|
Name |
Accession |
Description |
Interval |
E-value |
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
94-682 |
0e+00 |
|
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: 761.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 94 SGYHYNTFTEVIEVMHSVGRGLVKLGMEPksEDKLHIFAATSHKWMKMFLGAQSQGIPIVTAYDTLGEKGLIHSLKQTSS 173
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKP--GDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETEC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 174 AAIFTDnqllgklinplkvaekiryviyydnisaedkrqggklyreaqeavdkikevrpdiklvsfdellelgqkakgei 253
Cdd:cd17639 79 SAIFTD-------------------------------------------------------------------------- 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 254 ephpPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVCDYVGDTDKLICFLPLAHIFEMAFELLSFHWGSCIG 333
Cdd:cd17639 85 ----GKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIG 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 334 YANVKTLTSASVRNCKSDLEEFQPTIMVGVAAVWETVKKGILNQINELPRVTKGIFWAAYHSKLKMQKMGiPGGDTIGNI 413
Cdd:cd17639 161 YGSPRTLTDKSKRGCKGDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALKEG-PGTPLLDEL 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 414 IFKKVRKATGGHLRYLLNGGSPISVNAQEFISNLICPMLIGYGLTETCASLCILNPGHFEYGVVGDLTGCVTVKLVDVEE 493
Cdd:cd17639 240 VFKKVRAALGGRLRYMLSGGAPLSADTQEFLNIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEE 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 494 LGY--FAKDNKGEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKTMNGEYIALEKLE 571
Cdd:cd17639 320 GGYstDKPPPRGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLE 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 572 SVYRSNSYVQNICVYADQNKVKPVGIIVPNHTPLVKLAKELGImkkQETDIEPYLHNKKLQNAVFEDMIKTAKKQGLVGI 651
Cdd:cd17639 400 SIYRSNPLVNNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGV---INSEWEELCEDKKLQKAVLKSLAETARAAGLEKF 476
|
570 580 590
....*....|....*....|....*....|.
gi 2112360039 652 ELLQGAVFFDDEWTPQNGFVTSAQKLQRKKI 682
Cdd:cd17639 477 EIPQGVVLLDEEWTPENGLVTAAQKLKRKEI 507
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
96-695 |
1.34e-158 |
|
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: 468.62 E-value: 1.34e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 96 YHYNTFTEVIEVMHSVGRGLVKLGMEPKSEDKLHIFAATSHKWMKMFLGAQSQGIPIVTAYDTLGEKGLIHSLKQTSSAA 175
Cdd:cd05927 3 YEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 176 IFTDnqllgklinplkvaekiryviyydnisaedkrqggklyreaqeavdkikevrPDIKLVSFDELLELGQKAKgeIEP 255
Cdd:cd05927 83 VFCD----------------------------------------------------AGVKVYSLEEFEKLGKKNK--VPP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 256 HPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGA--TINVCDYVGDTDKLICFLPLAHIFEMAFELLSFHWGSCIG 333
Cdd:cd05927 109 PPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVfkILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 334 Y--ANVKTLTSasvrncksDLEEFQPTIMVGVAAVWETVKKGILNQINELPRVTKGIFWAAYHSKLKMQKMGIPGGDTI- 410
Cdd:cd05927 189 FysGDIRLLLD--------DIKALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALNYKLAELRSGVVRASPFw 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 411 GNIIFKKVRKATGGHLRYLLNGGSPISVNAQEFI-SNLICPMLIGYGLTETCASLCILNPGHFEYGVVGDLTGCVTVKLV 489
Cdd:cd05927 261 DKLVFNKIKQALGGNVRLMLTGSAPLSPEVLEFLrVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLV 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 490 DVEELGYFAKDN--KGEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKTMNGEYIAL 567
Cdd:cd05927 341 DVPEMNYDAKDPnpRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAP 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 568 EKLESVYRSNSYVQNICVYADQNKVKPVGIIVPNHTPLVKLAKELGIMKKqetDIEPYLHNKKLQNAVFEDMIKTAKKQG 647
Cdd:cd05927 421 EKIENIYARSPFVAQIFVYGDSLKSFLVAIVVPDPDVLKEWAASKGGGTG---SFEELCKNPEVKKAILEDLVRLGKENG 497
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 2112360039 648 LVGIELLQGAVFFDDEWTPQNGFVTSAQKLQRKKILKAVEKDVESVYA 695
Cdd:cd05927 498 LKGFEQVKAIHLEPEPFSVENGLLTPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
2-695 |
1.10e-131 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 404.50 E-value: 1.10e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 2 AVTVTVGeARPGETapRRAAKVAEkaLDRPPNMKCSTVYEFILECCEKHGGKNAIGWRDIIDVHEETktiekfnkkSGQM 81
Cdd:PLN02387 28 GVPVDVG-GEPGYA--IRNARFPE--LVETPWEGATTLAALFEQSCKKYSDKRLLGTRKLISREFET---------SSDG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 82 EKVDKnwlyYELSGYHYNTFTEVIEVMHSVGRGLVKLGMepKSEDKLHIFAATSHKWMKMFLGAQSQGIPIVTAYDTLGE 161
Cdd:PLN02387 94 RKFEK----LHLGEYEWITYGQVFERVCNFASGLVALGH--NKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 162 KGLIHSLKQTSSAAIFTDNQLLGKLINPLKVAEKIRYVIYYDNISAEDkrqggklyreaqeavDKIKEVRPDIKLVSFDE 241
Cdd:PLN02387 168 EALCHSLNETEVTTVICDSKQLKKLIDISSQLETVKRVIYMDDEGVDS---------------DSSLSGSSNWTVSSFSE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 242 LLELGQKAKgeIEPHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVCDyVGDTDKLICFLPLAHIFEMAF 321
Cdd:PLN02387 233 VEKLGKENP--VDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPK-LGKNDVYLAYLPLAHILELAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 322 ELLSFHWGSCIGYANVKTLTSAS---VRNCKSDLEEFQPTIMVGVAAVWETVKKGILNQINELPRVTKGIFWAAYHSKLk 398
Cdd:PLN02387 310 ESVMAAVGAAIGYGSPLTLTDTSnkiKKGTKGDASALKPTLMTAVPAILDRVRDGVRKKVDAKGGLAKKLFDIAYKRRL- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 399 mqkMGIPGG--DTIG-------NIIFKKVRKATGGHLRYLLNGGSPISVNAQEFISnlIC---PMLIGYGLTETCASLCI 466
Cdd:PLN02387 389 ---AAIEGSwfGAWGlekllwdALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFIN--IClgaPIGQGYGLTETCAGATF 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 467 LNPGHFEYGVVGDLTGCVTVKLVDVEELGYFAKDN---KGEIWVKGENVLPEYYKNEEETKE--SLTEDG--WFKTGDIG 539
Cdd:PLN02387 464 SEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLISDKpmpRGEIVIGGPSVTLGYFKNQEKTDEvyKVDERGmrWFYTGDIG 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 540 MWTDTGSLKIIDRKKNLVKTMNGEYIALEKLESVYRSNSYVQNICVYADQNKVKPVGIIVPNHTPLVKLAKELGImkkQE 619
Cdd:PLN02387 544 QFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGI---DY 620
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2112360039 620 TDIEPYLHNKKLQNAVFEDMIKTAKKQGLVGIELLQGAVFFDDEWTPQNGFVTSAQKLQRKKILKAVEKDVESVYA 695
Cdd:PLN02387 621 SNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
38-696 |
1.10e-131 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 404.74 E-value: 1.10e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 38 TVYEFILECCEKHGGKNAIGWRDIIDVHEETKTIEKFNKKSgqmekvdknWLYYELSGYHYNTFTEVIEVMHSVGRGLVK 117
Cdd:PTZ00216 70 NFLQRLERICKERGDRRALAYRPVERVEKEVVKDADGKERT---------MEVTHFNETRYITYAELWERIVNFGRGLAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 118 LGMEPKSedKLHIFAATSHKWMKMFLGAQSQGIPIVTAYDTLGEKGLIHSLKQTSSAAIFTDNQLLGKLINPLKVAE-KI 196
Cdd:PTZ00216 141 LGLTKGS--NVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGKNVPNLLRLMKSGGmPN 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 197 RYVIYYDNISAedkrqggklyreaqeAVDKiKEVRpdikLVSFDELLELGQKAKGEIEPHPPT-RDDISCIMYTSGSTGD 275
Cdd:PTZ00216 219 TTIIYLDSLPA---------------SVDT-EGCR----LVAWTDVVAKGHSAGSHHPLNIPEnNDDLALIMYTSGTTGD 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 276 PKGVVLKHSNVVAGVGGATINVCDYVGDT--DKLIC-FLPLAHIFEMAFELLSFHWGSCIGYANVKTLTSASVRNCkSDL 352
Cdd:PTZ00216 279 PKGVMHTHGSLTAGILALEDRLNDLIGPPeeDETYCsYLPLAHIMEFGVTNIFLARGALIGFGSPRTLTDTFARPH-GDL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 353 EEFQPTIMVGVAAVWETVKKGILNQineLPRV---TKGIFWAAYHSKLKMQKmgiPGGDT--IGNIIFKKVRKATGGHLR 427
Cdd:PTZ00216 358 TEFRPVFLIGVPRIFDTIKKAVEAK---LPPVgslKRRVFDHAYQSRLRALK---EGKDTpyWNEKVFSAPRAVLGGRVR 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 428 YLLNGGSPISVNAQEFISNLICPMLIGYGLTETCASLCILNPGHFEYGVVGDLTGCVTVKLVDVEElgYFAKDN---KGE 504
Cdd:PTZ00216 432 AMLSGGGPLSAATQEFVNVVFGMVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEE--YKHTDTpepRGE 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 505 IWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKTMNGEYIALEKLESVYRSNSYVQN-- 582
Cdd:PTZ00216 510 ILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALYGQNELVVPng 589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 583 ICVYADQNKVKPVGIIVPNHTPLVKLAKELGImkkqETDIEPYLHNKKLQNAVFEDMIKTAKKQGLVGIELLQGAVFFDD 662
Cdd:PTZ00216 590 VCVLVHPARSYICALVLTDEAKAMAFAKEHGI----EGEYPAILKDPEFQKKATESLQETARAAGRKSFEIVRHVRVLSD 665
|
650 660 670
....*....|....*....|....*....|....
gi 2112360039 663 EWTPQNGFVTSAQKLQRKKILKAVEKDVESVYAD 696
Cdd:PTZ00216 666 EWTPENGVLTAAMKLKRRVIDERYADLIKELFAD 699
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
70-696 |
2.59e-125 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 385.22 E-value: 2.59e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 70 TIEKFNKKSGQMEKVDKNWLYYelsgyhynTFTEVIEVMHSVGRGLVKLGMEPksEDKLHIFAATSHKWMKMFLGAQS-Q 148
Cdd:COG1022 20 RAARFPDRVALREKEDGIWQSL--------TWAEFAERVRALAAGLLALGVKP--GDRVAILSDNRPEWVIADLAILAaG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 149 GIPiVTAYDTLGEKGLIHSLKQTSSAAIFTDNQ-LLGKLINPLKVAEKIRYVIYYDNisaedkrqggklyreaqeavdki 227
Cdd:COG1022 90 AVT-VPIYPTSSAEEVAYILNDSGAKVLFVEDQeQLDKLLEVRDELPSLRHIVVLDP----------------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 228 KEVRPDIKLVSFDELLELGQKAK--GEIE--PHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVggATINVCDYVGD 303
Cdd:COG1022 146 RGLRDDPRLLSLDELLALGREVAdpAELEarRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNA--RALLERLPLGP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 304 TDKLICFLPLAHIFEMAFELLSFHWGSCIGYANvktltsaSVRNCKSDLEEFQPTIMVGVAAVWETVKKGILNQINELPR 383
Cdd:COG1022 224 GDRTLSFLPLAHVFERTVSYYALAAGATVAFAE-------SPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 384 VTKGIF-WA---AY-HSKLKMQKMGIPGGDTIGN-----IIFKKVRKATGGHLRYLLNGGSPISVNAQEFISNLICPMLI 453
Cdd:COG1022 297 LKRKLFrWAlavGRrYARARLAGKSPSLLLRLKHaladkLVFSKLREALGGRLRFAVSGGAALGPELARFFRALGIPVLE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 454 GYGLTETCASLCILNPGHFEYGVVGDLTGCVTVKLvdveelgyfakDNKGEIWVKGENVLPEYYKNEEETKESLTEDGWF 533
Cdd:COG1022 377 GYGLTETSPVITVNRPGDNRIGTVGPPLPGVEVKI-----------AEDGEILVRGPNVMKGYYKNPEATAEAFDADGWL 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 534 KTGDIGMWTDTGSLKIIDRKKNLVKTMNGEYIALEKLESVYRSNSYVQNICVYADQNKVkPVGIIVPNHTPLVKLAKELG 613
Cdd:COG1022 446 HTGDIGELDEDGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDGRPF-LAALIVPDFEALGEWAEENG 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 614 ImkkQETDIEPYLHNKKLQNAVFEDmIKTAKKqGLVGIELLQGAVFFDDEWTPQNGFVTSAQKLQRKKILKAVEKDVESV 693
Cdd:COG1022 525 L---PYTSYAELAQDPEVRALIQEE-VDRANA-GLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEAL 599
|
...
gi 2112360039 694 YAD 696
Cdd:COG1022 600 YAG 602
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
4-695 |
8.16e-105 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 333.71 E-value: 8.16e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 4 TVTVGEARPGETAPRRAAKVAEKALDR----PPNMKCSTVYEFILECCEKHGGKNAIGWRDIIDvheetktiekfnkksg 79
Cdd:PLN02430 5 AAQVEEGVKGKDGKPSVGPVYRNLLSKkgfpPIDSDITTAWDIFSKSVEKYPDNKMLGWRRIVD---------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 80 qmEKVDKnwlyyelsgYHYNTFTEVIEVMHSVGRGLVKLGMEPKSedKLHIFAATSHKWMKMFLGAQSQGIPIVTAYDTL 159
Cdd:PLN02430 69 --GKVGP---------YMWKTYKEVYEEVLQIGSALRASGAEPGS--RVGIYGSNCPQWIVAMEACAAHSLICVPLYDTL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 160 GEKGLIHSLKQTSSAAIFTDNQLLGKLINP-LKVAEKIRYVIYYDNISAEDKrqggklyreaqeavDKIKEVrpDIKLVS 238
Cdd:PLN02430 136 GPGAVDYIVDHAEIDFVFVQDKKIKELLEPdCKSAKRLKAIVSFTSVTEEES--------------DKASQI--GVKTYS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 239 FDELLELGQKAKGEiePHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGatINVC-----DYVGDTDKLICFLPL 313
Cdd:PLN02430 200 WIDFLHMGKENPSE--TNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRG--VDLFmeqfeDKMTHDDVYLSFLPL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 314 AHIFEMAFELLSFHWGSCIGY--ANVKTLtsasvrncKSDLEEFQPTIMVGVAAVWETVKKGILNQINELPRVTKGIFWA 391
Cdd:PLN02430 276 AHILDRMIEEYFFRKGASVGYyhGDLNAL--------RDDLMELKPTLLAGVPRVFERIHEGIQKALQELNPRRRLIFNA 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 392 AYHSKLKMQKMGI------PGGDTIGniiFKKVRKATGGHLRYLLNGGSPISVNAQEFISNLICPMLI-GYGLTETCASL 464
Cdd:PLN02430 348 LYKYKLAWMNRGYshkkasPMADFLA---FRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVqGYGLTETLGPT 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 465 CILNPGHFEY-GVVGDLTGCVTVKLVDVEELGY--FAKDNKGEIWVKGENVLPEYYKNEEETKESLtEDGWFKTGDIGMW 541
Cdd:PLN02430 425 TLGFPDEMCMlGTVGAPAVYNELRLEEVPEMGYdpLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEI 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 542 TDTGSLKIIDRKKNLVKTMNGEYIALEKLESVYRSNSYVQNICVYADQNKVKPVGIIVPNHTPLVKLAKELGIMKKqetd 621
Cdd:PLN02430 504 LPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGS---- 579
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2112360039 622 IEPYLHNKKLQNAVFEDMIKTAKKQGLVGIELLQGAVFFDDEWTPQNGFVTSAQKLQRKKILKAVEKDVESVYA 695
Cdd:PLN02430 580 FEELCSLPELKEHILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMYR 653
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
96-695 |
9.36e-101 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 322.82 E-value: 9.36e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 96 YHYNTFTEVIEVMHSVGRGLVKLGMEPksEDKLHIFAATSHKWMKMFLGAQSQGIPIVTAYDTLGEKGLIHSLKQTSSAA 175
Cdd:PLN02736 76 YKWMTYGEAGTARTAIGSGLVQHGIPK--GACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 176 IFTDNQLLGKLINPLKVAEKIRYVIYYdnisaedkrqGGklyreAQEAVDKIKeVRPDIKLVSFDELLELGQKAkgEIEP 255
Cdd:PLN02736 154 IFCVPQTLNTLLSCLSEIPSVRLIVVV----------GG-----ADEPLPSLP-SGTGVEIVTYSKLLAQGRSS--PQPF 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 256 HPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVCDYVGDTdkLICFLPLAHIFEMAFELLSFHWGSCIGY- 334
Cdd:PLN02736 216 RPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDV--HISYLPLAHIYERVNQIVMLHYGVAVGFy 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 335 --ANVKTLtsasvrnckSDLEEFQPTIMVGVAAVWETVKKGILNQINELPRVTKGIFWAAYHSKLKMQKMGIPGGDTIGN 412
Cdd:PLN02736 294 qgDNLKLM---------DDLAALRPTIFCSVPRLYNRIYDGITNAVKESGGLKERLFNAAYNAKKQALENGKNPSPMWDR 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 413 IIFKKVRKATGGHLRYLLNGGSPISVNAQEFISnlIC---PMLIGYGLTETCASLCILNPGHFEYGVVGDLTGCVTVKLV 489
Cdd:PLN02736 365 LVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLR--ICfggRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLV 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 490 DVEELGYFAKDN---KGEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKTMNGEYIA 566
Cdd:PLN02736 443 DVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIA 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 567 LEKLESVYRSNSYVQNICVYADQNKVKPVGIIVPNHTPLVKLAKELGImkkQETDIEPYLHNKKLQNAVFEDMIKTAKKQ 646
Cdd:PLN02736 523 PEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGI---KYEDLKQLCNDPRVRAAVLADMDAVGREA 599
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 2112360039 647 GLVGIELLQGAVFFDDEWTPQNGFVTSAQKLQRKKILKAVEKDVESVYA 695
Cdd:PLN02736 600 QLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYA 648
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
95-682 |
4.13e-92 |
|
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: 293.73 E-value: 4.13e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 95 GYHYNTFTEVIEVMHSVGRGLVKLGMEPksEDKLHIFAATSHKWMKMFLGAQSQGIPIVTAYDTLGekglihslkqtssa 174
Cdd:cd05907 2 VWQPITWAEFAEEVRALAKGLIALGVEP--GDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSS-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 175 aiftdnqllgklinplkvAEKIRYVIyydnisaedkrqggklyREAQeavdkikevrpdiklvsfdellelgqkAKGEIE 254
Cdd:cd05907 66 ------------------AEQIAYIL-----------------NDSE---------------------------AKALFV 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 255 PHPptrDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVcdYVGDTDKLICFLPLAHIFE-MAFELLSFHWGSCIG 333
Cdd:cd05907 84 EDP---DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERL--PATEGDRHLSFLPLAHVFErRAGLYVPLLAGARIY 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 334 YAnvktltsASVRNCKSDLEEFQPTIMVGVAAVWETVKKGIlnQINELPRVTKGIFwaayhsklkmqkmgipggdtigni 413
Cdd:cd05907 159 FA-------SSAETLLDDLSEVRPTVFLAVPRVWEKVYAAI--KVKAVPGLKRKLF------------------------ 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 414 ifkkvRKATGGHLRYLLNGGSPISVNAQEFISNLICPMLIGYGLTETCASLCILNPGHFEYGVVGDLTGCVTVKLVDvee 493
Cdd:cd05907 206 -----DLAVGGRLRFAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD--- 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 494 lgyfakdnKGEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKTMNGEYIALEKLESV 573
Cdd:cd05907 278 --------DGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENA 349
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 574 YRSNSYVQNICVYADQnKVKPVGIIVPNHTPLVKLAKELGImkkQETDIEPYLHNKKLQnAVFEDMIKTAKKQgLVGIEL 653
Cdd:cd05907 350 LKASPLISQAVVIGDG-RPFLVALIVPDPEALEAWAEEHGI---AYTDVAELAANPAVR-AEIEAAVEAANAR-LSRYEQ 423
|
570 580
....*....|....*....|....*....
gi 2112360039 654 LQGAVFFDDEWTPQNGFVTSAQKLQRKKI 682
Cdd:cd05907 424 IKKFLLLPEPFTIENGELTPTLKLKRPVI 452
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
1-696 |
7.96e-84 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 278.26 E-value: 7.96e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 1 MAVTVTVGEARPGETAPRRAAKV-----AEKAL-DRPPNMKcsTVYEFILECCEKHGGKNAIGWRDIIDvheetktiekf 74
Cdd:PLN02861 3 ETYTVKVEESRPATGGKPSAGPVyrsiyAKDGLlDLPADID--SPWQFFSDAVKKYPNNQMLGRRQVTD----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 75 nKKSGqmekvDKNWLYYElsgyhyntftEVIEVMHSVGRGLVKLGMEPKseDKLHIFAATSHKWMKMFLGAQSQGIPIVT 154
Cdd:PLN02861 70 -SKVG-----PYVWLTYK----------EVYDAAIRIGSAIRSRGVNPG--DRCGIYGSNCPEWIIAMEACNSQGITYVP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 155 AYDTLGEKGLIHSLKQTSSAAIFTDNQLLGKLINPL-KVAEKIRYVIYYDNISAEDKRQGGKLyreaqeavdkikevrpD 233
Cdd:PLN02861 132 LYDTLGANAVEFIINHAEVSIAFVQESKISSILSCLpKCSSNLKTIVSFGDVSSEQKEEAEEL----------------G 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 234 IKLVSFDELLELGqkaKGEIEPHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGAT--INVCDYVGDT-DKLICF 310
Cdd:PLN02861 196 VSCFSWEEFSLMG---SLDCELPPKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDhlLKVTDRVATEeDSYFSY 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 311 LPLAHIFEMAFELLSFHWGSCIGYANvktltsASVRNCKSDLEEFQPTIMVGVAAVWETVKKGILNQINELPRVTKGIFW 390
Cdd:PLN02861 273 LPLAHVYDQVIETYCISKGASIGFWQ------GDIRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFD 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 391 AAYHSKLKMQKMGIPGGDT---IGNIIFKKVRKATGGHLRYLLNGGSPISVNAQEFISNLICPMLI-GYGLTETCASLCI 466
Cdd:PLN02861 347 FAYNYKLGNLRKGLKQEEAsprLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSqGYGLTESCGGCFT 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 467 LNPGHFEY-GVVGDLTGCVTVKLVDVEELGYFAKDN--KGEIWVKGENVLPEYYKNEEETKESLTeDGWFKTGDIGMWTD 543
Cdd:PLN02861 427 SIANVFSMvGTVGVPMTTIEARLESVPEMGYDALSDvpRGEICLRGNTLFSGYHKRQDLTEEVLI-DGWFHTGDIGEWQP 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 544 TGSLKIIDRKKNLVKTMNGEYIALEKLESVYRSNSYVQNICVYADQNKVKPVGIIVPNHTPLVKLAKElgimKKQETDIE 623
Cdd:PLN02861 506 NGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAAN----NNKTGDFK 581
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2112360039 624 PYLHNKKLQNAVFEDMIKTAKKQGLVGIELLQGAVFFDDEWTPQNGFVTSAQKLQRKKILKAVEKDVESVYAD 696
Cdd:PLN02861 582 SLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYSE 654
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
70-694 |
6.17e-82 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 273.43 E-value: 6.17e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 70 TIEKF--NKKSGQMEKVDKnwlyyELSGYHYNTFTEVIEVMHSVGRGLVKLGMepKSEDKLHIFAATSHKWMKMFLGAQS 147
Cdd:PLN02614 54 SVEKYpnNPMLGRREIVDG-----KPGKYVWQTYQEVYDIVIKLGNSLRSVGV--KDEAKCGIYGANSPEWIISMEACNA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 148 QGIPIVTAYDTLGEKGLIHSLKQTSSAAIFTDNQLLGKLINPL-KVAEKIRYVIYYDNISAEDKRQGGKLyreaqeavdk 226
Cdd:PLN02614 127 HGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISELFKTCpNSTEYMKTVVSFGGVSREQKEEAETF---------- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 227 ikevrpDIKLVSFDELLELGQKAKGEIEPHPPTrdDISCIMYTSGSTGDPKGVVLKHSNVV---AGVGGATINVCDYVGD 303
Cdd:PLN02614 197 ------GLVIYAWDEFLKLGEGKQYDLPIKKKS--DICTIMYTSGTTGDPKGVMISNESIVtliAGVIRLLKSANAALTV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 304 TDKLICFLPLAHIFEMAFELLSFHWGSCIGY--ANVKTLTSasvrncksDLEEFQPTIMVGVAAVWETVKKGILNQINEL 381
Cdd:PLN02614 269 KDVYLSYLPLAHIFDRVIEECFIQHGAAIGFwrGDVKLLIE--------DLGELKPTIFCAVPRVLDRVYSGLQKKLSDG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 382 PRVTKGIFWAAYHSKLKMQKMG---IPGGDTIGNIIFKKVRKATGGHLRYLLNGGSPISVNAQEFISNL-ICPMLIGYGL 457
Cdd:PLN02614 341 GFLKKFVFDSAFSYKFGNMKKGqshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVaCCHVLQGYGL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 458 TETCASLCILNPGHFEY-GVVGDLTGCVTVKLVDVEELGY--FAKDNKGEIWVKGENVLPEYYKNEEETKESLTeDGWFK 534
Cdd:PLN02614 421 TESCAGTFVSLPDELDMlGTVGPPVPNVDIRLESVPEMEYdaLASTPRGEICIRGKTLFSGYYKREDLTKEVLI-DGWLH 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 535 TGDIGMWTDTGSLKIIDRKKNLVKTMNGEYIALEKLESVYRSNSYVQNICVYADQNKVKPVGIIVPNHTPLVKLAKELGI 614
Cdd:PLN02614 500 TGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGV 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 615 mkkqETDIEPYLHNKKLQNAVFEDMIKTAKKQGLVGIELLQGA----VFFDDEwtpqNGFVTSAQKLQRKKILKAVEKDV 690
Cdd:PLN02614 580 ----SGDYNALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIhldpVPFDME----RDLLTPTFKKKRPQLLKYYQSVI 651
|
....
gi 2112360039 691 ESVY 694
Cdd:PLN02614 652 DEMY 655
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
100-559 |
2.17e-81 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 264.56 E-value: 2.17e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 100 TFTEVIEVMHSVGRGLVKLGMEPksEDKLHIFAATSHKWMKMFLGAQSQGIPIVTAYDTLGEKGLIHSLKQTSSAAIFTD 179
Cdd:pfam00501 23 TYRELDERANRLAAGLRALGVGK--GDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLITD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 180 -NQLLGKLINPLKVAEKIRYVIYYDNISaedkrqggklyrEAQEAVDKIKEVRPDIKLVsfdellelgqkakgeiEPHPP 258
Cdd:pfam00501 101 dALKLEELLEALGKLEVVKLVLVLDRDP------------VLKEEPLPEEAKPADVPPP----------------PPPPP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 259 TRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGA--TINVCDYVGDTDKLICFLPLAHIFEMAFELL-SFHWGSCIGYa 335
Cdd:pfam00501 153 DPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIkrVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLgPLLAGATVVL- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 336 nVKTLTSASVRNCKSDLEEFQPTIMVGVAAVWetvkkgilNQINELPRVTKGIFwaayhsklkmqkmgipggdtigniif 415
Cdd:pfam00501 232 -PPGFPALDPAALLELIERYKVTVLYGVPTLL--------NMLLEAGAPKRALL-------------------------- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 416 kkvrkatgGHLRYLLNGGSPISVNAQEFISN-LICPMLIGYGLTETCASLCILNPG---HFEYGVVGDLTGCVTVKLVDV 491
Cdd:pfam00501 277 --------SSLRLVLSGGAPLPPELARRFRElFGGALVNGYGLTETTGVVTTPLPLdedLRSLGSVGRPLPGTEVKIVDD 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2112360039 492 EELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKT 559
Cdd:pfam00501 349 ETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKL 416
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
261-682 |
6.59e-67 |
|
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: 227.63 E-value: 6.59e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 261 DDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVCDYVGdtDKLICFLPLAHIFEMAFELLSFHWGSCIGYANVKTL 340
Cdd:cd17640 88 DDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPG--DRFLSILPIWHSYERSAEYFIFACGCSQAYTSIRTL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 341 tsasvrncKSDLEEFQPTIMVGVAAVWETVKKGILNQINELPRVTKGIFWAAyhsklkmqkmgipggdtigniifkkvrk 420
Cdd:cd17640 166 --------KDDLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFF---------------------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 421 ATGGHLRYLLNGGSPISVNAQEFISNLICPMLIGYGLTETCASLCILNPGHFEYGVVGDLTGCVTVKLVDVEELGYFAKD 500
Cdd:cd17640 210 LSGGIFKFGISGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 501 NKGEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKTMNGEYIALEKLESVYRSNSYV 580
Cdd:cd17640 290 EKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFI 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 581 QNICVYA-DQnkvKPVG-IIVPNHTPLVKLAKELGImkKQETDIEPYLHNKKLqNAVFEDMIKT--AKKQGLVGIELLQG 656
Cdd:cd17640 370 EQIMVVGqDQ---KRLGaLIVPNFEELEKWAKESGV--KLANDRSQLLASKKV-LKLYKNEIKDeiSNRPGFKSFEQIAP 443
|
410 420
....*....|....*....|....*.
gi 2112360039 657 AVFFDDEWTPqNGFVTSAQKLQRKKI 682
Cdd:cd17640 444 FALLEEPFIE-NGEMTQTMKIKRNVV 468
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
261-645 |
1.22e-58 |
|
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: 204.98 E-value: 1.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 261 DDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGatINVCDYVGDTDKLICFLPLAHIFEMAFE-LLSFHWGSCIGYanVKT 339
Cdd:cd05914 89 DDVALINYTSGTTGNSKGVMLTYRNIVSNVDG--VKEVVLLGKGDKILSILPLHHIYPLTFTlLLPLLNGAHVVF--LDK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 340 LTSASVRNcksdLEEFQPTIMVGVAAVWETVKKGILNqinELPRVTKGIFwaayhsKLKMQKmgIPGGDTIGNIIFKKVR 419
Cdd:cd05914 165 IPSAKIIA----LAFAQVTPTLGVPVPLVIEKIFKMD---IIPKLTLKKF------KFKLAK--KINNRKIRKLAFKKVH 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 420 KATGGHLRYLLNGGSPISVNAQEFISNLICPMLIGYGLTETCASLCILNPGHFEYGVVGDLTGCVTVKLVDVEelgyfAK 499
Cdd:cd05914 230 EAFGGNIKEFVIGGAKINPDVEEFLRTIGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPD-----PA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 500 DNKGEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKTMNGEYIALEKLESVYRSNSY 579
Cdd:cd05914 305 TGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPF 384
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2112360039 580 VQnICVYADQNKvKPVGIIVPNhtPLVKLAKELGIMKKQETDIEPYL--HNKKLQN--------AVFEDMIKTAKK 645
Cdd:cd05914 385 VL-ESLVVVQEK-KLVALAYID--PDFLDVKALKQRNIIDAIKWEVRdkVNQKVPNykkiskvkIVKEEFEKTPKG 456
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
100-685 |
1.76e-52 |
|
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: 189.22 E-value: 1.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 100 TFTEVIEVMHSVGRGLVKLGMEPKseDKLHIFAATSHKWMKMFLGAQSQGIPIVTAYDTLGEKGLIHSLKQTSSAAIFtd 179
Cdd:cd05932 8 TWGEVADKARRLAAALRALGLEPG--SKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALF-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 180 nqlLGKLinplkvaekiryviyyDNISAEDKRQGGKLYREAQEAVDKIKEVRpdiklvSFDELLELGQKAKGEIEPHPpt 259
Cdd:cd05932 84 ---VGKL----------------DDWKAMAPGVPEGLISISLPPPSAANCQY------QWDDLIAQHPPLEERPTRFP-- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 260 rDDISCIMYTSGSTGDPKGVVLKHSNVvAGVGGATINVCDyVGDTDKLICFLPLAHIFE-MAFELLSFHWGSCIGYANvk 338
Cdd:cd05932 137 -EQLATLIYTSGTTGQPKGVMLTFGSF-AWAAQAGIEHIG-TEENDRMLSYLPLAHVTErVFVEGGSLYGGVLVAFAE-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 339 tltsaSVRNCKSDLEEFQPTIMVGVAAVWETVKKGIlnqinelprvtkgifwaayHSKLKMQKMG----IPggdTIGNII 414
Cdd:cd05932 212 -----SLDTFVEDVQRARPTLFFSVPRLWTKFQQGV-------------------QDKIPQQKLNlllkIP---VVNSLV 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 415 FKKVRKATG-GHLRYLLNGGSPISVNAQEFISNLICPMLIGYGLTETCASLCILNPGHFEYGVVGDLTGCVTVKLvdvee 493
Cdd:cd05932 265 KRKVLKGLGlDQCRLAGCGSAPVPPALLEWYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRI----- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 494 lgyfakDNKGEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKTMNGEYIALEKLESV 573
Cdd:cd05932 340 ------SEDGEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENK 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 574 YRSNSYVQNICVYAdQNKVKPVGIIVPNhtplvklakELGIMKKQETDIEPYLHNKKlqnAVFEDMIKTAKKQglvgiEL 653
Cdd:cd05932 414 LAEHDRVEMVCVIG-SGLPAPLALVVLS---------EEARLRADAFARAELEASLR---AHLARVNSTLDSH-----EQ 475
|
570 580 590
....*....|....*....|....*....|..
gi 2112360039 654 LQGAVFFDDEWTPQNGFVTSAQKLQRKKILKA 685
Cdd:cd05932 476 LAGIVVVKDPWSIDNGILTPTLKIKRNVLEKA 507
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
100-643 |
6.92e-51 |
|
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: 184.34 E-value: 6.92e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 100 TFTEVIEVMHSVGRGLVKLGMEPKseDKLHIFAATSHKWMKMFLGAQSQGIPIVTAYDTLGEKGLIHSLKQTSSAAIFTD 179
Cdd:cd05911 12 TYAQLRTLSRRLAAGLRKLGLKKG--DVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 180 NQLLGKLINPLKVAEKIRYVIYYDnisaeDKRQGgklyREAQEAVDKIKEVRPDIKLVSFDELLElgqkakgeiephppt 259
Cdd:cd05911 90 PDGLEKVKEAAKELGPKDKIIVLD-----DKPDG----VLSIEDLLSPTLGEEDEDLPPPLKDGK--------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 260 rDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVCDYVGDTDKLICFLPLAHIFEmafeLLSFHWGSCIGYANVkt 339
Cdd:cd05911 146 -DDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYHIYG----LFTTLASLLNGATVI-- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 340 LTSasvrncKSDLEEFqptimvgvaavWETVKKgilNQINELPRVtkgifwaayhsklkmqkmgiPggdTIGNIIFK--K 417
Cdd:cd05911 219 IMP------KFDSELF-----------LDLIEK---YKITFLYLV--------------------P---PIAAALAKspL 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 418 VRKATGGHLRYLLNGGSPISVNAQEFISNLI--CPMLIGYGLTETCASLCILNPGHFEYGVVGDLTGCVTVKLVDV---E 492
Cdd:cd05911 256 LDKYDLSSLRVILSGGAPLSKELQELLAKRFpnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDdgkD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 493 ELGYfakDNKGEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKtMNGEYIALEKLES 572
Cdd:cd05911 336 SLGP---NEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIK-YKGFQVAPAELEA 411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2112360039 573 VYRSNSYVQNICVYADQNKVK---PVGIIVPNHTPLVkLAKEL-GIMKKQETDIepylhnKKLQNAVF--EDMIKTA 643
Cdd:cd05911 412 VLLEHPGVADAAVIGIPDEVSgelPRAYVVRKPGEKL-TEKEVkDYVAKKVASY------KQLRGGVVfvDEIPKSA 481
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
266-587 |
1.63e-43 |
|
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: 163.06 E-value: 1.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 266 IMYTSGSTGDPKGVVLKHSNVVAgvggATINVCDYVGDT--DKLICFLPLAHIFEMAFELL-SFHWGSCIGYanvktLTS 342
Cdd:COG0318 105 ILYTSGTTGRPKGVMLTHRNLLA----NAAAIAAALGLTpgDVVLVALPLFHVFGLTVGLLaPLLAGATLVL-----LPR 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 343 ASVRNCKSDLEEFQPTIMVGVAAVWetvkkgilNQINELPRVTKGIFwaayhsklkmqkmgipggdtigniifkkvrkat 422
Cdd:COG0318 176 FDPERVLELIERERVTVLFGVPTML--------ARLLRHPEFARYDL--------------------------------- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 423 gGHLRYLLNGGSPISVN-AQEFISNLICPMLIGYGLTETCAsLCILNPGHFEY---GVVGDLTGCVTVKLVDVE--ELgy 496
Cdd:COG0318 215 -SSLRLVVSGGAPLPPElLERFEERFGVRIVEGYGLTETSP-VVTVNPEDPGErrpGSVGRPLPGVEVRIVDEDgrEL-- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 497 fAKDNKGEIWVKGENVLPEYYKNEEETKESLtEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKTmNGEYIALEKLESVYRS 576
Cdd:COG0318 291 -PPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIIS-GGENVYPAEVEEVLAA 367
|
330
....*....|.
gi 2112360039 577 NSYVQNICVYA 587
Cdd:COG0318 368 HPGVAEAAVVG 378
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
262-573 |
1.00e-42 |
|
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: 157.83 E-value: 1.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 262 DISCIMYTSGSTGDPKGVVLKHSNVVAGVggATINVCDYVGDTDKLICFLPLAHIFEMAFELLSFHWGSCIGYANVKTLT 341
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAA--AALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 342 SASvrnckSDLEEFQPTIMVGVAAVWETvkkgILNQINElprvtkgifwaayhsklkmqkmgipggdtigniifkkvRKA 421
Cdd:cd04433 79 AAL-----ELIEREKVTILLGVPTLLAR----LLKAPES--------------------------------------AGY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 422 TGGHLRYLLNGGSPISVNAQEFISNLI-CPMLIGYGLTETCASLCILNP--GHFEYGVVGDLTGCVTVKLVDVEElGYFA 498
Cdd:cd04433 112 DLSSLRALVSGGAPLPPELLERFEEAPgIKLVNGYGLTETGGTVATGPPddDARKPGSVGRPVPGVEVRIVDPDG-GELP 190
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2112360039 499 KDNKGEIWVKGENVLPEYYKNEEETkESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKTmNGEYIALEKLESV 573
Cdd:cd04433 191 PGEIGELVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKS-GGENVYPAEVEAV 263
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
208-641 |
1.02e-42 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 165.28 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 208 EDKRQGGKLYReaQEAVDKIKEVRPD-----IKLVSFDELLElGQKAKGEIEPHPPtrDDISCIMYTSGSTGDPKGVVLK 282
Cdd:PTZ00342 251 EDISLGPLEYD--KEKLEKIKDLKEKakklgISIILFDDMTK-NKTTNYKIQNEDP--DFITSIVYTSGTSGKPKGVMLS 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 283 HSNVVAGVggatINVCD------YVGDTDklICFLPLAHIFEMAFELLSFHWGSCIgyanvkTLTSASVRNCKSDLEEFQ 356
Cdd:PTZ00342 326 NKNLYNTV----VPLCKhsifkkYNPKTH--LSYLPISHIYERVIAYLSFMLGGTI------NIWSKDINYFSKDIYNSK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 357 PTIMVGVAAVWETVKKGILNQINELP----RVTKGIFwaayhsKLKMQKMGIPGGDTIGNI--IFKKVRKATGGHLRYLL 430
Cdd:PTZ00342 394 GNILAGVPKVFNRIYTNIMTEINNLPplkrFLVKKIL------SLRKSNNNGGFSKFLEGIthISSKIKDKVNPNLEVIL 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 431 NGGSPISVNAQEFISNLICPMLI-GYGLTETCASLCI--LNPGHFEYgVVGDLTGCVTVKLVDVEElgYFAKDN--KGEI 505
Cdd:PTZ00342 468 NGGGKLSPKIAEELSVLLNVNYYqGYGLTETTGPIFVqhADDNNTES-IGGPISPNTKYKVRTWET--YKATDTlpKGEL 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 506 WVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKTMNGEYIALEKLESVYRSNSYVQNICV 585
Cdd:PTZ00342 545 LIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVV 624
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2112360039 586 YADQNKVKPVGIIVPNHTPLVKLAKELGIMKKQETDIEPYLHN---KKLQNAVFEDMIK 641
Cdd:PTZ00342 625 YGDDSMDGPLAIISVDKYLLFKCLKDDNMLESTGINEKNYLEKltdETINNNIYVDYVK 683
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
95-566 |
1.23e-42 |
|
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: 163.30 E-value: 1.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 95 GYHYNTFTEVIEVMHSVGRGLVKLGMEpksedKLH---IFAATSHKWMKMFLGAQSQGIPIVTAYDTLGEKGLIHSLKQT 171
Cdd:cd05933 5 KWHTLTYKEYYEACRQAAKAFLKLGLE-----RFHgvgILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 172 SSAAIFTDNQllgklinplKVAEKIRYViyydnisaEDKRQGGKL---YREaqeavdKIKEVRPdiKLVSFDELLELGQK 248
Cdd:cd05933 80 EANILVVENQ---------KQLQKILQI--------QDKLPHLKAiiqYKE------PLKEKEP--NLYSWDEFMELGRS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 249 AKGE-----IEPHPPtrDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVcDYVGDTDK---LICFLPLAHIFEMA 320
Cdd:cd05933 135 IPDEqldaiISSQKP--NQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHM-DLRPATVGqesVVSYLPLSHIAAQI 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 321 FEL-LSFHWGSCIGYANVKTLTSASVrnckSDLEEFQPTIMVGVAAVWETVKKGILNQINELPRVTKGIF-WAA-----Y 393
Cdd:cd05933 212 LDIwLPIKVGGQVYFAQPDALKGTLV----KTLREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIAsWAKgvgleT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 394 HSKLKMQKMGIPGGDTIGN-IIFKKVRKATG-GHLRYLLNGGSPISVNAQEFISNLICPMLIGYGLTETCASLCILNPGH 471
Cdd:cd05933 288 NLKLMGGESPSPLFYRLAKkLVFKKVRKALGlDRCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNPQA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 472 FEYGVVGD-LTGCvTVKLVDVEelgyfaKDNKGEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKII 550
Cdd:cd05933 368 YRLLSCGKaLPGC-KTKIHNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYIT 440
|
490
....*....|....*.
gi 2112360039 551 DRKKNLVKTMNGEYIA 566
Cdd:cd05933 441 GRIKELIITAGGENVP 456
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
236-557 |
9.19e-42 |
|
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: 158.11 E-value: 9.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 236 LVSFDELLELGQKAKGEIEPHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVCDYVGDTDKLICFLPLAH 315
Cdd:cd05936 100 LIVAVSFTDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEGDDVVLAALPLFH 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 316 IFEMAFELLSFhwgSCIGYANVkTLTSASVRNCKSDLEEFQPTIMVGVAAvwetvkkgILNQINELPRVTKGIFwaayhs 395
Cdd:cd05936 180 VFGLTVALLLP---LALGATIV-LIPRFRPIGVLKEIRKHRVTIFPGVPT--------MYIALLNAPEFKKRDF------ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 396 klkmqkmgipggdtigniifkkvrkatgGHLRYLLNGGSPISVNAQEFISNLI-CPMLIGYGLTETCASLCiLNPGHFEY 474
Cdd:cd05936 242 ----------------------------SSLRLCISGGAPLPVEVAERFEELTgVPIVEGYGLTETSPVVA-VNPLDGPR 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 475 --GVVG-DLTGcVTVKLVDVEelGYFAKDNK-GEIWVKGENVLPEYYKNEEETKESLTeDGWFKTGDIGMWTDTGSLKII 550
Cdd:cd05936 293 kpGSIGiPLPG-TEVKIVDDD--GEELPPGEvGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIV 368
|
....*..
gi 2112360039 551 DRKKNLV 557
Cdd:cd05936 369 DRKKDMI 375
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
100-571 |
3.50e-38 |
|
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: 149.88 E-value: 3.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 100 TFTEVIEVMHSVGRGLVKLGMEPKseDKLHIFAATSHKWMKMFLGAQSQG-IPIVTAYDTLGEKgLIHSLKQTSSAAIFT 178
Cdd:cd17641 13 TWADYADRVRAFALGLLALGVGRG--DVVAILGDNRPEWVWAELAAQAIGaLSLGIYQDSMAEE-VAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 179 -DNQLLGKLINPLKVAEKIRYVIYYDnisaedkRQGGKLYReaqeavdkikevrpDIKLVSFDELLELGQKA------KG 251
Cdd:cd17641 90 eDEEQVDKLLEIADRIPSVRYVIYCD-------PRGMRKYD--------------DPRLISFEDVVALGRALdrrdpgLY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 252 EIEPHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGvgGATINVCDYVGDTDKLICFLPLAHIFEMAfellsfhwgsc 331
Cdd:cd17641 149 EREVAAGKGEDVAVLCTTSGTTGKPKLAMLSHGNFLGH--CAAYLAADPLGPGDEYVSVLPLPWIGEQM----------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 332 igYANVKTLTSASVRNC-------KSDLEEFQPTIMVGVAAVWETVKKGILNQINELPRVTKGIFWAAYHSKLKM---QK 401
Cdd:cd17641 216 --YSVGQALVCGFIVNFpeepetmMEDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKLGLRAldrGK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 402 MGIPGGDTIGN-------IIFKKVRKATG-GHLRYLLNGGSPISVNAQEFISNLICPMLIGYGLTETCASLCILNPGHFE 473
Cdd:cd17641 294 RGRPVSLWLRLaswladaLLFRPLRDRLGfSRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVD 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 474 YGVVGdltgcvtVKLVDVEelgyFAKDNKGEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRK 553
Cdd:cd17641 374 PDTVG-------VPFPGTE----VRIDEVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRA 442
|
490
....*....|....*...
gi 2112360039 554 KNLVKTMNGEYIALEKLE 571
Cdd:cd17641 443 KDVGTTSDGTRFSPQFIE 460
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
100-557 |
8.54e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 141.97 E-value: 8.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 100 TFTEVIEVMHSVGRGLVKLGMEPKseDKLHIFAATSHKWMKMFLGAQSQG---IPIVTAYdTLGEKGLIhsLKQTSSAAI 176
Cdd:PRK07656 32 TYAELNARVRRAAAALAALGIGKG--DRVAIWAPNSPHWVIAALGALKAGavvVPLNTRY-TADEAAYI--LARGDAKAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 177 FTDNQLLGKLINPLKVAEKIRYVIYYDNISAEDkrqggklyreaqeavdkikevrPDIKLVSFDELLELGQKAKGEIEPH 256
Cdd:PRK07656 107 FVLGLFLGVDYSATTRLPALEHVVICETEEDDP----------------------HTEKMKTFTDFLAAGDPAERAPEVD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 257 PptrDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGatinVCDYVGDT--DKLICFLPLAHIFemafeLLSFHWGSCIgy 334
Cdd:PRK07656 165 P---DDVADILFTSGTTGRPKGAMLTHRQLLSNAAD----WAEYLGLTegDRYLAANPFFHVF-----GYKAGVNAPL-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 335 ANVKTLTSASVrncksdleeFQPtimvgvAAVWETVKKgilnqinelPRVTkgIFwaayhsklkmqkmgiPGGDTIGNII 414
Cdd:PRK07656 231 MRGATILPLPV---------FDP------DEVFRLIET---------ERIT--VL---------------PGPPTMYNSL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 415 FKKVRKATG--GHLRYLLNGGSPISVN-AQEFISNLICPMLI-GYGLTETCASLCILNPGH-FEY--GVVGdlTGCVTVK 487
Cdd:PRK07656 270 LQHPDRSAEdlSSLRLAVTGAASMPVAlLERFESELGVDIVLtGYGLSEASGVTTFNRLDDdRKTvaGTIG--TAIAGVE 347
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2112360039 488 LVDVEELGYFAKDNK-GEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLV 557
Cdd:PRK07656 348 NKIVNELGEEVPVGEvGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF 418
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
251-672 |
1.49e-35 |
|
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: 142.21 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 251 GEIEPHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVCDYVgDTDKLICFLPLAHIfeMAFELLSfhwgs 330
Cdd:cd17632 213 APLFRPEPDDDPLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRP-PASITLNFMPMSHI--AGRISLY----- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 331 cIGYANVKTLTSASVRNCKS---DLEEFQPTIMVGVAAVWETVKKGILNQINElpRVTKGIFWAAYHSKLKMQkmgipgg 407
Cdd:cd17632 285 -GTLARGGTAYFAAASDMSTlfdDLALVRPTELFLVPRVCDMLFQRYQAELDR--RSVAGADAETLAERVKAE------- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 408 dtigniIFKKVRkatGGHLRYLLNGGSPISVNAQEFISNLI-CPMLIGYGLTETCASLC---ILNPGHFEYgvvgdltgc 483
Cdd:cd17632 355 ------LRERVL---GGRLLAAVCGSAPLSAEMKAFMESLLdLDLHDGYGSTEAGAVILdgvIVRPPVLDY--------- 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 484 vtvKLVDVEELGYFAKDN---KGEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKTM 560
Cdd:cd17632 417 ---KLVDVPELGYFRTDRphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLS 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 561 NGEYIALEKLESVYRSNSYVQNICVYADQNKVKPVGIIVPNHTPLVklakelgimkkQETDIEpylhnkkLQNAVFEDMI 640
Cdd:cd17632 494 QGEFVTVARLEAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDALA-----------GEDTAR-------LRAALAESLQ 555
|
410 420 430
....*....|....*....|....*....|..
gi 2112360039 641 KTAKKQGLVGIELLQGAVFFDDEWTPQNGFVT 672
Cdd:cd17632 556 RIAREAGLQSYEIPRDFLIETEPFTIANGLLS 587
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
261-573 |
6.29e-34 |
|
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: 135.05 E-value: 6.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 261 DDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVCdyVGDTDKLICFLPLAHIfemafellsfhwgsciGYANVKTL 340
Cdd:cd17631 98 DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALD--LGPDDVLLVVAPLFHI----------------GGLGVFTL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 341 tsasvrncksdleefqPTIMVGVAAV----WETVKkgILNQINElPRVTKgiFWAAyhsklkmqkmgiPggdTIGNIIFK 416
Cdd:cd17631 160 ----------------PTLLRGGTVVilrkFDPET--VLDLIER-HRVTS--FFLV------------P---TMIQALLQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 417 KVRKATGGH--LRYLLNGGSPISVNAQEFISNLICPMLIGYGLTETCASLCILNPGHFE--YGVVGDLTGCVTVKLVDve 492
Cdd:cd17631 204 HPRFATTDLssLRAVIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSPEDHRrkLGSAGRPVFFVEVRIVD-- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 493 ELGYFAKDNK-GEIWVKGENVLPEYYKNEEETKESLtEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKTmNGEYIALEKLE 571
Cdd:cd17631 282 PDGREVPPGEvGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMIIS-GGENVYPAEVE 359
|
..
gi 2112360039 572 SV 573
Cdd:cd17631 360 DV 361
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
238-573 |
3.66e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 131.08 E-value: 3.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 238 SFDELLelgqKAKGEIEPHPPTR-DDISCIMYTSGSTGDPKGVVLKHSNVVAGvggaTINVCDY--VGDTDKLICFLPLA 314
Cdd:PRK06187 147 EYEELL----AAASDTFDFPDIDeNDAAAMLYTSGTTGHPKGVVLSHRNLFLH----SLAVCAWlkLSRDDVYLVIVPMF 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 315 HIFEMAFELLSFHWGSCIGYAnvktltsasvrncksdlEEFQPTimvgvaAVWETVkkgilnqinELPRVTKgIFwaayh 394
Cdd:PRK06187 219 HVHAWGLPYLALMAGAKQVIP-----------------RRFDPE------NLLDLI---------ETERVTF-FF----- 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 395 sklkmqkmGIPggdTIGNIIFKKVRKATG--GHLRYLLNGGSPISVN-AQEFISNLICPMLIGYGLTETCASLCILNP-- 469
Cdd:PRK06187 261 --------AVP---TIWQMLLKAPRAYFVdfSSLRLVIYGGAALPPAlLREFKEKFGIDLVQGYGMTETSPVVSVLPPed 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 470 ---GHFEY-GVVGDLTGCVTVKLVDvEELGYFAKDNK--GEIWVKGENVLPEYYKNEEETKESLtEDGWFKTGDIGMWTD 543
Cdd:PRK06187 330 qlpGQWTKrRSAGRPLPGVEARIVD-DDGDELPPDGGevGEIIVRGPWLMQGYWNRPEATAETI-DGGWLHTGDVGYIDE 407
|
330 340 350
....*....|....*....|....*....|
gi 2112360039 544 TGSLKIIDRKKNLVKTmNGEYIALEKLESV 573
Cdd:PRK06187 408 DGYLYITDRIKDVIIS-GGENIYPRELEDA 436
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
259-573 |
4.69e-31 |
|
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: 127.74 E-value: 4.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 259 TRDDISCIMYTSGSTGDPKGVVLKHSNVVAgvggatiNVCDYVGDTDK-------LICFLPLAHIFEMAFELLSfhwGSC 331
Cdd:cd05904 156 KQDDVAALLYSSGTTGRSKGVMLTHRNLIA-------MVAQFVAGEGSnsdsedvFLCVLPMFHIYGLSSFALG---LLR 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 332 IGyANVKTLTSASVRNCKSDLEEFQ-------PTIMVGVaavwetVKKGILNQinelprvtkgifwaayHSKLKmqkmgi 404
Cdd:cd05904 226 LG-ATVVVMPRFDLEELLAAIERYKvthlpvvPPIVLAL------VKSPIVDK----------------YDLSS------ 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 405 pggdtigniifkkvrkatgghLRYLLNGGSPISVNAQE-FISNLICPMLI-GYGLTETCA-SLCILNPGHF--EYGVVGD 479
Cdd:cd05904 277 ---------------------LRQIMSGAAPLGKELIEaFRAKFPNVDLGqGYGMTESTGvVAMCFAPEKDraKYGSVGR 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 480 LTGCVTVKLVDVEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKt 559
Cdd:cd05904 336 LVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIK- 414
|
330
....*....|....
gi 2112360039 560 MNGEYIALEKLESV 573
Cdd:cd05904 415 YKGFQVAPAELEAL 428
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
187-581 |
1.69e-30 |
|
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: 125.89 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 187 INP-LKVAEKIRYviYYDNISA---EDKRQGGKLYREAQEAVDKIKEVRPD----IKLVSFDELLELGQKAKGEIEPHPP 258
Cdd:cd05926 69 LNPaYKKAEFEFY--LADLGSKlvlTPKGELGPASRAASKLGLAILELALDvgvlIRAPSAESLSNLLADKKNAKSEGVP 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 259 TRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVCdyVGDTDKLICFLPLAHIFEMAFELLS--FHWGSCIgyan 336
Cdd:cd05926 147 LPDDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYK--LTPDDRTLVVMPLFHVHGLVASLLStlAAGGSVV---- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 337 VKTLTSASVrnCKSDLEEFQPTimvgvaavWETVkkgilnqinelprvtkgifwaayhsklkmqkmgIPggdTIGNIIFK 416
Cdd:cd05926 221 LPPRFSAST--FWPDVRDYNAT--------WYTA---------------------------------VP---TIHQILLN 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 417 KVRKATGG---HLRYLLNGGSPISVN-AQEFISNLICPMLIGYGLTETC--ASLCILNPGHFEYGVVGDLTGcvtVKLVD 490
Cdd:cd05926 255 RPEPNPESpppKLRFIRSCSASLPPAvLEALEATFGAPVLEAYGMTEAAhqMTSNPLPPGPRKPGSVGKPVG---VEVRI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 491 VEELGYFAKDN-KGEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVktmN--GEYIAL 567
Cdd:cd05926 332 LDEDGEILPPGvVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELI---NrgGEKISP 408
|
410
....*....|....
gi 2112360039 568 EKLESVYRSNSYVQ 581
Cdd:cd05926 409 LEVDGVLLSHPAVL 422
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
100-682 |
3.29e-29 |
|
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: 122.64 E-value: 3.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 100 TFTEVIEVMHSVGRGLVKLGMepKSEDKLHIFAATSHKWMKMFLGAQSQGIPIVTAYDTLGEKGLIHSLKQTSSAAIFTD 179
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGL--KQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 180 NQLLGKLINplkVAEKIRYViyyDNISAEDKRQGgklYREAQEAVDKIKEVRP------DIKLVSFDEllelgqkakgei 253
Cdd:cd17642 124 KKGLQKVLN---VQKKLKII---KTIIILDSKED---YKGYQCLYTFITQNLPpgfneyDFKPPSFDR------------ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 254 ephpptRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGAT-INVCDYVGDTDKLICFLPLAHIFEMAfellsfhwgSCI 332
Cdd:cd17642 183 ------DEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARdPIFGNQIIPDTAILTVIPFHHGFGMF---------TTL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 333 GYAnvktltsasvrncksdleefqptiMVGVAAVWetvkkgilnqineLPRVTKGIFWAAYHSKLKMQKMGIPggdTIGN 412
Cdd:cd17642 248 GYL------------------------ICGFRVVL-------------MYKFEEELFLRSLQDYKVQSALLVP---TLFA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 413 IIFKK--VRKATGGHLRYLLNGGSPISVNAQEFISNLICPMLI--GYGLTETCASLCILNPGHFEYGVVGDLTGCVTVKL 488
Cdd:cd17642 288 FFAKStlVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIrqGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 489 VDVEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKtMNGEYIALE 568
Cdd:cd17642 368 VDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIK-YKGYQVPPA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 569 KLESVYRSNSYVQNICVyadqnkvkpVGIIVPN--HTPLVKLAKELGImkkqetdiepYLHNKKLQNAVfEDMIKTAKKq 646
Cdd:cd17642 447 ELESILLQHPKIFDAGV---------AGIPDEDagELPAAVVVLEAGK----------TMTEKEVMDYV-ASQVSTAKR- 505
|
570 580 590
....*....|....*....|....*....|....*.
gi 2112360039 647 glvgielLQGAVFFDDEwTPQNgfvtSAQKLQRKKI 682
Cdd:cd17642 506 -------LRGGVKFVDE-VPKG----LTGKIDRRKI 529
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
233-604 |
5.45e-28 |
|
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: 117.55 E-value: 5.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 233 DIKLVSFDELlELGQKAKGEIEPHPPTrDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVcdYVGDTDKLICFLP 312
Cdd:TIGR01923 85 DFQADSLDRI-EAAGRYETSLSASFNM-DQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENL--GFTEDDNWLLSLP 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 313 LAHIfemafellsfhwgscigyanvktltsasvrnckSDLEEFQPTIMVGVAAVWETVKKGILNQINELPrVTkgifwaa 392
Cdd:TIGR01923 161 LYHI---------------------------------SGLSILFRWLIEGATLRIVDKFNQLLEMIANER-VT------- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 393 yHSKLKMQKMgipggdtigniifKKVRKATGGH--LRYLLNGGSPISvnaQEFISNLIC---PMLIGYGLTETCASLCIL 467
Cdd:TIGR01923 200 -HISLVPTQL-------------NRLLDEGGHNenLRKILLGGSAIP---APLIEEAQQyglPIYLSYGMTETCSQVTTA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 468 NPGHF-EYGVVGDLTGCVTVKL-VDveelgyfAKDNKGEIWVKGENVLPEYYKNEEETkESLTEDGWFKTGDIGMWTDTG 545
Cdd:TIGR01923 263 TPEMLhARPDVGRPLAGREIKIkVD-------NKEGHGEIMVKGANLMKGYLYQGELT-PAFEQQGWFNTGDIGELDGEG 334
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2112360039 546 SLKIIDRKKNLVKTmNGEYIALEKLESVYRSNSYVQNICVYADQNK---VKPVGIIVPNHTP 604
Cdd:TIGR01923 335 FLYVLGRRDDLIIS-GGENIYPEEIETVLYQHPGIQEAVVVPKPDAewgQVPVAYIVSESDI 395
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
100-585 |
1.79e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 113.52 E-value: 1.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 100 TFTEVIEVMHSVGRGLVKLGMepKSEDKLHIFAATShkwMKMFLgaqsqgipivtaydtlgekgLIHSLKQTSSAAIFTD 179
Cdd:PRK03640 29 TFMELHEAVVSVAGKLAALGV--KKGDRVALLMKNG---MEMIL--------------------VIHALQQLGAVAVLLN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 180 NQLLGKLIN-PLKVAEkIRYVIYYDNIsaEDKRQGGKLyreaqeavdkikevrpdiklVSFDELlelGQKAKGEIEPHPP 258
Cdd:PRK03640 84 TRLSREELLwQLDDAE-VKCLITDDDF--EAKLIPGIS--------------------VKFAEL---MNGPKEEAEIQEE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 259 -TRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVCdyVGDTDKLICFLPLAHIfemafELLSFHWGSCIGYANV 337
Cdd:PRK03640 138 fDLDEVATIMYTSGTTGKPKGVIQTYGNHWWSAVGSALNLG--LTEDDCWLAAVPIFHI-----SGLSILMRSVIYGMRV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 338 KTLTSASVRNCKSDLEEFQPTIMVGVAAVWETVkkgilnqINELPRvtkgifwAAYHSklkmqkmgipggdtigniifkk 417
Cdd:PRK03640 211 VLVEKFDAEKINKLLQTGGVTIISVVSTMLQRL-------LERLGE-------GTYPS---------------------- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 418 vrkatggHLRYLLNGGSPISVNAQEfisnlIC-----PMLIGYGLTETCASLCILNPghfEY-----GVVGDLTGCVTVK 487
Cdd:PRK03640 255 -------SFRCMLLGGGPAPKPLLE-----QCkekgiPVYQSYGMTETASQIVTLSP---EDaltklGSAGKPLFPCELK 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 488 LVDveELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLtEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKTmNGEYIAL 567
Cdd:PRK03640 320 IEK--DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLIIS-GGENIYP 395
|
490
....*....|....*...
gi 2112360039 568 EKLESVYRSNSYVQNICV 585
Cdd:PRK03640 396 AEIEEVLLSHPGVAEAGV 413
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
224-557 |
2.54e-26 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 114.00 E-value: 2.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 224 VDKIKEVRPDIKL---VSFDELLELG---QKAKGEIEphpptRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINV 297
Cdd:PRK08974 168 VKYIKRLVPKYHLpdaISFRSALHKGrrmQYVKPELV-----PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAY 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 298 CDYVGDTDKL-ICFLPLAHIFEMAFE-LLSFHWGSCigyaNVKTLTSASVRNCKSDLEEFQPTIMVGVaavwETVKKGIL 375
Cdd:PRK08974 243 GPLLHPGKELvVTALPLYHIFALTVNcLLFIELGGQ----NLLITNPRDIPGFVKELKKYPFTAITGV----NTLFNALL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 376 NQINelprvtkgiFWAAYHSKLKMQkmgIPGGDTIGNIIFKKVRKATGGHLryllnggspisvnaqefisnlicpmLIGY 455
Cdd:PRK08974 315 NNEE---------FQELDFSSLKLS---VGGGMAVQQAVAERWVKLTGQYL-------------------------LEGY 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 456 GLTEtCASLCILNPGHFEY--GVVGDLTGCVTVKLVDvEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLtEDGWF 533
Cdd:PRK08974 358 GLTE-CSPLVSVNPYDLDYysGSIGLPVPSTEIKLVD-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWL 434
|
330 340
....*....|....*....|....
gi 2112360039 534 KTGDIGMWTDTGSLKIIDRKKNLV 557
Cdd:PRK08974 435 ATGDIAVMDEEGFLRIVDRKKDMI 458
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
218-573 |
1.83e-25 |
|
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: 111.22 E-value: 1.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 218 REAQEAVDKIKEVR--PDIKLVSFDELLElgqkAKGEIEPHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATI 295
Cdd:cd05906 126 AELVAEFAGLETLSglPGIRVLSIEELLD----TAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQ 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 296 NvCDYVGDTDKLIcFLPLAHIFEmafeLLSFH-WGSCIGYANVKTLTSASVRNcksdleefqPTimvgvaaVWetvkkgi 374
Cdd:cd05906 202 H-NGLTPQDVFLN-WVPLDHVGG----LVELHlRAVYLGCQQVHVPTEEILAD---------PL-------RW------- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 375 LNQINELpRVTkgIFWA---AYhSKLKMQKMGIPGGDtiGNIifkkvrkatgGHLRYLLNGGSPISVN-AQEFI------ 444
Cdd:cd05906 253 LDLIDRY-RVT--ITWApnfAF-ALLNDLLEEIEDGT--WDL----------SSLRYLVNAGEAVVAKtIRRLLrllepy 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 445 ---SNLICPmliGYGLTETCASlCILNPGHFEYGVVGDLT---------GcVTVKLVDvEELGYFAKDNKGEIWVKGENV 512
Cdd:cd05906 317 glpPDAIRP---AFGMTETCSG-VIYSRSFPTYDHSQALEfvslgrpipG-VSMRIVD-DEGQLLPEGEVGRLQVRGPVV 390
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2112360039 513 LPEYYKNEEETKESLTEDGWFKTGDIGmWTDTGSLKIIDRKKNLVkTMNGEYIALEKLESV 573
Cdd:cd05906 391 TKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTKDTI-IVNGVNYYSHEIEAA 449
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
261-576 |
3.58e-25 |
|
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: 108.59 E-value: 3.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 261 DDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVCDYvgDTDKLICFLPLAHIFEMAFELLSFHWGscigyANVKTL 340
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLT--EDDNWLCALPLFHISGLSILMRSVIYG-----MTVYLV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 341 TSASVRNCKSDLEEFQPTIMVGVAAvwetvkkgILNQINElprvtkgIFWAAYHSklkmqkmgipggdtigniifkkvrk 420
Cdd:cd05912 150 DKFDAEQVLHLINSGKVTIISVVPT--------MLQRLLE-------ILGEGYPN------------------------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 421 atggHLRYLLNGGSPISVNAQEFISNLICPMLIGYGLTETCASLCILNPGHFE--YGVVGDLTGCVTVKLVDVEElgyfA 498
Cdd:cd05912 190 ----NLRCILLGGGPAPKPLLEQCKEKGIPVYQSYGMTETCSQIVTLSPEDALnkIGSAGKPLFPVELKIEDDGQ----P 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2112360039 499 KDNKGEIWVKGENVLPEYYKNEEETKESlTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKTmNGEYIALEKLESVYRS 576
Cdd:cd05912 262 PYEVGEILLKGPNVTKGYLNRPDATEES-FENGWFKTGDIGYLDEEGFLYVLDRRSDLIIS-GGENIYPAEIEEVLLS 337
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
262-601 |
5.71e-25 |
|
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: 108.53 E-value: 5.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 262 DISCIMYTSGSTGDPKGVVLKHSNVVAGVGgATINVCDYVGDtDKLICFLPLAHIFEMAFELLSFHW--GSCIgyanvkT 339
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVR-ALVDAWRWTED-DVLLHVLPLHHVHGLVNALLCPLFagASVE------F 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 340 LTSASVRNCKSDLEEFQPTIMVGVAAVWetvkkgilnqinelprvTKGIfwaAYHSKLKMQKMGIpggdtigniifkkvR 419
Cdd:cd05941 162 LPKFDPKEVAISRLMPSITVFMGVPTIY-----------------TRLL---QYYEAHFTDPQFA--------------R 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 420 KATGGHLRYLLNGGSPISVNAQEFISNLIC-PMLIGYGLTETCASLCilNPGHFEY--GVVGDLTGCVTVKLVDVEELGY 496
Cdd:cd05941 208 AAAAERLRLMVSGSAALPVPTLEEWEAITGhTLLERYGMTEIGMALS--NPLDGERrpGTVGMPLPGVQARIVDEETGEP 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 497 FAKDNKGEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKTMNGEYI-ALEkLESVYR 575
Cdd:cd05941 286 LPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSGGYKVsALE-IERVLL 364
|
330 340
....*....|....*....|....*....
gi 2112360039 576 SNSYVQNICVYADQNKV---KPVGIIVPN 601
Cdd:cd05941 365 AHPGVSECAVIGVPDPDwgeRVVAVVVLR 393
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
223-557 |
1.10e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 108.70 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 223 AVDKIKEVRPDIKL---VSFDELLELGQ-KAKGEIEPHPptrDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVC 298
Cdd:PRK05677 168 VVKHVKKMVPAYHLpqaVKFNDALAKGAgQPVTEANPQA---DDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMG 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 299 DYVGD-TDKLICFLPLAHIFemAFellSFHWGSCIGYANVKTLTSASvrnckSDLEEfqptiMVGVAAVWETvkKGILNq 377
Cdd:PRK05677 245 SNLNEgCEILIAPLPLYHIY--AF---TFHCMAMMLIGNHNILISNP-----RDLPA-----MVKELGKWKF--SGFVG- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 378 INELprvtkgiFWAAYHSKlkmqkmgipggdtigniifkKVRKATGGHLRYLLNGGSPISVNAQEFISNLI-CPMLIGYG 456
Cdd:PRK05677 307 LNTL-------FVALCNNE--------------------AFRKLDFSALKLTLSGGMALQLATAERWKEVTgCAICEGYG 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 457 LTETCASLCILNPGHFEYGVVGDLTGCVTVKLVDvEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTEDGWFKTG 536
Cdd:PRK05677 360 MTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVID-DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTG 438
|
330 340
....*....|....*....|.
gi 2112360039 537 DIGMWTDTGSLKIIDRKKNLV 557
Cdd:PRK05677 439 DIALIQEDGYMRIVDRKKDMI 459
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
144-557 |
1.42e-24 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 108.37 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 144 GAQSQGIPIVTAYDTLGEKGLIHSLKQTSSAAIFTDNqLLGKLINPLKVAEKIRYVIyydnisaedKRQGGKLYREAQ-- 221
Cdd:PRK12492 94 GALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLN-MFGKLVQEVLPDTGIEYLI---------EAKMGDLLPAAKgw 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 222 ---EAVDKIKEVRPDIKL---VSFDELLELGQKAKgeIEPHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATI 295
Cdd:PRK12492 164 lvnTVVDKVKKMVPAYHLpqaVPFKQALRQGRGLS--LKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 296 NVCDYVGDTDKL--------ICFLPLAHIFemAFEllsfhwGSCI-----GYANVKTLTSASVRNCKSDLEEFQPTIMVG 362
Cdd:PRK12492 242 CLSQLGPDGQPLmkegqevmIAPLPLYHIY--AFT------ANCMcmmvsGNHNVLITNPRDIPGFIKELGKWRFSALLG 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 363 vaavwetvkkgiLNQInelprvtkgiFWAAyhsklkmqkMGIPGgdtigniiFKKVRKAtggHLRYLLNGGSP-ISVNAQ 441
Cdd:PRK12492 314 ------------LNTL----------FVAL---------MDHPG--------FKDLDFS---ALKLTNSGGTAlVKATAE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 442 EFISNLICPMLIGYGLTETCASLCIlNP--GHFEYGVVGDLTGCVTVKLVDvEELGYFAKDNKGEIWVKGENVLPEYYKN 519
Cdd:PRK12492 352 RWEQLTGCTIVEGYGLTETSPVAST-NPygELARLGTVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQ 429
|
410 420 430
....*....|....*....|....*....|....*...
gi 2112360039 520 EEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLV 557
Cdd:PRK12492 430 PEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLI 467
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
187-573 |
1.42e-23 |
|
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: 105.02 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 187 INPLKVAEKIRYVIYYdnisAEDK-----RQGGKLYreaQEAVDKIKEVRPDIKLVSFDELLELGQKAKGE----IEPHP 257
Cdd:cd12119 80 INPRLFPEQIAYIINH----AEDRvvfvdRDFLPLL---EAIAPRLPTVEHVVVMTDDAAMPEPAGVGVLAyeelLAAES 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 258 PTRD-------DISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVCDYVGDTDKLICFLPLahifemafellsFH--- 327
Cdd:cd12119 153 PEYDwpdfdenTAAAICYTSGTTGNPKGVVYSHRSLVLHAMAALLTDGLGLSESDVVLPVVPM------------FHvna 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 328 WGscIGYANV----------KTLTSASVRNCksdLEEFQPTIMVGVAAVWETVkkgilnqineLPRVTKgifwaayhskl 397
Cdd:cd12119 221 WG--LPYAAAmvgaklvlpgPYLDPASLAEL---IEREGVTFAAGVPTVWQGL----------LDHLEA----------- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 398 kmqkmgipggdtigniifkkvRKATGGHLRYLLNGGSPISVNAQEFISNLICPMLIGYGLTETC--ASLCILNPGHFEYG 475
Cdd:cd12119 275 ---------------------NGRDLSSLRRVVIGGSAVPRSLIEAFEERGVRVIHAWGMTETSplGTVARPPSEHSNLS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 476 VVGDL-----TG----CVTVKLVDvEELGYFAKDNK--GEIWVKGENVLPEYYKNEEETkESLTEDGWFKTGDIGMWTDT 544
Cdd:cd12119 334 EDEQLalrakQGrpvpGVELRIVD-DDGRELPWDGKavGELQVRGPWVTKSYYKNDEES-EALTEDGWLRTGDVATIDED 411
|
410 420
....*....|....*....|....*....
gi 2112360039 545 GSLKIIDRKKNLVKTmNGEYIALEKLESV 573
Cdd:cd12119 412 GYLTITDRSKDVIKS-GGEWISSVELENA 439
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
237-559 |
2.28e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 104.70 E-value: 2.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 237 VSFDELLELGQKAKGEIEPHP-PTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVCDYVGDTDKLICFLPLAH 315
Cdd:PRK05605 194 VPWETLVDAAIGGDGSDVSHPrPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPGLGDGPERVLAALPMFH 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 316 IFEMAfelLSFHWGSCIGyANVKTLTSASVRNCKSDLEEFQPTIMVGVAAVWETVKKgilnqinelprvtkgifwAAyhs 395
Cdd:PRK05605 274 AYGLT---LCLTLAVSIG-GELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAE------------------AA--- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 396 klKMQKMGIPGgdtigniifkkvrkatgghLRYLLNGGSPISVNAQEFISNLICPMLI-GYGLTETcASLCILNP--GHF 472
Cdd:PRK05605 329 --EERGVDLSG-------------------VRNAFSGAMALPVSTVELWEKLTGGLLVeGYGLTET-SPIIVGNPmsDDR 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 473 EYGVVGDLTGCVTVKLVDVEELGY-FAKDNKGEIWVKGENVLPEYYKNEEETKESLtEDGWFKTGDIGMWTDTGSLKIID 551
Cdd:PRK05605 387 RPGYVGVPFPDTEVRIVDPEDPDEtMPDGEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVD 465
|
....*...
gi 2112360039 552 RKKNLVKT 559
Cdd:PRK05605 466 RIKELIIT 473
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
142-572 |
7.77e-23 |
|
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: 102.41 E-value: 7.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 142 FLGAQSQG-IPIVTAYdTLGEKGLIHSLKQTSSAAIFTDNQLLGKL-INPLKVAEKIRYVIYYDNIsaedKRQGGKLyre 219
Cdd:cd05909 48 NFALALSGkVPVMLNY-TAGLRELRACIKLAGIKTVLTSKQFIEKLkLHHLFDVEYDARIVYLEDL----RAKISKA--- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 220 aqeavDKIKeVRPDIKLVSFDELLELGQkakgeiepHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATiNVCD 299
Cdd:cd05909 120 -----DKCK-AFLAGKFPPKWLLRIFGV--------APVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQIT-AIFD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 300 YVGDtDKLICFLPLahifemafellsFHwgsCIGYanvktltsasvrncksdleefqptimvgVAAVWETVKKGILNQIN 379
Cdd:cd05909 185 PNPE-DVVFGALPF------------FH---SFGL----------------------------TGCLWLPLLSGIKVVFH 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 380 ELPRVTKGIFWAAYHSKLKMqkmgIPGGDTIGNIIFKKVRKATGGHLRYLLNGGSPISVN-AQEFISNLICPMLIGYGLT 458
Cdd:cd05909 221 PNPLDYKKIPELIYDKKATI----LLGTPTFLRGYARAAHPEDFSSLRLVVAGAEKLKDTlRQEFQEKFGIRILEGYGTT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 459 ETCASLCILNPG-HFEYGVVGDLTGCVTVKLVDVEELGYFAKDNKGEIWVKGENVLpEYYKNEEETKESLTEDGWFKTGD 537
Cdd:cd05909 297 ECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVM-LGYLNEPELTSFAFGDGWYDTGD 375
|
410 420 430
....*....|....*....|....*....|....*
gi 2112360039 538 IGMWTDTGSLKIIDRKKNLVKtMNGEYIALEKLES 572
Cdd:cd05909 376 IGKIDGEGFLTITGRLSRFAK-IAGEMVSLEAIED 409
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
224-557 |
9.51e-23 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 102.79 E-value: 9.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 224 VDKIKEVRPDIKL---VSFDELLELGQKAKgeIEPHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGV--GGATINVC 298
Cdd:PRK07059 166 VRRVKKMVPAWSLpghVRFNDALAEGARQT--FKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqMEAWLQPA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 299 -DYVGDTDKL--ICFLPLAHIFEMAfelLSFHWGSCIGYANVKTLTSASVRNCKSDLEEFQPTIMVGVaavwETVKKGIL 375
Cdd:PRK07059 244 fEKKPRPDQLnfVCALPLYHIFALT---VCGLLGMRTGGRNILIPNPRDIPGFIKELKKYQVHIFPAV----NTLYNALL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 376 NQinelPRVTKGIFwaayhSKLKMqkmGIPGGDTIGNIIFKKVRKATGghlryllnggspisvnaqefisnliCPMLIGY 455
Cdd:PRK07059 317 NN----PDFDKLDF-----SKLIV---ANGGGMAVQRPVAERWLEMTG-------------------------CPITEGY 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 456 GLTETCASLCIlNPGHfeygvVGDLTGCVTVKL----VDVEE-------LGyfakdNKGEIWVKGENVLPEYYKNEEETK 524
Cdd:PRK07059 360 GLSETSPVATC-NPVD-----ATEFSGTIGLPLpsteVSIRDddgndlpLG-----EPGEICIRGPQVMAGYWNRPDETA 428
|
330 340 350
....*....|....*....|....*....|...
gi 2112360039 525 ESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLV 557
Cdd:PRK07059 429 KVMTADGFFRTGDVGVMDERGYTKIVDRKKDMI 461
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
100-586 |
2.78e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 101.39 E-value: 2.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 100 TFTEVIEVMHSVGRGLVKLGMEPKseDKLHIFAATSHKWMKMFLGAQSQGIPIVTAYDTLGEKGLIHSLKQTSSAAIFTD 179
Cdd:PRK12583 47 TWRQLADAVDRLARGLLALGVQPG--DRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 180 N--------QLLGKLINPLKVAE----------KIRYVIYYDNISAEdkrqGGKLYREAQEAVDKIKevrpdiklvsfDE 241
Cdd:PRK12583 125 DafktsdyhAMLQELLPGLAEGQpgalacerlpELRGVVSLAPAPPP----GFLAWHELQARGETVS-----------RE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 242 LLELGQKAKgeiephppTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGvgGATINVCDYVGDTDKLICFLPLAHIFEMAF 321
Cdd:PRK12583 190 ALAERQASL--------DRDDPINIQYTSGTTGFPKGATLSHHNILNN--GYFVAESLGLTEHDRLCVPVPLYHCFGMVL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 322 -ELLSFHWGSCIGYANvktltsasvrncksdlEEFQPTI-MVGVAAVWETVKKGILNQ-INELPRVTKGIFwaayhsKLK 398
Cdd:PRK12583 260 aNLGCMTVGACLVYPN----------------EAFDPLAtLQAVEEERCTALYGVPTMfIAELDHPQRGNF------DLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 399 MQKMGIPGGDTIGNIIFKKVrkatgghlryllnggspisvnaqefISNLICP-MLIGYGLTETcaslcilNPGHFEYGVV 477
Cdd:PRK12583 318 SLRTGIMAGAPCPIEVMRRV-------------------------MDEMHMAeVQIAYGMTET-------SPVSLQTTAA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 478 GDLTGCVT----------VKLVDVEElGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSL 547
Cdd:PRK12583 366 DDLERRVEtvgrtqphleVKVVDPDG-ATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYV 444
|
490 500 510
....*....|....*....|....*....|....*....
gi 2112360039 548 KIIDRKKNLVkTMNGEYIALEKLESVYRSNSYVQNICVY 586
Cdd:PRK12583 445 RIVGRSKDMI-IRGGENIYPREIEEFLFTHPAVADVQVF 482
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
223-557 |
4.29e-22 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 100.72 E-value: 4.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 223 AVDKIKEVRPDIKL---VSFDELLELGQK---AKGEIEPhpptrDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATin 296
Cdd:PRK08751 169 VVKYVKKLVPEYRIngaIRFREALALGRKhsmPTLQIEP-----DDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAH-- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 297 vcDYVGDTDKL-------ICFLPLAHIFEMAFELLSFhwgSCIGYANVKTLTSASVRNCKSDLEEFQPTIMVGVaavwET 369
Cdd:PRK08751 242 --QWLAGTGKLeegcevvITALPLYHIFALTANGLVF---MKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGV----NT 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 370 VKKGILNqinelprvTKGiFWAAYHSKLKMQkmgIPGGDTIGNIIFKKVRKATGghlryllnggspisvnaqefisnliC 449
Cdd:PRK08751 313 LFNGLLN--------TPG-FDQIDFSSLKMT---LGGGMAVQRSVAERWKQVTG-------------------------L 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 450 PMLIGYGLTETCASLCIlNPGHF-EY-GVVG----DLTGCVTVKLVDVEELGYFakdnkGEIWVKGENVLPEYYKNEEET 523
Cdd:PRK08751 356 TLVEAYGLTETSPAACI-NPLTLkEYnGSIGlpipSTDACIKDDAGTVLAIGEI-----GELCIKGPQVMKGYWKRPEET 429
|
330 340 350
....*....|....*....|....*....|....
gi 2112360039 524 KESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLV 557
Cdd:PRK08751 430 AKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI 463
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
262-587 |
7.85e-22 |
|
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: 98.52 E-value: 7.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 262 DISCIMYTSGSTGDPKGVVLKHSNVV-AGVGGATINVcdyVGDTDKLICFLPLAHIFEMAFELLsfhwgscigyanvktl 340
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLTfAGYYSARRFG---LGEDDVYLTVLPLFHINAQAVSVL---------------- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 341 tsasvrncksdleefqPTIMVGVAAVWetvkkgilnqineLPRVTKGIFWAayhsklKMQKMGIpggdTIGNIIfkkvrk 420
Cdd:cd05934 143 ----------------AALSVGATLVL-------------LPRFSASRFWS------DVRRYGA----TVTNYL------ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 421 atGGHLRYLLNggSPISVN------------------AQEFISNLICPMLIGYGLTETCASLCILNPGHFEYGVVGDLTG 482
Cdd:cd05934 178 --GAMLSYLLA--QPPSPDdrahrlraaygapnppelHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 483 CVTVKLVDVE--ELgyfAKDNKGEIWVKGEN---VLPEYYKNEEETKESLtEDGWFKTGDIGMWTDTGSLKIIDRKKNLV 557
Cdd:cd05934 254 GYEVRIVDDDgqEL---PAGEPGELVIRGLRgwgFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMI 329
|
330 340 350
....*....|....*....|....*....|
gi 2112360039 558 KtMNGEYIALEKLESVYRSNSYVQNICVYA 587
Cdd:cd05934 330 R-RRGENISSAEVERAILRHPAVREAAVVA 358
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
213-557 |
1.58e-21 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 99.26 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 213 GGKLYREAQEAVDKIKEVRPDIKLVSFDELLElGQKAKGEIEPHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVV--AGV 290
Cdd:PRK07529 166 LARYLPGPKRLAVPLIRRKAHARILDFDAELA-RQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVanAWL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 291 GGATInvcdYVGDTDKLICFLPLAHIFE-MAFELLSFHWGscigyANVKTLTSASVRNcksdleefqPTIMvgvAAVWET 369
Cdd:PRK07529 245 GALLL----GLGPGDTVFCGLPLFHVNAlLVTGLAPLARG-----AHVVLATPQGYRG---------PGVI---ANFWKI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 370 VKKgilNQINELPRVTkgifwAAYHSKLKMQkmgiPGGDTIGNiifkkvrkatgghLRYLLNGGSPISVN-AQEFISNLI 448
Cdd:PRK07529 304 VER---YRINFLSGVP-----TVYAALLQVP----VDGHDISS-------------LRYALCGAAPLPVEvFRRFEAATG 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 449 CPMLIGYGLTE-TCASLCilNP--GHFEYGVVG-DLTGCvTVKLVDVEELGYF----AKDNKGEIWVKGENVLPEYYkNE 520
Cdd:PRK07529 359 VRIVEGYGLTEaTCVSSV--NPpdGERRIGSVGlRLPYQ-RVRVVILDDAGRYlrdcAVDEVGVLCIAGPNVFSGYL-EA 434
|
330 340 350
....*....|....*....|....*....|....*..
gi 2112360039 521 EETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLV 557
Cdd:PRK07529 435 AHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLI 471
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
225-640 |
1.86e-21 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 98.76 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 225 DKIKEVRPDIKLVSFDellelgqkakGEIEPHPPTR-DDISCIMYTSGSTGDPKGVVLKHSNVVAGVG---GATINVCDY 300
Cdd:PLN02574 171 SKRIEFPKFYELIKED----------FDFVPKPVIKqDDVAAIMYSSGTTGASKGVVLTHRNLIAMVElfvRFEASQYEY 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 301 VGDTDKLICFLPLAHIFEMAF---ELLSfhwgscigyanvktLTSASVRNCKSDLEEfqptiMVGVAAVWetvkkgilnQ 377
Cdd:PLN02574 241 PGSDNVYLAALPMFHIYGLSLfvvGLLS--------------LGSTIVVMRRFDASD-----MVKVIDRF---------K 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 378 INELPrVTKGIFWAAYHSKlkmqkmgipggdtigniifKKVRKATGGHLRYLLNGGSPISVNA-QEFISNLICPMLI-GY 455
Cdd:PLN02574 293 VTHFP-VVPPILMALTKKA-------------------KGVCGEVLKSLKQVSCGAAPLSGKFiQDFVQTLPHVDFIqGY 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 456 GLTETCA-SLCILNPGHFE-YGVVGDLTGCVTVKLVDVEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTEDGWF 533
Cdd:PLN02574 353 GMTESTAvGTRGFNTEKLSkYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWL 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 534 KTGDIGMWTDTGSLKIIDRKKNLVKtMNGEYIALEKLESVYRSNSYVQNICVYADQNKVK---PVGIIVpnHTPLVKLAK 610
Cdd:PLN02574 433 RTGDIAYFDEDGYLYIVDRLKEIIK-YKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECgeiPVAFVV--RRQGSTLSQ 509
|
410 420 430
....*....|....*....|....*....|
gi 2112360039 611 ElGIMKKQETDIEPYlhnKKLQNAVFEDMI 640
Cdd:PLN02574 510 E-AVINYVAKQVAPY---KKVRKVVFVQSI 535
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
261-586 |
3.71e-21 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 95.42 E-value: 3.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 261 DDISCIMYTSGSTGDPKGVVLKHSNVVAGvggaTINVCDYVGDT--DKLICFLPLAHIFEMAFELLSF--HWGSCI---- 332
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNN----GYFIGERLGLTeqDRLCIPVPLFHCFGSVLGVLACltHGATMVfpsp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 333 GYANVKTLTSasvrncksdLEEFQPTIMVGVAAVWetvkkgilnqINELPRVTKGIFwaayhsKLKMQKMGIPGGDTIGN 412
Cdd:cd05917 78 SFDPLAVLEA---------IEKEKCTALHGVPTMF----------IAELEHPDFDKF------DLSSLRTGIMAGAPCPP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 413 IIFKKVRKAtgghlryllnggspisVNAQEfisnlicpMLIGYGLTETCA-SLCILNPGHFE--YGVVGDLTGCVTVKLV 489
Cdd:cd05917 133 ELMKRVIEV----------------MNMKD--------VTIAYGMTETSPvSTQTRTDDSIEkrVNTVGRIMPHTEAKIV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 490 DVEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVkTMNGEYIALEK 569
Cdd:cd05917 189 DPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGENIYPRE 267
|
330
....*....|....*..
gi 2112360039 570 LESVYRSNSYVQNICVY 586
Cdd:cd05917 268 IEEFLHTHPKVSDVQVV 284
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
237-640 |
7.19e-21 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 96.97 E-value: 7.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 237 VSFDELLELGQKAKGEIEPHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINV-CDYVGDTDKLiCFLPLAH 315
Cdd:PLN02330 160 VNWKELLEAADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVgPEMIGQVVTL-GLIPFFH 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 316 IFEMAfellsfhwGSCigYANVKTLTSASVRNcKSDLEEFQPTIMVGVAAVWETVKKGILNQINElPRVTKGIFwaayhS 395
Cdd:PLN02330 239 IYGIT--------GIC--CATLRNKGKVVVMS-RFELRTFLNALITQEVSFAPIVPPIILNLVKN-PIVEEFDL-----S 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 396 KLKMQKMGIPGGDTIGNIIFKKVRKATGghlryllnggspisVNAQEfisnlicpmliGYGLTE-TCASLCILNP--GH- 471
Cdd:PLN02330 302 KLKLQAIMTAAAPLAPELLTAFEAKFPG--------------VQVQE-----------AYGLTEhSCITLTHGDPekGHg 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 472 -FEYGVVGDLTGCVTVKLVDVEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKII 550
Cdd:PLN02330 357 iAKKNSVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIV 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 551 DRKKNLVKtMNGEYIALEKLESVYRSNSYVQNICVYA---DQNKVKPVGIIVPNhtplvKLAKElgimkkQETDIEPYL- 626
Cdd:PLN02330 437 DRIKELIK-YKGFQVAPAELEAILLTHPSVEDAAVVPlpdEEAGEIPAACVVIN-----PKAKE------SEEDILNFVa 504
|
410
....*....|....*...
gi 2112360039 627 ----HNKKLQNAVFEDMI 640
Cdd:PLN02330 505 anvaHYKKVRVVQFVDSI 522
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
172-576 |
1.23e-20 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 95.58 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 172 SSAAIFTDNQLLGKL---INPLKVAEKIRYVIYYdnisaedkrQGGKLYREAQEAVDKIKEVRP----DIKLVSFDELLE 244
Cdd:cd05922 34 LSFAVAYAGGRLGLVfvpLNPTLKESVLRYLVAD---------AGGRIVLADAGAADRLRDALPaspdPGTVLDADGIRA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 245 LGQKAKGeiepHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGvGGATINVCDYVGDtDKLICFLPLAHIFEMAFELL 324
Cdd:cd05922 105 ARASAPA----HEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLAN-ARSIAEYLGITAD-DRALTVLPLSYDYGLSVLNT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 325 SFHWGSCIGYANVKTLTSASVRNCKsdleEFQPTIMVGVAAVWEtvkkgILnqinelprvtkgifwaayhSKLKMQKMGI 404
Cdd:cd05922 179 HLLRGATLVLTNDGVLDDAFWEDLR----EHGATGLAGVPSTYA-----ML-------------------TRLGFDPAKL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 405 PggdtigniifkkvrkatggHLRYLLNGGSPISvnaQEFISNLiCPMLIG------YGLTETCASLCILNPG--HFEYGV 476
Cdd:cd05922 231 P-------------------SLRYLTQAGGRLP---QETIARL-RELLPGaqvyvmYGQTEATRRMTYLPPEriLEKPGS 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 477 VG-DLTGCvtvKLVDVEELGYFAKDNK-GEIWVKGENVLPEYYKNE-EETKESLTEDGwFKTGDIGMWTDTGSLKIIDRK 553
Cdd:cd05922 288 IGlAIPGG---EFEILDDDGTPTPPGEpGEIVHRGPNVMKGYWNDPpYRRKEGRGGGV-LHTGDLARRDEDGFLFIVGRR 363
|
410 420
....*....|....*....|...
gi 2112360039 554 KNLVKTMnGEYIALEKLESVYRS 576
Cdd:cd05922 364 DRMIKLF-GNRISPTEIEAAARS 385
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
261-585 |
1.91e-20 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 94.47 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 261 DDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGAtinVCDYVGD-TDKLICFLPLAHIfemafellsfhwgscigyanvkt 339
Cdd:cd05935 84 DDLALIPYTSGTTGLPKGCMHTHFSAAANALQS---AVWTGLTpSDVILACLPLFHV----------------------- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 340 ltsasvrncksdlEEFQPTIMVGVAAVWETVKKGILNQ--INELPRVTKGIFWAAYHSKLKmqkmgipggDTIGNIIFKK 417
Cdd:cd05935 138 -------------TGFVGSLNTAVYVGGTYVLMARWDRetALELIEKYKVTFWTNIPTMLV---------DLLATPEFKT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 418 VRKATgghLRYLLNGGSPISVNAQEFISNLI-CPMLIGYGLTETCASLCILNPGHFEYGVVGDLTGCVTVKLVDVEELGY 496
Cdd:cd05935 196 RDLSS---LKVLTGGGAPMPPAVAEKLLKLTgLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 497 FAKDNKGEIWVKGENVLPEYYKNEEETKESLTEDG---WFKTGDIGMWTDTGSLKIIDRKKNLVKtMNGEYIALEKLESV 573
Cdd:cd05935 273 LPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMIN-VSGFKVWPAEVEAK 351
|
330
....*....|..
gi 2112360039 574 YRSNSYVQNICV 585
Cdd:cd05935 352 LYKHPAI*EVCV 363
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
219-557 |
2.53e-20 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 94.94 E-value: 2.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 219 EAQEAVDKIKEVRPDIKLVSFDE-----LLELGQKAKGEIEPHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGvgGA 293
Cdd:PRK07514 109 ANFAWLSKIAAAAGAPHVETLDAdgtgsLLEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSN--AL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 294 TINVCDYVGDTDKLICFLPLahifemafellsFHwgscigyanVKTLTSASvrNCksdleefqpTIMVGVAAVWetVKKG 373
Cdd:PRK07514 187 TLVDYWRFTPDDVLIHALPI------------FH---------THGLFVAT--NV---------ALLAGASMIF--LPKF 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 374 ILNQ-INELPRVTkgIFwaayhsklkmqkMGIPggdTIgniifkKVR--------KATGGHLRYLLNGGSPISVNA-QEF 443
Cdd:PRK07514 233 DPDAvLALMPRAT--VM------------MGVP---TF------YTRllqeprltREAAAHMRLFISGSAPLLAEThREF 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 444 ISNLICPMLIGYGLTETCASlcILNPGHFEY--GVVG-DLTGcVTVKLVDVEELGYFAKDNKGEIWVKGENVLPEYYKNE 520
Cdd:PRK07514 290 QERTGHAILERYGMTETNMN--TSNPYDGERraGTVGfPLPG-VSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMP 366
|
330 340 350
....*....|....*....|....*....|....*..
gi 2112360039 521 EETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLV 557
Cdd:PRK07514 367 EKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDLI 403
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
266-606 |
4.61e-20 |
|
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: 91.62 E-value: 4.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 266 IMYTSGSTGDPKGVVLKHSNVVAGVGGATINVcdYVGDTDKLICFLPLahifemafellsFHWGsciGYANVktltsasV 345
Cdd:cd17630 5 VILTSGSTGTPKAVVHTAANLLASAAGLHSRL--GFGGGDSWLLSLPL------------YHVG---GLAIL-------V 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 346 RNcksdleefqptimvgVAAVWETVkkgilnqineLPRVTkgifWAAYHSKLkmqkmgiPGGDT--------IGNIIFKK 417
Cdd:cd17630 61 RS---------------LLAGAELV----------LLERN----QALAEDLA-------PPGVThvslvptqLQRLLDSG 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 418 VRKATGGHLRYLLNGGSPISVNAQEFISNLICPMLIGYGLTETCASLCILNPGHFEYGVVGDLTGCVTVKLVDveelgyf 497
Cdd:cd17630 105 QGPAALKSLRAVLLGGAPIPPELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 498 akdnKGEIWVKGENVLPEYYKNEEEtkESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKTmNGEYIALEKLESVYRSN 577
Cdd:cd17630 178 ----DGEIWVGGASLAMGYLRGQLV--PEFNEDGWFTTKDLGELHADGRLTVLGRADNMIIS-GGENIQPEEIEAALAAH 250
|
330 340 350
....*....|....*....|....*....|..
gi 2112360039 578 SYVQNICVYADQNKV---KPVGIIVPNHTPLV 606
Cdd:cd17630 251 PAVRDAFVVGVPDEElgqRPVAVIVGRGPADP 282
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
256-587 |
1.04e-19 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 92.44 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 256 HPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAgvggatiNVCDY-----VGDTDKLICFLPLAHIfemafellsfhwgs 330
Cdd:cd05903 88 PAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSA-------SIRQYaerlgLGPGDVFLVASPMAHQ-------------- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 331 cIGYanVKTLTSASVRNCKSDLEEfqptimvgvaaVWETVKkgILNQINElPRVTkgIFWAAyhsklkmqkmgIPGGDTI 410
Cdd:cd05903 147 -TGF--VYGFTLPLLLGAPVVLQD-----------IWDPDK--ALALMRE-HGVT--FMMGA-----------TPFLTDL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 411 GNIIFKKVRKATggHLRYLLNGGSPISVN----AQEFISNLICPMligYGLTETCASLCILNPGHFEYGVVGDltGC--- 483
Cdd:cd05903 197 LNAVEEAGEPLS--RLRTFVCGGATVPRSlarrAAELLGAKVCSA---YGSTECPGAVTSITPAPEDRRLYTD--GRplp 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 484 -VTVKLVDvEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLtEDGWFKTGDIGMWTDTGSLKIIDRKKNLVkTMNG 562
Cdd:cd05903 270 gVEIKVVD-DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAA-PEGWFRTGDLARLDEDGYLRITGRSKDII-IRGG 346
|
330 340
....*....|....*....|....*
gi 2112360039 563 EYIALEKLESVYRSNSYVQNICVYA 587
Cdd:cd05903 347 ENIPVLEVEDLLLGHPGVIEAAVVA 371
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
262-587 |
1.11e-19 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 90.78 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 262 DISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVCDYVGDtDKLICFLPLAHIFEMAFELLS-FHWGSCIGYANVKTL 340
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVG-DVTYLPLPATHIGGLWWILTClIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 341 TSASvrnckSDLEEFQPTIMVGVAAVWETVKKGILNQINELPRvtkgifwaayhsklkmqkmgipggdtigniifkkvrk 420
Cdd:cd17635 81 KSLF-----KILTTNAVTTTCLVPTLLSKLVSELKSANATVPS------------------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 421 atgghLRYLLNGGS-PISVNAQEFISNLICPMLIGYGLTETCASLCI-LNPGHFEYGVVGDLTGCVTVKLVDVEELGYfA 498
Cdd:cd17635 119 -----LRLIGYGGSrAIAADVRFIEATGLTNTAQVYGLSETGTALCLpTDDDSIEINAVGRPYPGVDVYLAATDGIAG-P 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 499 KDNKGEIWVKGENVLPEYYKNEEETKESLTeDGWFKTGDIGMWTDTGSLKIIDRKKNLVkTMNGEYIALEKLESVYRSNS 578
Cdd:cd17635 193 SASFGTIWIKSPANMLGYWNNPERTAEVLI-DGWVNTGDLGERREDGFLFITGRSSESI-NCGGVKIAPDEVERIAEGVS 270
|
....*....
gi 2112360039 579 YVQNICVYA 587
Cdd:cd17635 271 GVQECACYE 279
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
254-600 |
1.23e-19 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 93.03 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 254 EPHPPT------RDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGatINVCDYVGDTDKLICFLPLAHIFEMAFELLSfh 327
Cdd:PRK05852 163 EPTPATstpeglRPDDAMIMFTGGTTGLPKMVPWTHANIASSVRA--IITGYRLSPRDATVAVMPLYHGHGLIAALLA-- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 328 wgscigyanvkTLTSASVrncksdleefqptimvgvaavwetvkkgILnqineLP---RVTKGIFWAAYHSKLKMQKMGI 404
Cdd:PRK05852 239 -----------TLASGGA----------------------------VL-----LPargRFSAHTFWDDIKAVGATWYTAV 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 405 PggdTIGNIIFKKVRKATGGH----LRYLLNGGSPISV-NAQEFISNLICPMLIGYGLTET---CASLCILNPGHFE--- 473
Cdd:PRK05852 275 P---TIHQILLERAATEPSGRkpaaLRFIRSCSAPLTAeTAQALQTEFAAPVVCAFGMTEAthqVTTTQIEGIGQTEnpv 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 474 --YGVVGDLTGcVTVKLV--DVEELGyfaKDNKGEIWVKGENVLPEYYKNEEETKESLTeDGWFKTGDIGMWTDTGSLKI 549
Cdd:PRK05852 352 vsTGLVGRSTG-AQIRIVgsDGLPLP---AGAVGEVWLRGTTVVRGYLGDPTITAANFT-DGWLRTGDLGSLSAAGDLSI 426
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2112360039 550 IDRKKNLVKTmNGEYIALEKLESVYRSNSYVQNICVYADQNKV--KPVG-IIVP 600
Cdd:PRK05852 427 RGRIKELINR-GGEKISPERVEGVLASHPNVMEAAVFGVPDQLygEAVAaVIVP 479
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
215-590 |
4.38e-19 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 91.07 E-value: 4.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 215 KLYREAQEAVDKIKEVRPDIKLVSFDELLElgqkaKGEIEPHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGAT 294
Cdd:PRK06839 108 KTFQNMALSMQKVSYVQRVISITSLKEIED-----RKIDNFVEKNESASFIICYTSGTTGKPKGAVLTQENMFWNALNNT 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 295 INVcDYVGDtDKLICFLPLAHIfemafellsfhwgSCIGYANVKTLTSASVRNCKsdlEEFQPTIMVgvaavwetvkkgi 374
Cdd:PRK06839 183 FAI-DLTMH-DRSIVLLPLFHI-------------GGIGLFAFPTLFAGGVIIVP---RKFEPTKAL------------- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 375 lnQINELPRVTKgifwaayhsklkmqKMGIPggdTIGNIIFKKVRKATGG--HLRYLLNGGSPISVN-AQEFISNLIcPM 451
Cdd:PRK06839 232 --SMIEKHKVTV--------------VMGVP---TIHQALINCSKFETTNlqSVRWFYNGGAPCPEElMREFIDRGF-LF 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 452 LIGYGLTETCASLCILNPGHF--EYGVVGDLTGCVTVKLVDvEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLtE 529
Cdd:PRK06839 292 GQGFGMTETSPTVFMLSEEDArrKVGSIGKPVLFCDYELID-ENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI-Q 369
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2112360039 530 DGWFKTGDIGMWTDTGSLKIIDRKKNLVKTmNGEYIALEKLESVYRSNSYVQNICVYADQN 590
Cdd:PRK06839 370 DGWLCTGDLARVDEDGFVYIVGRKKEMIIS-GGENIYPLEVEQVINKLSDVYEVAVVGRQH 429
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
262-556 |
5.21e-19 |
|
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: 88.71 E-value: 5.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 262 DISCIMYTSGSTGDPKGVVLKHSNVVagvgGATINVCDYVGDT--DKLICFLPLAHIFemafellsfhwgsciGYAN--- 336
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTL----RAAAAWADCADLTedDRYLIINPFFHTF---------------GYKAgiv 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 337 VKTLTSASVrncksdleefQPTIMVGVAAVWETVKKgilNQINELPRVTkgifwAAYHSKLkmqkmGIPGgdtigniifk 416
Cdd:cd17638 62 ACLLTGATV----------VPVAVFDVDAILEAIER---ERITVLPGPP-----TLFQSLL-----DHPG---------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 417 kVRKATGGHLRYLLNGGSPISVNAQEFI-SNL-ICPMLIGYGLTET-CASLCilNPGHFEYGV---VGDLTGCVTVKLVD 490
Cdd:cd17638 109 -RKKFDLSSLRAAVTGAATVPVELVRRMrSELgFETVLTAYGLTEAgVATMC--RPGDDAETVattCGRACPGFEVRIAD 185
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2112360039 491 veelgyfakdnKGEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNL 556
Cdd:cd17638 186 -----------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDM 240
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
223-599 |
7.00e-19 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 90.42 E-value: 7.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 223 AVDKIKEV--RPDIKLV----------SFDELLELGQKAKGEIEPHPptrDDISCIMYTSGSTGDPKGVVLKHSNVVAGV 290
Cdd:PLN02246 132 YVDKLKGLaeDDGVTVVtiddppegclHFSELTQADENELPEVEISP---DDVVALPYSSGTTGLPKGVMLTHKGLVTSV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 291 G----GATINVcdYVGDTDKLICFLPLAHIFEMAFELL-SFHWGSCI----GYANVKTLtsASVRNCKSDLEEFQPTIMV 361
Cdd:PLN02246 209 AqqvdGENPNL--YFHSDDVILCVLPMFHIYSLNSVLLcGLRVGAAIlimpKFEIGALL--ELIQRHKVTIAPFVPPIVL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 362 GVAavwetvkkgilnqinELPRVTKgifwaayhSKLKMQKMGIPGGDTIGniifKKVRKATGGHLryllnggsPISVNAQ 441
Cdd:PLN02246 285 AIA---------------KSPVVEK--------YDLSSIRMVLSGAAPLG----KELEDAFRAKL--------PNAVLGQ 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 442 efisnlicpmliGYGLTE--TCASLCIL---NPGHFEYGVVGDLTGCVTVKLVDVE---ELGYfakdNK-GEIWVKGENV 512
Cdd:PLN02246 330 ------------GYGMTEagPVLAMCLAfakEPFPVKSGSCGTVVRNAELKIVDPEtgaSLPR----NQpGEICIRGPQI 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 513 LPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKtMNGEYIALEKLESVYRSNSYVQNICVYADQNKV 592
Cdd:PLN02246 394 MKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIK-YKGFQVAPAELEALLISHPSIADAAVVPMKDEV 472
|
410
....*....|
gi 2112360039 593 K---PVGIIV 599
Cdd:PLN02246 473 AgevPVAFVV 482
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
229-585 |
2.17e-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: 88.09 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 229 EVRPDIKLVSFDELLELGQKAKGEIEPHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGAtiNVCDYVGDTDKLI 308
Cdd:TIGR01733 88 GLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWL--ARRYGLDPDDRVL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 309 CFLPLAH---IFEMafellsfhWGSCIGYANVKTLTSASVRNCKSDL----EEFQPTIMVGVAAVWETVKKGILNQINEL 381
Cdd:TIGR01733 166 QFASLSFdasVEEI--------FGALLAGATLVVPPEDEERDDAALLaaliAEHPVTVLNLTPSLLALLAAALPPALASL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 382 PRVtkgifwaayhsklkmqkmgIPGGDTIGNIIFKKVRKATGGhlRYLLNGGSP----ISVNAQEF---ISNLICPMLIG 454
Cdd:TIGR01733 238 RLV-------------------ILGGEALTPALVDRWRARGPG--ARLINLYGPtettVWSTATLVdpdDAPRESPVPIG 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 455 YGLteTCASLCILNPGHfeygvvgdltgcvtvKLVDVEELgyfakdnkGEIWVKGENVLPEYYKNEEETKESLTEDG--- 531
Cdd:TIGR01733 297 RPL--ANTRLYVLDDDL---------------RPVPVGVV--------GELYIGGPGVARGYLNRPELTAERFVPDPfag 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2112360039 532 -----WFKTGDIGMWTDTGSLKIIDRKKNLVKtMNGEYIALEKLESVYRSNSYVQNICV 585
Cdd:TIGR01733 352 gdgarLYRTGDLVRYLPDGNLEFLGRIDDQVK-IRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
261-557 |
1.06e-17 |
|
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: 86.77 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 261 DDISCIMYTSGSTGDPKGVVLKHSNVVAgvggatiNVCDYVGDT-----DKLICFLPLAHifEMAfeLLSFHWgSCIgYA 335
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHENLVH-------NMFAILNSTewktkDRILSWMPLTH--DMG--LIAFHL-APL-IA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 336 NVKTLtsasvrncksdleeFQPTIMVgvaavwetvkkgILNQINELPRVTKgifwaayhsklkmQKMGIPGGDTIGNIIF 415
Cdd:cd05908 173 GMNQY--------------LMPTRLF------------IRRPILWLKKASE-------------HKATIVSSPNFGYKYF 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 416 KKVRKATG------GHLRYLLNGGSPISVN-AQEFISNLIC------PMLIGYGLTETCASLCILNPG-HFEYGVVGD-- 479
Cdd:cd05908 214 LKTLKPEKandwdlSSIRMILNGAEPIDYElCHEFLDHMSKyglkrnAILPVYGLAEASVGASLPKAQsPFKTITLGRrh 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 480 LTGCVTVKLVDVE--------ELGY---------FAKDNK-------GEIWVKGENVLPEYYKNEEETKESLTEDGWFKT 535
Cdd:cd05908 294 VTHGEPEPEVDKKdsecltfvEVGKpidetdiriCDEDNKilpdgyiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKT 373
|
330 340
....*....|....*....|..
gi 2112360039 536 GDIGMWTDtGSLKIIDRKKNLV 557
Cdd:cd05908 374 GDLGFIRN-GRLVITGREKDII 394
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
261-573 |
9.27e-17 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 84.08 E-value: 9.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 261 DDISCIMYTSGSTGDPKGVVLKHSNVVAGvGGATINVCDYvGDTDKLICFLPLAHIFEMAFELLSFHWGSC---IGYANV 337
Cdd:PLN02860 172 DDAVLICFTSGTTGRPKGVTISHSALIVQ-SLAKIAIVGY-GEDDVYLHTAPLCHIGGLSSALAMLMVGAChvlLPKFDA 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 338 KTLTSAsvrncksdLEEFQPTIMVGVAAvwetvkkgILNQINELPRVTKGifWAAYHSklkmqkmgipggdtigniifkk 417
Cdd:PLN02860 250 KAALQA--------IKQHNVTSMITVPA--------MMADLISLTRKSMT--WKVFPS---------------------- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 418 VRKatgghlryLLNGGSPISVNAQEFISNLI--CPMLIGYGLTETCASLCIL---------------NPGHFEYGVVGDL 480
Cdd:PLN02860 290 VRK--------ILNGGGSLSSRLLPDAKKLFpnAKLFSAYGMTEACSSLTFMtlhdptlespkqtlqTVNQTKSSSVHQP 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 481 TG-CVTVKLVDVE-ELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVK 558
Cdd:PLN02860 362 QGvCVGKPAPHVElKIGLDESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIK 441
|
330
....*....|....*
gi 2112360039 559 TmNGEYIALEKLESV 573
Cdd:PLN02860 442 T-GGENVYPEEVEAV 455
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
100-559 |
1.10e-16 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 83.68 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 100 TFTEVIEVMHSVGRGLVKLGmePKSEDKLHIFAATSHKWMKMFLGAQSQGIPIVTAYDTLGEKGLIHSLKQTSSAAIFTD 179
Cdd:TIGR03098 27 TYAALSERVLALASGLRGLG--LARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 180 NQLLGKLINPLKVAEKIRYVIYYDnisaedkrqggklyreaqeAVDKIKEVRPDIKLVSFDELLELGqkakGEIEPHPPT 259
Cdd:TIGR03098 105 SERLDLLHPALPGCHDLRTLIIVG-------------------DPAHASEGHPGEEPASWPKLLALG----DADPPHPVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 260 RDDISCIMYTSGSTGDPKGVVLKHSNVVAGvggaTINVCDYVGDT--DKLICFLPLAhiFEMAFELL--SFHWGscigyA 335
Cdd:TIGR03098 162 DSDMAAILYTSGSTGRPKGVVLSHRNLVAG----AQSVATYLENRpdDRLLAVLPLS--FDYGFNQLttAFYVG-----A 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 336 NVKTLTSASVRNCKSDLEEFQPTIMVGVAAVWetvkkgilnqinelprvtkgifwaayhskLKMQKMGIPGGDTigniif 415
Cdd:TIGR03098 231 TVVLHDYLLPRDVLKALEKHGITGLAAVPPLW-----------------------------AQLAQLDWPESAA------ 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 416 kkvrkatgGHLRYLLNGG---SPISVNA-QEFISNL-ICPMligYGLTETCASlCILNPGHFEY--GVVGDLTGCVTVkL 488
Cdd:TIGR03098 276 --------PSLRYLTNSGgamPRATLSRlRSFLPNArLFLM---YGLTEAFRS-TYLPPEEVDRrpDSIGKAIPNAEV-L 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 489 VDVEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKE------------SLTEDGWFkTGDIGMWTDTGSLKIIDRKKNL 556
Cdd:TIGR03098 343 VLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAErfrplppfpgelHLPELAVW-SGDTVRRDEEGFLYFVGRRDEM 421
|
...
gi 2112360039 557 VKT 559
Cdd:TIGR03098 422 IKT 424
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
254-556 |
1.17e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 83.32 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 254 EPHPPTRddISCIMYTSGSTGDPKGVVLKHSNVVAgvggATIN--VCDYVGDTDKLICFLPLAHIfemafellsfhwgsc 331
Cdd:PRK09088 130 PSIPPER--VSLILFTSGTSGQPKGVMLSERNLQQ----TAHNfgVLGRVDAHSSFLCDAPMFHI--------------- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 332 IGYANvktltsaSVRncksdleefqPTIMVGVAavwetvkkgILnqinelprVTKGIFWAAYHSKLKMQKMGI------- 404
Cdd:PRK09088 189 IGLIT-------SVR----------PVLAVGGS---------IL--------VSNGFEPKRTLGRLGDPALGIthyfcvp 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 405 ---------PGGDTigniifkkvrkATGGHLRYLLNGGSPisvNAQEFISNLI---CPMLIGYGLTETCASLCI-LNPGH 471
Cdd:PRK09088 235 qmaqafraqPGFDA-----------AALRHLTALFTGGAP---HAAEDILGWLddgIPMVDGFGMSEAGTVFGMsVDCDV 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 472 F--EYGVVGDLTGCVTVKLVDVEELGYFAKDnKGEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKI 549
Cdd:PRK09088 301 IraKAGAAGIPTPTVQTRVVDDQGNDCPAGV-PGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWV 379
|
....*..
gi 2112360039 550 IDRKKNL 556
Cdd:PRK09088 380 VDRKKDM 386
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
261-557 |
1.25e-16 |
|
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: 82.14 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 261 DDISCIMYTSGSTGDPKGVVLKHSNVV--AGVGGAtinVCDYvGDTDKLICFLPLAHIFEMAFELLS-FH------WGSC 331
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVynAWMLAL---NSLF-DPDDVLLCGLPLFHVNGSVVTLLTpLAsgahvvLAGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 332 IGYANvktltSASVRNCKSDLEEFQPTIMVGVAAVWETVkkgilnqinelprvtkgifwaayhsklkmqkMGIPGGDTIG 411
Cdd:cd05944 78 AGYRN-----PGLFDNFWKLVERYRITSLSTVPTVYAAL-------------------------------LQVPVNADIS 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 412 NiifkkvrkatgghLRYLLNGGSPISVNA-QEFISNLICPMLIGYGLTE-TCASLCILNPGHFEYGVVGDLTGCVTVKLV 489
Cdd:cd05944 122 S-------------LRFAMSGAAPLPVELrARFEDATGLPVVEGYGLTEaTCLVAVNPPDGPKRPGSVGLRLPYARVRIK 188
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2112360039 490 DVEELGYF----AKDNKGEIWVKGENVLPEYYkNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLV 557
Cdd:cd05944 189 VLDGVGRLlrdcAPDEVGEICVAGPGVFGGYL-YTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI 259
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
237-585 |
1.32e-16 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 83.19 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 237 VSFDELLelgQKAKGEIEPHPP-TRDDISCIMYTSGSTGDPKGVVLKHSNVV-AGVGGATINVcdyVGDTDKLICFLPLA 314
Cdd:PRK08008 151 SSFTQLK---AQQPATLCYAPPlSTDDTAEILFTSGTTSRPKGVVITHYNLRfAGYYSAWQCA---LRDDDVYLTVMPAF 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 315 HI-FEMAFELLSFHWGSCI----GYanvktltSAS-----VRNCKSDLEEFQP----TIMVGVAAVWEtvKKGILNQIne 380
Cdd:PRK08008 225 HIdCQCTAAMAAFSAGATFvlleKY-------SARafwgqVCKYRATITECIPmmirTLMVQPPSAND--RQHCLREV-- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 381 lprvtkgifwaayhsklkmqkmgipggdtigniifkkvrkatgghLRYLlnggsPISVNAQE-FISNLICPMLIGYGLTE 459
Cdd:PRK08008 294 ---------------------------------------------MFYL-----NLSDQEKDaFEERFGVRLLTSYGMTE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 460 TCAslcilnpghfeyGVVGDLTG-------------CVTVKLVDvEELGYFAKDNKGEIWVKGE---NVLPEYYKNEEET 523
Cdd:PRK08008 324 TIV------------GIIGDRPGdkrrwpsigrpgfCYEAEIRD-DHNRPLPAGEIGEICIKGVpgkTIFKEYYLDPKAT 390
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2112360039 524 KESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKTmNGEYIALEKLESVYRSNSYVQNICV 585
Cdd:PRK08008 391 AKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKR-GGENVSCVELENIIATHPKIQDIVV 451
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
142-552 |
3.96e-16 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 82.08 E-value: 3.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 142 FLGAQSQGIPIVTAYDTLGEKGLIHSLKQTSSAAIFTDNQLL--GKLINP-------LKVAEKIRYVIYYDNISAEDKRQ 212
Cdd:COG0365 81 MLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLrgGKVIDLkekvdeaLEELPSLEHVIVVGRTGADVPME 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 213 GGklyreaqeavdkikevrpdiklVSFDELLElgqKAKGEIEPHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGG 292
Cdd:COG0365 161 GD----------------------LDWDELLA---AASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAAT 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 293 ATINVCDyVGDTDKLICFLPLAHIFemafellsFHWGSCIG----------------YANVKTLTSAsvrncksdLEEFQ 356
Cdd:COG0365 216 TAKYVLD-LKPGDVFWCTADIGWAT--------GHSYIVYGpllngatvvlyegrpdFPDPGRLWEL--------IEKYG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 357 PTIMVGVAAVWETVKKgilnqinelprvtKGIFWAAYHSkLKmqkmgipggdtigniifkkvrkatggHLRYLLNGGSPI 436
Cdd:COG0365 279 VTVFFTAPTAIRALMK-------------AGDEPLKKYD-LS--------------------------SLRLLGSAGEPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 437 SVNAQEFISNLI-CPMLIGYGLTETCASLCILNPGhfeygvvGDL----TGC----VTVKLVDveELGYFAKDN-KGEIW 506
Cdd:COG0365 319 NPEVWEWWYEAVgVPIVDGWGQTETGGIFISNLPG-------LPVkpgsMGKpvpgYDVAVVD--EDGNPVPPGeEGELV 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2112360039 507 VKGEN--VLPEYYKNEEETKESL--TEDGWFKTGDIGMWTDTGSLKIIDR 552
Cdd:COG0365 390 IKGPWpgMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGR 439
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
254-556 |
4.52e-16 |
|
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: 81.90 E-value: 4.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 254 EPHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVggATINVCDYVGDTDKLICFLPLAHIFEMAFELLSFHWGsciG 333
Cdd:cd05931 142 PPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANV--RQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYS---G 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 334 YANVKTLTSASVRNCKSDLE---EFQPTIMVGvaavwetvkkgilnqinelPRvtkgiFwaAYhsklkmqkmgipggdti 410
Cdd:cd05931 217 GPSVLMSPAAFLRRPLRWLRlisRYRATISAA-------------------PN-----F--AY----------------- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 411 gNIIFKKVRKATG-----GHLRYLLNGGSPISVNA-QEFI-----SNL----ICPmliGYGLTETC--ASLCILNPG--- 470
Cdd:cd05931 254 -DLCVRRVRDEDLegldlSSWRVALNGAEPVRPATlRRFAeafapFGFrpeaFRP---SYGLAEATlfVSGGPPGTGpvv 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 471 ------HFEYGVVG---------DLTGC------VTVKLVDVEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKE---- 525
Cdd:cd05931 330 lrvdrdALAGRAVAvaaddpaarELVSCgrplpdQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAEtfga 409
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2112360039 526 --SLTEDGWFKTGDIGMWTD-----TGSLK--IIDRKKNL 556
Cdd:cd05931 410 laATDEGGWLRTGDLGFLHDgelyiTGRLKdlIIVRGRNH 449
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
158-571 |
5.83e-16 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 82.28 E-value: 5.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 158 TLGEKGLIHSLKQTSSAAIFTDNQLLGKLIN---PLKVAEKIRyVIYYDNIsaedkrqggklyREAQEAVDKIKEVRPDI 234
Cdd:PRK08633 698 TASEAALKSAIEQAQIKTVITSRKFLEKLKNkgfDLELPENVK-VIYLEDL------------KAKISKVDKLTALLAAR 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 235 KLVSFdeLLELgqkakgeIEPHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVCdyVGDTDKLICFLPLA 314
Cdd:PRK08633 765 LLPAR--LLKR-------LYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFN--LRNDDVILSSLPFF 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 315 HifemAFELLSFHWGS-CIGYANVktltsasvrnCKSDleefqPTIMVGVAAVWETVKKGILnqinelprVTKGIFWAAY 393
Cdd:PRK08633 834 H----SFGLTVTLWLPlLEGIKVV----------YHPD-----PTDALGIAKLVAKHRATIL--------LGTPTFLRLY 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 394 hsklkmqkmgipggdtignIIFKKVRKATGGHLRYLLNGGS--PISVnAQEFISNLICPMLIGYGLTETCASLCILNPGH 471
Cdd:PRK08633 887 -------------------LRNKKLHPLMFASLRLVVAGAEklKPEV-ADAFEEKFGIRILEGYGATETSPVASVNLPDV 946
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 472 FEYGV----------VG-DLTGcVTVKLVDVEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTE---DGWFKTGD 537
Cdd:PRK08633 947 LAADFkrqtgskegsVGmPLPG-VAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIKDidgIGWYVTGD 1025
|
410 420 430
....*....|....*....|....*....|....
gi 2112360039 538 IGMWTDTGSLKIIDRKKNLVKtMNGEYIALEKLE 571
Cdd:PRK08633 1026 KGHLDEDGFLTITDRYSRFAK-IGGEMVPLGAVE 1058
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
100-683 |
1.14e-15 |
|
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: 80.49 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 100 TFTEVIEVMHSVGRGLVKLGMEPksEDKLHIFAATSHKWMKMFLGAQSQGI-PIVTAYDTLGEKgLIHSLKQTSSAAIFT 178
Cdd:cd05959 31 TYAELEAEARRVAGALRALGVKR--EERVLLIMLDTVDFPTAFLGAIRAGIvPVPVNTLLTPDD-YAYYLEDSRARVVVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 179 DNQLLGKLINPLKVAEKIRYVIyydnISAEDKRqggklyreaqeavdkikevrPDIKLVSFDELLELGQkakGEIEPHPP 258
Cdd:cd05959 108 SGELAPVLAAALTKSEHTLVVL----IVSGGAG--------------------PEAGALLLAELVAAEA---EQLKPAAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 259 TRDDISCIMYTSGSTGDPKGVVLKHSNVVAgvggatinVCD-YVGDTDKL----ICF----------LPLAHIFEMAFEl 323
Cdd:cd05959 161 HADDPAFWLYSSGSTGRPKGVVHLHADIYW--------TAElYARNVLGIreddVCFsaaklffaygLGNSLTFPLSVG- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 324 lsfhwGSCIGYANVKTLTSASVRncksdLEEFQPTIMVGVAAVwetvkkgilnqinelprvtkgifwaaYHSKLKMQKMG 403
Cdd:cd05959 232 -----ATTVLMPERPTPAAVFKR-----IRRYRPTVFFGVPTL--------------------------YAAMLAAPNLP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 404 IPGGDTIgniifkkvrkatgghlRYLLNGGSPISVNA-QEFISNLICPMLIGYGLTETCASLCILNPGHFEYGVVGDLTG 482
Cdd:cd05959 276 SRDLSSL----------------RLCVSAGEALPAEVgERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVP 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 483 CVTVKLVDveELGYFAKDNK-GEIWVKGENVLPEYYKNEEETKESLtEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKtMN 561
Cdd:cd05959 340 GYEVELRD--EDGGDVADGEpGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDMLK-VS 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 562 GEYIALEKLESVYRSNSYVQNICVYA---DQNKVKPVGIIVPnhtplvklakelgimkKQETDiepylhnkklQNAVFED 638
Cdd:cd05959 416 GIWVSPFEVESALVQHPAVLEAAVVGvedEDGLTKPKAFVVL----------------RPGYE----------DSEALEE 469
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 2112360039 639 MIKTAKKQGLVGIELLQGAVFFDDewTPQngfvTSAQKLQRKKIL 683
Cdd:cd05959 470 ELKEFVKDRLAPYKYPRWIVFVDE--LPK----TATGKIQRFKLR 508
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
239-573 |
1.26e-15 |
|
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: 80.04 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 239 FDELLELGqkaKGEIEPHPPT--RDDIScIMYTSGSTGDPKGVVLKHSnvvagvgGATINVCD--YVGDTDKLICFLpla 314
Cdd:cd12118 113 YEDLLAEG---DPDFEWIPPAdeWDPIA-LNYTSGTTGRPKGVVYHHR-------GAYLNALAniLEWEMKQHPVYL--- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 315 HIFEMafellsFHwgsCIGYANVKTLTSASVRN-CksdLEEFQPTimvgvaAVWETVKKGILNQINELPRVTKGIFWAAY 393
Cdd:cd12118 179 WTLPM------FH---CNGWCFPWTVAAVGGTNvC---LRKVDAK------AIYDLIEKHKVTHFCGAPTVLNMLANAPP 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 394 HSKLKmqkmgIPGgdtigniifkKVRKATGGhlryllnggSPISVNAQEFISNLICPMLIGYGLTETC--ASLCILNPG- 470
Cdd:cd12118 241 SDARP-----LPH----------RVHVMTAG---------APPPAAVLAKMEELGFDVTHVYGLTETYgpATVCAWKPEw 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 471 -----------HFEYGVvgDLTGCVTVKLVDVEELGYFAKDNK--GEIWVKGENVLPEYYKNEEETKESLtEDGWFKTGD 537
Cdd:cd12118 297 delpteerarlKARQGV--RYVGLEEVDVLDPETMKPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGD 373
|
330 340 350
....*....|....*....|....*....|....*.
gi 2112360039 538 IGMWTDTGSLKIIDRKKNLVKTmNGEYIALEKLESV 573
Cdd:cd12118 374 LAVIHPDGYIEIKDRSKDIIIS-GGENISSVEVEGV 408
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
245-573 |
3.72e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 78.77 E-value: 3.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 245 LGQKAKGEIEPHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVCdyVGDTDKLICFLPLAHIFEMAFELL 324
Cdd:PRK06145 133 LAQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALG--LTASERLLVVGPLYHVGAFDLPGI 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 325 SFHWGSciGYANVktltsasvrncksdLEEFQPtimvgvaavwETVKKGIlnqinELPRVTKGIFWAAYHSKLkmqkMGI 404
Cdd:PRK06145 211 AVLWVG--GTLRI--------------HREFDP----------EAVLAAI-----ERHRLTCAWMAPVMLSRV----LTV 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 405 PGGDtigniifkkvrKATGGHLRYLLNGG--SPISvNAQEFISNLICPMLI-GYGLTETCASLCILNPGHF--EYGVVGD 479
Cdd:PRK06145 256 PDRD-----------RFDLDSLAWCIGGGekTPES-RIRDFTRVFTRARYIdAYGLTETCSGDTLMEAGREieKIGSTGR 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 480 LTGCVTVKLVDvEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTeDGWFKTGDIGMWTDTGSLKIIDRKKNLVKT 559
Cdd:PRK06145 324 ALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFY-GDWFRSGDVGYLDEEGFLYLTDRKKDMIIS 401
|
330
....*....|....
gi 2112360039 560 mNGEYIALEKLESV 573
Cdd:PRK06145 402 -GGENIASSEVERV 414
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
100-696 |
5.27e-15 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 78.63 E-value: 5.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 100 TFTEVIEVMHSVGRGLVKLGMEPksEDKLHIFAATSHKWMKMFLGAQSQGIP---IVTAYDTLGEK--GLIHSLKQTSSA 174
Cdd:cd05921 27 TYAEALRQVRAIAQGLLDLGLSA--ERPLLILSGNSIEHALMALAAMYAGVPaapVSPAYSLMSQDlaKLKHLFELLKPG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 175 AIFtdnqllgklinplkvaekiryviyydnisAEDkrqgGKLYREAQEAVDK-------IKEVRPDIKLVSFDELLElgQ 247
Cdd:cd05921 105 LVF-----------------------------AQD----AAPFARALAAIFPlgtplvvSRNAVAGRGAISFAELAA--T 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 248 KAKGEIEPHPP--TRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVCDYVGDTDKLICFLPLAHIF--EMAFEL 323
Cdd:cd05921 150 PPTAAVDAAFAavGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPPVLVDWLPWNHTFggNHNFNL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 324 LSFHWGSCigYAN----VKTLTSASVRNcksdLEEFQPTIMVGVAAVWETVkkgilnqINELPRvtKGIFWAAYHSKLKM 399
Cdd:cd05921 230 VLYNGGTL--YIDdgkpMPGGFEETLRN----LREISPTVYFNVPAGWEML-------VAALEK--DEALRRRFFKRLKL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 400 qkMGIpGGDTIGNIIFKKVRK---ATGGHlryllnggsPIsvnaqefisnlicPMLIGYGLTETCASLCILNPGHFEYGV 476
Cdd:cd05921 295 --MFY-AGAGLSQDVWDRLQAlavATVGE---------RI-------------PMMAGLGATETAPTATFTHWPTERSGL 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 477 VGDLTGCVTVKLVDVeelgyfakDNKGEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGslkiiDRKKNL 556
Cdd:cd05921 350 IGLPAPGTELKLVPS--------GGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLADPD-----DPAKGL 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 557 V---------KTMNGEYIALEKL--ESVYRSNSYVQNIcVYADQNKVKPVGIIVPNHTPLVKLAkelgimKKQETDIEPY 625
Cdd:cd05921 417 VfdgrvaedfKLASGTWVSVGPLraRAVAACAPLVHDA-VVAGEDRAEVGALVFPDLLACRRLV------GLQEASDAEV 489
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2112360039 626 LHNKKLQnAVFEDMIKTAKKQG------LVGIELLQGAVFFDDEWTPQNGFVTSAQKLQRKKilkaveKDVESVYAD 696
Cdd:cd05921 490 LRHAKVR-AAFRDRLAALNGEAtgsssrIARALLLDEPPSIDKGEITDKGYINQRAVLERRA------ALVERLYAD 559
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
257-601 |
9.37e-15 |
|
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: 76.96 E-value: 9.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 257 PPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGV--GGATINVcdYVGDTdklicflpLAHIFEMAF-----ELLSfhwg 329
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVsqPPARLDV--GPGSR--------VAQVLSIAFdacigEIFS---- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 330 sCIGYANvkTLtsasvrncksdleefqptIMVGVAAVWETVKKgilnQINELPrVTKGIFwaayhSKLKMQkmGIPggdt 409
Cdd:cd17653 167 -TLCNGG--TL------------------VLADPSDPFAHVAR----TVDALM-STPSIL-----STLSPQ--DFP---- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 410 igniifkkvrkatggHLRYLLNGGSPISVNAQEFISNLICpMLIGYGLTET--CASLCILNPGHFEygVVGDLTGCVTVK 487
Cdd:cd17653 210 ---------------NLKTIFLGGEAVPPSLLDRWSPGRR-LYNAYGPTECtiSSTMTELLPGQPV--TIGKPIPNSTCY 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 488 LVDvEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTEDGW------FKTGDIGMWTDTGSLKIIDRKKNLVKtMN 561
Cdd:cd17653 272 ILD-ADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFwpgsrmYRTGDYGRWTEDGGLEFLGREDNQVK-VR 349
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2112360039 562 GEYIALEKLESVyrsnsyvqnicVYADQNKVKPVGIIVPN 601
Cdd:cd17653 350 GFRINLEEIEEV-----------VLQSQPEVTQAAAIVVN 378
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
261-612 |
1.49e-14 |
|
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: 76.52 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 261 DDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGAtinVCDYVGDTDKLIcflplAHIFEMAFELLSFHW-GSCIGYANVKT 339
Cdd:cd05945 97 DDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWM---LSDFPLGPGDVF-----LNQAPFSFDLSVMDLyPALASGATLVP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 340 LTSASVRNCKS---DLEEFQPTIMVGVAAVWETV-KKGILNQiNELPRVTKGIFwaayhsklkmqkmgipggdtIGNIIF 415
Cdd:cd05945 169 VPRDATADPKQlfrFLAEHGITVWVSTPSFAAMClLSPTFTP-ESLPSLRHFLF--------------------CGEVLP 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 416 KKVRKATGGHLryllnggsPisvnaQEFISNLicpmligYGLTET---CASLCILNPGHFEYGVV--GDLTGCVTVKLVD 490
Cdd:cd05945 228 HKTARALQQRF--------P-----DARIYNT-------YGPTEAtvaVTYIEVTPEVLDGYDRLpiGYAKPGAKLVILD 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 491 vEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTED---GWFKTGDIGMWTDTGSLKIIDRKKNLVKtMNGEYIAL 567
Cdd:cd05945 288 -EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVK-LNGYRIEL 365
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2112360039 568 EKLESVYRSNSYVQNICV---YADQNKVKPVGIIVPNHTPLVKLAKEL 612
Cdd:cd05945 366 EEIEAALRQVPGVKEAVVvpkYKGEKVTELIAFVVPKPGAEAGLTKAI 413
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
249-585 |
1.49e-14 |
|
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: 76.86 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 249 AKGEIEPHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGAtinvcDYVGDT--DKLICFLPLAhiFE-MAFELls 325
Cdd:cd12117 124 GPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNT-----NYVTLGpdDRVLQTSPLA--FDaSTFEI-- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 326 fhWGScigyanvkTLTSASVRNCKS----DLEEFQPTIMV-GVAAVWETVkkGILNQINEL-PRVTKGifwaayhsklkm 399
Cdd:cd12117 195 --WGA--------LLNGARLVLAPKgtllDPDALGALIAEeGVTVLWLTA--ALFNQLADEdPECFAG------------ 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 400 qkmgipggdtigniifkkvrkatgghLRYLLNGG---SPISVNAqefiSNLICP---MLIGYGLTE--TCASLCILNPGH 471
Cdd:cd12117 251 --------------------------LRELLTGGevvSPPHVRR----VLAACPglrLVNGYGPTEntTFTTSHVVTELD 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 472 FEYGVV--GDLTGCVTVKLVDvEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTEDGW------FKTGDIGMWTD 543
Cdd:cd12117 301 EVAGSIpiGRPIANTRVYVLD-EDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFgpgerlYRTGDLARWLP 379
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2112360039 544 TGSLKIIDRKKNLVKtMNGEYIALEKLESVYRSNSYVQNICV 585
Cdd:cd12117 380 DGRLEFLGRIDDQVK-IRGFRIELGEIEAALRAHPGVREAVV 420
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
100-543 |
2.56e-14 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 76.46 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 100 TFTEVIEVMHSVGRGLVKLGMEPksEDKLHIFAATSHKWMKMFLGAQSQGIPIVT---AYDTLG---EKgLIHSLKQTSS 173
Cdd:PRK08180 71 TYAEALERVRAIAQALLDRGLSA--ERPLMILSGNSIEHALLALAAMYAGVPYAPvspAYSLVSqdfGK-LRHVLELLTP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 174 AAIFtdnqllgklinplkvaekiryviyydnisAEDkrqgGKLYREAQEAVDK-------IKEVRPDIKLVSFDELLELG 246
Cdd:PRK08180 148 GLVF-----------------------------ADD----GAAFARALAAVVPadvevvaVRGAVPGRAATPFAALLATP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 247 QKAKGEiEPHPPTR-DDISCIMYTSGSTGDPKGVVLKHSNVVAGVggATINVC-DYVGDTDK-LICFLPLAHIFEMAFEL 323
Cdd:PRK08180 195 PTAAVD-AAHAAVGpDTIAKFLFTSGSTGLPKAVINTHRMLCANQ--QMLAQTfPFLAEEPPvLVDWLPWNHTFGGNHNL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 324 -LSFHWGSCIgYAN----VKTLTSASVRNcksdLEEFQPTIMVGVAAVWETVKkGILNQINELPRvtkgifwaAYHSKLK 398
Cdd:PRK08180 272 gIVLYNGGTL-YIDdgkpTPGGFDETLRN----LREISPTVYFNVPKGWEMLV-PALERDAALRR--------RFFSRLK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 399 MQKMGipgGDTIGNIIFKKVRKATGGHLryllngGSPIsvnaqefisnlicPMLIGYGLTETCASLCILNPGHFEYGVVG 478
Cdd:PRK08180 338 LLFYA---GAALSQDVWDRLDRVAEATC------GERI-------------RMMTGLGMTETAPSATFTTGPLSRAGNIG 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2112360039 479 -DLTGCvTVKLVDVeelgyfakDNKGEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTD 543
Cdd:PRK08180 396 lPAPGC-EVKLVPV--------GGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVD 452
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
254-559 |
4.51e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 75.03 E-value: 4.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 254 EPHPptrDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGgATINVCDYVGDtDKLICFLPLAHIFEMAFELL-SFHWGSCI 332
Cdd:PRK07787 124 EPDP---DAPALIVYTSGTTGPPKGVVLSRRAIAADLD-ALAEAWQWTAD-DVLVHGLPLFHVHGLVLGVLgPLRIGNRF 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 333 GYAnVKTLTSASVRNCKSDleefqPTIMVGVAAVWetvkkgilNQINELPRvtkgifwAAyhsklkmqkmgipggdtign 412
Cdd:PRK07787 199 VHT-GRPTPEAYAQALSEG-----GTLYFGVPTVW--------SRIAADPE-------AA-------------------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 413 iifKKVRKAtgghlRYLLNGGSPISVNAQEFISNLICPMLIG-YGLTETCASLCILNPGHFEYGVVG-DLTGcVTVKLVD 490
Cdd:PRK07787 238 ---RALRGA-----RLLVSGSAALPVPVFDRLAALTGHRPVErYGMTETLITLSTRADGERRPGWVGlPLAG-VETRLVD 308
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2112360039 491 vEELGYFAKDNK--GEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKK-NLVKT 559
Cdd:PRK07787 309 -EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGREStDLIKS 379
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
261-580 |
3.49e-13 |
|
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: 72.18 E-value: 3.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 261 DDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVcdYVGDTDKLICFLPL---AHIFEMAFELLSfhwGSCI----- 332
Cdd:cd05930 93 DDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAY--PLTPGDRVLQFTSFsfdVSVWEIFGALLA---GATLvvlpe 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 333 -GYANVKTLTSAsvrncksdLEEFQPTIMVGVAAVWETvkkgILNQINElprvtkgifwAAYHSklkmqkmgipggdtig 411
Cdd:cd05930 168 eVRKDPEALADL--------LAEEGITVLHLTPSLLRL----LLQELEL----------AALPS---------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 412 niifkkvrkatgghLRYLLNGGSPISVNAQEFISNLICPMLI--GYGLTET--CASLCILNPGHFEYGVV--GDLTGCVT 485
Cdd:cd05930 210 --------------LRLVLVGGEALPPDLVRRWRELLPGARLvnLYGPTEAtvDATYYRVPPDDEEDGRVpiGRPIPNTR 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 486 VKLVDvEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTEDGWF------KTGDIGMWTDTGSLKIIDRKKNLVKt 559
Cdd:cd05930 276 VYVLD-ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGpgermyRTGDLVRWLPDGNLEFLGRIDDQVK- 353
|
330 340
....*....|....*....|.
gi 2112360039 560 MNGEYIALEKLESVYRSNSYV 580
Cdd:cd05930 354 IRGYRIELGEIEAALLAHPGV 374
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
247-576 |
3.99e-13 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 72.24 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 247 QKAKGEIEPHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATinvCDY---VGDTDkLICFlPLAHIF------ 317
Cdd:PRK09274 160 DGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALR---EDYgiePGEID-LPTF-PLFALFgpalgm 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 318 -----EMAFellsfhwgSCIGYANVKTLTSAsvrncksdLEEFQPTIMVGVAAVWETV-KKGILNQINeLP---RVTKGi 388
Cdd:PRK09274 235 tsvipDMDP--------TRPATVDPAKLFAA--------IERYGVTNLFGSPALLERLgRYGEANGIK-LPslrRVISA- 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 389 fwaayhsklkmqkmGIPggdtigniifkkVRKATGGHLRYLLNGGSPIsvnaqefisnlicpmLIGYGLTE-----TCAS 463
Cdd:PRK09274 297 --------------GAP------------VPIAVIERFRAMLPPDAEI---------------LTPYGATEalpisSIES 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 464 LCIL---------NPGHfeygVVGDLTGCVTVKLV-----------DVEELgyfAKDNKGEIWVKGENVLPEYYKNEEET 523
Cdd:PRK09274 336 REILfatraatdnGAGI----CVGRPVDGVEVRIIaisdapipewdDALRL---ATGEIGEIVVAGPMVTRSYYNRPEAT 408
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2112360039 524 KESLTEDG----WFKTGDIGMWTDTGSLKIIDRKKNLVKTMNGEY--IALEK----LESVYRS 576
Cdd:PRK09274 409 RLAKIPDGqgdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLytIPCERifntHPGVKRS 471
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
227-572 |
5.52e-13 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 72.69 E-value: 5.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 227 IKEVRPDIKLVSFDEL---LELGQKAKGEIEPHPPTR-------DDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATIN 296
Cdd:PRK06814 749 IEALEFGIRIIYLEDVraqIGLADKIKGLLAGRFPLVyfcnrdpDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAAR 828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 297 VcDYvGDTDKLICFLPLAHIFE----MAFELLS----FHWGSCIGYANVKTLTSASvrncksdleefQPTIMVGVaavwE 368
Cdd:PRK06814 829 I-DF-SPEDKVFNALPVFHSFGltggLVLPLLSgvkvFLYPSPLHYRIIPELIYDT-----------NATILFGT----D 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 369 TvkkgilnqinelprvtkgiFWAAYhsklkmqkmgipggdtigniifkkvrkATGGH------LRYLLNGGSPISVNAQE 442
Cdd:PRK06814 892 T-------------------FLNGY---------------------------ARYAHpydfrsLRYVFAGAEKVKEETRQ 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 443 FISN-LICPMLIGYGLTETCASLCILNPGHFEYGVVGDLTGCVTVKLVDVEELgyfakDNKGEIWVKGENVLPEYYKNEE 521
Cdd:PRK06814 926 TWMEkFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGI-----DEGGRLFVRGPNVMLGYLRAEN 1000
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2112360039 522 ETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKtMNGEYIALEKLES 572
Cdd:PRK06814 1001 PGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAK-IAGEMISLAAVEE 1050
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
100-575 |
1.05e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 71.12 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 100 TFTEVIEVMHSVGRGLVKLGMEPKseDKLHIFAATSHKWMKMFLGAQSQGIPIVTAYDTLGEKGLIHSLKQTSSAAIFTD 179
Cdd:PRK08316 38 TYAELDAAVNRVAAALLDLGLKKG--DRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 180 NQLLGKLINPLKvaekiryviyydnisaedkrqggKLYREAQEAVDKIKEVRPDIKLVSFDELLELGQKAKGEIEPHPpt 259
Cdd:PRK08316 116 PALAPTAEAALA-----------------------LLPVDTLILSLVLGGREAPGGWLDFADWAEAGSVAEPDVELAD-- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 260 rDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINvCDYVGDTDKLICfLPLAHIFEMAFELLSFHWgscIGYANVkT 339
Cdd:PRK08316 171 -DDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVA-GDMSADDIPLHA-LPLYHCAQLDVFLGPYLY---VGATNV-I 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 340 LTSASVRNCKSDLEEFQPTIMVGVAAVW--------------ETVKKG----------ILNQINE-LPRVTkgiFWAAYh 394
Cdd:PRK08316 244 LDAPDPELILRTIEAERITSFFAPPTVWisllrhpdfdtrdlSSLRKGyygasimpveVLKELRErLPGLR---FYNCY- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 395 sklkmqkmgipgGDT-IGNIifkkvrkAT----GGHLRYLLNGGSPIsvnaqefisnlicpmligygltetcaslciLNp 469
Cdd:PRK08316 320 ------------GQTeIAPL-------ATvlgpEEHLRRPGSAGRPV------------------------------LN- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 470 ghfeygvvgdltgcVTVKLVDvEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLtEDGWFKTGDIGMWTDTGSLKI 549
Cdd:PRK08316 350 --------------VETRVVD-DDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITV 413
|
490 500
....*....|....*....|....*..
gi 2112360039 550 IDRKKNLVKTmNGEYIA-LEKLESVYR 575
Cdd:PRK08316 414 VDRKKDMIKT-GGENVAsREVEEALYT 439
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
265-585 |
1.28e-12 |
|
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: 69.61 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 265 CIMYTSGSTGDPKGVVLKHSNVVAGvgGATINVCDYVGDTDKLICFLPLAHIFEMAFELLSFHWGScigyANV---KTLT 341
Cdd:cd17637 4 VIIHTAAVAGRPRGAVLSHGNLIAA--NLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGG----ANVvmeKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 342 SASVRncksDLEEFQPTIMVGVAAVWETvkkgILNQINELPRVTkgifwaayhSKLKmQKMGIPGGDTIgniifKKVRKA 421
Cdd:cd17637 78 AEALE----LIEEEKVTLMGSFPPILSN----LLDAAEKSGVDL---------SSLR-HVLGLDAPETI-----QRFEET 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 422 TGGHLryllnggspisvnaqefisnlicpmLIGYGLTETCASLCiLNPGHFEYGVVGDLTGCVTVKLVDveELGYFAKDN 501
Cdd:cd17637 135 TGATF-------------------------WSLYGQTETSGLVT-LSPYRERPGSAGRPGPLVRVRIVD--DNDRPVPAG 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 502 K-GEIWVKGENVLPEYYKNEEETkESLTEDGWFKTGDIGMWTDTGSLKIIDRK--KNLVKTmNGEYIALEKLESVYRSNS 578
Cdd:cd17637 187 EtGEIVVRGPLVFQGYWNLPELT-AYTFRNGWHHTGDLGRFDEDGYLWYAGRKpeKELIKP-GGENVYPAEVEKVILEHP 264
|
....*..
gi 2112360039 579 YVQNICV 585
Cdd:cd17637 265 AIAEVCV 271
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
261-585 |
1.35e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 70.83 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 261 DDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVCDYVGDTDKLICFLPLAHIFEMAfellsfhwgscigyanvktl 340
Cdd:PRK06710 206 NDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEEVVLGVLPFFHVYGMT-------------------- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 341 tsaSVRNCksdleefqpTIMVGVAAVWetvkkgilnqineLPRV-TKGIFWAAYHSKLKMqkmgIPGGDTIGNIIFKK-- 417
Cdd:PRK06710 266 ---AVMNL---------SIMQGYKMVL-------------IPKFdMKMVFEAIKKHKVTL----FPGAPTIYIALLNSpl 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 418 VRKATGGHLRYLLNGGSPISVNAQEFISNLICPMLI-GYGLTETCASLcilnpgHFEYGVVGDLTGCVTVKLVDVE---- 492
Cdd:PRK06710 317 LKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVeGYGLTESSPVT------HSNFLWEKRVPGSIGVPWPDTEamim 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 493 --ELGYFAKDNK-GEIWVKGENVLPEYYKNEEETKESLtEDGWFKTGDIGMWTDTGSLKIIDRKKNLVkTMNGEYIALEK 569
Cdd:PRK06710 391 slETGEALPPGEiGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPRE 468
|
330
....*....|....*.
gi 2112360039 570 LESVYRSNSYVQNICV 585
Cdd:PRK06710 469 VEEVLYEHEKVQEVVT 484
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
261-604 |
2.18e-12 |
|
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: 69.80 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 261 DDISCIMYTSGSTGDPKGVVLKHSNVVAGVggatinvcdYVGDTDKLICFLPLAH--IFEMAFELlsFHWGSCIGYANVK 338
Cdd:cd17650 93 EDLAYVIYTSGTTGKPKGVMVEHRNVAHAA---------HAWRREYELDSFPVRLlqMASFSFDV--FAGDFARSLLNGG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 339 TLTSasvrnCKSDLEeFQPtimvgvAAVWETVKKGILNQINELPRVTKGIFWAAYHSKLKMQKMG--IPGGDTIGNIIFK 416
Cdd:cd17650 162 TLVI-----CPDEVK-LDP------AALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRllIVGSDGCKAQDFK 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 417 KVRKATGGHLRyllnggspiSVNAqefisnlicpmligYGLTETCaslciLNPGHFEYGVVGDLTGC----------VTV 486
Cdd:cd17650 230 TLAARFGQGMR---------IINS--------------YGVTEAT-----IDSTYYEEGRDPLGDSAnvpigrplpnTAM 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 487 KLVDvEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTEDGW------FKTGDIGMWTDTGSLKIIDRKKNLVKtM 560
Cdd:cd17650 282 YVLD-ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVK-I 359
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2112360039 561 NGEYIALEKLESVYRSNSYVQNICVYADQNKVKP---VGIIVPNHTP 604
Cdd:cd17650 360 RGFRIELGEIESQLARHPAIDEAVVAVREDKGGEarlCAYVVAAATL 406
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
231-573 |
2.82e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 69.81 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 231 RPDIKLVSFDELL-ELGqkakgeiEPHPPT---RDDISCIMYTSGSTGDPKGVVLKHSNVVAGVggatinvcdyvgdtdk 306
Cdd:PRK07786 147 SSDDSVLGYEDLLaEAG-------PAHAPVdipNDSPALIMYTSGTTGRPKGAVLTHANLTGQA---------------- 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 307 licflpLAHIFEMAFELlsfhwGSCIGYANVKTLTSASVRNCKSDLEEFQPTIMVGVAAvwetVKKGILNQINELPRVTk 386
Cdd:PRK07786 204 ------MTCLRTNGADI-----NSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGA----FDPGQLLDVLEAEKVT- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 387 GIF-----WAAYHS---------KLKMQKMG-IPGGDTIgniifkkvrkatgghLRYLlnggspisvnAQEFISNLIcpm 451
Cdd:PRK07786 268 GIFlvpaqWQAVCAeqqarprdlALRVLSWGaAPASDTL---------------LRQM----------AATFPEAQI--- 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 452 LIGYGLTETCASLCIL--NPGHFEYGVVGDLTGCVTVKLVDvEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLtE 529
Cdd:PRK07786 320 LAAFGQTEMSPVTCMLlgEDAIRKLGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF-A 397
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2112360039 530 DGWFKTGDIGMWTDTGSLKIIDRKKNLVKTmNGEYIALEKLESV 573
Cdd:PRK07786 398 GGWFHSGDLVRQDEEGYVWVVDRKKDMIIS-GGENIYCAEVENV 440
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
238-557 |
3.02e-12 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 69.45 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 238 SFDELLELGQKA--------KGEIEPHpptrDDIScIMYTSGSTGDPKGVVLKHSNVVagvggatiNVCDYVGDT----- 304
Cdd:PRK08315 173 NFDELLALGRAVddaelaarQATLDPD----DPIN-IQYTSGTTGFPKGATLTHRNIL--------NNGYFIGEAmklte 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 305 -DKLICFLPLAHIFEMAFELLSF--HwGSCIGYANvktltsasvrncksdlEEFQPtimvgvAAVWETVKKGilnqinel 381
Cdd:PRK08315 240 eDRLCIPVPLYHCFGMVLGNLACvtH-GATMVYPG----------------EGFDP------LATLAAVEEE-------- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 382 pRVTkgifwAAYhsklkmqkmGIPggdTIgnII-------FKKVRKATgghLRYLLNGGS--PISV--------NAQEfi 444
Cdd:PRK08315 289 -RCT-----ALY---------GVP---TM--FIaeldhpdFARFDLSS---LRTGIMAGSpcPIEVmkrvidkmHMSE-- 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 445 snlicpMLIGYGLTETcaslcilNPGHFEYGV----------VGDLTGCVTVKLVDVEELGYFAKDNKGEIWVKGENVLP 514
Cdd:PRK08315 344 ------VTIAYGMTET-------SPVSTQTRTddplekrvttVGRALPHLEVKIVDPETGETVPRGEQGELCTRGYSVMK 410
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2112360039 515 EYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLV 557
Cdd:PRK08315 411 GYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMI 453
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
234-557 |
9.11e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 68.10 E-value: 9.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 234 IKLVSFDELLelgqkAKGEIEPHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVgGATINVCDYVGDTDKLICFLPL 313
Cdd:PRK07768 130 IRVLTVADLL-----AADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANA-EAMFVAAEFDVETDVMVSWLPL 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 314 AHIFEMafellsfhwgscIGYanvktLTSASVRNCksdleefqptimvgvaavwETVKkgilnqINELPRVTKGIFWAAY 393
Cdd:PRK07768 204 FHDMGM------------VGF-----LTVPMYFGA-------------------ELVK------VTPMDFLRDPLLWAEL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 394 HSKLKmqkmgipGGDTIG-----NIIFKKVRK-ATGGH-----LRYLLNGGSPISVNAQEFISNLICP-------MLIGY 455
Cdd:PRK07768 242 ISKYR-------GTMTAApnfayALLARRLRRqAKPGAfdlssLRFALNGAEPIDPADVEDLLDAGARfglrpeaILPAY 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 456 GLTETCASLCILNPGHfeyGVVGD------------------------------LTGCvTVKLVDvEELGYFAKDNKGEI 505
Cdd:PRK07768 315 GMAEATLAVSFSPCGA---GLVVDevdadllaalrravpatkgntrrlatlgppLPGL-EVRVVD-EDGQVLPPRGVGVI 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2112360039 506 WVKGENVLPeYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLV 557
Cdd:PRK07768 390 ELRGESVTP-GYLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVI 440
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
223-557 |
1.25e-11 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 67.47 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 223 AVDKIKEVRPDIklvSFDELLELGQKAKgeiEPHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAG----VGGATINVC 298
Cdd:PRK06087 155 GVDKLAPATSSL---SLSQIIADYEPLT---TAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASerayCARLNLTWQ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 299 DyvgdtdklICFL--PLAHIfemafelLSFHWGscigyanvktLTSASVRNCKSDLEE-FQPTimvgvAAVwetvkkGIL 375
Cdd:PRK06087 229 D--------VFMMpaPLGHA-------TGFLHG----------VTAPFLIGARSVLLDiFTPD-----ACL------ALL 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 376 NQinelPRVTkgifWAAYHSKLKMqkmgipggDTIGNIIFKKVRKATgghLRYLLNGGSPISVN-AQEFISNLIcPMLIG 454
Cdd:PRK06087 273 EQ----QRCT----CMLGATPFIY--------DLLNLLEKQPADLSA---LRFFLCGGTTIPKKvARECQQRGI-KLLSV 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 455 YGLTETCASL------CILNPGHFE-YGVVGdltgcVTVKLVDvEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESL 527
Cdd:PRK06087 333 YGSTESSPHAvvnlddPLSRFMHTDgYAAAG-----VEIKVVD-EARKTLPPGCEGEEASRGPNVFMGYLDEPELTARAL 406
|
330 340 350
....*....|....*....|....*....|
gi 2112360039 528 TEDGWFKTGDIGMWTDTGSLKIIDRKKNLV 557
Cdd:PRK06087 407 DEEGWYYSGDLCRMDEAGYIKITGRKKDII 436
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
261-612 |
6.46e-11 |
|
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: 65.18 E-value: 6.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 261 DDISCIMYTSGSTGDPKGVVLKHSNVVagvGGATINVCDYVGDT--DKLICflpLAHIFeMAFEL---LSFHW---GSCI 332
Cdd:cd05919 91 DDIAYLLYSSGTTGPPKGVMHAHRDPL---LFADAMAREALGLTpgDRVFS---SAKMF-FGYGLgnsLWFPLavgASAV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 333 GYAnvktlTSASVRNCKSDLEEFQPTIMVGVAAVWETVkkgilnqinelpRVTKGIFWAAYHSklkmqkmgipggdtign 412
Cdd:cd05919 164 LNP-----GWPTAERVLATLARFRPTVLYGVPTFYANL------------LDSCAGSPDALRS----------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 413 iifkkvrkatgghLRYLLNGGSPISVN-AQEFISNLICPMLIGYGLTETCASLCILNPGHFEYGVVGDLTGCVTVKLVDv 491
Cdd:cd05919 210 -------------LRLCVSAGEALPRGlGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 492 eELGYFAKDNK-GEIWVKGENVLPEYYKNEEETKESLtEDGWFKTGDI------GMWTDTGslkiidRKKNLVKtMNGEY 564
Cdd:cd05919 276 -EEGHTIPPGEeGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKfcrdadGWYTHAG------RADDMLK-VGGQW 346
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2112360039 565 IALEKLESVYRSNSYVQNICVYA---DQNKVKPVGIIVPN--HTPLVKLAKEL 612
Cdd:cd05919 347 VSPVEVESLIIQHPAVAEAAVVAvpeSTGLSRLTAFVVLKspAAPQESLARDI 399
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
228-591 |
8.46e-11 |
|
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: 64.66 E-value: 8.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 228 KEVRPDIKLVSFDELLELGQ-KAKGEIEPHPPTR-DDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVcdYVGDTD 305
Cdd:cd17655 102 SHLQPPIAFIGLIDLLDEDTiYHEESENLEPVSKsDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVI--YQGEHL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 306 KLICFLPL---AHIFEMAFELLSFHwgscigyanvktlTSASVRncKSDLEEFQPTImvgvaavwETVKKGILNQINELP 382
Cdd:cd17655 180 RVALFASIsfdASVTEIFASLLSGN-------------TLYIVR--KETVLDGQALT--------QYIRQNRITIIDLTP 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 383 RVTKGIFWAAYHSKLKMQKMgIPGGDTIGNIIFKKVRKATGGHLRYLlnggspisvNAqefisnlicpmligYGLTET-- 460
Cdd:cd17655 237 AHLKLLDAADDSEGLSLKHL-IVGGEALSTELAKKIIELFGTNPTIT---------NA--------------YGPTETtv 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 461 CASLCILNPGHFEYGVV--GDLTGCVTVKLVDvEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTEDGW------ 532
Cdd:cd17655 293 DASIYQYEPETDQQVSVpiGKPLGNTRIYILD-QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFvpgerm 371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2112360039 533 FKTGDIGMWTDTGSLKIIDRKKNLVKtMNGEYIALEKLESVYRSNSYVQNICVYA--DQNK 591
Cdd:cd17655 372 YRTGDLARWLPDGNIEFLGRIDHQVK-IRGYRIELGEIEARLLQHPDIKEAVVIArkDEQG 431
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
143-571 |
8.73e-11 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 65.12 E-value: 8.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 143 LGAQSQG-IPIVTAYdTLGEKGLIHSLKQTSSAAIFTDNQLL--GKLIN-PLKVAEkIRYViyydnisaedkrqggklYR 218
Cdd:PRK08043 273 FGASLRRrIPAMMNY-TAGVKGLTSAITAAEIKTIFTSRQFLdkGKLWHlPEQLTQ-VRWV-----------------YL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 219 EaqeavDKIKEVRPDIKLVSFDELLelgQKAKGEIEPHPptrDDISCIMYTSGSTGDPKGVVLKHSNVVAGVggATI-NV 297
Cdd:PRK08043 334 E-----DLKDDVTTADKLWIFAHLL---MPRLAQVKQQP---EDAALILFTSGSEGHPKGVVHSHKSLLANV--EQIkTI 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 298 CDYVGDtDKLICFLPLAHIFEMAFELLS--------FHWGSCIGYANVKTLTSAsvRNCksdleefqpTIMVGVAAvwet 369
Cdd:PRK08043 401 ADFTPN-DRFMSALPLFHSFGLTVGLFTplltgaevFLYPSPLHYRIVPELVYD--RNC---------TVLFGTST---- 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 370 vkkgilnqinelprvtkgiFWAAYhsklkmqkmgipggdtigniifkkVRKATG---GHLRYLLNGGSPISVN-AQEFIS 445
Cdd:PRK08043 465 -------------------FLGNY------------------------ARFANPydfARLRYVVAGAEKLQEStKQLWQD 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 446 NLICPMLIGYGLTEtCASLCILN-PGHFEYGVVGDLTGCVTVKLVDVEELgyfakDNKGEIWVKGENVLPEYYKNEE--- 521
Cdd:PRK08043 502 KFGLRILEGYGVTE-CAPVVSINvPMAAKPGTVGRILPGMDARLLSVPGI-----EQGGRLQLKGPNIMNGYLRVEKpgv 575
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2112360039 522 ------ETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKtMNGEYIALEKLE 571
Cdd:PRK08043 576 levptaENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAK-IAGEMVSLEMVE 630
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
254-557 |
9.43e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 65.14 E-value: 9.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 254 EPHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVggatINVCDYVG--DTDKLICFLPLAHIFEMAFELLSFHWGSC 331
Cdd:PRK07769 173 VPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNV----LQVIDALEgqEGDRGVSWLPFFHDMGLITVLLPALLGHY 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 332 IgyanvktltsasvrncksdleefqpTIMVGVAAV-----WetvkkgilnqINELPRV---TKGIFWAA-----YHSKLK 398
Cdd:PRK07769 249 I-------------------------TFMSPAAFVrrpgrW----------IRELARKpggTGGTFSAApnfafEHAAAR 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 399 -MQKMGIPGGDtIGNIIfkkvrkatgghlrYLLNGGSPISVNAQEFISNLICPmligYGLTETC---------ASLCI-- 466
Cdd:PRK07769 294 gLPKDGEPPLD-LSNVK-------------GLLNGSEPVSPASMRKFNEAFAP----YGLPPTAikpsygmaeATLFVst 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 467 ----------------LNPGHF-------EYGVVGDLTGCVTVK----LVDVEELGYFAKDNKGEIWVKGENVLPEYYKN 519
Cdd:PRK07769 356 tpmdeeptviyvdrdeLNAGRFvevpadaPNAVAQVSAGKVGVSewavIVDPETASELPDGQIGEIWLHGNNIGTGYWGK 435
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2112360039 520 EEETKESL----------------TEDG-WFKTGDIGMWTDtGSLKIIDRKKNLV 557
Cdd:PRK07769 436 PEETAATFqnilksrlseshaegaPDDAlWVRTGDYGVYFD-GELYITGRVKDLV 489
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
164-612 |
1.26e-10 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 64.42 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 164 LIHSLKQTSSAAIFTDNQLLGKLINPLKVAEKIRYVIYYDNISAEDKRqggklyreaqeavdkiKEVRPDIKLVSFDELL 243
Cdd:PRK05620 103 IVHIINHAEDEVIVADPRLAEQLGEILKECPCVRAVVFIGPSDADSAA----------------AHMPEGIKVYSYEALL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 244 ElGQKAkgeIEPHPPT-RDDISCIMYTSGSTGDPKGVVLKHSNVVagVGGATINVCDYVGDTD--KLICFLPLAHIFEMA 320
Cdd:PRK05620 167 D-GRST---VYDWPELdETTAAAICYSTGTTGAPKGVVYSHRSLY--LQSLSLRTTDSLAVTHgeSFLCCVPIYHVLSWG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 321 FELLSFHWGScigyanvktltsasvrncksdleefqPTIMVGVAAVWETVKKGILNQineLPRVTKGI--FWAA---YHS 395
Cdd:PRK05620 241 VPLAAFMSGT--------------------------PLVFPGPDLSAPTLAKIIATA---MPRVAHGVptLWIQlmvHYL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 396 KLKMQKMGipggdtigniifkkvrkatgghLRYLLNGGSPISvnaqefisnlicPMLIG-------------YGLTETCA 462
Cdd:PRK05620 292 KNPPERMS----------------------LQEIYVGGSAVP------------PILIKaweerygvdvvhvWGMTETSP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 463 SLCILNP----------------GHF----EYGVVGDltGCVTVklvdveelgyfAKD-NKGEIWVKGENVLPEYYKNE- 520
Cdd:PRK05620 338 VGTVARPpsgvsgearwayrvsqGRFpaslEYRIVND--GQVME-----------STDrNEGEIQVRGNWVTASYYHSPt 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 521 ---------------EETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKTmNGEYIALEKLESVYRSNSYVQNICV 585
Cdd:PRK05620 405 eegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRS-GGEWIYSAQLENYIMAAPEVVECAV 483
|
490 500 510
....*....|....*....|....*....|....*.
gi 2112360039 586 --YADQNKV-KPVGIIV------PNHTPLVKLAKEL 612
Cdd:PRK05620 484 igYPDDKWGeRPLAVTVlapgiePTRETAERLRDQL 519
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
175-573 |
1.63e-10 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 64.00 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 175 AIFTDNQLLgklinPL--KVAEKI----RYVIYYDNISAEDKRQGGKLYREaqeavDKIKEVRPDIKLVSFDEllelgqk 248
Cdd:PRK06018 114 VVITDLTFV-----PIleKIADKLpsveRYVVLTDAAHMPQTTLKNAVAYE-----EWIAEADGDFAWKTFDE------- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 249 akgeiephpptrdDISCIM-YTSGSTGDPKGVVLKH-SNVVAGVggaTINVCDYVG--DTDKLICFLPLahifemafell 324
Cdd:PRK06018 177 -------------NTAAGMcYTSGTTGDPKGVLYSHrSNVLHAL---MANNGDALGtsAADTMLPVVPL----------- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 325 sFH---WGscIGYANVKTLTSASVRNCKSD-------LEEFQPTIMVGVAAVWEtvkkgILNQinelprvtkgifwaayh 394
Cdd:PRK06018 230 -FHansWG--IAFSAPSMGTKLVMPGAKLDgasvyelLDTEKVTFTAGVPTVWL-----MLLQ----------------- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 395 sklKMQKMGipggdtigniifkkvrkATGGHLRYLLNGGSPISVNAQEFISNLICPMLIGYGLTETC--ASLCILnPGHF 472
Cdd:PRK06018 285 ---YMEKEG-----------------LKLPHLKMVVCGGSAMPRSMIKAFEDMGVEVRHAWGMTEMSplGTLAAL-KPPF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 473 EygvvgDLTG---------------CVTVKLVDvEELGYFAKDNK--GEIWVKGENVLPEYYKNEEETkesLTEDGWFKT 535
Cdd:PRK06018 344 S-----KLPGdarldvlqkqgyppfGVEMKITD-DAGKELPWDGKtfGRLKVRGPAVAAAYYRVDGEI---LDDDGFFDT 414
|
410 420 430
....*....|....*....|....*....|....*...
gi 2112360039 536 GDIGMWTDTGSLKIIDRKKNLVKTmNGEYIALEKLESV 573
Cdd:PRK06018 415 GDVATIDAYGYMRITDRSKDVIKS-GGEWISSIDLENL 451
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
455-575 |
1.68e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 64.20 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 455 YGLTETC--ASLCILNPG------------HFEYGVVGDLTGCVTVklVDVEELGYFAKDNK--GEIWVKGENVLPEYYK 518
Cdd:PRK08162 327 YGLTETYgpATVCAWQPEwdalplderaqlKARQGVRYPLQEGVTV--LDPDTMQPVPADGEtiGEIMFRGNIVMKGYLK 404
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2112360039 519 NEEETKESLtEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKTmNGEYIALEKLESV-YR 575
Cdd:PRK08162 405 NPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIIS-GGENISSIEVEDVlYR 460
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
164-557 |
1.95e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 63.83 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 164 LIHSLKQTSSAAIFTDNQLLGKLInPLKVAEKIRYVI---YYDNISAEDKRQGGKLYREAQEAvdkikEVRPDIKLVSFD 240
Cdd:PRK08314 100 LAHYVTDSGARVAIVGSELAPKVA-PAVGNLRLRHVIvaqYSDYLPAEPEIAVPAWLRAEPPL-----QALAPGGVVAWK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 241 ELLELGQKAKgeiePHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGAtinvCDYVGDT--DKLICFLPLAHIFE 318
Cdd:PRK08314 174 EALAAGLAPP----PHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGS----VLWSNSTpeSVVLAVLPLFHVTG 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 319 MAFELLSfhwgscigyanvktltsasvrncksdleefqpTIMVGVAAV----W--ETVKKGIlnqinELPRVTkgiFWAA 392
Cdd:PRK08314 246 MVHSMNA--------------------------------PIYAGATVVlmprWdrEAAARLI-----ERYRVT---HWTN 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 393 yhsklkMQKMGIpggDTIGNiifKKVRKATGGHLRYLLNGGSPI--SVnAQEFISNLICPMLIGYGLTETcASLCILNP- 469
Cdd:PRK08314 286 ------IPTMVV---DFLAS---PGLAERDLSSLRYIGGGGAAMpeAV-AERLKELTGLDYVEGYGLTET-MAQTHSNPp 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 470 GHFEYGVVGDLTGCVTVKLVDVEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTE-DG--WFKTGDIGMWTDTGS 546
Cdd:PRK08314 352 DRPKLQCLGIPTFGVDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFIEiDGkrFFRTGDLGRMDEEGY 431
|
410
....*....|.
gi 2112360039 547 LKIIDRKKNLV 557
Cdd:PRK08314 432 FFITDRLKRMI 442
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
186-605 |
2.35e-10 |
|
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: 63.30 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 186 LINPLKVAEKIRYVIYYDNISAedkrqggklyreAQEAVDKikEVRPDIKLvSFDELLELGQK--------AKGEIEPHP 257
Cdd:cd05923 82 LINPRLKAAELAELIERGEMTA------------AVIAVDA--QVMDAIFQ-SGVRVLALSDLvglgepesAGPLIEDPP 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 258 PTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVCDYVGDTDKLICFLPLAHIFEMaFELLSfhwGSCIGYANV 337
Cdd:cd05923 147 REPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRHNVVLGLMPLYHVIGF-FAVLV---AALALDGTY 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 338 KTLTSASVRNCKSDLEEFQPTIMVGVAAVWETVKKGILNQINELPRVTKGIFwaayhsklkmqkmgipGGDTIGNIIFKK 417
Cdd:cd05923 223 VVVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTF----------------AGATMPDAVLER 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 418 VrkatgghlryllnggspisvnaQEFISNLICPMligYGLTETCASL--------CILNPGHFEYGVVGDLTGCVTVKLV 489
Cdd:cd05923 287 V----------------------NQHLPGEKVNI---YGTTEAMNSLymrdartgTEMRPGFFSEVRIVRIGGSPDEALA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 490 DVEElgyfakdnkGEIWVK--GENVLPEYYKNEEETKESLtEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKTmNGEYIAL 567
Cdd:cd05923 342 NGEE---------GELIVAaaADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMIIS-GGENIHP 410
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2112360039 568 EKLESVYRSNSYVQNICV--YADQNKVKPV-GIIVPNHTPL 605
Cdd:cd05923 411 SEIERVLSRHPGVTEVVVigVADERWGQSVtACVVPREGTL 451
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
252-574 |
4.90e-10 |
|
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: 62.48 E-value: 4.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 252 EIEPHP----PTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVCDYVGDTDkLICFLPLAhIFEMAFELlsfh 327
Cdd:cd05910 72 EAEPDAfigiPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVD-LATFPLFA-LFGPALGL---- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 328 wGSCIGYANVKTLTSASVRNCKSDLEEFQPTIMVGVAAVWETVKKGILNQINELPRvtkgifwaayhsklkmqkmgipgg 407
Cdd:cd05910 146 -TSVIPDMDPTRPARADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPS------------------------ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 408 dtigniifkkvrkatgghLRYLLNGGSPISVNAQEFISNLICP---MLIGYGLTEtCASLCI-----LNPGHFEY----- 474
Cdd:cd05910 201 ------------------LRRVLSAGAPVPIALAARLRKMLSDeaeILTPYGATE-ALPVSSigsreLLATTTAAtsgga 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 475 GV-VGDLTGCVTVKLVDVEELGYFAKDNK--------GEIWVKGENVLPEYYKNEEETKESLTEDG----WFKTGDIGMW 541
Cdd:cd05910 262 GTcVGRPIPGVRVRIIEIDDEPIAEWDDTlelprgeiGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYL 341
|
330 340 350
....*....|....*....|....*....|...
gi 2112360039 542 TDTGSLKIIDRKKNLVKTMNGEYIAlEKLESVY 574
Cdd:cd05910 342 DDEGRLWFCGRKAHRVITTGGTLYT-EPVERVF 373
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
261-585 |
5.73e-10 |
|
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: 61.94 E-value: 5.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 261 DDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVcdYVGDTDKLICFLPLAHIF---EMafellsfhWGSCIGYANV 337
Cdd:cd17643 93 DDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWF--GFNEDDVWTLFHSYAFDFsvwEI--------WGALLHGGRL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 338 KTLTSASVRncksDLEEFqptimvgvaavWETVKKG---ILNQinelprvTKGIFWAAyhsklkMQKMGIPGGDTIGnii 414
Cdd:cd17643 163 VVVPYEVAR----SPEDF-----------ARLLRDEgvtVLNQ-------TPSAFYQL------VEAADRDGRDPLA--- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 415 fkkvrkatgghLRYLLNGGSPISVN-----AQEFISNliCPMLI-GYGLTETC--ASLCILNPGHFEYG---VVGDLTGC 483
Cdd:cd17643 212 -----------LRYVIFGGEALEAAmlrpwAGRFGLD--RPQLVnMYGITETTvhVTFRPLDAADLPAAaasPIGRPLPG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 484 VTVKLVDvEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTEDGW-------FKTGDIGMWTDTGSLKIIDRKKNL 556
Cdd:cd17643 279 LRVYVLD-ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFggpgsrmYRTGDLARRLPDGELEYLGRADEQ 357
|
330 340
....*....|....*....|....*....
gi 2112360039 557 VKtMNGEYIALEKLESVYRSNSYVQNICV 585
Cdd:cd17643 358 VK-IRGFRIELGEIEAALATHPSVRDAAV 385
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
100-587 |
7.27e-10 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 62.08 E-value: 7.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 100 TFTEVIEVMHSVGRGLVKLGMEPKseDKLHIFAATSHKWMKMFLGAQSQG---IPIVTAYdtlgeKG--LIHSLKQTSSA 174
Cdd:PRK06155 48 TYAEAARAAAAAAHALAAAGVKRG--DRVALMCGNRIEFLDVFLGCAWLGaiaVPINTAL-----RGpqLEHILRNSGAR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 175 AIFTDNQLLgklinplkvaekiryviyydnisaedkrqggklyrEAQEAVDKIKEVRPDIKLVsfDELLELGQKAKGEIE 254
Cdd:PRK06155 121 LLVVEAALL-----------------------------------AALEAADPGDLPLPAVWLL--DAPASVSVPAGWSTA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 255 PHPPTRD----------DISCIMYTSGSTGDPKGVVLKHS-------NVVAGVGgatinvcdyVGDTDKLICFLPLahif 317
Cdd:PRK06155 164 PLPPLDApapaaavqpgDTAAILYTSGTTGPSKGVCCPHAqfywwgrNSAEDLE---------IGADDVLYTTLPL---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 318 emafellsFHwgscigyanvktlTSAsvrncksdLEEFQPTIMVGVAAVWEtvkkgilnqinelPRVTKGIFWAAyhskl 397
Cdd:PRK06155 231 --------FH-------------TNA--------LNAFFQALLAGATYVLE-------------PRFSASGFWPA----- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 398 kMQKMGIPGGDTIG---NIIFKK-VRKATGGH-LRYLLNGGSPISVnAQEFISNLICPMLIGYGLTETcASLCILNPGHF 472
Cdd:PRK06155 264 -VRRHGATVTYLLGamvSILLSQpARESDRAHrVRVALGPGVPAAL-HAAFRERFGVDLLDGYGSTET-NFVIAVTHGSQ 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 473 EYGVVGDLTGCVTVKLVDvEELGYFAKDNKGEIWVKGEN---VLPEYYKNEEETKESLtEDGWFKTGDIGMWTDTGSLKI 549
Cdd:PRK06155 341 RPGSMGRLAPGFEARVVD-EHDQELPDGEPGELLLRADEpfaFATGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRF 418
|
490 500 510
....*....|....*....|....*....|....*...
gi 2112360039 550 IDRKKNLVKtMNGEYIALEKLESVYRSNSYVQNICVYA 587
Cdd:PRK06155 419 VDRIKDAIR-RRGENISSFEVEQVLLSHPAVAAAAVFP 455
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
261-559 |
1.19e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 61.16 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 261 DDISCIMYTSGSTGDPKGVVLKHSNVVagvGGATINVCDY--VGDTDKLICfLPLAHIFEMAFellsfhwgscigyanVK 338
Cdd:PRK06188 168 PDIAGLAYTGGTTGKPKGVMGTHRSIA---TMAQIQLAEWewPADPRFLMC-TPLSHAGGAFF---------------LP 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 339 TLT-SASVRNCKSdleeFQPtimvgvAAVWETVKKgilNQINELPRVTKGIFWAAYHSKLkmqkmgipggdtigniifkk 417
Cdd:PRK06188 229 TLLrGGTVIVLAK----FDP------AEVLRAIEE---QRITATFLVPTMIYALLDHPDL-------------------- 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 418 vRKATGGHLRYLLNGGSPIS-VNAQEFIsNLICPMLIG-YGLTETCASLCILNPGHFEYGVVGDLTGC------VTVKLV 489
Cdd:PRK06188 276 -RTRDLSSLETVYYGASPMSpVRLAEAI-ERFGPIFAQyYGQTEAPMVITYLRKRDHDPDDPKRLTSCgrptpgLRVALL 353
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 490 DvEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLtEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKT 559
Cdd:PRK06188 354 D-EDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMIVT 421
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
259-612 |
1.32e-09 |
|
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: 60.95 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 259 TRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVCDYVGDtDKLICFLPLAHIFEMAFELLsFHWGscIGyANVK 338
Cdd:cd05958 95 ASDDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLRED-DRFVGSPPLAFTFGLGGVLL-FPFG--VG-ASGV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 339 TLTSASVRNCKSDLEEFQPTIMVGVAavweTVKKGILNQINELPRVTKGIfwaayhsklkmqKMGIPGGDTIGNIIFKKV 418
Cdd:cd05958 170 LLEEATPDLLLSAIARYKPTVLFTAP----TAYRAMLAHPDAAGPDLSSL------------RKCVSAGEALPAALHRAW 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 419 RKATGghlryllnggspisvnaqefisnliCPMLIGYGLTETCASLCILNPGHFEYGVVGDLTGCVTVKLVDveELGYFA 498
Cdd:cd05958 234 KEATG-------------------------IPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD--DEGNPV 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 499 KDNK-GEIWVKGENVlpeYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKTmNGEYIALEKLESVYRSN 577
Cdd:cd05958 287 PDGTiGRLAVRGPTG---CRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVS-GGYNIAPPEVEDVLLQH 362
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2112360039 578 SYVQNICVYA--DQNK-VKPVGIIV--PNHTPLVKLAKEL 612
Cdd:cd05958 363 PAVAECAVVGhpDESRgVVVKAFVVlrPGVIPGPVLAREL 402
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
266-576 |
1.82e-09 |
|
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: 60.63 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 266 IMYTSGSTGDPKGVVLKHSNVVAGVGGATINVCdyVGDTDKLICFLPLA---HIFEMafeLLSFHWGSCIGyanvktltS 342
Cdd:cd05918 111 VIFTSGSTGKPKGVVIEHRALSTSALAHGRALG--LTSESRVLQFASYTfdvSILEI---FTTLAAGGCLC--------I 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 343 ASVRNCKSDLEEFqptimvgvaavwetvkkgilnqINELpRVTkgifwaayHSKLkmqkmgIPggdTIGNIIfkkvRKAT 422
Cdd:cd05918 178 PSEEDRLNDLAGF----------------------INRL-RVT--------WAFL------TP---SVARLL----DPED 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 423 GGHLRYLLNGGSPISVNAQEFISNLICpMLIGYGLTETC-ASLCILNPGHFEYGVVGDLTGCVT--VKLVDVEELgyFAK 499
Cdd:cd05918 214 VPSLRTLVLGGEALTQSDVDTWADRVR-LINAYGPAECTiAATVSPVVPSTDPRNIGRPLGATCwvVDPDNHDRL--VPI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 500 DNKGEIWVKGENVLPEYYKNEEETKESLTED-GW------------FKTGDIGMWTDTGSLKIIDRKKNLVKtMNGEYIA 566
Cdd:cd05918 291 GAVGELLIEGPILARGYLNDPEKTAAAFIEDpAWlkqegsgrgrrlYRTGDLVRYNPDGSLEYVGRKDTQVK-IRGQRVE 369
|
330
....*....|
gi 2112360039 567 LEKLESVYRS 576
Cdd:cd05918 370 LGEIEHHLRQ 379
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
242-609 |
2.40e-09 |
|
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: 60.00 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 242 LLELGQKAKGEIEPHPPTR-DDISCIMYTSGSTGDPKGVVLKHSNVV---AGVGGATinvcdYVGDTDKLICFLPLAhiF 317
Cdd:cd12116 106 LLALAAAAAAPAAPRTPVSpDDLAYVIYTSGSTGRPKGVVVSHRNLVnflHSMRERL-----GLGPGDRLLAVTTYA--F 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 318 EMA-FELLsfhwgscigyanVKTLTSASVRNCKSD-----------LEEFQPTIMVGVAAVWETVKKgilNQINELPRVT 385
Cdd:cd12116 179 DISlLELL------------LPLLAGARVVIAPREtqrdpealarlIEAHSITVMQATPATWRMLLD---AGWQGRAGLT 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 386 kgifwaayhsklkmqkmgipggdtigniifkkvrkatgghlryLLNGGSPISVN-AQEFIS------NLicpmligYGLT 458
Cdd:cd12116 244 -------------------------------------------ALCGGEALPPDlAARLLSrvgslwNL-------YGPT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 459 ETC--ASLCILNPGHfEYGVVGDLTGCVTVKLVDvEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTEDG----- 531
Cdd:cd12116 274 ETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLD-AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPfagpg 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 532 --WFKTGDIGMWTDTGSLKIIDRKKNLVKtMNGEYIALEKLESVYRSNSYVQNICV--YADQNKVKPVGIIVPNHTPLVK 607
Cdd:cd12116 352 srLYRTGDLVRRRADGRLEYLGRADGQVK-IRGHRIELGEIEAALAAHPGVAQAAVvvREDGGDRRLVAYVVLKAGAAPD 430
|
..
gi 2112360039 608 LA 609
Cdd:cd12116 431 AA 432
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
260-552 |
3.24e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 60.05 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 260 RDDISCIMYTSGSTGDPKGVVLKHSN---VVagvggaTINVCDYVGDT---DKLICFLPLAHifemafellsfhwgsciG 333
Cdd:PRK07470 162 HDDPCWFFFTSGTTGRPKAAVLTHGQmafVI------TNHLADLMPGTteqDASLVVAPLSH-----------------G 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 334 yANVKTLTSASvRNCKSDL---EEFQPtimvgvAAVWETVKKGilnqinelpRVTKgIFwaayhsklkmqkmGIPggdTI 410
Cdd:PRK07470 219 -AGIHQLCQVA-RGAATVLlpsERFDP------AEVWALVERH---------RVTN-LF-------------TVP---TI 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 411 GNIIFKKVRKATGGH--LRYLLNGGSPISVNAQEFISNLICPMLIGY-GLTETCASLCILNP-GHFEYGVVGDLTGC--- 483
Cdd:PRK07470 265 LKMLVEHPAVDRYDHssLRYVIYAGAPMYRADQKRALAKLGKVLVQYfGLGEVTGNITVLPPaLHDAEDGPDARIGTcgf 344
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2112360039 484 ------VTVKLVDVEELGYFAKdnkGEIWVKGENVLPEYYKNEEETKESLtEDGWFKTGDIGMWTDTGSLKIIDR 552
Cdd:PRK07470 345 ertgmeVQIQDDEGRELPPGET---GEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGR 415
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
234-573 |
4.06e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 59.72 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 234 IKLVSFDELLElGQKAKGEIephpPTRDD--ISCIMYTSGSTGDPKGVVLKH-SNVVAGVGGATINVCDyVGDTDKLICF 310
Cdd:PRK07008 152 TPLLCYETLVG-AQDGDYDW----PRFDEnqASSLCYTSGTTGNPKGALYSHrSTVLHAYGAALPDAMG-LSARDAVLPV 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 311 LPLAHIFEmafellsfhWGscIGYAnvKTLTSASVRNCKSDL---------EEFQPTIMVGVAAVWEtvkkGILNQINEl 381
Cdd:PRK07008 226 VPMFHVNA---------WG--LPYS--APLTGAKLVLPGPDLdgkslyeliEAERVTFSAGVPTVWL----GLLNHMRE- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 382 prvtkgifwaayhsklkmqkmgipggdtigniifKKVRKATgghLRYLLNGGS---PISVNAqeFISNLICPMLIGYGLT 458
Cdd:PRK07008 288 ----------------------------------AGLRFST---LRRTVIGGSacpPAMIRT--FEDEYGVEVIHAWGMT 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 459 ETC--ASLCILNPGHFEYGV---------VGDLTGCVTVKLVDVE--ELGYfakDNK--GEIWVKGENVLPEYYKNEEet 523
Cdd:PRK07008 329 EMSplGTLCKLKWKHSQLPLdeqrkllekQGRVIYGVDMKIVGDDgrELPW---DGKafGDLQVRGPWVIDRYFRGDA-- 403
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2112360039 524 keSLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKTmNGEYIALEKLESV 573
Cdd:PRK07008 404 --SPLVDGWFPTGDVATIDADGFMQITDRSKDVIKS-GGEWISSIDIENV 450
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
235-573 |
4.42e-09 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 59.65 E-value: 4.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 235 KLVSFDELLELGQKAKGEIEPHPPTR--------DDIScIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVcdYVGDTDK 306
Cdd:PLN03102 153 KRPSSEELDYECLIQRGEPTPSLVARmfriqdehDPIS-LNYTSGTTADPKGVVISHRGAYLSTLSAIIGW--EMGTCPV 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 307 LICFLPLAHIfemafELLSFHWGSCigyanVKTLTSASVRNCKS-----DLEEFQPTIMVGVAAVWETVKKGilNQINEL 381
Cdd:PLN03102 230 YLWTLPMFHC-----NGWTFTWGTA-----ARGGTSVCMRHVTApeiykNIEMHNVTHMCCVPTVFNILLKG--NSLDLS 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 382 PRvtkgifwaayhsklkmqkmgipggdtigniifkkvrkatGGHLRYLLNGGSPISVNAQEfISNLICPMLIGYGLTETC 461
Cdd:PLN03102 298 PR---------------------------------------SGPVHVLTGGSPPPAALVKK-VQRLGFQVMHAYGLTEAT 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 462 ASLCILN--------PGHFEY------GVvgDLTGCVTVKLVDVEELGYFAKDNK--GEIWVKGENVLPEYYKNEEETKE 525
Cdd:PLN03102 338 GPVLFCEwqdewnrlPENQQMelkarqGV--SILGLADVDVKNKETQESVPRDGKtmGEIVIKGSSIMKGYLKNPKATSE 415
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2112360039 526 SLtEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKTmNGEYIALEKLESV 573
Cdd:PLN03102 416 AF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIIS-GGENISSVEVENV 461
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
241-590 |
6.12e-09 |
|
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: 58.89 E-value: 6.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 241 ELLELGQKAKGEIEPHPPT-RDDISCIMYTSGSTGDPKGVVLKHSNVVagvggatiNVCDY------VGDTDKLICFLPL 313
Cdd:cd17651 115 LLDQPGAAAGADAEPDPALdADDLAYVIYTSGSTGRPKGVVMPHRSLA--------NLVAWqarassLGPGARTLQFAGL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 314 AhiFEMAF-ELLSFhwgscIGYANVKTLTSASVRNcksDLEEFqptimvgvAAVWETvkkgilNQINE--LPRVTkgIFW 390
Cdd:cd17651 187 G--FDVSVqEIFST-----LCAGATLVLPPEEVRT---DPPAL--------AAWLDE------QRISRvfLPTVA--LRA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 391 AAYHSKlkmqkmgiPGGdtigniifkkvrkATGGHLRYLLNGGSPISVNA--QEFISNLICPMLI-GYGLTE----TCAS 463
Cdd:cd17651 241 LAEHGR--------PLG-------------VRLAALRYLLTGGEQLVLTEdlREFCAGLPGLRLHnHYGPTEthvvTALS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 464 LCILNPGHFEYGVVGDLTGCVTVKLVDvEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTEDGW------FKTGD 537
Cdd:cd17651 300 LPGDPAAWPAPPPIGRPIDNTRVYVLD-AALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFvpgarmYRTGD 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2112360039 538 IGMWTDTGSLKIIDRKKNLVKtMNGEYIALEKLESVYRSNSYVQNICVYADQN 590
Cdd:cd17651 379 LARWLPDGELEFLGRADDQVK-IRGFRIELGEIEAALARHPGVREAVVLARED 430
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
237-587 |
8.07e-09 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 58.53 E-value: 8.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 237 VSFDELL-----ELGQKAKGEIEPHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVggatINVCDYVGDTDKLICFL 311
Cdd:PRK13295 168 DSFEALLitpawEQEPDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANI----VPYAERLGLGADDVILM 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 312 --PLAHifemafeLLSFHWGSCIgyanvktltsasvrncksdleefqpTIMVGVAAV----WETVKKGILNQinelprvT 385
Cdd:PRK13295 244 asPMAH-------QTGFMYGLMM-------------------------PVMLGATAVlqdiWDPARAAELIR-------T 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 386 KGIFWaayhsklkmqkmgipggdTIGNIIF----KKVRKATG---GHLRYLLNGGSPIS----VNAQEFISNLICPmliG 454
Cdd:PRK13295 285 EGVTF------------------TMASTPFltdlTRAVKESGrpvSSLRTFLCAGAPIPgalvERARAALGAKIVS---A 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 455 YGLTETCASLCILNPGHFEYGVVGDltGC----VTVKLVDvEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESltED 530
Cdd:PRK13295 344 WGMTENGAVTLTKLDDPDERASTTD--GCplpgVEVRVVD-ADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTD--AD 418
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2112360039 531 GWFKTGDIGMWTDTGSLKIIDRKKNLVkTMNGEYIALEKLESVYRSNSYVQNICVYA 587
Cdd:PRK13295 419 GWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEALLYRHPAIAQVAIVA 474
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
503-562 |
1.64e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 57.74 E-value: 1.64e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 503 GEIWVKGENVLPEYYKNEEETKESLtEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKTmNG 562
Cdd:PRK06178 415 GEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV-NG 472
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
261-612 |
2.07e-08 |
|
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: 57.06 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 261 DDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVcdYVGDTDKLICFLPLAhiFEMAFELLSFHWgsCIGYANVktL 340
Cdd:cd17644 106 ENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEY--GITSSDRVLQFASIA--FDVAAEEIYVTL--LSGATLV--L 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 341 TSASVRnckSDLEEFqptimvgvaavWETVKKGILNQINELPRvtkgiFWAAYHSKLKMQKMGIPggdtigniifkkvrk 420
Cdd:cd17644 178 RPEEMR---SSLEDF-----------VQYIQQWQLTVLSLPPA-----YWHLLVLELLLSTIDLP--------------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 421 atgGHLRYLLNGGS---PISVNA-QEFISNLIcPMLIGYGLTETC--ASLCILNPGHFEYG---VVGDLTGCVTVKLVDv 491
Cdd:cd17644 224 ---SSLRLVIVGGEavqPELVRQwQKNVGNFI-QLINVYGPTEATiaATVCRLTQLTERNItsvPIGRPIANTQVYILD- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 492 EELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTEDGW--------FKTGDIGMWTDTGSLKIIDRKKNLVKtMNGE 563
Cdd:cd17644 299 ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFnsseserlYKTGDLARYLPDGNIEYLGRIDNQVK-IRGF 377
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2112360039 564 YIALEKLESVYRSNSYVQNICVYA--DQNKVKP-VGIIVPnHTPLVKLAKEL 612
Cdd:cd17644 378 RIELGEIEAVLSQHNDVKTAVVIVreDQPGNKRlVAYIVP-HYEESPSTVEL 428
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
100-543 |
3.99e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 56.59 E-value: 3.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 100 TFTEVIEVMHSVGRGLVKLGMEPksEDKLHIFAATSHKWMKMFLGAQSQGI---PIVTAYDTLGekglihslkqtssaai 176
Cdd:PRK12582 82 TYGEAKRAVDALAQALLDLGLDP--GRPVMILSGNSIEHALMTLAAMQAGVpaaPVSPAYSLMS---------------- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 177 fTDNQLLGKLINplKVAEKIRYViyydnisaedkrQGGKLYREAQEAVD----KIKEVRPD---IKLVSFDELLelGQKA 249
Cdd:PRK12582 144 -HDHAKLKHLFD--LVKPRVVFA------------QSGAPFARALAALDlldvTVVHVTGPgegIASIAFADLA--ATPP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 250 KGEIEPhppTRDDISC-----IMYTSGSTGDPKGVVLKH---SNVVAGVGGATINVCDyvGDTDKLICFLPLAHIF--EM 319
Cdd:PRK12582 207 TAAVAA---AIAAITPdtvakYLFTSGSTGMPKAVINTQrmmCANIAMQEQLRPREPD--PPPPVSLDWMPWNHTMggNA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 320 AFELLSfhWGSCIGYAN----VKTLTSASVRNcksdLEEFQPTIM----VGVAAVWETVKKGilnqinelPRVTKGIFwa 391
Cdd:PRK12582 282 NFNGLL--WGGGTLYIDdgkpLPGMFEETIRN----LREISPTVYgnvpAGYAMLAEAMEKD--------DALRRSFF-- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 392 ayhskLKMQKMGIpGGDTIGNIIFKKVR----KATGGHLryllnggspisvnaqefisnlicPMLIGYGLTETCASLCIL 467
Cdd:PRK12582 346 -----KNLRLMAY-GGATLSDDLYERMQalavRTTGHRI-----------------------PFYTGYGATETAPTTTGT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 468 npgHFEYGVVGdLTGC----VTVKLVDVEElgyfakdnKGEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTD 543
Cdd:PRK12582 397 ---HWDTERVG-LIGLplpgVELKLAPVGD--------KYEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVD 464
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
266-587 |
4.72e-08 |
|
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: 55.84 E-value: 4.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 266 IMYTSGSTGDPKGVVLKHSnvvagvggatinvcdyvgdtdklicflPLAHIFEMAFELLSFHWGSCIgyanvktLTSASV 345
Cdd:cd17649 99 VIYTSGSTGTPKGVAVSHG---------------------------PLAAHCQATAERYGLTPGDRE-------LQFASF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 346 rNCKSDLEEFQPTIMVGVAAV------WETVKKgILNQINELpRVTKGIFWAAYHSKLkMQKMGIPGGDtigniifkkVR 419
Cdd:cd17649 145 -NFDGAHEQLLPPLICGACVVlrpdelWASADE-LAEMVREL-GVTVLDLPPAYLQQL-AEEADRTGDG---------RP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 420 KAtgghLRYLLNGGSPISVNAQEFISNLICPMLIGYGLTETC--ASLCILNPGHFEYGV---VGDLTGCVTVKLVDvEEL 494
Cdd:cd17649 212 PS----LRLYIFGGEALSPELLRRWLKAPVRLFNAYGPTEATvtPLVWKCEAGAARAGAsmpIGRPLGGRSAYILD-ADL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 495 GYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTEDG-------WFKTGDIGMWTDTGSLKIIDRKKNLVKtMNGEYIAL 567
Cdd:cd17649 287 NPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPfgapgsrLYRTGDLARWRDDGVIEYLGRVDHQVK-IRGFRIEL 365
|
330 340
....*....|....*....|
gi 2112360039 568 EKLESVYRSNSYVQNICVYA 587
Cdd:cd17649 366 GEIEAALLEHPGVREAAVVA 385
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
242-557 |
8.04e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 55.33 E-value: 8.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 242 LLELGQKAKGEIEPHPptRDDISCIMYTSGSTGDPKGVVLKHSNVVAgvggatiNV----CDYVGDTDK-------LICF 310
Cdd:PRK05850 143 LLDLDSPRGSDARPRD--LPSTAYLQYTSGSTRTPAGVMVSHRNVIA-------NFeqlmSDYFGDTGGvpppdttVVSW 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 311 LPLAHifEMAFELlsfhwGSCIgyanvktltsasvrncksdleefqpTIMVGVAAVwetvkkgILNQINELPRVTKgifW 390
Cdd:PRK05850 214 LPFYH--DMGLVL-----GVCA-------------------------PILGGCPAV-------LTSPVAFLQRPAR---W 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 391 aayhsklkMQKMGI-PGGDTIG-NIIFK-KVRKATG--------GHLRYLLNGGSPISVNA-QEFIS-----NL----IC 449
Cdd:PRK05850 252 --------MQLLASnPHAFSAApNFAFElAVRKTSDddmagldlGGVLGIISGSERVHPATlKRFADrfapfNLretaIR 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 450 PmliGYGLTETCASLCILNPG------HFEY-----GVV-----GDLTGCV--------TVKLVDVEELGYFAKDNKGEI 505
Cdd:PRK05850 324 P---SYGLAEATVYVATREPGqppesvRFDYeklsaGHAkrcetGGGTPLVsygsprspTVRIVDPDTCIECPAGTVGEI 400
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2112360039 506 WVKGENVLPEYYKNEEETKESL----------TEDG-WFKTGDIGMWTDtGSLKIIDRKKNLV 557
Cdd:PRK05850 401 WVHGDNVAAGYWQKPEETERTFgatlvdpspgTPEGpWLRTGDLGFISE-GELFIVGRIKDLL 462
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
239-591 |
1.04e-07 |
|
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: 54.97 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 239 FDELLELGQKAKGEIEPHPPTR--DDISCIMYTSGSTGDPKGVVLKHSnvvagvggATINVCD------YVGDTDKLICF 310
Cdd:cd12114 102 FDVLILDLDALAAPAPPPPVDVapDDLAYVIFTSGSTGTPKGVMISHR--------AALNTILdinrrfAVGPDDRVLAL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 311 LPLAhiFEMA----FELLSF----------------HWgscigyanvktltsasvrncKSDLEEFQPTIMVGVAAVWETV 370
Cdd:cd12114 174 SSLS--FDLSvydiFGALSAgatlvlpdearrrdpaHW--------------------AELIERHGVTLWNSVPALLEML 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 371 KkGILNQINELPRvtkgifwaayhsKLKMQKMGipgGDTIGNIIFKKVRkATGGHLRYLLNGGS----------PISVNA 440
Cdd:cd12114 232 L-DVLEAAQALLP------------SLRLVLLS---GDWIPLDLPARLR-ALAPDARLISLGGAteasiwsiyhPIDEVP 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 441 QEFISnlicpmlIGYGLTETCASLCILNPG--HFEYGVVGdltgcvtvklvdveelgyfakdnkgEIWVKGENVLPEYYK 518
Cdd:cd12114 295 PDWRS-------IPYGRPLANQRYRVLDPRgrDCPDWVPG-------------------------ELWIGGRGVALGYLG 342
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2112360039 519 NEEETKESLTEDG----WFKTGDIGMWTDTGSLKIIDRKKNLVKtMNGEYIALEKLESVYRSNSYVQNICVYADQNK 591
Cdd:cd12114 343 DPELTAARFVTHPdgerLYRTGDLGRYRPDGTLEFLGRRDGQVK-VRGYRIELGEIEAALQAHPGVARAVVVVLGDP 418
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
454-585 |
1.15e-07 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 54.88 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 454 GYGLTETCASLCI-LNPGHfeyGVVGDLTGCVTVKLVDveelgyfakdnkGEIWVKGENVLPEYYKNEEETkeSLT-EDG 531
Cdd:PRK09029 270 GYGLTEMASTVCAkRADGL---AGVGSPLPGREVKLVD------------GEIWLRGASLALGYWRQGQLV--PLVnDEG 332
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2112360039 532 WFKTGDIGMWTDtGSLKIIDRKKNLVKTmNGEYIALEKLESVYRSNSYVQNICV 585
Cdd:PRK09029 333 WFATRDRGEWQN-GELTILGRLDNLFFS-GGEGIQPEEIERVINQHPLVQQVFV 384
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
503-571 |
1.53e-07 |
|
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: 54.38 E-value: 1.53e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2112360039 503 GEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVktmN--GEYIALEKLE 571
Cdd:COG1021 381 GELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQI---NrgGEKIAAEEVE 448
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
485-546 |
2.29e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 53.98 E-value: 2.29e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2112360039 485 TVKLVDVEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGS 546
Cdd:PRK06164 360 RVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQ 421
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
269-573 |
5.15e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 52.85 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 269 TSGSTGDPKGVVLKHSNVVAGVGGATINVcDYVGDTDKLICFLPLAHIFEMAFELLSFHWGSCIGYANVKTLTSASVRnC 348
Cdd:PRK05851 160 TAGSTGTPRTAILSPGAVLSNLRGLNARV-GLDAATDVGCSWLPLYHDMGLAFLLTAALAGAPLWLAPTTAFSASPFR-W 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 349 KSDLEEFQPTImvgVAAvwetvkkgilnqinelPRVtkgifwaAYhsklkmqkmgipggdtigNIIFKKVRKATG---GH 425
Cdd:PRK05851 238 LSWLSDSRATL---TAA----------------PNF-------AY------------------NLIGKYARRVSDvdlGA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 426 LRYLLNGGSPISVNAQEFISNLICP-------MLIGYGLTE-TCAsLCILNPG---HFE------------YGVVGDLTG 482
Cdd:PRK05851 274 LRVALNGGEPVDCDGFERFATAMAPfgfdagaAAPSYGLAEsTCA-VTVPVPGiglRVDevttddgsgarrHAVLGNPIP 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 483 CVTVKLVDVEELGYFAKDNKGEIWVKGENVLPEYYKneeetKESLTEDGWFKTGDIGMWTDtGSLKIIDRKKNLVkTMNG 562
Cdd:PRK05851 353 GMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLG-----QAPIDPDDWFPTGDLGYLVD-GGLVVCGRAKELI-TVAG 425
|
330
....*....|.
gi 2112360039 563 EYIALEKLESV 573
Cdd:PRK05851 426 RNIFPTEIERV 436
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
255-287 |
5.86e-07 |
|
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: 52.94 E-value: 5.86e-07
10 20 30
....*....|....*....|....*....|...
gi 2112360039 255 PHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVV 287
Cdd:COG1020 611 PVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALV 643
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
503-571 |
1.29e-06 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 51.54 E-value: 1.29e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2112360039 503 GEIWVKGENVLPEYYKNEEETKEsLTEDGWFKTGDIGMWTDtGSLKIIDRKKNLVkTMNGEYIALEKLE 571
Cdd:PRK09192 412 GHICVRGPSLMSGYFRDEESQDV-LAADGWLDTGDLGYLLD-GYLYITGRAKDLI-IINGRNIWPQDIE 477
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
261-613 |
1.56e-06 |
|
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: 51.02 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 261 DDISCIMYTSGSTGDPKGVVLKHSNVVagvggatiNVCDYVGDTdklicflplahiFEMAfellsfhwgscigyANVKTL 340
Cdd:cd17645 104 DDLAYVIYTSGSTGLPKGVMIEHHNLV--------NLCEWHRPY------------FGVT--------------PADKSL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 341 TSASVRNCKSDLEEFqPTIMVGvaAVWETVKKGILNQINELPRV--TKGIFWAAYHSKLKMQKMGIPGGDtigniifkkv 418
Cdd:cd17645 150 VYASFSFDASAWEIF-PHLTAG--AALHVVPSERRLDLDALNDYfnQEGITISFLPTGAAEQFMQLDNQS---------- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 419 rkatgghLRYLLNGGSPISV---NAQEFISNlicpmligYGLTEtCASLCILNPGHFEYG--VVGDLTGCVTVKLVDvEE 493
Cdd:cd17645 217 -------LRVLLTGGDKLKKierKGYKLVNN--------YGPTE-NTVVATSFEIDKPYAniPIGKPIDNTRVYILD-EA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 494 LGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTEDGW------FKTGDIGMWTDTGSLKIIDRKKNLVKtMNGEYIAL 567
Cdd:cd17645 280 LQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFvpgermYRTGDLAKFLPDGNIEFLGRLDQQVK-IRGYRIEP 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2112360039 568 EKLESVYRSNSYVQNICVYA----DQNKVKPVGIIVPNHTPLVKLAKELG 613
Cdd:cd17645 359 GEIEPFLMNHPLIELAAVLAkedaDGRKYLVAYVTAPEEIPHEELREWLK 408
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
261-556 |
2.18e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 51.32 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 261 DDISCIMYTSGSTGDPKGVVLKHSNVVA-------GVGgatINvcdyVGDTDKLICFLPLAHIFEMAFELLS--FHWGSC 331
Cdd:PRK05691 166 DDIAFLQYTSGSTALPKGVQVSHGNLVAneqlirhGFG---ID----LNPDDVIVSWLPLYHDMGLIGGLLQpiFSGVPC 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 332 IGYANVKTLTSaSVRNCKSdLEEFQPTIMVGVAAVW----ETVKKGILNQINeLPRvtkgifWAAYHSklkmqkmgipGG 407
Cdd:PRK05691 239 VLMSPAYFLER-PLRWLEA-ISEYGGTISGGPDFAYrlcsERVSESALERLD-LSR------WRVAYS----------GS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 408 DTIgniifkkvRKATgghLRYLLNGGSPISVNAQEFISNlicpmligYGLTEtcASLCI------------------LNP 469
Cdd:PRK05691 300 EPI--------RQDS---LERFAEKFAACGFDPDSFFAS--------YGLAE--ATLFVsggrrgqgipaleldaeaLAR 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 470 GHFEYGVVGDLTGCVT------VKLVDVEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTE-DG--WFKTGDIGM 540
Cdd:PRK05691 359 NRAEPGTGSVLMSCGRsqpghaVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEhDGrtWLRTGDLGF 438
|
330 340
....*....|....*....|...
gi 2112360039 541 WTD-----TGSLK--IIDRKKNL 556
Cdd:PRK05691 439 LRDgelfvTGRLKdmLIVRGHNL 461
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
100-600 |
2.91e-06 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 50.22 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 100 TFTEVIEVMHSVGRGLVKLGMEPksEDKLHIFAATSHKWMKMFLGAQSQGIPIVTAYDTLGEKGLIHSLKQTSSAAIFTD 179
Cdd:TIGR02262 32 SYGELEAQVRRLAAALRRLGVKR--EERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 180 NQLLgklinplkvaekiryviyydnisaedkrqggKLYREAQEAVDKIKEV----RPDIKLVSFDELLELGQKakgEIEP 255
Cdd:TIGR02262 110 GALL-------------------------------PVIKAALGKSPHLEHRvvvgRPEAGEVQLAELLATESE---QFKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 256 HPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVCDYVGDTdklICFlPLAHIFemafellsFHWGscIGYA 335
Cdd:TIGR02262 156 AATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDD---VCF-SAAKLF--------FAYG--LGNA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 336 nvktLTSASVRNCKSDLEEFQPTimvgVAAVWETvkkgilnqineLPRVTKGIFWAA---YHSKLKMQKMgipggdtign 412
Cdd:TIGR02262 222 ----LTFPMSVGATTVLMGERPT----PDAVFDR-----------LRRHQPTIFYGVptlYAAMLADPNL---------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 413 iifkkvRKATGGHLRYLLNGGSPISVN-AQEFISNLICPMLIGYGLTETCASLCILNPGHFEYGVVGDLTGCVTVKLVDv 491
Cdd:TIGR02262 273 ------PSEDQVRLRLCTSAGEALPAEvGQRWQARFGVDIVDGIGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVG- 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 492 EELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLtEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKtMNGEYIALEKLE 571
Cdd:TIGR02262 346 DGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTF-QGEWTRSGDKYVRNDDGSYTYAGRTDDMLK-VSGIYVSPFEIE 423
|
490 500 510
....*....|....*....|....*....|..
gi 2112360039 572 SVYRSNSYVQNICV--YADQNK-VKPVGIIVP 600
Cdd:TIGR02262 424 SALIQHPAVLEAAVvgVADEDGlIKPKAFVVL 455
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
455-604 |
3.76e-06 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 49.99 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 455 YGLTETCASLCILNPGHFEYG--VVGDLTGCVTVKLVDveelgyfakDNKGEIWVKGENVLPEYYKNEEETkeslteDGW 532
Cdd:PRK07445 261 YGMTETASQIATLKPDDFLAGnnSSGQVLPHAQITIPA---------NQTGNITIQAQSLALGYYPQILDS------QGI 325
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2112360039 533 FKTGDIGMWTDTGSLKIIDRKKNLVKTmNGEYIALEKLESVYRSNSYVQNICVY--ADQN---KVkpVGIIVPNHTP 604
Cdd:PRK07445 326 FETDDLGYLDAQGYLHILGRNSQKIIT-GGENVYPAEVEAAILATGLVQDVCVLglPDPHwgeVV--TAIYVPKDPS 399
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
455-573 |
4.04e-06 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 49.84 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 455 YGLTETC--ASLCILNPG------------HFEYGVvgDLTGCVTVKLVDVEELGYFAKDNK--GEIWVKGENVLPEYYK 518
Cdd:PLN02479 341 YGLSETYgpSTVCAWKPEwdslppeeqarlNARQGV--RYIGLEGLDVVDTKTMKPVPADGKtmGEIVMRGNMVMKGYLK 418
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2112360039 519 NEEETKESLtEDGWFKTGDIGMWTDTGSLKIIDRKKNLVKTmNGEYIALEKLESV 573
Cdd:PLN02479 419 NPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIIS-GGENISSLEVENV 471
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
488-619 |
4.22e-06 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 49.89 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 488 LVDVEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESL-TEDGW--FKTGDIGMWTDtGSLKIIDRKKNLVKtMNGEY 564
Cdd:PRK04813 330 LIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGYLED-GLLFYQGRIDFQIK-LNGYR 407
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 565 IALEKLESVYRSNSYVQNICV--YADQNKVKP-VGIIVPNHTplvKLAKELGIMK--KQE 619
Cdd:PRK04813 408 IELEEIEQNLRQSSYVESAVVvpYNKDHKVQYlIAYVVPKEE---DFEREFELTKaiKKE 464
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
261-538 |
5.27e-06 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 49.62 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 261 DDISCIMYTSGSTGDPKGVVLKHSNVVAG---VGGATINVCDYVgDTDKLICFLPLAHIFEMAFELLSF-HWGSCI-GYA 335
Cdd:PRK05857 169 EDPLAMIFTSGTTGEPKAVLLANRTFFAVpdiLQKEGLNWVTWV-VGETTYSPLPATHIGGLWWILTCLmHGGLCVtGGE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 336 NVKTLTSASVRNcKSDLEEFQPTIMVGVAavwetvkkgilnqinelprvtkgifwaayhSKLKMQKMGIPGgdtigniif 415
Cdd:PRK05857 248 NTTSLLEILTTN-AVATTCLVPTLLSKLV------------------------------SELKSANATVPS--------- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 416 kkvrkatgghLRYLLNGGSPISVNAQEFISNLICPMLIGYGLTET-CASLCILNP----GHFEYGVVGDLTGCVTVKLVD 490
Cdd:PRK05857 288 ----------LRLVGYGGSRAIAADVRFIEATGVRTAQVYGLSETgCTALCLPTDdgsiVKIEAGAVGRPYPGVDVYLAA 357
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2112360039 491 VEELGYFAKDNK-----GEIWVKGENVLPEYYKNEEETKESLTeDGWFKTGDI 538
Cdd:PRK05857 358 TDGIGPTAPGAGpsasfGTLWIKSPANMLGYWNNPERTAEVLI-DGWVNTGDL 409
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
259-585 |
5.46e-06 |
|
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: 49.24 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 259 TRDDISCIMYTSGSTGDPKGVVLKHSNVVagvggATINVCDYVGDTDKL--------ICFlPLAhIFEMaFELLSFhwGS 330
Cdd:cd12115 103 DPDDLAYVIYTSGSTGRPKGVAIEHRNAA-----AFLQWAAAAFSAEELagvlastsICF-DLS-VFEL-FGPLAT--GG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 331 CIGYA-NVKTLTSASVRnCKSDLEEFQPTIMvgvAAvwetvkkgiLNQINELPRVTKGIFWAayhsklkmqkmgipgGDT 409
Cdd:cd12115 173 KVVLAdNVLALPDLPAA-AEVTLINTVPSAA---AE---------LLRHDALPASVRVVNLA---------------GEP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 410 IGNIIFKKVRKATGGhlryllnggspisvnaqEFISNLicpmligYGLTE--TCASLCILNPGHFEYGVVGDLTGCVTVK 487
Cdd:cd12115 225 LPRDLVQRLYARLQV-----------------ERVVNL-------YGPSEdtTYSTVAPVPPGASGEVSIGRPLANTQAY 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 488 LVDvEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTEDGW------FKTGDIGMWTDTGSLKIIDRKKNLVKtMN 561
Cdd:cd12115 281 VLD-RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFgpgarlYRTGDLVRWRPDGLLEFLGRADNQVK-VR 358
|
330 340
....*....|....*....|....
gi 2112360039 562 GEYIALEKLESVYRSNSYVQNICV 585
Cdd:cd12115 359 GFRIELGEIEAALRSIPGVREAVV 382
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
234-601 |
1.02e-05 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 49.08 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 234 IKLVSFDELLelgQKAKGEIEPHPPTRDDISCIMY-----TSGSTGDPKGVVLKHSNVVAGVggATINVCDYVGDTDK-- 306
Cdd:PTZ00297 572 ITLIPYEFVE---QKGRLCPVPLKEHVTTDTVFTYvvdntTSASGDGLAVVRVTHADVLRDI--STLVMTGVLPSSFKkh 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 307 -LICFLPLAHIFEMAFELLSFHWGSCIGYANVKTLTSASVRncksdleeFQPTIMVGVAAVWETVKKGILNQINELPRVT 385
Cdd:PTZ00297 647 lMVHFTPFAMLFNRVFVLGLFAHGSAVATVDAAHLQRAFVK--------FQPTILVAAPSLFSTSRLQLSRANERYSAVY 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 386 KGIFWAAYHSKLKMQKMGIPGGDTIGNIIFKKVRKATGGHLRYLLNGGS--PISVNAQEFISNLICPMLIGYGLTETCAS 463
Cdd:PTZ00297 719 SWLFERAFQLRSRLINIHRRDSSLLRFIFFRATQELLGGCVEKIVLCVSeeSTSFSLLEHISVCYVPCLREVFFLPSEGV 798
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 464 LCIlnpghfeygvvgDLTGCVTVKlVDVEELGYFAKDNKgeiwvKGENVLpeyykneeeTKESLTEdgwfKTGDIG-MWT 542
Cdd:PTZ00297 799 FCV------------DGTPAPSLQ-VDLEPFDEPSDGAG-----IGQLVL---------AKKGEPR----RTLPIAaQWK 847
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 543 DTGSLKIIDRKKNLVKTMNGEYIALEKLESVYRSNSYVQNICVYADqnKVKP-VGIIVPN 601
Cdd:PTZ00297 848 RDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYAD--PSRPiIAIVSPN 905
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
233-287 |
1.25e-05 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 48.35 E-value: 1.25e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2112360039 233 DIKLVSFDELLELGQKAKGEIEPHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVV 287
Cdd:PRK04813 115 GIPVITLDELKDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGVQISHDNLV 169
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
261-593 |
1.37e-05 |
|
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: 48.24 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 261 DDISCIMYTSGSTGDPKGVVLKHSNVVagvggatiNVcdyvgdtdklicflpLAHIFEMAFELLSfhwgscigyANVKTL 340
Cdd:cd17656 128 DDLLYIIYTSGTTGKPKGVQLEHKNMV--------NL---------------LHFEREKTNINFS---------DKVLQF 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 341 TSASVRNCksdLEEFQPTIMVG--VAAVWETVKKGIlNQINEL---PRVTKGIFWAAYHSKLKMQKMGIPGgdtigniIF 415
Cdd:cd17656 176 ATCSFDVC---YQEIFSTLLSGgtLYIIREETKRDV-EQLFDLvkrHNIEVVFLPVAFLKFIFSEREFINR-------FP 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 416 KKVRKAtgghlryllnggspISVNAQEFISNLICPMLIG--------YGLTET-CASLCILNPG-HF-EYGVVGDLTGCV 484
Cdd:cd17656 245 TCVKHI--------------ITAGEQLVITNEFKEMLHEhnvhlhnhYGPSEThVVTTYTINPEaEIpELPPIGKPISNT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 485 TVKLVDvEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTEDGW------FKTGDIGMWTDTGSLKIIDRKKNLVK 558
Cdd:cd17656 311 WIYILD-QEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVK 389
|
330 340 350
....*....|....*....|....*....|....*..
gi 2112360039 559 tMNGEYIALEKLESVYRSNSYVQN--ICVYADQNKVK 593
Cdd:cd17656 390 -IRGYRIELGEIEAQLLNHPGVSEavVLDKADDKGEK 425
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
100-307 |
1.86e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 47.96 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 100 TFTEVIEVMHSVGRGLVKLGMEPksEDKLHIFAATSHKWMKMFLGA-QSQGIPIVTAYD-TLGEkgLIHSLKQTSSAAIF 177
Cdd:PRK07798 30 TYAELEERANRLAHYLIAQGLGP--GDHVGIYARNRIEYVEAMLGAfKARAVPVNVNYRyVEDE--LRYLLDDSDAVALV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 178 TDNQLLGKLINPLKVAEKIRYVIYYDNISAEDKRQGGklyreaqeavdkikevrpdiklVSFDELLelgqkAKGEIEPHP 257
Cdd:PRK07798 106 YEREFAPRVAEVLPRLPKLRTLVVVEDGSGNDLLPGA----------------------VDYEDAL-----AAGSPERDF 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2112360039 258 PTR--DDIScIMYTSGSTGDPKGVVLKHSNV-VAGVGGATINVCDYVGDTDKL 307
Cdd:PRK07798 159 GERspDDLY-LLYTGGTTGMPKGVMWRQEDIfRVLLGGRDFATGEPIEDEEEL 210
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
205-284 |
1.86e-05 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 48.01 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 205 ISAEDKRQGGK---LYREAQEAV----DKIKEV----RPDIKLVSFDE-----LLELGQKAKGEIEPHPPTRDDISCIMY 268
Cdd:TIGR02188 165 ITADEGLRGGKvipLKAIVDEALekcpVSVEHVlvvrRTGNPVVPWVEgrdvwWHDLMAKASAYCEPEPMDSEDPLFILY 244
|
90
....*....|....*.
gi 2112360039 269 TSGSTGDPKGVVlkHS 284
Cdd:TIGR02188 245 TSGSTGKPKGVL--HT 258
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
254-557 |
2.49e-05 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 47.43 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 254 EPHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVvagvggaTINVCDYVGDTDKL------ICFLPLAHifEMAFELLSFH 327
Cdd:PRK12476 186 VPVELDTDDVSHLQYTSGSTRPPVGVEITHRAV-------GTNLVQMILSIDLLdrnthgVSWLPLYH--DMGLSMIGFP 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 328 wGSCIGYAnvkTLTSasvrncksdleefqPTIMVGVAAVWetvkkgilnqINELPR--VTKGIFWAA--YHSKLKMQKMG 403
Cdd:PRK12476 257 -AVYGGHS---TLMS--------------PTAFVRRPQRW----------IKALSEgsRTGRVVTAApnFAYEWAAQRGL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 404 IPGGDTI--GNIIfkkvrkatgghlryLLNGGSPISVNAQEFISNLICPmligYGLTETC---------ASLCI------ 466
Cdd:PRK12476 309 PAEGDDIdlSNVV--------------LIIGSEPVSIDAVTTFNKAFAP----YGLPRTAfkpsygiaeATLFVatiapd 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 467 ------------LNPG--------------HFEYGVVGDLTGCVTVKLVDVEELGyfakDNK-GEIWVKGENVLPEYYKN 519
Cdd:PRK12476 371 aepsvvyldreqLGAGravrvaadapnavaHVSCGQVARSQWAVIVDPDTGAELP----DGEvGEIWLHGDNIGRGYWGR 446
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2112360039 520 EEETKESL----------------TEDG--WFKTGDIGMWTDtGSLKIIDRKKNLV 557
Cdd:PRK12476 447 PEETERTFgaklqsrlaegshadgAADDgtWLRTGDLGVYLD-GELYITGRIADLI 501
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
503-572 |
6.05e-05 |
|
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: 46.17 E-value: 6.05e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 503 GEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVkTMNGEYIALEKLES 572
Cdd:cd05920 336 GELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQI-NRGGEKIAAEEVEN 404
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
258-559 |
6.32e-05 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 45.81 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 258 PTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGvGGATinvCDYVGDTDKLICFLPLAHIFEMAFELLSFhwgsCIGYANV 337
Cdd:PRK07824 32 PIDDDVALVVATSGTTGTPKGAMLTAAALTAS-ADAT---HDRLGGPGQWLLALPAHHIAGLQVLVRSV----IAGSEPV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 338 KTLTSASvrncksdleeFQPTIMVGVAAVWETvkkgilnqinelPRVtkgifwaaYHSKLKMQ---KMGIPGGDTIgnii 414
Cdd:PRK07824 104 ELDVSAG----------FDPTALPRAVAELGG------------GRR--------YTSLVPMQlakALDDPAATAA---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 415 fkkvrkatgghLRYL---LNGGSPISVNAQEFISNLICPMLIGYGLTETCASlCILNpghfeyGVvgDLTGcVTVKLVDv 491
Cdd:PRK07824 150 -----------LAELdavLVGGGPAPAPVLDAAAAAGINVVRTYGMSETSGG-CVYD------GV--PLDG-VRVRVED- 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2112360039 492 eelgyfakdnkGEIWVKGEnVLPEYYKNEEETKeSLTEDGWFKTGDIGMWTDtGSLKIIDRKKNLVKT 559
Cdd:PRK07824 208 -----------GRIALGGP-TLAKGYRNPVDPD-PFAEPGWFRTDDLGALDD-GVLTVLGRADDAIST 261
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
229-288 |
6.93e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 46.04 E-value: 6.93e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 229 EVRPDIKLVSFDELLElgqKAKGEIEPHPPTRDDISCIMYTSGSTGDPKGVVLKHSNVVA 288
Cdd:PRK04319 176 DVEEGPGTLDFNALME---QASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQ 232
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
257-315 |
7.48e-05 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 45.77 E-value: 7.48e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2112360039 257 PPTRDDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGATINVCDyVGDTDKLICFLPLAH 315
Cdd:PRK09192 172 RPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDGLK-VRPGDRCVSWLPFYH 229
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
205-284 |
8.99e-05 |
|
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: 45.63 E-value: 8.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 205 ISAEDKRQGGK---LYREAQEAVDKIKEVRPDIKL------VSFDE-----LLELGQKAKGEIEPHPPTRDDISCIMYTS 270
Cdd:cd05966 161 ITADGGYRGGKvipLKEIVDEALEKCPSVEKVLVVkrtggeVPMTEgrdlwWHDLMAKQSPECEPEWMDSEDPLFILYTS 240
|
90
....*....|....
gi 2112360039 271 GSTGDPKGVVlkHS 284
Cdd:cd05966 241 GSTGKPKGVV--HT 252
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
503-553 |
9.89e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 45.28 E-value: 9.89e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2112360039 503 GEIWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRK 553
Cdd:PRK08276 341 GTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDRK 391
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
232-287 |
1.44e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 45.42 E-value: 1.44e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2112360039 232 PDIKLVSFDELLelgqkAKGEIEPHPPTR-DDISCIMYTSGSTGDPKGVVLKHSNVV 287
Cdd:PRK10252 573 PDLTSLCYNAPL-----APQGAAPLQLSQpHHTAYIIFTSGSTGRPKGVMVGQTAIV 624
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
261-612 |
1.62e-04 |
|
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: 44.73 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 261 DDISCIMYTSGSTGDPKGVVLKHsNVVAGvggatinvcDYVGDTDKLICFLPLAHIFEMA---------FELL--SFHWG 329
Cdd:cd05971 88 DDPALIIYTSGTTGPPKGALHAH-RVLLG---------HLPGVQFPFNLFPRDGDLYWTPadwawigglLDVLlpSLYFG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 330 scigyanvktltsASVRNCKSdlEEFQPTIMVGVAAVWetvkkGILNQIneLPRVTKGIFWAAY----HSKLKMQKMGiP 405
Cdd:cd05971 158 -------------VPVLAHRM--TKFDPKAALDLMSRY-----GVTTAF--LPPTALKMMRQQGeqlkHAQVKLRAIA-T 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 406 GGDTIGNIIFKKVRKATGghlryllnggspISVNaqEFISNLICPMLIGyglteTCASLCILNPGHFEYGVVGDltgcvT 485
Cdd:cd05971 215 GGESLGEELLGWAREQFG------------VEVN--EFYGQTECNLVIG-----NCSALFPIKPGSMGKPIPGH-----R 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 486 VKLVDV--EELgyfAKDNKGEIWVK--GENVLPEYYKNEEETKESLTEDgWFKTGDIGMWTDTGSLKIIDRKKNLVKTmN 561
Cdd:cd05971 271 VAIVDDngTPL---PPGEVGEIAVElpDPVAFLGYWNNPSATEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDDVITS-S 345
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2112360039 562 GEYIALEKLESVYRSNSYVQNICVYA--DQNK---VKPVGIIVPNHTPLVKLAKEL 612
Cdd:cd05971 346 GYRIGPAEIEECLLKHPAVLMAAVVGipDPIRgeiVKAFVVLNPGETPSDALAREI 401
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
220-293 |
1.90e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 45.15 E-value: 1.90e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2112360039 220 AQEAVDKIKEVRPDIKLVSFDELLELGQKAKGEiepHPPTR---DDISCIMYTSGSTGDPKGVVLKHSNVVAGVGGA 293
Cdd:PRK12467 615 TQSHLLAQLPVPAGLRSLCLDEPADLLCGYSGH---NPEVAldpDNLAYVIYTSGSTGQPKGVAISHGALANYVCVI 688
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
257-287 |
2.17e-04 |
|
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: 44.19 E-value: 2.17e-04
10 20 30
....*....|....*....|....*....|.
gi 2112360039 257 PPTRDDISCIMYTSGSTGDPKGVVLKHSNVV 287
Cdd:cd17646 134 PPRPDNLAYVIYTSGSTGRPKGVMVTHAGIV 164
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
455-557 |
4.64e-04 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 43.15 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 455 YGLTET-----CASLCILN-PGhfeygVVGDLTGCVTVKLVDvEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLT 528
Cdd:PRK12406 303 YGSTESgavtfATSEDALShPG-----TVGKAAPGAELRFVD-EDGRPLPQGEIGEIYSRIAGNPDFTYHNKPEKRAEID 376
|
90 100
....*....|....*....|....*....
gi 2112360039 529 EDGWFKTGDIGMWTDTGSLKIIDRKKNLV 557
Cdd:PRK12406 377 RGGFITSGDVGYLDADGYLFLCDRKRDMV 405
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
261-602 |
4.88e-04 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 43.19 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 261 DDISCIMYTSGSTGDPKGVVLkhSNVVAGVGGATINVCDYVGDTDKLICFLPL----AHIFEMAFELLSfhwGSCIGYAN 336
Cdd:cd05937 87 DDPAILIYTSGTTGLPKAAAI--SWRRTLVTSNLLSHDLNLKNGDRTYTCMPLyhgtAAFLGACNCLMS---GGTLALSR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 337 vktltSASVRNCKSDLEEFQPTIMVGVAavwetvkkgilnqinELPRVtkgiFWAAYHSKL-KMQKMGIPGGDTIGNIIF 415
Cdd:cd05937 162 -----KFSASQFWKDVRDSGATIIQYVG---------------ELCRY----LLSTPPSPYdRDHKVRVAWGNGLRPDIW 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 416 KKVRKatgghlRYllngGSPIsvnAQEFisnlicpmligYGLTETCASLCILNPGHFEYGVVGD--------LTGCVTVK 487
Cdd:cd05937 218 ERFRE------RF----NVPE---IGEF-----------YAATEGVFALTNHNVGDFGAGAIGHhglirrwkFENQVVLV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 488 LVDVEElGYFAKDNK------------GEIWV----KGENVLPEYYKNEEETKESLTE------DGWFKTGDIGMWTDTG 545
Cdd:cd05937 274 KMDPET-DDPIRDPKtgfcvrapvgepGEMLGrvpfKNREAFQGYLHNEDATESKLVRdvfrkgDIYFRTGDLLRQDADG 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2112360039 546 SLKIIDRkknLVKTM--NGEYIALEKLESVyrsnsyvqnICVYADQNKVKPVGIIVPNH 602
Cdd:cd05937 353 RWYFLDR---LGDTFrwKSENVSTTEVADV---------LGAHPDIAEANVYGVKVPGH 399
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
231-280 |
5.20e-04 |
|
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: 43.46 E-value: 5.20e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2112360039 231 RPDIKLVSFDELLELG-QKAKGEIEPHPPT---RDDISCIMYTSGSTGDPKGVV 280
Cdd:cd05967 196 RPQVPADLTKPGRDLDwSELLAKAEPVDCVpvaATDPLYILYTSGTTGKPKGVV 249
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
261-286 |
5.75e-04 |
|
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: 43.01 E-value: 5.75e-04
10 20
....*....|....*....|....*.
gi 2112360039 261 DDISCIMYTSGSTGDPKGVVLKHSNV 286
Cdd:cd17652 93 DNLAYVIYTSGSTGRPKGVVVTHRGL 118
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
503-557 |
7.19e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 42.76 E-value: 7.19e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2112360039 503 GEIWVKGENVLpEYYKNEEETKESLTEDG-WFKTGDIGMWTDTGSLKIIDRKKNLV 557
Cdd:PRK13391 354 GTIWFEGGRPF-EYLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMI 408
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
454-585 |
7.29e-04 |
|
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: 42.29 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 454 GYGLTETCASLCILNPGHFEYGVVGDLTGCVTVKLVDVE--ELgyfAKDNKGEIWVKGENVLPEYYKNEEETKESlTEDG 531
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDgrEV---PDGEVGEIVARGPTVMAGYWNRPEVNARR-TRGG 217
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2112360039 532 WFKTGDIGMWTDTGSLKIIDRKKNLVKTMnGEYIALEKLESVYRSNSYVQNICV 585
Cdd:cd17636 218 WHHTNDLGRREPDGSLSFVGPKTRMIKSG-AENIYPAEVERCLRQHPAVADAAV 270
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
505-580 |
9.63e-04 |
|
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: 42.42 E-value: 9.63e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2112360039 505 IWVKGENVLPEYYKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVkTMNGEYIALEKLESVYRSNSYV 580
Cdd:cd05915 363 VQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLI-KSGGEWISSVDLENALMGHPKV 437
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
219-315 |
1.25e-03 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 42.17 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 219 EAQEAVDKIKE-VRPDIKLVSFDE--------LLELGQKAKGEIEPHPPTR-----DDISCIMYTSGSTGDPKGVVLKHS 284
Cdd:PRK08279 143 ELVEAFEEARAdLARPPRLWVAGGdtlddpegYEDLAAAAAGAPTTNPASRsgvtaKDTAFYIYTSGTTGLPKAAVMSHM 222
|
90 100 110
....*....|....*....|....*....|...
gi 2112360039 285 NVVAGVG--GATINvcdyVGDTDKLICFLPLAH 315
Cdd:PRK08279 223 RWLKAMGgfGGLLR----LTPDDVLYCCLPLYH 251
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
160-310 |
1.34e-03 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 41.87 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 160 GEKGLIHSLKQTSSAAIFTDNQLL--GKLINplkVAEKIRYVIyydnisaedkrqggKLYREAQEAV---DKIKEVRPDI 234
Cdd:cd05943 158 GVPGVLDRFGQIEPKVLFAVDAYTynGKRHD---VREKVAELV--------------KGLPSLLAVVvvpYTVAAGQPDL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 235 ----KLVSFDELLelGQKAKGEIEPHPPTRDDISCIMYTSGSTGDPKGVVlkHsnvvaGVGGATINV-------CDyVGD 303
Cdd:cd05943 221 skiaKALTLEDFL--ATGAAGELEFEPLPFDHPLYILYSSGTTGLPKCIV--H-----GAGGTLLQHlkehilhCD-LRP 290
|
....*..
gi 2112360039 304 TDKLICF 310
Cdd:cd05943 291 GDRLFYY 297
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
244-315 |
1.36e-03 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 41.64 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 244 ELGQKAKGEIEPHPPTRDDIS-----CIMYTSGSTGDPKGVVLKHSN---VVAGVG-GATINVCDYVGDTdklicfLPLA 314
Cdd:cd05939 82 NLLDPLLTQSSTEPPSQDDVNfrdklFYIYTSGTTGLPKAAVIVHSRyyrIAAGAYyAFGMRPEDVVYDC------LPLY 155
|
.
gi 2112360039 315 H 315
Cdd:cd05939 156 H 156
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
244-284 |
1.99e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 41.28 E-value: 1.99e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2112360039 244 ELGQKAKGEIEPHPPTRDDISCIMYTSGSTGDPKGVVlkHS 284
Cdd:PRK00174 228 ELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGVL--HT 266
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
261-606 |
2.04e-03 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 41.69 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 261 DDISCIMYTSGSTGDPKGVVLKHSNVVAgvggatinvcdyvgdtdkLICFLPLAHIFEMAFELLSFHwgsciGYAnvktl 340
Cdd:PRK12467 1718 QNLAYVIYTSGSTGRPKGAGNRHGALVN------------------RLCATQEAYQLSAADVVLQFT-----SFA----- 1769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 341 TSASVrncksdlEEFQPTIMVG----VAAVWETVKKGILNQINELPRVTKGIFWAAYHSKLkMQKMGIPGGDTigniifk 416
Cdd:PRK12467 1770 FDVSV-------WELFWPLINGarlvIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQL-LQMDEQVEHPL------- 1834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 417 kvrkatggHLRYLLNGGSPISVNAQEFISNLICPMLI--GYGLTETcaslcILNPGHFEYGvVGDLTGCVTVKL-VDVEE 493
Cdd:PRK12467 1835 --------SLRRVVCGGEALEVEALRPWLERLPDTGLfnLYGPTET-----AVDVTHWTCR-RKDLEGRDSVPIgQPIAN 1900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 494 LGYFAKDNK---------GEIWVKGENVLPEYYKNEEETKESLTEDGW-------FKTGDIGMWTDTGSLKIIDRKKNLV 557
Cdd:PRK12467 1901 LSTYILDASlnpvpigvaGELYLGGVGLARGYLNRPALTAERFVADPFgtvgsrlYRTGDLARYRADGVIEYLGRIDHQV 1980
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2112360039 558 KtMNGEYIALEKLESVYRSNSYVQNICVYADQ--NKVKPVGIIVPNHTPLV 606
Cdd:PRK12467 1981 K-IRGFRIELGEIEARLREQGGVREAVVIAQDgaNGKQLVAYVVPTDPGLV 2030
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
252-288 |
2.57e-03 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 41.48 E-value: 2.57e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2112360039 252 EIEPHPptrDDISCIMYTSGSTGDPKGVVLKHSNVVA 288
Cdd:PRK12316 649 GTELNP---ENLAYVIYTSGSTGKPKGAGNRHRALSN 682
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
237-625 |
2.96e-03 |
|
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: 40.94 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 237 VSFDELLElgqKAKGEIE-PHPPTR---DDISCIMYTSGSTGDPKGVvlKHSNVvagvggatinvcdyvgdtdklicfLP 312
Cdd:cd05970 160 IDFRKLIK---NASPDFErPTANSYpcgEDILLVYFSSGTTGMPKMV--EHDFT------------------------YP 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 313 LAHIFEMAF----ELLSFH-------WGSCI-GYANVKTLTSASVrnCKSDLEEFQPtimvgvAAVWETVKKGILNQINE 380
Cdd:cd05970 211 LGHIVTAKYwqnvREGGLHltvadtgWGKAVwGKIYGQWIAGAAV--FVYDYDKFDP------KALLEKLSKYGVTTFCA 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 381 LPRVTKGIFWAAY-HSKLKMQKMGIPGGDTIGNIIFKKVRKATGGHLRYllnggspisvnaqefisnlicpmliGYGLTE 459
Cdd:cd05970 283 PPTIYRFLIREDLsRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLME-------------------------GFGQTE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 460 TcaSLCILNPGHFEY--GVVGDLTGCVTVKLVDVE----ELGyfakdNKGEIWVKGENVLP-----EYYKNEEETKESLt 528
Cdd:cd05970 338 T--TLTIATFPWMEPkpGSMGKPAPGYEIDLIDREgrscEAG-----EEGEIVIRTSKGKPvglfgGYYKDAEKTAEVW- 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 529 EDGWFKTGDIGMWTDTGSLKIIDRKKNLVKTmNGEYIALEKLESVYRSNSYVQNICV--YADQNK---VKPVGIIVPNHT 603
Cdd:cd05970 410 HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKS-SGYRIGPFEVESALIQHPAVLECAVtgVPDPIRgqvVKATIVLAKGYE 488
|
410 420
....*....|....*....|..
gi 2112360039 604 PLVKLAKELGIMKKQETdiEPY 625
Cdd:cd05970 489 PSEELKKELQDHVKKVT--APY 508
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
100-283 |
4.27e-03 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 40.17 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 100 TFTEVIEVMHSVGRGLVKLGMepKSEDKLHIFAATSHKWMKMFLGAQSQGIPIVTAYDTLGEKGLIHSLKQTSSAAIFTD 179
Cdd:cd05968 93 TYGELLYEVKRLANGLRALGV--GKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 180 NQLL--GKLINPLKVAEKIRyviyydnisaedkrqggklyrEAQEAVDKIKEVR---PDIKLVSFDELLELGQKAKGEIE 254
Cdd:cd05968 171 DGFTrrGREVNLKEEADKAC---------------------AQCPTVEKVVVVRhlgNDFTPAKGRDLSYDEEKETAGDG 229
|
170 180
....*....|....*....|....*....
gi 2112360039 255 PHPPTRDDISCIMYTSGSTGDPKGVVLKH 283
Cdd:cd05968 230 AERTESEDPLMIIYTSGTTGKPKGTVHVH 258
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
499-585 |
4.48e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 40.15 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 499 KDNKGEIWVKGenvlPEY---YKNEEETKESLTEDGWFKTGDIGMWTDTGSLKIIDRKKNLVkTMNGEYIALEKLESVYR 575
Cdd:PRK07638 330 KGEIGTVYVKS----PQFfmgYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIESVLH 404
|
90
....*....|
gi 2112360039 576 SNSYVQNICV 585
Cdd:PRK07638 405 EHPAVDEIVV 414
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
262-287 |
5.28e-03 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 39.69 E-value: 5.28e-03
10 20
....*....|....*....|....*.
gi 2112360039 262 DISCIMYTSGSTGDPKGVVLKHSNVV 287
Cdd:cd17648 95 DLAYAIYTSGTTGKPKGVLVEHGSVV 120
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
251-601 |
5.88e-03 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 40.14 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 251 GEIEPHPPTR---DDISCIMYTSGSTGDPKGVVLKHsnvvagvgGATINVCdyvgdtdklicflplaHIFEMAFELlsfh 327
Cdd:PRK12467 3224 GYSENNPSTRvmgENLAYVIYTSGSTGKPKGVGVRH--------GALANHL----------------CWIAEAYEL---- 3275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 328 wgscigYANVKTLTSASVrNCKSDLEEFQPTIMVG----VAA--VWETVKkgILNQINElPRVTKGIFWAAYhsklkMQK 401
Cdd:PRK12467 3276 ------DANDRVLLFMSF-SFDGAQERFLWTLICGgclvVRDndLWDPEE--LWQAIHA-HRISIACFPPAY-----LQQ 3340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 402 MGIPGGdtigniifkkvrKATGGHLRYLLNGGSPISVNAQEFISNLICPMLI--GYGLTEtcaslCILNPGHFEYGV--- 476
Cdd:PRK12467 3341 FAEDAG------------GADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLtnGYGPTE-----AVVTVTLWKCGGdav 3403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112360039 477 -------VGDLTGCVTVKLVDvEELGYFAKDNKGEIWVKGENVLPEYYKNEEETKESLTEDGW-------FKTGDIGMWT 542
Cdd:PRK12467 3404 ceapyapIGRPVAGRSIYVLD-GQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFsgsggrlYRTGDLARYR 3482
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2112360039 543 DTGSLKIIDRKKNLVKtMNGEYIALEKLESVYRSNSYVQNICVYA--DQNKVKPVGIIVPN 601
Cdd:PRK12467 3483 ADGVIEYLGRIDHQVK-IRGFRIELGEIEARLLQHPSVREAVVLArdGAGGKQLVAYVVPA 3542
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
244-290 |
6.59e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 39.66 E-value: 6.59e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2112360039 244 ELGQKAKGEIEPHPPTRDDISCIMYTSGSTGDPKGVVLKHSNV-VAGV 290
Cdd:PRK07867 135 ELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVaSAGV 182
|
|
| |
