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Conserved domains on  [gi|1436945972|emb|SUA53145|]
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2,3-dihydroxybenzoate-AMP ligase [Oligella urethralis]

Protein Classification

(2,3-dihydroxybenzoyl)adenylate synthase( domain architecture ID 11436966)

(2,3-dihydroxybenzoyl)adenylate synthase catalyzes the activation of the carboxylate group of 2,3-dihydroxy-benzoate via a reversible ATP-dependent pyrophosphate exchange reactions to yield the acyladenylate intermediate (2,3-dihydroxybenzoyl)adenylate, such as in the biosynthesis of the siderophore enterobactin

EC:  6.2.1.-
Gene Ontology:  GO:0019290|GO:0008668
SCOP:  4007642|4002922

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
1-522 0e+00

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: 644.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972   1 MEFTLFPQERAETYIANGLWQGESLFEFFERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQS 80
Cdd:COG1021     3 EGFTPWPEEFAARYREAGYWRGETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  81 ANVLEFFYVLFGLYYLGALPIFCLDGHRSYEIGHIAKFSQARVYLRLCKHES---DSTAEQIIhhfsGDLPHLEIIKTV- 156
Cdd:COG1021    83 PNVAEFVIVFFALFRAGAIPVFALPAHRRAEISHFAEQSEAVAYIIPDRHRGfdyRALARELQ----AEVPSLRHVLVVg 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 157 ----FQG--ELPQCDGDRSKlkekthyQPVDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLV 230
Cdd:COG1021   159 dageFTSldALLAAPADLSE-------PRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 231 LPVSHNFPMSSPGFLGVIYAGATLVIADNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAK 310
Cdd:COG1021   232 LPAAHNFPLSSPGVLGVLYAGGTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAK 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 311 FSSELAARLLDTLDLTLQQVYGMAEGLVNYTRLDDNREVQINTQGKRLSDFDEIQILDLEGKVLGVGEVGVITTRGPYTI 390
Cdd:COG1021   312 LSPELARRVRPALGCTLQQVFGMAEGLVNYTRLDDPEEVILTTQGRPISPDDEVRIVDEDGNPVPPGEVGELLTRGPYTI 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 391 NAYFAPDEVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLG 470
Cdd:COG1021   392 RGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLG 471
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1436945972 471 EKICVQIITDkPDNFNLVKVRKYLTQQHIALNKLPDVVSVVDEFDFTLIGKV 522
Cdd:COG1021   472 ERSCAFVVPR-GEPLTLAELRRFLRERGLAAFKLPDRLEFVDALPLTAVGKI 522
 
Name Accession Description Interval E-value
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
1-522 0e+00

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: 644.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972   1 MEFTLFPQERAETYIANGLWQGESLFEFFERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQS 80
Cdd:COG1021     3 EGFTPWPEEFAARYREAGYWRGETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  81 ANVLEFFYVLFGLYYLGALPIFCLDGHRSYEIGHIAKFSQARVYLRLCKHES---DSTAEQIIhhfsGDLPHLEIIKTV- 156
Cdd:COG1021    83 PNVAEFVIVFFALFRAGAIPVFALPAHRRAEISHFAEQSEAVAYIIPDRHRGfdyRALARELQ----AEVPSLRHVLVVg 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 157 ----FQG--ELPQCDGDRSKlkekthyQPVDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLV 230
Cdd:COG1021   159 dageFTSldALLAAPADLSE-------PRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 231 LPVSHNFPMSSPGFLGVIYAGATLVIADNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAK 310
Cdd:COG1021   232 LPAAHNFPLSSPGVLGVLYAGGTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAK 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 311 FSSELAARLLDTLDLTLQQVYGMAEGLVNYTRLDDNREVQINTQGKRLSDFDEIQILDLEGKVLGVGEVGVITTRGPYTI 390
Cdd:COG1021   312 LSPELARRVRPALGCTLQQVFGMAEGLVNYTRLDDPEEVILTTQGRPISPDDEVRIVDEDGNPVPPGEVGELLTRGPYTI 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 391 NAYFAPDEVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLG 470
Cdd:COG1021   392 RGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLG 471
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1436945972 471 EKICVQIITDkPDNFNLVKVRKYLTQQHIALNKLPDVVSVVDEFDFTLIGKV 522
Cdd:COG1021   472 ERSCAFVVPR-GEPLTLAELRRFLRERGLAAFKLPDRLEFVDALPLTAVGKI 522
DHB_AMP_lig TIGR02275
2,3-dihydroxybenzoate-AMP ligase; Proteins in this family belong to the AMP-binding enzyme ...
2-522 0e+00

2,3-dihydroxybenzoate-AMP ligase; Proteins in this family belong to the AMP-binding enzyme family (pfam00501). Members activate 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate; many are involved in synthesis of siderophores such as enterobactin, vibriobactin, vulnibactin, etc. The most closely related proteine believed to differ in function activates salicylate rather than DHB. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 274063 [Multi-domain]  Cd Length: 526  Bit Score: 521.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972   2 EFTLFPQERAETYIANGLWQGESLFEFFERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSA 81
Cdd:TIGR02275   2 EFTPWPEELAERYREKGYWQDKPLTDILRDQAARYPDAIAIICGNRQWSYRELDQRADNLAAGLTKLGIKQGDTAVVQLP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  82 NVLEFFYVLFGLYYLGALPIFCLDGHRSYEIGHIAKFSQARVYLRLCKHE---SDSTAEQIIHHfsgdLPHLEIIktVFQ 158
Cdd:TIGR02275  82 NIAEFYIVFFALLKLGVAPVLALFSHRKSELTAYASQIEPALYIIDRAHSlfdYDDFARQLQSK----LPTLRNI--IVA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 159 GELPQCDGDR--SKLKEKTHYQPVDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHN 236
Cdd:TIGR02275 156 GQTGEAELFLwlESPAEPVKFPPTKSDEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICWLTQQTRYLCALPAAHN 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 237 FPMSSPGFLGVIYAGATLVIADNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELA 316
Cdd:TIGR02275 236 YPLSSPGALGVFYAGGCVVLAPDPSPTDCFPLIERHKVTVTALVPPAVALWMQAASKSRADLSSLKLLQVGGAKFSAAAA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 317 ARLLDTLDLTLQQVYGMAEGLVNYTRLDDNREVQINTQGKRLSDFDEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAP 396
Cdd:TIGR02275 316 RRVPAVFGCQLQQVFGMAEGLVNYTRLDDPAEIIFTTQGRPMSPDDEVRVVDDHGNPVAPGETGMLLTRGPYTFRGYYKA 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 397 DEVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQ 476
Cdd:TIGR02275 396 PEHNAAAFDAEGFYYTGDLVRLTPEGYIVVVGRAKDQINRGGEKIAAEEIENLLLAHPAVHDAALVSMPDELLGEKSCAF 475
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 1436945972 477 IITdKPDNFNLVKVRKYLTQQHIALNKLPDVVSVVDEFDFTLIGKV 522
Cdd:TIGR02275 476 IVV-RDPALKAAQLRRFLRERGLAEYKLPDRVEFVDSLPLTAVGKV 520
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
9-522 0e+00

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: 521.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972   9 ERAETYIANGLWQGESLFEFFERSCQKFATNTALVLGEDEVSYEAFYFKA--LAWGewLHEQGVRKDDLVVLQSANVLEF 86
Cdd:cd05920     1 EFARRYRAAGYWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRAdrLAAG--LRGLGIRPGDRVVVQLPNVAEF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  87 FYVLFGLYYLGALPIFCLDGHRSYEIGHIAKFSQARVYlrlckhesdstaeqiihhfsgdlphleIIKTVFQGELPQCDG 166
Cdd:cd05920    79 VVLFFALLRLGAVPVLALPSHRRSELSAFCAHAEAVAY---------------------------IVPDRHAGFDHRALA 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 167 drsklKEKTHYQPvdsrAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHNFPMSSPGFLG 246
Cdd:cd05920   132 -----RELAESIP----EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLACPGVLG 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 247 VIYAGATLVIADNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLT 326
Cdd:cd05920   203 TLLAGGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCT 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 327 LQQVYGMAEGLVNYTRLDDNREVQINTQGKRLSDFDEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTE 406
Cdd:cd05920   283 LQQVFGMAEGLLNYTRLDDPDEVIIHTQGRPMSPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTP 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 407 DGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITdKPDNFN 486
Cdd:cd05920   363 DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVL-RDPPPS 441
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 1436945972 487 LVKVRKYLTQQHIALNKLPDVVSVVDEFDFTLIGKV 522
Cdd:cd05920   442 AAQLRRFLRERGLAAYKLPDRIEFVDSLPLTAVGKI 477
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
2-522 6.07e-164

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 475.63  E-value: 6.07e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972   2 EFTLFPQERAETYIANGLWQGESLFEFFERSCQKFATntALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSA 81
Cdd:PRK10946    4 PFTRWPEEFARRYREKGYWQDLPLTDILTRHAASDAI--AVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  82 NVLEFFYVLFGLYYLGALPIFCLDGHRSYEIGHIAKFSQARVYLRLCKHE---SDSTAEQIIHHfsgdLPHLEIIktVFQ 158
Cdd:PRK10946   82 NVAEFYITFFALLKLGVAPVNALFSHQRSELNAYASQIEPALLIADRQHAlfsDDDFLNTLVAE----HSSLRVV--LLL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 159 GELPQCDGDRSKLKEKTHYQPVDSRA--VAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHN 236
Cdd:PRK10946  156 NDDGEHSLDDAINHPAEDFTATPSPAdeVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAHN 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 237 FPMSSPGFLGVIYAGATLVIADNSSPTECFGLIERHKITQTSLVPSLVVAWLN--SAMIDKFDLSSLEVVQVGGAKFSSE 314
Cdd:PRK10946  236 YPMSSPGALGVFLAGGTVVLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQaiAEGGSRAQLASLKLLQVGGARLSET 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 315 LAARLLDTLDLTLQQVYGMAEGLVNYTRLDDNREVQINTQGKRLSDFDEIQILDLEGKVLGVGEVGVITTRGPYTINAYF 394
Cdd:PRK10946  316 LARRIPAELGCQLQQVFGMAEGLVNYTRLDDSDERIFTTQGRPMSPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYY 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 395 APDEVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKIC 474
Cdd:PRK10946  396 KSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSC 475
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 1436945972 475 VQIITDKPdnFNLVKVRKYLTQQHIALNKLPDVVSVVDEFDFTLIGKV 522
Cdd:PRK10946  476 AFLVVKEP--LKAVQLRRFLREQGIAEFKLPDRVECVDSLPLTAVGKV 521
AMP-binding pfam00501
AMP-binding enzyme;
29-437 3.33e-73

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 238.37  E-value: 3.33e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  29 FERSCQKFATNTALVLGEDE-VSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGALPIFCLDGH 107
Cdd:pfam00501   1 LERQAARTPDKTALEVGEGRrLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 108 RSYEIGHIAKFSQARVYL---RLCKHESDSTAEQIIHHfsGDLPHLEIIKTVFQGELPQCDGDRSKLKEKThyQPVDSRA 184
Cdd:pfam00501  81 PAEELAYILEDSGAKVLItddALKLEELLEALGKLEVV--KLVLVLDRDPVLKEEPLPEEAKPADVPPPPP--PPPDPDD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 185 VAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVA----NLQQDTKHLLVLPVSHNFPMSSpGFLGVIYAGATLVIADNS 260
Cdd:pfam00501 157 LAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLSL-GLLGPLLAGATVVLPPGF 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 261 ---SPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAE-- 335
Cdd:pfam00501 236 palDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTEtt 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 336 GLVNYTRLDDNREVQINTQGKRLSDfDEIQILD-LEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGFYITGD 414
Cdd:pfam00501 316 GVVTTPLPLDEDLRSLGSVGRPLPG-TEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGD 394
                         410       420
                  ....*....|....*....|...
gi 1436945972 415 LGYLDENNNITVTGRLKEVINRA 437
Cdd:pfam00501 395 LGRRDEDGYLEIVGRKKDQIKLG 417
 
Name Accession Description Interval E-value
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
1-522 0e+00

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: 644.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972   1 MEFTLFPQERAETYIANGLWQGESLFEFFERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQS 80
Cdd:COG1021     3 EGFTPWPEEFAARYREAGYWRGETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  81 ANVLEFFYVLFGLYYLGALPIFCLDGHRSYEIGHIAKFSQARVYLRLCKHES---DSTAEQIIhhfsGDLPHLEIIKTV- 156
Cdd:COG1021    83 PNVAEFVIVFFALFRAGAIPVFALPAHRRAEISHFAEQSEAVAYIIPDRHRGfdyRALARELQ----AEVPSLRHVLVVg 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 157 ----FQG--ELPQCDGDRSKlkekthyQPVDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLV 230
Cdd:COG1021   159 dageFTSldALLAAPADLSE-------PRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 231 LPVSHNFPMSSPGFLGVIYAGATLVIADNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAK 310
Cdd:COG1021   232 LPAAHNFPLSSPGVLGVLYAGGTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAK 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 311 FSSELAARLLDTLDLTLQQVYGMAEGLVNYTRLDDNREVQINTQGKRLSDFDEIQILDLEGKVLGVGEVGVITTRGPYTI 390
Cdd:COG1021   312 LSPELARRVRPALGCTLQQVFGMAEGLVNYTRLDDPEEVILTTQGRPISPDDEVRIVDEDGNPVPPGEVGELLTRGPYTI 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 391 NAYFAPDEVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLG 470
Cdd:COG1021   392 RGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLG 471
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1436945972 471 EKICVQIITDkPDNFNLVKVRKYLTQQHIALNKLPDVVSVVDEFDFTLIGKV 522
Cdd:COG1021   472 ERSCAFVVPR-GEPLTLAELRRFLRERGLAAFKLPDRLEFVDALPLTAVGKI 522
DHB_AMP_lig TIGR02275
2,3-dihydroxybenzoate-AMP ligase; Proteins in this family belong to the AMP-binding enzyme ...
2-522 0e+00

2,3-dihydroxybenzoate-AMP ligase; Proteins in this family belong to the AMP-binding enzyme family (pfam00501). Members activate 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate; many are involved in synthesis of siderophores such as enterobactin, vibriobactin, vulnibactin, etc. The most closely related proteine believed to differ in function activates salicylate rather than DHB. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 274063 [Multi-domain]  Cd Length: 526  Bit Score: 521.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972   2 EFTLFPQERAETYIANGLWQGESLFEFFERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSA 81
Cdd:TIGR02275   2 EFTPWPEELAERYREKGYWQDKPLTDILRDQAARYPDAIAIICGNRQWSYRELDQRADNLAAGLTKLGIKQGDTAVVQLP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  82 NVLEFFYVLFGLYYLGALPIFCLDGHRSYEIGHIAKFSQARVYLRLCKHE---SDSTAEQIIHHfsgdLPHLEIIktVFQ 158
Cdd:TIGR02275  82 NIAEFYIVFFALLKLGVAPVLALFSHRKSELTAYASQIEPALYIIDRAHSlfdYDDFARQLQSK----LPTLRNI--IVA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 159 GELPQCDGDR--SKLKEKTHYQPVDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHN 236
Cdd:TIGR02275 156 GQTGEAELFLwlESPAEPVKFPPTKSDEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICWLTQQTRYLCALPAAHN 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 237 FPMSSPGFLGVIYAGATLVIADNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELA 316
Cdd:TIGR02275 236 YPLSSPGALGVFYAGGCVVLAPDPSPTDCFPLIERHKVTVTALVPPAVALWMQAASKSRADLSSLKLLQVGGAKFSAAAA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 317 ARLLDTLDLTLQQVYGMAEGLVNYTRLDDNREVQINTQGKRLSDFDEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAP 396
Cdd:TIGR02275 316 RRVPAVFGCQLQQVFGMAEGLVNYTRLDDPAEIIFTTQGRPMSPDDEVRVVDDHGNPVAPGETGMLLTRGPYTFRGYYKA 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 397 DEVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQ 476
Cdd:TIGR02275 396 PEHNAAAFDAEGFYYTGDLVRLTPEGYIVVVGRAKDQINRGGEKIAAEEIENLLLAHPAVHDAALVSMPDELLGEKSCAF 475
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 1436945972 477 IITdKPDNFNLVKVRKYLTQQHIALNKLPDVVSVVDEFDFTLIGKV 522
Cdd:TIGR02275 476 IVV-RDPALKAAQLRRFLRERGLAEYKLPDRVEFVDSLPLTAVGKV 520
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
9-522 0e+00

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: 521.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972   9 ERAETYIANGLWQGESLFEFFERSCQKFATNTALVLGEDEVSYEAFYFKA--LAWGewLHEQGVRKDDLVVLQSANVLEF 86
Cdd:cd05920     1 EFARRYRAAGYWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRAdrLAAG--LRGLGIRPGDRVVVQLPNVAEF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  87 FYVLFGLYYLGALPIFCLDGHRSYEIGHIAKFSQARVYlrlckhesdstaeqiihhfsgdlphleIIKTVFQGELPQCDG 166
Cdd:cd05920    79 VVLFFALLRLGAVPVLALPSHRRSELSAFCAHAEAVAY---------------------------IVPDRHAGFDHRALA 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 167 drsklKEKTHYQPvdsrAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHNFPMSSPGFLG 246
Cdd:cd05920   132 -----RELAESIP----EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLACPGVLG 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 247 VIYAGATLVIADNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLT 326
Cdd:cd05920   203 TLLAGGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCT 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 327 LQQVYGMAEGLVNYTRLDDNREVQINTQGKRLSDFDEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTE 406
Cdd:cd05920   283 LQQVFGMAEGLLNYTRLDDPDEVIIHTQGRPMSPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTP 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 407 DGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITdKPDNFN 486
Cdd:cd05920   363 DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVL-RDPPPS 441
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 1436945972 487 LVKVRKYLTQQHIALNKLPDVVSVVDEFDFTLIGKV 522
Cdd:cd05920   442 AAQLRRFLRERGLAAYKLPDRIEFVDSLPLTAVGKI 477
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
2-522 6.07e-164

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 475.63  E-value: 6.07e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972   2 EFTLFPQERAETYIANGLWQGESLFEFFERSCQKFATntALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSA 81
Cdd:PRK10946    4 PFTRWPEEFARRYREKGYWQDLPLTDILTRHAASDAI--AVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  82 NVLEFFYVLFGLYYLGALPIFCLDGHRSYEIGHIAKFSQARVYLRLCKHE---SDSTAEQIIHHfsgdLPHLEIIktVFQ 158
Cdd:PRK10946   82 NVAEFYITFFALLKLGVAPVNALFSHQRSELNAYASQIEPALLIADRQHAlfsDDDFLNTLVAE----HSSLRVV--LLL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 159 GELPQCDGDRSKLKEKTHYQPVDSRA--VAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHN 236
Cdd:PRK10946  156 NDDGEHSLDDAINHPAEDFTATPSPAdeVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAHN 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 237 FPMSSPGFLGVIYAGATLVIADNSSPTECFGLIERHKITQTSLVPSLVVAWLN--SAMIDKFDLSSLEVVQVGGAKFSSE 314
Cdd:PRK10946  236 YPMSSPGALGVFLAGGTVVLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQaiAEGGSRAQLASLKLLQVGGARLSET 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 315 LAARLLDTLDLTLQQVYGMAEGLVNYTRLDDNREVQINTQGKRLSDFDEIQILDLEGKVLGVGEVGVITTRGPYTINAYF 394
Cdd:PRK10946  316 LARRIPAELGCQLQQVFGMAEGLVNYTRLDDSDERIFTTQGRPMSPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYY 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 395 APDEVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKIC 474
Cdd:PRK10946  396 KSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSC 475
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 1436945972 475 VQIITDKPdnFNLVKVRKYLTQQHIALNKLPDVVSVVDEFDFTLIGKV 522
Cdd:PRK10946  476 AFLVVKEP--LKAVQLRRFLREQGIAEFKLPDRVECVDSLPLTAVGKV 521
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
25-524 4.43e-101

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: 311.74  E-value: 4.43e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  25 LFEFFERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGA--LPIF 102
Cdd:COG0318     1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAvvVPLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 103 CLDGHRsyEIGHIAKFSQARVYLrlckhesdstaeqiihhfsgdlphleiiktvfqgelpqcdgdrsklkekthyqpvds 182
Cdd:COG0318    81 PRLTAE--ELAYILEDSGARALV--------------------------------------------------------- 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 183 raVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHNFPMSSpGFLGVIYAGATLVIADNSSP 262
Cdd:COG0318   102 --TALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTV-GLLAPLLAGATLVLLPRFDP 178
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 263 TECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAE-GLVNYT 341
Cdd:COG0318   179 ERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTEtSPVVTV 258
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 342 RLDDNREVQINTQGKRLSDFdEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFtEDGFYITGDLGYLDEN 421
Cdd:COG0318   259 NPEDPGERRPGSVGRPLPGV-EVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDED 336
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 422 NNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPDNFNLVKVRKYLtQQHIAL 501
Cdd:COG0318   337 GYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFL-RERLAR 415
                         490       500
                  ....*....|....*....|...
gi 1436945972 502 NKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:COG0318   416 YKVPRRVEFVDELPRTASGKIDR 438
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
185-523 1.56e-87

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: 273.01  E-value: 1.56e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 185 VAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHNFPMSspGFLGVIYAGATLVIADNSSPTE 264
Cdd:cd04433     2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF--GLLGALLAGGTVVLLPKFDPEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 265 CFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAE--GLVNYTR 342
Cdd:cd04433    80 ALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTEtgGTVATGP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 343 LDDNREvQINTQGKRLSDFdEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEvNKRSFTEDGFYITGDLGYLDENN 422
Cdd:cd04433   160 PDDDAR-KPGSVGRPVPGV-EVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPE-ATAAVDEDGWYRTGDLGRLDEDG 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 423 NITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPDNFNLVKVRKYLtQQHIALN 502
Cdd:cd04433   237 YLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHV-RERLAPY 315
                         330       340
                  ....*....|....*....|.
gi 1436945972 503 KLPDVVSVVDEFDFTLIGKVR 523
Cdd:cd04433   316 KVPRRVVFVDALPRTASGKID 336
AMP-binding pfam00501
AMP-binding enzyme;
29-437 3.33e-73

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 238.37  E-value: 3.33e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  29 FERSCQKFATNTALVLGEDE-VSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGALPIFCLDGH 107
Cdd:pfam00501   1 LERQAARTPDKTALEVGEGRrLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 108 RSYEIGHIAKFSQARVYL---RLCKHESDSTAEQIIHHfsGDLPHLEIIKTVFQGELPQCDGDRSKLKEKThyQPVDSRA 184
Cdd:pfam00501  81 PAEELAYILEDSGAKVLItddALKLEELLEALGKLEVV--KLVLVLDRDPVLKEEPLPEEAKPADVPPPPP--PPPDPDD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 185 VAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVA----NLQQDTKHLLVLPVSHNFPMSSpGFLGVIYAGATLVIADNS 260
Cdd:pfam00501 157 LAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLSL-GLLGPLLAGATVVLPPGF 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 261 ---SPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAE-- 335
Cdd:pfam00501 236 palDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTEtt 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 336 GLVNYTRLDDNREVQINTQGKRLSDfDEIQILD-LEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGFYITGD 414
Cdd:pfam00501 316 GVVTTPLPLDEDLRSLGSVGRPLPG-TEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGD 394
                         410       420
                  ....*....|....*....|...
gi 1436945972 415 LGYLDENNNITVTGRLKEVINRA 437
Cdd:pfam00501 395 LGRRDEDGYLEIVGRKKDQIKLG 417
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
25-524 4.61e-66

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: 221.28  E-value: 4.61e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  25 LFEFFERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGAL--PIF 102
Cdd:cd05936     1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVvvPLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 103 CLDGHRsyEIGHIAKFSQARVYlrlckhesdstaeqiihhfsgdlphleIIKTVFQGELpqcdgdrsKLKEKTHYQPVDS 182
Cdd:cd05936    81 PLYTPR--ELEHILNDSGAKAL---------------------------IVAVSFTDLL--------AAGAPLGERVALT 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 183 R-AVAFLQLSGGTTGLPKLIPRTHDdylysvresAVVANLQQ-----------DTKHLLVLPVSHNFPMSSPGFLGvIYA 250
Cdd:cd05936   124 PeDVAVLQYTSGTTGVPKGAMLTHR---------NLVANALQikawledllegDDVVLAALPLFHVFGLTVALLLP-LAL 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 251 GATLVIADNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQV 330
Cdd:cd05936   194 GATIVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEG 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 331 YGMAEG--LVNYTRLDDNRevQINTQGKRLSDFdEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTeDG 408
Cdd:cd05936   274 YGLTETspVVAVNPLDGPR--KPGSIGIPLPGT-EVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV-DG 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 409 FYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPDNFNLV 488
Cdd:cd05936   350 WLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEE 429
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 1436945972 489 KVRKYLtQQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd05936   430 EIIAFC-REQLAGYKVPRQVEFRDELPKSAVGKILR 464
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
49-524 4.76e-66

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: 220.33  E-value: 4.76e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  49 VSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGA-----LPIFcldghRSYEIGHIAKFSQARV 123
Cdd:cd05903     2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAvtnpiLPFF-----REHELAFILRRAKAKV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 124 YlrlckhesdstaeqiihhfsgdlphleIIKTVFQGELPQCDGDrsklkekthyqpvdsrAVAFLQLSGGTTGLPKLIPR 203
Cdd:cd05903    77 F---------------------------VVPERFRQFDPAAMPD----------------AVALLLFTSGTTGEPKGVMH 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 204 THDDYLYSVRESAVVANLQQDTKHLLVLPVSHnFPMSSPGFLGVIYAGATLVIADNSSPTECFGLIERHKITQTSLVPSL 283
Cdd:cd05903   114 SHNTLSASIRQYAERLGLGPGDVFLVASPMAH-QTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPF 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 284 VVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAEGLVNYTRLDDNREVQINTQGKRLSDFDE 363
Cdd:cd05903   193 LTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPEDRRLYTDGRPLPGVE 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 364 IQILDLEGKVLGVGEVGVITTRGPYTINAYF-APDevNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIM 442
Cdd:cd05903   273 IKVVDDTGATLAPGVEGELLSRGPSVFLGYLdRPD--LTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIP 350
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 443 PSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPDNFNLVKVRKYLTQQHIALNKLPDVVSVVDEFDFTLIGKV 522
Cdd:cd05903   351 VLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQGVAKQYWPERLVHVDDLPRTPSGKV 430

                  ..
gi 1436945972 523 RR 524
Cdd:cd05903   431 QK 432
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
29-524 1.89e-62

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: 210.54  E-value: 1.89e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  29 FERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGAlpIFCLDGHR 108
Cdd:cd17631     1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGA--VFVPLNFR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 109 --SYEIGHIAKFSQARVYLRlckhesdstaeqiihhfsgDLphleiiktvfqgelpqcdgdrsklkekthyqpvdsravA 186
Cdd:cd17631    79 ltPPEVAYILADSGAKVLFD-------------------DL--------------------------------------A 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 187 FLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHNFPMSSPGfLGVIYAGATLVIADNSSPTECF 266
Cdd:cd17631   102 LLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFT-LPTLLRGGTVVILRKFDPETVL 180
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 267 GLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKfSSELAARLLDTLDLTLQQVYGMAE--GLVNYTRLD 344
Cdd:cd17631   181 DLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAP-MPERLLRALQARGVKFVQGYGMTEtsPGVTFLSPE 259
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 345 DNREVqINTQGKRLSdFDEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFtEDGFYITGDLGYLDENNNI 424
Cdd:cd17631   260 DHRRK-LGSAGRPVF-FVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYL 336
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 425 TVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPDNFNLVKVRKYLTqQHIALNKL 504
Cdd:cd17631   337 YIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCR-ERLARYKI 415
                         490       500
                  ....*....|....*....|
gi 1436945972 505 PDVVSVVDEFDFTLIGKVRR 524
Cdd:cd17631   416 PKSVEFVDALPRNATGKILK 435
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
57-522 1.97e-62

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: 212.07  E-value: 1.97e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  57 KALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLF-----GLYYLGALPIFcldghRSYEIGHIAKFSQARVylrLCKHE 131
Cdd:cd05911    19 LSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLgclfaGGIFSAANPIY-----TADELAHQLKISKPKV---IFTDP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 132 SD----STAEQIIhhfsGDLPHLEIIKTVFQGELPQCDGDRSKLKEKTHYQPVDSRA----VAFLQLSGGTTGLPKLIPR 203
Cdd:cd05911    91 DGlekvKEAAKEL----GPKDKIIVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDgkddTAAILYSSGTTGLPKGVCL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 204 THDDY---LYSVReSAVVANLQQDTKHLLVLPVSHNFPMSSpgFLGVIYAGATLVIADNSSPTECFGLIERHKITQTSLV 280
Cdd:cd05911   167 SHRNLianLSQVQ-TFLYGNDGSNDVILGFLPLYHIYGLFT--TLASLLNGATVIIMPKFDSELFLDLIEKYKITFLYLV 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 281 PSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAAR-LLDTLDLTLQQVYGMAE--GLVNYTRLDDNRevqINTQGKR 357
Cdd:cd05911   244 PPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELlAKRFPNATIKQGYGMTEtgGILTVNPDGDDK---PGSVGRL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 358 LSDFdEIQILDLEGK-VLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINR 436
Cdd:cd05911   321 LPNV-EAKIVDDDGKdSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 437 AGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGE--KICV-----QIITDKpdnfnlvKVRKYLtQQHIALNK-LPDVV 508
Cdd:cd05911   400 KGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGElpRAYVvrkpgEKLTEK-------EVKDYV-AKKVASYKqLRGGV 471
                         490
                  ....*....|....
gi 1436945972 509 SVVDEFDFTLIGKV 522
Cdd:cd05911   472 VFVDEIPKSASGKI 485
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
6-524 8.54e-62

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 211.92  E-value: 8.54e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972   6 FPQERAETYIANGLWQGESLFEFFERSCQKFATNTALVlgeDE----VSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSA 81
Cdd:PRK06087    6 FNEQRRAAYRQQGYWGDASLADYWQQTARAMPDKIAVV---DNhgasYTYSALDHAASRLANWLLAKGIEPGDRVAFQLP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  82 NVLEFFYVLFGLYYLGALPIFCLDGHRSYEIGHIAKFSQARVYLRLCKHESdSTAEQIIHHFSGDLPHLEIIKTVFQGEL 161
Cdd:PRK06087   83 GWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQ-TRPVDLILPLQNQLPQLQQIVGVDKLAP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 162 PQCDGDRSKLKEK----THYQPVDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHnf 237
Cdd:PRK06087  162 ATSSLSLSQIIADyeplTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGH-- 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 238 pmsSPGFL-GVI---YAGATLVIADNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSS 313
Cdd:PRK06087  240 ---ATGFLhGVTapfLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPK 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 314 ELAaRLLDTLDLTLQQVYGMAEGLVN-YTRLDDNREVQINTQGKRLSDFdEIQILDLEGKVLGVGEVGVITTRGPYTINA 392
Cdd:PRK06087  317 KVA-RECQQRGIKLLSVYGSTESSPHaVVNLDDPLSRFMHTDGYAAAGV-EIKVVDEARKTLPPGCEGEEASRGPNVFMG 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 393 YFAPDEVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEK 472
Cdd:PRK06087  395 YLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGER 474
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1436945972 473 ICVQIITDKPDN-FNLVKVRKYLTQQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:PRK06087  475 SCAYVVLKAPHHsLTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQK 527
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
37-524 1.31e-58

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: 202.16  E-value: 1.31e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  37 ATNTALVLGED--EVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGA--LPI---FCLDGHRS 109
Cdd:cd05926     1 PDAPALVVPGStpALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAvvAPLnpaYKKAEFEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 110 YeighiakFSQARVYLRLCKHESDSTAEQIIHHFSGDLPHLEIIKTVFQ-----GELPQCDGDRSKLKEKTHYQPVDsra 184
Cdd:cd05926    81 Y-------LADLGSKLVLTPKGELGPASRAASKLGLAILELALDVGVLIrapsaESLSNLLADKKNAKSEGVPLPDD--- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 185 VAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHnfpmsSPGFLGV----IYAGATLVIADNS 260
Cdd:cd05926   151 LALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFH-----VHGLVASllstLAAGGSVVLPPRF 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 261 SPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFD-LSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAEG--L 337
Cdd:cd05926   226 SASTFWPDVRDYNATWYTAVPTIHQILLNRPEPNPESpPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAahQ 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 338 VNYTRLDDNReVQINTQGKrlSDFDEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGFYITGDLGY 417
Cdd:cd05926   306 MTSNPLPPGP-RKPGSVGK--PVGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGY 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 418 LDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPDNFNLVKVRKYLtQQ 497
Cdd:cd05926   383 LDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFC-RK 461
                         490       500
                  ....*....|....*....|....*..
gi 1436945972 498 HIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd05926   462 HLAAFKVPKKVYFVDELPKTATGKIQR 488
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
188-524 1.02e-55

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: 190.18  E-value: 1.02e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 188 LQLSGGTTGLPKLIPRTHddylYSV-RESAVVANLQQDT-KHLLVLPVS--HNFPMSSpGFLGVIYAGATLVIADNS-SP 262
Cdd:cd05917     7 IQFTSGTTGSPKGATLTH----HNIvNNGYFIGERLGLTeQDRLCIPVPlfHCFGSVL-GVLACLTHGATMVFPSPSfDP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 263 TECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQV-YGMAEG--LVN 339
Cdd:cd05917    82 LAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIaYGMTETspVST 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 340 YTRLDDNREVQINTQGkRLSDFDEIQILDLEGK-VLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGFYITGDLGYL 418
Cdd:cd05917   162 QTRTDDSIEKRVNTVG-RIMPHTEAKIVDPEGGiVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 419 DENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPDNFNLVKVRKYLTQQh 498
Cdd:cd05917   241 DEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKAYCKGK- 319
                         330       340
                  ....*....|....*....|....*.
gi 1436945972 499 IALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd05917   320 IAHYKVPRYVFFVDEFPLTVSGKIQK 345
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
27-522 1.09e-55

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 194.64  E-value: 1.09e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  27 EFFERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGAL--PI-FC 103
Cdd:PRK06187   10 RILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVlhPInIR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 104 LdghRSYEIGHIAKFSQARVYLrlckheSDSTAEQIIHHFSGDLPHLEIIKTVFQGELPQCDGDRSKLKEK-----THY- 177
Cdd:PRK06187   90 L---KPEEIAYILNDAEDRVVL------VDSEFVPLLAAILPQLPTVRTVIVEGDGPAAPLAPEVGEYEELlaaasDTFd 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 178 -QPVDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHNFPMSSPgFLGvIYAGATLVI 256
Cdd:PRK06187  161 fPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLP-YLA-LMAGAKQVI 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 257 ADNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAE- 335
Cdd:PRK06187  239 PRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTEt 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 336 -GLVNYTRLDDNREVQIN---TQGKRLSDFdEIQILDLEGKVLGV--GEVGVITTRGPYTINAYFAPDEVNKRSFtEDGF 409
Cdd:PRK06187  319 sPVVSVLPPEDQLPGQWTkrrSAGRPLPGV-EARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAETI-DGGW 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 410 YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKIcVQIITDKPD-NFNLV 488
Cdd:PRK06187  397 LHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERP-VAVVVLKPGaTLDAK 475
                         490       500       510
                  ....*....|....*....|....*....|....
gi 1436945972 489 KVRKYLtQQHIALNKLPDVVSVVDEFDFTLIGKV 522
Cdd:PRK06187  476 ELRAFL-RGRLAKFKLPKRIAFVDELPRTSVGKI 508
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
30-524 1.47e-55

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 194.35  E-value: 1.47e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  30 ERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGAL-----PIFCL 104
Cdd:PRK07656   12 ARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVvvplnTRYTA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 105 DghrsyEIGHIAKFSQARVYLRLckhesdstaEQIIHHF---SGDLPHLEIIKTVfqgelPQCDGDRSKLKEKTHYQ--- 178
Cdd:PRK07656   92 D-----EAAYILARGDAKALFVL---------GLFLGVDysaTTRLPALEHVVIC-----ETEEDDPHTEKMKTFTDfla 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 179 ---------PVDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHNFPMSSpGFLGVIY 249
Cdd:PRK07656  153 agdpaerapEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKA-GVNAPLM 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 250 AGATLVIADNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGA--------KFSSELAARLLD 321
Cdd:PRK07656  232 RGATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAAsmpvalleRFESELGVDIVL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 322 TLdltlqqvYGMAE--GLVNYTRLDDNREVQINTQGKRLSDFdEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEV 399
Cdd:PRK07656  312 TG-------YGLSEasGVTTFNRLDDDRKTVAGTIGTAIAGV-ENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEA 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 400 NKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIIT 479
Cdd:PRK07656  384 TAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVL 463
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 1436945972 480 DKPDNFNLVKVRKYlTQQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:PRK07656  464 KPGAELTEEELIAY-CREHLAKYKVPRSIEFLDELPKNATGKVLK 507
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
1-524 7.00e-55

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 193.35  E-value: 7.00e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972   1 MEF--TLFPQERAEtYIANGLWQGESLFEFFER---SCQKFATNTALVLGEDE---VSYE--AFYFKALAWGewLHEQGV 70
Cdd:PRK13295    1 MEFdaVLLPPRRAA-SIAAGHWHDRTINDDLDAcvaSCPDKTAVTAVRLGTGAprrFTYRelAALVDRVAVG--LARLGV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  71 RKDDLVVLQSANVLEFFYVLFGLYYLGA-----LPIFcldghRSYEIGHIAKFSQARVYLrLCKHESDSTAEQIIHHFSG 145
Cdd:PRK13295   78 GRGDVVSCQLPNWWEFTVLYLACSRIGAvlnplMPIF-----RERELSFMLKHAESKVLV-VPKTFRGFDHAAMARRLRP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 146 DLPHLEIIkTVFQGelpqcDGDRS--KL-------KEKTHYQPVDSRA-----VAFLQLSGGTTGLPKLIPRTHDDYLYS 211
Cdd:PRK13295  152 ELPALRHV-VVVGG-----DGADSfeALlitpaweQEPDAPAILARLRpgpddVTQLIYTSGTTGEPKGVMHTANTLMAN 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 212 VRESAVVANLQQDTKHLLVLPVSHnfpmsSPGFL-GV---IYAGATLVIADNSSPTECFGLIERHKITQTSLVPSLVVAW 287
Cdd:PRK13295  226 IVPYAERLGLGADDVILMASPMAH-----QTGFMyGLmmpVMLGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDL 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 288 LNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAE-GLVNYTRLDDNREVQINTQGKRLSDFdEIQI 366
Cdd:PRK13295  301 TRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTEnGAVTLTKLDDPDERASTTDGCPLPGV-EVRV 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 367 LDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFteDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEI 446
Cdd:PRK13295  380 VDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTDA--DGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEI 457
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1436945972 447 EELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPDNFNLVKVRKYLTQQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:PRK13295  458 EALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFLKAQKVAKQYIPERLVVRDALPRTPSGKIQK 535
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
34-471 6.41e-54

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: 189.75  E-value: 6.41e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  34 QKFATNTALV--LGEDEVSYEAFY--FKALAWGewLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGAL-----PIFCL 104
Cdd:cd05904    16 SAHPSRPALIdaATGRALTYAELErrVRRLAAG--LAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVvttanPLSTP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 105 DghrsyEIGHIAKFSQARVYLRLCKhesdsTAEQIIhhfSGDLPhleiikTVFQGELP-QCDGDRSKLKEKTHYQPVDSR 183
Cdd:cd05904    94 A-----EIAKQVKDSGAKLAFTTAE-----LAEKLA---SLALP------VVLLDSAEfDSLSFSDLLFEADEAEPPVVV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 184 A----VAFLQLSGGTTGLPKLIPRTHDDYLYSVR--ESAVVANLQQDTKHLLVLPVSHNFPMSSPgFLGVIYAGATLVIA 257
Cdd:cd05904   155 IkqddVAALLYSSGTTGRSKGVMLTHRNLIAMVAqfVAGEGSNSDSEDVFLCVLPMFHIYGLSSF-ALGLLRLGATVVVM 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 258 DNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTL-DLTLQQVYGMAE- 335
Cdd:cd05904   234 PRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFpNVDLGQGYGMTEs 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 336 -GLVNYTRLDDNREVQINTQGKRLSDFdEIQILDLE-GKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGFYITG 413
Cdd:cd05904   314 tGVVAMCFAPEKDRAKYGSVGRLVPNV-EAKIVDPEtGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTG 392
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1436945972 414 DLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGE 471
Cdd:cd05904   393 DLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGE 450
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
22-524 1.92e-50

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 181.51  E-value: 1.92e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  22 GESLFEFFERSCQKFATNTALVLGEDEVSYE----AFYFKALAWGewLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLG 97
Cdd:PRK12583   17 TQTIGDAFDATVARFPDREALVVRHQALRYTwrqlADAVDRLARG--LLALGVQPGDRVGIWAPNCAEWLLTQFATARIG 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  98 ALPIFCLDGHRSYEIGHIAKFSQAR---------------VYLRLCKHESDSTAEQIIHHfsgDLPHLEII--------- 153
Cdd:PRK12583   95 AILVNINPAYRASELEYALGQSGVRwvicadafktsdyhaMLQELLPGLAEGQPGALACE---RLPELRGVvslapappp 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 154 -KTVFQGELPQCDG-DRSKLKEKThyQPVDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVL 231
Cdd:PRK12583  172 gFLAWHELQARGETvSREALAERQ--ASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPV 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 232 PVSHNFPMSSPGfLGVIYAGATLVI-ADNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAK 310
Cdd:PRK12583  250 PLYHCFGMVLAN-LGCMTVGACLVYpNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAP 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 311 FSSELAARLLDTLDLTLQQV-YGMAEG--LVNYTRLDDNREVQINTQGKRLSDFdEIQILDLEGKVLGVGEVGVITTRGP 387
Cdd:PRK12583  329 CPIEVMRRVMDEMHMAEVQIaYGMTETspVSLQTTAADDLERRVETVGRTQPHL-EVKVVDPDGATVPRGEIGELCTRGY 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 388 YTINAYFAPDEVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDE 467
Cdd:PRK12583  408 SVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDE 487
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1436945972 468 LLGEKICVQIITDKPDNFNLVKVRKYLTQQhIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:PRK12583  488 KYGEEIVAWVRLHPGHAASEEELREFCKAR-IAHFKVPRYFRFVDEFPMTVTGKVQK 543
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
48-524 4.25e-50

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: 177.67  E-value: 4.25e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  48 EVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGALPIFCLDGHRSYEIGHIAKfsqarvylrl 127
Cdd:cd05935     1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILN---------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 128 ckhesDSTAEQIIHHfsgdlphleiiktvfqgelpqcdgdrSKLKEkthyqpvdsraVAFLQLSGGTTGLPKLIPRTHDD 207
Cdd:cd05935    71 -----DSGAKVAVVG--------------------------SELDD-----------LALIPYTSGTTGLPKGCMHTHFS 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 208 YLYSVRESAVVANLQQDTKHLLVLPVSHnfpmsSPGFLGV----IYAGATLVIADNSSPTECFGLIERHKITQTSLVPSL 283
Cdd:cd05935   109 AAANALQSAVWTGLTPSDVILACLPLFH-----VTGFVGSlntaVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTM 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 284 VVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAEGLvNYTRLDDNREVQINTQGKRLSDFDe 363
Cdd:cd05935   184 LVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETM-SQTHTNPPLRPKLQCLGIP*FGVD- 261
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 364 IQILDLE-GKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDG---FYITGDLGYLDENNNITVTGRLKEVINRAGE 439
Cdd:cd05935   262 ARVIDIEtGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGF 341
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 440 KIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITD-----KPDNFNLVKVRKyltqQHIALNKLPDVVSVVDEF 514
Cdd:cd05935   342 KVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRpeyrgKVTEEDIIEWAR----EQMAAYKYPREVEFVDEL 417
                         490
                  ....*....|
gi 1436945972 515 DFTLIGKVRR 524
Cdd:cd05935   418 PRSASGKILW 427
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
24-522 2.48e-47

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


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 172.45  E-value: 2.48e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  24 SLFEFFERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQ-GVRKDDLVVLQSANVLEFFYVLFGLYYLGAL--P 100
Cdd:PRK08314   11 SLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVvvP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 101 IFCLDghRSYEIGHIAKFSQARV-------YLRLCK-HESDSTAEQIIHHFSGDLP-HLEIIKTVF---QGELPQCDGDR 168
Cdd:PRK08314   91 VNPMN--REEELAHYVTDSGARVaivgselAPKVAPaVGNLRLRHVIVAQYSDYLPaEPEIAVPAWlraEPPLQALAPGG 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 169 SKLKEKT---HYQP----VDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHNFPMSS 241
Cdd:PRK08314  169 VVAWKEAlaaGLAPpphtAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVH 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 242 pGFLGVIYAGATLVIA---DNSSPTEcfgLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAAR 318
Cdd:PRK08314  249 -SMNAPIYAGATVVLMprwDREAAAR---LIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMPEAVAER 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 319 LLDTLDLTLQQVYGMAEgLVNYTRLDDNREVQINTQGKRLSDFDEiQILDLE-GKVLGVGEVGVITTRGPYTINAYFAPD 397
Cdd:PRK08314  325 LKELTGLDYVEGYGLTE-TMAQTHSNPPDRPKLQCLGIPTFGVDA-RVIDPEtLEELPPGEVGEIVVHGPQVFKGYWNRP 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 398 EVNKRSFTE-DG--FYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKic 474
Cdd:PRK08314  403 EATAEAFIEiDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGET-- 480
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1436945972 475 VQ-IITDKPDNFNLVKVRKYLT--QQHIALNKLPDVVSVVDEFDFTLIGKV 522
Cdd:PRK08314  481 VKaVVVLRPEARGKTTEEEIIAwaREHMAAYKYPRIVEFVDSLPKSGSGKI 531
PRK06145 PRK06145
acyl-CoA synthetase; Validated
40-522 2.79e-47

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 171.61  E-value: 2.79e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  40 TALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGA--LPI-FCLDGHrsyEIGHIA 116
Cdd:PRK06145   19 AALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAvfLPInYRLAAD---EVAYIL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 117 KFSQARVYLrlckHESDSTAEQIIHHfsgdlphleiiKTVFQGELPQCDGDR--SKLKEKTHYQPVDSRAVAFLQLSGGT 194
Cdd:PRK06145   96 GDAGAKLLL----VDEEFDAIVALET-----------PKIVIDAAAQADSRRlaQGGLEIPPQAAVAPTDLVRLMYTSGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 195 TGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHNFPMSSPGfLGVIYAGATLVIADNSSPTECFGLIERHKI 274
Cdd:PRK06145  161 TDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPG-IAVLWVGGTLRIHREFDPEAVLAAIERHRL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 275 TQTSLVPSLVVAWLNSAMIDKFDLSSLEVVqVGGAKFSSELAARLLDTLDLTLQQV--YGMAEGLVNYTRLDDNREVQ-I 351
Cdd:PRK06145  240 TCAWMAPVMLSRVLTVPDRDRFDLDSLAWC-IGGGEKTPESRIRDFTRVFTRARYIdaYGLTETCSGDTLMEAGREIEkI 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 352 NTQGKRLSDFdEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTeDGFYITGDLGYLDENNNITVTGRLK 431
Cdd:PRK06145  319 GSTGRALAHV-EIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFY-GDWFRSGDVGYLDEEGFLYLTDRKK 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 432 EVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPDNFNLVKVRKYlTQQHIALNKLPDVVSVV 511
Cdd:PRK06145  397 DMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRH-CRQRLASFKVPRQLKVR 475
                         490
                  ....*....|.
gi 1436945972 512 DEFDFTLIGKV 522
Cdd:PRK06145  476 DELPRNPSGKV 486
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
22-524 8.06e-46

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 168.09  E-value: 8.06e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  22 GESLFEFFERScQKFATNTALV--LGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGAL 99
Cdd:cd17642    17 GEQLHKAMKRY-ASVPGTIAFTdaHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVG 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 100 PIFCLDGHRSYEIGHIAKFSQARVYLrlckhESDSTAEQIIHhFSGDLPHLEII-----KTVFQGElpQCD------GDR 168
Cdd:cd17642    96 VAPTNDIYNERELDHSLNISKPTIVF-----CSKKGLQKVLN-VQKKLKIIKTIiildsKEDYKGY--QCLytfitqNLP 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 169 SKLKEKTHYQPVDSR--AVAFLQLSGGTTGLPKLIPRTHDDYLY---SVRESAVVANLQQDTKHLLVLPVSHNFPMSSpg 243
Cdd:cd17642   168 PGFNEYDFKPPSFDRdeQVALIMNSSGSTGLPKGVQLTHKNIVArfsHARDPIFGNQIIPDTAILTVIPFHHGFGMFT-- 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 244 FLGVIYAGATLVIADNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELA-ARLLDT 322
Cdd:cd17642   246 TLGYLICGFRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGeAVAKRF 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 323 LDLTLQQVYGMAEGLVNYTRLDDNrEVQINTQGKrLSDFDEIQILDLE-GKVLGVGEVGVITTRGPYTINAYFAPDEVNK 401
Cdd:cd17642   326 KLPGIRQGYGLTETTSAILITPEG-DDKPGAVGK-VVPFFYAKVVDLDtGKTLGPNERGELCVKGPMIMKGYVNNPEATK 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 402 RSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDK 481
Cdd:cd17642   404 ALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEA 483
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 1436945972 482 PDNFNLVKVRKYLTQQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd17642   484 GKTMTEKEVMDYVASQVSTAKRLRGGVKFVDEVPKGLTGKIDR 526
PRK08315 PRK08315
AMP-binding domain protein; Validated
22-523 7.60e-45

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 166.14  E-value: 7.60e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  22 GESLFEFFERSCQKFATNTALVLGEDEV--SYEAFYFK--ALAWGewLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLG 97
Cdd:PRK08315   15 EQTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEvdALAKG--LLALGIEKGDRVGIWAPNVPEWVLTQFATAKIG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  98 ALPIFCLDGHRSYEIGHIAKFSQARVyLRLCKHESDSTAEQII-------------HHFSGDLPHLEIIktVFQGELPQC 164
Cdd:PRK08315   93 AILVTINPAYRLSELEYALNQSGCKA-LIAADGFKDSDYVAMLyelapelatcepgQLQSARLPELRRV--IFLGDEKHP 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 165 DGDR----SKLKEKTHYQPVDSRAVAF-------LQLSGGTTGLPKLIPRTHDDYL---YSVRESAvvaNLQQDTKhlLV 230
Cdd:PRK08315  170 GMLNfdelLALGRAVDDAELAARQATLdpddpinIQYTSGTTGFPKGATLTHRNILnngYFIGEAM---KLTEEDR--LC 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 231 LPVS--HNFPMSSpGFLGVIYAGATLVI-ADNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSL------ 301
Cdd:PRK08315  245 IPVPlyHCFGMVL-GNLACVTHGATMVYpGEGFDPLATLAAVEEERCTALYGVPTMFIAELDHPDFARFDLSSLrtgima 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 302 ------EVV-QVGGAKFSSELAarlldtldltlqQVYGMAEG--LVNYTRLDDNREVQINTQGkRLSDFDEIQILDLE-G 371
Cdd:PRK08315  324 gspcpiEVMkRVIDKMHMSEVT------------IAYGMTETspVSTQTRTDDPLEKRVTTVG-RALPHLEVKIVDPEtG 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 372 KVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLY 451
Cdd:PRK08315  391 ETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLY 470
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1436945972 452 AHPDVKDVLVTGVPDELLGEKICVQIITDKPDNFNLVKVRKYLTQQhIALNKLPDVVSVVDEFDFTLIGKVR 523
Cdd:PRK08315  471 THPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGK-IAHYKIPRYIRFVDEFPMTVTGKIQ 541
PRK07470 PRK07470
acyl-CoA synthetase; Validated
25-475 7.74e-43

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 159.82  E-value: 7.74e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  25 LFEFFERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGAlpIFCL 104
Cdd:PRK07470    9 LAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGA--VWVP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 105 DGHRSY--EIGHIAKFSQARVYLrlCKHESDSTAEqIIHHFSGDLPHLEIIKTVFQGE-----LPQCDGDRSKLKEKTHY 177
Cdd:PRK07470   87 TNFRQTpdEVAYLAEASGARAMI--CHADFPEHAA-AVRAASPDLTHVVAIGGARAGLdyealVARHLGARVANAAVDHD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 178 QPvdsravAFLQLSGGTTGLPKLIPRTHDDYLYsvresaVVAN----LQQDTKH----LLVLPVSHNfpmsspgfLGV-- 247
Cdd:PRK07470  164 DP------CWFFFTSGTTGRPKAAVLTHGQMAF------VITNhladLMPGTTEqdasLVVAPLSHG--------AGIhq 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 248 ---IYAGATLVI--ADNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDT 322
Cdd:PRK07470  224 lcqVARGAATVLlpSERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAK 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 323 LDLTLQQVYGMAEGLVNYTRL-------DDNREVQINTQGKRLSDFdEIQILDLEGKVLGVGEVGVITTRGPYTINAYFA 395
Cdd:PRK07470  304 LGKVLVQYFGLGEVTGNITVLppalhdaEDGPDARIGTCGFERTGM-EVQIQDDEGRELPPGETGEICVIGPAVFAGYYN 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 396 PDEVNKRSFtEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGE---K 472
Cdd:PRK07470  383 NPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEvgvA 461

                  ...
gi 1436945972 473 ICV 475
Cdd:PRK07470  462 VCV 464
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
185-524 4.43e-41

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: 150.73  E-value: 4.43e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 185 VAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHNFPMSSpGFLGVIYAGATLVIADNSSPTE 264
Cdd:cd17638     2 VSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKA-GIVACLLTGATVVPVAVFDVDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 265 CFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQV-YGMAE-GLVNYTR 342
Cdd:cd17638    81 ILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTaYGLTEaGVATMCR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 343 LDDNREVQINTQGKRLSDFdEIQILDlEGKVLgvgevgvitTRGPYTINAYFAPDEVNKRSFTEDGFYITGDLGYLDENN 422
Cdd:cd17638   161 PGDDAETVATTCGRACPGF-EVRIAD-DGEVL---------VRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERG 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 423 NITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPDNFNLVKVRKYlTQQHIALN 502
Cdd:cd17638   230 YLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAW-CRERLANY 308
                         330       340
                  ....*....|....*....|..
gi 1436945972 503 KLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd17638   309 KVPRFVRFLDELPRNASGKVMK 330
PLN02246 PLN02246
4-coumarate--CoA ligase
14-471 9.08e-41

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 154.37  E-value: 9.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  14 YIANGLwqgeSLFEF-FERScQKFATNTALVLGE--DEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVL 90
Cdd:PLN02246   18 YIPNHL----PLHDYcFERL-SEFSDRPCLIDGAtgRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAF 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  91 FGLYYLGAL-----PIFCldghrSYEIGHIAKFSQARVY---------LRLCKHESDSTAEQIIHHFSGDLPHLEIIKTV 156
Cdd:PLN02246   93 LGASRRGAVtttanPFYT-----PAEIAKQAKASGAKLIitqscyvdkLKGLAEDDGVTVVTIDDPPEGCLHFSELTQAD 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 157 fQGELPQCDgdrsklkekthYQPVDsraVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVAN----LQQDTKHLLVLP 232
Cdd:PLN02246  168 -ENELPEVE-----------ISPDD---VVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENpnlyFHSDDVILCVLP 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 233 VSHNFPMSSPGFLGvIYAGATLVIADNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFS 312
Cdd:PLN02246  233 MFHIYSLNSVLLCG-LRVGAAILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLG 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 313 SEL--AARLLDTLDLTLQQvYGMAE-GLVNYTRLDDNRE-----------VQINTqgkrlsdfdEIQILDLE-GKVLGVG 377
Cdd:PLN02246  312 KELedAFRAKLPNAVLGQG-YGMTEaGPVLAMCLAFAKEpfpvksgscgtVVRNA---------ELKIVDPEtGASLPRN 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 378 EVGVITTRGPYTINAYFAPDEVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVK 457
Cdd:PLN02246  382 QPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIA 461
                         490
                  ....*....|....
gi 1436945972 458 DVLVTGVPDELLGE 471
Cdd:PLN02246  462 DAAVVPMKDEVAGE 475
PRK07529 PRK07529
AMP-binding domain protein; Validated
23-471 4.78e-40

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 153.57  E-value: 4.78e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  23 ESLFEFFERSCQKFATNTAL--VLGEDE------VSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLY 94
Cdd:PRK07529   25 ASTYELLSRAAARHPDAPALsfLLDADPldrpetWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGE 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  95 YLG-ALPI-FCLDGHrsyEIGHIAKFSQARVYLRLcKHESDS----TAEQIIHHfsgdLPHLEIIKTVFQGE-LPQCDGD 167
Cdd:PRK07529  105 AAGiANPInPLLEPE---QIAELLRAAGAKVLVTL-GPFPGTdiwqKVAEVLAA----LPELRTVVEVDLARyLPGPKRL 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 168 RSKLKEKTHY------------QPVDSRA---------VAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTK 226
Cdd:PRK07529  177 AVPLIRRKAHarildfdaelarQPGDRLFsgrpigpddVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDT 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 227 HLLVLPVSHNFPmSSPGFLGVIYAGATLVIAdnsSPT---------ECFGLIERHKITQTSLVPSLVVAWLNSAmIDKFD 297
Cdd:PRK07529  257 VFCGLPLFHVNA-LLVTGLAPLARGAHVVLA---TPQgyrgpgviaNFWKIVERYRINFLSGVPTVYAALLQVP-VDGHD 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 298 LSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAEGLVNYTRLDDNREVQINTQGKRLSDFD-EIQILDLEGKVL-- 374
Cdd:PRK07529  332 ISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPDGERRIGSVGLRLPYQRvRVVILDDAGRYLrd 411
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 375 -GVGEVGVITTRGPYTINAYFAPDEvNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAH 453
Cdd:PRK07529  412 cAVDEVGVLCIAGPNVFSGYLEAAH-NKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRH 490
                         490
                  ....*....|....*...
gi 1436945972 454 PDVKDVLVTGVPDELLGE 471
Cdd:PRK07529  491 PAVALAAAVGRPDAHAGE 508
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
191-522 1.25e-39

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: 147.24  E-value: 1.25e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 191 SGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHNFPmSSPGFLGVIYAGATLVIADNS---SPT---E 264
Cdd:cd05944    10 TGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNG-SVVTLLTPLASGAHVVLAGPAgyrNPGlfdN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 265 CFGLIERHKITQTSLVPSLVVAWLnsAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAEGLVNYTRLD 344
Cdd:cd05944    89 FWKLVERYRITSLSTVPTVYAALL--QVPVNADISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNP 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 345 DNREVQINTQGKRLSDFD-EIQILDLEGKVL---GVGEVGVITTRGPYTINAYFApDEVNKRSFTEDGFYITGDLGYLDE 420
Cdd:cd05944   167 PDGPKRPGSVGLRLPYARvRIKVLDGVGRLLrdcAPDEVGEICVAGPGVFGGYLY-TEGNKNAFVADGWLNTGDLGRLDA 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 421 NNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEkICVQIITDKPDNFNLVKVRKYLTQQHIA 500
Cdd:cd05944   246 DGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGE-LPVAYVQLKPGAVVEEEELLAWARDHVP 324
                         330       340
                  ....*....|....*....|...
gi 1436945972 501 LN-KLPDVVSVVDEFDFTLIGKV 522
Cdd:cd05944   325 ERaAVPKHIEVLEELPVTAVGKV 347
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
50-524 8.57e-39

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: 146.82  E-value: 8.57e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  50 SYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGAlPIFCLDGHRS-YEIGHIAKFSQARVYLRLC 128
Cdd:TIGR01923   1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGA-EIAMLNTRLTeNERTNQLEDLDVQLLLTDS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 129 KHESDSTAEQIIHHFSGDLPHLEIIKTVFQGELPqcdgdrsklkekthyqpvdsravAFLQLSGGTTGLPKLIPRTHDDY 208
Cdd:TIGR01923  80 LLEEKDFQADSLDRIEAAGRYETSLSASFNMDQI-----------------------ATLMFTSGTTGKPKAVPHTFRNH 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 209 LYSVRESAVVANLQQDTKHLLVLPVSHnfpMSSPGFL-GVIYAGATLVIADNSSptECFGLIERHKITQTSLVPSLvvaw 287
Cdd:TIGR01923 137 YASAVGSKENLGFTEDDNWLLSLPLYH---ISGLSILfRWLIEGATLRIVDKFN--QLLEMIANERVTHISLVPTQ---- 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 288 LNSAMIDKFDLSSLEVVQVGGAKFSSELAaRLLDTLDLTLQQVYGMAEG---LVNYTRLDDNREVQINtqgkRLSDFDEI 364
Cdd:TIGR01923 208 LNRLLDEGGHNENLRKILLGGSAIPAPLI-EEAQQYGLPIYLSYGMTETcsqVTTATPEMLHARPDVG----RPLAGREI 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 365 QIldlegKVLGVGEVGVITTRGPYTINAYFAPDEVNKrSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPS 444
Cdd:TIGR01923 283 KI-----KVDNKEGHGEIMVKGANLMKGYLYQGELTP-AFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPE 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 445 EIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPdnFNLVKVRKYLTqQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:TIGR01923 357 EIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESD--ISQAKLIAYLT-EKLAKYKVPIAFEKLDELPYNASGKILR 433
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
40-524 2.48e-38

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 146.65  E-value: 2.48e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  40 TALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGALPIFcldghrsyeighiakfs 119
Cdd:PRK03640   19 TAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVL----------------- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 120 qarVYLRLCKHE-----SDSTAEQIIhhFSGDLPH-LEIIKTVFQGELPQcdgdrSKLKEKTHYQPVDSRAVAFLQLSGG 193
Cdd:PRK03640   82 ---LNTRLSREEllwqlDDAEVKCLI--TDDDFEAkLIPGISVKFAELMN-----GPKEEAEIQEEFDLDEVATIMYTSG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 194 TTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHnfpMS--SPGFLGVIYaGATLVIADNSSPTECFGLIER 271
Cdd:PRK03640  152 TTGKPKGVIQTYGNHWWSAVGSALNLGLTEDDCWLAAVPIFH---ISglSILMRSVIY-GMRVVLVEKFDAEKINKLLQT 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 272 HKITQTSLVPSLVvawlnSAMIDKFDL----SSLEVVQVGG---AKFSSELAARLLDTLDLTlqqvYGMAEGLVNYTRLD 344
Cdd:PRK03640  228 GGVTIISVVSTML-----QRLLERLGEgtypSSFRCMLLGGgpaPKPLLEQCKEKGIPVYQS----YGMTETASQIVTLS 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 345 -DNREVQINTQGKRLsdFD-EIQILDlEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFtEDGFYITGDLGYLDENN 422
Cdd:PRK03640  299 pEDALTKLGSAGKPL--FPcELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEG 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 423 NITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPdnFNLVKVRKYLtQQHIALN 502
Cdd:PRK03640  375 FLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGE--VTEEELRHFC-EEKLAKY 451
                         490       500
                  ....*....|....*....|..
gi 1436945972 503 KLPDVVSVVDEFDFTLIGKVRR 524
Cdd:PRK03640  452 KVPKRFYFVEELPRNASGKLLR 473
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
188-524 5.82e-38

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: 145.21  E-value: 5.82e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 188 LQLSGGTTGLPKLIPRTHDDYLYS---VRESAVVANLQQDTKHLLVLPVSHNFPMSSpgFLGVIYAGATLVIADNSSPTE 264
Cdd:cd05929   130 MLYSGGTTGRPKGIKRGLPGGPPDndtLMAAALGFGPGADSVYLSPAPLYHAAPFRW--SMTALFMGGTLVLMEKFDPEE 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 265 CFGLIERHKITQTSLVPSLVV--AWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAEGlvnytr 342
Cdd:cd05929   208 FLRLIERYRVTFAQFVPTMFVrlLKLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEG------ 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 343 lddNREVQINTQ---------GKRLSDfdEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEvNKRSFTEDGFYITG 413
Cdd:cd05929   282 ---QGLTIINGEewlthpgsvGRAVLG--KVHILDEDGNEVPPGEIGEVYFANGPGFEYTNDPEK-TAAARNEGGWSTLG 355
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 414 DLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKI--CVQIITDKPDNFNLVK-- 489
Cdd:cd05929   356 DVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVhaVVQPAPGADAGTALAEel 435
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1436945972 490 ---VRKYLTQQhialnKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd05929   436 iafLRDRLSRY-----KCPRSIEFVAELPRDDTGKLYR 468
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
48-524 1.24e-37

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: 143.26  E-value: 1.24e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  48 EVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGALPIFcldghrsyeighiakfsqarVYLRL 127
Cdd:cd05912     1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVL--------------------LNTRL 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 128 CKHEsdsTAEQIIhhfsgdlphleiiktvfqgelpqcDGDrsklkekthyqpVDSRAVAFLQLSGGTTGLPKLIPRTHDD 207
Cdd:cd05912    61 TPNE---LAFQLK------------------------DSD------------VKLDDIATIMYTSGTTGKPKGVQQTFGN 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 208 YLYSVRESAVVANLQQDTKHLLVLPVSHnfpMS--SPGFLGVIYaGATLVIADNSSPTECFGLIERHKITQTSLVPSLVv 285
Cdd:cd05912   102 HWWSAIGSALNLGLTEDDNWLCALPLFH---ISglSILMRSVIY-GMTVYLVDKFDAEQVLHLINSGKVTIISVVPTML- 176
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 286 AWLNSAMIDKFDlSSLEVVQVGGAKFSSELAARLLDTLDLTLQQvYGMAEG---LVNYTRLDdnREVQINTQGKRLSDFd 362
Cdd:cd05912   177 QRLLEILGEGYP-NNLRCILLGGGPAPKPLLEQCKEKGIPVYQS-YGMTETcsqIVTLSPED--ALNKIGSAGKPLFPV- 251
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 363 EIQILDLEGKVLGVGEvgvITTRGPYTINAYFAPDEVNKRSFtEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIM 442
Cdd:cd05912   252 ELKIEDDGQPPYEVGE---ILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIY 327
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 443 PSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPdnFNLVKVRKYLtQQHIALNKLPDVVSVVDEFDFTLIGKV 522
Cdd:cd05912   328 PAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERP--ISEEELIAYC-SEKLAKYKVPKKIYFVDELPRTASGKL 404

                  ..
gi 1436945972 523 RR 524
Cdd:cd05912   405 LR 406
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
46-524 3.51e-37

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: 142.05  E-value: 3.51e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  46 EDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGALPIfCLDGHRSYEIGhiakfsqarvyl 125
Cdd:cd05934     1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLV-PINTALRGDEL------------ 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 126 rlckhesdstaEQIIHHfSGdlPHLEIIKTVfqgelpqcdgdrsklkekthyqpvdsravAFLQLSGgTTGLPKLIPRTH 205
Cdd:cd05934    68 -----------AYIIDH-SG--AQLVVVDPA-----------------------------SILYTSG-TTGPPKGVVITH 103
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 206 DDYLYSVRESAVVANLQQDTKHLLVLPVSHNFPMSSpGFLGVIYAGATLVIADNSSPTECFGLIERHKITQTSLVPSLVV 285
Cdd:cd05934   104 ANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAV-SVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLS 182
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 286 AWLnsAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAEglVNYTRLDDNREVQINTQGKRLSDFDEIQ 365
Cdd:cd05934   183 YLL--AQPPSPDDRAHRLRAAYGAPNPPELHEEFEERFGVRLLEGYGMTE--TIVGVIGPRDEPRRPGSIGRPAPGYEVR 258
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 366 ILDLEGKVLGVGEVG--VITTRGPYTINA-YFAPDEVNKRSFtEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIM 442
Cdd:cd05934   259 IVDDDGQELPAGEPGelVIRGLRGWGFFKgYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENIS 337
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 443 PSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPDNFNLVKVRKYLTQQhIALNKLPDVVSVVDEFDFTLIGKV 522
Cdd:cd05934   338 SAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQ-LAYFKVPRYIRFVDDLPKTPTEKV 416

                  ..
gi 1436945972 523 RR 524
Cdd:cd05934   417 AK 418
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
40-524 3.89e-37

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


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 144.48  E-value: 3.89e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  40 TALV-LGED----EVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGALPIFCLDGHRSYEIGH 114
Cdd:COG0365    26 VALIwEGEDgeerTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALAD 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 115 IAKFSQARV------YLRLCK-HESDSTAEQIIhhfsGDLPHLEIIkTVFQGELPQC--DGDRS------KLKEKTHYQP 179
Cdd:COG0365   106 RIEDAEAKVlitadgGLRGGKvIDLKEKVDEAL----EELPSLEHV-IVVGRTGADVpmEGDLDwdellaAASAEFEPEP 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 180 VDSRAVAFLQLSGGTTGLPKLIPRTHDDYLysvresavvanLQQDTKHLLVLPVSHN---FPMSSPGF--------LGVI 248
Cdd:COG0365   181 TDADDPLFILYTSGTTGKPKGVVHTHGGYL-----------VHAATTAKYVLDLKPGdvfWCTADIGWatghsyivYGPL 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 249 YAGATLVIADNS----SPTECFGLIERHKITQTSLVPSLVVAWLNS--AMIDKFDLSSLEVVQVGGAKFSSELAARLLDT 322
Cdd:COG0365   250 LNGATVVLYEGRpdfpDPGRLWELIEKYGVTVFFTAPTAIRALMKAgdEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEA 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 323 LDLTLQQVYGMAE---GLVNYTRLDDNREVQIntqGKRLSDFDeIQILDLEGKVLGVGEVGVITTRGPY----------- 388
Cdd:COG0365   330 VGVPIVDGWGQTEtggIFISNLPGLPVKPGSM---GKPVPGYD-VAVVDEDGNPVPPGEEGELVIKGPWpgmfrgywndp 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 389 --TINAYFApdevnkrsfTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPD 466
Cdd:COG0365   406 erYRETYFG---------RFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPD 476
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1436945972 467 ELLGEKIC--VQIITDKPDNFNLVK-----VRKyltqqHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:COG0365   477 EIRGQVVKafVVLKPGVEPSDELAKelqahVRE-----ELGPYAYPREIEFVDELPKTRSGKIMR 536
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
184-524 7.17e-37

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: 139.00  E-value: 7.17e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 184 AVAFLQLSGGTTGLPKLIPRTHDDYLYSVResAVVANLQQD--TKHLLVLPVSHnfpmssPGFLGVI----YAGATLVIa 257
Cdd:cd17630     1 RLATVILTSGSTGTPKAVVHTAANLLASAA--GLHSRLGFGggDSWLLSLPLYH------VGGLAILvrslLAGAELVL- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 258 dnssPTECFGLIERH---KITQTSLVPslvvAWLNSAMIDKFD---LSSLEVVQVGGAKFSSELAARLLDTLDLTLQqVY 331
Cdd:cd17630    72 ----LERNQALAEDLappGVTHVSLVP----TQLQRLLDSGQGpaaLKSLRAVLLGGAPIPPELLERAADRGIPLYT-TY 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 332 GMAE--GLVNYTRLDDNREvqiNTQGKRLsDFDEIQILDlegkvlgvgeVGVITTRGPYTINAYFAPDEVNKrsFTEDGF 409
Cdd:cd17630   143 GMTEtaSQVATKRPDGFGR---GGVGVLL-PGRELRIVE----------DGEIWVGGASLAMGYLRGQLVPE--FNEDGW 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 410 YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPdnFNLVK 489
Cdd:cd17630   207 FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGP--ADPAE 284
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1436945972 490 VRKYLtQQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd17630   285 LRAWL-KDKLARFKLPKRIYPVPELPRTGGGKVDR 318
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
180-524 2.27e-36

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: 139.78  E-value: 2.27e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 180 VDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHllvlpvshnFPMSSPG--------FLGVIYAG 251
Cdd:cd05972    78 TDAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIH---------WNIADPGwakgawssFFGPWLLG 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 252 ATLVI--ADNSSPTECFGLIERHKITQTSLVPSLVVAWLnSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQ 329
Cdd:cd05972   149 ATVFVyeGPRFDAERILELLERYGVTSFCGPPTAYRMLI-KQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRD 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 330 VYGMAE-GLVNYTRLDdnREVQINTQGKRLSDFDeIQILDLEGKVLGVGEVGVITTR-GPYTINAYFAPDEVNKRSFTED 407
Cdd:cd05972   228 GYGQTEtGLTVGNFPD--MPVKPGSMGRPTPGYD-VAIIDDDGRELPPGEEGDIAIKlPPPGLFLGYVGDPEKTEASIRG 304
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 408 GFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGE--KICVQIITDKPDNF 485
Cdd:cd05972   305 DYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEvvKAFVVLTSGYEPSE 384
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1436945972 486 NLVKVRKYLTQQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd05972   385 ELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRR 423
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
6-524 2.65e-36

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


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 142.09  E-value: 2.65e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972   6 FPQERAETyIAnglWQGESLFEFFERSCQKFATNTAL-VLGEDeVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVL 84
Cdd:PRK06710   11 YPEEIPST-IS---YDIQPLHKYVEQMASRYPEKKALhFLGKD-ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  85 EFFYVLFGLYYLGALPIFCLDGHRSYEIGHIAKFSQARVYL-------RLCKHESDSTAEQIIHHFSGDL---------P 148
Cdd:PRK06710   86 QAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILcldlvfpRVTNVQSATKIEHVIVTRIADFlpfpknllyP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 149 HLE-----IIKTVFQGELPQCDGDRSKLKEKTHYQPVD-SRAVAFLQLSGGTTGLPKLIPRTHDD----------YLYSV 212
Cdd:PRK06710  166 FVQkkqsnLVVKVSESETIHLWNSVEKEVNTGVEVPCDpENDLALLQYTGGTTGFPKGVMLTHKNlvsntlmgvqWLYNC 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 213 RESAVVAnlqqdtkhLLVLPVSHNFPMSSPGFLGVIyAGATLVIADNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAM 292
Cdd:PRK06710  246 KEGEEVV--------LGVLPFFHVYGMTAVMNLSIM-QGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPL 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 293 IDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAEGL-VNYTRLDDNREVQiNTQGKRLSDFDEiQILDLE- 370
Cdd:PRK06710  317 LKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSpVTHSNFLWEKRVP-GSIGVPWPDTEA-MIMSLEt 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 371 GKVLGVGEVGVITTRGPYTINAYF-APDEVnkRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEEL 449
Cdd:PRK06710  395 GEALPPGEIGEIVVKGPQIMKGYWnKPEET--AAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEV 472
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1436945972 450 LYAHPDVKDVLVTGVPDELLGEKICVQIITDKPDNFNLVKVRKYlTQQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:PRK06710  473 LYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQF-ARKYLAAYKVPKVYEFRDELPKTTVGKILR 546
PRK06164 PRK06164
acyl-CoA synthetase; Validated
40-524 1.01e-35

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 139.88  E-value: 1.01e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  40 TALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGALPIFCLDGHRSYEIGHIAKFS 119
Cdd:PRK06164   27 VALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRG 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 120 QARVY--------------LRLCKHESDSTAEQII--HHFSGDLP-HLEIIKT-VFQGELP---QCDGDRSklkekthyQ 178
Cdd:PRK06164  107 RARWLvvwpgfkgidfaaiLAAVPPDALPPLRAIAvvDDAADATPaPAPGARVqLFALPDPappAAAGERA--------A 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 179 PVDSRAVAFLqlSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHNFPMSspGFLGVIYAGATLVIAD 258
Cdd:PRK06164  179 DPDAGALLFT--TSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFS--TLLGALAGGAPLVCEP 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 259 NSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKfDLSSLEVVqvGGAKFS---SELAARLLDTLDLTLQqVYGMAE 335
Cdd:PRK06164  255 VFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERA-DFPSARLF--GFASFApalGELAALARARGVPLTG-LYGSSE 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 336 --GLVNYTRLDDNREVQINTQGKRLSDFDEIQILD-LEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGFYIT 412
Cdd:PRK06164  331 vqALVALQPATDPVSVRIEGGGRPASPEARVRARDpQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRT 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 413 GDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVpdELLGEKICVQ--IITD--KPDNFNLV 488
Cdd:PRK06164  411 GDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKTVPVAfvIPTDgaSPDEAGLM 488
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 1436945972 489 KVrkylTQQHIALNKLPDVVSVVDEFDFTLIG---KVRR 524
Cdd:PRK06164  489 AA----CREALAGFKVPARVQVVEAFPVTESAngaKIQK 523
PRK08316 PRK08316
acyl-CoA synthetase; Validated
31-467 5.22e-35

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 137.76  E-value: 5.22e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  31 RSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGA--LPI-FCLDGH 107
Cdd:PRK08316   19 RSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAvhVPVnFMLTGE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 108 rsyEIGHIAKFSQARVYLrlckHESD--STAEQIihhfSGDLPHLEIIKTVFQGELPQCDGDRSKLKEKTHYQP------ 179
Cdd:PRK08316   99 ---ELAYILDHSGARAFL----VDPAlaPTAEAA----LALLPVDTLILSLVLGGREAPGGWLDFADWAEAGSVaepdve 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 180 VDSRAVAFLQLSGGTTGLPKLIPRTHD----DYLysvreSAVVA-NLQQDTKHLLVLPVSHNFPMSSpgFLG-VIYAGAT 253
Cdd:PRK08316  168 LADDDLAQILYTSGTESLPKGAMLTHRaliaEYV-----SCIVAgDMSADDIPLHALPLYHCAQLDV--FLGpYLYVGAT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 254 LVIADNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFS----SELAARLLDTLDLTLqq 329
Cdd:PRK08316  241 NVILDAPDPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPvevlKELRERLPGLRFYNC-- 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 330 vYGMAE--GLVNYTRLDDNREvQINTQGkRLSDFDEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFtED 407
Cdd:PRK08316  319 -YGQTEiaPLATVLGPEEHLR-RPGSAG-RPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF-RG 394
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 408 GFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDE 467
Cdd:PRK08316  395 GWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDP 454
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
23-524 6.89e-35

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: 136.87  E-value: 6.89e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  23 ESLFEFFERSCQKFATNTALVL--GEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGALP 100
Cdd:cd05923     1 QTVFEMLRRAASRAPDACAIADpaRGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 101 IFCLDGHRSYEIGHIAKFSQARVYLRlckhesdstaeqiihhfSGDLPHLEIIKTVFQGELPQcdGDRSKLKEKTHYQPV 180
Cdd:cd05923    81 ALINPRLKAAELAELIERGEMTAAVI-----------------AVDAQVMDAIFQSGVRVLAL--SDLVGLGEPESAGPL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 181 ------DSRAVAFLQLSGGTTGLPK--LIPRTHddylysvRESAVVA------NLQQDTKHLL-VLPVSHNFpmsspGFL 245
Cdd:cd05923   142 iedpprEPEQPAFVFYTSGTTGLPKgaVIPQRA-------AESRVLFmstqagLRHGRHNVVLgLMPLYHVI-----GFF 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 246 GVIYA----GATLVIADNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLD 321
Cdd:cd05923   210 AVLVAalalDGTYVVVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQ 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 322 TLDLTLQQVYGMAEGLvNYTRLDDNRevqintQGKRLSD--FDEIQILDLEGKV---LGVGEVG--VITTRGPYTINAYF 394
Cdd:cd05923   290 HLPGEKVNIYGTTEAM-NSLYMRDAR------TGTEMRPgfFSEVRIVRIGGSPdeaLANGEEGelIVAAAADAAFTGYL 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 395 APDEVNKRSFtEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGeKIC 474
Cdd:cd05923   363 NQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWG-QSV 440
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 1436945972 475 VQIITDKPDNFNLVKVRKYLTQQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd05923   441 TACVVPREGTLSADELDQFCRASELADFKRPRRYFFLDELPKNAMNKVLR 490
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
21-471 1.89e-34

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


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 136.69  E-value: 1.89e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  21 QGESLFEFFERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGAL- 99
Cdd:PRK07059   21 QYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVv 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 100 ----PIFCldghrSYEIGHIAKFSQARVYLRLckhES-DSTAEQIIHHFS---------GDLPHLE----------IIKT 155
Cdd:PRK07059  101 vnvnPLYT-----PRELEHQLKDSGAEAIVVL---ENfATTVQQVLAKTAvkhvvvasmGDLLGFKghivnfvvrrVKKM 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 156 VFQGELPQC--------DGDRSKLKeKTHYQPVDsraVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAV----VANLQQ 223
Cdd:PRK07059  173 VPAWSLPGHvrfndalaEGARQTFK-PVKLGPDD---VAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAwlqpAFEKKP 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 224 DTKHLLV---LPVSHNFPMSSPGFLGVIYAGATLVIADnssPTECFGLIERHKITQTSLVP---SLVVAWLNSAMIDKFD 297
Cdd:PRK07059  249 RPDQLNFvcaLPLYHIFALTVCGLLGMRTGGRNILIPN---PRDIPGFIKELKKYQVHIFPavnTLYNALLNNPDFDKLD 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 298 LSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAEG--LVNYTRLDDNREVqiNTQGKRLSDfDEIQILDLEGKVLG 375
Cdd:PRK07059  326 FSKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETspVATCNPVDATEFS--GTIGLPLPS-TEVSIRDDDGNDLP 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 376 VGEVGVITTRGPYTINAYFA-PDEvNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHP 454
Cdd:PRK07059  403 LGEPGEICIRGPQVMAGYWNrPDE-TAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHP 481
                         490
                  ....*....|....*..
gi 1436945972 455 DVKDVLVTGVPDELLGE 471
Cdd:PRK07059  482 GVLEVAAVGVPDEHSGE 498
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
38-524 2.29e-34

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 135.37  E-value: 2.29e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  38 TNTALVLGEDEVSYEAFYFKALAWGEWL-HEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGA----LPIFCLDGHRSYEI 112
Cdd:PRK06839   17 DRIAIITEEEEMTYKQLHEYVSKVAAYLiYELNVKKGERIAILSQNSLEYIVLLFAIAKVECiavpLNIRLTENELIFQL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 113 ghiaKFSQARVYLrlCKHESDSTAEQIIHHFSgdLPHLEIIKTVFQGElpqcDGDRSKLKEKTHYQPVdsravaFLQLSG 192
Cdd:PRK06839   97 ----KDSGTTVLF--VEKTFQNMALSMQKVSY--VQRVISITSLKEIE----DRKIDNFVEKNESASF------IICYTS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 193 GTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSH-------NFPmsspgflgVIYAGATLVIADNSSPTEC 265
Cdd:PRK06839  159 GTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHiggiglfAFP--------TLFAGGVIIVPRKFEPTKA 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 266 FGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAaRLLDTLDLTLQQVYGMAE-GLVNYTRLD 344
Cdd:PRK06839  231 LSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELM-REFIDRGFLFGQGFGMTEtSPTVFMLSE 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 345 DNREVQINTQGKRLSdFDEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFtEDGFYITGDLGYLDENNNI 424
Cdd:PRK06839  310 EDARRKVGSIGKPVL-FCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFV 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 425 TVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEkICVQIITDKPDNFNLVKVRKYLTQQHIALNKL 504
Cdd:PRK06839  388 YIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGE-IPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKI 466
                         490       500
                  ....*....|....*....|
gi 1436945972 505 PDVVSVVDEFDFTLIGKVRR 524
Cdd:PRK06839  467 PKEIVFLKELPKNATGKIQK 486
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
65-524 2.31e-34

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: 134.88  E-value: 2.31e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  65 LHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLG-ALPIFCLD---GHRSYEIGHIAKFSQARVYLrlckheSDSTAEQii 140
Cdd:cd05922    10 LLEAGGVRGERVVLILPNRFTYIELSFAVAYAGgRLGLVFVPlnpTLKESVLRYLVADAGGRIVL------ADAGAAD-- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 141 hHFSGDLPHLEIIKTVFQGElpQCDGDRSKLKEkthyQPVDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVAN 220
Cdd:cd05922    82 -RLRDALPASPDPGTVLDAD--GIRAARASAPA----HEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 221 LQQDTKHLLVLPVSHNFPMSSpgFLGVIYAGATLVIADNSSPTECF-GLIERHKITQTSLVPSLVvAWLNSAMIDKFDLS 299
Cdd:cd05922   155 ITADDRALTVLPLSYDYGLSV--LNTHLLRGATLVLTNDGVLDDAFwEDLREHGATGLAGVPSTY-AMLTRLGFDPAKLP 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 300 SLEVVQVGGAKFSSELAARLLDTLDLTLQQV-YGMAEGLVNYTRLDDNREV-QINTQGKRLSDfDEIQILDLEGKVLGVG 377
Cdd:cd05922   232 SLRYLTQAGGRLPQETIARLRELLPGAQVYVmYGQTEATRRMTYLPPERILeKPGSIGLAIPG-GEFEILDDDGTPTPPG 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 378 EVGVITTRGPYTINAYF-APDEVNKRSFTEDGFYiTGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDV 456
Cdd:cd05922   311 EPGEIVHRGPNVMKGYWnDPPYRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI 389
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1436945972 457 KDVLVTGVPDElLGEKICVQIITdkPDNFNLVKVRKYLTQQhIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd05922   390 IEAAAVGLPDP-LGEKLALFVTA--PDKIDPKDVLRSLAER-LPPYKVPATVRVVDELPLTASGKVDY 453
PRK06188 PRK06188
acyl-CoA synthetase; Validated
185-524 2.87e-34

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 135.50  E-value: 2.87e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 185 VAFLQLSGGTTGLPKLIPRTHddylysvRESAVVANLQ-------QDTKHLLVLPVSHnfpMSSPGFLGVIYAGATLVIA 257
Cdd:PRK06188  170 IAGLAYTGGTTGKPKGVMGTH-------RSIATMAQIQlaewewpADPRFLMCTPLSH---AGGAFFLPTLLRGGTVIVL 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 258 DNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAEGL 337
Cdd:PRK06188  240 AKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAP 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 338 VNYTRLDdnREVQINTQGKRLSD------FDEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFtEDGFYI 411
Cdd:PRK06188  320 MVITYLR--KRDHDPDDPKRLTScgrptpGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-RDGWLH 396
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 412 TGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGE--KICVQIITD-KPDN---F 485
Cdd:PRK06188  397 TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEavTAVVVLRPGaAVDAaelQ 476
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1436945972 486 NLVKVRKYLTQQhialnklPDVVSVVDEFDFTLIGKVRR 524
Cdd:PRK06188  477 AHVKERKGSVHA-------PKQVDFVDSLPLTALGKPDK 508
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
180-522 5.30e-34

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: 134.68  E-value: 5.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 180 VDSRAVAFLQLSGGTTGLPKLIprthddyLYSVRE---------SAVVANLQQDTKHLLVLPVSH----NFPMSSPgflg 246
Cdd:cd12119   160 FDENTAAAICYTSGTTGNPKGV-------VYSHRSlvlhamaalLTDGLGLSESDVVLPVVPMFHvnawGLPYAAA---- 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 247 viYAGATLVIAD-NSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDL 325
Cdd:cd12119   229 --MVGAKLVLPGpYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEERGVR 306
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 326 TLQqVYGMAE----GLVNYTR---LDDNREVQIN---TQGkRLSDFDEIQILDLEGKVL-----GVGEVGVittRGPYTI 390
Cdd:cd12119   307 VIH-AWGMTEtsplGTVARPPsehSNLSEDEQLAlraKQG-RPVPGVELRIVDDDGRELpwdgkAVGELQV---RGPWVT 381
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 391 NAYFAPDEvNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLG 470
Cdd:cd12119   382 KSYYKNDE-ESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWG 460
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1436945972 471 EKIcVQIITDKPD-NFNLVKVRKYLTQqhiALNK--LPDVVSVVDEFDFTLIGKV 522
Cdd:cd12119   461 ERP-LAVVVLKEGaTVTAEELLEFLAD---KVAKwwLPDDVVFVDEIPKTSTGKI 511
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
49-524 3.92e-33

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: 131.18  E-value: 3.92e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  49 VSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGALPIfcldghrsyeighiakfsqaRVYlrlc 128
Cdd:cd05907     6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPV--------------------PIY---- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 129 kheSDSTAEQIiHHFsgdLPHLEIiKTVFQGElpqcdgdrsklkekthyqPVDsraVAFLQLSGGTTGLPKLIPRTHDDY 208
Cdd:cd05907    62 ---PTSSAEQI-AYI---LNDSEA-KALFVED------------------PDD---LATIIYTSGTTGRPKGVMLSHRNI 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 209 LYSVRESAVVANLQQDTKHLLVLPVSHNFPMSSpGFLGVIYAGATLVIAdnSSPTECFGLIERHKITQTSLVPSLV---- 284
Cdd:cd05907   113 LSNALALAERLPATEGDRHLSFLPLAHVFERRA-GLYVPLLAGARIYFA--SSAETLLDDLSEVRPTVFLAVPRVWekvy 189
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 285 -------VAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAaRLLDTLDLTLQQVYGMAE--GLVNYTRLDDNRevqINTQG 355
Cdd:cd05907   190 aaikvkaVPGLKRKLFDLAVGGRLRFAASGGAPLPAELL-HFFRALGIPVYEGYGLTEtsAVVTLNPPGDNR---IGTVG 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 356 KRLSDFdEIQIldlegkvlgvGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVI- 434
Cdd:cd05907   266 KPLPGV-EVRI----------ADDGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIi 334
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 435 NRAGEKIMPSEIEELLYAHPDVKDVLVTG----------VPDELLGEKICVQIITDKPDNFNLVK---VRKYLTQQHIAL 501
Cdd:cd05907   335 TSGGKNISPEPIENALKASPLISQAVVIGdgrpflvaliVPDPEALEAWAEEHGIAYTDVAELAAnpaVRAEIEAAVEAA 414
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 1436945972 502 NK-LPDVVSV-----------VDEFDFTLIGKVRR 524
Cdd:cd05907   415 NArLSRYEQIkkflllpepftIENGELTPTLKLKR 449
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
64-473 4.67e-33

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


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 131.95  E-value: 4.67e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  64 WLHEQGVRKDDLVVLQSANVLEFFYVLF-----GLYYLgalpifCLDGHRSY-EIGHIAKFSQARVylrLCKHES-DSTA 136
Cdd:PRK08276   27 GLRALGLREGDVVAILLENNPEFFEVYWaarrsGLYYT------PINWHLTAaEIAYIVDDSGAKV---LIVSAAlADTA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 137 EQIIHHFSGDLPHLeiikTVFQGELPQCDGDRSKLKEKTHYQPVDSRAVAFLQLSGGTTGLPKLI--PRTHDDYLYSVRE 214
Cdd:PRK08276   98 AELAAELPAGVPLL----LVVAGPVPGFRSYEEALAAQPDTPIADETAGADMLYSSGTTGRPKGIkrPLPGLDPDEAPGM 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 215 SAVVANLQ----QDTKHLLVLPVSH----NFPMSspgflgVIYAGATLVIADNSSPTECFGLIERHKITQTSLVPSLVVA 286
Cdd:PRK08276  174 MLALLGFGmyggPDSVYLSPAPLYHtaplRFGMS------ALALGGTVVVMEKFDAEEALALIERYRVTHSQLVPTMFVR 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 287 WLN--SAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAEGlvnytrlddNREVQINTQ---------G 355
Cdd:PRK08276  248 MLKlpEEVRARYDVSSLRVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSEG---------GGVTVITSEdwlahpgsvG 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 356 KRLsdFDEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVIN 435
Cdd:PRK08276  319 KAV--LGEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMII 396
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1436945972 436 RAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKI 473
Cdd:PRK08276  397 SGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERV 434
PRK06178 PRK06178
acyl-CoA synthetase; Validated
63-524 2.64e-32

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 130.55  E-value: 2.64e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  63 EWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGAL-----PIFcldghRSYEIGHIAKFSQARVYLRLckhesDSTAE 137
Cdd:PRK06178   73 ALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVhvpvsPLF-----REHELSYELNDAGAEVLLAL-----DQLAP 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 138 QIIHHfSGDLPHLEIIKTVFQGELP----------------QCDGDRSKLK------EKTHYQPVDSRAVAFLQLSGGTT 195
Cdd:PRK06178  143 VVEQV-RAETSLRHVIVTSLADVLPaeptlplpdslraprlAAAGAIDLLPalractAPVPLPPPALDALAALNYTGGTT 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 196 GLPKLIPRTHDDYLYSVRESAVVA-NLQQDTKHLLVLPV----SHNFpmsspGFLGVIYAGATLVIADNSSPTECFGLIE 270
Cdd:PRK06178  222 GMPKGCEHTQRDMVYTAAAAYAVAvVGGEDSVFLSFLPEfwiaGENF-----GLLFPLFSGATLVLLARWDAVAFMAAVE 296
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 271 RHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEvvQVGGAKFSSELAARLLDTLDLTLQQV-----YGMAEglvnyTRLDD 345
Cdd:PRK06178  297 RYRVTRTVMLVDNAVELMDHPRFAEYDLSSLR--QVRVVSFVKKLNPDYRQRWRALTGSVlaeaaWGMTE-----THTCD 369
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 346 NRevqinTQGKRLSDFD---------------EIQILDLE-GKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFtEDGF 409
Cdd:PRK06178  370 TF-----TAGFQDDDFDllsqpvfvglpvpgtEFKICDFEtGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGW 443
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 410 YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEkICVQIITDKPDNFNLVK 489
Cdd:PRK06178  444 LHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQ-VPVAFVQLKPGADLTAA 522
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 1436945972 490 VRKYLTQQHIALNKLPdVVSVVDEFDFTLIGKVRR 524
Cdd:PRK06178  523 ALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRK 556
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
190-524 5.83e-32

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: 125.21  E-value: 5.83e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 190 LSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHNfpMSSPGFLGVIYAGATLVIADNSSPTECFGLI 269
Cdd:cd17633     7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHS--LFLYGAISALYLGGTFIGQRKFNPKSWIRKI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 270 ERHKITQTSLVPSLVVAWLNSAMIDkfdlSSLEVVQVGGAKFSSELAARLLDTL-DLTLQQVYGMAE-GLVNYTRLDDNR 347
Cdd:cd17633    85 NQYNATVIYLVPTMLQALARTLEPE----SKIKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSElSFITYNFNQESR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 348 EVqiNTQGKRLSDFdEIQILDLEGkvlgvGEVGVITTRGPYTINAYfapdeVNKRSFTEDGFYITGDLGYLDENNNITVT 427
Cdd:cd17633   161 PP--NSVGRPFPNV-EIEIRNADG-----GEIGKIFVKSEMVFSGY-----VRGGFSNPDGWMSVGDIGYVDEEGYLYLV 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 428 GRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEkICVQIITDkpDNFNLVKVRKYLTQQhIALNKLPDV 507
Cdd:cd17633   228 GRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGE-IAVALYSG--DKLTYKQLKRFLKQK-LSRYEIPKK 303
                         330
                  ....*....|....*..
gi 1436945972 508 VSVVDEFDFTLIGKVRR 524
Cdd:cd17633   304 IIFVDSLPYTSSGKIAR 320
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
39-524 2.76e-31

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: 125.72  E-value: 2.76e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  39 NTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGA--LPIfclDghrsyeighiA 116
Cdd:cd05930     3 AVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAayVPL---D----------P 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 117 KFSQARV-YLRlckheSDSTAEQIIHHfSGDLPHleIIKTvfqgelpqcdgdrsklkekthyqpvdsravaflqlSGgTT 195
Cdd:cd05930    70 SYPAERLaYIL-----EDSGAKLVLTD-PDDLAY--VIYT-----------------------------------SG-ST 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 196 GLPKLIPRTHddylysvreSAVVANLQQDTKHLLVLP-------VSHNFPMSSPGFLGVIYAGATLVIADNS---SPTEC 265
Cdd:cd05930   106 GKPKGVMVEH---------RGLVNLLLWMQEAYPLTPgdrvlqfTSFSFDVSVWEIFGALLAGATLVVLPEEvrkDPEAL 176
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 266 FGLIERHKITQTSLVPSLVVAWLNSAmiDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQ-VYGMAEGLVN--YTR 342
Cdd:cd05930   177 ADLLAEEGITVLHLTPSLLRLLLQEL--ELAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVnLYGPTEATVDatYYR 254
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 343 LDDNRE----VQIntqGKRLSDfDEIQILDLEGKVLGVGEVG--VIT----TRGpytinaYFAPDEVNKRSFTEDGF--- 409
Cdd:cd05930   255 VPPDDEedgrVPI---GRPIPN-TRVYVLDENLRPVPPGVPGelYIGgaglARG------YLNRPELTAERFVPNPFgpg 324
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 410 ---YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPDNFN 486
Cdd:cd05930   325 ermYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELD 404
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 1436945972 487 LVKVRKYLTQqhialnKLPD-----VVSVVDEFDFTLIGKVRR 524
Cdd:cd05930   405 EEELRAHLAE------RLPDymvpsAFVVLDALPLTPNGKVDR 441
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
23-524 2.91e-31

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


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 127.48  E-value: 2.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  23 ESLFEFFERSCQKFATNTALV-LGEdEVSYEAFYFKALAWGEWL-HEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGALP 100
Cdd:PRK08974   23 QSLVDMFEQAVARYADQPAFInMGE-VMTFRKLEERSRAFAAYLqNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 101 IFCLDGHRSYEIGHIAKFSQARVYLRLCKHESdsTAEQIIhhFSGDLPHL----------------------EIIKTVFQ 158
Cdd:PRK08974  102 VNVNPLYTPRELEHQLNDSGAKAIVIVSNFAH--TLEKVV--FKTPVKHViltrmgdqlstakgtlvnfvvkYIKRLVPK 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 159 GELPQCDGDRSKLKEKTHYQPV----DSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRES-AVVANLQQDTKHLLV--L 231
Cdd:PRK08974  178 YHLPDAISFRSALHKGRRMQYVkpelVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAkAAYGPLLHPGKELVVtaL 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 232 PVSHNFPMSSPGFLgVIYAGATLVIADNssPTECFGLI---ERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGG 308
Cdd:PRK08974  258 PLYHIFALTVNCLL-FIELGGQNLLITN--PRDIPGFVkelKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGG 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 309 AKFSSELAARLLDTLDLTLQQVYGMAEG--LVNYTRLD-DNREVQI-----NTqgkrlsdfdEIQILDLEGKVLGVGEVG 380
Cdd:PRK08974  335 MAVQQAVAERWVKLTGQYLLEGYGLTECspLVSVNPYDlDYYSGSIglpvpST---------EIKLVDDDGNEVPPGEPG 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 381 VITTRGPYTINAYF----APDEVNKrsfteDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDV 456
Cdd:PRK08974  406 ELWVKGPQVMLGYWqrpeATDEVIK-----DGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKV 480
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1436945972 457 KDVLVTGVPDELLGE--KICVqiitdkpdnfnlVKVRKYLTQ--------QHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:PRK08974  481 LEVAAVGVPSEVSGEavKIFV------------VKKDPSLTEeelithcrRHLTGYKVPKLVEFRDELPKSNVGKILR 546
PRK07788 PRK07788
acyl-CoA synthetase; Validated
40-524 7.02e-31

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 126.20  E-value: 7.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  40 TALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGAlPIFCLDGHRSYEigHIAKFS 119
Cdd:PRK07788   66 AALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGA-RIILLNTGFSGP--QLAEVA 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 120 qARVYLRLCKHESDSTAeqIIHHFSGDLPHLEIIKTVFQGELPQCDGDRSkLKE-----KTHYQPVDSRAVAFLQLSGGT 194
Cdd:PRK07788  143 -AREGVKALVYDDEFTD--LLSALPPDLGRLRAWGGNPDDDEPSGSTDET-LDDliagsSTAPLPKPPKPGGIVILTSGT 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 195 TGLPKLIPRTHddylysVRESAVVANL------QQDTKHLLVLPVSHnfpmsSPGF--LGVIYA-GATLVIADNSSPTEC 265
Cdd:PRK07788  219 TGTPKGAPRPE------PSPLAPLAGLlsrvpfRAGETTLLPAPMFH-----ATGWahLTLAMAlGSTVVLRRRFDPEAT 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 266 FGLIERHKITQTSLVPSLVVAWLNSA--MIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAEglVNYTRL 343
Cdd:PRK07788  288 LEDIAKHKATALVVVPVMLSRILDLGpeVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTE--VAFATI 365
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 344 DDNREVQIN--TQGKRLSDFdEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDevNKRsfTEDGFYITGDLGYLDEN 421
Cdd:PRK07788  366 ATPEDLAEApgTVGRPPKGV-TVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGR--DKQ--IIDGLLSSGDVGYFDED 440
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 422 NNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPDNFNLVKVRKYLtQQHIAL 501
Cdd:PRK07788  441 GLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYV-RDNLAR 519
                         490       500
                  ....*....|....*....|...
gi 1436945972 502 NKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:PRK07788  520 YKVPRDVVFLDELPRNPTGKVLK 542
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
183-524 1.24e-30

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: 121.98  E-value: 1.24e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 183 RAVAFLQLSGGTTGLPKLIPRTHDDyLYSVRESAVVA--NLQQDTKHLLVLPVSHNFPMSSpGFLGVIYAGATLVIADNS 260
Cdd:cd17635     1 EDPLAVIFTSGTTGEPKAVLLANKT-FFAVPDILQKEglNWVVGDVTYLPLPATHIGGLWW-ILTCLIHGGLCVTGGENT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 261 SPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAEgLVNY 340
Cdd:cd17635    79 TYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSE-TGTA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 341 TRLD-DNREVQINTQGKRLSDFDeIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGFYiTGDLGYLD 419
Cdd:cd17635   158 LCLPtDDDSIEINAVGRPYPGVD-VYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWVN-TGDLGERR 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 420 ENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPDNFNLVKVRKYLTQQHI 499
Cdd:cd17635   236 EDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAIRALKHTIRREL 315
                         330       340
                  ....*....|....*....|....*
gi 1436945972 500 ALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd17635   316 EPYARPSTIVIVTDIPRTQSGKVKR 340
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
65-524 1.25e-30

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: 123.77  E-value: 1.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  65 LHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGAL--PIFcldghrsyeighiAKFSQARVYLRLckheSDSTAEQIIHH 142
Cdd:cd05969    17 LKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVicPLF-------------SAFGPEAIRDRL----ENSEAKVLITT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 143 fsgdlphleiiktvfqgelpqcdgdrSKLKEKThyqpvDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQ 222
Cdd:cd05969    80 --------------------------EELYERT-----DPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLH 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 223 QDTKHllvlpvshnFPMSSPGFL-GVIYA-------GATLVIADNS-SPTECFGLIERHKITQTSLVPSLV--VAWLNSA 291
Cdd:cd05969   129 PDDIY---------WCTADPGWVtGTVYGiwapwlnGVTNVVYEGRfDAESWYGIIERVKVTVWYTAPTAIrmLMKEGDE 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 292 MIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAEG----LVNYTRLDdnreVQINTQGKRLSDFdEIQIL 367
Cdd:cd05969   200 LARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETgsimIANYPCMP----IKPGSMGKPLPGV-KAAVV 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 368 DLEGKVLGVGEVGVITTRG--PYTINAYFAPDEVNKRSFTeDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSE 445
Cdd:cd05969   275 DENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSFI-DGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFE 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 446 IEELLYAHPDVKDVLVTGVPDELLGEKIcVQIITDKPDNFNLVKVRKYL---TQQHIALNKLPDVVSVVDEFDFTLIGKV 522
Cdd:cd05969   354 VESALMEHPAVAEAGVIGKPDPLRGEII-KAFISLKEGFEPSDELKEEIinfVRQKLGAHVAPREIEFVDNLPKTRSGKI 432

                  ..
gi 1436945972 523 RR 524
Cdd:cd05969   433 MR 434
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
24-524 1.77e-30

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


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 124.88  E-value: 1.77e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  24 SLFEFFERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWL-HEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGALPIF 102
Cdd:PRK05677   25 NIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLqQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVN 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 103 CLDGHRSYEIGHiaKFSQARVYLRLCKHESDSTAEQIIHHFS---------GD-LPHLE----------IIKTVFQGELP 162
Cdd:PRK05677  105 TNPLYTAREMEH--QFNDSGAKALVCLANMAHLAEKVLPKTGvkhvivtevADmLPPLKrllinavvkhVKKMVPAYHLP 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 163 QCDGDRSKLKeKTHYQPV-----DSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRE-SAVVANLQQDTKHLLV--LPVS 234
Cdd:PRK05677  183 QAVKFNDALA-KGAGQPVteanpQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQcRALMGSNLNEGCEILIapLPLY 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 235 HnfpmsspgflgvIYA-----GATLVIADN----SSPTECFGLIE---RHKITQTSLVPSLVVAWLNSAMIDKFDLSSLE 302
Cdd:PRK05677  262 H------------IYAftfhcMAMMLIGNHniliSNPRDLPAMVKelgKWKFSGFVGLNTLFVALCNNEAFRKLDFSALK 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 303 VVQVGGAKFSSELAARLLDTLDLTLQQVYGMAEG--LVNYTRLDDnreVQINTQGKRLSDfDEIQILDLEGKVLGVGEVG 380
Cdd:PRK05677  330 LTLSGGMALQLATAERWKEVTGCAICEGYGMTETspVVSVNPSQA---IQVGTIGIPVPS-TLCKVIDDDGNELPLGEVG 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 381 VITTRGPYTINAYFAPDEVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVL 460
Cdd:PRK05677  406 ELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCA 485
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1436945972 461 VTGVPDELLGEKICVQIITdKPDnfnlVKVRKYLTQQHIALN----KLPDVVSVVDEFDFTLIGKVRR 524
Cdd:PRK05677  486 AIGVPDEKSGEAIKVFVVV-KPG----ETLTKEQVMEHMRANltgyKVPKAVEFRDELPTTNVGKILR 548
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
191-513 4.31e-30

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: 120.95  E-value: 4.31e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 191 SGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHNFPMS----SP---------GFLGVIYAGATLVIA 257
Cdd:cd05924    11 TGGTTGMPKGVMWRQEDIFRMLMGGADFGTGEFTPSEDAHKAAAAAAGTVmfpaPPlmhgtgswtAFGGLLGGQTVVLPD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 258 DNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDK--FDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQ-VYGMA 334
Cdd:cd05924    91 DRFDPEEVWRTIEKHKVTSMTIVGDAMARPLIDALRDAgpYDLSSLFAISSGGALLSPEVKQGLLELVPNITLVdAFGSS 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 335 EGLVNYTRLDDNRevqINTQGKRLSDFDEIQILDLEGKVL--GVGEVGVITTRGpYTINAYFAPDEVNKRSFTE-DG--F 409
Cdd:cd05924   171 ETGFTGSGHSAGS---GPETGPFTRANPDTVVLDDDGRVVppGSGGVGWIARRG-HIPLGYYGDEAKTAETFPEvDGvrY 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 410 YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPDNFNLVK 489
Cdd:cd05924   247 AVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREGAGVDLEE 326
                         330       340
                  ....*....|....*....|....
gi 1436945972 490 VRKYLTQQhIALNKLPDVVSVVDE 513
Cdd:cd05924   327 LREHCRTR-IARYKLPKQVVFVDE 349
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
193-524 2.62e-29

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: 120.09  E-value: 2.62e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 193 GTTGLPKLIPRTHDDYLYSVResaVVANLQQDTKH---LLVLPVSH-----NfpmsspGFLGVIYAGATLVIADNSSPTE 264
Cdd:cd05941    99 GTTGRPKGVVLTHANLAANVR---ALVDAWRWTEDdvlLHVLPLHHvhglvN------ALLCPLFAGASVEFLPKFDPKE 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 265 CFGLIERHKITQTSLVPS----LVVAW----LNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAEG 336
Cdd:cd05941   170 VAISRLMPSITVFMGVPTiytrLLQYYeahfTDPQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEI 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 337 LVNYT-RLDDNREVqiNTQGKRLSDFdEIQILDLE-GKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGFYITGD 414
Cdd:cd05941   250 GMALSnPLDGERRP--GTVGMPLPGV-QARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGD 326
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 415 LGYLDENNNITVTGRLK-EVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPD-NFNLVKVRK 492
Cdd:cd05941   327 LGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAaALSLEELKE 406
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1436945972 493 YLtQQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd05941   407 WA-KQRLAPYKRPRRLILVDELPRNAMGKVNK 437
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
41-524 2.99e-29

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: 121.06  E-value: 2.99e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  41 ALVLGEDEVSYEAFYFKALAW-----GEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGALPIFCLDGHRSYEIghI 115
Cdd:cd05970    35 ALVWCDDAGEERIFTFAELADysdktANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDI--V 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 116 AKFSQARVYLRLCKHESDstaeqIIHHFSGDLPHLEIIKTVFQ--GELPQ--CDGDRSKLKEKTHYQPVDSRA------V 185
Cdd:cd05970   113 YRIESADIKMIVAIAEDN-----IPEEIEKAAPECPSKPKLVWvgDPVPEgwIDFRKLIKNASPDFERPTANSypcgedI 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 186 AFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHNFPMsspgfLGVIY----AGATLVIADNS- 260
Cdd:cd05970   188 LLVYFSSGTTGMPKMVEHDFTYPLGHIVTAKYWQNVREGGLHLTVADTGWGKAV-----WGKIYgqwiAGAAVFVYDYDk 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 261 -SPTECFGLIERHKITqTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAEGLVN 339
Cdd:cd05970   263 fDPKALLEKLSKYGVT-TFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLT 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 340 YTRLDdNREVQINTQGKRLSDFDeIQILDLEGKVLGVGEVGVITTR----GPYTINAYFAPDEVNKRSFTEDGFYITGDL 415
Cdd:cd05970   342 IATFP-WMEPKPGSMGKPAPGYE-IDLIDREGRSCEAGEEGEIVIRtskgKPVGLFGGYYKDAEKTAEVWHDGYYHTGDA 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 416 GYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKpdNFNLVKVRKYLT 495
Cdd:cd05970   420 AWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAK--GYEPSEELKKEL 497
                         490       500       510
                  ....*....|....*....|....*....|...
gi 1436945972 496 QQHI----ALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd05970   498 QDHVkkvtAPYKYPRIVEFVDELPKTISGKIRR 530
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
186-482 3.72e-29

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 120.76  E-value: 3.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 186 AFLQLSGGTTGLPKLIPRTHDDYLYSVResAVVANLQ---QDTKhLLVLPVSHNFpmsspGFLGVIYA-----GATLVIA 257
Cdd:PRK05852  179 AMIMFTGGTTGLPKMVPWTHANIASSVR--AIITGYRlspRDAT-VAVMPLYHGH-----GLIAALLAtlasgGAVLLPA 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 258 DNSSPTECF-GLIERHKITQTSLVPSLVVAWLNSAMIDKFDL--SSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMA 334
Cdd:PRK05852  251 RGRFSAHTFwDDIKAVGATWYTAVPTIHQILLERAATEPSGRkpAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMT 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 335 EGL--VNYTRLD-----DNREVQINTQGKrlSDFDEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTeD 407
Cdd:PRK05852  331 EAThqVTTTQIEgigqtENPVVSTGLVGR--STGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFT-D 407
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1436945972 408 GFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKP 482
Cdd:PRK05852  408 GWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRES 482
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
23-515 4.73e-29

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 120.98  E-value: 4.73e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  23 ESLFEFFERSCQKFATNTAL---VLGE-DEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGA 98
Cdd:COG1022    11 DTLPDLLRRRAARFPDRVALrekEDGIwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  99 --LPIFCLDGHRsyEIGHIAKFSQARVYLrlckHESDSTAEQIIHHFsGDLPHLE-IIktVFQGELPQCDGDRSKLKE-- 173
Cdd:COG1022    91 vtVPIYPTSSAE--EVAYILNDSGAKVLF----VEDQEQLDKLLEVR-DELPSLRhIV--VLDPRGLRDDPRLLSLDEll 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 174 ---KTHYQP--VDSRA-------VAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSH------ 235
Cdd:COG1022   162 algREVADPaeLEARRaavkpddLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHvfertv 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 236 -----------NFPmSSPG-------------FLGV------IYAGATLVIADNSSPTE-----CFGL-IERHKITQTSL 279
Cdd:COG1022   242 syyalaagatvAFA-ESPDtlaedlrevkptfMLAVprvwekVYAGIQAKAEEAGGLKRklfrwALAVgRRYARARLAGK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 280 VPSLVvAWLNSAMIDKFDLSSL--------EVVQVGGAKFSSELAA---------RLldtldltlqqVYGMAE--GLVNY 340
Cdd:COG1022   321 SPSLL-LRLKHALADKLVFSKLrealggrlRFAVSGGAALGPELARffralgipvLE----------GYGLTEtsPVITV 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 341 TRLDDNRevqINTQGKRLSDFdEIQIldlegkvlgvGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGFYITGDLGYLDE 420
Cdd:COG1022   390 NRPGDNR---IGTVGPPLPGV-EVKI----------AEDGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDE 455
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 421 NNNITVTGRLKEVI-NRAGEKIMPSEIEELLYAHPDVKDVLVTGvpDellGEKICVQIITDKPDNfnlvkVRKYLTQQHI 499
Cdd:COG1022   456 DGFLRITGRKKDLIvTSGGKNVAPQPIENALKASPLIEQAVVVG--D---GRPFLAALIVPDFEA-----LGEWAEENGL 525
                         570
                  ....*....|....*....
gi 1436945972 500 ALNKLPDVVS---VVDEFD 515
Cdd:COG1022   526 PYTSYAELAQdpeVRALIQ 544
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
23-524 8.44e-29

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


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 119.93  E-value: 8.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  23 ESLFEFFERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQ-GVRKDDLVVLQSANVLEFFYVLFGLYYLGALPI 101
Cdd:PRK12492   24 KSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 102 FCLDGHRSYEIGHIAKFSQAR--VYLRLCKHE-----SDSTAEQIIHHFSGD-LPHLE----------IIKTVFQGELPQ 163
Cdd:PRK12492  104 NTNPLYTAREMRHQFKDSGARalVYLNMFGKLvqevlPDTGIEYLIEAKMGDlLPAAKgwlvntvvdkVKKMVPAYHLPQ 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 164 CDGDRSKLKE------KTHYQPVDSraVAFLQLSGGTTGLPKLIPRTHDDYLYSVREsaVVANLQQDTKHLLVLPVSHNF 237
Cdd:PRK12492  184 AVPFKQALRQgrglslKPVPVGLDD--IAVLQYTGGTTGLAKGAMLTHGNLVANMLQ--VRACLSQLGPDGQPLMKEGQE 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 238 PMSSPGFLGVIYAGAT----LVIADN-----SSPTECFGLI-ERHKITQTSLV--PSLVVAWLNSAMIDKFDLSSLEVVQ 305
Cdd:PRK12492  260 VMIAPLPLYHIYAFTAncmcMMVSGNhnvliTNPRDIPGFIkELGKWRFSALLglNTLFVALMDHPGFKDLDFSALKLTN 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 306 VGGAKFSSELAARLLDTLDLTLQQVYGMAEGLVNYTRLDDNREVQINTQGKRLSDfDEIQILDLEGKVLGVGEVGVITTR 385
Cdd:PRK12492  340 SGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELARLGTVGIPVPG-TALKVIDDDGNELPLGERGELCIK 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 386 GPYTINAYFAPDEVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVP 465
Cdd:PRK12492  419 GPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVP 498
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1436945972 466 DELLGEKICVQIITDKPdNFNLVKVRKYLTQQHIALnKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:PRK12492  499 DERSGEAVKLFVVARDP-GLSVEELKAYCKENFTGY-KVPKHIVLRDSLPMTPVGKILR 555
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
65-521 9.04e-29

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 119.41  E-value: 9.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  65 LHEQGVRKDDLVVLQSANVLEFFYVLF-----GLYYLgalpifCLDGHRSY-EIGHIAKFSQARVYLrlCKHESDSTAEQ 138
Cdd:PRK13391   41 FRSLGLKRGDHVAIFMENNLRYLEVCWaaersGLYYT------CVNSHLTPaEAAYIVDDSGARALI--TSAAKLDVARA 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 139 IIHHFSGDLPHLEIIKtvfQGELPQCDGdrskLKEKTHYQPV----DSRAVAFLQLSGGTTGLPKLI--PRTHDDYLYSV 212
Cdd:PRK13391  113 LLKQCPGVRHRLVLDG---DGELEGFVG----YAEAVAGLPAtpiaDESLGTDMLYSSGTTGRPKGIkrPLPEQPPDTPL 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 213 RESAVVANL---QQDTKHLLVLPVSHNFPMSSPGFlgVIYAGATLVIADNSSPTECFGLIERHKITQTSLVPSLVVAWLN 289
Cdd:PRK13391  186 PLTAFLQRLwgfRSDMVYLSPAPLYHSAPQRAVML--VIRLGGTVIVMEHFDAEQYLALIEEYGVTHTQLVPTMFSRMLK 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 290 --SAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAEGLvNYTRLDdNREVQIN--TQGKRLsdFDEIQ 365
Cdd:PRK13391  264 lpEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGL-GFTACD-SEEWLAHpgTVGRAM--FGDLH 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 366 ILDLEGKVLGVGEVGVITTRG--PYTinaYFAPDEVNKRSFTEDGFYIT-GDLGYLDENNNITVTGRLKEVINRAGEKIM 442
Cdd:PRK13391  340 ILDDDGAELPPGEPGTIWFEGgrPFE---YLNDPAKTAEARHPDGTWSTvGDIGYVDEDGYLYLTDRAAFMIISGGVNIY 416
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 443 PSEIEELLYAHPDVKDVLVTGVPDELLGE--KICVQIITDKPDNFNLV-KVRKYLtQQHIALNKLPDVVSVVDEFDFTLI 519
Cdd:PRK13391  417 PQEAENLLITHPKVADAAVFGVPNEDLGEevKAVVQPVDGVDPGPALAaELIAFC-RQRLSRQKCPRSIDFEDELPRLPT 495

                  ..
gi 1436945972 520 GK 521
Cdd:PRK13391  496 GK 497
PRK07798 PRK07798
acyl-CoA synthetase; Validated
39-513 1.01e-28

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 119.60  E-value: 1.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  39 NTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGALPIfcldghrsyeighiakf 118
Cdd:PRK07798   19 RVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPV----------------- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 119 sqaRVYLRLCKHE-----SDSTAEQIIHH--FSG-------DLPHLeiiKTVFQGElpqcDGDRSklkekthyqPVDSRA 184
Cdd:PRK07798   82 ---NVNYRYVEDElryllDDSDAVALVYEreFAPrvaevlpRLPKL---RTLVVVE----DGSGN---------DLLPGA 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 185 VAFLQL----------------------SGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQ-DTKHLLVLPVSHNFPMS- 240
Cdd:PRK07798  143 VDYEDAlaagsperdfgerspddlyllyTGGTTGMPKGVMWRQEDIFRVLLGGRDFATGEPiEDEEELAKRAAAGPGMRr 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 241 ---SP--------GFLGVIYAGATLVIADNSS--PTECFGLIERHKITQTSLV------PslvvawlnsaMID------K 295
Cdd:PRK07798  223 fpaPPlmhgagqwAAFAALFSGQTVVLLPDVRfdADEVWRTIEREKVNVITIVgdamarP----------LLDaleargP 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 296 FDLSSLEVVQVGGAKFSSELAARLLDTL-DLTLQQVYGMAEGLVNYTRLDDNREVQinTQGKRLSDFDEIQILDLEGKVL 374
Cdd:PRK07798  293 YDLSSLFAIASGGALFSPSVKEALLELLpNVVLTDSIGSSETGFGGSGTVAKGAVH--TGGPRFTIGPRTVVLDEDGNPV 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 375 --GVGEVGVITtRGPYTINAYFAPDEVNKRSFTE-DG--FYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEEL 449
Cdd:PRK07798  371 epGSGEIGWIA-RRGHIPLGYYKDPEKTAETFPTiDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEA 449
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1436945972 450 LYAHPDVKDVLVTGVPDELLGEKIcVQIITDKPD-NFNLVKVRKYLTqQHIALNKLPDVVSVVDE 513
Cdd:PRK07798  450 LKAHPDVADALVVGVPDERWGQEV-VAVVQLREGaRPDLAELRAHCR-SSLAGYKVPRAIWFVDE 512
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
28-474 1.44e-28

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: 118.56  E-value: 1.44e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  28 FFERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGAL--PI-FCL 104
Cdd:cd12118     9 FLERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVlnALnTRL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 105 DghrSYEIGHIAKFSQARVYlrlckhesdstaeqiihhfsgdlphleIIKTVFQGELPQCDGDRSKLKEkthyQPVDSRA 184
Cdd:cd12118    89 D---AEEIAFILRHSEAKVL---------------------------FVDREFEYEDLLAEGDPDFEWI----PPADEWD 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 185 VAFLQLSGGTTGLPKLIPRTHDD-YLYSVreSAVVAN-LQQDTKHLLVLPVSH----NFPMSSPGFlgviyaGATLVIAD 258
Cdd:cd12118   135 PIALNYTSGTTGRPKGVVYHHRGaYLNAL--ANILEWeMKQHPVYLWTLPMFHcngwCFPWTVAAV------GGTNVCLR 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 259 NSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQqVYGMAE--G 336
Cdd:cd12118   207 KVDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEELGFDVTH-VYGLTEtyG 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 337 LV-------NYTRL-DDNREVQINTQGKRLSDFDEIQILDLEGK--VLGVGE-VGVITTRGPYTINAYFAPDEVNKRSFt 405
Cdd:cd12118   286 PAtvcawkpEWDELpTEERARLKARQGVRYVGLEEVDVLDPETMkpVPRDGKtIGEIVFRGNIVMKGYLKNPEATAEAF- 364
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1436945972 406 EDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKIC 474
Cdd:cd12118   365 RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPC 433
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
45-456 1.77e-28

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: 118.92  E-value: 1.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  45 GEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGALPIFCLDGHRSYEIGH-IAKFSQARV 123
Cdd:cd05906    36 SEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPNArLRKLRHIWQ 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 124 YLRLCKHESDSTAEQIIHHFSGDLPHLEIiKTVFQGELPQCDGDrsklkekTHYQPVDSRAVAFLQLSGGTTGLPKLIPR 203
Cdd:cd05906   116 LLGSPVVLTDAELVAEFAGLETLSGLPGI-RVLSIEELLDTAAD-------HDLPQSRPDDLALLMLTSGSTGFPKAVPL 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 204 THDDYLYSVRESAVVANLQQDT--------KHLLVLPVSHNFPMsspgFLGV--IYAGATLVIADnssPTECFGLIERHK 273
Cdd:cd05906   188 THRNILARSAGKIQHNGLTPQDvflnwvplDHVGGLVELHLRAV----YLGCqqVHVPTEEILAD---PLRWLDLIDRYR 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 274 ITQT---SLVPSLVVAWLNSAMIDKFDLSSLE--------VVQVGGAKFSSELAARLLDTLDLTLqqVYGMAE------- 335
Cdd:cd05906   261 VTITwapNFAFALLNDLLEEIEDGTWDLSSLRylvnageaVVAKTIRRLLRLLEPYGLPPDAIRP--AFGMTEtcsgviy 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 336 --GLVNYTRLDDNREVQIntqGKRLSDFDeIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGFYITG 413
Cdd:cd05906   339 srSFPTYDHSQALEFVSL---GRPIPGVS-MRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTG 414
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1436945972 414 DLGYLDeNNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDV 456
Cdd:cd05906   415 DLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGV 456
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
41-522 1.84e-28

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 118.57  E-value: 1.84e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  41 ALVLGE--DEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGaLPIFCLDGHRSY-EIGHIAK 117
Cdd:PRK13390   15 AVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSG-LYITAINHHLTApEADYIVG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 118 FSQARVYLrlckheSDSTAEQIIHHFSGDLPhleiIKTVFQGELPQCDGDRSKLK---EKTHYQPVDsravAFLQLSGGT 194
Cdd:PRK13390   94 DSGARVLV------ASAALDGLAAKVGADLP----LRLSFGGEIDGFGSFEAALAgagPRLTEQPCG----AVMLYSSGT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 195 TGLPKLI----PRTHDDY-----------LYSVRESAVvanlqqdtkHLLVLPVSHNFPMSspgFLGVIYA-GATLVIAD 258
Cdd:PRK13390  160 TGFPKGIqpdlPGRDVDApgdpivaiaraFYDISESDI---------YYSSAPIYHAAPLR---WCSMVHAlGGTVVLAK 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 259 NSSPTECFGLIERHKITQTSLVPSLVVAWL--NSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAEg 336
Cdd:PRK13390  228 RFDAQATLGHVERYRITVTQMVPTMFVRLLklDADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE- 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 337 LVNYTRLDDNREVQINTQGKRlSDFDEIQILDLEGKVLGVGEVGVIT-TRGPYTINAYFAPDEVNKRSFTEDGFYIT-GD 414
Cdd:PRK13390  307 AHGMTFIDSPDWLAHPGSVGR-SVLGDLHICDDDGNELPAGRIGTVYfERDRLPFRYLNDPEKTAAAQHPAHPFWTTvGD 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 415 LGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKI--CVQIITDKPDNFNLVKVRK 492
Cdd:PRK13390  386 LGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVkaVIQLVEGIRGSDELARELI 465
                         490       500       510
                  ....*....|....*....|....*....|
gi 1436945972 493 YLTQQHIALNKLPDVVSVVDEFDFTLIGKV 522
Cdd:PRK13390  466 DYTRSRIAHYKAPRSVEFVDELPRTPTGKL 495
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
22-522 2.08e-28

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 118.63  E-value: 2.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  22 GESLFEFFERSCQKFATNTALVLgED------EVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYY 95
Cdd:PRK08008    6 GQHLRQMWDDLADVYGHKTALIF-ESsggvvrRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  96 LGALPIFCLDGHRSYEIGHIAKFSQARvyLRLCKHESDSTAEQIIHHFSGDLPHLEIIKTVfqgeLPQCDG--DRSKLKE 173
Cdd:PRK08008   85 IGAIMVPINARLLREESAWILQNSQAS--LLVTSAQFYPMYRQIQQEDATPLRHICLTRVA----LPADDGvsSFTQLKA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 174 K-----THYQPVDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSH-NFPMSSPgfLGV 247
Cdd:PRK08008  159 QqpatlCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHiDCQCTAA--MAA 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 248 IYAGATLVIADNSSPTECFGLIERHKITQTSLVPSLV--------VAW------------LNSAMIDKFDLSSLEVVQVg 307
Cdd:PRK08008  237 FSAGATFVLLEKYSARAFWGQVCKYRATITECIPMMIrtlmvqppSANdrqhclrevmfyLNLSDQEKDAFEERFGVRL- 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 308 gakFSSelaarlldtldltlqqvYGMAE---GLVNYTRLDDNREVQINTQGKRLsdfdEIQILDLEGKVLGVGEVGVITT 384
Cdd:PRK08008  316 ---LTS-----------------YGMTEtivGIIGDRPGDKRRWPSIGRPGFCY----EAEIRDDHNRPLPAGEIGEICI 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 385 RG-P-YTI-NAYFAPDEVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLV 461
Cdd:PRK08008  372 KGvPgKTIfKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVV 451
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1436945972 462 TGVPDELLGEKICVQIITDKPDNFNLVKVRKYlTQQHIALNKLPDVVSVVDEFDFTLIGKV 522
Cdd:PRK08008  452 VGIKDSIRDEAIKAFVVLNEGETLSEEEFFAF-CEQNMAKFKVPSYLEIRKDLPRNCSGKI 511
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
179-522 3.44e-28

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


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 117.43  E-value: 3.44e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 179 PVDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHNFPMSSPGFLgVIYAGATLVIAD 258
Cdd:cd05909   143 PVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWL-PLLSGIKVVFHP 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 259 NSSPTECFG-LIERHKITQTSLVPSLVVAWLNSAmiDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAEG- 336
Cdd:cd05909   222 NPLDYKKIPeLIYDKKATILLGTPTFLRGYARAA--HPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECs 299
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 337 ---LVNyTRLDDNREvqiNTQGkRLSDFDEIQILDLEGKV-LGVGEVGVITTRGPYTINAYFAPDEvnKRSFT-EDGFYI 411
Cdd:cd05909   300 pviSVN-TPQSPNKE---GTVG-RPLPGMEVKIVSVETHEeVPIGEGGLLLVRGPNVMLGYLNEPE--LTSFAfGDGWYD 372
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 412 TGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAH-PDVKDVLVTGVPDELLGEKICVQIITDKPDNFNLvkv 490
Cdd:cd05909   373 TGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTTTDTDPSSL--- 449
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1436945972 491 RKYLTQQHIALNKLPDVVSVVDEFDFTLIGKV 522
Cdd:cd05909   450 NDILKNAGISNLAKPSYIHQVEEIPLLGTGKP 481
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
185-524 4.07e-28

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: 116.81  E-value: 4.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 185 VAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAV-VANLQQDTKHLLVLPVSHNFpmsspGFLGVI----YAGATLVIADN 259
Cdd:cd05958    99 ICILAFTSGTTGAPKATMHFHRDPLASADRYAVnVLRLREDDRFVGSPPLAFTF-----GLGGVLlfpfGVGASGVLLEE 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 260 SSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAEGLVN 339
Cdd:cd05958   174 ATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHI 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 340 Y--TRLDDNRevqINTQGKRLSDFdEIQILDLEGKVLGVGEVGVITTRGPytiNAYFAPDEVNKRSFTEDGFYITGDLGY 417
Cdd:cd05958   254 FisARPGDAR---PGATGKPVPGY-EAKVVDDEGNPVPDGTIGRLAVRGP---TGCRYLADKRQRTYVQGGWNITGDTYS 326
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 418 LDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITdKPDNF---NLVKVRKYL 494
Cdd:cd05958   327 RDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVL-RPGVIpgpVLARELQDH 405
                         330       340       350
                  ....*....|....*....|....*....|
gi 1436945972 495 TQQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd05958   406 AKAHIAPYKYPRAIEFVTELPRTATGKLQR 435
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
180-524 4.35e-28

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 118.06  E-value: 4.35e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 180 VDSRAVAFLQLSGGTTGLPKLIPRTHDDylysvresaVVANLQQDTKHLLV--------------LPVSHNFPMSSPGFL 245
Cdd:PRK08751  205 IEPDDIAFLQYTGGTTGVAKGAMLTHRN---------LVANMQQAHQWLAGtgkleegcevvitaLPLYHIFALTANGLV 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 246 GVIYAGATLVIadnSSPTECFGLI---ERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDT 322
Cdd:PRK08751  276 FMKIGGCNHLI---SNPRDMPGFVkelKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQV 352
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 323 LDLTLQQVYGMAE----GLVNYTRLDDNRevqiNTQGKRLSDFDeIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDE 398
Cdd:PRK08751  353 TGLTLVEAYGLTEtspaACINPLTLKEYN----GSIGLPIPSTD-ACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPE 427
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 399 VNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQII 478
Cdd:PRK08751  428 ETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIV 507
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1436945972 479 TDKPdNFNLVKVRKYlTQQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:PRK08751  508 KKDP-ALTAEDVKAH-ARANLTGYKQPRIIEFRKELPKTNVGKILR 551
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
202-475 4.52e-28

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: 114.67  E-value: 4.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 202 PR----THDDYLYSVRESAVVANLQQDTKHLLVLPVSHNFPMSSPgfLGVIYAGATLVIADNSSPTECFGLIERHKITQT 277
Cdd:cd17637    15 PRgavlSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLA--LATFHAGGANVVMEKFDPAEALELIEEEKVTLM 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 278 SLVPSLVVAWLNSAMIDKFDLSSLEVV-------------QVGGAKFSSelaarlldtldltlqqVYGMAE--GLVNYTR 342
Cdd:cd17637    93 GSFPPILSNLLDAAEKSGVDLSSLRHVlgldapetiqrfeETTGATFWS----------------LYGQTEtsGLVTLSP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 343 LDD-----NREVQINTqgkrlsdfdeIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFtEDGFYITGDLGY 417
Cdd:cd17637   157 YRErpgsaGRPGPLVR----------VRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGR 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1436945972 418 LDENNNITVTGRL--KEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKI---CV 475
Cdd:cd17637   226 FDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIkavCV 288
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
41-508 1.02e-27

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


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 116.34  E-value: 1.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  41 ALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGALPIfCLDGH-RSYEIGHIAKFS 119
Cdd:PRK12406    4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAV-PVNWHfKPEEIAYILEDS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 120 QARVylrLCKHESdstaeqIIHHFSGDLP-HLEIIKTVFQGEL-------------PQCDGD-RSKLKEKTHYQPVDSRA 184
Cdd:PRK12406   83 GARV---LIAHAD------LLHGLASALPaGVTVLSVPTPPEIaaayrispalltpPAGAIDwEGWLAQQEPYDGPPVPQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 185 VAFLQLSGGTTGLPKLIPR---THDDYLYSVRESAVVANLQQDTKHLLVLPVSHnfpmSSPGFLGV--IYAGATLVIADN 259
Cdd:PRK12406  154 PQSMIYTSGTTGHPKGVRRaapTPEQAAAAEQMRALIYGLKPGIRALLTGPLYH----SAPNAYGLraGRLGGVLVLQPR 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 260 SSPTECFGLIERHKITQTSLVPSLVVAWLN--SAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAE-G 336
Cdd:PRK12406  230 FDPEELLQLIERHRITHMHMVPTMFIRLLKlpEEVRAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTEsG 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 337 LVNYTRLDD--NREvqiNTQGKrLSDFDEIQILDLEGKVLGVGEVGVITTRGP-YTINAYFAPDEvNKRSFTEDGFYITG 413
Cdd:PRK12406  310 AVTFATSEDalSHP---GTVGK-AAPGAELRFVDEDGRPLPQGEIGEIYSRIAgNPDFTYHNKPE-KRAEIDRGGFITSG 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 414 DLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPDNFNLVKVRKY 493
Cdd:PRK12406  385 DVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQ 464
                         490
                  ....*....|....*
gi 1436945972 494 LtQQHIALNKLPDVV 508
Cdd:PRK12406  465 L-KARLAGYKVPKHI 478
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
24-524 5.98e-27

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 114.31  E-value: 5.98e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  24 SLFEFFERSCQKFATNTALVlgedevsyEAFYFKALAWGEWLHEQ----------GVRKDDLVVLQSANVLEFFYVLFGL 93
Cdd:PLN02330   29 TLPDFVLQDAELYADKVAFV--------EAVTGKAVTYGEVVRDTrrfakalrslGLRKGQVVVVVLPNVAEYGIVALGI 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  94 Y-----YLGALPIfcldGHRSyEIGHIAKFSQARVYLrlckhESDSTAEQIIhhfSGDLPHLEIIKTVFQGELPQCD--- 165
Cdd:PLN02330  101 MaaggvFSGANPT----ALES-EIKKQAEAAGAKLIV-----TNDTNYGKVK---GLGLPVIVLGEEKIEGAVNWKElle 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 166 -GDRSKlkEKTHYQPVDSRAVAFLQLSGGTTGLPKLIPRTHDDY-------LYSVRESAV--VANLQqdtkhllVLPVSH 235
Cdd:PLN02330  168 aADRAG--DTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLvanlcssLFSVGPEMIgqVVTLG-------LIPFFH 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 236 NFpmsspGFLGVIYA-----GATLVIADNSSPTECFGLIErHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEV--VQVGG 308
Cdd:PLN02330  239 IY-----GITGICCAtlrnkGKVVVMSRFELRTFLNALIT-QEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLqaIMTAA 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 309 AKFSSEL-AARLLDTLDLTLQQVYGMAE-GLVNYTRLDDNREVQI---NTQGKRLSDFdEIQILDLE-GKVLGVGEVGVI 382
Cdd:PLN02330  313 APLAPELlTAFEAKFPGVQVQEAYGLTEhSCITLTHGDPEKGHGIakkNSVGFILPNL-EVKFIDPDtGRSLPKNTPGEL 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 383 TTRGPYTINAYFAPDEVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVT 462
Cdd:PLN02330  392 CVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVV 471
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1436945972 463 GVPDELLGEKICVQIITDKPDNFNLVKVRKYLTqQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:PLN02330  472 PLPDEEAGEIPAACVVINPKAKESEEDILNFVA-ANVAHYKKVRVVQFVDSIPKSLSGKIMR 532
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
214-483 7.71e-27

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: 110.85  E-value: 7.71e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 214 ESAVVANLQQ---DTKHLLVLPVSH-NFPMSSpgfLGVIYAGATLVIADNSSPTECFGLIERHKITQTSLVPSLV--VAW 287
Cdd:cd17636    28 QALVLAVLQAideGTVFLNSGPLFHiGTLMFT---LATFHAGGTNVFVRRVDAEEVLELIEAERCTHAFLLPPTIdqIVE 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 288 LNSAmiDKFDLSSLEVVQvggAKFSSELAARLLDTLDLTLQQVYGMAE--GLVNYTRLDDNrevQINTQGkRLSDFDEIQ 365
Cdd:cd17636   105 LNAD--GLYDLSSLRSSP---AAPEWNDMATVDTSPWGRKPGGYGQTEvmGLATFAALGGG---AIGGAG-RPSPLVQVR 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 366 ILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTeDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSE 445
Cdd:cd17636   176 ILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR-GGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAE 254
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1436945972 446 IEELLYAHPDVKDVLVTGVPDELLGEKICVqIITDKPD 483
Cdd:cd17636   255 VERCLRQHPAVADAAVIGVPDPRWAQSVKA-IVVLKPG 291
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
42-524 1.01e-26

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: 112.92  E-value: 1.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  42 LVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGALpIFCLDghrsyeighiakfsqa 121
Cdd:cd05914     1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAI-AVPIL---------------- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 122 rvylrlckheSDSTAEQIiHHFsgdLPHLEIiKTVFQGElpqcdgdrsklKEKthyqpvdsraVAFLQLSGGTTGLPKLI 201
Cdd:cd05914    64 ----------AEFTADEV-HHI---LNHSEA-KAIFVSD-----------EDD----------VALINYTSGTTGNSKGV 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 202 PRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHNFPMSSPGFLGViYAGATLVIADNSSP-----------TECFG--- 267
Cdd:cd05914   108 MLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPL-LNGAHVVFLDKIPSakiialafaqvTPTLGvpv 186
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 268 LIERHKITQTSLVPSLVVAWLNSAMIDK-FDLSSLEVVQ---------------VGGAKFSSELAaRLLDTLDLTLQQVY 331
Cdd:cd05914   187 PLVIEKIFKMDIIPKLTLKKFKFKLAKKiNNRKIRKLAFkkvheafggnikefvIGGAKINPDVE-EFLRTIGFPYTIGY 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 332 GMAEG--LVNYTRldDNREVqINTQGKRLSDFdEIQILDLEGKVlgvgEVGVITTRGPYTINAYFAPDEVNKRSFTEDGF 409
Cdd:cd05914   266 GMTETapIISYSP--PNRIR-LGSAGKVIDGV-EVRIDSPDPAT----GEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW 337
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 410 YITGDLGYLDENNNITVTGRLKEVI-NRAGEKIMPSEIEELLYAHPDV--KDVLVTGVPDELLG------EKICVQIITD 480
Cdd:cd05914   338 FHTGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPFVleSLVVVQEKKLVALAyidpdfLDVKALKQRN 417
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 1436945972 481 KPDNFnLVKVRKYLTQQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd05914   418 IIDAI-KWEVRDKVNQKVPNYKKISKVKIVKEEFEKTPKGKIKR 460
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
180-524 4.57e-26

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


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 112.02  E-value: 4.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 180 VDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRES-AVVANL-QQDTKHLLVLPVSHNFPMSSPGFLGViYAGATLVIA 257
Cdd:PRK05605  216 PTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGkAWVPGLgDGPERVLAALPMFHAYGLTLCLTLAV-SIGGELVLL 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 258 DNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAEG- 336
Cdd:PRK05605  295 PAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETs 374
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 337 -LVNYTRLDDNRevQINTQGKRLSDfDEIQILDLE--GKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFtEDGFYITG 413
Cdd:PRK05605  375 pIIVGNPMSDDR--RPGYVGVPFPD-TEVRIVDPEdpDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTG 450
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 414 DLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPDNFNLVKVRKY 493
Cdd:PRK05605  451 DVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAY 530
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1436945972 494 LtQQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:PRK05605  531 C-REHLTRYKVPRRFYHVDELPRDQLGKVRR 560
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
46-467 5.29e-26

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: 111.04  E-value: 5.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  46 EDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGALPIfcldghrSYEIGHIAKFSQARvyl 125
Cdd:cd05908    13 EKFVSYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAV-------PVSIGSNEEHKLKL--- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 126 rlckhesdstaeqiihhfsgdlphLEIIKTVFQGELPQCDGDRSKLKEKthyqpvdsraVAFLQLSGGTTGLPKLIPRTH 205
Cdd:cd05908    83 ------------------------NKVWNTLKNPYLITEEEVLCELADE----------LAFIQFSSGSTGDPKGVMLTH 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 206 DDYLYSVResAVVANLQQDTKHLLV--LPVSHNFPMSSpGFLGVIYAGATLVIADNS----SPTECFGLIERHKITQTS- 278
Cdd:cd05908   129 ENLVHNMF--AILNSTEWKTKDRILswMPLTHDMGLIA-FHLAPLIAGMNQYLMPTRlfirRPILWLKKASEHKATIVSs 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 279 --LVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSEL------AARLLDTLDLTLQQVYGMAEGLVNYTRLD------ 344
Cdd:cd05908   206 pnFGYKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELchefldHMSKYGLKRNAILPVYGLAEASVGASLPKaqspfk 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 345 ----DNREVQINTQGKRLS----------------DFDEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSF 404
Cdd:cd05908   286 titlGRRHVTHGEPEPEVDkkdsecltfvevgkpiDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVF 365
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1436945972 405 TEDGFYITGDLGYLdENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVK--DVLVTGVPDE 467
Cdd:cd05908   366 TDDGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVElgRVVACGVNNS 429
PRK13382 PRK13382
bile acid CoA ligase;
190-524 2.99e-25

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 109.08  E-value: 2.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 190 LSGGTTGLPKLIPRTHD-DYLYSvreSAVVAN--LQQDTKHLLVLPVSHNFpmsspGFLGVIYAGA---TLVIADNSSPT 263
Cdd:PRK13382  203 LTSGTTGTPKGARRSGPgGIGTL---KAILDRtpWRAEEPTVIVAPMFHAW-----GFSQLVLAASlacTIVTRRRFDPE 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 264 ECFGLIERHKITQTSLVPSLV--VAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAE-GLVNY 340
Cdd:PRK13382  275 ATLDLIDRHRATGLAVVPVMFdrIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEaGMIAT 354
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 341 TRLDDNREvQINTQGKRlSDFDEIQILDLEGKVLGVGEVGVITTRGPYTINAYFApdevNKRSFTEDGFYITGDLGYLDE 420
Cdd:PRK13382  355 ATPADLRA-APDTAGRP-AEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTS----GSTKDFHDGFMASGDVGYLDE 428
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 421 NNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITdKPDNFNLVKVRKYLTQQHIA 500
Cdd:PRK13382  429 NGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVL-KPGASATPETLKQHVRDNLA 507
                         330       340
                  ....*....|....*....|....
gi 1436945972 501 LNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:PRK13382  508 NYKVPRDIVVLDELPRGATGKILR 531
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
40-524 3.50e-25

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: 108.61  E-value: 3.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  40 TALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGALPI---FCLDGHrsyEIGHIA 116
Cdd:cd05959    21 TAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVpvnTLLTPD---DYAYYL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 117 KFSQARVYLrlckhESDSTAEQIIHHFSGDLPHLEIIkTVFQGELPQCD-GDRSKL--KEKTHYQPVDSRA--VAFLQLS 191
Cdd:cd05959    98 EDSRARVVV-----VSGELAPVLAAALTKSEHTLVVL-IVSGGAGPEAGaLLLAELvaAEAEQLKPAATHAddPAFWLYS 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 192 GGTTGLPKLIPRTHDDyLYSVRESAV--VANLQQDTKHLLV--------LPVSHNFPMSspgflgviyAGATLVI-ADNS 260
Cdd:cd05959   172 SGSTGRPKGVVHLHAD-IYWTAELYArnVLGIREDDVCFSAaklffaygLGNSLTFPLS---------VGATTVLmPERP 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 261 SPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAEGLVNY 340
Cdd:cd05959   242 TPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIF 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 341 TrldDNR--EVQINTQGKRLSDFdEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFtEDGFYITGDLGYL 418
Cdd:cd05959   322 L---SNRpgRVRYGTTGKPVPGY-EVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVR 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 419 DENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDE--LLGEKICVQIITDKPDNFNLVKVRKYLTQ 496
Cdd:cd05959   397 DDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEdgLTKPKAFVVLRPGYEDSEALEEELKEFVK 476
                         490       500
                  ....*....|....*....|....*...
gi 1436945972 497 QHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd05959   477 DRLAPYKYPRWIVFVDELPKTATGKIQR 504
PRK07638 PRK07638
acyl-CoA synthetase; Validated
40-524 3.83e-25

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 108.33  E-value: 3.83e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  40 TALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSaNVLEFFYVLFGLYYLG--ALPifcLDghrsyeighiAK 117
Cdd:PRK07638   18 IAIKENDRVLTYKDWFESVCKVANWLNEKESKNKTIAILLE-NRIEFLQLFAGAAMAGwtCVP---LD----------IK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 118 FSQARVYLRLCKHESDST-AEQiihHFSGDLPHLE--IIktvfqgELPQCDGDRSKlkEKTHYQPVDSRAVA--FLQLSG 192
Cdd:PRK07638   84 WKQDELKERLAISNADMIvTER---YKLNDLPDEEgrVI------EIDEWKRMIEK--YLPTYAPIENVQNApfYMGFTS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 193 GTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLL--VLPVSHnfpmsspgFL-GVI---YAGATLVIADNSSPTECF 266
Cdd:PRK07638  153 GSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIagTLVHSL--------FLyGAIstlYVGQTVHLMRKFIPNQVL 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 267 GLIERHKITQTSLVPSLVVAWLNsamIDKFDLSSLEVVqVGGAKFSSELAARLLDTL-DLTLQQVYGMAEgLVNYTRLDD 345
Cdd:PRK07638  225 DKLETENISVMYTVPTMLESLYK---ENRVIENKMKII-SSGAKWEAEAKEKIKNIFpYAKLYEFYGASE-LSFVTALVD 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 346 NR-EVQINTQGKRLSDFdEIQILDLEGKVLGVGEVGVITTRGPYTINAYFApDEVNKRSFTEDGFYITGDLGYLDENNNI 424
Cdd:PRK07638  300 EEsERRPNSVGRPFHNV-QVRICNEAGEEVQKGEIGTVYVKSPQFFMGYII-GGVLARELNADGWMTVRDVGYEDEEGFI 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 425 TVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKIcVQIITdkpDNFNLVKVRKYLTQQhIALNKL 504
Cdd:PRK07638  378 YIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKP-VAIIK---GSATKQQLKSFCLQR-LSSFKI 452
                         490       500
                  ....*....|....*....|
gi 1436945972 505 PDVVSVVDEFDFTLIGKVRR 524
Cdd:PRK07638  453 PKEWHFVDEIPYTNSGKIAR 472
PLN02574 PLN02574
4-coumarate--CoA ligase-like
179-482 5.65e-25

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 108.39  E-value: 5.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 179 PVDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVR-----ESAVVANLQQDTKHLLVLPVSHNFPMSSpgF-LGVIYAGA 252
Cdd:PLN02574  194 VIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVElfvrfEASQYEYPGSDNVYLAALPMFHIYGLSL--FvVGLLSLGS 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 253 TLVIADNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAM-IDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQV- 330
Cdd:PLN02574  272 TIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKgVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQg 351
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 331 YGMAEGLVNYTRLDDNREVQINTQGKRLSDFDEIQILDLE-GKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGF 409
Cdd:PLN02574  352 YGMTESTAVGTRGFNTEKLSKYSSVGLLAPNMQAKVVDWStGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW 431
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1436945972 410 YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEkICVQIITDKP 482
Cdd:PLN02574  432 LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGE-IPVAFVVRRQ 503
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
40-524 2.59e-24

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: 105.24  E-value: 2.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  40 TALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGALPIFCLDGHRSYEIGHIAKFS 119
Cdd:cd05919     2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 120 QARVYLRlckhesdstaeqiihhfSGDlphleiiktvfqgelpqcdgdrsklkekthyqpvdsrAVAFLQLSGGTTGLPK 199
Cdd:cd05919    82 EARLVVT-----------------SAD-------------------------------------DIAYLLYSSGTTGPPK 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 200 LIPRTHDDYLYSVRESAV-VANLQQDTKHLLVLPVSHNFPMSSpGFLGVIYAGATLVIADNS-SPTECFGLIERHKITQT 277
Cdd:cd05919   108 GVMHAHRDPLLFADAMAReALGLTPGDRVFSSAKMFFGYGLGN-SLWFPLAVGASAVLNPGWpTAERVLATLARFRPTVL 186
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 278 SLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAEglVNYTRLDdNR--EVQINTQG 355
Cdd:cd05919   187 YGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATE--VGHIFLS-NRpgAWRLGSTG 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 356 KRLSDFdEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFtEDGFYITGDLGYLDENNNITVTGRLKEVIN 435
Cdd:cd05919   264 RPVPGY-EIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRADDMLK 341
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 436 RAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVqIITDKPDNFNLVKVRKYLTQ---QHIALNKLPDVVSVVD 512
Cdd:cd05919   342 VGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTA-FVVLKSPAAPQESLARDIHRhllERLSAHKVPRRIAFVD 420
                         490
                  ....*....|..
gi 1436945972 513 EFDFTLIGKVRR 524
Cdd:cd05919   421 ELPRTATGKLQR 432
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
179-448 1.85e-23

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


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 103.92  E-value: 1.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 179 PVDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLV-LPVSHNFPMSspGFLGV-IYAGATLVi 256
Cdd:PRK07768  148 ETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSwLPLFHDMGMV--GFLTVpMYFGAELV- 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 257 adNSSPTECFG-------LIERHKITQTsLVP----SLVVAWLNSAMIDK-FDLSSLEVVQVG---------------GA 309
Cdd:PRK07768  225 --KVTPMDFLRdpllwaeLISKYRGTMT-AAPnfayALLARRLRRQAKPGaFDLSSLRFALNGaepidpadvedlldaGA 301
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 310 KFSSELAArlldtldltLQQVYGMAEGLVNYT--------RLD---------DNREVQIN--------TQGKRLSDFdEI 364
Cdd:PRK07768  302 RFGLRPEA---------ILPAYGMAEATLAVSfspcgaglVVDevdadllaaLRRAVPATkgntrrlaTLGPPLPGL-EV 371
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 365 QILDLEGKVLGVGEVGVITTRGP-----YTINAYFAPDEvnkrsfTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGE 439
Cdd:PRK07768  372 RVVDEDGQVLPPRGVGVIELRGEsvtpgYLTMDGFIPAQ------DADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGR 445

                  ....*....
gi 1436945972 440 KIMPSEIEE 448
Cdd:PRK07768  446 NIYPTDIER 454
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
30-524 5.46e-23

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 102.53  E-value: 5.46e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  30 ERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGALPIFCLDGHRS 109
Cdd:PRK06155   28 ARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRG 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 110 YEIGHIAKFSQARVYLrlckheSDSTAEQIIHHFS---GDLPHLEIIKTVFQG---------ELPQCDgdrsklkekthy 177
Cdd:PRK06155  108 PQLEHILRNSGARLLV------VEAALLAALEAADpgdLPLPAVWLLDAPASVsvpagwstaPLPPLD------------ 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 178 QPVDSRAV------AFLQLSGgTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHNFPMSSpgFLGVIYAG 251
Cdd:PRK06155  170 APAPAAAVqpgdtaAILYTSG-TTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNA--FFQALLAG 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 252 ATLVIADNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGG--AKFSSELAARLLDTLDLTlqq 329
Cdd:PRK06155  247 ATYVLEPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGvpAALHAAFRERFGVDLLDG--- 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 330 vYGMAE-GLVNYTRLDDNREvqiNTQGkRLSDFDEIQILDLEGKVLGVGEVGVITTRG--PYTI-NAYFAPDEVNKRSFT 405
Cdd:PRK06155  324 -YGSTEtNFVIAVTHGSQRP---GSMG-RLAPGFEARVVDEHDQELPDGEPGELLLRAdePFAFaTGYFGMPEKTVEAWR 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 406 EDGFYiTGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPDNF 485
Cdd:PRK06155  399 NLWFH-TGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTAL 477
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 1436945972 486 NLVKVRKYLTQQhIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:PRK06155  478 EPVALVRHCEPR-LAYFAVPRYVEFVAALPKTENGKVQK 515
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
193-524 1.60e-22

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 101.03  E-value: 1.60e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 193 GTTGLPKLIPRTHDDYLY-SVRESAVVANLQQDTkHLLVLPVSHNFPMSSPgfLGVIYAGATLVIADNSSPTECFGLIER 271
Cdd:PLN02860  182 GTTGRPKGVTISHSALIVqSLAKIAIVGYGEDDV-YLHTAPLCHIGGLSSA--LAMLMVGACHVLLPKFDAKAALQAIKQ 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 272 HKITQTSLVPSL---VVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAEGLVNYT--RLDDN 346
Cdd:PLN02860  259 HNVTSMITVPAMmadLISLTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEACSSLTfmTLHDP 338
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 347 RevqINTQGKRLSDFDEIQILDLE-------GKV-----LGVG-----EVGVITTRGPYTINAYFAPDEVNKRSFTEDGF 409
Cdd:PLN02860  339 T---LESPKQTLQTVNQTKSSSVHqpqgvcvGKPaphveLKIGldessRVGRILTRGPHVMLGYWGQNSETASVLSNDGW 415
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 410 YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKI--CVQI-------ITD 480
Cdd:PLN02860  416 LDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVvaCVRLrdgwiwsDNE 495
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1436945972 481 KPD---NFNLVK--VRKYLTQQHIALNKLPDVVSV-VDEFDFTLIGKVRR 524
Cdd:PLN02860  496 KENakkNLTLSSetLRHHCREKNLSRFKIPKLFVQwRKPFPLTTTGKIRR 545
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
27-524 1.80e-22

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: 100.48  E-value: 1.80e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  27 EFFERSCQKFATNTALVLGEDEVSYEAFYFKA--LAWgeWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGA--LPI- 101
Cdd:cd17655     1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERAnqLAR--TLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGayLPId 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 102 --FCLDghrsyEIGHIAKFSQARVYLrlckhesdsTAEQIIHhfsgdlphleiiKTVFQGELPQCDGDRSKLKEKTHYQP 179
Cdd:cd17655    79 pdYPEE-----RIQYILEDSGADILL---------TQSHLQP------------PIAFIGLIDLLDEDTIYHEESENLEP 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 180 V-DSRAVAFLQLSGGTTGLPKLIPRTHD---DYLYSVRESAVvanlqQDTKHLLVLPVSHNFPMSSPGFLGVIYAGATLV 255
Cdd:cd17655   133 VsKSDDLAYVIYTSGSTGKPKGVMIEHRgvvNLVEWANKVIY-----QGEHLRVALFASISFDASVTEIFASLLSGNTLY 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 256 I---ADNSSPTECFGLIERHKITQTSLVPSLVVawlnsaMIDKFDLS---SLEVVQVGGAKFSSELAARLLDTLDLTLQQ 329
Cdd:cd17655   208 IvrkETVLDGQALTQYIRQNRITIIDLTPAHLK------LLDAADDSeglSLKHLIVGGEALSTELAKKIIELFGTNPTI 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 330 --VYGMAEGLV-----NYTRLDDNRE-VQIntqGKRLSDFdEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNK 401
Cdd:cd17655   282 tnAYGPTETTVdasiyQYEPETDQQVsVPI---GKPLGNT-RIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTA 357
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 402 RSFTEDGF------YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICV 475
Cdd:cd17655   358 EKFVDDPFvpgermYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCA 437
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1436945972 476 QIITDKpdNFNLVKVRKYLTQQhialnkLPD--VVSV---VDEFDFTLIGKVRR 524
Cdd:cd17655   438 YIVSEK--ELPVAQLREFLARE------LPDymIPSYfikLDEIPLTPNGKVDR 483
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
179-471 1.06e-20

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: 95.46  E-value: 1.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 179 PVDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRES-AVVANLQQD----TKHLLVLPVSHNFPMSSPGFLG---VIYA 250
Cdd:cd05967   226 PVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSmRNIYGIKPGdvwwAASDVGWVVGHSYIVYGPLLHGattVLYE 305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 251 GATLVIADnssPTECFGLIERHKITQTSLVPSLVVAW----LNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLT 326
Cdd:cd05967   306 GKPVGTPD---PGAFWRVIEKYQVNALFTAPTAIRAIrkedPDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVP 382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 327 LQQVYGMAEG----LVNYTRLDDnREVQINTQGKRLSDFDeIQILDLEGKVLGVGEVGVITTRGPY---TINAYFAPDEV 399
Cdd:cd05967   383 VIDHWWQTETgwpiTANPVGLEP-LPIKAGSPGKPVPGYQ-VQVLDEDGEPVGPNELGNIVIKLPLppgCLLTLWKNDER 460
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1436945972 400 NKRSFTED--GFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGE 471
Cdd:cd05967   461 FKKLYLSKfpGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQ 534
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
65-524 1.43e-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: 94.04  E-value: 1.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  65 LHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGA--LPIFCLDGHRSYEighiakfsqarvyLRLckheSDSTAEQIIHH 142
Cdd:cd05971    23 LKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAiaVPLFALFGPEALE-------------YRL----SNSGASALVTD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 143 FSGDLphleiiktvfqgelpqcdgdrsklkekthyqpvdsravAFLQLSGGTTGLPKLIPRTHDDYLysvresavvanlq 222
Cdd:cd05971    86 GSDDP--------------------------------------ALIIYTSGTTGPPKGALHAHRVLL------------- 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 223 qdtKHLLVLPVSHN-FP-----MSSP-------GFLGVI----YAGATLVI--ADNSSPTECFGLIERHKITQTSLVPS- 282
Cdd:cd05971   115 ---GHLPGVQFPFNlFPrdgdlYWTPadwawigGLLDVLlpslYFGVPVLAhrMTKFDPKAALDLMSRYGVTTAFLPPTa 191
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 283 LVVAWLNSAMIDKFDLSsLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAEGLVNYTRLDDNREVQINTQGKRLSDFD 362
Cdd:cd05971   192 LKMMRQQGEQLKHAQVK-LRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNCSALFPIKPGSMGKPIPGHR 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 363 eIQILDLEGKVLGVGEVGVITTR--GPYTINAYFAPDEVNKRSFTEDgFYITGDLGYLDENNNITVTGRLKEVINRAGEK 440
Cdd:cd05971   271 -VAIVDDNGTPLPPGEVGEIAVElpDPVAFLGYWNNPSATEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYR 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 441 IMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITD---------KPDNFNLVKVRkyltqqhIALNKLPDVVSVV 511
Cdd:cd05971   349 IGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNpgetpsdalAREIQELVKTR-------LAAHEYPREIEFV 421
                         490
                  ....*....|...
gi 1436945972 512 DEFDFTLIGKVRR 524
Cdd:cd05971   422 NELPRTATGKIRR 434
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
179-522 8.39e-20

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: 92.64  E-value: 8.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 179 PVDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSvresavvanLQQDTKHLL-VLPVSHNFPMSSPGFL--------GVIY 249
Cdd:cd17634   228 AMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVY---------AATTMKYVFdYGPGDIYWCTADVGWVtghsyllyGPLA 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 250 AGATLVIADNS----SPTECFGLIERHKITQTSLVPSLV--VAWLNSAMIDKFDLSSLEVVQVGGAKFSSE---LAARLL 320
Cdd:cd17634   299 CGATTLLYEGVpnwpTPARMWQVVDKHGVNILYTAPTAIraLMAAGDDAIEGTDRSSLRILGSVGEPINPEayeWYWKKI 378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 321 DTLDLTLQQVYGMAE---GLVNYTRLDDNREVQINTQ---GKRlsdfdeIQILDLEGKVLGVGEVG--VITTRGPYTINA 392
Cdd:cd17634   379 GKEKCPVVDTWWQTEtggFMITPLPGAIELKAGSATRpvfGVQ------PAVVDNEGHPQPGGTEGnlVITDPWPGQTRT 452
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 393 YFAPDEVNKRSF--TEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLG 470
Cdd:cd17634   453 LFGDHERFEQTYfsTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKG 532
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1436945972 471 EKICVQII-----TDKPDNFNlvKVRKYLTQQhIALNKLPDVVSVVDEFDFTLIGKV 522
Cdd:cd17634   533 QAPYAYVVlnhgvEPSPELYA--ELRNWVRKE-IGPLATPDVVHWVDSLPKTRSGKI 586
PRK09192 PRK09192
fatty acyl-AMP ligase;
178-477 1.84e-19

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 91.61  E-value: 1.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 178 QPVDSRAVAFLQLSGGTTGLPKLIPRTHddylysvreSAVVANLQQDTKH-LLV---------LPVSHNfpMSSPGFLgv 247
Cdd:PRK09192  171 PRPTPDDIAYLQYSSGSTRFPRGVIITH---------RALMANLRAISHDgLKVrpgdrcvswLPFYHD--MGLVGFL-- 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 248 iyagATLVIADNSS---PTECFG--------LIERHKITqTSLVPS----LVVAWLNSAMIDKFDLSSLEVVQVGGAKFS 312
Cdd:PRK09192  238 ----LTPVATQLSVdylPTRDFArrplqwldLISRNRGT-ISYSPPfgyeLCARRVNSKDLAELDLSCWRVAGIGADMIR 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 313 SEL----AARLLDTLDLTLQQV--YGMAEG----------------LVNYTRL-DDNREVQINTQGKRLSDF-------- 361
Cdd:PRK09192  313 PDVlhqfAEAFAPAGFDDKAFMpsYGLAEAtlavsfsplgsgivveEVDRDRLeYQGKAVAPGAETRRVRTFvncgkalp 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 362 -DEIQILDLEGKVLGVGEVGVITTRGPYTINAYFApDEVNKRSFTEDGFYITGDLGYLdENNNITVTGRLKEVINRAGEK 440
Cdd:PRK09192  393 gHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFR-DEESQDVLAADGWLDTGDLGYL-LDGYLYITGRAKDLIIINGRN 470
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1436945972 441 IMPSEIEELLYAHPDVK--DVLVTGVPDElLGEKICVQI 477
Cdd:PRK09192  471 IWPQDIEWIAEQEPELRsgDAAAFSIAQE-NGEKIVLLV 508
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
65-522 2.77e-19

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


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 90.99  E-value: 2.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  65 LHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGALPI---FCLDghrSYEIGHIAKFSQARVYLrlckheSDSTAEQIIH 141
Cdd:PRK07786   59 LSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVpvnFRLT---PPEIAFLVSDCGAHVVV------TEAALAPVAT 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 142 HFSGDLPHLEIIKTVfqGELPQCD--GDRSKLKEKTH-YQPVD--SRAVAFLQLSGGTTGLPKLIPRTHDDyLYSVRESA 216
Cdd:PRK07786  130 AVRDIVPLLSTVVVA--GGSSDDSvlGYEDLLAEAGPaHAPVDipNDSPALIMYTSGTTGRPKGAVLTHAN-LTGQAMTC 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 217 VVANlQQDTKH---LLVLPVSHNFPMSS--PGFLgviyAGATLVIADNSS--PTECFGLIERHKITQTSLVPSLVVAWLN 289
Cdd:PRK07786  207 LRTN-GADINSdvgFVGVPLFHIAGIGSmlPGLL----LGAPTVIYPLGAfdPGQLLDVLEAEKVTGIFLVPAQWQAVCA 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 290 SAMIDKFDLSsLEVVQVGGAKFS-SELAARLLDTLDLTLQQVYGMAE-GLVNYTRLDDNREVQINTQGKRLsDFDEIQIL 367
Cdd:PRK07786  282 EQQARPRDLA-LRVLSWGAAPASdTLLRQMAATFPEAQILAAFGQTEmSPVTCMLLGEDAIRKLGSVGKVI-PTVAARVV 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 368 DLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFtEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIE 447
Cdd:PRK07786  360 DENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF-AGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVE 438
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1436945972 448 ELLYAHPDVKDVLVTGVPDELLGE-KICVQIITDKPDNFNLVKVRKYLTQQhIALNKLPDVVSVVDEFDFTLIGKV 522
Cdd:PRK07786  439 NVLASHPDIVEVAVIGRADEKWGEvPVAVAAVRNDDAALTLEDLAEFLTDR-LARYKHPKALEIVDALPRNPAGKV 513
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
193-461 1.00e-18

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: 88.48  E-value: 1.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 193 GTTGLPKLIPRTHDDylysvresavVANLQQDTKHLLVLPVSHNFPM-SSPGF-------LGVIYAGATLVIADNS---- 260
Cdd:TIGR01733 130 GSTGRPKGVVVTHRS----------LVNLLAWLARRYGLDPDDRVLQfASLSFdasveeiFGALLAGATLVVPPEDeerd 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 261 SPTECFGLIERHKITQTSLVPSLVVAWLNSamiDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQ-VYGMAEGLVN 339
Cdd:TIGR01733 200 DAALLAALIAEHPVTVLNLTPSLLALLAAA---LPPALASLRLVILGGEALTPALVDRWRARGPGARLInLYGPTETTVW 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 340 --YTRL--DDNREVQINTQGKRLSDFdEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGF------ 409
Cdd:TIGR01733 277 stATLVdpDDAPRESPVPIGRPLANT-RLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFaggdga 355
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1436945972 410 --YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLV 461
Cdd:TIGR01733 356 rlYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
139-504 1.10e-18

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 89.42  E-value: 1.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 139 IIHHFSGDL---PHLEIIKTVfqGELPQC---DGDRSKLKEKTH-----YQPVDSRAVAFLQLSGGTTGLPKLIPRTHDD 207
Cdd:PTZ00237  201 VITLFRNDItseSDLKKIETI--PTIPNTlswYDEIKKIKENNQspfyeYVPVESSHPLYILYTSGTTGNSKAVVRSNGP 278
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 208 YLYSVRESAvvANLQQDTKHLLVLPVSHNFPMSSPGFL-GVIYAGATLV------IADNSSPTECFGLIERHKITQTSLV 280
Cdd:PTZ00237  279 HLVGLKYYW--RSIIEKDIPTVVFSHSSIGWVSFHGFLyGSLSLGNTFVmfeggiIKNKHIEDDLWNTIEKHKVTHTLTL 356
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 281 PSlVVAWLN------SAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAEGLVNYTRLDDNREVQINTQ 354
Cdd:PTZ00237  357 PK-TIRYLIktdpeaTIIRSKYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGYGQTEIGITYLYCYGHINIPYNAT 435
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 355 GKRlSDFDEIQILDLEGKVLGVGEVGVITTRGPYT---INAYFAPDEVNKRSFTE-DGFYITGDLGYLDENNNITVTGRL 430
Cdd:PTZ00237  436 GVP-SIFIKPSILSEDGKELNVNEIGEVAFKLPMPpsfATTFYKNDEKFKQLFSKfPGYYNSGDLGFKDENGYYTIVSRS 514
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1436945972 431 KEVINRAGEKIMPSEIEELLYAHPDVKDvlvtgvpdellgekiCVQIITDKPDNFN----LVKVRKYLTQQHIALNKL 504
Cdd:PTZ00237  515 DDQIKISGNKVQLNTIETSILKHPLVLE---------------CCSIGIYDPDCYNvpigLLVLKQDQSNQSIDLNKL 577
PRK07514 PRK07514
malonyl-CoA synthase; Validated
363-522 1.36e-18

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 88.78  E-value: 1.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 363 EIQILDLE-GKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKI 441
Cdd:PRK07514  331 SLRVTDPEtGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNV 410
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 442 MPSEIEELLYAHPDVKDVLVTGVPDELLGEKIcVQIITDKPD-NFNLVKVRKYLTQQhIALNKLPDVVSVVDEFDFTLIG 520
Cdd:PRK07514  411 YPKEVEGEIDELPGVVESAVIGVPHPDFGEGV-TAVVVPKPGaALDEAAILAALKGR-LARFKQPKRVFFVDELPRNTMG 488

                  ..
gi 1436945972 521 KV 522
Cdd:PRK07514  489 KV 490
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
45-456 1.82e-18

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: 88.45  E-value: 1.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  45 GEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANvLEFFYVLFGLYYLGALPIFCLD---GHRSYEIGHIAKFSQA 121
Cdd:cd05931    21 REETLTYAELDRRARAIAARLQAVGKPGDRVLLLAPPG-LDFVAAFLGCLYAGAIAVPLPPptpGRHAERLAAILADAGP 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 122 RVYLrlckhesdSTAEQIihhfsgDLPHLEIIKTVFQGELPQCDGDRSKLKEKTHYQP--VDSRAVAFLQLSGGTTGLPK 199
Cdd:cd05931   100 RVVL--------TTAAAL------AAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPpsPDPDDIAYLQYTSGSTGTPK 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 200 LIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHNfpMSSPGFLGV-IYAGATLVIAdnsSPTEcF--------GLIE 270
Cdd:cd05931   166 GVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHD--MGLIGGLLTpLYSGGPSVLM---SPAA-FlrrplrwlRLIS 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 271 RHKITqTSLVPS----LVVAWLNSAMIDKFDLSSLEVVQVGG--------AKFSSELAA---RLLDTLDLtlqqvYGMAE 335
Cdd:cd05931   240 RYRAT-ISAAPNfaydLCVRRVRDEDLEGLDLSSWRVALNGAepvrpatlRRFAEAFAPfgfRPEAFRPS-----YGLAE 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 336 --GLVNYTRLDDNREV-----QINTQGKRLSDFD-----------------EIQILDLEG-KVLGVGEVGVITTRGPYTI 390
Cdd:cd05931   314 atLFVSGGPPGTGPVVlrvdrDALAGRAVAVAADdpaarelvscgrplpdqEVRIVDPETgRELPDGEVGEIWVRGPSVA 393
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1436945972 391 NAYFAPDEVNKRSF------TEDGFYITGDLGYLDENNnITVTGRLKEVINRAGEKIMPSEIEELLYAHPDV 456
Cdd:cd05931   394 SGYWGRPEATAETFgalaatDEGGWLRTGDLGFLHDGE-LYITGRLKDLIIVRGRNHYPQDIEATAEEAHPA 464
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
178-475 2.93e-18

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 88.44  E-value: 2.93e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  178 QPVDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHNF--------PMSSpGFLGVIY 249
Cdd:PRK08633   777 PTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFgltvtlwlPLLE-GIKVVYH 855
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  250 AgatlviadnsSPTECFG---LIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLT 326
Cdd:PRK08633   856 P----------DPTDALGiakLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIR 925
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  327 LQQVYGMAE----GLVNytrLDDNREVQINTQ--------GKRLSDFdEIQILDLE-GKVLGVGEVGVITTRGPYTINAY 393
Cdd:PRK08633   926 ILEGYGATEtspvASVN---LPDVLAADFKRQtgskegsvGMPLPGV-AVRIVDPEtFEELPPGEDGLILIGGPQVMKGY 1001
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  394 F-APDEVNK--RSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYA--HPDVKDVLVTGVPDEL 468
Cdd:PRK08633  1002 LgDPEKTAEviKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKalGGEEVVFAVTAVPDEK 1081

                   ....*..
gi 1436945972  469 LGEKICV 475
Cdd:PRK08633  1082 KGEKLVV 1088
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
190-524 3.07e-18

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 87.74  E-value: 3.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 190 LSGGTTGLPKLIPRTHddylySVRES-AVVANLQQDTKhllvLPVSHNFPMSSPGFLGVIYAGATLVIADNSSPtecfgL 268
Cdd:PRK13383  181 LTSGTTGKPKGVPRAP-----QLRSAvGVWVTILDRTR----LRTGSRISVAMPMFHGLGLGMLMLTIALGGTV-----L 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 269 IERH-----KITQTSL--------VPSLVVAWLN--SAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGM 333
Cdd:PRK13383  247 THRHfdaeaALAQASLhradaftaVPVVLARILElpPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGS 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 334 AE----GLVNYTRLDDNREvqinTQGKRLSDFdEIQILDLEGKVLGvgevgvittrgPYTINAYFAPDEVNKRSFTE--- 406
Cdd:PRK13383  327 TEvgigALATPADLRDAPE----TVGKPVAGC-PVRILDRNNRPVG-----------PRVTGRIFVGGELAGTRYTDggg 390
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 407 ----DGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKP 482
Cdd:PRK13383  391 kavvDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPG 470
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1436945972 483 DNFNLVKVRKYLtQQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:PRK13383  471 SGVDAAQLRDYL-KDRVSRFEQPRDINIVSSIPRNPTGKVLR 511
PRK07787 PRK07787
acyl-CoA synthetase; Validated
331-524 1.58e-17

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 85.04  E-value: 1.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 331 YGMAEGLVNY-TRLDDNRevQINTQGKRLSDFdEIQILDLEGKVLGV-GE-VGVITTRGPYTINAYFAPDEVNKRSFTED 407
Cdd:PRK07787  273 YGMTETLITLsTRADGER--RPGWVGLPLAGV-ETRLVDEDGGPVPHdGEtVGELQVRGPTLFDGYLNRPDATAAAFTAD 349
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 408 GFYITGDLGYLDENNNITVTGRLK-EVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIIT-DKPDNF 485
Cdd:PRK07787  350 GWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGaDDVAAD 429
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1436945972 486 NLVKvrkyLTQQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:PRK07787  430 ELID----FVAQQLSVHKRPREVRFVDALPRNAMGKVLK 464
PRK09088 PRK09088
acyl-CoA synthetase; Validated
363-524 1.82e-17

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 85.24  E-value: 1.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 363 EIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIM 442
Cdd:PRK09088  316 QTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVY 395
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 443 PSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPDNFNLVKVRKYLTQQhIALNKLPDVVSVVDEFDFTLIGKV 522
Cdd:PRK09088  396 PAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTR-LAKYKVPKHLRLVDALPRTASGKL 474

                  ..
gi 1436945972 523 RR 524
Cdd:PRK09088  475 QK 476
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
33-522 5.84e-17

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 83.65  E-value: 5.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  33 CQKFATNTALVLGEDEV------------SYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGALp 100
Cdd:PRK06018   12 CHRIIDHAARIHGNREVvtrsvegpivrtTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAI- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 101 ifCldgH----RSY--EIGHIAKFSQARVYLrlckheSDSTAEQIIHHFSGDLPHLE--IIKT--------------VFQ 158
Cdd:PRK06018   91 --C---HtvnpRLFpeQIAWIINHAEDRVVI------TDLTFVPILEKIADKLPSVEryVVLTdaahmpqttlknavAYE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 159 GELPQCDGDrSKLKEkthyqpVDSRAVAFLQLSGGTTGLPKLIprthddyLYSVRES---AVVANL-------QQDTkhl 228
Cdd:PRK06018  160 EWIAEADGD-FAWKT------FDENTAAGMCYTSGTTGDPKGV-------LYSHRSNvlhALMANNgdalgtsAADT--- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 229 lVLPVshnFPMSSPGFLGVIYA----GATLVIA----DNSSPTEcfgLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSS 300
Cdd:PRK06018  223 -MLPV---VPLFHANSWGIAFSapsmGTKLVMPgaklDGASVYE---LLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPH 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 301 LEVVQVGGAKFSSELAaRLLDTLDLTLQQVYGMAE----GLVN-----YTRL-DDNREVQINTQGK-------RLSDfDE 363
Cdd:PRK06018  296 LKMVVCGGSAMPRSMI-KAFEDMGVEVRHAWGMTEmsplGTLAalkppFSKLpGDARLDVLQKQGYppfgvemKITD-DA 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 364 IQILDLEGKVLGVGEVgvittRGPYTINAYFapdEVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMP 443
Cdd:PRK06018  374 GKELPWDGKTFGRLKV-----RGPAVAAAYY---RVDGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISS 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 444 SEIEELLYAHPDVKDVLVTGVPDELLGEKIcVQIITDKPD-NFNLVKVRKYLtQQHIALNKLPDVVSVVDEFDFTLIGKV 522
Cdd:PRK06018  446 IDLENLAVGHPKVAEAAVIGVYHPKWDERP-LLIVQLKPGeTATREEILKYM-DGKIAKWWMPDDVAFVDAIPHTATGKI 523
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
49-473 6.44e-17

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: 83.18  E-value: 6.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  49 VSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGalpifCLDGHRSyeighiakfsqarvylrlc 128
Cdd:cd17640     6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALG-----AVDVVRG------------------- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 129 kheSDSTAEQIIHHFSgdlpHLEIIKTVFQGelpqcdgdrsklkekthyqpvDSRAVAFLQLSGGTTGLPKLIPRTHDDY 208
Cdd:cd17640    62 ---SDSSVEELLYILN----HSESVALVVEN---------------------DSDDLATIIYTSGTTGNPKGVMLTHANL 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 209 LYSVRESAVVANLQQDTKHLLVLPVSHNFPMSSPGFLgvIYAGATLVIadnSSPTECFGLIERHKITQTSLVPSLvvaW- 287
Cdd:cd17640   114 LHQIRSLSDIVPPQPGDRFLSILPIWHSYERSAEYFI--FACGCSQAY---TSIRTLKDDLKRVKPHYIVSVPRL---We 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 288 -LNSAMIDKFDLSS---------------LEVVQVGGAKFSSELAaRLLDTLDLTLQQVYGMAE--GLVNYTRLDDNRev 349
Cdd:cd17640   186 sLYSGIQKQVSKSSpikqflflfflsggiFKFGISGGGALPPHVD-TFFEAIGIEVLNGYGLTEtsPVVSARRLKCNV-- 262
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 350 qINTQGKRLSDfDEIQILDLEGK-VLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGFYITGDLGYLDENNNITVTG 428
Cdd:cd17640   263 -RGSVGRPLPG-TEIKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTG 340
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1436945972 429 RLKEVIN-RAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKI 473
Cdd:cd17640   341 RAKDTIVlSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLGALI 386
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
355-524 8.15e-17

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: 83.28  E-value: 8.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 355 GKRLSDFDeIQILDLEGKVLGVGEVGVITTR-GPYTINAYFAP--DEVNKRSFTEDG-FYITGDLGYLDENNNITVTGRL 430
Cdd:cd05928   346 GKASPPYD-VQIIDDNGNVLPPGTEGDIGIRvKPIRPFGLFSGyvDNPEKTAATIRGdFYLTGDRGIMDEDGYFWFMGRA 424
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 431 KEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKP-DNFNLVKVRKYLtQQHI----ALNKLP 505
Cdd:cd05928   425 DDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQfLSHDPEQLTKEL-QQHVksvtAPYKYP 503
                         170
                  ....*....|....*....
gi 1436945972 506 DVVSVVDEFDFTLIGKVRR 524
Cdd:cd05928   504 RKVEFVQELPKTVTGKIQR 522
PLN03102 PLN03102
acyl-activating enzyme; Provisional
28-497 9.75e-17

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 83.14  E-value: 9.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  28 FFERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGAL--PIFC-L 104
Cdd:PLN03102   19 FLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVlnPINTrL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 105 DghrSYEIGHIAKFSQARVYLrlCKHESDSTAEQIIHHFSGD--LPHLEII--------KTVFQGELP-QC---DGDRSK 170
Cdd:PLN03102   99 D---ATSIAAILRHAKPKILF--VDRSFEPLAREVLHLLSSEdsNLNLPVIfiheidfpKRPSSEELDyECliqRGEPTP 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 171 LKEKTHYQPVDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHNFPMSSPgfLGVIYA 250
Cdd:PLN03102  174 SLVARMFRIQDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFT--WGTAAR 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 251 GATLVIADNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQv 330
Cdd:PLN03102  252 GGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRLGFQVMHA- 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 331 YGMAE--GLV-------NYTRLDDNREVQINT-QGKR---LSDFDEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPD 397
Cdd:PLN03102  331 YGLTEatGPVlfcewqdEWNRLPENQQMELKArQGVSilgLADVDVKNKETQESVPRDGKTMGEIVIKGSSIMKGYLKNP 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 398 EVNKRSFtEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQI 477
Cdd:PLN03102  411 KATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFV 489
                         490       500
                  ....*....|....*....|
gi 1436945972 478 ITDKPDNFNLVKVRKYLTQQ 497
Cdd:PLN03102  490 VLEKGETTKEDRVDKLVTRE 509
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
185-524 9.86e-17

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: 82.36  E-value: 9.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 185 VAFLQLSGGTTGLPKLIPRTHddylysvreSAVVANLQQDTKHLLVLPVSHNFPMSSPGF---LGVIYA----GATLVIA 257
Cdd:cd17653   107 LAYIIFTSGSTGIPKGVMVPH---------RGVLNYVSQPPARLDVGPGSRVAQVLSIAFdacIGEIFStlcnGGTLVLA 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 258 DNSSPtecFGLIERhKITQTSLVPSLVvawlnsAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLqqVYGMAEG- 336
Cdd:cd17653   178 DPSDP---FAHVAR-TVDALMSTPSIL------STLSPQDFPNLKTIFLGGEAVPPSLLDRWSPGRRLYN--AYGPTECt 245
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 337 -LVNYTRLDDNREVQIntqGKRLSDFDeIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGF------ 409
Cdd:cd17653   246 iSSTMTELLPGQPVTI---GKPIPNST-CYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFwpgsrm 321
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 410 YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYA-HPDVKDVLVTGVPDELlgekicVQIITdkPDNFNLV 488
Cdd:cd17653   322 YRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQsQPEVTQAAAIVVNGRL------VAFVT--PETVDVD 393
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1436945972 489 KVRKYLtQQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd17653   394 GLRSEL-AKHLPSYAVPDRIIALDSFPLTANGKVDR 428
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
178-524 3.90e-16

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 79.70  E-value: 3.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 178 QPVDSrAVAFLQLSGGTTGLPKLIPRTHDDYLYSVreSAVVANLQQDTKHLLVLPVSHNFPMSSpgFLGVIYAGATLVIA 257
Cdd:PRK07824   31 EPIDD-DVALVVATSGTTGTPKGAMLTAAALTASA--DATHDRLGGPGQWLLALPAHHIAGLQV--LVRSVIAGSEPVEL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 258 DNS---SPTECFGLIERHKI--TQTSLVPS-LVVAWLNSAMIDKfdLSSLEVVQVGGAKFSSELAARLLDTLDLTLQqVY 331
Cdd:PRK07824  106 DVSagfDPTALPRAVAELGGgrRYTSLVPMqLAKALDDPAATAA--LAELDAVLVGGGPAPAPVLDAAAAAGINVVR-TY 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 332 GMAE---GLVNYTRLDDNREVQINtqgkrlsdfdeiqildlEGKV-LGvgevgvittrGPYTINAYFAPDEvnKRSFTED 407
Cdd:PRK07824  183 GMSEtsgGCVYDGVPLDGVRVRVE-----------------DGRIaLG----------GPTLAKGYRNPVD--PDPFAEP 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 408 GFYITGDLGYLDeNNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPDNFNL 487
Cdd:PRK07824  234 GWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTL 312
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1436945972 488 VKVRKYLTQQhIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:PRK07824  313 EALRAHVART-LDRTAAPRELHVVDELPRRGIGKVDR 348
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
178-524 3.93e-16

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: 80.59  E-value: 3.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 178 QPVDsraVAFLQLSGGTTGLPKLIPRTHDDYlysvresAVVANLQQDTKHLLVLPVSH------NFPMSSPGFLGVIYAG 251
Cdd:cd17650    91 QPED---LAYVIYTSGTTGKPKGVMVEHRNV-------AHAAHAWRREYELDSFPVRLlqmasfSFDVFAGDFARSLLNG 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 252 ATLVIADNS---SPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGG----AKFSSELAARLLDTLD 324
Cdd:cd17650   161 GTLVICPDEvklDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSdgckAQDFKTLAARFGQGMR 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 325 LTLQqvYGMAEGLVN--YTRLDDNREVQINTQ--GKRLSDFdEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVN 400
Cdd:cd17650   241 IINS--YGVTEATIDstYYEEGRDPLGDSANVpiGRPLPNT-AMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELT 317
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 401 KRSFTEDGF------YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKIC 474
Cdd:cd17650   318 AERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLC 397
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1436945972 475 VQIITDkpDNFNLVKVRKYLTqQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd17650   398 AYVVAA--ATLNTAELRAFLA-KELPSYMIPSYYVQLDALPLTPNGKVDR 444
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
164-524 5.61e-16

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: 80.25  E-value: 5.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 164 CDGD-RSKLKEKThyqpvdsravaFLQLS-GGTTGLPKLIPrthddylYSVRESAVVANLQQDTkhLLVLPVSHNFPMSS 241
Cdd:cd05973    78 TDAAnRHKLDSDP-----------FVMMFtSGTTGLPKGVP-------VPLRALAAFGAYLRDA--VDLRPEDSFWNAAD 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 242 PGF-LGVIYA--------GATLVIADNSSPTECFGLIERHKITQTSLVP----SLVVAWLNSAMIDKfdlSSLEVVQVGG 308
Cdd:cd05973   138 PGWaYGLYYAitgplalgHPTILLEGGFSVESTWRVIERLGVTNLAGSPtayrLLMAAGAEVPARPK---GRLRRVSSAG 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 309 AKFSSELAARLLDTLDLTLQQVYGMAE-GLVNYTRLDDNREVQINTQGKRLSDFdEIQILDLEGKVLGVGEVGVIT---T 384
Cdd:cd05973   215 EPLTPEVIRWFDAALGVPIHDHYGQTElGMVLANHHALEHPVHAGSAGRAMPGW-RVAVLDDDGDELGPGEPGRLAidiA 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 385 RGP-YTINAYFAPDEvnkrSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTG 463
Cdd:cd05973   294 NSPlMWFRGYQLPDT----PAIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIG 369
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1436945972 464 VPDELLGE--KICVQIITDKPDNFNLVKVRKYLTQQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd05973   370 VPDPERTEvvKAFVVLRGGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQR 432
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
186-524 8.74e-16

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: 79.79  E-value: 8.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 186 AFLQLSGGTTGLPKLIPRTHDDYL-YSVRESAVVANLQQDtkHLLVLpVSHNFPMSSPGFLGVIYAGATLVIADN---SS 261
Cdd:cd17644   109 AYVIYTSGSTGKPKGVMIEHQSLVnLSHGLIKEYGITSSD--RVLQF-ASIAFDVAAEEIYVTLLSGATLVLRPEemrSS 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 262 PTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDL-SSLEVVQVGGAKFSSELAA--RLLDTLDLTLQQVYGMAEGLV 338
Cdd:cd17644   186 LEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLpSSLRLVIVGGEAVQPELVRqwQKNVGNFIQLINVYGPTEATI 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 339 NYT--RLDDNREVQIN--TQGKRLSDFdEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGF----- 409
Cdd:cd17644   266 AATvcRLTQLTERNITsvPIGRPIANT-QVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFnsses 344
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 410 ---YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPDNFN 486
Cdd:cd17644   345 erlYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPS 424
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1436945972 487 LVKVRKYLTqqhialNKLPDVV-----SVVDEFDFTLIGKVRR 524
Cdd:cd17644   425 TVELRQFLK------AKLPDYMipsafVVLEELPLTPNGKIDR 461
PRK08308 PRK08308
acyl-CoA synthetase; Validated
412-524 1.18e-15

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 78.92  E-value: 1.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 412 TGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPdnFNLVKVR 491
Cdd:PRK08308  295 TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEE--IDPVQLR 372
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1436945972 492 KYlTQQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:PRK08308  373 EW-CIQHLAPYQVPHEIESVTEIPKNANGKVSR 404
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
34-524 1.65e-15

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: 78.83  E-value: 1.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  34 QKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGA--LPIfclDGHrsye 111
Cdd:cd05945     2 AANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHayVPL---DAS---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 112 ighiakfsqarvylrlckhesdSTAEQIihhfsgdlphLEIIKTVfQGELPQCDGDrsklkekthyqpvdsrAVAFLQLS 191
Cdd:cd05945    75 ----------------------SPAERI----------REILDAA-KPALLIADGD----------------DNAYIIFT 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 192 GGTTGLPKLIPRTHD---------DYLYSVRESAVVANlQQDtkhllvlpvsHNFPMSSPGFLGVIYAGATLVIADN--- 259
Cdd:cd05945   106 SGSTGRPKGVQISHDnlvsftnwmLSDFPLGPGDVFLN-QAP----------FSFDLSVMDLYPALASGATLVPVPRdat 174
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 260 SSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTL-DLTLQQVYGMAE--G 336
Cdd:cd05945   175 ADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEatV 254
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 337 LVNYTR-----LDDNREVQIntqGKRLSDFDeIQILDLEGKVLGVGEVGVITTRGPYTINAYFA-PDEVNKRSFTEDGF- 409
Cdd:cd05945   255 AVTYIEvtpevLDGYDRLPI---GYAKPGAK-LVILDEDGRPVPPGEKGELVISGPSVSKGYLNnPEKTAAAFFPDEGQr 330
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 410 -YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPDNF-NL 487
Cdd:cd05945   331 aYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAgLT 410
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 1436945972 488 VKVRKYLtQQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd05945   411 KAIKAEL-AERLPPYMIPRRFVYLDELPLNANGKIDR 446
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
135-463 1.70e-15

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 79.05  E-value: 1.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 135 TAEQIIHH------FSGDLPHLEIIKTVFQGELP----------QCDGDRSKLKEKthYQPVDSRAVAF------LQLSG 192
Cdd:cd05932    69 TIRYVLEHseskalFVGKLDDWKAMAPGVPEGLIsislpppsaaNCQYQWDDLIAQ--HPPLEERPTRFpeqlatLIYTS 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 193 GTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHNFPMSSPgFLGVIYAGATLVIADN----------SSP 262
Cdd:cd05932   147 GTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFV-EGGSLYGGVLVAFAESldtfvedvqrARP 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 263 TECFGlIER----------HKITQTSLVPSLVVAWLNSaMIDKFDLSSLEVVQV----GGAKFSSELAARLLDTLDLTLQ 328
Cdd:cd05932   226 TLFFS-VPRlwtkfqqgvqDKIPQQKLNLLLKIPVVNS-LVKRKVLKGLGLDQCrlagCGSAPVPPALLEWYRSLGLNIL 303
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 329 QVYGMAEGLVnYTRLDDNREVQINTQGKRLSDFdEIQIldlegkvlgvGEVGVITTRGPYTINAYFAPDEVNKRSFTEDG 408
Cdd:cd05932   304 EAYGMTENFA-YSHLNYPGRDKIGTVGNAGPGV-EVRI----------SEDGEILVRSPALMMGYYKDPEATAEAFTADG 371
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1436945972 409 FYITGDLGYLDENNNITVTGRLKEVINRA-GEKIMPSEIEELLYAHPDVKDVLVTG 463
Cdd:cd05932   372 FLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIG 427
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
180-488 2.34e-15

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


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 78.70  E-value: 2.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 180 VDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHNFPMSSPGFLGVIyAGATLVIADN 259
Cdd:PRK06334  180 KDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLL-SGVPVVFAYN 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 260 S-SPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTL-DLTLQQVYGMAE-- 335
Cdd:PRK06334  259 PlYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFpHIQLRQGYGTTEcs 338
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 336 ---GLVNYTRLDDNREVQINTQGKrlsdfdEIQILDLEGKV-LGVGEVGVITTRGPYTINAYFAPDEvnKRSFTE---DG 408
Cdd:PRK06334  339 pviTINTVNSPKHESCVGMPIRGM------DVLIVSEETKVpVSSGETGLVLTRGTSLFSGYLGEDF--GQGFVElggET 410
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 409 FYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAH------PDVKDVLVTGVPdellGEKICVQIITDKP 482
Cdd:PRK06334  411 WYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGfgqnaaDHAGPLVVCGLP----GEKVRLCLFTTFP 486

                  ....*.
gi 1436945972 483 DNFNLV 488
Cdd:PRK06334  487 TSISEV 492
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
27-524 4.29e-15

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: 77.70  E-value: 4.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  27 EFFERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGA--LPifcL 104
Cdd:cd17646     2 ALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAayLP---L 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 105 D-GHRSYEIGHIAKFSQARVYLrlckhesdsTAEQIIHHFSGDLPHLEIIKTVF---QGELPQcdgdrsklkekthyQPV 180
Cdd:cd17646    79 DpGYPADRLAYMLADAGPAVVL---------TTADLAARLPAGGDVALLGDEALaapPATPPL--------------VPP 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 181 DSRAVAFLQLSGGTTGLPKLIPRTHddylysvresAVVAN--LQQDTKHLL-----VL---PVShnFPMSSPGFLGVIYA 250
Cdd:cd17646   136 RPDNLAYVIYTSGSTGRPKGVMVTH----------AGIVNrlLWMQDEYPLgpgdrVLqktPLS--FDVSVWELFWPLVA 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 251 GATLVIAD---NSSPTECFGLIERHKITQTSLVPSLVVAWLNSAmiDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTL 327
Cdd:cd17646   204 GARLVVARpggHRDPAYLAALIREHGVTTCHFVPSMLRVFLAEP--AAGSCASLRRVFCSGEALPPELAARFLALPGAEL 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 328 QQVYGMAEGLVN-----YTRLDDNREVQI-----NTQgkrlsdfdeIQILDLEGKVLGVGEVGVITTRGPYTINAYF-AP 396
Cdd:cd17646   282 HNLYGPTEAAIDvthwpVRGPAETPSVPIgrpvpNTR---------LYVLDDALRPVPVGVPGELYLGGVQLARGYLgRP 352
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 397 DEVNKRsFTEDGF------YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLG 470
Cdd:cd17646   353 ALTAER-FVPDPFgpgsrmYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGA 431
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1436945972 471 EKIcVQIITDKPDNF--NLVKVRKYLTqQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd17646   432 ARL-VGYVVPAAGAAgpDTAALRAHLA-ERLPEYMVPAAFVVLDALPLTANGKLDR 485
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
27-524 4.86e-15

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: 77.63  E-value: 4.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  27 EFFERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGA--LPIfcl 104
Cdd:cd12117     1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAayVPL--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 105 dgHRSYEIGHIAK-FSQARVYLRLCKHESdstaeqiihhfsGDLPHLEIIKTVFQGELPQCDGDRSKLkekthyqPVDSR 183
Cdd:cd12117    78 --DPELPAERLAFmLADAGAKVLLTDRSL------------AGRAGGLEVAVVIDEALDAGPAGNPAV-------PVSPD 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 184 AVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVAnLQQDTKHLLVLPVShnFPMSSPGFLGVIYAGATLVIADNS--- 260
Cdd:cd12117   137 DLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNTNYVT-LGPDDRVLQTSPLA--FDASTFEIWGALLNGARLVLAPKGtll 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 261 SPTECFGLIERHKITqtslvpslvVAWLNSAMidkFD---------LSSLEVVQVGGAKFSSELAARLLDTL-DLTLQQV 330
Cdd:cd12117   214 DPDALGALIAEEGVT---------VLWLTAAL---FNqladedpecFAGLRELLTGGEVVSPPHVRRVLAACpGLRLVNG 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 331 YGMAEGLVNYTRL------DDNREVQIntqGKRLSDfDEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSF 404
Cdd:cd12117   282 YGPTENTTFTTSHvvteldEVAGSIPI---GRPIAN-TRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERF 357
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 405 TEDGF------YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQII 478
Cdd:cd12117   358 VADPFgpgerlYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVV 437
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1436945972 479 TDKPdnFNLVKVRKYLTQqhialnKLPD-----VVSVVDEFDFTLIGKVRR 524
Cdd:cd12117   438 AEGA--LDAAELRAFLRE------RLPAymvpaAFVVLDELPLTANGKVDR 480
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
45-521 6.04e-15

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 77.52  E-value: 6.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  45 GEDEVSYEAFYFKALAWGEWLHEQ-GVRKDDLVVLQSANVLEFFYVLFGLYYLGAlpIFC-LDGHRS-YEIGHIAKFSQA 121
Cdd:PRK05620   35 EQEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGA--VFNpLNKQLMnDQIVHIINHAED 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 122 RVYLRLCKhesdsTAEQ---IIHH--------FSG----------DLPHLEIikTVFQGELpqcDGdRSklkekTHYQ-P 179
Cdd:PRK05620  113 EVIVADPR-----LAEQlgeILKEcpcvravvFIGpsdadsaaahMPEGIKV--YSYEALL---DG-RS-----TVYDwP 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 180 -VDSRAVAFLQLSGGTTGLPKLIPRTHDD-YLYS--VRESAVVAnLQQDTKHLLVLPVSHNFPMSSPgfLGVIYAGATLV 255
Cdd:PRK05620  177 eLDETTAAAICYSTGTTGAPKGVVYSHRSlYLQSlsLRTTDSLA-VTHGESFLCCVPIYHVLSWGVP--LAAFMSGTPLV 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 256 I--ADNSSPTECfglierhKITQTSL------VPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTL 327
Cdd:PRK05620  254 FpgPDLSAPTLA-------KIIATAMprvahgVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDV 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 328 QQVYGMAE------------GLVNYTRlDDNREvqinTQGkRLSDFDEIQILDlEGKVLGVGE--VGVITTRGPYTINAY 393
Cdd:PRK05620  327 VHVWGMTEtspvgtvarppsGVSGEAR-WAYRV----SQG-RFPASLEYRIVN-DGQVMESTDrnEGEIQVRGNWVTASY 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 394 FAPD----------------EVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVK 457
Cdd:PRK05620  400 YHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVV 479
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1436945972 458 DVLVTGVPDELLGEK-ICVQIITD--KPDNFNLVKVRKYLTQQhIALNKLPDVVSVVDEFDFTLIGK 521
Cdd:PRK05620  480 ECAVIGYPDDKWGERpLAVTVLAPgiEPTRETAERLRDQLRDR-LPNWMLPEYWTFVDEIDKTSVGK 545
ttLC_FACS_like cd05915
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
178-524 1.04e-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. 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: 76.70  E-value: 1.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 178 QPVDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTK--HLLVLPVSHnfpMSSPGFLGVI--YAGAT 253
Cdd:cd05915   148 VRVPERAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKdvVLPVVPMFH---VNAWCLPYAAtlVGAKQ 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 254 LVIADNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAmiDKFDLSSLEVVQV-GGAKFSSELAARLLDTLDLTLQQVYG 332
Cdd:cd05915   225 VLPGPRLDPASLVELFDGEGVTFTAGVPTVWLALADYL--ESTGHRLKTLRRLvVGGSAAPRSLIARFERMGVEVRQGYG 302
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 333 MAE---------GLVNYTRLDDNREVQINTQGKrLSDFDE-IQILD-------LEGKVlgvgeVGVITTRGPYTINAYFA 395
Cdd:cd05915   303 LTEtspvvvqnfVKSHLESLSEEEKLTLKAKTG-LPIPLVrLRVADeegrpvpKDGKA-----LGEVQLKGPWITGGYYG 376
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 396 PDEVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICV 475
Cdd:cd05915   377 NEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLA 456
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1436945972 476 qIITDKPDNFNLVKVRKYLTQQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd05915   457 -VVVPRGEKPTPEELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGKFLK 504
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
50-517 2.73e-14

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 75.08  E-value: 2.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  50 SYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGALPIFCLDGHRSYEIGHIAKFSQARVYLrlck 129
Cdd:cd05940     5 TYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV---- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 130 hesdstaeqiihhfsgdlphleiiktvfqgelpqcdgdrsklkekthyqpVDSravAFLQLSGGTTGLPKLIPRTHDDYL 209
Cdd:cd05940    81 --------------------------------------------------VDA---ALYIYTSGTTGLPKAAIISHRRAW 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 210 ysvRESAVVA----NLQQDTKHLlVLPVSHNfPMSSPGFLGVIYAGATLVIADNSSPTECFGLIERHKITQTSLVPSLVV 285
Cdd:cd05940   108 ---RGGAFFAgsggALPSDVLYT-CLPLYHS-TALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGELCR 182
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 286 AWLNSAMIDKFDLSSLEVVQVGGAKFS--SELAARLLDTLDLTlqqVYGMAEG---LVNYTRLDD----NREVQINTQGK 356
Cdd:cd05940   183 YLLNQPPKPTERKHKVRMIFGNGLRPDiwEEFKERFGVPRIAE---FYAATEGnsgFINFFGKPGaigrNPSLLRKVAPL 259
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 357 RLSDFDEIQ---ILDLEGKV--LGVGEVGV----ITTRGPYTinAYFAPDEVNKRSFTE-----DGFYITGDLGYLDENN 422
Cdd:cd05940   260 ALVKYDLESgepIRDAEGRCikVPRGEPGLlisrINPLEPFD--GYTDPAATEKKILRDvfkkgDAWFNTGDLMRLDGEG 337
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 423 NITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKI-CVQIITDKPDNFNLVKVRKYLtQQHIAL 501
Cdd:cd05940   338 FWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAgMAAIVLQPNEEFDLSALAAHL-EKNLPG 416
                         490
                  ....*....|....*.
gi 1436945972 502 NKLPDVVSVVDEFDFT 517
Cdd:cd05940   417 YARPLFLRLQPEMEIT 432
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
407-497 2.74e-14

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 75.03  E-value: 2.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 407 DGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKIcVQIITDKPDNFN 486
Cdd:PRK07445  323 QGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVV-TAIYVPKDPSIS 401
                          90
                  ....*....|.
gi 1436945972 487 LVKVRKYLTQQ 497
Cdd:PRK07445  402 LEELKTAIKDQ 412
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
193-524 3.48e-14

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: 75.22  E-value: 3.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 193 GTTGLPKLIPRTHDDY-LYSVRESAVVANLQQDTkhlLVLPVSHNFPMSSPGFL-GVIYAGATLVI----ADNSSPTECF 266
Cdd:cd05968   246 GTTGKPKGTVHVHAGFpLKAAQDMYFQFDLKPGD---LLTWFTDLGWMMGPWLIfGGLILGATMVLydgaPDHPKADRLW 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 267 GLIERHKITQTSLVPSLVVAWL--NSAMIDKFDLSSLEVVQVGGAKFSSElaarlldTLDLTLQQVYGMAEGLVNYTrld 344
Cdd:cd05968   323 RMVEDHEITHLGLSPTLIRALKprGDAPVNAHDLSSLRVLGSTGEPWNPE-------PWNWLFETVGKGRNPIINYS--- 392
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 345 DNREVQINTQGKRL------SDFD------EIQILDLEGKVLgVGEVGVITTRGPYT-------------INAYFapdev 399
Cdd:cd05968   393 GGTEISGGILGNVLikpikpSSFNgpvpgmKADVLDESGKPA-RPEVGELVLLAPWPgmtrgfwrdedryLETYW----- 466
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 400 nkRSFteDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIIT 479
Cdd:cd05968   467 --SRF--DNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVL 542
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1436945972 480 dKPDNFNLVKVRKYL---TQQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd05968   543 -KPGVTPTEALAEELmerVADELGKPLSPERILFVKDLPKTRNAKVMR 589
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
181-524 3.60e-14

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: 74.60  E-value: 3.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 181 DSRAVAFLQLSG---------GTTGLPKLIPRTHddylysvresAVVANLQQD-TKHLLVLPVSHNFPMSSPGFLGVIY- 249
Cdd:cd17652    82 DARPALLLTTPDnlayviytsGSTGRPKGVVVTH----------RGLANLAAAqIAAFDVGPGSRVLQFASPSFDASVWe 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 250 ------AGATLVIADNS---SPTECFGLIERHKITQTSLVPSlVVAWLNSAmidkfDLSSLEVVQVGGAKFSSELAARLL 320
Cdd:cd17652   152 llmallAGATLVLAPAEellPGEPLADLLREHRITHVTLPPA-ALAALPPD-----DLPDLRTLVVAGEACPAELVDRWA 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 321 DTLDLTLQqvYGMAEGLVNYTR---LDDNREVQINT--QGKRLSdfdeiqILDLEGKVLGVGEVGVITTRGPYTINAYFA 395
Cdd:cd17652   226 PGRRMINA--YGPTETTVCATMagpLPGGGVPPIGRpvPGTRVY------VLDARLRPVPPGVPGELYIAGAGLARGYLN 297
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 396 PDEVNKRSFTEDGF-------YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTgVPDEL 468
Cdd:cd17652   298 RPGLTAERFVADPFgapgsrmYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVV-VRDDR 376
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 469 LGEK----ICVQIITDKPDNFNLvkvRKYLTQQHIAlNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd17652   377 PGDKrlvaYVVPAPGAAPTAAEL---RAHLAERLPG-YMVPAAFVVLDALPLTPNGKLDR 432
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
29-524 5.12e-14

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: 74.30  E-value: 5.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  29 FERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGA--LPifcLD- 105
Cdd:cd17651     1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAayVP---LDp 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 106 GHRSYEIGHIAKFSQARVYLRlckHEsdstaeqiihHFSGDLPHLEIIKT-VFQGELPQCDGDRsklkektHYQPVDSRA 184
Cdd:cd17651    78 AYPAERLAFMLADAGPVLVLT---HP----------ALAGELAVELVAVTlLDQPGAAAGADAE-------PDPALDADD 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 185 VAFLQLSGGTTGLPKLIprthddylysVRESAVVANL-QQDTKHLLVLPVSHNFPMSSPGF-------LGVIYAGATLVI 256
Cdd:cd17651   138 LAYVIYTSGSTGRPKGV----------VMPHRSLANLvAWQARASSLGPGARTLQFAGLGFdvsvqeiFSTLCAGATLVL 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 257 ADNS---SPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQV--Y 331
Cdd:cd17651   208 PPEEvrtDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLVLTEDLREFCAGLPGLRLHnhY 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 332 GMAEG-LVNYTRLDdnreVQINTQGKRLS-----DFDEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFT 405
Cdd:cd17651   288 GPTEThVVTALSLP----GDPAAWPAPPPigrpiDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFV 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 406 EDGF------YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDElLGEKICVQIIT 479
Cdd:cd17651   364 PDPFvpgarmYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDR-PGEKRLVAYVV 442
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 1436945972 480 DKPDNFNLVKVRKYLTQQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd17651   443 GDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDR 487
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
363-524 6.40e-14

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 74.13  E-value: 6.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 363 EIQILDLEGKVLGVGEVGVITTRGPY-----TI--------NAYFAPDEvnkrsftedGFYITGDLGYLDENNNITVTGR 429
Cdd:cd05966   420 EPAILDEEGNEVEGEVEGYLVIKRPWpgmarTIygdheryeDTYFSKFP---------GYYFTGDGARRDEDGYYWITGR 490
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 430 LKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVqIITDKPDNFNLVKVRKYLTQQ---HIALNKLPD 506
Cdd:cd05966   491 VDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYA-FVTLKDGEEPSDELRKELRKHvrkEIGPIATPD 569
                         170
                  ....*....|....*....
gi 1436945972 507 VVSVVDEFDFTLIGKV-RR 524
Cdd:cd05966   570 KIQFVPGLPKTRSGKImRR 588
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
193-524 7.08e-14

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: 73.50  E-value: 7.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 193 GTTGLPKLIPRTHddylysvresAVVANLQQDTKHLL--------VLPVSHNFPMSSPGFLGVIYAGATLVIADNS---S 261
Cdd:cd17643   103 GSTGRPKGVVVSH----------ANVLALFAATQRWFgfneddvwTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEvarS 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 262 PTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQV---YGMAEG-- 336
Cdd:cd17643   173 PEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLDRPQLvnmYGITETtv 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 337 LVNYTRLD--DNREVQINTQGKRLSDFdEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGF----- 409
Cdd:cd17643   253 HVTFRPLDaaDLPAAAASPIGRPLPGL-RVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFggpgs 331
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 410 --YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPDNFNL 487
Cdd:cd17643   332 rmYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADI 411
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1436945972 488 VKVRKYLtQQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd17643   412 AELRALL-KELLPDYMVPARYVPLDALPLTVNGKLDR 447
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
39-524 1.52e-13

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: 72.71  E-value: 1.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  39 NTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVL---QSANVLeffYVLFGLYYLGA--LPifcLD-GHRSYEI 112
Cdd:cd12116     3 ATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVylpRSARLV---AAMLAVLKAGAayVP---LDpDYPADRL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 113 GHIAKfsQARVYLRLCkheSDSTAEQIIHhfSGDLPHLEIIKTVFQGELPQcdgdrsklkekthyQPVDSRAVAFLQLSG 192
Cdd:cd12116    77 RYILE--DAEPALVLT---DDALPDRLPA--GLPVLLLALAAAAAAPAAPR--------------TPVSPDDLAYVIYTS 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 193 GTTGLPKLIPRTH---DDYLYSVRESAvvaNLQQDTKHLLVLPVShnFPMSSPGFLGVIYAGATLVIA---DNSSPTECF 266
Cdd:cd12116   136 GSTGRPKGVVVSHrnlVNFLHSMRERL---GLGPGDRLLAVTTYA--FDISLLELLLPLLAGARVVIApreTQRDPEALA 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 267 GLIERHKITQTSLVPS-----LVVAWLNSAmidkfdlsSLEVVqVGGAKFSSELAARLLDTLDLTLQqVYGMAEGLV--N 339
Cdd:cd12116   211 RLIEAHSITVMQATPAtwrmlLDAGWQGRA--------GLTAL-CGGEALPPDLAARLLSRVGSLWN-LYGPTETTIwsT 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 340 YTRLDD-NREVQI-----NTQgkrlsdfdeIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGF---- 409
Cdd:cd12116   281 AARVTAaAGPIPIgrplaNTQ---------VYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFagpg 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 410 ---YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVqIITDKPDNFN 486
Cdd:cd12116   352 srlYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAY-VVLKAGAAPD 430
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 1436945972 487 LVKVRKYLtQQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd12116   431 AAALRAHL-RATLPAYMVPSAFVRLDALPLTANGKLDR 467
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
173-524 3.58e-13

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: 71.63  E-value: 3.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 173 EKTHYQPVDSRA----------VAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVshNFPMSSP 242
Cdd:cd17649    74 ERLRYMLEDSGAglllthhprqLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASF--NFDGAHE 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 243 GFLGVIYAGATLVIADNS---SPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDL-SSLEVVQVGGAKFSSELAAR 318
Cdd:cd17649   152 QLLPPLICGACVVLRPDElwaSADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDGRpPSLRLYIFGGEALSPELLRR 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 319 LLDTLDLTLQQvYGMAEGLVNYTRLD---DNREVQINTQGKRLSDFDEIQILDLEGKVLGVGEVGVITTRGPYTINAYFA 395
Cdd:cd17649   232 WLKAPVRLFNA-YGPTEATVTPLVWKceaGAARAGASMPIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLG 310
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 396 PDEVNKRSFTEDGF-------YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDEl 468
Cdd:cd17649   311 RPELTAERFVPDPFgapgsrlYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGA- 389
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1436945972 469 LGEKICVQIITDKPDNFNLVKVRkylTQQHIAlNKLPD-----VVSVVDEFDFTLIGKVRR 524
Cdd:cd17649   390 GGKQLVAYVVLRAAAAQPELRAQ---LRTALR-ASLPDymvpaHLVFLARLPLTPNGKLDR 446
PRK12316 PRK12316
peptide synthase; Provisional
27-469 4.01e-13

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 72.68  E-value: 4.01e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972   27 EFFERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGALPIfCLDG 106
Cdd:PRK12316  3061 RLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYV-PLDP 3139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  107 HRSYEighiakfsqarvylRLCKHESDSTAEQIIHHFSGDLPHLEIIKTVFqgelpqCDGDRSKLKEKTHYQPVDSRAVA 186
Cdd:PRK12316  3140 EYPEE--------------RLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLD------LDRGDENYAEANPAIRTMPENLA 3199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  187 FLQLSGGTTGLPKLIPRTHDDYlySVRESAVVANLQQDTKHLLVLPVSHNFPMSSPGFLGVIYAGATLVIADN---SSPT 263
Cdd:PRK12316  3200 YVIYTSGSTGKPKGVGIRHSAL--SNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPedwRDPA 3277
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  264 ECFGLIERHKITQTSLVPSLVVAWLNSamIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLqqVYGMAEGLVNYTRL 343
Cdd:PRK12316  3278 LLVELINSEGVDVLHAYPSMLQAFLEE--EDAHRCTSLKRIVCGGEALPADLQQQVFAGLPLYN--LYGPTEATITVTHW 3353
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  344 DDNREVQINTQGKRLSDFDEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGF------YITGDLGY 417
Cdd:PRK12316  3354 QCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLAR 3433
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1436945972  418 LDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELL 469
Cdd:PRK12316  3434 YRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQL 3485
PRK12467 PRK12467
peptide synthase; Provisional
22-467 5.64e-13

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 72.12  E-value: 5.64e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972   22 GESLFEFFERSCQKFATNTALVLGEDEVSYEAFYFKA--LAWgeWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGA- 98
Cdd:PRK12467   511 PDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQAnrLAH--VLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGa 588
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972   99 -LPifcLDGHRSYEighiakfsqarvylRLCKHESDSTAEQIIHHfsgdlPHLeiiktvfQGELPQCDGDRS-----KLK 172
Cdd:PRK12467   589 yVP---LDPEYPQD--------------RLAYMLDDSGVRLLLTQ-----SHL-------LAQLPVPAGLRSlcldePAD 639
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  173 EKTHYQ------PVDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVShnFPMSSPGFLG 246
Cdd:PRK12467   640 LLCGYSghnpevALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFA--FDLGVTELFG 717
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  247 VIYAGATLVIADNS---SPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKfdLSSLEVVQVGGAKFSSELAARLLDTL 323
Cdd:PRK12467   718 ALASGATLHLLPPDcarDAEAFAALMADQGVTVLKIVPSHLQALLQASRVAL--PRPQRALVCGGEALQVDLLARVRALG 795
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  324 DLTLQQ-VYGMAEGLVNYTRL---DDNREVQINTQGKRLSDFDeIQILDLEGKVLGVGEVGVITTRG----------PYT 389
Cdd:PRK12467   796 PGARLInHYGPTETTVGVSTYelsDEERDFGNVPIGQPLANLG-LYILDHYLNPVPVGVVGELYIGGaglargyhrrPAL 874
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  390 INAYFAPDevnkrSFTEDG--FYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDE 467
Cdd:PRK12467   875 TAERFVPD-----PFGADGgrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGD 949
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
29-524 6.03e-13

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: 71.81  E-value: 6.03e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972   29 FERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGA--LPifcLD- 105
Cdd:COG1020    482 FEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAayVP---LDp 558
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  106 ---GHRsyeIGHIAKFSQARVYLrlckheSDSTAEQIIHHFSGDLPHLEiiktvfQGELPQCDGDRSKLkekthyqPVDS 182
Cdd:COG1020    559 aypAER---LAYMLEDAGARLVL------TQSALAARLPELGVPVLALD------ALALAAEPATNPPV-------PVTP 616
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  183 RAVAFLQLSGGTTGLPK--LIprTHD---DYLYSVREsavVANLQQDTKHLLVLPVShnFPMSSPGFLGVIYAGATLVIA 257
Cdd:COG1020    617 DDLAYVIYTSGSTGRPKgvMV--EHRalvNLLAWMQR---RYGLGPGDRVLQFASLS--FDASVWEIFGALLSGATLVLA 689
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  258 DNS---SPTECFGLIERHKITQTSLVPSLVVAWLNSAmidKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQ-VYGM 333
Cdd:COG1020    690 PPEarrDPAALAELLARHRVTVLNLTPSLLRALLDAA---PEALPSLRLVLVGGEALPPELVRRWRARLPGARLVnLYGP 766
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  334 AEGLV--NYTRLDDNREVQ----I-----NTQgkrlsdfdeIQILDLEGKVLGVGEVG--VIT----TRGpytinaYFAP 396
Cdd:COG1020    767 TETTVdsTYYEVTPPDADGgsvpIgrpiaNTR---------VYVLDAHLQPVPVGVPGelYIGgaglARG------YLNR 831
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  397 DEVNKRSFTEDGF-------YITGDLGYLDENNNITVTGRL----KevINraGEKIMPSEIEELLYAHPDVKDVLVTGVP 465
Cdd:COG1020    832 PELTAERFVADPFgfpgarlYRTGDLARWLPDGNLEFLGRAddqvK--IR--GFRIELGEIEAALLQHPGVREAVVVARE 907
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1436945972  466 DElLGEKICVQIITDKPDNFNLVKVRKYLTQQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:COG1020    908 DA-PGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDR 965
PRK08162 PRK08162
acyl-CoA synthetase; Validated
28-474 1.24e-12

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 69.98  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  28 FFERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGALpIFCLDGH 107
Cdd:PRK08162   23 FLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAV-LNTLNTR 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 108 RSYE-IGHIAKFSQARVYLrlckheSDSTAEQIIHHFSGDLPHLEIIktVFQGELPQCDGDRskLKEKTHYQ-------- 178
Cdd:PRK08162  102 LDAAsIAFMLRHGEAKVLI------VDTEFAEVAREALALLPGPKPL--VIDVDDPEYPGGR--FIGALDYEaflasgdp 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 179 ------PVDS-RAVAfLQLSGGTTGLPKLIPRTHDD-YLYSVrESAVVANLQQDTKHLLVLPVSH-N---FPMSspgflg 246
Cdd:PRK08162  172 dfawtlPADEwDAIA-LNYTSGTTGNPKGVVYHHRGaYLNAL-SNILAWGMPKHPVYLWTLPMFHcNgwcFPWT------ 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 247 VIYAGATLVIADNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLT 326
Cdd:PRK08162  244 VAARAGTNVCLRKVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAGAAPPAAVIAKMEEIGFDL 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 327 LQqVYGMAE----GLVN-----YTRLDDNREVQINT-QGKRLSDFDEIQILDLEG--KVLGVGE-VGVITTRGPYTINAY 393
Cdd:PRK08162  324 TH-VYGLTEtygpATVCawqpeWDALPLDERAQLKArQGVRYPLQEGVTVLDPDTmqPVPADGEtIGEIMFRGNIVMKGY 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 394 FAPDEVNKRSFtEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKI 473
Cdd:PRK08162  403 LKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVP 481

                  .
gi 1436945972 474 C 474
Cdd:PRK08162  482 C 482
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
188-468 3.54e-12

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: 68.36  E-value: 3.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 188 LQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVlpvshnfpmSSPG--------FLGVIYAGATLVIADN 259
Cdd:cd05974    90 LYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGDVHWNI---------SSPGwakhawscFFAPWNAGATVFLFNY 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 260 S--SPTECFGLIERHKITqTSLVPSLVVAWLNSAMIDKFDLSSLEVVQvGGAKFSSELAARLLDTLDLTLQQVYGMAEGl 337
Cdd:cd05974   161 ArfDAKRVLAALVRYGVT-TLCAPPTVWRMLIQQDLASFDVKLREVVG-AGEPLNPEVIEQVRRAWGLTIRDGYGQTET- 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 338 vnyTRLDDN---REVQINTQGKRLSDFdEIQILDLEGKVLGVGEVG-VITTRGPYTINAYFAPDEVNKRSFTEDGFYITG 413
Cdd:cd05974   238 ---TALVGNspgQPVKAGSMGRPLPGY-RVALLDPDGAPATEGEVAlDLGDTRPVGLMKGYAGDPDKTAHAMRGGYYRTG 313
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1436945972 414 DLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDEL 468
Cdd:cd05974   314 DIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPV 368
PRK07867 PRK07867
acyl-CoA synthetase; Validated
331-524 4.25e-12

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 68.55  E-value: 4.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 331 YGMAEGLVNYTRLDDNREVQINtqgkRLsdFDEIQILDLE-------------GKVLGVGEVG-VITTRGPYTINAYFAP 396
Cdd:PRK07867  297 FGSTEGGVAITRTPDTPPGALG----PL--PPGVAIVDPDtgtecppaedadgRLLNADEAIGeLVNTAGPGGFEGYYND 370
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 397 DEVNKRSFtEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQ 476
Cdd:PRK07867  371 PEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAA 449
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1436945972 477 IITDKPDNFNLVKVRKYLTQQ-HIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:PRK07867  450 LVLAPGAKFDPDAFAEFLAAQpDLGPKQWPSYVRVCAELPRTATFKVLK 498
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
366-473 6.38e-12

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 68.00  E-value: 6.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 366 ILDLEGKVLGVGEVG--VITTRGPYTINAYFAPDEVNKRSFtEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMP 443
Cdd:PRK04319  389 IVDDQGNELPPNRMGnlAIKKGWPSMMRGIWNNPEKYESYF-AGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGP 467
                          90       100       110
                  ....*....|....*....|....*....|
gi 1436945972 444 SEIEELLYAHPDVKDVLVTGVPDELLGEKI 473
Cdd:PRK04319  468 FEVESKLMEHPAVAEAGVIGKPDPVRGEII 497
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
365-474 7.15e-12

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 67.86  E-value: 7.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 365 QILDLEGKVLGVGEVG--VITT------RGPYT-----INAYFApdevnkrsfTEDGFYITGDLGYLDENNNITVTGRLK 431
Cdd:PRK00174  436 AVVDEEGNPLEGGEGGnlVIKDpwpgmmRTIYGdherfVKTYFS---------TFKGMYFTGDGARRDEDGYYWITGRVD 506
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1436945972 432 EVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKIC 474
Cdd:PRK00174  507 DVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIY 549
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
181-524 7.99e-12

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


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 67.42  E-value: 7.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 181 DSRAVAFLQLSGGTTGLPKLIprthddyLYSVRES---AVVANL-------QQDTkhllVLPVshnFPMSSPGFLGVIYA 250
Cdd:PRK07008  174 DENQASSLCYTSGTTGNPKGA-------LYSHRSTvlhAYGAALpdamglsARDA----VLPV---VPMFHVNAWGLPYS 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 251 ----GATLVIA----DNSSPTEcfgLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGA--------KFSSE 314
Cdd:PRK07008  240 apltGAKLVLPgpdlDGKSLYE---LIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSacppamirTFEDE 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 315 LAARLLDtldltlqqVYGMAE----GLV---NYTRLDDNREVQ---INTQGKRLSDFDeIQILDLEGKVL---GV--GEV 379
Cdd:PRK07008  317 YGVEVIH--------AWGMTEmsplGTLcklKWKHSQLPLDEQrklLEKQGRVIYGVD-MKIVGDDGRELpwdGKafGDL 387
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 380 GVittRGPYTINAYFAPDEvnkrSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDV 459
Cdd:PRK07008  388 QV---RGPWVIDRYFRGDA----SPLVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEA 460
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1436945972 460 LVTGVPDELLGEKICVqIITDKPD---------NFNLVKVRKYltqqhialnKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:PRK07008  461 ACIACAHPKWDERPLL-VVVKRPGaevtreellAFYEGKVAKW---------WIPDDVVFVDAIPHTATGKLQK 524
PRK12467 PRK12467
peptide synthase; Provisional
180-524 9.13e-12

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 68.26  E-value: 9.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  180 VDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVShnFPMSSPGFLGVIYAGATLVIADN 259
Cdd:PRK12467  3234 VMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFS--FDGAQERFLWTLICGGCLVVRDN 3311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  260 S--SPTECFGLIERHKITQTSLVPSLVVAWLNSAmiDKFDLSSLEVVQVGG-AKFSSELAARLLDTLDLTLQQVYGMAEG 336
Cdd:PRK12467  3312 DlwDPEELWQAIHAHRISIACFPPAYLQQFAEDA--GGADCASLDIYVFGGeAVPPAAFEQVKRKLKPRGLTNGYGPTEA 3389
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  337 LVNYTRLDDNREVQINTQ----GKRLSDFdEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGF--- 409
Cdd:PRK12467  3390 VVTVTLWKCGGDAVCEAPyapiGRPVAGR-SIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFsgs 3468
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  410 ----YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDElLGEKICVQIITDKPDNF 485
Cdd:PRK12467  3469 ggrlYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGA-GGKQLVAYVVPADPQGD 3547
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1436945972  486 NLVKVRKYLTqqhialNKLPDV-----VSVVDEFDFTLIGKVRR 524
Cdd:PRK12467  3548 WRETLRDHLA------ASLPDYmvpaqLLVLAAMPLGPNGKVDR 3585
PLN02479 PLN02479
acetate-CoA ligase
379-483 1.73e-11

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 66.41  E-value: 1.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 379 VGVITTRGPYTINAYFAPDEVNKRSFtEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKD 458
Cdd:PLN02479  402 MGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLE 480
                          90       100
                  ....*....|....*....|....*
gi 1436945972 459 VLVTGVPDELLGEKICVqIITDKPD 483
Cdd:PLN02479  481 ASVVARPDERWGESPCA-FVTLKPG 504
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
23-461 2.15e-11

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 66.61  E-value: 2.15e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972   23 ESLFEFFERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGA--LP 100
Cdd:PRK10252   458 TTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAawLP 537
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  101 ifcLDghRSYEIGHIAK-FSQARVYLRLckhesdSTAEQiihhfSGDLPHLEIIkTVFQGELPQCDGDRSKLKEKthyQP 179
Cdd:PRK10252   538 ---LD--TGYPDDRLKMmLEDARPSLLI------TTADQ-----LPRFADVPDL-TSLCYNAPLAPQGAAPLQLS---QP 597
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  180 VDSRAVAFlqlSGGTTGLPKLIPRTHDDYL---------YSVRESAVVAnlqQDTkhllvlPVShnFPMSSPGFLGVIYA 250
Cdd:PRK10252   598 HHTAYIIF---TSGSTGRPKGVMVGQTAIVnrllwmqnhYPLTADDVVL---QKT------PCS--FDVSVWEFFWPFIA 663
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  251 GATLVIADNSS---PTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQV--GGAKFSSELAARLLDTLDL 325
Cdd:PRK10252   664 GAKLVMAEPEAhrdPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVfcSGEALPADLCREWQQLTGA 743
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  326 TLQQVYGMAEGLVNYT-------RLDDNR--EVQI-----NTQgkrlsdfdeIQILDLEGKVLGVGEVGVITTRGPYTIN 391
Cdd:PRK10252   744 PLHNLYGPTEAAVDVSwypafgeELAAVRgsSVPIgypvwNTG---------LRILDARMRPVPPGVAGDLYLTGIQLAQ 814
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1436945972  392 AYFAPDEVNKRSFTEDGF------YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLV 461
Cdd:PRK10252   815 GYLGRPDLTASRFIADPFapgermYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVT 890
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
330-475 3.65e-11

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


Pssm-ID: 341296 [Multi-domain]  Cd Length: 569  Bit Score: 65.52  E-value: 3.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 330 VYGMAEGLVNYTRlddNREVQIntqgkrlsDFDEIQIlDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGF 409
Cdd:cd17641   354 LYGQTELAGAYTV---HRDGDV--------DPDTVGV-PFPGTEVRIDEVGEILVRSPGVFVGYYKNPEATAEDFDEDGW 421
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1436945972 410 YITGDLGYLDENNNITVTGRLKEVINRA-GEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICV 475
Cdd:cd17641   422 LHTGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQFIENKLKFSPYIAEAVVLGAGRPYLTAFICI 488
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
33-467 6.29e-11

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 64.51  E-value: 6.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  33 CQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEffyVLfgLYYLGALpifcldghrsyEI 112
Cdd:PRK09029   13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPE---TL--LAYLALL-----------QC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 113 GhiakfsqARVyLRLCKHESDSTAEQIihhfsgdLPHLEIIKTVFQGELPQCDGDRSK-LKEKTHYQPV--DSRAVAFLQ 189
Cdd:PRK09029   77 G-------ARV-LPLNPQLPQPLLEEL-------LPSLTLDFALVLEGENTFSALTSLhLQLVEGAHAVawQPQRLATMT 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 190 LSGGTTGLPKLIPRTHDDYLysvrESAV-VANL----QQDTkHLLVLPVSHnfpMSSpgfLGVIY----AGATLVIADNS 260
Cdd:PRK09029  142 LTSGSTGLPKAAVHTAQAHL----ASAEgVLSLmpftAQDS-WLLSLPLFH---VSG---QGIVWrwlyAGATLVVRDKQ 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 261 SPTECFglierHKITQTSLVPSLVVAWLNsamiDKFDLSSLEVVQVGGAKFSSELAARLLDTLdltlqqV-----YGM-- 333
Cdd:PRK09029  211 PLEQAL-----AGCTHASLVPTQLWRLLD----NRSEPLSLKAVLLGGAAIPVELTEQAEQQG------IrcwcgYGLte 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 334 ---------AEGLVNYTRLDDNREVqintqgkRLSDfDEIQIldlEGKVLGVGevgvittrgpytinaYFAPDEVnkRSF 404
Cdd:PRK09029  276 mastvcakrADGLAGVGSPLPGREV-------KLVD-GEIWL---RGASLALG---------------YWRQGQL--VPL 327
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1436945972 405 T-EDGFYITGDLGYLDeNNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDE 467
Cdd:PRK09029  328 VnDEGWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADA 390
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
193-522 1.55e-10

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: 63.26  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 193 GTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVShnFPMSSPGFLGVIYAGATLVIADNSSPTE--CFG--L 268
Cdd:cd17654   128 GTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLT--FDPSVVEIFLSLSSGATLLIVPTSVKVLpsKLAdiL 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 269 IERHKITQTSLVPSLVVAWLnSAMIDKFDLS---SLEVVQVGGAKF--SSELAARLLDTLDLTLQQVYGMAE----GLVN 339
Cdd:cd17654   206 FKRHRITVLQATPTLFRRFG-SQSIKSTVLSatsSLRVLALGGEPFpsLVILSSWRGKGNRTRIFNIYGITEvscwALAY 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 340 YTRLDDNrEVQINTQGKRLSdfdeIQILDLEG-KVLGVGEVGVITTRGpytinayFAPDEVNKRSFTedgFYITGDLGYL 418
Cdd:cd17654   285 KVPEEDS-PVQLGSPLLGTV----IEVRDQNGsEGTGQVFLGGLNRVC-------ILDDEVTVPKGT---MRATGDFVTV 349
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 419 dENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLgekicVQIITDKPdNFNLVKVRKYLTQQH 498
Cdd:cd17654   350 -KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQRL-----IAFIVGES-SSSRIHKELQLTLLS 422
                         330       340
                  ....*....|....*....|....
gi 1436945972 499 IAlnKLPDVVSVVDEFDFTLIGKV 522
Cdd:cd17654   423 SH--AIPDTFVQIDKLPLTSHGKV 444
PRK12316 PRK12316
peptide synthase; Provisional
24-461 1.72e-10

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 64.21  E-value: 1.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972   24 SLFEFFERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGA--LPi 101
Cdd:PRK12316   512 GVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGayVP- 590
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  102 fcLDGHRSYEighiakfsqarvylRLCKHESDSTAEQIIH--HFSGDLPhleiiktvFQGELPQCDGDRSKLKEKTHY-- 177
Cdd:PRK12316   591 --LDPEYPAE--------------RLAYMLEDSGVQLLLSqsHLGRKLP--------LAAGVQVLDLDRPAAWLEGYSee 646
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  178 ---QPVDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVShnFPMSSPGFLGVIYAGATL 254
Cdd:PRK12316   647 npgTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFS--FDVSVWEFFWPLMSGARL 724
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  255 VIA---DNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDkfDLSSLEVVQVGGAKFSSELAARLLDTL-DLTLQQV 330
Cdd:PRK12316   725 VVAapgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVA--SCTSLRRIVCSGEALPADAQEQVFAKLpQAGLYNL 802
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  331 YGMAEGLVNYT----RLDDNREVQIntqGKRLSDFdEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTE 406
Cdd:PRK12316   803 YGPTEAAIDVThwtcVEEGGDSVPI---GRPIANL-ACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVP 878
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1436945972  407 DGF------YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLV 461
Cdd:PRK12316   879 SPFvagermYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAV 939
PRK12316 PRK12316
peptide synthase; Provisional
2-465 2.02e-10

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 63.82  E-value: 2.02e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972    2 EFTLFPQERAETYIAngLW--------QGESLFEFFERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKD 73
Cdd:PRK12316  4524 ELQLLEKAEQQRIVA--LWnrtdagypATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPE 4601
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972   74 DLVVLQSANVLEFFYVLFGLYYLGA--LPifcLDGHRSYEighiakfsqarvylRLCKHESDSTAEQIIHHfSGDLPHLE 151
Cdd:PRK12316  4602 VLVGIAMERSAEMMVGLLAVLKAGGayVP---LDPEYPRE--------------RLAYMMEDSGAALLLTQ-SHLLQRLP 4663
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  152 IIKTVFQGELPQcDGDRSKLKEKTHYQPVDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVL 231
Cdd:PRK12316  4664 IPDGLASLALDR-DEDWEGFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFM 4742
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  232 PVShnFPMSSPGFLGVIYAGATLVIADNS--SPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKfDLSSLEVVQVGGA 309
Cdd:PRK12316  4743 SFS--FDGSHEGLYHPLINGASVVIRDDSlwDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDG-EPPSLRVYCFGGE 4819
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  310 KFSSELAARL-LDTLDLTLQQVYGMAEGLVNYTRLDDNREVQINTQ----GKRLSDFdEIQILDLEGKVLGVGEVGVITT 384
Cdd:PRK12316  4820 AVAQASYDLAwRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAAympiGTPLGNR-SGYVLDGQLNPLPVGVAGELYL 4898
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  385 RGPYTINAYFAPDEVNKRSFTEDGF-------YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVK 457
Cdd:PRK12316  4899 GGEGVARGYLERPALTAERFVPDPFgapggrlYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVR 4978

                   ....*...
gi 1436945972  458 DVLVTGVP 465
Cdd:PRK12316  4979 EAVVIAQE 4986
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
149-447 2.20e-10

long-chain-fatty acid--ACP ligase MbtM;


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 62.86  E-value: 2.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 149 HLEIIKTVfQGELPQCDGDRSKLKEK-THYQPVDSRAVAFLQLSGGTTGlpklIPRThddylYSVRESAVVANLQQDTKH 227
Cdd:PRK05851  118 HLERLRAV-DSSVTVHDLATAAHTNRsASLTPPDSGGPAVLQGTAGSTG----TPRT-----AILSPGAVLSNLRGLNAR 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 228 LLV----------LPVSHNfpMSSPGFLGVIYAGATLVIAdnssPTECFglierhkitqtSLVPSLVVAWL--------- 288
Cdd:PRK05851  188 VGLdaatdvgcswLPLYHD--MGLAFLLTAALAGAPLWLA----PTTAF-----------SASPFRWLSWLsdsratlta 250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 289 --NSA--MIDKF-------DLSSLEVVQVGG--------AKFSSELAarLLDTLDLTLQQVYGMAE------------GL 337
Cdd:PRK05851  251 apNFAynLIGKYarrvsdvDLGALRVALNGGepvdcdgfERFATAMA--PFGFDAGAAAPSYGLAEstcavtvpvpgiGL 328
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 338 -VNYTRLDDNREVQINTQGKRLSDFDEIQILDLEGKVLGVG-EVGVITTRGPYTINAYFAPDEVNKrsfteDGFYITGDL 415
Cdd:PRK05851  329 rVDEVTTDDGSGARRHAVLGNPIPGMEVRISPGDGAAGVAGrEIGEIEIRGASMMSGYLGQAPIDP-----DDWFPTGDL 403
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1436945972 416 GYLDENNnITVTGRLKEVINRAGEKIMPSEIE 447
Cdd:PRK05851  404 GYLVDGG-LVVCGRAKELITVAGRNIFPTEIE 434
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
180-524 2.76e-10

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: 62.33  E-value: 2.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 180 VDSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVShnFPMSSPGFLGVIYAGATLVIADN 259
Cdd:cd12115   102 TDPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEELAGVLASTSIC--FDLSVFELFGPLATGGKVVLADN 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 260 SsptecFGLIERHKITQTSL---VPSLVVAWLNsamIDKFDlSSLEVVQVGGAKFSSELAARLLDTLDLTLQQ-VYGMAE 335
Cdd:cd12115   180 V-----LALPDLPAAAEVTLintVPSAAAELLR---HDALP-ASVRVVNLAGEPLPRDLVQRLYARLQVERVVnLYGPSE 250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 336 GLVNYT----RLDDNREVQI-----NTQgkrlsdfdeIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTE 406
Cdd:cd12115   251 DTTYSTvapvPPGASGEVSIgrplaNTQ---------AYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLP 321
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 407 DGF------YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITD 480
Cdd:cd12115   322 DPFgpgarlYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAE 401
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1436945972 481 KPDNFNLVKVRKYLtQQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd12115   402 PGAAGLVEDLRRHL-GTRLPAYMVPSRFVRLDALPLTPNGKIDR 444
prpE PRK10524
propionyl-CoA synthetase; Provisional
364-471 2.94e-10

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 62.66  E-value: 2.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 364 IQILD-LEGKVLGVGEVGVITTRGPYT--------------INAYFapdevnkRSFTEDgFYITGDLGYLDENNNITVTG 428
Cdd:PRK10524  422 VKLLNeVTGEPCGPNEKGVLVIEGPLPpgcmqtvwgdddrfVKTYW-------SLFGRQ-VYSTFDWGIRDADGYYFILG 493
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1436945972 429 RLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGE 471
Cdd:PRK10524  494 RTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQ 536
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
330-463 1.51e-09

Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) 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. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It 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: 341256 [Multi-domain]  Cd Length: 596  Bit Score: 60.45  E-value: 1.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 330 VYGMAE--GLVNYTRLDDNRevqINTQGKRLSDfdeiqildLEGKVL-----GVGEvgvITTRGPYTINAYFAPDEVNKR 402
Cdd:cd05933   350 LYGMSEtsGPHTISNPQAYR---LLSCGKALPG--------CKTKIHnpdadGIGE---ICFWGRHVFMGYLNMEDKTEE 415
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1436945972 403 SFTEDGFYITGDLGYLDENNNITVTGRLKEVINRA-GEKIMPSEIEELLYAH-PDVKDVLVTG 463
Cdd:cd05933   416 AIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAgGENVPPVPIEDAVKKElPIISNAMLIG 478
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
29-275 1.87e-09

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 60.27  E-value: 1.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  29 FERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLG---ALPIFCLD 105
Cdd:PRK08279   43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGavvALLNTQQR 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 106 GHRsyeIGHIAKFSQARVYLrlckhesdsTAEQIIHHFSGDLPHLEIIKTVF---QGELPQCDGDRSkLKEKTHYQPVDS 182
Cdd:PRK08279  123 GAV---LAHSLNLVDAKHLI---------VGEELVEAFEEARADLARPPRLWvagGDTLDDPEGYED-LAAAAAGAPTTN 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 183 RAV---------AFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVSHNFP-MSSPGflGVIYAGA 252
Cdd:PRK08279  190 PASrsgvtakdtAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGgTVAWS--SVLAAGA 267
                         250       260
                  ....*....|....*....|...
gi 1436945972 253 TLVIADNSSPTECFGLIERHKIT 275
Cdd:PRK08279  268 TLALRRKFSASRFWDDVRRYRAT 290
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
41-524 1.88e-09

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: 59.80  E-value: 1.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  41 ALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGA--LPIfclDGHRSYE-IGHIAK 117
Cdd:cd17656     6 AVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGafVPI---DPEYPEErRIYIML 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 118 FSQARVYLRLCKHESDSTAEQIIHHFSGDLphleiiktvfqgeLPQCDGDRSKLKekthyqpVDSRAVAFLQLSGGTTGL 197
Cdd:cd17656    83 DSGVRVVLTQRHLKSKLSFNKSTILLEDPS-------------ISQEDTSNIDYI-------NNSDDLLYIIYTSGTTGK 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 198 PKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLPVShnFPMSSPGFLGVIYAGATLVIADNSSPTEC---FGLIERHKI 274
Cdd:cd17656   143 PKGVQLEHKNMVNLLHFEREKTNINFSDKVLQFATCS--FDVCYQEIFSTLLSGGTLYIIREETKRDVeqlFDLVKRHNI 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 275 tQTSLVPSLVVAWLNS--AMIDKFDLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGMAEG-LVNYTRLDDNREVQ- 350
Cdd:cd17656   221 -EVVFLPVAFLKFIFSerEFINRFPTCVKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSEThVVTTYTINPEAEIPe 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 351 INTQGKRLSDFDeIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGF------YITGDLGYLDENNNI 424
Cdd:cd17656   300 LPPIGKPISNTW-IYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNI 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 425 TVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKpdNFNLVKVRKYLTQQhIALNKL 504
Cdd:cd17656   379 EFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQ--ELNISQLREYLAKQ-LPEYMI 455
                         490       500
                  ....*....|....*....|
gi 1436945972 505 PDVVSVVDEFDFTLIGKVRR 524
Cdd:cd17656   456 PSFFVPLDQLPLTPNGKVDR 475
PRK09274 PRK09274
peptide synthase; Provisional
58-457 1.93e-09

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 59.91  E-value: 1.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  58 ALAWGewLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGALPIF------------CLD-GHRSYEIGhIAKFSQARVY 124
Cdd:PRK09274   53 AIAHG--LNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLvdpgmgiknlkqCLAeAQPDAFIG-IPKAHLARRL 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 125 LRLCKhesdSTAEQIIhhfsgdlphleiikTVFQGELPqcdGDRS-----KLKEKTHYQPVDSR-----AVAFlqlSGGT 194
Cdd:PRK09274  130 FGWGK----PSVRRLV--------------TVGGRLLW---GGTTlatllRDGAAAPFPMADLApddmaAILF---TSGS 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 195 TGLPKLIPRTHDDYLysvresAVVANLQQDTKH------LLVLPVshnFPMSSPGflgviyAGATLVI--ADNSSPTEC- 265
Cdd:PRK09274  186 TGTPKGVVYTHGMFE------AQIEALREDYGIepgeidLPTFPL---FALFGPA------LGMTSVIpdMDPTRPATVd 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 266 ----FGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSSLEVVQVGGAKFSSELAARLLD--TLDLTLQQVYGMAEGL-- 337
Cdd:PRK09274  251 paklFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAmlPPDAEILTPYGATEALpi 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 338 ---VNYTRLDDNRevQINTQGK-----RLSDFDEIQILDL---------EGKVLGVGEVGVITTRGPYTINAYFAPDEVN 400
Cdd:PRK09274  331 ssiESREILFATR--AATDNGAgicvgRPVDGVEVRIIAIsdapipewdDALRLATGEIGEIVVAGPMVTRSYYNRPEAT 408
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1436945972 401 KRSFTEDG----FYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVK 457
Cdd:PRK09274  409 RLAKIPDGqgdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVK 469
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
331-497 4.77e-09

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 58.88  E-value: 4.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 331 YGMAEGLVNYTRLDDNREVQIntqGKrlsDFDEIQILDLE-------------GKVL----GVGEVgvITTRGPYTINAY 393
Cdd:PRK13388  295 YGSSEGAVIVVREPGTPPGSI---GR---GAPGVAIYNPEtltecavarfdahGALLnadeAIGEL--VNTAGAGFFEGY 366
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 394 FAPDEVNKRSFtEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKI 473
Cdd:PRK13388  367 YNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQV 445
                         170       180
                  ....*....|....*....|....
gi 1436945972 474 CVQIITDKPDNFNLVKVRKYLTQQ 497
Cdd:PRK13388  446 MAALVLRDGATFDPDAFAAFLAAQ 469
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
39-524 1.41e-08

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: 57.28  E-value: 1.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  39 NTALVLGEDEVSYE--AFYFKALAWgeWLHEQGVRKDDLV-VL------QSANVLeffyvlfGLYYLGA--LPIfcldgh 107
Cdd:cd12114     3 ATAVICGDGTLTYGelAERARRVAG--ALKAAGVRPGDLVaVTlpkgpeQVVAVL-------GILAAGAayVPV------ 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 108 rsyEIGHIAkfsqarvyLRLCKHESDSTAEQIIHHFSGDLPHLEIIKTVFQGELPQCDGDRSKLkekthyQPVDSRAVAF 187
Cdd:cd12114    68 ---DIDQPA--------ARREAILADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPP------VDVAPDDLAY 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 188 LQLSGGTTGLPKLIPRTHDdylysvresaVVANLQQDTKHLL-------VLPVSH-NFPMSSPGFLGVIYAGATLVI--- 256
Cdd:cd12114   131 VIFTSGSTGTPKGVMISHR----------AALNTILDINRRFavgpddrVLALSSlSFDLSVYDIFGALSAGATLVLpde 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 257 ADNSSPTECFGLIERHKITQTSLVPSLV---VAWLNSAMIDkfdLSSLEVVQVGGAKFSSELAARLLDTLDLTLQQVYGM 333
Cdd:cd12114   201 ARRRDPAHWAELIERHGVTLWNSVPALLemlLDVLEAAQAL---LPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGG 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 334 A-EGLV--NYTRLDD-NREVQINTQGKRLSDfDEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDG- 408
Cdd:cd12114   278 AtEASIwsIYHPIDEvPPDWRSIPYGRPLAN-QRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHPd 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 409 ---FYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDEllGEK-ICVQIITDKPDN 484
Cdd:cd12114   357 gerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP--GGKrLAAFVVPDNDGT 434
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 1436945972 485 FNLVKVRKYLTQQHIALNKLPDVVSVVDEFDFTLIGKVRR 524
Cdd:cd12114   435 PIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDR 474
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
445-521 2.04e-08

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: 51.01  E-value: 2.04e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1436945972 445 EIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITDKPDNFNLVKVRKYLTqQHIALNKLPDVVSVVDEFDFTLIGK 521
Cdd:pfam13193   1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVR-EELGPYAVPKEVVFVDELPKTRSGK 76
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
380-509 4.19e-08

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: 55.68  E-value: 4.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 380 GVITTRGPYTINAYFAPDEVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKE-VINRAGEKIMPSEIEELLYAHPDVKD 458
Cdd:cd17639   331 GEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDlVKLQNGEYIALEKLESIYRSNPLVNN 410
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1436945972 459 VLVTGVPDEllgEKICVQIITdkpdnfNLVKVRKYLTQQHIALNKLPDVVS 509
Cdd:cd17639   411 ICVYADPDK---SYPVAIVVP------NEKHLTKLAEKHGVINSEWEELCE 452
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
181-524 8.07e-07

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: 51.40  E-value: 8.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 181 DSRAVAFLQLSGGTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVlpVSHNFPMSSPGFLGVIYAGATLVIADNS 260
Cdd:cd17645   102 NPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVY--ASFSFDASAWEIFPHLTAGAALHVVPSE 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 261 SPTECFGL---IERHKITqtslvpslvVAWLNSAMIDKF---DLSSLEVVQVGGAKFsselaaRLLDTLDLTLQQVYGMA 334
Cdd:cd17645   180 RRLDLDALndyFNQEGIT---------ISFLPTGAAEQFmqlDNQSLRVLLTGGDKL------KKIERKGYKLVNNYGPT 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 335 EGLVNYTRLDDNREVQINTQGKRLsDFDEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGF----- 409
Cdd:cd17645   245 ENTVVATSFEIDKPYANIPIGKPI-DNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFvpger 323
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 410 -YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKICVQIITdkPDNFNLV 488
Cdd:cd17645   324 mYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTA--PEEIPHE 401
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1436945972 489 KVRKYLTqqhialNKLPDVV-----SVVDEFDFTLIGKVRR 524
Cdd:cd17645   402 ELREWLK------NDLPDYMiptyfVHLKALPLTANGKVDR 436
PRK12467 PRK12467
peptide synthase; Provisional
22-461 8.20e-07

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 52.09  E-value: 8.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972   22 GESLFEFFERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGA--L 99
Cdd:PRK12467  1573 ARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGayV 1652
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  100 PifcLDGHRSYEighiakfsqarvylRLCKHESDSTAEQIIHHfSGDLPHLEIIKTVFQGELPQCDGDRSKLKEKTHYQP 179
Cdd:PRK12467  1653 P---LDPEYPRE--------------RLAYMIEDSGIELLLTQ-SHLQARLPLPDGLRSLVLDQEDDWLEGYSDSNPAVN 1714
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  180 VDSRAVAFLQLSGGTTGLPKLIPRTHDdylysvresAVVANL-------QQDTKHLLVLPVSHNFPMSSPGFLGVIYAGA 252
Cdd:PRK12467  1715 LAPQNLAYVIYTSGSTGRPKGAGNRHG---------ALVNRLcatqeayQLSAADVVLQFTSFAFDVSVWELFWPLINGA 1785
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  253 TLVIADNS---SPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSsLEVVQVGGAKFSSElAARLLDTLDLTLQQ 329
Cdd:PRK12467  1786 RLVIAPPGahrDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLS-LRRVVCGGEALEVE-ALRPWLERLPDTGL 1863
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  330 V--YGMAEGLVNYT----RLDDNREVQINTQGKRLSDFdEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRS 403
Cdd:PRK12467  1864 FnlYGPTETAVDVThwtcRRKDLEGRDSVPIGQPIANL-STYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAER 1942
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1436945972  404 FTEDGF-------YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLV 461
Cdd:PRK12467  1943 FVADPFgtvgsrlYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVV 2007
PRK05691 PRK05691
peptide synthase; Validated
23-471 1.32e-06

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 51.71  E-value: 1.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972   23 ESLFEFFERSCQKFATNTALVLGEDEVSYEAFYFKALAWGEWLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGA--LP 100
Cdd:PRK05691  3720 QSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAgyLP 3799
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  101 ifcLD-GHRSYEIGHIAKFSqaRVYLRLCKHESDSTAEQIIHHFSG-DLPHLEIIKTVFQGELPQCDGDRsklkekthYQ 178
Cdd:PRK05691  3800 ---LDpGLPAQRLQRIIELS--RTPVLVCSAACREQARALLDELGCaNRPRLLVWEEVQAGEVASHNPGI--------YS 3866
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  179 PVDSraVAFLQLSGGTTGLPKLIPRTHDDYLYSvrESAVVANLQQDTKHLLVLPVSHNFPMSSPGFLGVIYAGATLVIAD 258
Cdd:PRK05691  3867 GPDN--LAYVIYTSGSTGLPKGVMVEQRGMLNN--QLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVP 3942
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  259 NS---SPTECFGLIERHKITQTSLVPSLVVAWLNSamiDKFDLSSLEVVQVGGAKFSSELAAR-LLDTLDLTLQQVYGMA 334
Cdd:PRK05691  3943 NAiahDPQGLLAHVQAQGITVLESVPSLIQGMLAE---DRQALDGLRWMLPTGEAMPPELARQwLQRYPQIGLVNAYGPA 4019
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  335 E--GLVNYTRLDDNrevqiNTQGKRL-----SDFDEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTED 407
Cdd:PRK05691  4020 EcsDDVAFFRVDLA-----STRGSYLpigspTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPH 4094
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1436945972  408 GF-------YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVtGVPDELLGE 471
Cdd:PRK05691  4095 PFgapgerlYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAV-AVQEGVNGK 4164
PLN02654 PLN02654
acetate-CoA ligase
408-473 1.42e-06

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 51.05  E-value: 1.42e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1436945972 408 GFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGVPDELLGEKI 473
Cdd:PLN02654  513 GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGI 578
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
372-522 3.02e-06

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 50.35  E-value: 3.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  372 KVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLY 451
Cdd:PRK06814   974 PVPGIDEGGRLFVRGPNVMLGYLRAENPGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAA 1053
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1436945972  452 A-HPDVKDVLVTgVPDELLGEKICvqIITDKPD----NFnlvkvRKYLTQQHIALNKLPDVVSVVDEFDFTLIGKV 522
Cdd:PRK06814  1054 ElWPDALHAAVS-IPDARKGERII--LLTTASDatraAF-----LAHAKAAGASELMVPAEIITIDEIPLLGTGKI 1121
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
380-482 2.34e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 47.28  E-value: 2.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 380 GVITTRGPYTINAYFAPDEVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKE-VINRAGEKImPSEIEELLYAH----- 453
Cdd:PTZ00216  508 GEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKAlAKNCLGEYI-ALEALEALYGQnelvv 586
                          90       100
                  ....*....|....*....|....*....
gi 1436945972 454 PDVKDVLVTgvPDEllgEKICVQIITDKP 482
Cdd:PTZ00216  587 PNGVCVLVH--PAR---SYICALVLTDEA 610
PRK05691 PRK05691
peptide synthase; Validated
371-450 2.37e-05

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 47.47  E-value: 2.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  371 GKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTE-DG--FYITGDLGYLDENNnITVTGRLKEVINRAGEKIMPSEIE 447
Cdd:PRK05691   389 LEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEhDGrtWLRTGDLGFLRDGE-LFVTGRLKDMLIVRGHNLYPQDIE 467

                   ...
gi 1436945972  448 ELL 450
Cdd:PRK05691   468 KTV 470
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
369-463 3.45e-05

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 46.68  E-value: 3.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 369 LEGKVLGVGEVGVITTRGPY-----------TINAYFAPDEVNKRSFTEDGFYITGD---------LGYLDENNNitvtg 428
Cdd:cd17632   414 LDYKLVDVPELGYFRTDRPHprgellvktdtLFPGYYKRPEVTAEVFDEDGFYRTGDvmaelgpdrLVYVDRRNN----- 488
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1436945972 429 rlkeVINRA-GEKIMPSEIEELLYAHPDVKDVLVTG 463
Cdd:cd17632   489 ----VLKLSqGEFVTVARLEAVFAASPLVRQIFVYG 520
PLN03051 PLN03051
acyl-activating enzyme; Provisional
176-303 3.72e-05

acyl-activating enzyme; Provisional


Pssm-ID: 215552 [Multi-domain]  Cd Length: 499  Bit Score: 46.35  E-value: 3.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 176 HYQPV--DSRAVAFLQLSGGTTGLPKLIPRTHddyLYSVReSAVVANLQQDTKHLLVL--PVSHNFPMSSPGFLGVIYAG 251
Cdd:PLN03051  110 EYSPVyaPVESVTNILFSSGTTGEPKAIPWTH---LSPLR-CASDGWAHMDIQPGDVVcwPTNLGWMMGPWLLYSAFLNG 185
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1436945972 252 ATLVIADNSSPTECFG-LIERHKITQTSLVPSLVVAW--LNSAMIDKFDLSSLEV 303
Cdd:PLN03051  186 ATLALYGGAPLGRGFGkFVQDAGVTVLGLVPSIVKAWrhTGAFAMEGLDWSKLRV 240
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
377-467 4.97e-05

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: 46.05  E-value: 4.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 377 GEVGVittRGPYTINAYFAPDEVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRA-GEKIMPSEIEELLYAHPD 455
Cdd:cd05927   356 GEVCI---RGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSqGEYVAPEKIENIYARSPF 432
                          90       100
                  ....*....|....*....|...
gi 1436945972 456 VKDVLVTG-----------VPDE 467
Cdd:cd05927   433 VAQIFVYGdslksflvaivVPDP 455
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
373-481 1.18e-04

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 44.70  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 373 VLGVGEVGVITTRGPYTINAYF---------APDEVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRAGEKIMP 443
Cdd:PRK08043  547 VPGIEQGGRLQLKGPNIMNGYLrvekpgvleVPTAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSL 626
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1436945972 444 SEIEEL-LYAHPDvKDVLVTGVPDELLGEKIcVQIITDK 481
Cdd:PRK08043  627 EMVEQLaLGVSPD-KQHATAIKSDASKGEAL-VLFTTDS 663
PRK05691 PRK05691
peptide synthase; Validated
186-461 1.39e-04

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 44.77  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  186 AFLQLSGGTTGLPKLIPRTHddylysvreSAVVANLQ--QDTKHLL---VL----PVShnFPMSS-PGFLGVIyAGATLV 255
Cdd:PRK05691  1276 AYVIYTSGSTGQPKGVGNTH---------AALAERLQwmQATYALDdsdVLmqkaPIS--FDVSVwECFWPLI-TGCRLV 1343
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  256 IA---DNSSPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDkfDLSSLEVVQVGGAKFSSELAARLLDTL-DLTLQQVY 331
Cdd:PRK05691  1344 LAgpgEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAA--ACTSLRRLFSGGEALPAELRNRVLQRLpQVQLHNRY 1421
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  332 GMAEGLVNYT----RLDDNREVQIntqGKRLSDFdEIQILDLEGKVL--GV-GEV---GVITTRG----PYTINAYFAPD 397
Cdd:PRK05691  1422 GPTETAINVThwqcQAEDGERSPI---GRPLGNV-LCRVLDAELNLLppGVaGELcigGAGLARGylgrPALTAERFVPD 1497
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1436945972  398 evnkrSFTEDG--FYITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLV 461
Cdd:PRK05691  1498 -----PLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAV 1558
PRK12316 PRK12316
peptide synthase; Provisional
185-461 1.48e-04

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 44.95  E-value: 1.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  185 VAFLQLSGGTTGLPKLIPRTHddylysvreSAVVANLQQDTKHLLVLP-------VSHNFPMSSPGFLGVIYAGATLVIA 257
Cdd:PRK12316  2148 LAYVIYTSGSTGLPKGVAVSH---------GALVAHCQAAGERYELSPadcelqfMSFSFDGAHEQWFHPLLNGARVLIR 2218
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  258 DNS--SPTECFGLIERHKITQTSLVPSLVVAWLNSAMIDKFDLSsLEVVQVGGAKFSSELAARLLDTLDLTLQQ-VYGMA 334
Cdd:PRK12316  2219 DDElwDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPA-VRVYCFGGEAVPAASLRLAWEALRPVYLFnGYGPT 2297
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  335 EGLVNYTRLDDNREVQINTQ----GKRLSDfDEIQILDLEGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDGF- 409
Cdd:PRK12316  2298 EAVVTPLLWKCRPQDPCGAAyvpiGRALGN-RRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFs 2376
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1436945972  410 ------YITGDLGYLDENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLV 461
Cdd:PRK12316  2377 asgerlYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVV 2434
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
180-456 2.30e-04

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 43.60  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 180 VDSRAVAFLQLSGGTTGLPKLIPRTHDD----------YLYS--VRESAVVANLqqdtkhllvlpvshnFPMS-SPGFLG 246
Cdd:COG1541    80 VPLEEIVRIHASSGTTGKPTVVGYTRKDldrwaelfarSLRAagVRPGDRVQNA---------------FGYGlFTGGLG 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 247 VIYA----GATLVIADNSSPTECFGLIERHKitQTSLV--PS--LVVA-WLNSAMIDKFDLsSLEVVQVGGAKFSSELAA 317
Cdd:COG1541   145 LHYGaerlGATVIPAGGGNTERQLRLMQDFG--PTVLVgtPSylLYLAeVAEEEGIDPRDL-SLKKGIFGGEPWSEEMRK 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 318 RLLDTLDLTLQQVYGMAE-------------GLVnytrlddnrevqintqgkrlsdFDE----IQILDLE-GKVLGVGEV 379
Cdd:COG1541   222 EIEERWGIKAYDIYGLTEvgpgvayeceaqdGLH----------------------IWEdhflVEIIDPEtGEPVPEGEE 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 380 G--VITTrgpytinayfapdevnkrsFTEDGF----YITGDLGYLDENNNIT---------VTGRLKEVINRAGEKIMPS 444
Cdd:COG1541   280 GelVVTT-------------------LTKEAMplirYRTGDLTRLLPEPCPCgrthprigrILGRADDMLIIRGVNVFPS 340
                         330
                  ....*....|..
gi 1436945972 445 EIEELLYAHPDV 456
Cdd:COG1541   341 QIEEVLLRIPEV 352
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
393-441 4.94e-04

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 42.78  E-value: 4.94e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1436945972 393 YFAPDEVNKRSFTEDGFYITGDLGYLDENNNITVTGRLKEVINRA-GEKI 441
Cdd:PTZ00342  555 YFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSqGEYI 604
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
58-464 6.58e-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: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 42.06  E-value: 6.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972  58 ALAWGewLHEQGVRKDDLVVLQSANVLEFFYVLFGLYYLGALPIFCLDGhrsyeighiakfsQARVYLRLCKHESDSTAe 137
Cdd:cd05910    14 RIAQG--LTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPG-------------MGRKNLKQCLQEAEPDA- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 138 qiihhfsgdlphleiiktvFQGElPQCDgdrsklkekthyqpvDSRAVAFlqlSGGTTGLPKLIPRTHDDY---LYSVRE 214
Cdd:cd05910    78 -------------------FIGI-PKAD---------------EPAAILF---TSGSTGTPKGVVYRHGTFaaqIDALRQ 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 215 SAVVANLQQDtkhllvLPVshnFPMSspGFLGVIYaGATLVIAD-------NSSPTECFGLIERHKITQTSLVPSL---V 284
Cdd:cd05910   120 LYGIRPGEVD------LAT---FPLF--ALFGPAL-GLTSVIPDmdptrpaRADPQKLVGAIRQYGVSIVFGSPALlerV 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 285 VAWlnSAMIDKfDLSSLEVVQVGGAKFSSELAA--RLLDTLDLTLQQVYGMAEGLvNYTRLDDnREVQINTQ-------- 354
Cdd:cd05910   188 ARY--CAQHGI-TLPSLRRVLSAGAPVPIALAArlRKMLSDEAEILTPYGATEAL-PVSSIGS-RELLATTTaatsggag 262
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 355 ---GKRLsDFDEIQILDL---------EGKVLGVGEVGVITTRGPYTINAYFAPDEVNKRSFTEDG----FYITGDLGYL 418
Cdd:cd05910   263 tcvGRPI-PGVRVRIIEIddepiaewdDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYL 341
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1436945972 419 DENNNITVTGRLKEVINRAGEKIMPSEIEELLYAHPDVKDVLVTGV 464
Cdd:cd05910   342 DDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV 387
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
193-462 4.35e-03

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: 39.45  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 193 GTTGLPKLIPRTHDDYLYSVRESAVVANLQQDTKHLLVLpvSHNFPMSSPGFLGVIYAGATLVIAdnsSPTECF----GL 268
Cdd:cd05918   116 GSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQFA--SYTFDVSILEIFTTLAAGGCLCIP---SEEDRLndlaGF 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 269 IERHKITQTSLVPSLvvawlnSAMIDKFDLSSLEVVQVGGAKFSSELAARllDTLDLTLQQVYGMAEGLVNYTRLDDNRE 348
Cdd:cd05918   191 INRLRVTWAFLTPSV------ARLLDPEDVPSLRTLVLGGEALTQSDVDT--WADRVRLINAYGPAECTIAATVSPVVPS 262
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945972 349 VQINTQGKRLS------DFDEIQILDLEGkvlGVGEV---GVITTRGpytinaYFAPDEVNKRSFTEDG----------- 408
Cdd:cd05918   263 TDPRNIGRPLGatcwvvDPDNHDRLVPIG---AVGELlieGPILARG------YLNDPEKTAAAFIEDPawlkqegsgrg 333
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1436945972 409 --FYITGDLGYLDENNNITVTGRL----KevINraGEKIMPSEIEELLYAH-PDVKDVLVT 462
Cdd:cd05918   334 rrLYRTGDLVRYNPDGSLEYVGRKdtqvK--IR--GQRVELGEIEHHLRQSlPGAKEVVVE 390
 
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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