRDHLAASLPDYMVPAQLL 3570

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   455 LVEKLPLTSSGKVDYEALARlkcPTTGAQDMMQSNgTNSLLQNIKKAVCDALLVKEVSDDDDFFAIGGDSLAA----AHL 530
Cdd:PRK12467 3571 VLAAMPLGPNGKVDRKALPD---PDAKGSREYVAP-RSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLAlqvlSRI 3646

                         570
                  ....*....|....*..
gi 22327387   531 SHSLGIDMRLIYQFRSP 547
Cdd:PRK12467 3647 RQSLGLKLSLRDLMSAP 3663
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 5-472 6.38e-60

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: 212.68  E-value: 6.38e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    5 VALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLslisssnislviacglssveshWLVERNVCPVLLfsmdekls 84
Cdd:cd17644   53 VGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLT----------------------YILEDAQISVLL-------- 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   85 vetgcssfvwpckkERQRKFCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFIDHIQEFLGA 164
Cdd:cd17644  103 --------------TQPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVT 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  165 ILSSTALVIPPftllkENMIS----IIDFLEEYSISRLLAVPS----MIRAILPTLQhrghnnKLQSCLKLVVLSGE--- 233
Cdd:cd17644  169 LLSGATLVLRP-----EEMRSsledFVQYIQQWQLTVLSLPPAywhlLVLELLLSTI------DLPSSLRLVIVGGEavq 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  234 PFPVSLWDSLHSLLPEtcFLNLYGSTEVSGDCTYFDcselPRLLKTEEIGSVPIGKSISNCKVVLLGDEDKPY----EGE 309
Cdd:cd17644  238 PELVRQWQKNVGNFIQ--LINVYGPTEATIAATVCR----LTQLTERNITSVPIGRPIANTQVYILDENLQPVpvgvPGE 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  310 ICVSGLCLSQGYMHSSiesegyvKLHNNSLCNHLTNDCGSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEI 389
Cdd:cd17644  312 LHIGGVGLARGYLNRP-------ELTAEKFISHPFNSSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEI 384

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  390 ETTLELNPDIAEAVVLLSRDETELASLKAFVVLNKESNSSdgiIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDY 469
Cdd:cd17644  385 EAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPS---TVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDR 461


                 ...
gi 22327387  470 EAL 472
Cdd:cd17644  462 RAL 464
PRK12467 PRK12467
peptide synthase; Provisional
 2-525 3.20e-59

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 223.50  E-value: 3.20e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387     2 PKV-VALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSLISSSnislviACGLSSVESHwLVERNVCP-----VL 75
Cdd:PRK12467 1623 PEVlVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDS------GIELLLTQSH-LQARLPLPdglrsLV 1695

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    76 LFSMDEKLSVEtgcsSFVWPCKKERQRKFCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFI 155
Cdd:PRK12467 1696 LDQEDDWLEGY----SDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFD 1771

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   156 DHIQEFLGAILSSTALVIPPFTLLKENMiSIIDFLEEYSISRLLAVPSMIRAILPTLQHRGHnnklqsCLKL--VVLSGE 233
Cdd:PRK12467 1772 VSVWELFWPLINGARLVIAPPGAHRDPE-QLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEH------PLSLrrVVCGGE 1844

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   234 PFPVSLWDSLHSLLPETCFLNLYGSTEVSGDCTYFDCselpRLLKTEEIGSVPIGKSISNCKVVLLGDEDKPYE----GE 309
Cdd:PRK12467 1845 ALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTC----RRKDLEGRDSVPIGQPIANLSTYILDASLNPVPigvaGE 1920

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   310 ICVSGLCLSQGYMH-SSIESEGYVKlhnnslcnHLTNDCGSQLyYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEE 388
Cdd:PRK12467 1921 LYLGGVGLARGYLNrPALTAERFVA--------DPFGTVGSRL-YRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGE 1991

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   389 IETTLELNPDIAEAVVlLSRDETELASLKAFVVLNKESNSSDGIIFS-----IRNWMGGKLPPVMIPNHFVLVEKLPLTS 463
Cdd:PRK12467 1992 IEARLREQGGVREAVV-IAQDGANGKQLVAYVVPTDPGLVDDDEAQValraiLKNHLKASLPEYMVPAHLVFLARMPLTP 2070

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327387   464 SGKVDYEALarlkcPTTGAQDMMQ--SNGTNSLLQNIKKAVCDALLVKEVSDDDDFFAIGGDSL 525
Cdd:PRK12467 2071 NGKLDRKAL-----PAPDASELQQayVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSI 2129
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
4-530 9.28e-59

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 220.69  E-value: 9.28e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387     4 VVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERvlslisssnislvIACGLSSVEshwlvernvcPVLLFSMDEKL 83
Cdd:PRK10252  510 SVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDR-------------LKMMLEDAR----------PSLLITTADQL 566

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    84 S-------VETGCSSFVW------PCKKERQRKFCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKT 150
Cdd:PRK10252  567 PrfadvpdLTSLCYNAPLapqgaaPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKT 646

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   151 SVGFIDHIQEFLGAILSSTALVI-PPFTllKENMISIIDFLEEYSISRLLAVPSMIRAILPTLQHRGHNNKLQScLKLVV 229
Cdd:PRK10252  647 PCSFDVSVWEFFWPFIAGAKLVMaEPEA--HRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCAS-LRQVF 723

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   230 LSGEPFPVSLWDSLHSLLpETCFLNLYGSTEVSGDCTYFDCSelPRLLKTEEIGSVPIGKSISNCKVVLLGDEDKP---- 305
Cdd:PRK10252  724 CSGEALPADLCREWQQLT-GAPLHNLYGPTEAAVDVSWYPAF--GEELAAVRGSSVPIGYPVWNTGLRILDARMRPvppg 800

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   306 YEGEICVSGLCLSQGYmhssiesegyvklhnnsLCN-HLTND--------CGSQLyYRTGDYGRQLSSGDLIFIGRRDRT 376
Cdd:PRK10252  801 VAGDLYLTGIQLAQGY-----------------LGRpDLTASrfiadpfaPGERM-YRTGDVARWLDDGAVEYLGRSDDQ 862

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   377 VKLNGKRMALEEIETTLELNPDIAEAV----VLLSRDET--ELASLKAFVVlnkeSNSSDGI-IFSIRNWMGGKLPPVMI 449
Cdd:PRK10252  863 LKIRGQRIELGEIDRAMQALPDVEQAVthacVINQAAATggDARQLVGYLV----SQSGLPLdTSALQAQLRERLPPHMV 938

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   450 PNHFVLVEKLPLTSSGKVDYEALARlkcPTTGAQDMMQ--SNGTNsllQNIKKAVCDALLVKEVSDDDDFFAIGGDSLAA 527
Cdd:PRK10252  939 PVVLLQLDQLPLSANGKLDRKALPL---PELKAQVPGRapKTGTE---TIIAAAFSSLLGCDVVDADADFFALGGHSLLA 1012


                  ...
gi 22327387   528 AHL 530
Cdd:PRK10252 1013 MKL 1015
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 4-475 4.66e-57

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: 204.27  E-value: 4.66e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    4 VVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVlslisssnislviacglssvesHWLVERnvcpvllfsmdekl 83
Cdd:COG0318   51 RVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEEL----------------------AYILED-------------- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   84 sveTGCSSFVwpckkerqrkFCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAfktSVGFIDHI----Q 159
Cdd:COG0318   95 ---SGARALV----------TALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVL---VALPLFHVfgltV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  160 EFLGAILSSTALVIPPFTLLKEnmisIIDFLEEYSISRLLAVPSMIRAILptlQHRGHNNKLQSCLKLVVLSGEPFPVSL 239
Cdd:COG0318  159 GLLAPLLAGATLVLLPRFDPER----VLELIERERVTVLFGVPTMLARLL---RHPEFARYDLSSLRLVVSGGAPLPPEL 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  240 WDSLHSLLpETCFLNLYGSTEVSGDCTYfdcseLPRLLKTEEIGSVpiGKSISNCKVVLLGDEDKPY----EGEICVSGL 315
Cdd:COG0318  232 LERFEERF-GVRIVEGYGLTETSPVVTV-----NPEDPGERRPGSV--GRPLPGVEVRIVDEDGRELppgeVGEIVVRGP 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  316 CLSQGYmhssiesegyvklHNNSlcnHLTNDCGSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLEL 395
Cdd:COG0318  304 NVMKGY-------------WNDP---EATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAA 367

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  396 NPDIAEAVVLLSRDETELASLKAFVVLNKESNSSDGiifSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEALARL 475
Cdd:COG0318  368 HPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAE---ELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRER 444
PRK12316 PRK12316
peptide synthase; Provisional
 2-548 6.19e-57

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 216.36  E-value: 6.19e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387     2 PKV-VALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSLISSSnislviacGLSSVESH-WLVERNVCPVLLFSM 79
Cdd:PRK12316 4600 PEVlVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDS--------GAALLLTQsHLLQRLPIPDGLASL 4671

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    80 D-EKLSVETGCSSFVwPCKKERQRKFCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFIDHI 158
Cdd:PRK12316 4672 AlDRDEDWEGFPAHD-PAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSH 4750

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   159 QEFLGAILSSTALVIPPFTL-LKENMISIIdflEEYSISRLLAVPSMIRAILPTLQHRGHNNKlqscLKLVVLSGEPFPV 237
Cdd:PRK12316 4751 EGLYHPLINGASVVIRDDSLwDPERLYAEI---HEHRVTVLVFPPVYLQQLAEHAERDGEPPS----LRVYCFGGEAVAQ 4823

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   238 SLWDSLHSLLPETCFLNLYGSTEVSGDCTYFDCselpRLLKTEEIGSVPIGKSISNCKVVLLGDEDKPYE----GEICVS 313
Cdd:PRK12316 4824 ASYDLAWRALKPVYLFNGYGPTETTVTVLLWKA----RDGDACGAAYMPIGTPLGNRSGYVLDGQLNPLPvgvaGELYLG 4899

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   314 GLCLSQGYMHS-SIESEGYVKlhnnslcnHLTNDCGSQLyYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETT 392
Cdd:PRK12316 4900 GEGVARGYLERpALTAERFVP--------DPFGAPGGRL-YRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEAR 4970

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   393 LELNPDIAEAVVlLSRDETELASLKAFVVLNKESNSSD-----GIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:PRK12316 4971 LREHPAVREAVV-IAQEGAVGKQLVGYVVPQDPALADAdeaqaELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKL 5049

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   468 DYEALARlkcPTTGAQDMMQSNGTNSLLQNIKKAVCDALLVKEVSDDDDFFAIGGDSLAA----AHLSHSLGIDMRLIYQ 543
Cdd:PRK12316 5050 DRKALPQ---PDASLLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAiqvtSRIQLELGLELPLREL 5126


                  ....*
gi 22327387   544 FRSPS 548
Cdd:PRK12316 5127 FQTPT 5131
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 5-472 3.95e-56

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: 201.38  E-value: 3.95e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    5 VALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLslisssnislviacglssveshwLVERNVCPVLLFSMDEKLS 84
Cdd:cd17643   40 VALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIA-----------------------FILADSGPSLLLTDPDDLA 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   85 vetgcssfvwpckkerqrkfcYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFIDHIQEFLGA 164
Cdd:cd17643   97 ---------------------YVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  165 ILSSTALVIPPFTLLKenmiSIIDF---LEEYSISRLLAVPSMIRAILPTLQHRGHNnklQSCLKLVVLSGEPFPVSL-- 239
Cdd:cd17643  156 LLHGGRLVVVPYEVAR----SPEDFarlLRDEGVTVLNQTPSAFYQLVEAADRDGRD---PLALRYVIFGGEALEAAMlr 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  240 -WDSlHSLLPETCFLNLYGSTEVSGDCTYfdcselpRLLKTEEIGSV---PIGKSISNCKVVLLGDEDKPY----EGEIC 311
Cdd:cd17643  229 pWAG-RFGLDRPQLVNMYGITETTVHVTF-------RPLDAADLPAAaasPIGRPLPGLRVYVLDADGRPVppgvVGELY 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  312 VSGLCLSQGYMhssieseGYVKLHNNSLCNHLTNDCGSQlYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIET 391
Cdd:cd17643  301 VSGAGVARGYL-------GRPELTAERFVANPFGGPGSR-MYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEA 372

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  392 TLELNPDIAEAVVLLSRDETELASLKAFVVLNKEsnsSDGIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEA 471
Cdd:cd17643  373 ALATHPSVRDAAVIVREDEPGDTRLVAYVVADDG---AAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAA 449


                 .
gi 22327387  472 L 472
Cdd:cd17643  450 L 450
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 4-474 8.11e-56

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: 200.23  E-value: 8.11e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    4 VVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSlisssnislviacglssveshwlVERNVCPVLLFSMDekl 83
Cdd:cd17653   49 VVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQA-----------------------ILRTSGATLLLTTD--- 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   84 svetgcssfvwpckkeRQRKFCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFIDHIQEFLG 163
Cdd:cd17653  103 ----------------SPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFS 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  164 AILSSTALVippftlLKENMISIIDFLEEYSIsrLLAVPSmiraILPTLQHRGHNNklqscLKLVVLSGEPFPVSLWDSL 243
Cdd:cd17653  167 TLCNGGTLV------LADPSDPFAHVARTVDA--LMSTPS----ILSTLSPQDFPN-----LKTIFLGGEAVPPSLLDRW 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  244 hslLPETCFLNLYGSTEVSGDCTYfdcselprlLKTEEIGSVPIGKSISNCKVVLLgDEDK-----PYEGEICVSGLCLS 318
Cdd:cd17653  230 ---SPGRRLYNAYGPTECTISSTM---------TELLPGQPVTIGKPIPNSTCYIL-DADLqpvpeGVVGEICISGVQVA 296

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  319 QGYMHSsiESEGYVKLHNNSLCNhltndcGSQLYyRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPD 398
Cdd:cd17653  297 RGYLGN--PALTASKFVPDPFWP------GSRMY-RTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQP 367

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22327387  399 IAE-AVVLLSRDetelaSLKAFVVlnKESNSSDGIIFSIRNwmggKLPPVMIPNHFVLVEKLPLTSSGKVDYEALAR 474
Cdd:cd17653  368 EVTqAAAIVVNG-----RLVAFVT--PETVDVDGLRSELAK----HLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 4-472 4.47e-55

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: 199.05  E-value: 4.47e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    4 VVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSLISSSNISLVIACGLSSVESHWLvernvCPVLLfsmdekL 83
Cdd:cd12116   39 RVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTDDALPDRLPAG-----LPVLL------L 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   84 SVETGCSSFVWPCKKERQRKFCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFIDHIQEFLG 163
Cdd:cd12116  108 ALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLL 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  164 AILSSTALVIPPFTLLKENMiSIIDFLEEYSISRLLAVPSMIRAILPTlQHRGHNNklqscLKLVVlSGEPFPVSLWDSL 243
Cdd:cd12116  188 PLLAGARVVIAPRETQRDPE-ALARLIEAHSITVMQATPATWRMLLDA-GWQGRAG-----LTALC-GGEALPPDLAARL 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  244 hsLLPETCFLNLYGSTEVsgdcTYFdcSELPRLlkTEEIGSVPIGKSISNCKVVLLGDEDKPYE----GEICVSGLCLSQ 319
Cdd:cd12116  260 --LSRVGSLWNLYGPTET----TIW--STAARV--TAAAGPIPIGRPLANTQVYVLDAALRPVPpgvpGELYIGGDGVAQ 329

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  320 GYMHS-SIESEGYVKLHnnslcnhlTNDCGSQLYyRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPD 398
Cdd:cd12116  330 GYLGRpALTAERFVPDP--------FAGPGSRLY-RTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPG 400

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327387  399 IAEAVVLLsRDETELASLKAFVVLnKESNSSDGIifSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEAL 472
Cdd:cd12116  401 VAQAAVVV-REDGGDRRLVAYVVL-KAGAAPDAA--ALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 4-472 9.88e-54

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: 194.61  E-value: 9.88e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    4 VVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLslisssnislviacglssveshWLVERNVCPVLLFSMDEkl 83
Cdd:cd17650   39 VVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQ----------------------YMLEDSGAKLLLTQPED-- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   84 svetgcssfvwpckkerqrkFCYLMYTSGSTGKPKGVCGTEQGLLN-RFLWMQEL----YPVVGEQRFAFKTSVGFIDhi 158
Cdd:cd17650   95 --------------------LAYVIYTSGTTGKPKGVMVEHRNVAHaAHAWRREYeldsFPVRLLQMASFSFDVFAGD-- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  159 qeFLGAILSSTALVIPPfTLLKENMISIIDFLEEYSISRLLAVPSMIRAILPTLQHRGHNnklQSCLKLVVLSGEPFPVS 238
Cdd:cd17650  153 --FARSLLNGGTLVICP-DEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLD---LSAMRLLIVGSDGCKAQ 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  239 lW--DSLHSLLPETCFLNLYGSTEVSGDCTYFDCSELPrllkTEEIGSVPIGKSISNCKVVLLGDEDKPYE----GEICV 312
Cdd:cd17650  227 -DfkTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDP----LGDSANVPIGRPLPNTAMYVLDERLQPQPvgvaGELYI 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  313 SGLCLSQGYMHS-SIESEGYVKLHNNSlcnhltndcGSQLyYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIET 391
Cdd:cd17650  302 GGAGVARGYLNRpELTAERFVENPFAP---------GERM-YRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIES 371

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  392 TLELNPDIAEAVVLLSRDETELASLKAFVVLNKESNSSDgiifsIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEA 471
Cdd:cd17650  372 QLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAE-----LRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRA 446


                 .
gi 22327387  472 L 472
Cdd:cd17650  447 L 447
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 4-475 1.23e-52

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: 192.37  E-value: 1.23e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    4 VVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSlisssnislviacglssveshwLVERNVCPVLLFSMDEKL 83
Cdd:cd05918   51 FVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHPLQRLQE----------------------ILQDTGAKVVLTSSPSDA 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   84 svetgcssfvwpckkerqrkfCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQR---FAfktSVGFIDHIQE 160
Cdd:cd05918  109 ---------------------AYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRvlqFA---SYTFDVSILE 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  161 FLGAILSSTALVIPPFTLLKENmisIIDFLEEYSISRLLAVPSMIRAILPtlqhrghnnKLQSCLKLVVLSGEPFPVSLW 240
Cdd:cd05918  165 IFTTLAAGGCLCIPSEEDRLND---LAGFINRLRVTWAFLTPSVARLLDP---------EDVPSLRTLVLGGEALTQSDV 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  241 DSLHSLlpeTCFLNLYGSTEVSGDCTYFDC--SELPRLlkteeIGSvPIGksiSNCKVVLLGDEDKPY----EGEICVSG 314
Cdd:cd05918  233 DTWADR---VRLINAYGPAECTIAATVSPVvpSTDPRN-----IGR-PLG---ATCWVVDPDNHDRLVpigaVGELLIEG 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  315 LCLSQGYMH-------SSIESEGYVKLHNNSlcnhltndCGSQLYyRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALE 387
Cdd:cd05918  301 PILARGYLNdpektaaAFIEDPAWLKQEGSG--------RGRRLY-RTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELG 371

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  388 EIETTLE-LNPDIAEAVV--LLSRDETELASLKAFVVLNKESNSSDGIIF--------------SIRNWMGGKLPPVMIP 450
Cdd:cd05918  372 EIEHHLRqSLPGAKEVVVevVKPKDGSSSPQLVAFVVLDGSSSGSGDGDSlflepsdefralvaELRSKLRQRLPSYMVP 451

                        490       500
                 ....*....|....*....|....*
gi 22327387  451 NHFVLVEKLPLTSSGKVDYEALARL 475
Cdd:cd05918  452 SVFLPLSHLPLTASGKIDRRALREL 476
PRK12316 PRK12316
peptide synthase; Provisional
 5-547 2.30e-52

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 201.72  E-value: 2.30e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387     5 VALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSLISSSNISLVIAcglssvESHwLVERNVCPVLLfsmdEKLS 84
Cdd:PRK12316 2056 VAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLT------QRH-LLERLPLPAGV----ARLP 2124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    85 VETGCSSFVWPCKKERQR----KFCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFIDHIQE 160
Cdd:PRK12316 2125 LDRDAEWADYPDTAPAVQlageNLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQ 2204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   161 FLGAILSSTALVIPPFTL-LKENMisiIDFLEEYSISRLLAVPSMIRAILPTLQHRGHNNKLQSClklvVLSGEPFPVSL 239
Cdd:PRK12316 2205 WFHPLLNGARVLIRDDELwDPEQL---YDEMERHGVTILDFPPVYLQQLAEHAERDGRPPAVRVY----CFGGEAVPAAS 2277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   240 WDSLHSLLPETCFLNLYGSTEVSGDCTYFDCselpRLLKTEEIGSVPIGKSISNCKVVLLGDEDKPYE----GEICVSGL 315
Cdd:PRK12316 2278 LRLAWEALRPVYLFNGYGPTEAVVTPLLWKC----RPQDPCGAAYVPIGRALGNRRAYILDADLNLLApgmaGELYLGGE 2353

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   316 CLSQGYM-HSSIESEGYVKLHNNSlcnhltndCGSQLyYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLE 394
Cdd:PRK12316 2354 GLARGYLnRPGLTAERFVPDPFSA--------SGERL-YRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQ 2424

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   395 LNPDIAEAVVlLSRDETELASLKAFVVlnkESNSSDGIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEALAR 474
Cdd:PRK12316 2425 AHPAVREAVV-VAQDGASGKQLVAYVV---PDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK 2500

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22327387   475 lkcPTTGAQDMMQSNGTNSLLQNIKKAVCDALLVKEVSDDDDFFAIGGDSLAA----AHLSHSLGIDMRLIYQFRSP 547
Cdd:PRK12316 2501 ---PDVSQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLAtqvvSRVRQDLGLEVPLRILFERP 2574
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 4-472 3.10e-52

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: 190.95  E-value: 3.10e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    4 VVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSLISSSNISLVIACGlssvesHWLVERNVCPVLLFSMDEKL 83
Cdd:cd12114   39 LVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLTDG------PDAQLDVAVFDVLILDLDAL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   84 S-VETGCSSFVWPckkerqRKFCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQR------FAFKTSVgfid 156
Cdd:cd12114  113 AaPAPPPPVDVAP------DDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRvlalssLSFDLSV---- 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  157 hiQEFLGAILSSTALVIPPFTLLKENmISIIDFLEEYSISRLLAVPsmirAILP-TLQHRGHNNKLQSCLKLVVLSGEPF 235
Cdd:cd12114  183 --YDIFGALSAGATLVLPDEARRRDP-AHWAELIERHGVTLWNSVP----ALLEmLLDVLEAAQALLPSLRLVLLSGDWI 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  236 PVSLWDSLHSLLPETCFLNLYGSTEVSGDCTYFDCSELPrllktEEIGSVPIGKSISN--CKVVLLGDEDKP--YEGEIC 311
Cdd:cd12114  256 PLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEVP-----PDWRSIPYGRPLANqrYRVLDPRGRDCPdwVPGELW 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  312 VSGLCLSQGYMHSSIESEgyvklhnnslcNHLTNDCGSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIET 391
Cdd:cd12114  331 IGGRGVALGYLGDPELTA-----------ARFVTHPDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEA 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  392 TLELNPDIAEAVVlLSRDETELASLKAFVVLNKESN--SSDgiifSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDY 469
Cdd:cd12114  400 ALQAHPGVARAVV-VVLGDPGGKRLAAFVVPDNDGTpiAPD----ALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDR 474


                 ...
gi 22327387  470 EAL 472
Cdd:cd12114  475 AAL 477
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 105-468 1.50e-51

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: 184.80  E-value: 1.50e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  105 CYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFIDHIQEFLGAILSSTALVIPPftllKENMI 184
Cdd:cd04433    3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLP----KFDPE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  185 SIIDFLEEYSISRLLAVPSMIRAILPTLQHRGHNnklQSCLKLVVLSGEPFPVSLWDSLHSLLPETcFLNLYGSTEVSGD 264
Cdd:cd04433   79 AALELIEREKVTILLGVPTLLARLLKAPESAGYD---LSSLRALVSGGAPLPPELLERFEEAPGIK-LVNGYGLTETGGT 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  265 CTYfdcseLPRLLKTEEIGSVpiGKSISNCKVVLLGDEDKPYE----GEICVSGLCLSQGYmhssiesegyvkLHNNSLC 340
Cdd:cd04433  155 VAT-----GPPDDDARKPGSV--GRPVPGVEVRIVDPDGGELPpgeiGELVVRGPSVMKGY------------WNNPEAT 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  341 NHLTNDcGsqlYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDETELASLKAFV 420
Cdd:cd04433  216 AAVDED-G---WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVV 291

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 22327387  421 VLNKESN-SSDGIIFSIRNwmggKLPPVMIPNHFVLVEKLPLTSSGKVD 468
Cdd:cd04433  292 VLRPGADlDAEELRAHVRE----RLAPYKVPRRVVFVDALPRTASGKID 336
AMP-binding pfam00501
AMP-binding enzyme;
4-379 2.88e-50

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 183.67  E-value: 2.88e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387      4 VVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSLISSSNISLVI---ACGLSSVESHWLVERNVCPVLLFSMD 80
Cdd:pfam00501   48 RVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLItddALKLEELLEALGKLEVVKLVLVLDRD 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387     81 ----EKLSVETGCSSFVWPCKKERQRKF--CYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYP----VVGEQRFAFKT 150
Cdd:pfam00501  128 pvlkEEPLPEEAKPADVPPPPPPPPDPDdlAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTL 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    151 SVGFI-DHIQEFLGAILSSTALVI-PPFTLLkeNMISIIDFLEEYSISRLLAVPSMIRAILptlQHRGHNNKLQSCLKLV 228
Cdd:pfam00501  208 PLFHDfGLSLGLLGPLLAGATVVLpPGFPAL--DPAALLELIERYKVTVLYGVPTLLNMLL---EAGAPKRALLSSLRLV 282

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    229 VLSGEPFPVSLWDSLHSLLPETcFLNLYGSTEVSGDCTYfdcsELPRLLKTEEIGSvpIGKSISNCKVVLLGDEDKPY-- 306
Cdd:pfam00501  283 LSGGAPLPPELARRFRELFGGA-LVNGYGLTETTGVVTT----PLPLDEDLRSLGS--VGRPLPGTEVKIVDDETGEPvp 355

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22327387    307 ---EGEICVSGLCLSQGYmhssiesegyvklHNNSlcnHLTNDC-GSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKL 379
Cdd:pfam00501  356 pgePGELCVRGPGVMKGY-------------LNDP---ELTAEAfDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKL 416
PRK12316 PRK12316
peptide synthase; Provisional
 4-527 5.81e-50

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 194.41  E-value: 5.81e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387     4 VVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSLISSSNISLVIACGLSSVESHWLVERnvcpVLLFSMDEKL 83
Cdd:PRK12316 3109 LVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQV----LDLDRGDENY 3184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    84 SVETgcssfvwPCKKERQRKFCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFiDHIQEFLG 163
Cdd:PRK12316 3185 AEAN-------PAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSF-DVFVEELF 3256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   164 AILSSTALVIPPFTLLKENMISIIDFLEEYSISRLLAVPSMIRAILPTLQHRGHNNklqscLKLVVLSGEPFPVSLWDSL 243
Cdd:PRK12316 3257 WPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTS-----LKRIVCGGEALPADLQQQV 3331

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   244 HSLLPetcFLNLYGSTEVSGDCTYFDCSElprllktEEIGSVPIGKSISNCKVVLLGDEDKPYE----GEICVSGLCLSQ 319
Cdd:PRK12316 3332 FAGLP---LYNLYGPTEATITVTHWQCVE-------EGKDAVPIGRPIANRACYILDGSLEPVPvgalGELYLGGEGLAR 3401

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   320 GYMHS-SIESEGYVKLHNNSlcnhltndcGSQLyYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPD 398
Cdd:PRK12316 3402 GYHNRpGLTAERFVPDPFVP---------GERL-YRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPW 3471

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   399 IAEAVVLlsrdETELASLKAFVVLNKESNSSDGIifsIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEALARlkcP 478
Cdd:PRK12316 3472 VREAVVL----AVDGRQLVAYVVPEDEAGDLREA---LKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPR---P 3541

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 22327387   479 TTGAQDMMQSNGTNSLLQNIKKAVCDALLVKEVSDDDDFFAIGGDSLAA 527
Cdd:PRK12316 3542 DAALLQQDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIIS 3590
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 3-472 4.40e-49

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: 181.90  E-value: 4.40e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    3 KVVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSLISSSNISLVIACG-----LSSVESHWLVERnvcPVLLF 77
Cdd:cd17656   39 SIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQRhlkskLSFNKSTILLED---PSISQ 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   78 SMDEKLSVETGCSSFVwpckkerqrkfcYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFIDH 157
Cdd:cd17656  116 EDTSNIDYINNSDDLL------------YIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLQFATCSFDVC 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  158 IQEFLGAILSSTALVIPPfTLLKENMISIIDFLEEYSISRLLAVPSMIRAILptlQHRGHNNKLQSCLKLVVLSGEPFPV 237
Cdd:cd17656  184 YQEIFSTLLSGGTLYIIR-EETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIF---SEREFINRFPTCVKHIITAGEQLVI 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  238 S--LWDSLHSllpETCFL-NLYGSTE--VSGDCTYFDCSELPRLlkteeigsVPIGKSISNCKVVLLGDEDKPYE----G 308
Cdd:cd17656  260 TneFKEMLHE---HNVHLhNHYGPSEthVVTTYTINPEAEIPEL--------PPIGKPISNTWIYILDQEQQLQPqgivG 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  309 EICVSGLCLSQGYM-HSSIESEGYVKLHNNSlcnhltndcgSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALE 387
Cdd:cd17656  329 ELYISGASVARGYLnRQELTAEKFFPDPFDP----------NERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELG 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  388 EIETTLELNPDIAEAVVLLSRDETELASLKAFVVLNKESNSSDgiifsIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:cd17656  399 EIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQ-----LREYLAKQLPEYMIPSFFVPLDQLPLTPNGKV 473


                 ....*
gi 22327387  468 DYEAL 472
Cdd:cd17656  474 DRKAL 478
PRK05691 PRK05691
peptide synthase; Validated
 5-527 7.71e-48

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 187.30  E-value: 7.71e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387     5 VALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSLISSsnislviaCGLSSVESH-WLVER-----NVCPVLLfs 78
Cdd:PRK05691 1184 VAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLAD--------SGVELLLTQsHLLERlpqaeGVSAIAL-- 1253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    79 mdEKLSVETgcssfvWPCKKERQR----KFCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGF 154
Cdd:PRK05691 1254 --DSLHLDS------WPSQAPGLHlhgdNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISF 1325

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   155 IDHIQEFLGAILSSTALVIP-------PFtllkenmiSIIDFLEEYSISRLLAVPsmirailPTLQHRGHNNKLQSC--L 225
Cdd:PRK05691 1326 DVSVWECFWPLITGCRLVLAgpgehrdPQ--------RIAELVQQYGVTTLHFVP-------PLLQLFIDEPLAAACtsL 1390

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   226 KLVVLSGEPFPVSLWDSLHSLLPETCFLNLYGSTEVSGDCTYFDCSelprllkTEEIGSVPIGKSISNCKVVLLGDEDKP 305
Cdd:PRK05691 1391 RRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVTHWQCQ-------AEDGERSPIGRPLGNVLCRVLDAELNL 1463

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   306 YE----GEICVSGLCLSQGYMHS-SIESEGYVKlhnnslcNHLTNDcGSQLYyRTGDYGRQLSSGDLIFIGRRDRTVKLN 380
Cdd:PRK05691 1464 LPpgvaGELCIGGAGLARGYLGRpALTAERFVP-------DPLGED-GARLY-RTGDRARWNADGALEYLGRLDQQVKLR 1534

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   381 GKRMALEEIETTLELNPDIAEAVVLLsRDETELASLKAFVVLNKESNSSDGiifSIRNWMGGKLPPVMIPNHFVLVEKLP 460
Cdd:PRK05691 1535 GFRVEPEEIQARLLAQPGVAQAAVLV-REGAAGAQLVGYYTGEAGQEAEAE---RLKAALAAELPEYMVPAQLIRLDQMP 1610

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22327387   461 LTSSGKVDYEALarlkcPTTGAQDMMQSNGTNSLLQNIKKAVCDALLVKEVSDDDDFFAIGGDSLAA 527
Cdd:PRK05691 1611 LGPSGKLDRRAL-----PEPVWQQREHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLA 1672
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 3-472 1.03e-42

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: 162.57  E-value: 1.03e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    3 KVVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSLISSSNISLVIAcglssveshwlvernvcpvllfsmdek 82
Cdd:cd17648   39 DLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDTGARVVIT--------------------------- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   83 lsvetgcssfvwpckkeRQRKFCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGE--QRFAFKTSVGFIDHIQE 160
Cdd:cd17648   92 -----------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNgdEAVLFFSNYVFDFFVEQ 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  161 FLGAILSSTALVIPPftllkENMIS----IIDFLEEYSISRLLAVPSMIRAI-LPTLQHrghnnklqscLKLVVLSGEPF 235
Cdd:cd17648  155 MTLALLNGQKLVVPP-----DEMRFdpdrFYAYINREKVTYLSGTPSVLQQYdLARLPH----------LKRVDAAGEEF 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  236 PVSLWDSLHSLLPETcFLNLYGSTEVSgdctyfdCSELPRLLKTEEIGSVPIGKSISNCKVVLLGDEDKPYE----GEIC 311
Cdd:cd17648  220 TAPVFEKLRSRFAGL-IINAYGPTETT-------VTNHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPvgavGELY 291

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  312 VSGLCLSQGYMH-----------SSIESEGYVKLHNNslcnhltndcgsQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLN 380
Cdd:cd17648  292 LGGDGVARGYLNrpeltaerflpNPFQTEQERARGRN------------ARLYKTGDLVRWLPSGELEYLGRNDFQVKIR 359

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  381 GKRMALEEIETTLELNPDIAEAVVLLSRDETELAS-----LKAFVVLNKESNSSDgiifSIRNWMGGKLPPVMIPNHFVL 455
Cdd:cd17648  360 GQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSriqkyLVGYYLPEPGHVPES----DLLSFLRAKLPRYMVPARLVR 435

                        490
                 ....*....|....*..
gi 22327387  456 VEKLPLTSSGKVDYEAL 472
Cdd:cd17648  436 LEGIPVTINGKLDVRAL 452
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 5-472 1.51e-42

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: 161.57  E-value: 1.51e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    5 VALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSLISSsnislviacglSSVEshwlvernvcpvLLFSMDEKLS 84
Cdd:cd17645   51 VGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLAD-----------SSAK------------ILLTNPDDLA 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   85 vetgcssfvwpckkerqrkfcYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFIDHIQEFLGA 164
Cdd:cd17645  108 ---------------------YVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPH 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  165 ILSSTAL-VIPPFTLLkeNMISIIDFLEEYSISRllavpsmirAILPTlqhrghnnklQSCLKLVVLSGEPFPVSLW--D 241
Cdd:cd17645  167 LTAGAALhVVPSERRL--DLDALNDYFNQEGITI---------SFLPT----------GAAEQFMQLDNQSLRVLLTggD 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  242 SLHSLLPETCFL-NLYGSTEVSGDCTYFDCSElprllkteEIGSVPIGKSISNCKVVLLGDEDK--P--YEGEICVSGLC 316
Cdd:cd17645  226 KLKKIERKGYKLvNNYGPTENTVVATSFEIDK--------PYANIPIGKPIDNTRVYILDEALQlqPigVAGELCIAGEG 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  317 LSQGYMHSsiESEGYVKLHNNSLCNhltndcGSQLYyRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELN 396
Cdd:cd17645  298 LARGYLNR--PELTAEKFIVHPFVP------GERMY-RTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNH 368

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22327387  397 PDIAEAVVLLSRDETELASLKAFVVLNKESNssdgiIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEAL 472
Cdd:cd17645  369 PLIELAAVLAKEDADGRKYLVAYVTAPEEIP-----HEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 5-472 3.81e-42

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: 160.61  E-value: 3.81e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    5 VALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVlslisssnislviacglssvesHWLVERNVCPVLLfsmdekls 84
Cdd:cd17649   40 VGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERL----------------------RYMLEDSGAGLLL-------- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   85 vetgcssfvwpckKERQRKFCYLMYTSGSTGKPKGVCgTEQGLLNRFLW-MQELYPVVGEQR---FAfktSVGFIDHIQE 160
Cdd:cd17649   90 -------------THHPRQLAYVIYTSGSTGTPKGVA-VSHGPLAAHCQaTAERYGLTPGDRelqFA---SFNFDGAHEQ 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  161 FLGAILSSTALVIPPFTLLKENMIsIIDFLEEYSISRLLAVPSMIRAILPTLQHRGHNNklQSCLKLVVLSGEPFPVSLW 240
Cdd:cd17649  153 LLPPLICGACVVLRPDELWASADE-LAEMVRELGVTVLDLPPAYLQQLAEEADRTGDGR--PPSLRLYIFGGEALSPELL 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  241 dsLHSLLPETCFLNLYGSTEVSGDCTYFDCSElprllKTEEIG-SVPIGKSISNCKVVLLGDEDKPYE----GEICVSGL 315
Cdd:cd17649  230 --RRWLKAPVRLFNAYGPTEATVTPLVWKCEA-----GAARAGaSMPIGRPLGGRSAYILDADLNPVPvgvtGELYIGGE 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  316 CLSQGYmhssiesegyvklHNNSlcnHLTND---------CGSQLYyRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMAL 386
Cdd:cd17649  303 GLARGY-------------LGRP---ELTAErfvpdpfgaPGSRLY-RTGDLARWRDDGVIEYLGRVDHQVKIRGFRIEL 365

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  387 EEIETTLELNPDIAEAVVLLsRDETELASLKAFVVLNKESNSSDgIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGK 466
Cdd:cd17649  366 GEIEAALLEHPGVREAAVVA-LDGAGGKQLVAYVVLRAAAAQPE-LRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGK 443


                 ....*.
gi 22327387  467 VDYEAL 472
Cdd:cd17649  444 LDRKAL 449
PRK05691 PRK05691
peptide synthase; Validated
 24-559 9.46e-38

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 154.94  E-value: 9.46e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    24 RCGEAFLPLDPSWPRERVLSLISSSNISlVIACGLSSVE-SHWLVERNVC---PVLLFSMDeklsVETGCSSFVWPCKKE 99
Cdd:PRK05691 3792 KAGAGYLPLDPGLPAQRLQRIIELSRTP-VLVCSAACREqARALLDELGCanrPRLLVWEE----VQAGEVASHNPGIYS 3866

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   100 RQRKFCYLMYTSGSTGKPKGVCGTEQGLLNRFLwMQELYPVVGEQRFAFKT-SVGFIDHIQEFLGAILSSTALVIPPFTL 178
Cdd:PRK05691 3867 GPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQL-SKVPYLALSEADVIAQTaSQSFDISVWQFLAAPLFGARVEIVPNAI 3945

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   179 LKENMiSIIDFLEEYSISRLLAVPSMIRAILPTlQHRGHNNklqscLKLVVLSGEPFPVSLWDSLHSLLPETCFLNLYGS 258
Cdd:PRK05691 3946 AHDPQ-GLLAHVQAQGITVLESVPSLIQGMLAE-DRQALDG-----LRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGP 4018

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   259 TEVSGDCTYFDCSelprlLKTEEIGSVPIGKSISNCKVVLLGDEDK--PYE--GEICVSGLCLSQGYMHSSIESEgyvkl 334
Cdd:PRK05691 4019 AECSDDVAFFRVD-----LASTRGSYLPIGSPTDNNRLYLLDEALElvPLGavGELCVAGTGVGRGYVGDPLRTA----- 4088

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   335 hnNSLCNHLTNDCGSQLYyRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLsRDETELA 414
Cdd:PRK05691 4089 --LAFVPHPFGAPGERLY-RTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAV-QEGVNGK 4164

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   415 SLKAFVVLNKESNSSDGIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEALARLKCPTTGAQDMMQSNgtNSL 494
Cdd:PRK05691 4165 HLVGYLVPHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQAYLAPR--NEL 4242

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327387   495 LQNIKKAVCDALLVKEVSDDDDFFAIGGDSLAAAHLSH------SLGIDMRLIYQFRSPSRLLIYLSEKEG 559
Cdd:PRK05691 4243 EQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASrvqkalQRNVPLRAMFECSTVEELAEYIEGLAG 4313
PRK05691 PRK05691
peptide synthase; Validated
 2-602 1.01e-36

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 151.47  E-value: 1.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387     2 PKV-VALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVlslisssnislviacglssvesHWLVERNVCPVLL---- 76
Cdd:PRK05691 2237 PQVrVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERL----------------------HYMIEDSGIGLLLsdra 2294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    77 --------------FSMDEKLSVETGCSSFVWPCKKERQRKfCYLMYTSGSTGKPKGVCGTE-------QGLLNRFlwmq 135
Cdd:PRK05691 2295 lfealgelpagvarWCLEDDAAALAAYSDAPLPFLSLPQHQ-AYLIYTSGSTGKPKGVVVSHgeiamhcQAVIERF---- 2369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   136 ELYPVVGEQRFafkTSVGFIDHIQEFLGAILSSTALVIPP---------FTLLKENMISIIDFLEEYSiSRLLavpsmir 206
Cdd:PRK05691 2370 GMRADDCELHF---YSINFDAASERLLVPLLCGARVVLRAqgqwgaeeiCQLIREQQVSILGFTPSYG-SQLA------- 2438

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   207 ailptlQHRGHNNKlQSCLKLVVLSGEPFPVSLWDSLHSLLPETCFLNLYGSTEVsgdCTYFDCSELPRLLKtEEIGSVP 286
Cdd:PRK05691 2439 ------QWLAGQGE-QLPVRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTET---VVMPLACLAPEQLE-EGAASVP 2507

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   287 IGKSISNcKVVLLGDED-----KPYEGEICVSGLCLSQGYmHS--SIESEGYVKlhnnslcNHLTNDcGSQLYyRTGDYG 359
Cdd:PRK05691 2508 IGRVVGA-RVAYILDADlalvpQGATGELYVGGAGLAQGY-HDrpGLTAERFVA-------DPFAAD-GGRLY-RTGDLV 2576

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   360 RQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDET--ELASLKAFVVLNKESNSSDGIIFSIR 437
Cdd:PRK05691 2577 RLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSgkQLAGYLVSAVAGQDDEAQAALREALK 2656

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   438 NWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEALArLKCPTTGAQDMMQSngTNSLLQNIKKAVCDALLVKEVSDDDDF 517
Cdd:PRK05691 2657 AHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALP-APDPELNRQAYQAP--RSELEQQLAQIWREVLNVERVGLGDNF 2733

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   518 FAIGGDSLaaahlshslgidmrLIYQFRSPSRLL-IYLSEkegklREDMQHNTTQKLDHKIESqngnglvSRTVPLHSGV 596
Cdd:PRK05691 2734 FELGGDSI--------------LSIQVVSRARQLgIHFSP-----RDLFQHQTVQTLAAVATH-------SEAAQAEQGP 2787


                  ....*.
gi 22327387   597 TSGPTP 602
Cdd:PRK05691 2788 LQGASG 2793
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
106-473 1.09e-33

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


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 136.56  E-value: 1.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   106 YLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQR------FAFKTSVGFIdhiqefLGAILSSTALVIPPFTLL 179
Cdd:PRK04813  147 YIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQflnqapYSFDLSVMDL------YPTLASGGTLVALPKDMT 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   180 KeNMISIIDFLEEYSISRLLAVPSMIRAIL--PTLQHRGHNNklqscLKLVVLSGEPFPVSLWDSLHSLLPETCFLNLYG 257
Cdd:PRK04813  221 A-NFKQLFETLPQLPINVWVSTPSFADMCLldPSFNEEHLPN-----LTHFLFCGEELPHKTAKKLLERFPSATIYNTYG 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   258 STEVSGDCTyfdcselpRLLKTEEI----GSVPIGKSISNCKVVLLGDEDKPY----EGEICVSGLCLSQGYMHSS---- 325
Cdd:PRK04813  295 PTEATVAVT--------SIEITDEMldqyKRLPIGYAKPDSPLLIIDEEGTKLpdgeQGEIVISGPSVSKGYLNNPekta 366

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   326 ---IESEGyvklhnnslcnhltndcgsQLYYRTGDYGRQlsSGDLIFI-GRRDRTVKLNGKRMALEEIETTLELNPDIAE 401
Cdd:PRK04813  367 eafFTFDG-------------------QPAYHTGDAGYL--EDGLLFYqGRIDFQIKLNGYRIELEEIEQNLRQSSYVES 425

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22327387   402 AVVLLSRDETELASLKAFVVLNKESNSSDGIIFS-IRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEALA 473
Cdd:PRK04813  426 AVVVPYNKDHKVQYLIAYVVPKEEDFEREFELTKaIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKALI 498
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 107-473 1.26e-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.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 132.56  E-value: 1.26e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  107 LMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFIDHIQEFLGAILSSTALVIPPFTLLKEnmiSI 186
Cdd:cd05922  122 LLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDD---AF 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  187 IDFLEEYSISRLLAVPS----MIRAILPTLqhrghnnKLQScLKLVVLSGEPFPVSLWDSLHSLLPETCFLNLYGSTEVS 262
Cdd:cd05922  199 WEDLREHGATGLAGVPStyamLTRLGFDPA-------KLPS-LRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEAT 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  263 GDCTYfdcseLPRLLKTEEIGSvpIGKSISNCKVVLLGDEDKPYE----GEICVSGLCLSQGYMHSSIESEGYVklhnns 338
Cdd:cd05922  271 RRMTY-----LPPERILEKPGS--IGLAIPGGEFEILDDDGTPTPpgepGEIVHRGPNVMKGYWNDPPYRRKEG------ 337

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  339 lcnhLTNDCgsqLYyrTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVlLSRDETELASLKA 418
Cdd:cd05922  338 ----RGGGV---LH--TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAA-VGLPDPLGEKLAL 407

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 22327387  419 FVVLNKESNSSDgiifsIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEALA 473
Cdd:cd05922  408 FVTAPDKIDPKD-----VLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
 3-472 1.26e-32

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: 132.60  E-value: 1.26e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    3 KVVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSLISSsnislviaCGLssveSHWLVERNVCPVLLFSMDEK 82
Cdd:cd17654   42 RAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKK--------CHV----SYLLQNKELDNAPLSFTPEH 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   83 LSVetgcssfvwpcKKERQRKFCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEqRFAFKTSVGFID-HIQEF 161
Cdd:cd17654  110 RHF-----------NIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSE-DILFLTSPLTFDpSVVEI 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  162 LGAILSSTALVIPPFTLLKENMISIIDFLEEYSISRLLAVPSMIRAILPTLQHRGHNNKLQScLKLVVLSGEPFPVSLWD 241
Cdd:cd17654  178 FLSLSSGATLLIVPTSVKVLPSKLADILFKRHRITVLQATPTLFRRFGSQSIKSTVLSATSS-LRVLALGGEPFPSLVIL 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  242 -SLHSLLPETCFLNLYGSTEVSGDCTYFDCselPRLLKTEEIGSVPIGKSISNCKVvllgdEDKPYEGEICVSGL---CL 317
Cdd:cd17654  257 sSWRGKGNRTRIFNIYGITEVSCWALAYKV---PEEDSPVQLGSPLLGTVIEVRDQ-----NGSEGTGQVFLGGLnrvCI 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  318 SQGYMhssiesegyvklhnnslcnhltnDCGSQLYYRTGDYgRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLE-LN 396
Cdd:cd17654  329 LDDEV-----------------------TVPKGTMRATGDF-VTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIEsCL 384

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22327387  397 PDIAEAVVLLSRDEtelasLKAFVVlnkeSNSSDGIIFSIRNWMggKLPPVMIPNHFVLVEKLPLTSSGKVDYEAL 472
Cdd:cd17654  385 GVESCAVTLSDQQR-----LIAFIV----GESSSSRIHKELQLT--LLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
 3-467 4.44e-30

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: 125.40  E-value: 4.44e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    3 KVVALYMPPSVEYVISVFSVLRCGEAFLPLDPSW-PRErvLSLISSSNISLVIACGLSSVESHWLVERNVCP---VLLF- 77
Cdd:cd05911   36 DVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYtADE--LAHQLKISKPKVIFTDPDGLEKVKEAAKELGPkdkIIVLd 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   78 -SMDEKLSVETGCSS-------FVWPCKKERQRKFCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPV---VGEQRF 146
Cdd:cd05911  114 dKPDGVLSIEDLLSPtlgeedeDLPPPLKDGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGndgSNDVIL 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  147 AFKTsvgfIDHIQEFLGAILSS----TALVIPPFtllkeNMISIIDFLEEYSISRLLAVPSMIRAIL--PTLQhrghNNK 220
Cdd:cd05911  194 GFLP----LYHIYGLFTTLASLlngaTVIIMPKF-----DSELFLDLIEKYKITFLYLVPPIAAALAksPLLD----KYD 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  221 LQScLKLVVLSGEPFPVSLWDSLHSLLPETCFLNLYGSTEVSGDCTYfdcseLPRLlkTEEIGSVpiGKSISNCKVVLLG 300
Cdd:cd05911  261 LSS-LRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTV-----NPDG--DDKPGSV--GRLLPNVEAKIVD 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  301 DEDKPY-----EGEICVSGLCLSQGYmhssiesegyvklHNNSLCNHLTNDcgSQLYYRTGDYGRQLSSGDLIFIGRRDR 375
Cdd:cd05911  331 DDGKDSlgpnePGEICVRGPQVMKGY-------------YNNPEATKETFD--EDGWLHTGDIGYFDEDGYLYIVDRKKE 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  376 TVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDE--TELAslKAFVVLNKESNSSDGiifSIRNWMGGKLppvmiPNHF 453
Cdd:cd05911  396 LIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEvsGELP--RAYVVRKPGEKLTEK---EVKDYVAKKV-----ASYK 465

                        490       500
                 ....*....|....*....|
gi 22327387  454 ------VLVEKLPLTSSGKV 467
Cdd:cd05911  466 qlrggvVFVDEIPKSASGKI 485
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
105-467 1.38e-29

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


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 125.22  E-value: 1.38e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  105 CYLMYTSGSTGKPKGVCGTEQGLLNRFLW-MQELYPVVGEQRFAFKTSVGFI-DHIQEFLGAILSSTALVI---PPFTLL 179
Cdd:COG0365  187 LFILYTSGTTGKPKGVVHTHGGYLVHAATtAKYVLDLKPGDVFWCTADIGWAtGHSYIVYGPLLNGATVVLyegRPDFPD 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  180 KENMISIIdflEEYSISRLLAVPSMIRAILPTLQHRGHNNKLqSCLKLVVLSGEPFPVSLWDSLHSLL--PetcFLNLYG 257
Cdd:COG0365  267 PGRLWELI---EKYGVTVFFTAPTAIRALMKAGDEPLKKYDL-SSLRLLGSAGEPLNPEVWEWWYEAVgvP---IVDGWG 339

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  258 STEVsgdCTYFdCSELPRL-LKteeIGSvpIGKSISNCKVVLLGDEDKPY----EGEICVSGLCLSQ--GYMHssiESEG 330
Cdd:COG0365  340 QTET---GGIF-ISNLPGLpVK---PGS--MGKPVPGYDVAVVDEDGNPVppgeEGELVIKGPWPGMfrGYWN---DPER 407

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  331 YVKlhnnSLCNHLTNdcgsqlYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDE 410
Cdd:COG0365  408 YRE----TYFGRFPG------WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDE 477

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 22327387  411 TELASLKAFVVLNKESNSSDGIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:COG0365  478 IRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKI 534
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
 4-472 3.50e-28

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: 120.32  E-value: 3.50e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    4 VVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERvlslisssnisLVIACGLSSveshwlvernvcPVLLFSMdEKL 83
Cdd:cd17647   47 VVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPAR-----------QNIYLGVAK------------PRGLIVI-RAA 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   84 SVETGCSSFvwPCkkerqrkfcyLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFiDHIQE--- 160
Cdd:cd17647  103 GVVVGPDSN--PT----------LSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTMLSGIAH-DPIQRdmf 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  161 ---FLGAilsstALVIPPftllKENMIS---IIDFLEEYSISRLLAVPSMIRAI-------LPTLQHR---GHNNKLQSC 224
Cdd:cd17647  170 tplFLGA-----QLLVPT----QDDIGTpgrLAEWMAKYGATVTHLTPAMGQLLtaqattpFPKLHHAffvGDILTKRDC 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  225 LklvvlsgepfpvslwdSLHSLLPETCFLNLYGSTEVSGDCTYFD---CSELPRLLKTEEiGSVPIGKSISNCKVVLLGD 301
Cdd:cd17647  241 L----------------RLQTLAENVRIVNMYGTTETQRAVSYFEvpsRSSDPTFLKNLK-DVMPAGRGMLNVQLLVVNR 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  302 EDKPYE------GEICVSGLCLSQGYMHS-SIESEGYVK--LHNNSLCNHLTNDCGS---QLY-------YRTGDYGRQL 362
Cdd:cd17647  304 NDRTQIcgigevGEIYVRAGGLAEGYRGLpELNKEKFVNnwFVEPDHWNYLDKDNNEpwrQFWlgprdrlYRTGDLGRYL 383

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  363 SSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDETELASLKAFVV--------------LNKESNS 428
Cdd:cd17647  384 PNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVprfdkpddesfaqeDVPKEVS 463

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....
gi 22327387  429 SDGI----------IFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEAL 472
Cdd:cd17647  464 TDPIvkgligyrklIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 107-548 4.91e-26

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: 116.32  E-value: 4.91e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    107 LMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFafkTSVGFIDH--IQE------FLGAilsstALVIP---- 174
Cdd:TIGR03443  420 LSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKF---TMLSGIAHdpIQRdmftplFLGA-----QLLVPtadd 491

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    175 ---PFTLlkenmisiIDFLEEYSISRLLAVPSM-------IRAILPTLQHR---GHNNKLQSCLklvvlsgepfpvslwd 241
Cdd:TIGR03443  492 igtPGRL--------AEWMAKYGATVTHLTPAMgqllsaqATTPIPSLHHAffvGDILTKRDCL---------------- 547

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    242 SLHSLLPETCFLNLYGSTEVSGDCTYFDC---SELPRLLKTEEiGSVPIGKSISNCK--VVLLGDEDKPYE----GEICV 312
Cdd:TIGR03443  548 RLQTLAENVCIVNMYGTTETQRAVSYFEIpsrSSDSTFLKNLK-DVMPAGKGMKNVQllVVNRNDRTQTCGvgevGEIYV 626

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    313 SGLCLSQGYMHS-SIESEGYVK--LHNNSLCNHLTNDCG---SQLY-------YRTGDYGRQLSSGDLIFIGRRDRTVKL 379
Cdd:TIGR03443  627 RAGGLAEGYLGLpELNAEKFVNnwFVDPSHWIDLDKENNkpeREFWlgprdrlYRTGDLGRYLPDGNVECCGRADDQVKI 706

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    380 NGKRMALEEIETTLELNPDIAEAVVLLSRDETE-------------LASLKAFVVLNKESNSSDGI----------IFSI 436
Cdd:TIGR03443  707 RGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEeptlvsyivpqdkSDELEEFKSEVDDEESSDPVvkglikyrklIKDI 786

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    437 RNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEAlarLKCPTTG----AQDMMQSNGTNSLLQNIKKAVCDALL----- 507
Cdd:TIGR03443  787 REYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPA---LPFPDTAqlaaVAKNRSASAADEEFTETEREIRDLWLellpn 863

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 22327387    508 -VKEVSDDDDFFAIGGDSLAAAH----LSHSLGIDMRLIYQFRSPS 548
Cdd:TIGR03443  864 rPATISPDDSFFDLGGHSILATRmifeLRKKLNVELPLGLIFKSPT 909
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
 3-472 6.27e-25

O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 162605 [Multi-domain]  Cd Length: 436  Bit Score: 109.08  E-value: 6.27e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387      3 KVVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSLISSSNISLVIACglSSVESHWLVERNVcPVLLFSMDEK 82
Cdd:TIGR01923   25 SRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTD--SLLEEKDFQADSL-DRIEAAGRYE 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387     83 LSVETGCSsfvwpckkerQRKFCYLMYTSGSTGKPKGVCGTeqgllnrflWMQELYPVVG-EQRFAFKTSVGF-----ID 156
Cdd:TIGR01923  102 TSLSASFN----------MDQIATLMFTSGTTGKPKAVPHT---------FRNHYASAVGsKENLGFTEDDNWllslpLY 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    157 HIQEF---LGAILSSTALVIP-PFTllkenmiSIIDFLEEYSISRLLAVPSMIRAILptlQHRGHNNKLQSCLklvvLSG 232
Cdd:TIGR01923  163 HISGLsilFRWLIEGATLRIVdKFN-------QLLEMIANERVTHISLVPTQLNRLL---DEGGHNENLRKIL----LGG 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    233 EPFPVSLWDSLHSL-LPetcFLNLYGSTEVSGDCTYFDCSELPrllkteeiGSVPIGKSISNCKVVLLGDeDKPYEGEIC 311
Cdd:TIGR01923  229 SAIPAPLIEEAQQYgLP---IYLSYGMTETCSQVTTATPEMLH--------ARPDVGRPLAGREIKIKVD-NKEGHGEIM 296

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    312 VSGLCLSQGYmhssiesegyvkLHNNSLcNHLTNDCGsqlYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIET 391
Cdd:TIGR01923  297 VKGANLMKGY------------LYQGEL-TPAFEQQG---WFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIET 360

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    392 TLELNPDIAEAVVLLSRDETELASLKAFVVLNKESNSSDGIifsirNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEA 471
Cdd:TIGR01923  361 VLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESDISQAKLI-----AYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQ 435


                   .
gi 22327387    472 L 472
Cdd:TIGR01923  436 L 436
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
 105-472 2.53e-24

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: 108.22  E-value: 2.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  105 CYLMYTSGSTGKPKGVCGTEQGLLnrflWMQELY--PVVGEQR-----------FA--------FKTSVGfidhiqeflg 163
Cdd:cd05959  166 AFWLYSSGSTGRPKGVVHLHADIY----WTAELYarNVLGIREddvcfsaaklfFAyglgnsltFPLSVG---------- 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  164 ailsSTALVIPPFTLLKenmiSIIDFLEEYSISRLLAVPSMIRAIL--PTLQHRGhnnklQSCLKLVVLSGEPFPVSLWD 241
Cdd:cd05959  232 ----ATTVLMPERPTPA----AVFKRIRRYRPTVFFGVPTLYAAMLaaPNLPSRD-----LSSLRLCVSAGEALPAEVGE 298

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  242 SLHSLLPETcFLNLYGSTEVsgdcTYFDCSELPRLLKteeIGSVpiGKSISNCKVVLLGDEDKPYE----GEICVSGLCL 317
Cdd:cd05959  299 RWKARFGLD-ILDGIGSTEM----LHIFLSNRPGRVR---YGTT--GKPVPGYEVELRDEDGGDVAdgepGELYVRGPSS 368

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  318 SQGYMHSSIES----EGYvklhnnslcnhltndcgsqlYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTL 393
Cdd:cd05959  369 ATMYWNNRDKTrdtfQGE--------------------WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESAL 428

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22327387  394 ELNPDIAEAVVLLSRDETELASLKAFVVLNKESNSSDGIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEAL 472
Cdd:cd05959  429 VQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 105-467 7.97e-23

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: 102.80  E-value: 7.97e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  105 CYLMYTSGSTGKPKGVCGTEQGLLNRflWMQELYPV-VGEQRFAFKTS-VGFIDHI-QEFLGAILSSTALVI---PPFTL 178
Cdd:cd05972   84 ALIYFTSGTTGLPKGVLHTHSYPLGH--IPTAAYWLgLRPDDIHWNIAdPGWAKGAwSSFFGPWLLGATVFVyegPRFDA 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  179 LKenmisIIDFLEEYSISRLLAVPSMIRAILPTLQHRGHnnklQSCLKLVVLSGEPfpvslwdslhsLLPETC-----FL 253
Cdd:cd05972  162 ER-----ILELLERYGVTSFCGPPTAYRMLIKQDLSSYK----FSHLRLVVSAGEP-----------LNPEVIewwraAT 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  254 NL-----YGSTEVSGDCTYFDCSEL-PrllkteeiGSvpIGKSISNCKVVLL---GDEDKPYE-GEICV--SGLCLSQGY 321
Cdd:cd05972  222 GLpirdgYGQTETGLTVGNFPDMPVkP--------GS--MGRPTPGYDVAIIdddGRELPPGEeGDIAIklPPPGLFLGY 291

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  322 MHSSIESEGyvKLHNNslcnhltndcgsqlYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAE 401
Cdd:cd05972  292 VGDPEKTEA--SIRGD--------------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAE 355

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22327387  402 AVVLLSRDETELASLKAFVVLNKESNSSDGIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:cd05972  356 AAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKI 421
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
 4-473 7.98e-23

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: 103.55  E-value: 7.98e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    4 VVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSLISSSNISLVIA--CGLSS------------VESHWLVER 69
Cdd:cd05926   41 RVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTpkGELGPasraasklglaiLELALDVGV 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   70 NVCPVllfsMDEKLSVETGCSSFVWPCKKERQRKFCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYpvvgeqrfafk 149
Cdd:cd05926  121 LIRAP----SAESLSNLLADKKNAKSEGVPLPDDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTY----------- 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  150 tSVGFID---------HIQEFLGAILSSTA----LVIPP-FTLLKenmisIIDFLEEYSISRLLAVPSMIRAILPTlqHR 215
Cdd:cd05926  186 -KLTPDDrtlvvmplfHVHGLVASLLSTLAaggsVVLPPrFSAST-----FWPDVRDYNATWYTAVPTIHQILLNR--PE 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  216 GHNNKLQSCLKLVVLSGEPFPVSLwdsLHSLlpETCF----LNLYGSTEVSGDCTyfdCSELPrlLKTEEIGSVPIGksi 291
Cdd:cd05926  258 PNPESPPPKLRFIRSCSASLPPAV---LEAL--EATFgapvLEAYGMTEAAHQMT---SNPLP--PGPRKPGSVGKP--- 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  292 SNCKVVLLGDEDKPY----EGEICVSGLCLSQGYMHSsiesegyvklHNNSLCNHLTNDcgsqlYYRTGDYGRQLSSGDL 367
Cdd:cd05926  325 VGVEVRILDEDGEILppgvVGEICLRGPNVTRGYLNN----------PEANAEAAFKDG-----WFRTGDLGYLDADGYL 389

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  368 IFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDETELASLKAFVVLNKESNSSDGiifSIRNWMGGKLPPV 447
Cdd:cd05926  390 FLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEE---ELRAFCRKHLAAF 466

                        490       500
                 ....*....|....*....|....*.
gi 22327387  448 MIPNHFVLVEKLPLTSSGKVDYEALA 473
Cdd:cd05926  467 KVPKKVYFVDELPKTATGKIQRRKVA 492
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 105-467 9.58e-23

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: 102.54  E-value: 9.58e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  105 CYLMYTSGSTGKPKGVCGTEQG-LLNRFLWMQELYPVVGEQR--------FAFKTSVGFIDHIQEFLGAILSSTALVipp 175
Cdd:cd05919   94 AYLLYSSGTTGPPKGVMHAHRDpLLFADAMAREALGLTPGDRvfssakmfFGYGLGNSLWFPLAVGASAVLNPGWPT--- 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  176 ftllKENMISIidfLEEYSISRLLAVPSMIRAILPTLQHRGHnnkLQSCLKLVVLSGEPFPVSLWDSL--HSLLPetcFL 253
Cdd:cd05919  171 ----AERVLAT---LARFRPTVLYGVPTFYANLLDSCAGSPD---ALRSLRLCVSAGEALPRGLGERWmeHFGGP---IL 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  254 NLYGSTEVSgdcTYFDCSELPRLlkteEIGSVpiGKSISNCKVVLLGDEDKPY----EGEICVSGLCLSQGYMHSSIESE 329
Cdd:cd05919  238 DGIGATEVG---HIFLSNRPGAW----RLGST--GRPVPGYEIRLVDEEGHTIppgeEGDLLVRGPSAAVGYWNNPEKSR 308

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  330 GYVKlhnnslcnhltndcgsQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRD 409
Cdd:cd05919  309 ATFN----------------GGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPE 372

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 22327387  410 ETELASLKAFVVLNKESNSSDGIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:cd05919  373 STGLSRLTAFVVLKSPAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKL 430
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
 105-467 3.39e-22

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: 102.27  E-value: 3.39e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  105 CYLMYTSGSTGKPKGVCGTEQGllnrflwmqelYPVVGEQRFAFKTSVGFIDHIQEF--LGAILSSTALVIPPF-----T 177
Cdd:cd17634  235 LFILYTSGTTGKPKGVLHTTGG-----------YLVYAATTMKYVFDYGPGDIYWCTadVGWVTGHSYLLYGPLacgatT 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  178 LLKENM------ISIIDFLEEYSISRLLAVPSMIRAILP--TLQHRGHNnklQSCLKLVVLSGEPFPVSLWD-SLHSLLP 248
Cdd:cd17634  304 LLYEGVpnwptpARMWQVVDKHGVNILYTAPTAIRALMAagDDAIEGTD---RSSLRILGSVGEPINPEAYEwYWKKIGK 380

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  249 ETC-FLNLYGSTEVSGDCtyfdCSELPRLlktEEIGSVPIGKSISNCKVVLLGDEDKPY----EGEIcVSGLCLSQGymh 323
Cdd:cd17634  381 EKCpVVDTWWQTETGGFM----ITPLPGA---IELKAGSATRPVFGVQPAVVDNEGHPQpggtEGNL-VITDPWPGQ--- 449

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  324 ssieSEGYVKLHNNSLCNHLTNDCGsqlYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAV 403
Cdd:cd17634  450 ----TRTLFGDHERFEQTYFSTFKG---MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAA 522

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327387  404 VLLSRDETELASLKAFVVLNKESNSSDGIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:cd17634  523 VVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
 105-475 1.10e-21

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: 97.40  E-value: 1.10e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  105 CYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFIDHIQEFLGAILSSTALVIPPFTLLKENMi 184
Cdd:cd17630    3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQALAED- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  185 siidfLEEYSISRLLAVPSMIRAILPTLQHRGhnnKLQScLKLVVLSGEPFPVSLWDSLHSL-LPetCFLNlYGSTEVSG 263
Cdd:cd17630   82 -----LAPPGVTHVSLVPTQLQRLLDSGQGPA---ALKS-LRAVLLGGAPIPPELLERAADRgIP--LYTT-YGMTETAS 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  264 DCTyfdcselprllkteeiGSVPIGKSISNCKVVLLGDE-DKPYEGEICVSGLCLSQGYMHSSIESEGyvklhnnslcnh 342
Cdd:cd17630  150 QVA----------------TKRPDGFGRGGVGVLLPGRElRIVEDGEIWVGGASLAMGYLRGQLVPEF------------ 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  343 ltNDCGsqlYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDETELASLKAFVVL 422
Cdd:cd17630  202 --NEDG---WFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVG 276

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 22327387  423 NKESNSSDgiifsIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEALARL 475
Cdd:cd17630  277 RGPADPAE-----LRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAW 324
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 105-467 3.35e-21

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: 97.75  E-value: 3.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  105 CYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVvGEQRFAFKTSVGFidHIQ----EFLGAILSSTALVIPPftllK 180
Cdd:cd05934   84 ASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGL-GEDDVYLTVLPLF--HINaqavSVLAALSVGATLVLLP----R 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  181 ENMISIIDFLEEYSISRLLAVPSMIRAIL---PTLQHRGHnnklqsclKLVVLSGEPFPVSLWDSLhsllpETCF----L 253
Cdd:cd05934  157 FSASRFWSDVRRYGATVTNYLGAMLSYLLaqpPSPDDRAH--------RLRAAYGAPNPPELHEEF-----EERFgvrlL 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  254 NLYGSTEVSGDCTyfdcSELPrllktEEIGSVPIGKSISNCKVVLLGDEDKPYE----GEICV---SGLCLSQGYMHSSI 326
Cdd:cd05934  224 EGYGMTETIVGVI----GPRD-----EPRRPGSIGRPAPGYEVRIVDDDGQELPagepGELVIrglRGWGFFKGYYNMPE 294

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  327 ESEgyvKLHNNslcnhltndcgsqLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLL 406
Cdd:cd05934  295 ATA---EAMRN-------------GWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVA 358

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22327387  407 SRDETELASLKAFVVLNK-ESNSSDgiifSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:cd05934  359 VPDEVGEDEVKAVVVLRPgETLDPE----ELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKV 416
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
 105-468 1.97e-20

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: 95.37  E-value: 1.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  105 CYLMYTSGSTGKPKGV-------------CGTEQGLLN--RFLWMQELYPVVGEQRFAFKTSvgfidhiqeFLGAilsst 169
Cdd:cd17631  101 ALLMYTSGTTGRPKGAmlthrnllwnavnALAALDLGPddVLLVVAPLFHIGGLGVFTLPTL---------LRGG----- 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  170 ALVIPPftllKENMISIIDFLEEYSISRLLAVPSMIRAILptlQHRGHNNKLQSCLKLVVLSGEPFPVSLWDSLHSLLPE 249
Cdd:cd17631  167 TVVILR----KFDPETVLDLIERHRVTSFFLVPTMIQALL---QHPRFATTDLSSLRAVIYGGAPMPERLLRALQARGVK 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  250 tcFLNLYGSTEVSGDCTYfdcseLPRLLKTEEIGSVpiGKSISNCKVVLLGDEDKPYE----GEICVSGLCLSQGYmhss 325
Cdd:cd17631  240 --FVQGYGMTETSPGVTF-----LSPEDHRRKLGSA--GRPVFFVEVRIVDPDGREVPpgevGEIVVRGPHVMAGY---- 306

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  326 iesegyvklHNNSLCNHLTNDCGsqlYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVL 405
Cdd:cd17631  307 ---------WNRPEATAAAFRDG---WFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVI 374

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22327387  406 LSRDETELASLKAFVVLnKESNSSDGIifSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVD 468
Cdd:cd17631  375 GVPDEKWGEAVVAVVVP-RPGAELDED--ELIAHCRERLARYKIPKSVEFVDALPRNATGKIL 434
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 106-467 3.95e-20

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: 94.42  E-value: 3.95e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  106 YLMYTSGSTGKPKGVCGTEQGLLNRFLWMQ---ELYPVVGEqrfAFKTSVGFiDHIQEFLGAILSSTALVIPpftLLKEN 182
Cdd:cd05971   92 LIIYTSGTTGPPKGALHAHRVLLGHLPGVQfpfNLFPRDGD---LYWTPADW-AWIGGLLDVLLPSLYFGVP---VLAHR 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  183 MI-----SIIDFLEEYSISRLLAVPS---MIRAILPTLQHRGHNnklqscLKLVVLSGEPFPVSL--WDSLHSLLPETCF 252
Cdd:cd05971  165 MTkfdpkAALDLMSRYGVTTAFLPPTalkMMRQQGEQLKHAQVK------LRAIATGGESLGEELlgWAREQFGVEVNEF 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  253 lnlYGSTE---VSGDCTyfdcselprLLKTEEIGSvpIGKSISNCKVVLLGDEDKPY----EGEICVSGLCLSQ--GYMH 323
Cdd:cd05971  239 ---YGQTEcnlVIGNCS---------ALFPIKPGS--MGKPIPGHRVAIVDDNGTPLppgeVGEIAVELPDPVAflGYWN 304

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  324 SSIESEgyVKLHNNslcnhltndcgsqlYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAV 403
Cdd:cd05971  305 NPSATE--KKMAGD--------------WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAA 368

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327387  404 VLLSRDETELASLKAFVVLNKESNSSDGIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:cd05971  369 VVGIPDPIRGEIVKAFVVLNPGETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKI 432
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
 5-472 4.66e-20

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: 94.08  E-value: 4.66e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    5 VALYMPPSVEYVISVFSVLRCGEAFLPLDPSW-PRERvlslisssnislviacglssveSHWLVERNVCPVLLFSMDEKL 83
Cdd:cd05935   29 VGICLQNSPQYVIAYFAIWRANAVVVPINPMLkEREL----------------------EYILNDSGAKVAVVGSELDDL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   84 SVetgcssfvwpckkerqrkfcyLMYTSGSTGKPKGVCGTeqgllNRFLWMQELYPVVGEQRFAFKTSVGFID--HIQEF 161
Cdd:cd05935   87 AL---------------------IPYTSGTTGLPKGCMHT-----HFSAAANALQSAVWTGLTPSDVILACLPlfHVTGF 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  162 LGAILSSTALVIPPFTLLKENMISIIDFLEEYSISRLLAVPSMIRAILPTLQHRGHNnklQSCLKLVVLSGEPFPVSLWD 241
Cdd:cd05935  141 VGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRD---LSSLKVLTGGGAPMPPAVAE 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  242 SLHSLLPeTCFLNLYGSTEVSGDCTyfdcSELPRLLKTEEIGsvpIGKSISNCKVVLL--GDEDKP-YEGEICVSGLCLS 318
Cdd:cd05935  218 KLLKLTG-LRFVEGYGLTETMSQTH----TNPPLRPKLQCLG---IP*FGVDARVIDIetGRELPPnEVGEIVVRGPQIF 289

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  319 QGYMHSSIESEgyvklhnnslcNHLTNDCGSQlYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPD 398
Cdd:cd05935  290 KGYWNRPEETE-----------ESFIEIKGRR-FFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPA 357

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22327387  399 IAEAVVLLSRDETELASLKAFVVLNKESN---SSDGIIfsirNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEAL 472
Cdd:cd05935  358 I*EVCVISVPDERVGEEVKAFIVLRPEYRgkvTEEDII----EWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
PRK06188 PRK06188
acyl-CoA synthetase; Validated
 106-472 5.09e-20

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 95.05  E-value: 5.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   106 YLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSvgfIDHiqeflgailSSTALVIPpfTLLKENMI- 184
Cdd:PRK06188  172 GLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTP---LSH---------AGGAFFLP--TLLRGGTVi 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   185 --------SIIDFLEEYSISRLLAVPSMIRAILPtlQHRGHNNKLQScLKLVVLSGEPF-PVSLWDSLHSLLPetCFLNL 255
Cdd:PRK06188  238 vlakfdpaEVLRAIEEQRITATFLVPTMIYALLD--HPDLRTRDLSS-LETVYYGASPMsPVRLAEAIERFGP--IFAQY 312

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   256 YGSTEVSGDCTYFD----CSELPRLLKTeeigsvpIGKSISNCKVVLLGDEDKPYE----GEICVSGLCLSQGYMHSSIE 327
Cdd:PRK06188  313 YGQTEAPMVITYLRkrdhDPDDPKRLTS-------CGRPTPGLRVALLDEDGREVAqgevGEICVRGPLVMDGYWNRPEE 385

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   328 SEGYVK---LHnnslcnhltndcgsqlyyrTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVV 404
Cdd:PRK06188  386 TAEAFRdgwLH-------------------TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAV 446

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22327387   405 LLSRDETELASLKAFVVLNKESNSS-DGIIFSIRNWMGgklpPVMIPNHFVLVEKLPLTSSGKVDYEAL 472
Cdd:PRK06188  447 IGVPDEKWGEAVTAVVVLRPGAAVDaAELQAHVKERKG----SVHAPKQVDFVDSLPLTALGKPDKKAL 511
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 63-468 1.06e-19

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 94.10  E-value: 1.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    63 SHWLVE----RNVCPVLLFSMDEKLSVETgcSSFVWPCKKERQRkfCYLMYTSGSTGKPKGVCgteqgLLNRFLWmqeLY 138
Cdd:PRK06187  128 RTVIVEgdgpAAPLAPEVGEYEELLAAAS--DTFDFPDIDENDA--AAMLYTSGTTGHPKGVV-----LSHRNLF---LH 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   139 PVVGEQRFAFKTSVGFID-----HIQEF---LGAILSSTALVIP---PFTLlkenmisIIDFLEEYSISRLLAVPSMIRA 207
Cdd:PRK06187  196 SLAVCAWLKLSRDDVYLVivpmfHVHAWglpYLALMAGAKQVIPrrfDPEN-------LLDLIETERVTFFFAVPTIWQM 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   208 ILPTLQHRGHNnklQSCLKLVVLSGEPFPVSL---WDSLHSllpetC-FLNLYGSTEVSGDCTyfdCSELPR--LLKTEE 281
Cdd:PRK06187  269 LLKAPRAYFVD---FSSLRLVIYGGAALPPALlreFKEKFG-----IdLVQGYGMTETSPVVS---VLPPEDqlPGQWTK 337

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   282 IGSVpiGKSISNCKVVLLGDEDKPYE------GEICVSGLCLSQGYMHSSIESEgyvKLhnnslcnhLTNDcgsqlYYRT 355
Cdd:PRK06187  338 RRSA--GRPLPGVEARIVDDDGDELPpdggevGEIIVRGPWLMQGYWNRPEATA---ET--------IDGG-----WLHT 399

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   356 GDYGRqLSSGDLIFIgrRDRT---VKLNGKRMALEEIETTLELNPDIAEAVVLLSRDETELASLKAFVVLNKESNSSDGi 432
Cdd:PRK06187  400 GDVGY-IDEDGYLYI--TDRIkdvIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAK- 475

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 22327387   433 ifSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVD 468
Cdd:PRK06187  476 --ELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKIL 509
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
 107-467 1.19e-19

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: 92.79  E-value: 1.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  107 LMYTSGSTGKPKGVCGTeqgllnrflWMQELYPVVGEqrfafKTSVGFID-----------HIQE----FLGAILSSTAL 171
Cdd:cd05912   82 IMYTSGTTGKPKGVQQT---------FGNHWWSAIGS-----ALNLGLTEddnwlcalplfHISGlsilMRSVIYGMTVY 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  172 VIPPF------TLLKENMISIIDfleeysisrllAVPSMIRAILPTLQHRGHNNklqscLKLVVLSGEPFPVSLWdslhs 245
Cdd:cd05912  148 LVDKFdaeqvlHLINSGKVTIIS-----------VVPTMLQRLLEILGEGYPNN-----LRCILLGGGPAPKPLL----- 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  246 llpETC------FLNLYGSTEVsgdctyfdCSE---LPRLLKTEEIGSVpiGKSISNCKVVLLGDEDKPYE-GEICVSGL 315
Cdd:cd05912  207 ---EQCkekgipVYQSYGMTET--------CSQivtLSPEDALNKIGSA--GKPLFPVELKIEDDGQPPYEvGEILLKGP 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  316 CLSQGYMHSsiESEGYVKLHNNslcnhltndcgsqlYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLEL 395
Cdd:cd05912  274 NVTKGYLNR--PDATEESFENG--------------WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLS 337

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22327387  396 NPDIAEAVVLLSRDETELASLKAFVVLNKESnSSDGIIfsirNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:cd05912  338 HPAIKEAGVVGIPDDKWGQVPVAFVVSERPI-SEEELI----AYCSEKLAKYKVPKKIYFVDELPRTASGKL 404
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
 4-467 4.67e-19

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: 91.29  E-value: 4.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    4 VVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWpRERvlslisssnislviacglssvESHWLVERNVCPVLlFSMDEkl 83
Cdd:cd05903   28 VVAFQLPNWWEFAVLYLACLRIGAVTNPILPFF-REH---------------------ELAFILRRAKAKVF-VVPER-- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   84 svetgcssFvwpckkeRQRKF-------CYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGfid 156
Cdd:cd05903   83 --------F-------RQFDPaampdavALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMA--- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  157 HIQEFLGAILSSTALVIPPFTLLKENMISIIDFLEEYSISRLLAVPSMIRAILPTLQHRGHNnklQSCLKLVVLSGEPFP 236
Cdd:cd05903  145 HQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEP---LSRLRTFVCGGATVP 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  237 VSLWDSLHSLLpETCFLNLYGSTEVSGDCTYFDCSELPRLLKTEeiGSVPIGKSISnckvvlLGDEDKPY-----EGEIC 311
Cdd:cd05903  222 RSLARRAAELL-GAKVCSAYGSTECPGAVTSITPAPEDRRLYTD--GRPLPGVEIK------VVDDTGATlapgvEGELL 292

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  312 VSGLCLSQGYMHSSiesegyvklhnnslcnHLTNDCGSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIET 391
Cdd:cd05903  293 SRGPSVFLGYLDRP----------------DLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVED 356

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22327387  392 TLELNPDIAEAVVLLSRDETELASLKAFVVLnkESNSSDGIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:cd05903  357 LLLGHPGVIEAAVVALPDERLGERACAVVVT--KSGALLTFDELVAYLDRQGVAKQYWPERLVHVDDLPRTPSGKV 430
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
 106-467 1.25e-17

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: 87.76  E-value: 1.25e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  106 YLMYTSGSTGKPKGVCGTEQGLLNRFLW-MQELYPV-VGEQRFAfKTSVGFI-DHIQEFLGAILSSTALVI----PPFTL 178
Cdd:cd05967  234 YILYTSGTTGKPKGVVRDNGGHAVALNWsMRNIYGIkPGDVWWA-ASDVGWVvGHSYIVYGPLLHGATTVLyegkPVGTP 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  179 LKENMISIIdflEEYSISRLLAVPSMIRAILPTLQHRGHNNKLQ-SCLKLVVLSGEPFPVSL--WDSLHSLLPetcFLNL 255
Cdd:cd05967  313 DPGAFWRVI---EKYQVNALFTAPTAIRAIRKEDPDGKYIKKYDlSSLRTLFLAGERLDPPTleWAENTLGVP---VIDH 386

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  256 YGSTE----VSGDCTYFDCSELPrllkteeIGSVpiGKSISNCKVVLLGDEDKPYE----GEICVsGLCLSQGYMHSSIE 327
Cdd:cd05967  387 WWQTEtgwpITANPVGLEPLPIK-------AGSP--GKPVPGYQVQVLDEDGEPVGpnelGNIVI-KLPLPPGCLLTLWK 456

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  328 S-EGYVKLHnnslcnhLTNDCGsqlYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLL 406
Cdd:cd05967  457 NdERFKKLY-------LSKFPG---YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVG 526

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22327387  407 SRDETELASLKAFVVLNKESNSSD-----GIIFSIRNWMGgklpPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:cd05967  527 VRDELKGQVPLGLVVLKEGVKITAeelekELVALVREQIG----PVAAFRLVIFVKRLPKTRSGKI 588
Ac_CoA_lig_AcsA TIGR02188
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ...
 106-467 3.38e-17

acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.


Pssm-ID: 274022 [Multi-domain]  Cd Length: 626  Bit Score: 86.53  E-value: 3.38e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    106 YLMYTSGSTGKPKGVCGTEQG-LLNRFLWMQELYPVVGEQRFAFKTSVGFID-HiqeflgailssTALVIPPF-----TL 178
Cdd:TIGR02188  241 FILYTSGSTGKPKGVLHTTGGyLLYAAMTMKYVFDIKDGDIFWCTADVGWITgH-----------SYIVYGPLangatTV 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    179 LKEN---------MISIIdflEEYSISRLLAVPSMIRAilptLQHRGHNN----KLQScLKLVVLSGEPFPVSLWDSLHS 245
Cdd:TIGR02188  310 MFEGvptypdpgrFWEII---EKHKVTIFYTAPTAIRA----LMRLGDEWvkkhDLSS-LRLLGSVGEPINPEAWMWYYK 381

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    246 LL-PETC-FLNLYGSTEVSGDCTyfdcSELPrllkteeiGSVPI-----GKSISNCKVVLLGDEDKPYEGEICVSGLCLS 318
Cdd:TIGR02188  382 VVgKERCpIVDTWWQTETGGIMI----TPLP--------GATPTkpgsaTLPFFGIEPAVVDEEGNPVEGPGEGGYLVIK 449

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    319 QGY--MHSSI--ESEGYVKLHNNSLcnhltndcgsQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLE 394
Cdd:TIGR02188  450 QPWpgMLRTIygDHERFVDTYFSPF----------PGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALV 519

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22327387    395 LNPDIAEAVVLLSRDETELASLKAFVVLNKESNSSDGIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:TIGR02188  520 SHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKI 592
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
 105-468 7.13e-17

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: 82.84  E-value: 7.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  105 CYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAfktSVGFIDHIQEFLGAI--LSSTALVIppfTLLKEN 182
Cdd:cd17633    3 FYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAIL---APGPLSHSLFLYGAIsaLYLGGTFI---GQRKFN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  183 MISIIDFLEEYSISRLLAVPSMIRAILPTLQHrghnnklQSCLKLVVLSGEPFPVSLWDSLHSLLPETCFLNLYGSTEVS 262
Cdd:cd17633   77 PKSWIRKINQYNATVIYLVPTMLQALARTLEP-------ESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELS 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  263 GDCTYFDCSELPRllkteeiGSVpiGKSISNCKVVLLgDEDKPYEGEICVSglclsqgymhSSIESEGYVklhnnsLCNH 342
Cdd:cd17633  150 FITYNFNQESRPP-------NSV--GRPFPNVEIEIR-NADGGEIGKIFVK----------SEMVFSGYV------RGGF 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  343 LTNDCgsqlYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDE--TELAslkAFV 420
Cdd:cd17633  204 SNPDG----WMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDArfGEIA---VAL 276

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 22327387  421 VLNKESNSSDgiifsIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVD 468
Cdd:cd17633  277 YSGDKLTYKQ-----LKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIA 319
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
 5-467 2.09e-16

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: 83.33  E-value: 2.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    5 VALYMPPSVEYVISVFSVLRCGEAFLPLDPSW-PRERVLSLISSSNISLVIACGLSSVEShwLVERNVCpVLLFSMDEKL 83
Cdd:cd05923   56 VAVVLPNSVEAVIALLALHRLGAVPALINPRLkAAELAELIERGEMTAAVIAVDAQVMDA--IFQSGVR-VLALSDLVGL 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   84 SVETGCS-SFVWPCKKERQRKFCYlmYTSGSTGKPKGVCGTEQGLLNRFLWMQElypVVGEQRFAFKTSVGF--IDHIQE 160
Cdd:cd05923  133 GEPESAGpLIEDPPREPEQPAFVF--YTSGTTGLPKGAVIPQRAAESRVLFMST---QAGLRHGRHNVVLGLmpLYHVIG 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  161 FLGAILSSTAL---VIPPFTLLKENMISIIdflEEYSISRLLAVPSMIRAILPTLQHRGhnNKLQScLKLVVLSGEPFPV 237
Cdd:cd05923  208 FFAVLVAALALdgtYVVVEEFDPADALKLI---EQERVTSLFATPTHLDALAAAAEFAG--LKLSS-LRHVTFAGATMPD 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  238 SLWDSLHSLLPETcFLNLYGSTEVSGDCTYFDCSELPRLLK--TEEIGSVPIGKSIsnckVVLLGDEDkpyEGEICVSgl 315
Cdd:cd05923  282 AVLERVNQHLPGE-KVNIYGTTEAMNSLYMRDARTGTEMRPgfFSEVRIVRIGGSP----DEALANGE---EGELIVA-- 351

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  316 clsqgyMHSSIESEGYVKLHNNSLCNHltndcgSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLEL 395
Cdd:cd05923  352 ------AAADAAFTGYLNQPEATAKKL------QDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSR 419

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22327387  396 NPDIAEAVVLLSRDETELASLKAFVVLNKESNSSDGIIFSIRNwmgGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:cd05923  420 HPGVTEVVVIGVADERWGQSVTACVVPREGTLSADELDQFCRA---SELADFKRPRRYFFLDELPKNAMNKV 488
PRK07788 PRK07788
acyl-CoA synthetase; Validated
 110-467 2.76e-16

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 83.44  E-value: 2.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   110 TSGSTGKPKGVCGTE-------QGLLNRFLWMQELYPVVGEQRFAfktSVGFIdHIQefLGAILSSTaLVIP----PFTL 178
Cdd:PRK07788  215 TSGTTGTPKGAPRPEpsplaplAGLLSRVPFRAGETTLLPAPMFH---ATGWA-HLT--LAMALGST-VVLRrrfdPEAT 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   179 LKEnmisiidfLEEYSISRLLAVPSMIRAILPTLQHRGHNNKLQScLKLVVLSGEPFPVSLWDSLHSLLPETCFlNLYGS 258
Cdd:PRK07788  288 LED--------IAKHKATALVVVPVMLSRILDLGPEVLAKYDTSS-LKIIFVSGSALSPELATRALEAFGPVLY-NLYGS 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   259 TEVSGdCTYFDCSELPRLLKTeeIGSVPIGksisnCKVVLLGDEDKPYE----GEIcvsglclsqgYMHSSIESEGYvkl 334
Cdd:PRK07788  358 TEVAF-ATIATPEDLAEAPGT--VGRPPKG-----VTVKILDENGNEVPrgvvGRI----------FVGNGFPFEGY--- 416

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   335 hnnslcnhltndcgsqlyyrTGDYGRQ-----LSSGD--------LIFI-GRRDRTVKLNGKRMALEEIETTLELNPDIA 400
Cdd:PRK07788  417 --------------------TDGRDKQiidglLSSGDvgyfdedgLLFVdGRDDDMIVSGGENVFPAEVEDLLAGHPDVV 476

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22327387   401 EAVVLLSRDETELASLKAFVVLNKESN-SSDgiifSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:PRK07788  477 EAAVIGVDDEEFGQRLRAFVVKAPGAAlDED----AIKDYVRDNLARYKVPRDVVFLDELPRNPTGKV 540
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
 107-467 3.68e-16

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 81.15  E-value: 3.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  107 LMYTSGSTGKPKGVcgteqgLLNRFLWMQELYPVVGEQRFAFKTSVGF----IDHIQEFLGAILS---STALVI-PPFTL 178
Cdd:cd17635    6 VIFTSGTTGEPKAV------LLANKTFFAVPDILQKEGLNWVVGDVTYlplpATHIGGLWWILTClihGGLCVTgGENTT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  179 LKenmiSIIDFLEEYSISRLLAVPSMIRAILPTLQhrghnNKLQSCLKL-VVLSGEPFPVSLWDSLHSLLPETCFLNLYG 257
Cdd:cd17635   80 YK----SLFKILTTNAVTTTCLVPTLLSKLVSELK-----SANATVPSLrLIGYGGSRAIAADVRFIEATGLTNTAQVYG 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  258 STEVSGDCtyfdCSELPRLLKteEIGSVpiGKSISNCKVVLLGDEDKPY----EGEICVSGLCLSQGYmhssiesegyvk 333
Cdd:cd17635  151 LSETGTAL----CLPTDDDSI--EINAV--GRPYPGVDVYLAATDGIAGpsasFGTIWIKSPANMLGY------------ 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  334 lHNNSlcnHLTNDCGSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDETEL 413
Cdd:cd17635  211 -WNNP---ERTAEVLIDGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFG 286

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 22327387  414 ASLKAFVVLN--KESNSSDGIIFSIRnwmgGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:cd17635  287 ELVGLAVVASaeLDENAIRALKHTIR----RELEPYARPSTIVIVTDIPRTQSGKV 338
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 107-467 4.16e-16

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 82.64  E-value: 4.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   107 LMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRF--------AFKTSVGFIdhiqeflgAILSSTALVIPpftL 178
Cdd:PRK07656  171 ILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYlaanpffhVFGYKAGVN--------APLMRGATILP---L 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   179 LKENMISIIDFLEEYSISRLLAVPSMIRAIlptLQHRGHNNKLQSCLKLVVLSGEPFPVSLWDSLHSLLPETCFLNLYGS 258
Cdd:PRK07656  240 PVFDPDEVFRLIETERITVLPGPPTMYNSL---LQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLTGYGL 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   259 TEVSGDCTyfdcseLPRLLKTEEIGSVPIGKSISNC--KVV-LLGDEDKPYE-GEICVSGLCLSQGYMH------SSIES 328
Cdd:PRK07656  317 SEASGVTT------FNRLDDDRKTVAGTIGTAIAGVenKIVnELGEEVPVGEvGELLVRGPNVMKGYYDdpeataAAIDA 390

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   329 EGYvkLHnnslcnhltndcgsqlyyrTGDYGRQLSSGDLIFIGRRdrtvklngKRMAL--------EEIETTLELNPDIA 400
Cdd:PRK07656  391 DGW--LH-------------------TGDLGRLDEEGYLYIVDRK--------KDMFIvggfnvypAEVEEVLYEHPAVA 441

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22327387   401 EAVVLLSRDETELASLKAFVVLNKESN-SSDGIIfsirNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:PRK07656  442 EAAVIGVPDERLGEVGKAYVVLKPGAElTEEELI----AYCREHLAKYKVPRSIEFLDELPKNATGKV 505
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
 5-472 8.97e-16

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: 81.46  E-value: 8.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    5 VALYMPPSVEYVISVFSVLRCGEAFLPLDPSwprervlslisssnislviacgLSSVESHWLVERNVCPVLLFSMDEKLS 84
Cdd:cd05936   52 VALMLPNCPQFPIAYFGALKAGAVVVPLNPL----------------------YTPRELEHILNDSGAKALIVAVSFTDL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   85 VETGCSSFVWPckkERQRK-FCYLMYTSGSTGKPKGVCGTEQGLLNRFL----WMQELYpvVGEQRF--------AFKTS 151
Cdd:cd05936  110 LAAGAPLGERV---ALTPEdVAVLQYTSGTTGVPKGAMLTHRNLVANALqikaWLEDLL--EGDDVVlaalplfhVFGLT 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  152 VGFidhiqeFLGAILSSTALVIPPFTLlkenmISIIDFLEEYSISRLLAVPSMIRAILptlQHRGHNNKLQSCLKLVVLS 231
Cdd:cd05936  185 VAL------LLPLALGATIVLIPRFRP-----IGVLKEIRKHRVTIFPGVPTMYIALL---NAPEFKKRDFSSLRLCISG 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  232 GEPFPVSLWDSLHSL----LPETcflnlYGSTEVSGDCTyfdCSELPRLLKteeIGSvpIGKSISNCKVVLLGDEDKPY- 306
Cdd:cd05936  251 GAPLPVEVAERFEELtgvpIVEG-----YGLTETSPVVA---VNPLDGPRK---PGS--IGIPLPGTEVKIVDDDGEELp 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  307 ---EGEICVSGLCLSQGYMHSSIESEgyvklhnnslcNHLTNDcgsqlYYRTGDYGRQLSSGDLIFIGRRdrtvklngKR 383
Cdd:cd05936  318 pgeVGELWVRGPQVMKGYWNRPEETA-----------EAFVDG-----WLRTGDIGYMDEDGYFFIVDRK--------KD 373

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  384 MAL--------EEIETTLELNPDIAEAVVLLSRDETELASLKAFVVLNKESN-SSDGIIfsirNWMGGKLPPVMIPNHFV 454
Cdd:cd05936  374 MIIvggfnvypREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASlTEEEII----AFCREQLAGYKVPRQVE 449

                        490
                 ....*....|....*...
gi 22327387  455 LVEKLPLTSSGKVDYEAL 472
Cdd:cd05936  450 FRDELPKSAVGKILRREL 467
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 107-400 1.14e-15

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


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 80.97  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  107 LMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQR-------FAFktsvgfidhiqefLGAILSSTAlVIPPFTLL 179
Cdd:cd05910   90 ILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVdlatfplFAL-------------FGPALGLTS-VIPDMDPT 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  180 KENMIS---IIDFLEEYSISRLLAVPsmirAILPTLQHRGHNNKLQ-SCLKLVVLSGEPFPVSLWDSLHSLL-PETCFLN 254
Cdd:cd05910  156 RPARADpqkLVGAIRQYGVSIVFGSP----ALLERVARYCAQHGITlPSLRRVLSAGAPVPIALAARLRKMLsDEAEILT 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  255 LYGSTEVSGDCTYFDcSEL--PRLLKTEEIGSVPIGKSISNCKVVLLGDEDKPYE-------------GEICVSGLCLSQ 319
Cdd:cd05910  232 PYGATEALPVSSIGS-RELlaTTTAATSGGAGTCVGRPIPGVRVRIIEIDDEPIAewddtlelprgeiGEITVTGPTVTP 310

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  320 GYMHSSiESEGYVKLHnnslcnhltnDCGSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDI 399
Cdd:cd05910  311 TYVNRP-VATALAKID----------DNSEGFWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGV 379


                 .
gi 22327387  400 A 400
Cdd:cd05910  380 R 380
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
 105-473 1.79e-15

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: 80.21  E-value: 1.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  105 CYLMYTSGSTGKPKGVCGTEQGLLNRFlwmqELYPV-----------VGEQRFAFKTSVGFIDHIQEFLGAilssTALVI 173
Cdd:cd05958  100 CILAFTSGTTGAPKATMHFHRDPLASA----DRYAVnvlrlreddrfVGSPPLAFTFGLGGVLLFPFGVGA----SGVLL 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  174 PPFTllKENMISIIdflEEYSISRLLAVPSMIRAILPTLQHRGHnnkLQSCLKLVVLSGEPFPVSLWDSlhsllpetcFL 253
Cdd:cd05958  172 EEAT--PDLLLSAI---ARYKPTVLFTAPTAYRAMLAHPDAAGP---DLSSLRKCVSAGEALPAALHRA---------WK 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  254 NLYGSTEVSGdctyFDCSELPRLL---KTEEIGSVPIGKSISNCKVVLLGDEDKPY-EGEIcvsGLCLSQGymhssieSE 329
Cdd:cd05958  235 EATGIPIIDG----IGSTEMFHIFisaRPGDARPGATGKPVPGYEAKVVDDEGNPVpDGTI---GRLAVRG-------PT 300

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  330 GYVKLHNNSLCNHLTND--CGSQLYYRTGDygrqlssGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLS 407
Cdd:cd05958  301 GCRYLADKRQRTYVQGGwnITGDTYSRDPD-------GYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGH 373

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22327387  408 RDETELASLKAFVVLNKESNSSDGIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEALA 473
Cdd:cd05958  374 PDESRGVVVKAFVVLRPGVIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
 107-467 2.10e-15

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: 80.40  E-value: 2.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  107 LMYTSGSTGKPKGVCGTEQGLLNRFL---WMQELYPvvgeqRFAFKTSVGFiDHIqeflGAI---------LSSTALVIP 174
Cdd:cd05906  172 LMLTSGSTGFPKAVPLTHRNILARSAgkiQHNGLTP-----QDVFLNWVPL-DHV----GGLvelhlravyLGCQQVHVP 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  175 PFTLLkENMISIIDFLEEYSISRLLAvP----SMIRAILPTLQHRGHNNklqSCLKLVVLSGEPFPVSLWDSLHSLL--- 247
Cdd:cd05906  242 TEEIL-ADPLRWLDLIDRYRVTITWA-PnfafALLNDLLEEIEDGTWDL---SSLRYLVNAGEAVVAKTIRRLLRLLepy 316

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  248 --PETCFLNLYGSTEVSGDCTYfdCSELPRLLKTEEIGSVPIGKSISNCKVVLLGDEDKPYE----GEICVSGLCLSQGY 321
Cdd:cd05906  317 glPPDAIRPAFGMTETCSGVIY--SRSFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPegevGRLQVRGPVVTKGY 394

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  322 mhssiesegyvklHNNSLCNH--LTNDcGsqlYYRTGDYGrQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDI 399
Cdd:cd05906  395 -------------YNNPEANAeaFTED-G---WFRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGV 456

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  400 ------AEAVVLLSRDETELAslkafVVLNKESNSSDG---IIFSIR----NWMGGKlPPVMIPnhfVLVEKLPLTSSGK 466
Cdd:cd05906  457 epsftaAFAVRDPGAETEELA-----IFFVPEYDLQDAlseTLRAIRsvvsREVGVS-PAYLIP---LPKEEIPKTSLGK 527


                 .
gi 22327387  467 V 467
Cdd:cd05906  528 I 528
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
 4-467 1.05e-14

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: 78.05  E-value: 1.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    4 VVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSLISSSNISLVI--ACGLSSVESHWLvernvcPVLLFSMDE 81
Cdd:cd05904   59 VVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFttAELAEKLASLAL------PVVLLDSAE 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   82 KLSVETGCSSFVWP---CKKER--QRKFCYLMYTSGSTGKPKGVCGTEQGL---LNRFLWMQELYPvVGEQRFafktsVG 153
Cdd:cd05904  133 FDSLSFSDLLFEADeaePPVVVikQDDVAALLYSSGTTGRSKGVMLTHRNLiamVAQFVAGEGSNS-DSEDVF-----LC 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  154 FID--HIQEFLG---AILS--STALVIPPFTLlkENMISIIdflEEYSISRLLAVPSMIRAIlpTLQHRGHNNKLQScLK 226
Cdd:cd05904  207 VLPmfHIYGLSSfalGLLRlgATVVVMPRFDL--EELLAAI---ERYKVTHLPVVPPIVLAL--VKSPIVDKYDLSS-LR 278

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  227 LVVLSGEPFPVSLWDSLHSLLPETCFLNLYGSTEVSGDCTYFDCSELPRllktEEIGSVpiGKSISN--CKVVllgD--- 301
Cdd:cd05904  279 QIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTGVVAMCFAPEKDR----AKYGSV--GRLVPNveAKIV---Dpet 349

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  302 -EDKPY--EGEICVSGLCLSQGYMH------SSIESEGYVklhnnslcnhltndcgsqlyyRTGDYGRQLSSGDLIFIGR 372
Cdd:cd05904  350 gESLPPnqTGELWIRGPSIMKGYLNnpeataATIDKEGWL---------------------HTGDLCYIDEDGYLFIVDR 408

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  373 RDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDET--ELAslKAFVVLNKESN-SSDGIIfsirNWMGGKLPPVMI 449
Cdd:cd05904  409 LKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEagEVP--MAFVVRKPGSSlTEDEIM----DFVAKQVAPYKK 482

                        490
                 ....*....|....*...
gi 22327387  450 PNHFVLVEKLPLTSSGKV 467
Cdd:cd05904  483 VRKVAFVDAIPKSPSGKI 500
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
 106-467 1.66e-14

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: 77.16  E-value: 1.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  106 YLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFI-DHIQEFLGAILSSTALVIPPFTLLKENMI 184
Cdd:cd05969   93 LLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYWCTADPGWVtGTVYGIWAPWLNGVTNVVYEGRFDAESWY 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  185 SIIdflEEYSISRLLAVPSMIRAILPTLQHRGHNNKLQScLKLVVLSGEPF--PVSLWDSLHSLLPetcFLNLYGSTEVS 262
Cdd:cd05969  173 GII---ERVKVTVWYTAPTAIRMLMKEGDELARKYDLSS-LRFIHSVGEPLnpEAIRWGMEVFGVP---IHDTWWQTETG 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  263 gdcTYFDCSELPRLLKteeIGSvpIGKSISNCKVVLL---GDEDKPYE-GEICV-SGL-CLSQGYMHssiESEGYvklhN 336
Cdd:cd05969  246 ---SIMIANYPCMPIK---PGS--MGKPLPGVKAAVVdenGNELPPGTkGILALkPGWpSMFRGIWN---DEERY----K 310

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  337 NSLCNHltndcgsqlYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDETELASL 416
Cdd:cd05969  311 NSFIDG---------WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEII 381

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 22327387  417 KAFVVLNKESNSSDGIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:cd05969  382 KAFISLKEGFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKI 432
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
 107-473 1.80e-14

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 77.34  E-value: 1.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   107 LMYTSGSTGKPKGVcgteqgllnrflwmqelyPVVGEQRFAFKTSVGFIDHIQEFLGailSSTALVIPPF---------- 176
Cdd:PRK13383  179 VLLTSGTTGKPKGV------------------PRAPQLRSAVGVWVTILDRTRLRTG---SRISVAMPMFhglglgmlml 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   177 ------TLLKENMISIIDFLEEYSISR---LLAVPSMIRAILPTLQHRGHNNKLqSCLKLVVLSGEPFPVSLWDSLHSLL 247
Cdd:PRK13383  238 tialggTVLTHRHFDAEAALAQASLHRadaFTAVPVVLARILELPPRVRARNPL-PQLRVVMSSGDRLDPTLGQRFMDTY 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   248 PETCFlNLYGSTEVSgdctyfdcseLPRLLKTEEIGSVP--IGKSISNCKVVLLGDEDKPY----EGEICVSGlclsqgy 321
Cdd:PRK13383  317 GDILY-NGYGSTEVG----------IGALATPADLRDAPetVGKPVAGCPVRILDRNNRPVgprvTGRIFVGG------- 378

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   322 mhsSIESEGYVKLHNNSLCNHLTNdcgsqlyyrTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAE 401
Cdd:PRK13383  379 ---ELAGTRYTDGGGKAVVDGMTS---------TGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVAD 446

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22327387   402 AVVLLSRDETELASLKAFVVLNKESNSSDGiifSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEALA 473
Cdd:PRK13383  447 NAVIGVPDERFGHRLAAFVVLHPGSGVDAA---QLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELP 515
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 107-467 2.84e-14

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 76.40  E-value: 2.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  107 LMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTSVGFIdhiQEFLGAILSSTALVIPpfTLLKENMISI 186
Cdd:cd05973   93 MMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAADPGWA---YGLYYAITGPLALGHP--TILLEGGFSV 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  187 ---IDFLEEYSISRLLAVPSMIRAILPTLQHRGHNNKLQscLKLVVLSGEPF--PVSLW--DSLHSLLPETcflnlYGST 259
Cdd:cd05973  168 estWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPKGR--LRRVSSAGEPLtpEVIRWfdAALGVPIHDH-----YGQT 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  260 EVSgdctYFDCSE--LPRLLKTEEIGSVPIGKSIsnckVVLLGDEDKPYEGEICVSGLclsqgYMHSS--IESEGYVKLH 335
Cdd:cd05973  241 ELG----MVLANHhaLEHPVHAGSAGRAMPGWRV----AVLDDDGDELGPGEPGRLAI-----DIANSplMWFRGYQLPD 307

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  336 NNSLCNHltndcgsqlYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDETELAS 415
Cdd:cd05973  308 TPAIDGG---------YYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEV 378

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 22327387  416 LKAFVVLNKESNSSDGIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:cd05973  379 VKAFVVLRGGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKI 430
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 92-472 3.88e-14

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: 76.52  E-value: 3.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   92 FVWPCKKERQRkfCYLMYTSGSTGKPKGVCGTeqgllNRFLWMQELyPVVGEQRFAFKTSVGFIDHIQEF--------LG 163
Cdd:cd12119  155 YDWPDFDENTA--AAICYTSGTTGNPKGVVYS-----HRSLVLHAM-AALLTDGLGLSESDVVLPVVPMFhvnawglpYA 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  164 AILSSTALVIP-PFTLLKenmiSIIDFLEEYSISRLLAVPSMIRAILPTLQHRGHNnklQSCLKLVVLSGEPFPVSLWDS 242
Cdd:cd12119  227 AAMVGAKLVLPgPYLDPA----SLAELIEREGVTFAAGVPTVWQGLLDHLEANGRD---LSSLRRVVIGGSAVPRSLIEA 299

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  243 LHSLLPETCflNLYGSTEVSGDCTyfdCSELP---RLLKTEEIGSVPI--GKSIS--NCKVVLLGDEDKPY----EGEIC 311
Cdd:cd12119  300 FEERGVRVI--HAWGMTETSPLGT---VARPPsehSNLSEDEQLALRAkqGRPVPgvELRIVDDDGRELPWdgkaVGELQ 374

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  312 VSGLCLSQGYMHSSIESEGyvklhnnslcnhLTNDcgsqLYYRTGDYGRQLSSGdliFIGRRDRT---VKLNGKRMALEE 388
Cdd:cd12119  375 VRGPWVTKSYYKNDEESEA------------LTED----GWLRTGDVATIDEDG---YLTITDRSkdvIKSGGEWISSVE 435

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  389 IETTLELNPDIAEAVVLLSRDEtelaslK------AFVVLNKESNSSDGiifSIRNWMGGKLPPVMIPNHFVLVEKLPLT 462
Cdd:cd12119  436 LENAIMAHPAVAEAAVIGVPHP------KwgerplAVVVLKEGATVTAE---ELLEFLADKVAKWWLPDDVVFVDEIPKT 506

                        410
                 ....*....|
gi 22327387  463 SSGKVDYEAL 472
Cdd:cd12119  507 STGKIDKKAL 516
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
 107-467 5.28e-14

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: 74.46  E-value: 5.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  107 LMYTSGSTGKPKGV-CGTEQGLLNRFLWMQ-------ELYPVVGEQRFAFKTSVGFIdhiqeflgAILSSTALVIPPFTL 178
Cdd:cd17638    5 IMFTSGTTGRSKGVmCAHRQTLRAAAAWADcadltedDRYLIINPFFHTFGYKAGIV--------ACLLTGATVVPVAVF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  179 lkeNMISIIDFLEEYSISRLLAVPSMIRAIlptLQHRGHNNKLQSCLKLVVLSGEPFPVSLWDSLHSLLPETCFLNLYGS 258
Cdd:cd17638   77 ---DVDAILEAIERERITVLPGPPTLFQSL---LDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  259 TEVSgdctyfdCSELPRLLKTEEIGSVPIGKSISNCKVVLLGDedkpyeGEICVSGLCLSQGYMH------SSIESEGYv 332
Cdd:cd17638  151 TEAG-------VATMCRPGDDAETVATTCGRACPGFEVRIADD------GEVLVRGYNVMQGYLDdpeataEAIDADGW- 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  333 kLHnnslcnhltndcgsqlyyrTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDETE 412
Cdd:cd17638  217 -LH-------------------TGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERM 276

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 22327387  413 LASLKAFVVLNKES--NSSDGIIFSIRNWMGGKLPpvmipnHFVL-VEKLPLTSSGKV 467
Cdd:cd17638  277 GEVGKAFVVARPGVtlTEEDVIAWCRERLANYKVP------RFVRfLDELPRNASGKV 328
assembly_YfgL TIGR03300
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ...
 677-1028 7.84e-14

outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274511 [Multi-domain]  Cd Length: 377  Bit Score: 74.58  E-value: 7.84e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    677 VSMQEIWKVHMESCVDASPL----VVLKDSktyLFIGSHSRKFSCIDAKSGSMYWETILEGRIegSAMVVGDFSQVVIGC 752
Cdd:TIGR03300   38 VKVDQVWSASVGDGVGHYYLrlqpAVAGGK---VYAADADGTVAALDAETGKRLWRVDLDERL--SGGVGADGGLVFVGT 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    753 YKGKLYFLDFSTGSLCWKFQACGEIKCQPVVDtsSQLIWCGSHDHTLYALD---------YRSQccVYKLQCGGSifASP 823
Cdd:TIGR03300  113 EKGEVIALDAEDGKELWRAKLSSEVLSPPLVA--NGLVVVRTNDGRLTALDaatgerlwtYSRV--TPPLTLRGS--ASP 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    824 AIDEGhsSLYVASTSGRVIAVSIKDSpfHTLWlfelEAPIF---GSLCI--------TPSTQNVICCLV--DGQVIAMSP 890
Cdd:TIGR03300  187 VIADG--GVLVGFAGGKLVALDLQTG--QPLW----EQRVAlpkGRTELerlvdvdgDPVVDGGQVYAVsyQGRVAALDL 258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    891 -SGTIIWRYRTGGPifAGPCMSHvlpSQVLVCCRNGCVYSLEPESGCLVWednigdpitasayidENLHFESHEL---LA 966
Cdd:TIGR03300  259 rSGRVLWKRDASSY--QGPAVDD---NRLYVTDADGVVVALDRRSGSELW---------------KNDELKYRQLtapAV 318

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22327387    967 SDRLVTVCSSSGRVHVL-RVRPSILSRDSHDSkvgeitrmelqADIFSSPVMIGGRIFVGCRD 1028
Cdd:TIGR03300  319 LGGYLVVGDFEGYLHWLdRDDGSFVARLKTDG-----------SGIASPPVVVGDGLLVQTRD 370
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
 105-467 1.65e-13

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: 74.83  E-value: 1.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  105 CYLMYTSGSTGKPKGVCGTEQGL-LNRFLWMQELYPVVGEQRFAFKTSVGFIDHIQEFLGAILSSTALVI----PPFtll 179
Cdd:cd05968  239 LMIIYTSGTTGKPKGTVHVHAGFpLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLydgaPDH--- 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  180 kENMISIIDFLEEYSISRLLAVPSMIRAILPTLQHRGHNNKLQScLKLVVLSGEPF-PVS-LWDSLHSLLPETCFLNLYG 257
Cdd:cd05968  316 -PKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSS-LRVLGSTGEPWnPEPwNWLFETVGKGRNPIINYSG 393

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  258 STEVSGD--CTYFdcselprllkTEEIGSVPIGKSISNCKVVLLGDEDKPY---EGEICVSG--LCLSQGYMHssiESEG 330
Cdd:cd05968  394 GTEISGGilGNVL----------IKPIKPSSFNGPVPGMKADVLDESGKPArpeVGELVLLApwPGMTRGFWR---DEDR 460

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  331 YVKLHNNSLCNhltndcgsqlYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDE 410
Cdd:cd05968  461 YLETYWSRFDN----------VWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHP 530

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 22327387  411 TELASLKAFVVLNKESNSSDGIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:cd05968  531 VKGEAIVCFVVLKPGVTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKV 587
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
 388-466 2.22e-13

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: 66.03  E-value: 2.22e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22327387    388 EIETTLELNPDIAEAVVLLSRDETELASLKAFVVLNKESnssDGIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGK 466
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGV---ELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
 107-467 2.98e-13

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


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 73.66  E-value: 2.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   107 LMYTSGSTGKPKGVCGTEQGLLNRFlwMQELYpvvgEQRFAFKTSVGFID----HIQEfLGAILSSTAL----VIPPFTL 178
Cdd:PRK07786  179 IMYTSGTTGRPKGAVLTHANLTGQA--MTCLR----TNGADINSDVGFVGvplfHIAG-IGSMLPGLLLgaptVIYPLGA 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   179 LKENmiSIIDFLEEYSISRLLAVPSMIRAILPTLQHRGHNnklqscLKLVVLS--GEPFPVSLWDSLHSLLPETCFLNLY 256
Cdd:PRK07786  252 FDPG--QLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRD------LALRVLSwgAAPASDTLLRQMAATFPEAQILAAF 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   257 GSTEVSGDCTYFDCSELPRllkteEIGSVpiGKSISN--CKVVllgDED----KPYE-GEICVSGLCLSQGYMhssiese 329
Cdd:PRK07786  324 GQTEMSPVTCMLLGEDAIR-----KLGSV--GKVIPTvaARVV---DENmndvPVGEvGEIVYRAPTLMSGYW------- 386

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   330 gyvklhNNSlcnHLTNDCGSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRD 409
Cdd:PRK07786  387 ------NNP---EATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRAD 457

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 22327387   410 ETELASLKAFVVLNkeSNSSDGIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:PRK07786  458 EKWGEVPVAVAAVR--NDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
PRK07638 PRK07638
acyl-CoA synthetase; Validated
 1-472 3.70e-13

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 73.27  E-value: 3.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387     1 MPKVVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSLISSSNISLVIA-----CGLSSVEshwlvernvCPVL 75
Cdd:PRK07638   49 KNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTeryklNDLPDEE---------GRVI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    76 LFS-MDEKLSVETGCSSFVwpckKERQRKFCYLMYTSGSTGKPKGVCGTEQGllnrflWMQELYPVVGEQRFAFKTSV-- 152
Cdd:PRK07638  120 EIDeWKRMIEKYLPTYAPI----ENVQNAPFYMGFTSGSTGKPKAFLRAQQS------WLHSFDCNVHDFHMKREDSVli 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   153 -GFIDHIQEFLGAI----LSSTALVIPPFTLLKenmisIIDFLEEYSISRLLAVPSMIRAILPTlqhrghNNKLQSCLKL 227
Cdd:PRK07638  190 aGTLVHSLFLYGAIstlyVGQTVHLMRKFIPNQ-----VLDKLETENISVMYTVPTMLESLYKE------NRVIENKMKI 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   228 VVlSGEPFPVSLWDSLHSLLPETCFLNLYGSTEVSgdctyFDCSelprlLKTEEIGSVP--IGKSISNCKVvllgdEDKP 305
Cdd:PRK07638  259 IS-SGAKWEAEAKEKIKNIFPYAKLYEFYGASELS-----FVTA-----LVDEESERRPnsVGRPFHNVQV-----RICN 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   306 YEGEICVSGlclSQG--YMHSSIESEGYVklhNNSLCNHLTNDCGsqlYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKR 383
Cdd:PRK07638  323 EAGEEVQKG---EIGtvYVKSPQFFMGYI---IGGVLARELNADG---WMTVRDVGYEDEEGFIYIVGREKNMILFGGIN 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   384 MALEEIETTLELNPDIAEAVVLLSRDetELASLKAFVVLNKESNSSdgiifSIRNWMGGKLPPVMIPNHFVLVEKLPLTS 463
Cdd:PRK07638  394 IFPEEIESVLHEHPAVDEIVVIGVPD--SYWGEKPVAIIKGSATKQ-----QLKSFCLQRLSSFKIPKEWHFVDEIPYTN 466


                  ....*....
gi 22327387   464 SGKVDYEAL 472
Cdd:PRK07638  467 SGKIARMEA 475
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
 251-468 5.11e-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: 71.53  E-value: 5.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  251 CFLNLYGSTEVSGDCTYFDCSELPrllkteeiGSVpiGKSISNCKVVLLGDEDKPYE----GEICVSGLCLSQGYmhssi 326
Cdd:cd17637  138 TFWSLYGQTETSGLVTLSPYRERP--------GSA--GRPGPLVRVRIVDDNDRPVPagetGEIVVRGPLVFQGY----- 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  327 esegyvkLHNNSLCNHlTNDCGsqlYYRTGDYGRQLSSGDLIFIGRR--DRTVKLNGKRMALEEIETTLELNPDIAEAVV 404
Cdd:cd17637  203 -------WNLPELTAY-TFRNG---WHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCV 271

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22327387  405 LLSRDETELASLKAFVVLN-KESNSSDGIIfsirNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVD 468
Cdd:cd17637  272 IGVPDPKWGEGIKAVCVLKpGATLTADELI----EFVGSRIARYKKPRYVVFVEALPKTADGSID 332
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 107-467 6.11e-13

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 72.22  E-value: 6.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  107 LMYTSGSTGKPKGVCGTEQ----GLLNRFLWMQeLYPvvGEQRFAFkTSVGFIDHIQEFLGAILSSTALVIPpFTLLKEN 182
Cdd:cd05974   90 LYFTSGTTSKPKLVEHTHRsypvGHLSTMYWIG-LKP--GDVHWNI-SSPGWAKHAWSCFFAPWNAGATVFL-FNYARFD 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  183 MISIIDFLEEYSISRLLAVPSMIRAILptlqhRGHNNKLQSCLKLVVLSGEPFPVSLWDSLHSLLPETcFLNLYGSTEVs 262
Cdd:cd05974  165 AKRVLAALVRYGVTTLCAPPTVWRMLI-----QQDLASFDVKLREVVGAGEPLNPEVIEQVRRAWGLT-IRDGYGQTET- 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  263 gdctyfdcselprllkTEEIGSVP--------IGKSISNCKVVLLGDEDKPY-EGEICvsglcLSQGYMHSSIESEGYvk 333
Cdd:cd05974  238 ----------------TALVGNSPgqpvkagsMGRPLPGYRVALLDPDGAPAtEGEVA-----LDLGDTRPVGLMKGY-- 294

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  334 lHNNslcNHLTNDCGSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDETEL 413
Cdd:cd05974  295 -AGD---PDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRL 370

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 22327387  414 ASLKAFVVLNKESNSSDGIIFSIRNWMGGKLPPVMIPNHFVLVEkLPLTSSGKV 467
Cdd:cd05974  371 SVPKAFIVLRAGYEPSPETALEIFRFSRERLAPYKRIRRLEFAE-LPKTISGKI 423
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
 109-474 7.38e-13

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 72.52  E-value: 7.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   109 YTSGSTGKPKGVCGTEQGLLnrflwMQELYPVV----GEQRFAFKTSVgfIDHIqeflGAILSSTALV--------IPPF 176
Cdd:PLN02860  179 FTSGTTGRPKGVTISHSALI-----VQSLAKIAivgyGEDDVYLHTAP--LCHI----GGLSSALAMLmvgachvlLPKF 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   177 tllkeNMISIIDFLEEYSISRLLAVPSMIRAILPTLQHRGhNNKLQSCLKLVVLSGEPFPVSLWDSLHSLLP-------- 248
Cdd:PLN02860  248 -----DAKAALQAIKQHNVTSMITVPAMMADLISLTRKSM-TWKVFPSVRKILNGGGSLSSRLLPDAKKLFPnaklfsay 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   249 ---ETC----FLNLYGSTEVSGDCTYFDCSElPRLLKTEEIGSVPIGKSISNCKVVLLGDEDKPyEGEICVSGLCLSQGY 321
Cdd:PLN02860  322 gmtEACssltFMTLHDPTLESPKQTLQTVNQ-TKSSSVHQPQGVCVGKPAPHVELKIGLDESSR-VGRILTRGPHVMLGY 399

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   322 MHSSIESegyvklhnnslcnhlTNDCGSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAE 401
Cdd:PLN02860  400 WGQNSET---------------ASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVAS 464

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   402 AVVLLSRDETELASLKAFVVLNkesnssDGIIFSIRNWMGGKLPPVM------------------IPNHFVLVEK-LPLT 462
Cdd:PLN02860  465 VVVVGVPDSRLTEMVVACVRLR------DGWIWSDNEKENAKKNLTLssetlrhhcreknlsrfkIPKLFVQWRKpFPLT 538

                         410
                  ....*....|..
gi 22327387   463 SSGKVDYEALAR 474
Cdd:PLN02860  539 TTGKIRRDEVRR 550
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
 106-467 8.18e-13

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: 72.59  E-value: 8.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  106 YLMYTSGSTGKPKGVCGTEQGLL----NRFLWMQELYPvvgEQRFAFKTSVGFID-HIQEFLGAILSSTALVI---PPFT 177
Cdd:cd05966  235 FILYTSGSTGKPKGVVHTTGGYLlyaaTTFKYVFDYHP---DDIYWCTADIGWITgHSYIVYGPLANGATTVMfegTPTY 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  178 LLKENMISIIdflEEYSISRLLAVPSMIRAilptLQHRG----HNNKLQScLKLVVLSGEPFPVSLWDSLHSLL-PETC- 251
Cdd:cd05966  312 PDPGRYWDIV---EKHKVTIFYTAPTAIRA----LMKFGdewvKKHDLSS-LRVLGSVGEPINPEAWMWYYEVIgKERCp 383

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  252 FLNLYGSTEVSGDCTyfdcSELPrllkteeiGSVPIgKSISNC------KVVLLGDEDKPYEGEicVSG-LCLSQGY--M 322
Cdd:cd05966  384 IVDTWWQTETGGIMI----TPLP--------GATPL-KPGSATrpffgiEPAILDEEGNEVEGE--VEGyLVIKRPWpgM 448

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  323 HSSI--ESEGYVKLHnnslcnhLTNDCGsqlYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIA 400
Cdd:cd05966  449 ARTIygDHERYEDTY-------FSKFPG---YYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVA 518

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22327387  401 EAVVLLSRDETELASLKAFVVLNKESNSSDGIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:cd05966  519 EAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKI 585
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 105-467 1.02e-12

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


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 70.77  E-value: 1.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  105 CYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRF--------AFKTSVGFidhiqefLGAILSSTALVIP-- 174
Cdd:cd05917    5 INIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLcipvplfhCFGSVLGV-------LACLTHGATMVFPsp 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  175 ---PFTLLKEnmisiidfLEEYSISRLLAVPSMIRAILptlqhrGHNNKLQ---SCLKLVVLSGEPFPVSLWDSLHSLLP 248
Cdd:cd05917   78 sfdPLAVLEA--------IEKEKCTALHGVPTMFIAEL------EHPDFDKfdlSSLRTGIMAGAPCPPELMKRVIEVMN 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  249 ETCFLNLYGSTEVSGDCTyfdCSEL--PRLLKTEEIGSV-PIGKS----ISNCKVVLLGDEdkpyeGEICVSGLCLSQGY 321
Cdd:cd05917  144 MKDVTIAYGMTETSPVST---QTRTddSIEKRVNTVGRImPHTEAkivdPEGGIVPPVGVP-----GELCIRGYSVMKGY 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  322 mhssiesegyvklHNNSLcnhLTNDCGSQ-LYYRTGDYGRQLSSGDLIFIGR-RDRTVKlNGKRMALEEIETTLELNPDI 399
Cdd:cd05917  216 -------------WNDPE---KTAEAIDGdGWLHTGDLAVMDEDGYCRIVGRiKDMIIR-GGENIYPREIEEFLHTHPKV 278

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22327387  400 AEAVVLLSRDETELASLKAFVVLNKESNSSDGiifSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:cd05917  279 SDVQVVGVPDERYGEEVCAWIRLKEGAELTEE---DIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKI 343
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
 107-467 1.02e-12

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 72.11  E-value: 1.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   107 LMYTSGSTGKPKGVCGTEQGLLNRfLWMqelypvVGEqrfafktSVGFIDH---------------IQEFLGAILSSTAL 171
Cdd:PRK12583  206 IQYTSGTTGFPKGATLSHHNILNN-GYF------VAE-------SLGLTEHdrlcvpvplyhcfgmVLANLGCMTVGACL 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   172 VIP-----PFTLLKEnmisiidfLEEYSISRLLAVPSMIRAilpTLQHRGHNNKLQSCLKLVVLSGEPFPVSLW----DS 242
Cdd:PRK12583  272 VYPneafdPLATLQA--------VEEERCTALYGVPTMFIA---ELDHPQRGNFDLSSLRTGIMAGAPCPIEVMrrvmDE 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   243 LHslLPETcfLNLYGSTEVSgDCTYFDCSELPRLLKTEEIGSVpigKSISNCKVV-LLGDEDKPYE-GEICVSGLCLSQG 320
Cdd:PRK12583  341 MH--MAEV--QIAYGMTETS-PVSLQTTAADDLERRVETVGRT---QPHLEVKVVdPDGATVPRGEiGELCTRGYSVMKG 412

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   321 YMHS------SIESEGYvkLHnnslcnhltndcgsqlyyrTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLE 394
Cdd:PRK12583  413 YWNNpeataeSIDEDGW--MH-------------------TGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLF 471

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22327387   395 LNPDIAEAVVLLSRDETELASLKAFVVLNKESNSSDGiifSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:PRK12583  472 THPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEE---ELREFCKARIAHFKVPRYFRFVDEFPMTVTGKV 541
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
107-467 1.76e-12

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 71.15  E-value: 1.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   107 LMYTSGSTGKPKGVCGTEQ-------------GLLNRFLWMQELyPvvgeqrfafktsvgfIDHIQEfLGAILSSTALVI 173
Cdd:PRK03640  146 IMYTSGTTGKPKGVIQTYGnhwwsavgsalnlGLTEDDCWLAAV-P---------------IFHISG-LSILMRSVIYGM 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   174 PPFTLLKENMISIIDFLEEYSISRLLAVPSMIRAILPTLQHRGHNNKLQSCLklvvLSGEPFPVSLWdslhsllpETCFL 253
Cdd:PRK03640  209 RVVLVEKFDAEKINKLLQTGGVTIISVVSTMLQRLLERLGEGTYPSSFRCML----LGGGPAPKPLL--------EQCKE 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   254 -NL-----YGSTEVsgdctyfdCSE---LPRLLKTEEIGSVpiGKSISNC--KVVLLGDEDKPYE-GEICVSGLCLSQGY 321
Cdd:PRK03640  277 kGIpvyqsYGMTET--------ASQivtLSPEDALTKLGSA--GKPLFPCelKIEKDGVVVPPFEeGEIVVKGPNVTKGY 346

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   322 mhssiesegyvkLHNNSLcnhlTNDCGSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAE 401
Cdd:PRK03640  347 ------------LNREDA----TRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAE 410

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22327387   402 AVVLLSRDETELASLKAFVVLNKESNSSDgiifsIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:PRK03640  411 AGVVGVPDDKWGQVPVAFVVKSGEVTEEE-----LRHFCEEKLAKYKVPKRFYFVEELPRNASGKL 471
PQQ_2 pfam13360
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
 680-898 1.89e-12

PQQ-like domain; This domain contains several repeats of the PQQ repeat.


Pssm-ID: 433144 [Multi-domain]  Cd Length: 233  Bit Score: 68.20  E-value: 1.89e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    680 QEIWKVHMESCVDASPLVvlkdSKTYLFIGSHSRKFSCIDAKSGSMYWETILEGRIEGSAMVVGDfsQVVIGCYKGKLYF 759
Cdd:pfam13360   14 AELWRVDLETGLGGGVAV----DGGRLFVATGGGQLVALDAATGKLLWRQTLSGEVLGAPLVAGG--RVFVVAGDGSLIA 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    760 LDFSTGSLCWKFQACGEikcQPVVDTSSQLIWcgsHDHTLYALDYRSQCCVYKLQCG--------------------GSI 819
Cdd:pfam13360   88 LDAADGRRLWSYQRSGE---PLALRSSGSPAV---VGDTVVAGFSSGKLVALDPATGkvrweaplaaprgtnelerlVDI 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    820 FASPAIDEGhsSLYVASTSGRVIAVSIKDSpfHTLWlfelEAPIFGSLCITPSTQNVICCLVDGQVIAMSP-SGTIIWRY 898
Cdd:pfam13360  162 TGTPVVAGG--RVFASAYQGRLVAFDAATG--RRLW----TREISGPNGPILDGDLLYVVSDDGELYALDRaTGAVVWKT 233
PRK09274 PRK09274
peptide synthase; Provisional
 109-384 2.26e-12

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 70.70  E-value: 2.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   109 YTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQR-------FAFktsvgfidhiqefLGAILSSTAlVIPPFTLLKE 181
Cdd:PRK09274  181 FTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIdlptfplFAL-------------FGPALGMTS-VIPDMDPTRP 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   182 ---NMISIIDFLEEYSISRLLAVPSMIRAILptlQH-RGHNNKLQScLKLVVLSGEPFPVSLWDSLHSLLPETC-FLNLY 256
Cdd:PRK09274  247 atvDPAKLFAAIERYGVTNLFGSPALLERLG---RYgEANGIKLPS-LRRVISAGAPVPIAVIERFRAMLPPDAeILTPY 322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   257 GSTE------VSGDCTYFDCSELprllkTEEIGSVPIGKSISNCKVVLLGDEDKPYE-------------GEICVSGLCL 317
Cdd:PRK09274  323 GATEalpissIESREILFATRAA-----TDNGAGICVGRPVDGVEVRIIAISDAPIPewddalrlatgeiGEIVVAGPMV 397

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22327387   318 SQGYmhssiesegyvklHNNSLCNHLT--NDCGSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRM 384
Cdd:PRK09274  398 TRSY-------------YNRPEATRLAkiPDGQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTL 453
PQQ COG1520
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ...
 677-1038 2.98e-12

Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441129 [Multi-domain]  Cd Length: 370  Bit Score: 69.46  E-value: 2.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  677 VSMQEIWKVHMESCVDA--SPLV-VLKDSKtyLFIGSHSRKFSCIDAKSGSMYWETILEGRIegSAMVVGDFSQVVIGCY 753
Cdd:COG1520   30 VKVKQLWSASVGDGVGKgySRLApAVAGDR--VYAADADGRVAALDAATGKELWRVDLGEPL--SGGVGADGGLVVVGTE 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  754 KGKLYFLDFSTGSLCWKfqacgeikcqpvvdtsSQLiwcgshdhtlyaldyrsqccvyklqcGGSIFASPAIDEGHssLY 833
Cdd:COG1520  106 DGEVIALDADDGEELWR----------------ARL--------------------------SSEVLAAPAVAGGR--VV 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  834 VASTSGRVIAVSIKDSpfHTLWLFELEAPIF-----GSLCITPSTqnVICCLVDGQVIAMSP-SGTIIWRYR-------- 899
Cdd:COG1520  142 VRTGDGRVYALDAATG--ERLWSYQRPVPALtlrgtSSPVIVGGA--VLVGFANGKLVALDLaNGQPLWEQRvaqprgrt 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  900 --------TGGPIFAGPcmshvlpsqvLVCCR--NGCVYSLEPESGCLVWEDNIgdpitaSAYidenlhfesHELLASDR 969
Cdd:COG1520  218 elerlvdvDGTPVVDGG----------VVYAVayQGRLAALDLRSGRVLWSRDL------SSY---------TGLAVDGN 272

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327387  970 LVTVCSSSGRVHVLRvrpsilsRDShdskvGEI--TRMELQADIFSSPVMIGGRIFVGCRDDYVHCLSLES 1038
Cdd:COG1520  273 NLYVTDDDGRVWALD-------RRN-----GAElwKQDALLYRGLTAPVVLGDYVVVGDFEGYLHWLSRDD 331
PRK06145 PRK06145
acyl-CoA synthetase; Validated
 107-467 3.60e-12

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 69.91  E-value: 3.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   107 LMYTSGSTGKPKGVcgteqgllnrflwmqelypVVGEQRFAFKTsvgfIDHIQEfLGAILSSTALVIPPF---------- 176
Cdd:PRK06145  154 LMYTSGTTDRPKGV-------------------MHSYGNLHWKS----IDHVIA-LGLTASERLLVVGPLyhvgafdlpg 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   177 --TLLKENMISII-DF-----LEEYSISRLLA---VPSMIRAILpTLQHRGHNNklQSCLKLVVLSGEPFPVSLWDSLHS 245
Cdd:PRK06145  210 iaVLWVGGTLRIHrEFdpeavLAAIERHRLTCawmAPVMLSRVL-TVPDRDRFD--LDSLAWCIGGGEKTPESRIRDFTR 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   246 LLPETCFLNLYGSTE-VSGDCTYFDCSELprllktEEIGSVpiGKSISNCKVVLLGDEDK----PYEGEICVSGLCLSQG 320
Cdd:PRK06145  287 VFTRARYIDAYGLTEtCSGDTLMEAGREI------EKIGST--GRALAHVEIRIADGAGRwlppNMKGEICMRGPKVTKG 358

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   321 YMHSSIES-EGYVklhnnslcnhltNDcgsqlYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDI 399
Cdd:PRK06145  359 YWKDPEKTaEAFY------------GD-----WFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEV 421

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22327387   400 AEAVVLLSRDETELASLKAFVVLNKESNSSdgiIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:PRK06145  422 AEAAVIGVHDDRWGERITAVVVLNPGATLT---LEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKV 486
PRK13382 PRK13382
bile acid CoA ligase;
100-467 5.68e-12

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 69.40  E-value: 5.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   100 RQRKFCYLMYTSGSTGKPKGVCGTEQG-------LLNRFLWMQELYPVVGEQRFAfktSVGFIdhiQEFLGAILSSTALV 172
Cdd:PRK13382  194 TGRKGRVILLTSGTTGTPKGARRSGPGgigtlkaILDRTPWRAEEPTVIVAPMFH---AWGFS---QLVLAASLACTIVT 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   173 IPPFTllKENMISIIDfleEYSISRLLAVPSMIRAILpTLQHRGHNNKLQSCLKLVVLSGEPFP----VSLWDSLHSLLp 248
Cdd:PRK13382  268 RRRFD--PEATLDLID---RHRATGLAVVPVMFDRIM-DLPAEVRNRYSGRSLRFAAASGSRMRpdvvIAFMDQFGDVI- 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   249 etcfLNLYGSTEVSGDCTyfdcsELPRLLKT--EEIGSVPIGKSISnckvVLLGDEDKPYEGEIcvsglclSQGYMHSSI 326
Cdd:PRK13382  341 ----YNNYNATEAGMIAT-----ATPADLRAapDTAGRPAEGTEIR----ILDQDFREVPTGEV-------GTIFVRNDT 400

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   327 ESEGYV-----KLHNNSLCnhltndcgsqlyyrTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAE 401
Cdd:PRK13382  401 QFDGYTsgstkDFHDGFMA--------------SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAE 466

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22327387   402 AVVLLSRDETELASLKAFVVLNKESNSSDGiifSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:PRK13382  467 AAVIGVDDEQYGQRLAAFVVLKPGASATPE---TLKQHVRDNLANYKVPRDIVVLDELPRGATGKI 529
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
 107-426 1.75e-11

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: 67.62  E-value: 1.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  107 LMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFafktsVGF--IDHIQEFLGAI-----LSSTALVIPPFTLL 179
Cdd:cd05907   92 IIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRH-----LSFlpLAHVFERRAGLyvpllAGARIYFASSAETL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  180 KEN--------MISIIDFLEE-YSISRLLAVPSMIRAILptLQHRGHNnklqscLKLVVLSGEPFPVSLWDSLHSL-LPe 249
Cdd:cd05907  167 LDDlsevrptvFLAVPRVWEKvYAAIKVKAVPGLKRKLF--DLAVGGR------LRFAASGGAPLPAELLHFFRALgIP- 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  250 tcFLNLYGSTEVSGDCTYfdcselpRLLKTEEIGSVpiGKSISNCKVVLlgDEDkpyeGEICVSGLCLSQGYmhssiese 329
Cdd:cd05907  238 --VYEGYGLTETSAVVTL-------NPPGDNRIGTV--GKPLPGVEVRI--ADD----GEILVRGPNVMLGY-------- 292

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  330 gyvklHNNSLCNHLTNDCgsQLYYRTGDYGRQLSSGDLIFIGRRDRTVKL-NGKRMALEEIETTLELNPDIAEAVVLLSR 408
Cdd:cd05907  293 -----YKNPEATAEALDA--DGWLHTGDLGEIDEDGFLHITGRKKDLIITsGGKNISPEPIENALKASPLISQAVVIGDG 365

                        330
                 ....*....|....*...
gi 22327387  409 deteLASLKAFVVLNKES 426
Cdd:cd05907  366 ----RPFLVALIVPDPEA 379
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
 5-474 5.87e-11

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: 65.77  E-value: 5.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    5 VALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSLisssnislviacgLSSVESHWLVERnvcpvllfsmdekls 84
Cdd:cd05941   40 VAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYV-------------ITDSEPSLVLDP--------------- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   85 vetgcssfvwpckkerqrkfCYLMYTSGSTGKPKGVCGTEQGLLN---------------RFLWMQELYPVVGeqrfafk 149
Cdd:cd05941   92 --------------------ALILYTSGTTGRPKGVVLTHANLAAnvralvdawrwteddVLLHVLPLHHVHG------- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  150 tsVGFIDHIQEFLGAilssTALVIPPFTLLKENMISiidflEEYSISRLLAVPSMIRAILPTLQH--RGHNNKLQSC--- 224
Cdd:cd05941  145 --LVNALLCPLFAGA----SVEFLPKFDPKEVAISR-----LMPSITVFMGVPTIYTRLLQYYEAhfTDPQFARAAAaer 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  225 LKLVVLSGEPFPVSL---WDSL--HSLLPEtcflnlYGSTEVSgdctyfdcSELPRLLKTEEI-GSVpiGKSISNCKVVL 298
Cdd:cd05941  214 LRLMVSGSAALPVPTleeWEAItgHTLLER------YGMTEIG--------MALSNPLDGERRpGTV--GMPLPGVQARI 277

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  299 LGDEDKPY-----EGEICVSGLCLSQGY--MHSSIESEgyvklhnnslcnhLTNDcGsqlYYRTGDYGRQLSSGDLIFIG 371
Cdd:cd05941  278 VDEETGEPlprgeVGEIQVRGPSVFKEYwnKPEATKEE-------------FTDD-G---WFKTGDLGVVDEDGYYWILG 340

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  372 R-RDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDETELASLKAFVVLNKESNSSDgiIFSIRNWMGGKLPPVMIP 450
Cdd:cd05941  341 RsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALS--LEELKEWAKQRLAPYKRP 418

                        490       500
                 ....*....|....*....|....
gi 22327387  451 NHFVLVEKLPLTSSGKVDYEALAR 474
Cdd:cd05941  419 RRLILVDELPRNAMGKVNKKELRK 442
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 106-469 7.26e-11

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


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 65.10  E-value: 7.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  106 YLMYTSGSTGKPKGVcgteqgllnrfLWMQELYPVVGEQRFAFKTSVGFIDHIQE------------------------- 160
Cdd:cd05924    7 YILYTGGTTGMPKGV-----------MWRQEDIFRMLMGGADFGTGEFTPSEDAHkaaaaaagtvmfpapplmhgtgswt 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  161 FLGAILSSTALVIPPFTLLKENMISIIdflEEYSISRLLAV-PSMIRAILPTLqhRGHNNKLQSCLKLVVLSGEPFPVSL 239
Cdd:cd05924   76 AFGGLLGGQTVVLPDDRFDPEEVWRTI---EKHKVTSMTIVgDAMARPLIDAL--RDAGPYDLSSLFAISSGGALLSPEV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  240 WDSLHSLLPETCFLNLYGSTEvsgdcTYFDCSELPRllkteeiGSVPIGKS--ISNCKVVLLGDEDKPYEGEICVSGLCL 317
Cdd:cd05924  151 KQGLLELVPNITLVDAFGSSE-----TGFTGSGHSA-------GSGPETGPftRANPDTVVLDDDGRVVPPGSGGVGWIA 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  318 SQGYMhssieSEGYVKLHNNSLCNHLTNDcgSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNP 397
Cdd:cd05924  219 RRGHI-----PLGYYGDEAKTAETFPEVD--GVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHP 291

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22327387  398 DIAEAVVLLSRDETELASLKAFVVLNKESNSSDGiifSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDY 469
Cdd:cd05924  292 AVYDVLVVGRPDERWGQEVVAVVQLREGAGVDLE---ELREHCRTRIARYKLPKQVVFVDEIERSPAGKADY 360
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
 352-466 1.98e-10

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 64.78  E-value: 1.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   352 YYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDETELASLKAFVVLNKESNSSDG 431
Cdd:PRK00174  484 MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDE 563

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 22327387   432 IIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGK 466
Cdd:PRK00174  564 LRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGK 598
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
 101-467 6.74e-10

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 63.07  E-value: 6.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   101 QRKFCYLMYTSGSTGKPKGVCGTEQGLLNRFLwmQELYPVvGEQRFAFKTSVGFID--HI-------------------- 158
Cdd:PLN02330  183 QTDLCALPFSSGTTGISKGVMLTHRNLVANLC--SSLFSV-GPEMIGQVVTLGLIPffHIygitgiccatlrnkgkvvvm 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   159 -----QEFLGAILS---STALVIPPFTL-LKENMIsiidfLEEYSISRLlavpsmirailptlqhrghnnKLQSclklVV 229
Cdd:PLN02330  260 srfelRTFLNALITqevSFAPIVPPIILnLVKNPI-----VEEFDLSKL---------------------KLQA----IM 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   230 LSGEPFPVSLWDSLHSLLPETCFLNLYGSTEVSgdC---TYFDCSELPRLLKTEEIGSVpigksISNCKVVLLGDED--- 303
Cdd:PLN02330  310 TAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHS--CitlTHGDPEKGHGIAKKNSVGFI-----LPNLEVKFIDPDTgrs 382

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   304 --KPYEGEICVSGLCLSQGYMHSSIESEGYVKlhnnslcnhltndcgSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNG 381
Cdd:PLN02330  383 lpKNTPGELCVRSQCVMQGYYNNKEETDRTID---------------EDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKG 447

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   382 KRMALEEIETTLELNPDIAEAVVLLSRDETELASLKAFVVLNKESNSSDGiifSIRNWMGGKLPPVMIPNHFVLVEKLPL 461
Cdd:PLN02330  448 FQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEE---DILNFVAANVAHYKKVRVVQFVDSIPK 524


                  ....*.
gi 22327387   462 TSSGKV 467
Cdd:PLN02330  525 SLSGKI 530
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 185-467 8.39e-10

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: 62.48  E-value: 8.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  185 SIIDFLEEYSISRLLAVPSMIRAILPTLQHRGHNNKLQSCLKlvvlSGEPfpvslwdslhsLLPET-------CFLNL-- 255
Cdd:cd05928  257 VILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKFPSLQHCVT----GGEP-----------LNPEVlekwkaqTGLDIye 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  256 -YGSTEVSGDCTYFdcselprllKTEEIGSVPIGKSISNCKVVLLGDED----KPYEGEICVS-----GLCLSQGYMHSS 325
Cdd:cd05928  322 gYGQTETGLICANF---------KGMKIKPGSMGKASPPYDVQIIDDNGnvlpPGTEGDIGIRvkpirPFGLFSGYVDNP 392

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  326 IESEgyvklhnnslcnhlTNDCGSqlYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVL 405
Cdd:cd05928  393 EKTA--------------ATIRGD--FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVV 456

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327387  406 LSRDETELASLKAFVVLNKESNSSD--GIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:cd05928  457 SSPDPIRGEVVKAFVVLAPQFLSHDpeQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKI 520
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
 108-475 8.89e-10

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 62.35  E-value: 8.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  108 MYTSGSTGKPKGVCGTEQGLlnrflwMQELYPVVgeQRFAFKTSVGFID-----HIQEFLGAI----LSSTALVIPPFTL 178
Cdd:cd05909  153 LFTSGSEGLPKGVVLSHKNL------LANVEQIT--AIFDPNPEDVVFGalpffHSFGLTGCLwlplLSGIKVVFHPNPL 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  179 lkeNMISIIDFLEEYSISRLLAVPSMIRAILptlqHRGHNNKLQScLKLVVLSGEPFPvslwDSLHSLLPETCFLNL--- 255
Cdd:cd05909  225 ---DYKKIPELIYDKKATILLGTPTFLRGYA----RAAHPEDFSS-LRLVVAGAEKLK----DTLRQEFQEKFGIRIleg 292

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  256 YGSTEVSgDCTYFDCSELPRllkteEIGSVpiGKSISNCKVVLLGDEDKPyEGEICVSGLCLSQG--YMhssiesEGYVK 333
Cdd:cd05909  293 YGTTECS-PVISVNTPQSPN-----KEGTV--GRPLPGMEVKIVSVETHE-EVPIGEGGLLLVRGpnVM------LGYLN 357

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  334 LHNnslcnhLTNDCGSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTL-ELNPDIAEA---------- 402
Cdd:cd05909  358 EPE------LTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILsEILPEDNEVavvsvpdgrk 431

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22327387  403 ----VVLLSRDETELASLKAFVvlnKESnssdgiifsirnwmggKLPPVMIPNHFVLVEKLPLTSSGKVDYEALARL 475
Cdd:cd05909  432 gekiVLLTTTTDTDPSSLNDIL---KNA----------------GISNLAKPSYIHQVEEIPLLGTGKPDYVTLKAL 489
PLN02430 PLN02430
long-chain-fatty-acid-CoA ligase
 105-426 9.00e-10

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178049 [Multi-domain]  Cd Length: 660  Bit Score: 62.53  E-value: 9.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   105 CYLMYTSGSTGKPKGVCGTEQGLLN-----------------------RFLWMQELYPVVGEQRFAFK-TSVGFI----- 155
Cdd:PLN02430  223 CTIMYTSGTSGDPKGVVLTHEAVATfvrgvdlfmeqfedkmthddvylSFLPLAHILDRMIEEYFFRKgASVGYYhgdln 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   156 ---DHIQEflgaiLSSTALVIPP--FTLLKENMIS-----------IIDFLEEYSISRLLAVPSMIRA--ILPTLQHRGH 217
Cdd:PLN02430  303 alrDDLME-----LKPTLLAGVPrvFERIHEGIQKalqelnprrrlIFNALYKYKLAWMNRGYSHKKAspMADFLAFRKV 377

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   218 NNKLQSCLKLVVLSGEPfpvsLWDSLHSLLPETC---FLNLYGSTEVSGDCT--YFD-------------CSELpRLLKT 279
Cdd:PLN02430  378 KAKLGGRLRLLISGGAP----LSTEIEEFLRVTScafVVQGYGLTETLGPTTlgFPDemcmlgtvgapavYNEL-RLEEV 452

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   280 EEIGSVPIGKsisnckvvllgdedkPYEGEICVSGLCLSQGYmhssiesegyvklHNNSlcnHLTNDCGSQLYYRTGDYG 359
Cdd:PLN02430  453 PEMGYDPLGE---------------PPRGEICVRGKCLFSGY-------------YKNP---ELTEEVMKDGWFHTGDIG 501

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22327387   360 RQLSSGDLIFIGRRDRTVKLN-GKRMALEEIETTLELNPDIAEAVVLlsrDETELASLKAFVVLNKES 426
Cdd:PLN02430  502 EILPNGVLKIIDRKKNLIKLSqGEYVALEYLENVYGQNPIVEDIWVY---GDSFKSMLVAVVVPNEEN 566
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
 352-475 1.44e-09

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: 61.70  E-value: 1.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  352 YYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDET--ELAslKAFVVLNKESNSS 429
Cdd:COG1021  410 FYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYlgERS--CAFVVPRGEPLTL 487

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 22327387  430 DgiifSIRNWMGGK-LPPVMIPNHFVLVEKLPLTSSGKVDYEALARL 475
Cdd:COG1021  488 A----ELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRAA 530
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
 185-467 1.72e-09

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: 61.74  E-value: 1.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  185 SIIDFLEEYSISRLLAVPSMIRAILPTLQHRGHNNKLQSClklvVLSGEPFPVSLWDSLHsllpETCFLNL---YGSTEV 261
Cdd:cd05970  267 ALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYC----TTAGEALNPEVFNTFK----EKTGIKLmegFGQTET 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  262 SGDCTYFDCSELprllkteEIGSvpIGKSISNCKVVLLGDEDKPY----EGEICVSglcLSQGYMHSSIEseGYVKLHNN 337
Cdd:cd05970  339 TLTIATFPWMEP-------KPGS--MGKPAPGYEIDLIDREGRSCeageEGEIVIR---TSKGKPVGLFG--GYYKDAEK 404

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  338 slcnhlTNDCGSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDETELASLK 417
Cdd:cd05970  405 ------TAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVK 478

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 22327387  418 AFVVLNKESNSSDGIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:cd05970  479 ATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKI 528
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
 4-404 2.22e-09

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: 61.21  E-value: 2.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    4 VVALYMPPSVEYVISVFSVLRCGEAFLPLDPSWPRERVLSLisssnislviacgLSSVESHwlVERNVCPVL-LFSMDEK 82
Cdd:cd05905   42 RVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFL-------------LGTCKVR--VALTVEACLkGLPKKLL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   83 LSVETGCS--SFVWP---------------------CKKERQRKFCYLMYTSGSTGKPKGVCGTEQGLLN--RFLWMQ-E 136
Cdd:cd05905  107 KSKTAAEIakKKGWPkildfvkipkskrsklkkwgpHPPTRDGDTAYIEYSFSSDGSLSGVAVSHSSLLAhcRALKEAcE 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  137 LY---PVVGEqrFAFKTSVGFIDHIqeFLGAILSSTALVIPPfTLLKENMISIIDFLEEYSISRLLAVPSMIRAIL---- 209
Cdd:cd05905  187 LYesrPLVTV--LDFKSGLGLWHGC--LLSVYSGHHTILIPP-ELMKTNPLLWLQTLSQYKVRDAYVKLRTLHWCLkdls 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  210 PTLQHRGHNNKLQSCLK-LVVLSGEPFPVSLWDSLHSL-----LPETCFLNLYGSTEVSGDCT-----------YFDCSE 272
Cdd:cd05905  262 STLASLKNRDVNLSSLRmCMVPCENRPRISSCDSFLKLfqtlgLSPRAVSTEFGTRVNPFICWqgtsgpepsrvYLDMRA 341

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  273 L------------PRLLKTEEIGSVPIGKSISnckVVllgDEDKPYE------GEICVSGLCLSQGYMHSSIESEGYVKL 334
Cdd:cd05905  342 LrhgvvrlderdkPNSLPLQDSGKVLPGAQVA---IV---NPETKGLckdgeiGEIWVNSPANASGYFLLDGETNDTFKV 415

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  335 HNNslcNHLTNDCGSQLYYRTGDYG--RQLSSG-------DLIF-IGRRDRTVKLNGKRMALEEIETTLEL-NPDIAEAV 403
Cdd:cd05905  416 FPS---TRLSTGITNNSYARTGLLGflRPTKCTdlnveehDLLFvVGSIDETLEVRGLRHHPSDIEATVMRvHPYRGRCA 492


                 .
gi 22327387  404 V 404
Cdd:cd05905  493 V 493
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
 105-468 5.36e-09

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: 59.24  E-value: 5.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  105 CYLMYTSGSTGKPKGVCGTEQGLLNRFL---WMQELypvvgEQRFAFKTSvGFIDHIQEFLGA----ILSSTALVIPPFt 177
Cdd:cd17636    3 VLAIYTAAFSGRPNGALLSHQALLAQALvlaVLQAI-----DEGTVFLNS-GPLFHIGTLMFTlatfHAGGTNVFVRRV- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  178 llkeNMISIIDFLEEYSISRLLAVPSMIRAILPTLQHRGHNnkLQSCLKLVVLSGEPFPVSLWDSlhsllPETCFLNLYG 257
Cdd:cd17636   76 ----DAEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYD--LSSLRSSPAAPEWNDMATVDTS-----PWGRKPGGYG 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  258 STEVSGDCTYFDcselprlLKTEEIGSVpiGKSISNCKVVLLGDEDK---PYE-GEICVSGLCLSQGYmhssiesegyvk 333
Cdd:cd17636  145 QTEVMGLATFAA-------LGGGAIGGA--GRPSPLVQVRILDEDGRevpDGEvGEIVARGPTVMAGY------------ 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  334 lhnnslCNH--LTNDCGSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDET 411
Cdd:cd17636  204 ------WNRpeVNARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPR 277

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 22327387  412 ELASLKAFVVLNK-ESNSSDGIIFSIRNwmggKLPPVMIPNHFVLVEKLPLTSSGKVD 468
Cdd:cd17636  278 WAQSVKAIVVLKPgASVTEAELIEHCRA----RIASYKKPKSVEFADALPRTAGGADD 331
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
 354-468 6.57e-09

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 59.70  E-value: 6.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   354 RTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDETELASLKAFVVLNK-ESNSSDGI 432
Cdd:PRK08008  401 HTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEgETLSEEEF 480

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 22327387   433 I-FSIRNWMGGKLPPVMipnhfVLVEKLPLTSSGKVD 468
Cdd:PRK08008  481 FaFCEQNMAKFKVPSYL-----EIRKDLPRNCSGKII 512
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
 186-475 1.03e-08

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 59.06  E-value: 1.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   186 IIDFLEEYSISRLLAVPSMIRAILPTLQHRghNNKLQScLKLVVLSGEPFPVSLWDSLHSLLPETCFLNLYGSTEVSGDC 265
Cdd:PRK06334  265 IVEMIDEAKVTFLGSTPVFFDYILKTAKKQ--ESCLPS-LRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTTECSPVI 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   266 TyFDCSELPrllKTEEIGSVPIgksiSNCKVVLLGDEDK-PYE----GEICVSGLCLSQGYMHSSiESEGYVKLhnnslc 340
Cdd:PRK06334  342 T-INTVNSP---KHESCVGMPI----RGMDVLIVSEETKvPVSsgetGLVLTRGTSLFSGYLGED-FGQGFVEL------ 406

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   341 nhltndcGSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIET------TLELNPDIAEAVVLLSRDETELA 414
Cdd:PRK06334  407 -------GGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESilmegfGQNAADHAGPLVVCGLPGEKVRL 479

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327387   415 SLkaFVVLNKESNSSDGIIFSIrnwmggKLPPVMIPNHFVLVEKLPLTSSGKVDYEALARL 475
Cdd:PRK06334  480 CL--FTTFPTSISEVNDILKNS------KTSSILKISYHHQVESIPMLGTGKPDYCSLNAL 532
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
109-476 1.40e-08

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 58.72  E-value: 1.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   109 YTSGSTGKPKGVCGTEQGLL---------------NRFLWMQELYPVVGEQRFAFKTsvgfidhiqeflgaiLSSTALVI 173
Cdd:PRK06839  156 YTSGTTGKPKGAVLTQENMFwnalnntfaidltmhDRSIVLLPLFHIGGIGLFAFPT---------------LFAGGVII 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   174 PPFTLLKENMISIIdflEEYSISRLLAVPSMIRAIL-------PTLQHrghnnklqscLKLVVLSGEPFPVSLWDSLHSL 246
Cdd:PRK06839  221 VPRKFEPTKALSMI---EKHKVTVVMGVPTIHQALIncskfetTNLQS----------VRWFYNGGAPCPEELMREFIDR 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   247 -LPetcFLNLYGSTEVSGdcTYFDCSELPRLLKteeIGSvpIGKSISNCKVVLLGDEDKPYE----GEICVSGLCLSQGY 321
Cdd:PRK06839  288 gFL---FGQGFGMTETSP--TVFMLSEEDARRK---VGS--IGKPVLFCDYELIDENKNKVEvgevGELLIRGPNVMKEY 357

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   322 MHSSIESEGYVKlhNNSLCnhltndcgsqlyyrTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAE 401
Cdd:PRK06839  358 WNRPDATEETIQ--DGWLC--------------TGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYE 421

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22327387   402 AVVLLSRDETELASLKAFVVLNKESNSSDGiifSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEALARLK 476
Cdd:PRK06839  422 VAVVGRQHVKWGEIPIAFIVKKSSSVLIEK---DVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQL 493
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
 106-467 1.51e-08

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 58.60  E-value: 1.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   106 YLMYTSGSTGKPKGVCGTEQGLLN--RFLWmQELYPVVGEQRFAFKTSVGFIDHIQEFLGAILSSTALVIPPFTLLKENM 183
Cdd:PTZ00237  258 YILYTSGTTGNSKAVVRSNGPHLVglKYYW-RSIIEKDIPTVVFSHSSIGWVSFHGFLYGSLSLGNTFVMFEGGIIKNKH 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   184 IS--IIDFLEEYSISRLLAVPSMIRAILPT--LQHRGHNNKLQSCLKLVVLSGEPFPVSLWDSLHSLLPETCfLNLYGST 259
Cdd:PTZ00237  337 IEddLWNTIEKHKVTHTLTLPKTIRYLIKTdpEATIIRSKYDLSNLKEIWCGGEVIEESIPEYIENKLKIKS-SRGYGQT 415

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   260 EvSGDCTYFDCSELPRLLKTEEIGSVPIGKSIsnckvvlLGDEDKPY-EGEIcvsGLCLSQGYMHSSIESEGYvklHNNS 338
Cdd:PTZ00237  416 E-IGITYLYCYGHINIPYNATGVPSIFIKPSI-------LSEDGKELnVNEI---GEVAFKLPMPPSFATTFY---KNDE 481

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   339 LCNHLTNDCGSqlYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDETELASLKA 418
Cdd:PTZ00237  482 KFKQLFSKFPG--YYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIG 559

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 22327387   419 FVVLN--KESNSSDGIIF--SIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:PTZ00237  560 LLVLKqdQSNQSIDLNKLknEINNIITQDIESLAVLRKIIIVNQLPKTKTGKI 612
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
 352-472 2.01e-08

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: 58.11  E-value: 2.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  352 YYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDETELASLKAFVVLNKESNSSDG 431
Cdd:cd05920  365 FYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSAAQ 444

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 22327387  432 IIFSIRNwMGgkLPPVMIPNHFVLVEKLPLTSSGKVDYEAL 472
Cdd:cd05920  445 LRRFLRE-RG--LAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
 5-467 2.05e-08

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 57.84  E-value: 2.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    5 VALYMPPSVEYVISVFSVLRCGEAFLPLDPSWprervlslisssnislviacglSSVESHWLVeRNVCPVLLFSMD-EKL 83
Cdd:cd05914   35 VALMGENRPEWGIAFFAIWTYGAIAVPILAEF----------------------TADEVHHIL-NHSEAKAIFVSDeDDV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   84 SVetgcssfvwpckkerqrkfcyLMYTSGSTGKPKGVCGTEQGLLNR------------------FLWMQELYPVVGEqr 145
Cdd:cd05914   92 AL---------------------INYTSGTTGNSKGVMLTYRNIVSNvdgvkevvllgkgdkilsILPLHHIYPLTFT-- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  146 FAFKTSVGfiDHIQeFLGAILSS----------TALVIPPFTLLKENmISIIDFLEEYSISRL---LAVPSMIRAILPTL 212
Cdd:cd05914  149 LLLPLLNG--AHVV-FLDKIPSAkiialafaqvTPTLGVPVPLVIEK-IFKMDIIPKLTLKKFkfkLAKKINNRKIRKLA 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  213 QHRGHnNKLQSCLKLVVLSGEPFPVSLWDSLHSLlpETCFLNLYGSTEvsgdCTYFDCSELPrllKTEEIGSVpiGKSIS 292
Cdd:cd05914  225 FKKVH-EAFGGNIKEFVIGGAKINPDVEEFLRTI--GFPYTIGYGMTE----TAPIISYSPP---NRIRLGSA--GKVID 292

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  293 NCKVVLLGDEDKPYEGEICVSGLCLSQGY------MHSSIESEGyvklhnnslcnhltndcgsqlYYRTGDYGRQLSSGD 366
Cdd:cd05914  293 GVEVRIDSPDPATGEGEIIVRGPNVMKGYyknpeaTAEAFDKDG---------------------WFHTGDLGKIDAEGY 351

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  367 LIFIGRRDRTVKL-NGKRMALEEIETTLELNPDIAEAVVLLSRDETELASL----KAFVVLNKESNSSDGIIFSIRNWMG 441
Cdd:cd05914  352 LYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVALAYidpdFLDVKALKQRNIIDAIKWEVRDKVN 431

                        490       500
                 ....*....|....*....|....*..
gi 22327387  442 GKLPPVMIPNHFVLV-EKLPLTSSGKV 467
Cdd:cd05914  432 QKVPNYKKISKVKIVkEEFEKTPKGKI 458
PRK09088 PRK09088
acyl-CoA synthetase; Validated
 107-467 2.42e-08

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 57.89  E-value: 2.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   107 LMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAFKTS----VGFIDHIQEFL---GAILSSTALViPPFTLL 179
Cdd:PRK09088  140 ILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPmfhiIGLITSVRPVLavgGSILVSNGFE-PKRTLG 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   180 KENMISIidfleeySISRLLAVPSMIRAILptlQHRGHNNKLQSCLKLVVLSGEPFPVS---LWdsLHSLLPETCFlnlY 256
Cdd:PRK09088  219 RLGDPAL-------GITHYFCVPQMAQAFR---AQPGFDAAALRHLTALFTGGAPHAAEdilGW--LDDGIPMVDG---F 283

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   257 GSTEVSgdcTYFDCSELPRLLKTEeIGSVPIGKSISNCKVVLLGDEDKP--YEGEICVSGLCLSQGYMHSSIESEgyvkl 334
Cdd:PRK09088  284 GMSEAG---TVFGMSVDCDVIRAK-AGAAGIPTPTVQTRVVDDQGNDCPagVPGELLLRGPNLSPGYWRRPQATA----- 354

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   335 hnnslcNHLTNDCgsqlYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDET--E 412
Cdd:PRK09088  355 ------RAFTGDG----WFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQwgE 424

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 22327387   413 LASLkafVVLNKESNSSDgiIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:PRK09088  425 VGYL---AIVPADGAPLD--LERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKL 474
PRK05691 PRK05691
peptide synthase; Validated
 350-548 3.85e-08

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 57.87  E-value: 3.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   350 QLYYRTGDYGRQlSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAE----AVVLLSRDETELASLKAFVVLN-K 424
Cdd:PRK05691  428 RTWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVRkgrvAAFAVNHQGEEGIGIAAEISRSvQ 506

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   425 ESNSSDGIIFSIRNWMGGKLPPVmiPNHFVLVE--KLPLTSSGKVDYEALA------RLKC----PTTGAQDMMQSNGTN 492
Cdd:PRK05691  507 KILPPQALIKSIRQAVAEACQEA--PSVVLLLNpgALPKTSSGKLQRSACRlrladgSLDSyalfPALQAVEAAQTAASG 584

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327387   493 SLLQNIKKAV-CDALLVKEVSDDDDFFAIGGDSLAA----AHLSHSLGIDMRLIYQFRSPS 548
Cdd:PRK05691  585 DELQARIAAIwCEQLKVEQVAADDHFFLLGGNSIAAtqvvARLRDELGIDLNLRQLFEAPT 645
PLN02654 PLN02654
acetate-CoA ligase
 106-467 6.05e-08

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 56.83  E-value: 6.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   106 YLMYTSGSTGKPKGVCGTEQGLLnrflwmqeLYPVVG-EQRFAFKTS--------VGFID-HIQEFLGAILSSTALVIPP 175
Cdd:PLN02654  279 FLLYTSGSTGKPKGVLHTTGGYM--------VYTATTfKYAFDYKPTdvywctadCGWITgHSYVTYGPMLNGATVLVFE 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   176 FTLLKENMISIIDFLEEYSISRLLAVPSMIRAILPTLQHRGHNNKLQScLKLVVLSGEPFPVSLWDSLHSLLPET-CFL- 253
Cdd:PLN02654  351 GAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKS-LRVLGSVGEPINPSAWRWFFNVVGDSrCPIs 429

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   254 NLYGSTEVSGdctyFDCSELPRLLKtEEIGSVPIgkSISNCKVVLLGDEDKPYEGEiCVSGLCLSQGYM---------HS 324
Cdd:PLN02654  430 DTWWQTETGG----FMITPLPGAWP-QKPGSATF--PFFGVQPVIVDEKGKEIEGE-CSGYLCVKKSWPgafrtlygdHE 501

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   325 SIESEgYVKLHNNslcnhltndcgsqlYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVV 404
Cdd:PLN02654  502 RYETT-YFKPFAG--------------YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAV 566

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22327387   405 LLSRDETELASLKAFVVLNKESNSSD----GIIFSIRNWMGGKLPPVMIpnHFvlVEKLPLTSSGKV 467
Cdd:PLN02654  567 VGIEHEVKGQGIYAFVTLVEGVPYSEelrkSLILTVRNQIGAFAAPDKI--HW--APGLPKTRSGKI 629
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
 307-472 6.59e-08

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


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 56.51  E-value: 6.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   307 EGEICVSGLCLSQGYMH-------SSIESEGyvklhnnslcnhltndcgsQLYYRTGDYGRQLSSGDLIFIGRRDRTVKL 379
Cdd:PRK08314  384 VGEIVVHGPQVFKGYWNrpeataeAFIEIDG-------------------KRFFRTGDLGRMDEEGYFFITDRLKRMINA 444

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   380 NGKRMALEEIETTLELNPDIAEAVVLLSRDETELASLKAFVVLNKESN---SSDGIIfsirNWMGGKLPPVMIPNHFVLV 456
Cdd:PRK08314  445 SGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARgktTEEEII----AWAREHMAAYKYPRIVEFV 520

                         170
                  ....*....|....*.
gi 22327387   457 EKLPLTSSGKVDYEAL 472
Cdd:PRK08314  521 DSLPKSGSGKILWRQL 536
PRK06178 PRK06178
acyl-CoA synthetase; Validated
 307-468 8.00e-08

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 56.20  E-value: 8.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   307 EGEICVSGLCLSQGYmhssiesegYVKLHNNSlcnHLTNDcGsqlYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMAL 386
Cdd:PRK06178  414 EGEIVVRTPSLLKGY---------WNKPEATA---EALRD-G---WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFP 477

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   387 EEIETTLELNPDIAEAVVLLSRDETELASLKAFVVLNKESNSSDGiifSIRNW----MGG-KLPPVMIpnhfvlVEKLPL 461
Cdd:PRK06178  478 SEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAA---ALQAWcrenMAVyKVPEIRI------VDALPM 548


                  ....*..
gi 22327387   462 TSSGKVD 468
Cdd:PRK06178  549 TATGKVR 555
PLN02574 PLN02574
4-coumarate--CoA ligase-like
 4-467 1.17e-07

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 55.62  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387     4 VVALYMPPSVEYVISVFSVLRCGEAFLPLDPSwprervlsLISSSNISLVIACGLSSVeshWLVERNVC-------PVLL 76
Cdd:PLN02574   94 VVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPS--------SSLGEIKKRVVDCSVGLA---FTSPENVEklsplgvPVIG 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    77 ----FSMDEKlSVETgcSSFVW-------PCKKE--RQRKFCYLMYTSGSTGKPKGVCGTEQGllnrFLWMQELYPVVGE 143
Cdd:PLN02574  163 vpenYDFDSK-RIEF--PKFYElikedfdFVPKPviKQDDVAAIMYSSGTTGASKGVVLTHRN----LIAMVELFVRFEA 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   144 QRFAFKTS------VGFIDHI---QEFLGAILS--STALVIPPFTLlkENMISIIDfleEYSISRLLAVPSMIRAILPTL 212
Cdd:PLN02574  236 SQYEYPGSdnvylaALPMFHIyglSLFVVGLLSlgSTIVVMRRFDA--SDMVKVID---RFKVTHFPVVPPILMALTKKA 310

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   213 qhRGHNNKLQSCLKLVVLSGEPFPVSLWDSLHSLLPETCFLNLYGSTEVSGDCTyfdcselpRLLKTEEI---GSVPIGK 289
Cdd:PLN02574  311 --KGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQGYGMTESTAVGT--------RGFNTEKLskySSVGLLA 380

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   290 SISNCKVVLLgdedkpyegeicVSGLCLSQG-----YMHSSIESEGYVklhNNSLCNHLTNDCGSQLyyRTGDYGRQLSS 364
Cdd:PLN02574  381 PNMQAKVVDW------------STGCLLPPGncgelWIQGPGVMKGYL---NNPKATQSTIDKDGWL--RTGDIAYFDED 443

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   365 GDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDETELASLKAFVVLNKESNSSDGiifSIRNWMGGKL 444
Cdd:PLN02574  444 GYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQE---AVINYVAKQV 520

                         490       500
                  ....*....|....*....|...
gi 22327387   445 PPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:PLN02574  521 APYKKVRKVVFVQSIPKSPAGKI 543
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
 85-423 1.34e-07

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: 55.30  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   85 VETGCSSFVWPCKKErqrKFCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQE-LYPVVGEQrfafKTSVGFID--HIQEF 161
Cdd:cd17639   74 NETECSAIFTDGKPD---DLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDrVPELLGPD----DRYLAYLPlaHIFEL 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  162 LGAILSSTALVI----PPFTLLKENMISIIDFLEEYSISRLLAVP----SMIRAILPTLQHRGHNNK------LQSCLKL 227
Cdd:cd17639  147 AAENVCLYRGGTigygSPRTLTDKSKRGCKGDLTEFKPTLMVGVPaiwdTIRKGVLAKLNPMGGLKRtlfwtaYQSKLKA 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  228 VvlsGEPFPVSLWDSL--------------------HSLLPETC-FLNL--------YGSTEVS--------GDCTY--- 267
Cdd:cd17639  227 L---KEGPGTPLLDELvfkkvraalggrlrymlsggAPLSADTQeFLNIvlcpviqgYGLTETCaggtvqdpGDLETgrv 303

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  268 ---FDCSELpRLLKTEEIGSVPigksisnckvvllgdeDKPY-EGEICVSGLCLSQGYmhssiesegyvklHNNSlcnHL 343
Cdd:cd17639  304 gppLPCCEI-KLVDWEEGGYST----------------DKPPpRGEILIRGPNVFKGY-------------YKNP---EK 350

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  344 TN-DCGSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKL-NGKRMALEEIETTLELNPDIAEAVVLLSRDETELAslkAFVV 421
Cdd:cd17639  351 TKeAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLqNGEYIALEKLESIYRSNPLVNNICVYADPDKSYPV---AIVV 427


                 ..
gi 22327387  422 LN 423
Cdd:cd17639  428 PN 429
BamB_YfgL cd10276
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ...
 706-1036 2.05e-07

Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is a non-essential component of the beta-barrel assembly machinery (Bam), a multi-subunit complex that inserts proteins with beta-barrel topology into the outer membrane. BamB has been found to interact with BamA, which in turn binds and stabilizes pre-folded beta-barrel proteins; it has been suggested that BamB participates in the stabilization.


Pssm-ID: 199834 [Multi-domain]  Cd Length: 358  Bit Score: 54.26  E-value: 2.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  706 LFIGSHSRKFSCIDAKSGSMYWETILeGRIEGSAMVVGDFSQVVIGCYKGKLYFLDFSTGSLCWKfqacgeikcqpvvdt 785
Cdd:cd10276   83 IFVGTESGYLYALDAKDGSELWRTEV-SDSQLLSPPTYADGKIYVGTGDGRLYYCNAETGKVVWN--------------- 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  786 ssqliwcgsHDHTLYALDYRSqccvyklqcggsiFASPAIDEGhsSLYVASTSGRVIAVSIKDspFHTLWLFELEAPIF- 864
Cdd:cd10276  147 ---------RTSTAPELSLRG-------------GAAPVGAYD--VVFVGDGNGTVVALNTGT--GVDIWEFSVSEPRGr 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  865 GSLC------ITPSTQNVICCLVDGQ--VIAM-SPSGTIIWRYRTGGpifaGPCMSHVLPSQVLVCCRNGCVYSLEPESG 935
Cdd:cd10276  201 TELPrmidssVTYVVVGGYLYSTSYQgyLVALdFESGQFLWSRKASG----GTSTSTDANGRVYVGDGEGSLYCLDASTG 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  936 CLVWEDNIGDP--ITASAYIDEnlhfeshellasDRLVTVCSSSGRVHVLRVRP-SILSRDSHDSKVGeitrmelqadIF 1012
Cdd:cd10276  277 DELWSQTVLLGrvLSSPAIYVG------------VYIYVTDNAEGYLYCLKDNDgLTVARVEVDYSQY----------IL 334

                        330       340
                 ....*....|....*....|....
gi 22327387 1013 SSPVMIGGRIFVGCRDDYVHCLSL 1036
Cdd:cd10276  335 QGPAVSDGWLYYGTDDGYLYALTR 358
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
 106-474 3.09e-07

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: 54.42  E-value: 3.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  106 YLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRF----AFKTSVGFID-HIQEFLGAI---LSSTALVI-PPF 176
Cdd:cd05908  110 FIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRIlswmPLTHDMGLIAfHLAPLIAGMnqyLMPTRLFIrRPI 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  177 TLLKEnmisiidfLEEYSISRLLAVPSMIRAILPTLQHRGHNNKLQSCLKLVVLSGEPFPVSLWDSLHSL-----LPETC 251
Cdd:cd05908  190 LWLKK--------ASEHKATIVSSPNFGYKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHmskygLKRNA 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  252 FLNLYGSTEVSGDCTYFDCSE-----------------LPRLLKTEEIGS--VPIGKSISNCKVVLLGDEDK----PYEG 308
Cdd:cd05908  262 ILPVYGLAEASVGASLPKAQSpfktitlgrrhvthgepEPEVDKKDSECLtfVEVGKPIDETDIRICDEDNKilpdGYIG 341

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  309 EICVSGLCLSQGYMHSSIESEgyvklhnnslcNHLTNDCgsqlYYRTGDYGRqLSSGDLIFIGRRDRTVKLNGKRMALEE 388
Cdd:cd05908  342 HIQIRGKNVTPGYYNNPEATA-----------KVFTDDG----WLKTGDLGF-IRNGRLVITGREKDIIFVNGQNVYPHD 405

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  389 IE-TTLELNPDIAEAVVLLSRDETELASLKAFVVLNKESNSSDGI-----IFSIRNWMGGKLPPVMIPnhfvlVEKLPLT 462
Cdd:cd05908  406 IErIAEELEGVELGRVVACGVNNSNTRNEEIFCFIEHRKSEDDFYplgkkIKKHLNKRGGWQINEVLP-----IRRIPKT 480

                        410
                 ....*....|..
gi 22327387  463 SSGKVDYEALAR 474
Cdd:cd05908  481 TSGKVKRYELAQ 492
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
 95-472 3.24e-07

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


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 54.27  E-value: 3.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    95 PCKKERQrkFCYLMYTSGSTGKPKGVCGTEQGLL-NRFLWMQELYPVVGEQRFAFKTSVGFidHIQEFLG----AILSST 169
Cdd:PRK06710  201 PCDPEND--LALLQYTGGTTGFPKGVMLTHKNLVsNTLMGVQWLYNCKEGEEVVLGVLPFF--HVYGMTAvmnlSIMQGY 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   170 ALVIPPftllKENMISIIDFLEEYSISRLLAVPSMIRAIL--PTLQHRGhnnklQSCLKLVVLSGEPFPVSLWDSLHSLL 247
Cdd:PRK06710  277 KMVLIP----KFDMKMVFEAIKKHKVTLFPGAPTIYIALLnsPLLKEYD-----ISSIRACISGSAPLPVEVQEKFETVT 347

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   248 PETcFLNLYGSTEvSGDCTYFDCselprLLKTEEIGSVPIGKSISNCKVVLL--GDEDKPYE-GEICVSGLCLSQGYMHS 324
Cdd:PRK06710  348 GGK-LVEGYGLTE-SSPVTHSNF-----LWEKRVPGSIGVPWPDTEAMIMSLetGEALPPGEiGEIVVKGPQIMKGYWNK 420

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   325 SIESEGYVKlhnnslcnhltndcgsQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVV 404
Cdd:PRK06710  421 PEETAAVLQ----------------DGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVT 484

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22327387   405 LLSRDETELASLKAFVVLNKESNSSDGiifSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEAL 472
Cdd:PRK06710  485 IGVPDPYRGETVKAFVVLKEGTECSEE---ELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
 105-404 3.43e-07

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: 54.14  E-value: 3.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  105 CYLMYTSGSTGKPKGVCGTEQGLLN---RFLWMQELYPVVGEQR--------------------FAFKTSVGF------- 154
Cdd:cd05927  117 ATICYTSGTTGNPKGVMLTHGNIVSnvaGVFKILEILNKINPTDvyisylplahifervvealfLYHGAKIGFysgdirl 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  155 -IDHIQEflgaiLSSTALVIPP-----------FTLLKENMI--SIIDFLEEYSISRLLavpsmirailptlqhRGHN-- 218
Cdd:cd05927  197 lLDDIKA-----LKPTVFPGVPrvlnriydkifNKVQAKGPLkrKLFNFALNYKLAELR---------------SGVVra 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  219 ---------NKLQSCL----KLVVLSGEPFPVSLWDSLHSLLpETCFLNLYGSTEVSGDCTY---FDCSelprllkteeI 282
Cdd:cd05927  257 spfwdklvfNKIKQALggnvRLMLTGSAPLSPEVLEFLRVAL-GCPVLEGYGQTECTAGATLtlpGDTS----------V 325

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  283 GSVpiGKSISNCKVVL--------LGDEDKPyEGEICVSGLCLSQGYMH------SSIESEGYvkLHnnslcnhltndcg 348
Cdd:cd05927  326 GHV--GGPLPCAEVKLvdvpemnyDAKDPNP-RGEVCIRGPNVFSGYYKdpektaEALDEDGW--LH------------- 387

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 22327387  349 sqlyyrTGDYGRQLSSGDLIFIGRRDRTVKL-NGKRMALEEIETTLELNPDIAEAVV 404
Cdd:cd05927  388 ------TGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFVAQIFV 438
PRK07470 PRK07470
acyl-CoA synthetase; Validated
 105-467 4.36e-07

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 53.89  E-value: 4.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   105 CYLMYTSGSTGKPKGVCGTEQGL----LNRflwMQELYPVVGEQRFAFKT---SVGFIDH--IQEFLGA---ILSSTALV 172
Cdd:PRK07470  166 CWFFFTSGTTGRPKAAVLTHGQMafviTNH---LADLMPGTTEQDASLVVaplSHGAGIHqlCQVARGAatvLLPSERFD 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   173 IPPFTLLkenmisiidfLEEYSISRLLAVPSMIRAIL--PTLQHRGHnnklqSCLKLVVLSGEP-FPVSLWDSLHSLLPe 249
Cdd:PRK07470  243 PAEVWAL----------VERHRVTNLFTVPTILKMLVehPAVDRYDH-----SSLRYVIYAGAPmYRADQKRALAKLGK- 306

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   250 tCFLNLYGSTEVSGDCTYfdcseLPRLLKTEEIG-SVPIGK----------SISNCKvvllGDEDKPYE-GEICVSGLCL 317
Cdd:PRK07470  307 -VLVQYFGLGEVTGNITV-----LPPALHDAEDGpDARIGTcgfertgmevQIQDDE----GRELPPGEtGEICVIGPAV 376

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   318 SQGYmhssiesegyvklHNNSLCNHLTNDCGsqlYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNP 397
Cdd:PRK07470  377 FAGY-------------YNNPEANAKAFRDG---WFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHP 440

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   398 DIAEAVVLLSRDETELASLKAFVVLnKESNSSDGIifSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:PRK07470  441 AVSEVAVLGVPDPVWGEVGVAVCVA-RDGAPVDEA--ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKI 507
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
92-468 5.10e-07

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 53.63  E-value: 5.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    92 FVWPCKKERQRkfCYLMYTSGSTGKPKGVCGTeqgllNRFLWMQELyPVVGEQRFAFKTSVGF-----IDHIQEF---LG 163
Cdd:PRK05620  173 YDWPELDETTA--AAICYSTGTTGAPKGVVYS-----HRSLYLQSL-SLRTTDSLAVTHGESFlccvpIYHVLSWgvpLA 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   164 AILSSTALVIPPFTLLKENMISIIdfleEYSISRLL-AVPSM-IRAILPTLQHRGHNNKLQSclklVVLSGEPFP---VS 238
Cdd:PRK05620  245 AFMSGTPLVFPGPDLSAPTLAKII----ATAMPRVAhGVPTLwIQLMVHYLKNPPERMSLQE----IYVGGSAVPpilIK 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   239 LW------DSLHSllpetcflnlYGSTEVSGDCTyfdCSELP-------RLLKTEEIGSVPIG---KSISNCKVVLLGDE 302
Cdd:PRK05620  317 AWeerygvDVVHV----------WGMTETSPVGT---VARPPsgvsgeaRWAYRVSQGRFPASleyRIVNDGQVMESTDR 383

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   303 DkpyEGEICVSGLCLSQGYMHSSIESEGYVKlhnNSLCNHLTNDCGSQL----YYRTGDYGRQLSSGDLIFIGRRDRTVK 378
Cdd:PRK05620  384 N---EGEIQVRGNWVTASYYHSPTEEGGGAA---STFRGEDVEDANDRFtadgWLRTGDVGSVTRDGFLTIHDRARDVIR 457

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   379 LNGKRMALEEIETTLELNPDIAEAVVLLSRDETELASLKAFVVLNKESNSSDGIIFSIRNWMGGKLPPVMIPNHFVLVEK 458
Cdd:PRK05620  458 SGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDE 537

                         410
                  ....*....|
gi 22327387   459 LPLTSSGKVD 468
Cdd:PRK05620  538 IDKTSVGKFD 547
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 4-477 5.48e-07

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: 53.40  E-value: 5.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    4 VVALYmPPSVEYVISVFSVLRCG----EAFLPLDPSWpRERVLSlisssnislVIA-CG----LSSVESHWLVERNVCPV 74
Cdd:cd05931   51 VLLLA-PPGLDFVAAFLGCLYAGaiavPLPPPTPGRH-AERLAA---------ILAdAGprvvLTTAAALAAVRAFAASR 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   75 LLFSMDEKLSV---ETGCSSfVWPCKKERQRKFCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFAfktS 151
Cdd:cd05931  120 PAAGTPRLLVVdllPDTSAA-DWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVV---S 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  152 ----------VGFIdhiqefLGAILSSTALV-IPPFTLLKENMIsiidFLEEysISR----LLAVPSMirAiLPTLQHRG 216
Cdd:cd05931  196 wlplyhdmglIGGL------LTPLYSGGPSVlMSPAAFLRRPLR----WLRL--ISRyratISAAPNF--A-YDLCVRRV 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  217 HNNKLQ----SCLKLVVLSGEpfPVSlWDSLHSL--------LPETCFLNLYGSTE----VSGD-------CTYFDCSEL 273
Cdd:cd05931  261 RDEDLEgldlSSWRVALNGAE--PVR-PATLRRFaeafapfgFRPEAFRPSYGLAEatlfVSGGppgtgpvVLRVDRDAL 337

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  274 P---RLLKTEEIGSVPI---GKSISNCKVVLLGDEDKPY-----EGEICVSGLCLSQGYMHSSIESEGYvklhnnslcNH 342
Cdd:cd05931  338 AgraVAVAADDPAARELvscGRPLPDQEVRIVDPETGRElpdgeVGEIWVRGPSVASGYWGRPEATAET---------FG 408

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  343 LTNDCGSQLYYRTGDYGRqLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLE-----LNPDIAEAVVLLSRDETELaslk 417
Cdd:cd05931  409 ALAATDEGGWLRTGDLGF-LHDGELYITGRLKDLIIVRGRNHYPQDIEATAEeahpaLRPGCVAAFSVPDDGEERL---- 483

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22327387  418 afVVLNKESnssdgiifsiRNWMGGKLPPVM------------IPNH-FVLVE--KLPLTSSGKVdyealARLKC 477
Cdd:cd05931  484 --VVVAEVE----------RGADPADLAAIAaairaavarehgVAPAdVVLVRpgSIPRTSSGKI-----QRRAC 541
BamB_YfgL cd10276
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ...
 724-1034 7.53e-07

Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is a non-essential component of the beta-barrel assembly machinery (Bam), a multi-subunit complex that inserts proteins with beta-barrel topology into the outer membrane. BamB has been found to interact with BamA, which in turn binds and stabilizes pre-folded beta-barrel proteins; it has been suggested that BamB participates in the stabilization.


Pssm-ID: 199834 [Multi-domain]  Cd Length: 358  Bit Score: 52.72  E-value: 7.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  724 SMYWETIL----EGRIEGSAMVVGDFsqVVIGCYKGKLYFLDFSTGSLCWKfqacgeikcqpvvdtssqliwcgshdhtl 799
Cdd:cd10276   15 EVLWSKSVgnggMAGIDLTPVVAGDM--VYAADANGQVSAFNATTGKIIWE----------------------------- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  800 yaldyrsqccvYKLQCGGSIFASPAIDEGHssLYVASTSGRVIAVSIKDSpfHTLW-----LFELEAPIF---GSLCITP 871
Cdd:cd10276   64 -----------TSLSGKGFLGGTPAVGNGK--IFVGTESGYLYALDAKDG--SELWrtevsDSQLLSPPTyadGKIYVGT 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  872 STQNVICCLVDgqviamspSGTIIWRYRTGGPIFAGPCMSHVL--PSQVLVCCRNGCVYSLEPESGCLVWEDNIGDPITA 949
Cdd:cd10276  129 GDGRLYYCNAE--------TGKVVWNRTSTAPELSLRGGAAPVgaYDVVFVGDGNGTVVALNTGTGVDIWEFSVSEPRGR 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  950 SA---YIDenlhfeshellaSDRLVTVcsSSGRVHVLRVRPSILSRDSHDSKVgeITRMELQAdIFSSPVMIGGRIFVGC 1026
Cdd:cd10276  201 TElprMID------------SSVTYVV--VGGYLYSTSYQGYLVALDFESGQF--LWSRKASG-GTSTSTDANGRVYVGD 263


                 ....*...
gi 22327387 1027 RDDYVHCL 1034
Cdd:cd10276  264 GEGSLYCL 271
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
352-475 1.14e-06

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 52.58  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   352 YYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDETELASLKAFVVLNKESN-SSD 430
Cdd:PRK05852  409 WLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPpTAE 488

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 22327387   431 GIIFSIRNwmggKLPPVMIPNHFVLVEKLPLTSSGKVDYEALARL 475
Cdd:PRK05852  489 ELVQFCRE----RLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQ 529
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
107-467 1.38e-06

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 52.06  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   107 LMYTSGSTGKPKGVCGTEQGLLnrflwmqelypvVGEQRFAFKTSVGFIDHIqeFLGAILS-STAL---VIPPF-----T 177
Cdd:PRK06087  192 VLFTSGTEGLPKGVMLTHNNIL------------ASERAYCARLNLTWQDVF--MMPAPLGhATGFlhgVTAPFligarS 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   178 LLKE--NMISIIDFLEEYSISRLLAVPSMIRAILPTLQHRGHNnklQSCLKLVVLSGEPFPvslwdslhSLLPETC---- 251
Cdd:PRK06087  258 VLLDifTPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQPAD---LSALRFFLCGGTTIP--------KKVARECqqrg 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   252 --FLNLYGSTEVS-------GDCtyfdcseLPRLLKTEEIG--SVPIGKSISNCKVVLLGDEdkpyeGEICVSGLCLSQG 320
Cdd:PRK06087  327 ikLLSVYGSTESSphavvnlDDP-------LSRFMHTDGYAaaGVEIKVVDEARKTLPPGCE-----GEEASRGPNVFMG 394

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   321 YmhssiesegyvkLHNNSLCNHLTNDCGsqlYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIA 400
Cdd:PRK06087  395 Y------------LDEPELTARALDEEG---WYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIH 459

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   401 EAVVLLSRDETELASLKAFVVLNKESNS---SDGIIFSIRNwmggKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:PRK06087  460 DACVVAMPDERLGERSCAYVVLKAPHHSltlEEVVAFFSRK----RVAKYKYPEHIVVIDKLPRTASGKI 525
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
 106-472 1.80e-06

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: 51.61  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  106 YLMYTSGSTGKPKGVcgtEQGLLNRflwmqelyPVVGEQRFAFKTSVGFIDHIQEFLGAILSSTALVIPPFTLLKENMIS 185
Cdd:cd05929  129 KMLYSGGTTGRPKGI---KRGLPGG--------PPDNDTLMAAALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTL 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  186 II----------DFLEEYSISRLLAVPSMIRAILPTLQHRGHNNKLQScLKLVVLSGEPFPVSLWDSLHSLLPETCFlNL 255
Cdd:cd05929  198 VLmekfdpeeflRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSS-LKRVIHAAAPCPPWVKEQWIDWGGPIIW-EY 275

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  256 YGSTEVSGDCtyfdcselprLLKTEEI----GSVpiGKSISNcKVVLLGDEDKPY----EGEIcvsglclsqgYMHSSIE 327
Cdd:cd05929  276 YGGTEGQGLT----------IINGEEWlthpGSV--GRAVLG-KVHILDEDGNEVppgeIGEV----------YFANGPG 332

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  328 SEgyvkLHNNSLCNHLTNDCGSqlyYRT-GDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLL 406
Cdd:cd05929  333 FE----YTNDPEKTAAARNEGG---WSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVG 405

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22327387  407 SRDETELASLKAFVVLNKESNSSDGIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEAL 472
Cdd:cd05929  406 VPDEELGQRVHAVVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
253-425 1.84e-06

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 52.02  E-value: 1.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  253 LNLYGSTEVSGDCTYfdcselpRLLKTEEIGSVpiGKSISNCKVVLlgDEDkpyeGEICVSGLCLSQGYMH------SSI 326
Cdd:COG1022  375 LEGYGLTETSPVITV-------NRPGDNRIGTV--GPPLPGVEVKI--AED----GEILVRGPNVMKGYYKnpeataEAF 439

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  327 ESEGYvklhnnslcnhltndcgsqlyYRTGDYGRQLSSGDLIFIGRRDRTVKL-NGKRMALEEIETTLELNPDIAEAVVL 405
Cdd:COG1022  440 DADGW---------------------LHTGDIGELDEDGFLRITGRKKDLIVTsGGKNVAPQPIENALKASPLIEQAVVV 498

                        170       180
                 ....*....|....*....|....*.
gi 22327387  406 ------LSrdetelaslkAFVVLNKE 425
Cdd:COG1022  499 gdgrpfLA----------ALIVPDFE 514
PRK08308 PRK08308
acyl-CoA synthetase; Validated
 354-467 2.11e-06

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 51.19  E-value: 2.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   354 RTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDETELASLKAFVvlnkesnSSDGII 433
Cdd:PRK08308  294 FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKV-------ISHEEI 366

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 22327387   434 --FSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:PRK08308  367 dpVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKV 402
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
 107-464 2.15e-06

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: 51.59  E-value: 2.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  107 LMYTSGSTGKPKGVCGTEQGLLNRFLWMQELYPVVGEQRFafkTSVGFIDHIQEFLGAILSSTALVIPPFTllkeNMISI 186
Cdd:cd17640   93 IIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRF---LSILPIWHSYERSAEYFIFACGCSQAYT----SIRTL 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  187 IDFLEEYSISRLLAVPSMIRAILPTLQHRGHNN-KLQSCLKLVVLSGE--PFPVSLWDSLHSLLpETCF-------LNLY 256
Cdd:cd17640  166 KDDLKRVKPHYIVSVPRLWESLYSGIQKQVSKSsPIKQFLFLFFLSGGifKFGISGGGALPPHV-DTFFeaigievLNGY 244

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  257 GSTEVSGDCTYfdcselpRLLKTEEIGSVpiGKSI--SNCKVV-LLGDEDKPYE--GEICVSGLCLSQGYMHSSIESegy 331
Cdd:cd17640  245 GLTETSPVVSA-------RRLKCNVRGSV--GRPLpgTEIKIVdPEGNVVLPPGekGIVWVRGPQVMKGYYKNPEAT--- 312

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  332 vklhnnslCNHLTNDcGsqlYYRTGDYGRQLSSGDLIFIGR-RDRTVKLNGKRMALEEIETTLELNPDIaEAVVLLSRDE 410
Cdd:cd17640  313 --------SKVLDSD-G---WFNTGDLGWLTCGGELVLTGRaKDTIVLSNGENVEPQPIEEALMRSPFI-EQIMVVGQDQ 379

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327387  411 TELAslkAFVVLNKE------SNSSDGIIFSIRNWMGGKLPPVMIPNHF-VLVEKLPLTSS 464
Cdd:cd17640  380 KRLG---ALIVPNFEelekwaKESGVKLANDRSQLLASKKVLKLYKNEIkDEISNRPGFKS 437
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 498-548 5.68e-06

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: 44.86  E-value: 5.68e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 22327387    498 IKKAVCDALLV--KEVSDDDDFFAIGGDSLAAAHLSHSL------GIDMRLIYQFRSPS 548
Cdd:pfam00550    3 LRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLeeefgvEIPPSDLFEHPTLA 61
PQQ_2 pfam13360
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
 839-1024 5.70e-06

PQQ-like domain; This domain contains several repeats of the PQQ repeat.


Pssm-ID: 433144 [Multi-domain]  Cd Length: 233  Bit Score: 48.94  E-value: 5.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    839 GRVIAVSIKDSpfHTLWLFELEAPifgSLCITPSTQNVICCLVD-GQVIAMSPS-GTIIWRYRTGGPIFAGPcmsHVLPS 916
Cdd:pfam13360    3 GVVTALDAATG--AELWRVDLETG---LGGGVAVDGGRLFVATGgGQLVALDAAtGKLLWRQTLSGEVLGAP---LVAGG 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    917 QVLVCCRNGCVYSLEPESGCLVWE-DNIGDPITasayidenlHFESHELLASDRLVTVCSSSGRVHVLRVRP------SI 989
Cdd:pfam13360   75 RVFVVAGDGSLIALDAADGRRLWSyQRSGEPLA---------LRSSGSPAVVGDTVVAGFSSGKLVALDPATgkvrweAP 145

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 22327387    990 LSRDShdskvgEITRMELQADIFSSPVMIGGRIFV 1024
Cdd:pfam13360  146 LAAPR------GTNELERLVDITGTPVVAGGRVFA 174
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
 352-466 7.61e-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: 49.96  E-value: 7.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  352 YYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDETELASLKAFVVLNKESNSSDG 431
Cdd:cd05943  485 VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDE 564

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 22327387  432 IIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGK 466
Cdd:cd05943  565 LRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGK 599
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
104-479 8.06e-06

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 50.03  E-value: 8.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   104 FCYLMYTSGSTGKPKGVCGTE-------QGLLNRFLWM--QELYPVVGEQRFAFK--TSVGFidhiqeflgAILSSTALV 172
Cdd:PRK06060  147 LAYATYTSGTTGPPKAAIHRHadpltfvDAMCRKALRLtpEDTGLCSARMYFAYGlgNSVWF---------PLATGGSAV 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   173 IPPFTLLKENMISIIDFLEEysiSRLLAVPSMIRAILPTLQhrghNNKLQScLKLVVLSGEPFPVSLWDSLHSLLPETCF 252
Cdd:PRK06060  218 INSAPVTPEAAAILSARFGP---SVLYGVPNFFARVIDSCS----PDSFRS-LRCVVSAGEALELGLAERLMEFFGGIPI 289

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   253 LNLYGSTEVsgdctyfdcselprllkteeiGSVPIGKSISNCKVVLLGDEDKPY----------------EGEICVSGLC 316
Cdd:PRK06060  290 LDGIGSTEV---------------------GQTFVSNRVDEWRLGTLGRVLPPYeirvvapdgttagpgvEGDLWVRGPA 348

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   317 LSQGYMH---SSIESEGYVKlhnnslcnhltndcgsqlyyrTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTL 393
Cdd:PRK06060  349 IAKGYWNrpdSPVANEGWLD---------------------TRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLI 407

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   394 ELNPDIAEAVVLLSRDETELASLKAFVVLNKESNSSDGIIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEALa 473
Cdd:PRK06060  408 IEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGAL- 486


                  ....*.
gi 22327387   474 RLKCPT 479
Cdd:PRK06060  487 RKQSPT 492
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
 352-467 8.72e-06

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 49.51  E-value: 8.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   352 YYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDETELASLKAFVVLNKESNSSDG 431
Cdd:PRK04319  433 WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEE 512

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 22327387   432 IIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:PRK04319  513 LKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKI 548
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 107-475 1.05e-05

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 49.92  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   107 LMYTSGSTGKPKGVCGTEQGLLnrflwmqelypvvgeqrfafktsvGFIDHIQEFLGA-----ILSStalvIPPF----- 176
Cdd:PRK08633  787 IIFSSGSEGEPKGVMLSHHNIL------------------------SNIEQISDVFNLrnddvILSS----LPFFhsfgl 838

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   177 --TL---LKENMIS-----------IIDFLEEYSISRLLAVPSMIRAILPTlqHRGHNNKLQScLKLVVLSGEPFPVSLW 240
Cdd:PRK08633  839 tvTLwlpLLEGIKVvyhpdptdalgIAKLVAKHRATILLGTPTFLRLYLRN--KKLHPLMFAS-LRLVVAGAEKLKPEVA 915

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   241 DSLhsllpETCF----LNLYGSTE----VSGDCTYFDCSELPRLLKTEEiGSV--PI-GKSIsncKVV--LLGDEDKPYE 307
Cdd:PRK08633  916 DAF-----EEKFgiriLEGYGATEtspvASVNLPDVLAADFKRQTGSKE-GSVgmPLpGVAV---RIVdpETFEELPPGE 986

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   308 -GEICVSGLCLSQGYMHSSIESEGYVKlhnnslcnhltnDCGSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMAL 386
Cdd:PRK08633  987 dGLILIGGPQVMKGYLGDPEKTAEVIK------------DIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPL 1054

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   387 ----EEIETTL-ELNPDIA----------EAVVLL-SRDETELASLKAFVvlnKESNssdgiifsirnwmggkLPPVMIP 450
Cdd:PRK08633 1055 gaveEELAKALgGEEVVFAvtavpdekkgEKLVVLhTCGAEDVEELKRAI---KESG----------------LPNLWKP 1115

                         410       420
                  ....*....|....*....|....*
gi 22327387   451 NHFVLVEKLPLTSSGKVDYEALARL 475
Cdd:PRK08633 1116 SRYFKVEALPLLGSGKLDLKGLKEL 1140
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
5-467 1.05e-05

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


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 49.28  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387     5 VALYMPPSVEYVISVFSVLRCGEAFLPLDPSW-PRERVLSLISSSNISLVIACGLSSVESHWLVERNVCPVLLFSMDEKL 83
Cdd:PRK08974   77 VALMMPNLLQYPIALFGILRAGMIVVNVNPLYtPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKTPVKHVILTRMGDQL 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387    84 SVETG---------------------CSSFVWPCKKERQRKF----------CYLMYTSGSTGKPKGVCGTEQGLLNRFL 132
Cdd:PRK08974  157 STAKGtlvnfvvkyikrlvpkyhlpdAISFRSALHKGRRMQYvkpelvpedlAFLQYTGGTTGVAKGAMLTHRNMLANLE 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   133 WMQELY-PVVGE-QRFA---------FKTSVG---FIDhiqeflgaiLSSTALVI------PPFtlLKEnmisiidfLEE 192
Cdd:PRK08974  237 QAKAAYgPLLHPgKELVvtalplyhiFALTVNcllFIE---------LGGQNLLItnprdiPGF--VKE--------LKK 297

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   193 YSISRLLAVPSMIRAILptlqhrgHNNKLQ----SCLKLVVLSGEPFPVSLWDSLHSLlPETCFLNLYGSTEvsgdctyf 268
Cdd:PRK08974  298 YPFTAITGVNTLFNALL-------NNEEFQeldfSSLKLSVGGGMAVQQAVAERWVKL-TGQYLLEGYGLTE-------- 361

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   269 dCSEL----PRLLKtEEIGSvpIGKSISNCKVVLLGDEDKPYE----GEICVSGLCLSQGYMHSSIESEGYVKlhnnslc 340
Cdd:PRK08974  362 -CSPLvsvnPYDLD-YYSGS--IGLPVPSTEIKLVDDDGNEVPpgepGELWVKGPQVMLGYWQRPEATDEVIK------- 430

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   341 nhltndcgsQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDETELASLKAFV 420
Cdd:PRK08974  431 ---------DGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFV 501

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 22327387   421 VLNKESNSSDGIIFSIRNWMGGklppVMIPNHFVLVEKLPLTSSGKV 467
Cdd:PRK08974  502 VKKDPSLTEEELITHCRRHLTG----YKVPKLVEFRDELPKSNVGKI 544
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
 142-475 1.42e-05

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 48.84  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   142 GEQRFAFKT------SV-GFIDHIQ-------------------EFLGAILSSTALVIPPFTLLKENMISIIdFLEEYSI 195
Cdd:PRK07445  133 GQIRFAIHTwetltaSVqGFQRYFQlqqvnsfcvlplyhvsglmQFMRSFLTGGKLVILPYKRLKSGQELPP-NPSDFFL 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   196 SrllAVPSMIRAILPtlqhrGHNNKLQScLKLVVLSGEPfpvsLWDSLhslLPETCFLNL-----YGSTEVSGD-CTyfd 269
Cdd:PRK07445  212 S---LVPTQLQRLLQ-----LRPQWLAQ-FRTILLGGAP----AWPSL---LEQARQLQLrlaptYGMTETASQiAT--- 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   270 cselprlLKTEEI--GSVPIGKSISNCKVVLLGDEDkpyeGEICVSGLCLSQGYmhssiesegYVKLHNnslcnhltndc 347
Cdd:PRK07445  273 -------LKPDDFlaGNNSSGQVLPHAQITIPANQT----GNITIQAQSLALGY---------YPQILD----------- 321

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   348 gSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDETELASLKAFVVLNKESN 427
Cdd:PRK07445  322 -SQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSI 400

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 22327387   428 SSDgiifSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEALARL 475
Cdd:PRK07445  401 SLE----ELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQI 444
BamB_YfgL cd10276
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ...
 680-862 1.59e-05

Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is a non-essential component of the beta-barrel assembly machinery (Bam), a multi-subunit complex that inserts proteins with beta-barrel topology into the outer membrane. BamB has been found to interact with BamA, which in turn binds and stabilizes pre-folded beta-barrel proteins; it has been suggested that BamB participates in the stabilization.


Pssm-ID: 199834 [Multi-domain]  Cd Length: 358  Bit Score: 48.48  E-value: 1.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  680 QEIWKVHMESCVDASPLVVlkdSKTYLFIGSHSRKFSCIDAKSGSMYWE---TILEGRIEGSAMVVGDFSQVVIGCYKGK 756
Cdd:cd10276  101 SELWRTEVSDSQLLSPPTY---ADGKIYVGTGDGRLYYCNAETGKVVWNrtsTAPELSLRGGAAPVGAYDVVFVGDGNGT 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  757 LYFLDFSTGSLCWKFQ---------ACGEIKCQ--PVVDTSsqliwcgshdhTLYALDYRSQCCVYKLQCG--------G 817
Cdd:cd10276  178 VVALNTGTGVDIWEFSvseprgrteLPRMIDSSvtYVVVGG-----------YLYSTSYQGYLVALDFESGqflwsrkaS 246

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 22327387  818 SIFASPAIDEGhsSLYVASTSGRVIAVSIKDSpfHTLWLFELEAP 862
Cdd:cd10276  247 GGTSTSTDANG--RVYVGDGEGSLYCLDASTG--DELWSQTVLLG 287
prpE PRK10524
propionyl-CoA synthetase; Provisional
 349-467 1.76e-05

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 48.79  E-value: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   349 SQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDEtelasLK-----AFVVLN 423
Cdd:PRK10524  471 GRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDA-----LKgqvavAFVVPK 545

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 22327387   424 KESNSSDGIIF-----SIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:PRK10524  546 DSDSLADREARlalekEIMALVDSQLGAVARPARVWFVSALPKTRSGKL 594
PRK06164 PRK06164
acyl-CoA synthetase; Validated
 352-465 3.32e-05

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 47.82  E-value: 3.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   352 YYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEA-VVLLSRD-ETELAslkAFVVLnKESNSS 429
Cdd:PRK06164  407 YFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAqVVGATRDgKTVPV---AFVIP-TDGASP 482

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 22327387   430 DGIifSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSG 465
Cdd:PRK06164  483 DEA--GLMAACREALAGFKVPARVQVVEAFPVTESA 516
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 350-545 4.48e-05

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 46.67  E-value: 4.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  350 QLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDETELASLK----AFVVLnke 425
Cdd:COG3433   76 AQPGRQADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLllivGAVAA--- 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  426 snsSDGIIFSIRNWMGGKLPPVMIPnhFVLVEKLPLTSSGKVDYEALARLKCPTTGAQ---DMMQSNG-TNSLLQNIKKA 501
Cdd:COG3433  153 ---LDGLAAAAALAALDKVPPDVVA--ASAVVALDALLLLALKVVARAAPALAAAEALlaaASPAPALeTALTEEELRAD 227

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 22327387  502 VCDALLVK--EVSDDDDFFAIGGDSLAAahlshslgidMRLIYQFR 545
Cdd:COG3433  228 VAELLGVDpeEIDPDDNLFDLGLDSIRL----------MQLVERWR 263
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
352-472 4.51e-05

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 47.29  E-value: 4.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   352 YYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDEteLASLK--AFVVLNKESNSS 429
Cdd:PRK10946  410 FYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDE--LMGEKscAFLVVKEPLKAV 487

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 22327387   430 DgiifsIRNWMGG------KLPpvmipNHFVLVEKLPLTSSGKVDYEAL 472
Cdd:PRK10946  488 Q-----LRRFLREqgiaefKLP-----DRVECVDSLPLTAVGKVDKKQL 526
PRK11138 PRK11138
outer membrane biogenesis protein BamB; Provisional
 719-1038 6.42e-05

outer membrane biogenesis protein BamB; Provisional


Pssm-ID: 236857 [Multi-domain]  Cd Length: 394  Bit Score: 46.46  E-value: 6.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   719 DAKSGSMYWETILEGRI-----EGSAMVVG----DFSQVVIGCYKGKLYFLDFSTGSLCWKFQACGEIKCQPVVDTSSQL 789
Cdd:PRK11138   85 DADTGKEIWSVDLSEKDgwfskNKSALLSGgvtvAGGKVYIGSEKGQVYALNAEDGEVAWQTKVAGEALSRPVVSDGLVL 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   790 IwcgshdHT----LYALDYRS--QCCVYKLQC------GGSifaSPAIDEGhsSLYVASTSGRVIAVsIKDSPfHTLWlf 857
Cdd:PRK11138  165 V------HTsngmLQALNESDgaVKWTVNLDVpsltlrGES---APATAFG--GAIVGGDNGRVSAV-LMEQG-QLIW-- 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   858 elEAPIFgslciTPSTQNVICCLVDgqvIAMSPsgtIIwryrTGGPIFAgpcMSHvlpsqvlvccrNGCVYSLEPESGCL 937
Cdd:PRK11138  230 --QQRIS-----QPTGATEIDRLVD---VDTTP---VV----VGGVVYA---LAY-----------NGNLVALDLRSGQI 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   938 VWEDNIG---DPITASAYI---DENlhfeshellasDRLVTVCSSSGrvhvlrvrpSILSRDShdskvgeitrmELQADI 1011
Cdd:PRK11138  279 VWKREYGsvnDFAVDGGRIylvDQN-----------DRVYALDTRGG---------VELWSQS-----------DLLHRL 327

                         330       340
                  ....*....|....*....|....*..
gi 22327387  1012 FSSPVMIGGRIFVGCRDDYVHCLSLES 1038
Cdd:PRK11138  328 LTAPVLYNGYLVVGDSEGYLHWINRED 354
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
 352-467 6.96e-05

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: 46.52  E-value: 6.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  352 YYRTGDYGRQLSSGdliFIGRRDRTVKL---NGKRMALEEIETTLELNPDIAEAVVLLSRDETELASLKAFVVLNK-ESN 427
Cdd:cd12118  368 WFHSGDLAVIHPDG---YIEIKDRSKDIiisGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEgAKV 444

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 22327387  428 SSDGIIFSIRNwmggKLPPVMIPNHFVLVEkLPLTSSGKV 467
Cdd:cd12118  445 TEEEIIAFCRE----HLAGFMVPKTVVFGE-LPKTSTGKI 479
PRK08316 PRK08316
acyl-CoA synthetase; Validated
 107-467 9.44e-05

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 46.08  E-value: 9.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   107 LMYTSGSTGKPKGVCGTEQGLlnrflwmqelypvvgeqrfafktsvgfidhIQEFLGAI----LSST------------- 169
Cdd:PRK08316  176 ILYTSGTESLPKGAMLTHRAL------------------------------IAEYVSCIvagdMSADdiplhalplyhca 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   170 ---ALVIPPFTLLKENMI-------SIIDFLEEYSISRLLAVPSMIRAILptlQHRGHNNKLQSCLKLVVLSGEPFPVSL 239
Cdd:PRK08316  226 qldVFLGPYLYVGATNVIldapdpeLILRTIEAERITSFFAPPTVWISLL---RHPDFDTRDLSSLRKGYYGASIMPVEV 302

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   240 WDSLHSLLPETCFLNLYGSTEVSgdctyfdcsELPRLLKTEE----IGSVpiGKSISNCKVVLLGDEDKPYE----GEIC 311
Cdd:PRK08316  303 LKELRERLPGLRFYNCYGQTEIA---------PLATVLGPEEhlrrPGSA--GRPVLNVETRVVDDDGNDVApgevGEIV 371

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   312 VSGLCLSQGYMHSSIESEGYVKlhnnslcnhltndCGsqlYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIET 391
Cdd:PRK08316  372 HRSPQLMLGYWDDPEKTAEAFR-------------GG---WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEE 435

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22327387   392 TLELNPDIAEAVVLLSRDETELASLKAFVVLNKESN-SSDGIIFSIRnwmgGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:PRK08316  436 ALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATvTEDELIAHCR----ARLAGFKVPKRVIFVDELPRNPSGKI 508
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
 110-265 1.23e-04

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 45.53  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  110 TSGSTGKPKGVCGTEQGLLN------RFLWMQELYPvvgEQRF--AF---KTSVGFIDHI-QEFLGAilsstaLVIPpft 177
Cdd:COG1541   91 SSGTTGKPTVVGYTRKDLDRwaelfaRSLRAAGVRP---GDRVqnAFgygLFTGGLGLHYgAERLGA------TVIP--- 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  178 llkenmIS------IIDFLEEYSISRLLAVPSMIRAILPTLQHRGHNNKlQSCLKLVVLSGEPFPVSLWDSLHSLLPETC 251
Cdd:COG1541  159 ------AGggnterQLRLMQDFGPTVLVGTPSYLLYLAEVAEEEGIDPR-DLSLKKGIFGGEPWSEEMRKEIEERWGIKA 231

                        170
                 ....*....|....*...
gi 22327387  252 FlNLYGSTE----VSGDC 265
Cdd:COG1541  232 Y-DIYGLTEvgpgVAYEC 248
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
 351-467 1.29e-04

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 45.90  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   351 LYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDETELASLKAFVVLnKESNSSD 430
Cdd:PRK06155  400 LWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVL-RDGTALE 478

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 22327387   431 GIifSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:PRK06155  479 PV--ALVRHCEPRLAYFAVPRYVEFVAALPKTENGKV 513
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
 301-467 1.55e-04

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


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 45.76  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   301 DEDKPY--EGEICVSGLCLSQGYMHSSIESEgyvklhnnslcNHLTNDcgsqlYYRTGDYGRQLSSGdliFIGRRDRTVK 378
Cdd:PRK05605  409 DETMPDgeEGELLVRGPQVFKGYWNRPEETA-----------KSFLDG-----WFRTGDVVVMEEDG---FIRIVDRIKE 469

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   379 L---NGKRMALEEIETTLELNPDIAEA-VVLLSRD---ETELASlkafVVLNkesnssDGIIF---SIRNWMGGKLPPVM 448
Cdd:PRK05605  470 LiitGGFNVYPAEVEEVLREHPGVEDAaVVGLPREdgsEEVVAA----VVLE------PGAALdpeGLRAYCREHLTRYK 539

                         170
                  ....*....|....*....
gi 22327387   449 IPNHFVLVEKLPLTSSGKV 467
Cdd:PRK05605  540 VPRRFYHVDELPRDQLGKV 558
PLN02736 PLN02736
long-chain acyl-CoA synthetase
 251-425 2.18e-04

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 45.09  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   251 CF----LNLYGSTEVSgdCTYFDCSELPRLlkteeIGSVpiGKSISNCKVVLLG-------DEDKPY-EGEICVSGLCLS 318
Cdd:PLN02736  399 CFggrvLEGYGMTETS--CVISGMDEGDNL-----SGHV--GSPNPACEVKLVDvpemnytSEDQPYpRGEICVRGPIIF 469

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   319 QGY------MHSSIESEGYvkLHnnslcnhltndcgsqlyyrTGDYGRQLSSGDLIFIGRRDRTVKL-NGKRMALEEIET 391
Cdd:PLN02736  470 KGYykdevqTREVIDEDGW--LH-------------------TGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIEN 528

                         170       180       190
                  ....*....|....*....|....*....|....
gi 22327387   392 TLELNPDIAEAVVllsRDETELASLKAFVVLNKE 425
Cdd:PLN02736  529 VYAKCKFVAQCFV---YGDSLNSSLVAVVVVDPE 559
PQQ pfam01011
PQQ enzyme repeat; The family represent a single repeat of a beta propeller. This propeller ...
 748-781 3.22e-04

PQQ enzyme repeat; The family represent a single repeat of a beta propeller. This propeller has been found in several enzymes which utilize pyrrolo-quinoline quinone as a prosthetic group.


Pssm-ID: 395799 [Multi-domain]  Cd Length: 36  Bit Score: 39.10  E-value: 3.22e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 22327387    748 VVIGCYKGKLYFLDFSTGSLCWKFQACGEIKCQP 781
Cdd:pfam01011    3 VYLGSDDGYLYALDAETGKVLWSFKTGGAVLSSP 36
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
352-475 3.51e-04

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 44.27  E-value: 3.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   352 YYRTGDYGrQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDEtELASLKAFVVLNKESNSSdg 431
Cdd:PRK07824  235 WFRTDDLG-ALDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDD-RLGQRVVAAVVGDGGPAP-- 310

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 22327387   432 IIFSIRNWMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEALARL 475
Cdd:PRK07824  311 TLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRR 354
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 190-475 5.88e-04

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


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 43.24  E-value: 5.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  190 LEEYSISRLLAVPSMIRAILptlqHRGHNNKLQScLKLVVLSGEPFPVSLWDSL--HSLLPetcFLNLYGSTEvsgdCTY 267
Cdd:cd05944   93 VERYRITSLSTVPTVYAALL----QVPVNADISS-LRFAMSGAAPLPVELRARFedATGLP---VVEGYGLTE----ATC 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  268 FDCSELPRllKTEEIGSVpiGKSISNCKV-VLLGDEDKPYE--------GEICVSGLCLSQGYMHSsiesegyvkLHNNs 338
Cdd:cd05944  161 LVAVNPPD--GPKRPGSV--GLRLPYARVrIKVLDGVGRLLrdcapdevGEICVAGPGVFGGYLYT---------EGNK- 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  339 lcnhltNDCGSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDET--ELASl 416
Cdd:cd05944  227 ------NAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHagELPV- 299

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  417 kAFVVLNKESNSSDGIIFSirnWMGGKLPP-VMIPNHFVLVEKLPLTSSGKVDYEALARL 475
Cdd:cd05944  300 -AYVQLKPGAVVEEEELLA---WARDHVPErAAVPKHIEVLEELPVTAVGKVFKPALRAD 355
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
 105-467 6.05e-04

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 43.50  E-value: 6.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   105 CYLMYTSGSTGKPKGVCGTEQGLlnrflwMQELYPVVgeQRFAFKT-SVGF----IDHIQEFL-GAILsstALVIPPFTL 178
Cdd:PRK13295  200 TQLIYTSGTTGEPKGVMHTANTL------MANIVPYA--ERLGLGAdDVILmaspMAHQTGFMyGLMM---PVMLGATAV 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   179 LKE--NMISIIDFLEEYSISRLLAVPSMIRAILPTLQHRGHNnklQSCLKLVVLSGEPFPVSLWDSLHSLLpETCFLNLY 256
Cdd:PRK13295  269 LQDiwDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRP---VSSLRTFLCAGAPIPGALVERARAAL-GAKIVSAW 344

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   257 GSTEvSGDCTYFDCSELPRLLKTEEIGSVPiGKSIsncKVVLLGDEDKP--YEGEICVSGLCLSQGYMHSSiesegyvkl 334
Cdd:PRK13295  345 GMTE-NGAVTLTKLDDPDERASTTDGCPLP-GVEV---RVVDADGAPLPagQIGRLQVRGCSNFGGYLKRP--------- 410

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   335 hnnslcnHLTNDcGSQLYYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDET--E 412
Cdd:PRK13295  411 -------QLNGT-DADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERlgE 482

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 22327387   413 LASlkAFVVLnkesNSSDGIIF-SIRNWMGG-KLPPVMIPNHFVLVEKLPLTSSGKV 467
Cdd:PRK13295  483 RAC--AFVVP----RPGQSLDFeEMVEFLKAqKVAKQYIPERLVVRDALPRTPSGKI 533
PRK07787 PRK07787
acyl-CoA synthetase; Validated
 352-474 1.05e-03

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 42.67  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   352 YYRTGDYGRQLSSGDLIFIGRR--DrTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDETELASLKAFVVLNKESNSS 429
Cdd:PRK07787  351 WFRTGDVAVVDPDGMHRIVGREstD-LIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAAD 429

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 22327387   430 DGIIFsirnwMGGKLPPVMIPNHFVLVEKLPLTSSGKVDYEALAR 474
Cdd:PRK07787  430 ELIDF-----VAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
PLN02479 PLN02479
acetate-CoA ligase
 352-467 1.44e-03

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 42.52  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   352 YYRTGDYGRQLSSGdliFIGRRDRTVKL---NGKRMALEEIETTLELNPDIAEAVVLLSRDETELASLKAFVVLNKESNS 428
Cdd:PLN02479  431 WFHSGDLGVKHPDG---YIEIKDRSKDIiisGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDK 507

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 22327387   429 SDGIIFS--IRNWMGGKLPPVMIPNHfVLVEKLPLTSSGKV 467
Cdd:PLN02479  508 SDEAALAedIMKFCRERLPAYWVPKS-VVFGPLPKTATGKI 547
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
 256-467 1.97e-03

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


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 42.12  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   256 YGSTEVSGDCTYFDCSELPRLlkteeiGSVPIGKSISNCKVVLLGDEDKPY--EGEICVSGLCLSQGYMH------SSIE 327
Cdd:PRK12492  365 YGLTETSPVASTNPYGELARL------GTVGIPVPGTALKVIDDDGNELPLgeRGELCIKGPQVMKGYWQqpeataEALD 438

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387   328 SEGYVKlhnnslcnhltndcgsqlyyrTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLS 407
Cdd:PRK12492  439 AEGWFK---------------------TGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGV 497

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327387   408 RDETELASLKAFVVLNKESNSSDGI-IFSIRNWMGGKlppvmIPNHFVLVEKLPLTSSGKV 467
Cdd:PRK12492  498 PDERSGEAVKLFVVARDPGLSVEELkAYCKENFTGYK-----VPKHIVLRDSLPMTPVGKI 553
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
 106-120 3.83e-03

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 41.28  E-value: 3.83e-03
                          10
                  ....*....|....*
gi 22327387   106 YLMYTSGSTGKPKGV 120
Cdd:PRK00174  249 FILYTSGSTGKPKGV 263
PLN02861 PLN02861
long-chain-fatty-acid-CoA ligase
 78-137 5.47e-03

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178452 [Multi-domain]  Cd Length: 660  Bit Score: 40.60  E-value: 5.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327387    78 SMDEKLSVETGCSSFVWP---------CKKERQRK--FCYLMYTSGSTGKPKGVCGTEQGLLNRFLWMQEL 137
Cdd:PLN02861  185 SEQKEEAEELGVSCFSWEefslmgsldCELPPKQKtdICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHL 255
ttLC_FACS_like cd05915
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 352-474 5.59e-03

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. 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, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.


Pssm-ID: 213283 [Multi-domain]  Cd Length: 509  Bit Score: 40.49  E-value: 5.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  352 YYRTGDYGRQLSSGDLIFIGRRDRTVKLNGKRMALEEIETTLELNPDIAEAVVLLSRDETELASLKAFVVLNKESNSSDG 431
Cdd:cd05915  390 FFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPEE 469

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 22327387  432 IIFSIRNWMGGKlppVMIPNHFVLVEKLPLTSSGKVDYEALAR 474
Cdd:cd05915  470 LNEHLLKAGFAK---WQLPDAYVFAEEIPRTSAGKFLKRALRE 509
PaaK cd05913
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ...
 110-272 7.03e-03

Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.


Pssm-ID: 341239 [Multi-domain]  Cd Length: 425  Bit Score: 39.91  E-value: 7.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  110 TSGSTGKPKGVCGTE------QGLLNRFLWMQELYPVVGEQ-RFAFK--TSvGFIDHI-QEFLGailsstALVIPPFTLL 179
Cdd:cd05913   86 SSGTTGKPTVVGYTKndldvwAELVARCLDAAGVTPGDRVQnAYGYGlfTG-GLGFHYgAERLG------ALVIPAGGGN 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327387  180 KENMISIIdflEEYSISRLLAVPSMIRAILPTLQHRGHNNKlQSCLKLVVLSGEPfpvslWDS-----LHSLLPETCFlN 254
Cdd:cd05913  159 TERQLQLI---KDFGPTVLCCTPSYALYLAEEAEEEGIDPR-ELSLKVGIFGAEP-----WTEemrkrIERRLGIKAY-D 228

                        170
                 ....*....|....*...
gi 22327387  255 LYGSTEVSGDCTYFDCSE 272
Cdd:cd05913  229 IYGLTEIIGPGVAFECEE 246
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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