|
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
|
|
|