|
Name |
Accession |
Description |
Interval |
E-value |
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
81-619 |
0e+00 |
|
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: 841.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 81 QPYQWLSYQEVADRAEFLGSGLLQHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADI 160
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 161 STVIVDKpqkavlllehverketpglkliilmdpfeealkergqkcGVVIKSMQAVEDCGQENHQAPVPPQPDDLSIVCF 240
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 241 TSGTTGNPKGAMLTHGNVVADFSGFLKVTE----------------------------------------GDIRLLSDDM 280
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEilnkinptdvyisylplahifervvealflyhgakigfysGDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 281 KALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWLLEFAAKRKQAEVRSGIIRNDSIWDELFFNKIQASLGGCVRMIVT 358
Cdd:cd05927 202 KALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 359 GAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWA--CKGEGEICVR 436
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAkdPNPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 437 GPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGD 516
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 517 SLKAFLVGIVVPDPEVMPSWA-QKRGIEGTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLL 595
Cdd:cd05927 442 SLKSFLVAIVVPDPDVLKEWAaSKGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|....
gi 327412329 596 TPTLKAKRPELREYFKKQIEELYS 619
Cdd:cd05927 522 TPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
37-619 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 647.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 37 RSViGSGPQLLTHY--YDDARTMYQVFRRGLSISGNGPCLGFRKPKQ----PYQWLSYQEVADRAEFLGSGLLQHNCK-- 108
Cdd:PLN02736 25 RSA-RSPLKLVSRFpdHPEIGTLHDNFVYAVETFRDYKYLGTRIRVDgtvgEYKWMTYGEAGTARTAIGSGLVQHGIPkg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 109 ACtdqfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVdKPQKAVLLLEHVerKETPGLKL 188
Cdd:PLN02736 104 AC----VGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCL--SEIPSVRL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 189 IILMDPFEEALKERGQKCGVVIKSMQAVEDCGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKV 268
Cdd:PLN02736 177 IVVVGGADEPLPSLPSGTGVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 269 TE------------------------------------GDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QANTPL 310
Cdd:PLN02736 257 TKfypsdvhisylplahiyervnqivmlhygvavgfyqGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNavKESGGL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 311 KRWLLEFAAKRKQAEVRSGiiRNDS-IWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECT 389
Cdd:PLN02736 337 KERLFNAAYNAKKQALENG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETS 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 390 AGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKG---EGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDI 466
Cdd:PLN02736 415 CVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDI 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 467 GKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGIE-GT 545
Cdd:PLN02736 495 GLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyED 574
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 327412329 546 YADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 619
Cdd:PLN02736 575 LKQLCNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYA 648
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
51-619 |
2.21e-162 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 477.67 E-value: 2.21e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 51 YDDARTMYQVFRRGLSISGNGPCLGFRKPKQpYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVEL 130
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVALREKEDGI-WQSLTWAEFAERVRALAAGLLALGVKP--GDRVAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 131 ACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAVLLLEHveRKETPGLKLIILMDPfeealkeRGQKCGVVI 210
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEV--RDELPSLRHIVVLDP-------RGLRDDPRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 211 KSMQAVEDCGQE-NHQAPVP-----PQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTEGD--------- 272
Cdd:COG1022 155 LSLDELLALGREvADPAELEarraaVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARAlleRLPLGPGDrtlsflpla 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 273 -----------------------IRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQAN--TPLKRWLLEFA---AKRKQA 324
Cdd:COG1022 235 hvfertvsyyalaagatvafaesPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEeaGGLKRKLFRWAlavGRRYAR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 325 EVRSGiiRNDSIW--------DELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTT 396
Cdd:COG1022 315 ARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPVITVNR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 397 PGDWTSGHVGAPLPCNHIKLVDveelnywackgEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLK 476
Cdd:COG1022 392 PGDNRIGTVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLR 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 477 IIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKaFLVGIVVPDPEVMPSWAQKRGIE-GTYADLCTNKDL 555
Cdd:COG1022 461 ITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDGRP-FLAALIVPDFEALGEWAEENGLPyTSYAELAQDPEV 539
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 327412329 556 KKAILEDMVRLGKesGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 619
Cdd:COG1022 540 RALIQEEVDRANA--GLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYA 601
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
81-606 |
2.92e-143 |
|
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: 423.54 E-value: 2.92e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 81 QPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADI 160
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEP--GDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 161 STVIVDKPqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhqapvppqpDDLSIVCF 240
Cdd:cd05907 79 KALFVEDP----------------------------------------------------------------DDLATIIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 241 TSGTTGNPKGAMLTHGNVVADFSGFLKV---TEGDIRL---------------------------------LSDDMKALC 284
Cdd:cd05907 95 TSGTTGRPKGVMLSHRNILSNALALAERlpaTEGDRHLsflplahvferraglyvpllagariyfassaetLLDDLSEVR 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 285 PTIFPVVPRLLNRMYDKIFSQANTPLKRWLLEFAAkrkqaevrsgiirndsiwdelffnkiqaslGGCVRMIVTGAAPAS 364
Cdd:cd05907 175 PTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV------------------------------GGRLRFAASGGAPLP 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 365 PTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveelnywackgEGEICVRGPNVFKGY 444
Cdd:cd05907 225 AELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPNVMLGY 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 445 LKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKaFLVG 524
Cdd:cd05907 293 YKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDGRP-FLVA 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 525 IVVPDPEVMPSWAQKRGIEG-TYADLCTNKDLKKAILEDMVRLGKEsgLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKR 603
Cdd:cd05907 372 LIVPDPEALEAWAEEHGIAYtDVAELAANPAVRAEIEAAVEAANAR--LSRYEQIKKFLLLPEPFTIENGELTPTLKLKR 449
|
...
gi 327412329 604 PEL 606
Cdd:cd05907 450 PVI 452
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
82-603 |
1.68e-136 |
|
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: 408.14 E-value: 1.68e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 82 PYQWLSYQEVADRAEFLGSGL----LQHNCKactdqfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINT 157
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLvelgLKPGDK------VAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 158 ADISTVIVDkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhqapvpPQPDDLSI 237
Cdd:cd17639 76 TECSAIFTD---------------------------------------------------------------GKPDDLAC 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 238 VCFTSGTTGNPKGAMLTHGNVVADFSG-------FLKVTE-----------------------------GDIRLLSDDMK 281
Cdd:cd17639 93 IMYTSGSTGNPKGVMLTHGNLVAGIAGlgdrvpeLLGPDDrylaylplahifelaaenvclyrggtigyGSPRTLTDKSK 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 282 ALC--------PTIFPVVPRLLNRMYDKIFSQANTP--LKRWLLEFAAKRKQAEVRSGIirnDS-IWDELFFNKIQASLG 350
Cdd:cd17639 173 RGCkgdltefkPTLMVGVPAIWDTIRKGVLAKLNPMggLKRTLFWTAYQSKLKALKEGP---GTpLLDELVFKKVRAALG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 351 GCVRMIVTGAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKGE 430
Cdd:cd17639 250 GRLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKPP 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 431 --GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPV 508
Cdd:cd17639 329 prGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLV 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 509 AQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRG-IEGTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDM 587
Cdd:cd17639 409 NNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGvINSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEE 488
|
570
....*....|....*.
gi 327412329 588 FSVQNGLLTPTLKAKR 603
Cdd:cd17639 489 WTPENGLVTAAQKLKR 504
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
53-618 |
2.31e-133 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 405.35 E-value: 2.31e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 53 DARTMYQVFRRGLSISGNGPCLGFRKPKQ----PYQWLSYQEVADRAEFLGSGLLQHNCKACTDqfIGVFAQNRPEWIIV 128
Cdd:PLN02430 40 DITTAWDIFSKSVEKYPDNKMLGWRRIVDgkvgPYMWKTYKEVYEEVLQIGSALRASGAEPGSR--VGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 129 ELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV-DKPQKAVLlleHVERKETPGLKLIILMDPFEEALKERGQKCG 207
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVqDKKIKELL---EPDCKSAKRLKAIVSFTSVTEEESDKASQIG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 208 VVIKSMQAVEDCGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG--------------------FLK 267
Cdd:PLN02430 195 VKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGvdlfmeqfedkmthddvylsFLP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 268 VTE---------------------GDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWLLEFAAKRKQA 324
Cdd:PLN02430 275 LAHildrmieeyffrkgasvgyyhGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYKLA 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 325 EVRSGIIRNDS--IWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS 402
Cdd:PLN02430 355 WMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMCM 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 403 -GHVGAPLPCNHIKLVDVEELNY--WACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIID 479
Cdd:PLN02430 435 lGTVGAPAVYNELRLEEVPEMGYdpLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIID 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 480 RKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGIEGTYADLCTNKDLKKAI 559
Cdd:PLN02430 514 RKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKEHI 593
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 327412329 560 LEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 618
Cdd:PLN02430 594 LSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMY 652
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
82-619 |
7.00e-133 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 404.22 E-value: 7.00e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 82 PYQWLSYQEVADRAEFLGSGLLQ------HNCkactdqfiGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYII 155
Cdd:PLN02861 74 PYVWLTYKEVYDAAIRIGSAIRSrgvnpgDRC--------GIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFII 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 156 NTADISTVIVDKPQKAVLLleHVERKETPGLKLIILMDPFEEALKERGQKCGVVIKSMQAVEDCGQENHQAPvPPQPDDL 235
Cdd:PLN02861 146 NHAEVSIAFVQESKISSIL--SCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELP-PKQKTDI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 236 SIVCFTSGTTGNPKGAMLTHGNVVADF---SGFLKVTE--------------------------------------GDIR 274
Cdd:PLN02861 223 CTIMYTSGTTGEPKGVILTNRAIIAEVlstDHLLKVTDrvateedsyfsylplahvydqvietyciskgasigfwqGDIR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 275 LLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWLLEFAAKRKQAEVRSGIIRNDS--IWDELFFNKIQASLG 350
Cdd:PLN02861 303 YLMEDVQALKPTIFCGVPRVYDRIYTGIMQkiSSGGMLRKKLFDFAYNYKLGNLRKGLKQEEAspRLDRLVFDKIKEGLG 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 351 GCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCtFTTPGDWTS--GHVGAPLPCNHIKLVDVEELNYWACK 428
Cdd:PLN02861 383 GRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGC-FTSIANVFSmvGTVGVPMTTIEARLESVPEMGYDALS 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 429 G--EGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQ 506
Cdd:PLN02861 462 DvpRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCP 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 507 PVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGIEGTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSD 586
Cdd:PLN02861 541 LIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPN 620
|
570 580 590
....*....|....*....|....*....|...
gi 327412329 587 MFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 619
Cdd:PLN02861 621 PFDIERDLITPTFKLKRPQLLKYYKDCIDQLYS 653
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
52-618 |
1.28e-131 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 400.94 E-value: 1.28e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 52 DDARTMYQVFRRGLSISGNGPCLGFR-----KPKQpYQWLSYQEVADRAEFLGSGLlqHNCKACTDQFIGVFAQNRPEWI 126
Cdd:PLN02614 42 EGMDSCWDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQEVYDIVIKLGNSL--RSVGVKDEAKCGIYGANSPEWI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 127 IVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDkpQKAVLLLEHVERKETPGLKLIILMDPFEEALKERGQKC 206
Cdd:PLN02614 119 ISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVE--EKKISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 207 GVVIKSMQAVEDCGqENHQAPVP-PQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG--------------------- 264
Cdd:PLN02614 197 GLVIYAWDEFLKLG-EGKQYDLPiKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGvirllksanaaltvkdvylsy 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 265 ------FLKVTE--------------GDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTP--LKRWLLEFAAKRK 322
Cdd:PLN02614 276 lplahiFDRVIEecfiqhgaaigfwrGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSAFSYK 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 323 QAEVRSGI--IRNDSIWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDW 400
Cdd:PLN02614 356 FGNMKKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDEL 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 401 TS-GHVGAPLPCNHIKLVDVEELNY--WACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKI 477
Cdd:PLN02614 436 DMlGTVGPPVPNVDIRLESVPEMEYdaLASTPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKI 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 478 IDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGIEGTYADLCTNKDLKK 557
Cdd:PLN02614 515 IDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKE 594
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 327412329 558 AILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 618
Cdd:PLN02614 595 FILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMY 655
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
44-619 |
1.13e-120 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 373.68 E-value: 1.13e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 44 PQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRK--PKQ----------------PYQWLSYQEVADRAEFLGSGLLQ- 104
Cdd:PLN02387 47 PELVETPWEGATTLAALFEQSCKKYSDKRLLGTRKliSREfetssdgrkfeklhlgEYEWITYGQVFERVCNFASGLVAl 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 105 -HNckacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQ--KAVLLLEHVERk 181
Cdd:PLN02387 127 gHN----KEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQlkKLIDISSQLET- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 182 etpgLKLIILM-DPFEEALKERGQKCGVVIKSMQAVEDCGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVA 260
Cdd:PLN02387 202 ----VKRVIYMdDEGVDSDSSLSGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 261 DFSGFLKVTEG----DIRL-------------------------------LSD-----------DMKALCPTIFPVVPRL 294
Cdd:PLN02387 278 TVAGVMTVVPKlgknDVYLaylplahilelaaesvmaavgaaigygspltLTDtsnkikkgtkgDASALKPTLMTAVPAI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 295 LNRMYDKIFSQANTP--LKRWLLEFAAKRKQAEVR------SGIIRndSIWDELFFNKIQASLGGCVRMIVTGAAPASPT 366
Cdd:PLN02387 358 LDRVRDGVRKKVDAKggLAKKLFDIAYKRRLAAIEgswfgaWGLEK--LLWDALVFKKIRAVLGGRIRFMLSGGAPLSGD 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 367 VLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKG---EGEICVRGPNVFKG 443
Cdd:PLN02387 436 TQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLISDKpmpRGEIVIGGPSVTLG 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 444 YLKDPDRTKEA--LDSDG--WLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLK 519
Cdd:PLN02387 516 YFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIMVHADPFH 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 520 AFLVGIVVPDPEVMPSWAQKRGIE-GTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPT 598
Cdd:PLN02387 596 SYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKIKLLPEPWTPESGLVTAA 675
|
650 660
....*....|....*....|.
gi 327412329 599 LKAKRPELREYFKKQIEELYS 619
Cdd:PLN02387 676 LKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
82-488 |
2.53e-110 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 337.75 E-value: 2.53e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 82 PYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADIS 161
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGVGK--GDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 162 TVIVDKPQKAVLLLEHVERKETPGLKLIILMDPFEEALKergqkcgvviksMQAVEDCGQENHQAPVPPQPDDLSIVCFT 241
Cdd:pfam00501 96 VLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEP------------LPEEAKPADVPPPPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 242 SGTTGNPKGAMLTHGNVVA-----------------------------DFS------GFL----------KVTEGDIRLL 276
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNLVAnvlsikrvrprgfglgpddrvlstlplfhDFGlslgllGPLlagatvvlppGFPALDPAAL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 277 SDDMKALCPTIFPVVPRLLNRMydkifsqantplkrwlleFAAKRKQAEVRSGiirndsiwdelffnkiqaslggcVRMI 356
Cdd:pfam00501 244 LELIERYKVTVLYGVPTLLNML------------------LEAGAPKRALLSS-----------------------LRLV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 357 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDW---TSGHVGAPLPCNHIKLVDVEELNYWACKGEGEI 433
Cdd:pfam00501 283 LSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGEL 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 327412329 434 CVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLA 488
Cdd:pfam00501 363 CVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
47-618 |
1.90e-85 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 281.48 E-value: 1.90e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 47 LTHYYDDARTMYQVFRRGLSISGNGPCLGFRKPK--------------QPY--------QWLSYQEVADRAEFLGSGL-- 102
Cdd:PTZ00216 61 LRNEWYYGPNFLQRLERICKERGDRRALAYRPVErvekevvkdadgkeRTMevthfnetRYITYAELWERIVNFGRGLae 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 103 --LQHNCKactdqfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADiSTVIVDKPQKAVLLLEHVER 180
Cdd:PTZ00216 141 lgLTKGSN------VAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETE-CKAIVCNGKNVPNLLRLMKS 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 181 KETPGLKLIILmdpfeEALKERGQKCGVVIKSMQAVEDCG---QENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGN 257
Cdd:PTZ00216 214 GGMPNTTIIYL-----DSLPASVDTEGCRLVAWTDVVAKGhsaGSHHPLNIPENNDDLALIMYTSGTTGDPKGVMHTHGS 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 258 VVA----------DFSGFLKVTE-----------------------------GDIRLLSD-------DMKALCPTIFPVV 291
Cdd:PTZ00216 289 LTAgilaledrlnDLIGPPEEDEtycsylplahimefgvtniflargaligfGSPRTLTDtfarphgDLTEFRPVFLIGV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 292 PRLLNRMydKIFSQANTP----LKRWLLEFAAKRKQAEVRSGiiRNDSIWDELFFNKIQASLGGCVRMIVTGAAPASPTV 367
Cdd:PTZ00216 369 PRIFDTI--KKAVEAKLPpvgsLKRRVFDHAYQSRLRALKEG--KDTPYWNEKVFSAPRAVLGGRVRAMLSGGGPLSAAT 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 368 LGFLRAALGCqVYEGYGQTE--CTAGCTFTtpGDWTSGHVGAPLPCNHIKLVDVEELNYwACKGE--GEICVRGPNVFKG 443
Cdd:PTZ00216 445 QEFVNVVFGM-VIQGWGLTEtvCCGGIQRT--GDLEPNAVGQLLKGVEMKLLDTEEYKH-TDTPEprGEILLRGPFLFKG 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 444 YLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQ----IYVHGDslK 519
Cdd:PTZ00216 521 YYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALYGQNELVVPngvcVLVHPA--R 598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 520 AFLVGIVVPDPEVMPSWAQKRGIEGTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTL 599
Cdd:PTZ00216 599 SYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFEIVRHVRVLSDEWTPENGVLTAAM 678
|
650
....*....|....*....
gi 327412329 600 KAKRPELREYFKKQIEELY 618
Cdd:PTZ00216 679 KLKRRVIDERYADLIKELF 697
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
81-604 |
1.76e-70 |
|
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: 235.33 E-value: 1.76e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 81 QPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADI 160
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKA--GEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 161 STVIVdkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqENHqapvppqPDDLSIVCF 240
Cdd:cd17640 79 VALVV--------------------------------------------------------END-------SDDLATIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 241 TSGTTGNPKGAMLTHGNV---VADFSGFLKVTEGD-------------------------------IRLLSDDMKALCPT 286
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLlhqIRSLSDIVPPQPGDrflsilpiwhsyersaeyfifacgcsqaytsIRTLKDDLKRVKPH 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 287 IFPVVPRLLNRMYDKIFSQ--ANTPLKRWLLEFAAkrkqaevrsgiirndsiwdelffnkiqasLGGCVRMIVTGAAPAS 364
Cdd:cd17640 176 YIVSVPRLWESLYSGIQKQvsKSSPIKQFLFLFFL-----------------------------SGGIFKFGISGGGALP 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 365 PTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGY 444
Cdd:cd17640 227 PHVDTFFEA-IGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGY 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 445 LKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKaFLVG 524
Cdd:cd17640 306 YKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQK-RLGA 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 525 IVVPDPEVMPSWAQKRGI---EGTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFsVQNGLLTPTLKA 601
Cdd:cd17640 385 LIVPNFEELEKWAKESGVklaNDRSQLLASKKVLKLYKNEIKDEISNRPGFKSFEQIAPFALLEEPF-IENGEMTQTMKI 463
|
...
gi 327412329 602 KRP 604
Cdd:cd17640 464 KRN 466
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
83-603 |
1.07e-68 |
|
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: 231.97 E-value: 1.07e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 83 YQWLSYQEVADRAEFLGSGLLQHNCKACTDqfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADIST 162
Cdd:cd05932 4 VVEFTWGEVADKARRLAAALRALGLEPGSK--IALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 163 VIVDKpqkavllLEHVERKE--TPGLKLIILMDPFEEALKERGqkcgvviksMQAVEDCGQENHQAPvPPQPDDLSIVCF 240
Cdd:cd05932 82 LFVGK-------LDDWKAMApgVPEGLISISLPPPSAANCQYQ---------WDDLIAQHPPLEERP-TRFPEQLATLIY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 241 TSGTTGNPKGAMLTHGNVVADFSGFLKV--TEGDIRLLS----------------------------------DDMKALC 284
Cdd:cd05932 145 TSGTTGQPKGVMLTFGSFAWAAQAGIEHigTEENDRMLSylplahvtervfveggslyggvlvafaesldtfvEDVQRAR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 285 PTIFPVVPRLL----NRMYDKIFSQAntpLKRWLlefaakrkQAEVRSGIIRndsiwdelffNKIQASLG-GCVRMIVTG 359
Cdd:cd05932 225 PTLFFSVPRLWtkfqQGVQDKIPQQK---LNLLL--------KIPVVNSLVK----------RKVLKGLGlDQCRLAGCG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 360 AAPASPTVLGFLRaALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveelnywackgEGEICVRGPN 439
Cdd:cd05932 284 SAPVPPALLEWYR-SLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEILVRSPA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 440 VFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLK 519
Cdd:cd05932 352 LMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSGLP 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 520 AfLVGIVVPDPEVMPSwaqkrgiegtyADLCTNKDLKKAILEDMVRLGKEsgLHSFEQVKAIHIHSDMFSVQNGLLTPTL 599
Cdd:cd05932 432 A-PLALVVLSEEARLR-----------ADAFARAELEASLRAHLARVNST--LDSHEQLAGIVVVKDPWSIDNGILTPTL 497
|
....
gi 327412329 600 KAKR 603
Cdd:cd05932 498 KIKR 501
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
57-530 |
6.54e-61 |
|
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: 209.28 E-value: 6.54e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 57 MYQVFRRGLSISGNGPCLGFRkpkqpYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYS 136
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG-----GRRLTYAELDARARRLAAALRALGVGP--GDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 137 MVVVPLYDTLGPGAIRYIINTADISTVIVdkpqkAVLLlehverketpglkliilmdpfeealkergqkcgvviksmqav 216
Cdd:COG0318 74 AVVVPLNPRLTAEELAYILEDSGARALVT-----ALIL------------------------------------------ 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 217 edcgqenhqapvppqpddlsivcFTSGTTGNPKGAMLTHGNVVA---DFSGFLKVTEGDiRLLS---------------- 277
Cdd:COG0318 107 -----------------------YTSGTTGRPKGVMLTHRNLLAnaaAIAAALGLTPGD-VVLValplfhvfgltvglla 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 278 --------------------DDMKALCPTIFPVVPRLLNRMYDkifsqantplkrwllefAAKRKQAEVRSgiirndsiw 337
Cdd:COG0318 163 pllagatlvllprfdpervlELIERERVTVLFGVPTMLARLLR-----------------HPEFARYDLSS--------- 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 338 delffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPCNHIK 415
Cdd:COG0318 217 ---------------LRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGRPLPGVEVR 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 416 LVDVE--ELnywACKGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYV 493
Cdd:COG0318 282 IVDEDgrEL---PPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENV 356
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 327412329 494 APEKIENIYIRSQPVAQIYV-------HGDSLKAFlvgiVVPDP 530
Cdd:COG0318 357 YPAEVEEVLAAHPGVAEAAVvgvpdekWGERVVAF----VVLRP 396
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
78-618 |
3.59e-60 |
|
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: 211.06 E-value: 3.59e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 78 KPKQPYQWLSYQEVADRAE-----FLGSGLLQHNCkactdqfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIR 152
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRqaakaFLKLGLERFHG-------VGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 153 YIINTADISTVIVDKPQKAVLLLEhvERKETPGLKLII-LMDPFEEalKERGQKcgvvikSMQAVEDCG-----QENHQA 226
Cdd:cd05933 74 YVAETSEANILVVENQKQLQKILQ--IQDKLPHLKAIIqYKEPLKE--KEPNLY------SWDEFMELGrsipdEQLDAI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 227 PVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG------FLKVTEG------------------DIRL------- 275
Cdd:cd05933 144 ISSQKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAasqhmdLRPATVGqesvvsylplshiaaqilDIWLpikvggq 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 276 ------------LSDDMKALCPTIFPVVPRLLNRMYDKI---FSQAnTPLKRWLLEFAaKRKQAEV-------RSGIIRN 333
Cdd:cd05933 224 vyfaqpdalkgtLVKTLREVRPTAFMGVPRVWEKIQEKMkavGAKS-GTLKRKIASWA-KGVGLETnlklmggESPSPLF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 334 DSIWDELFFNKIQASLG--GCVRMIvTGAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPC 411
Cdd:cd05933 302 YRLAKKLVFKKVRKALGldRCQKFF-TGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 412 NHIKLVDVEelnywaCKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGE 491
Cdd:cd05933 380 CKTKIHNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGE 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 492 YVAPEKIENIYIRSQP-VAQIYVHGDSLKaFLVGIVV------PD---------PEVMpSWAQKRGIEGTY-ADLCTNKD 554
Cdd:cd05933 454 NVPPVPIEDAVKKELPiISNAMLIGDKRK-FLSMLLTlkcevnPEtgepldeltEEAI-EFCRKLGSQATRvSEIAGGKD 531
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 327412329 555 LK--KAILEDMVRLGKESGLHSFEQVKAIHIHSDmFSVQNGLLTPTLKAKRPELREYFKKQIEELY 618
Cdd:cd05933 532 PKvyEAIEEGIKRVNKKAISNAQKIQKWVILEKD-FSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
86-540 |
4.43e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 206.29 E-value: 4.43e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 165
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGK-GDR-VAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 166 -------DKPQKAVL-LLEHVERKETP-GLKLIILMDPFEEALKergqkcgvviksmqavedCGQENHQAPvPPQPDDLS 236
Cdd:PRK07656 109 lglflgvDYSATTRLpALEHVVICETEeDDPHTEKMKTFTDFLA------------------AGDPAERAP-EVDPDDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 237 IVCFTSGTTGNPKGAMLTHGNV---VADFSGFLKVTEGDiRLLS--------------------------------DDMK 281
Cdd:PRK07656 170 DILFTSGTTGRPKGAMLTHRQLlsnAADWAEYLGLTEGD-RYLAanpffhvfgykagvnaplmrgatilplpvfdpDEVF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 282 ALC----PTIFPVVPRLLNRMYDkifsqantplkrwllefAAKRKQAEVRSgiirndsiwdelffnkiqaslggcVRMIV 357
Cdd:PRK07656 249 RLIeterITVLPGPPTMYNSLLQ-----------------HPDRSAEDLSS------------------------LRLAV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 358 TGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGCTFTTPGD---WTSGHVGAPLPCNHIKLVDveELNYWACKGE-GE 432
Cdd:PRK07656 288 TGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAGVENKIVN--ELGEEVPVGEvGE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 433 ICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIY 512
Cdd:PRK07656 366 LLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGFNVYPAEVEEVLYEHPAVAEAA 444
|
490 500 510
....*....|....*....|....*....|....*...
gi 327412329 513 V-------HGDSLKAFLV---GIVVPDPEVMpSWAQKR 540
Cdd:PRK07656 445 VigvpderLGEVGKAYVVlkpGAELTEEELI-AYCREH 481
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
83-569 |
1.89e-57 |
|
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: 203.04 E-value: 1.89e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 83 YQWLSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADIST 162
Cdd:cd17641 9 WQEFTWADYADRVRAFALGLLALGVG--RGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 163 VIVDKPQKAVLLLEHveRKETPGLKLIILMDP------------FEEALKERGQkcgvvikSMQAVEDCGQENHQAPVpp 230
Cdd:cd17641 87 VIAEDEEQVDKLLEI--ADRIPSVRYVIYCDPrgmrkyddprliSFEDVVALGR-------ALDRRDPGLYEREVAAG-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 231 QPDDLSIVCFTSGTTGNPKGAMLTHGNVV---------------ADFSGFL--------------KVTEGDI-------R 274
Cdd:cd17641 156 KGEDVAVLCTTSGTTGKPKLAMLSHGNFLghcaaylaadplgpgDEYVSVLplpwigeqmysvgqALVCGFIvnfpeepE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 275 LLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWL--------LEFAAKRKQAEVRSGIIRNDS-IWDELFFN 343
Cdd:cd17641 236 TMMEDLREIGPTFVLLPPRVWEGIAADVRArmMDATPFKRFMfelgmklgLRALDRGKRGRPVSLWLRLASwLADALLFR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 344 KIQASLG-GCVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTEcTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDVee 421
Cdd:cd17641 316 PLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTE-LAGAYTVHRdGDVDPDTVGVPFPGTEVRIDEV-- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 422 lnywackgeGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENI 501
Cdd:cd17641 392 ---------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENK 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 327412329 502 YIRSQPVAQIYVHGDSlKAFLVGIVVPDPEVMPSWAQKRGIE-GTYADLCTNKDLKKAILEDMVRLGKE 569
Cdd:cd17641 463 LKFSPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKVNAS 530
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
86-596 |
7.92e-56 |
|
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: 198.83 E-value: 7.92e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLGSgllQHNCKACTD--QFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTV 163
Cdd:cd17632 68 ITYAELWERVGAVAA---AHDPEQPVRpgDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 164 IVDKPQKAV---LLLEHverketPGLKLIILMDPFEEALKER-----------GQKCGVVIKSMQAVEDCGQENHQAPVP 229
Cdd:cd17632 145 AVSAEHLDLaveAVLEG------GTPPRLVVFDHRPEVDAHRaalesarerlaAVGIPVTTLTLIAVRGRDLPPAPLFRP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 230 PQPDD-LSIVCFTSGTTGNPKGAMLTHgNVVADF--------------------------------SGFLK-------VT 269
Cdd:cd17632 219 EPDDDpLALLIYTSGSTGTPKGAMYTE-RLVATFwlkvssiqdirppasitlnfmpmshiagrislYGTLArggtayfAA 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 270 EGDIRLLSDDMKALCPTIFPVVPRLlnrmYDKIFSQANTPLKRWL-----LEFAAKRKQAEVRsgiirndsiwdelffnk 344
Cdd:cd17632 298 ASDMSTLFDDLALVRPTELFLVPRV----CDMLFQRYQAELDRRSvagadAETLAERVKAELR----------------- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 345 iQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTtpgdwtSGHVGAPlPCNHIKLVDVEELNY 424
Cdd:cd17632 357 -ERVLGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE--AGAVIL------DGVIVRP-PVLDYKLVDVPELGY 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 425 WACKG---EGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENI 501
Cdd:cd17632 427 FRTDRphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAV 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 502 YIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMpswaqkrgiegtyaDLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAI 581
Cdd:cd17632 507 FAASPLVRQIFVYGNSERAYLLAVVVPTQDAL--------------AGEDTARLRAALAESLQRIAREAGLQSYEIPRDF 572
|
570
....*....|....*
gi 327412329 582 HIHSDMFSVQNGLLT 596
Cdd:cd17632 573 LIETEPFTIANGLLS 587
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
86-603 |
4.65e-55 |
|
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: 193.81 E-value: 4.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLgSGLLQHNCKACTDQfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 165
Cdd:cd05914 8 LTYKDLADNIAKF-ALLLKINGVGTGDR-VALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 166 DKPqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhqapvppqpDDLSIVCFTSGTT 245
Cdd:cd05914 86 SDE----------------------------------------------------------------DDVALINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 246 GNPKGAMLTHGNVVADFSG---FLKVTEGDIRLlsddmkALCPT--IFPVVPRLLNRMY-------------DKIFSQAN 307
Cdd:cd05914 102 GNSKGVMLTYRNIVSNVDGvkeVVLLGKGDKIL------SILPLhhIYPLTFTLLLPLLngahvvfldkipsAKIIALAF 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 308 ---TPL----KRWLLEfaAKRKQAEVRS-----------GIIRNDSIWdELFFNKIQASLGGCVRMIVTGAAPASPTVLG 369
Cdd:cd05914 176 aqvTPTlgvpVPLVIE--KIFKMDIIPKltlkkfkfklaKKINNRKIR-KLAFKKVHEAFGGNIKEFVIGGAKINPDVEE 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 370 FLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPlpcnhIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPD 449
Cdd:cd05914 253 FLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKV-----IDGVEVRIDSPDPATGEGEIIVRGPNVMKGYYKNPE 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 450 RTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVA--QIYVHGDSLKAflvgIVV 527
Cdd:cd05914 327 ATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLesLVVVQEKKLVA----LAY 402
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 327412329 528 PDPEVMPSWAQKrgiegtyadlctNKDLKKAILEDmVRLGKESGLHSFEQVKAIHIHSDMFSVqngllTPTLKAKR 603
Cdd:cd05914 403 IDPDFLDVKALK------------QRNIIDAIKWE-VRDKVNQKVPNYKKISKVKIVKEEFEK-----TPKGKIKR 460
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
58-523 |
6.00e-52 |
|
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: 185.46 E-value: 6.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 58 YQVFRRGLSISGNGPCLGFRKpkqpyQWLSYQEVADRAEFLGSGLLQHNCKaCTDQfIGVFAQNRPEWIIVELACYTYSM 137
Cdd:cd05936 2 ADLLEEAARRFPDKTALIFMG-----RKLTYRELDALAEAFAAGLQNLGVQ-PGDR-VALMLPNCPQFPIAYFGALKAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 138 VVVPLYDTLGPGAIRYIINTADISTVIVDkpqkavlllehverketpglkliilmDPFEEALKergqkcgvviksmqave 217
Cdd:cd05936 75 VVVPLNPLYTPRELEHILNDSGAKALIVA--------------------------VSFTDLLA----------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 218 dcGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEG-------------------------- 271
Cdd:cd05936 112 --AGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDllegddvvlaalplfhvfgltvalll 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 272 ---------------DIRLLsDDMKALCPTIFPVVPRLLNRmydkifsqantplkrwLLEFAAKRKqaEVRSGIirndsi 336
Cdd:cd05936 190 plalgativliprfrPIGVL-KEIRKHRVTIFPGVPTMYIA----------------LLNAPEFKK--RDFSSL------ 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 337 wdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT-SGHVGAPLPCNHIK 415
Cdd:cd05936 245 -----------------RLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRkPGSIGIPLPGTEVK 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 416 LVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAP 495
Cdd:cd05936 308 IVD-DDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGFNVYP 384
|
490 500 510
....*....|....*....|....*....|....*
gi 327412329 496 EKIENIYIRSQPVAQIYV-------HGDSLKAFLV 523
Cdd:cd05936 385 REVEEVLYEHPAVAEAAVvgvpdpySGEAVKAFVV 419
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
86-523 |
7.18e-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: 183.18 E-value: 7.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 165
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLK--KGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 166 DKPQKAVLLLehVERKETPGLKlIILMDPFEEALKERGQkcgvviksMQAVEDCGQENHQAPVPPQ-PDDLSIVCFTSGT 244
Cdd:cd05911 89 DPDGLEKVKE--AAKELGPKDK-IIVLDDKPDGVLSIED--------LLSPTLGEEDEDLPPPLKDgKDDTAAILYSSGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 245 TGNPKGAMLTHGNVVADFS---GFLKVTEG--DIRLL------------------------------SDDMKALCP---- 285
Cdd:cd05911 158 TGLPKGVCLSHRNLIANLSqvqTFLYGNDGsnDVILGflplyhiyglfttlasllngatviimpkfdSELFLDLIEkyki 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 286 TIFPVVPRLLNRMydkifsqANTPLkrwllefaakrkqaevrsgiirndsiwdelfFNKIQASlggCVRMIVTGAAPASP 365
Cdd:cd05911 238 TFLYLVPPIAAAL-------AKSPL-------------------------------LDKYDLS---SLRVILSGGAPLSK 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 366 TVLGFLRAALG-CQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGY 444
Cdd:cd05911 277 ELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGY 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 445 LKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIyIRSQP------VAQIY--VHGD 516
Cdd:cd05911 357 YNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAV-LLEHPgvadaaVIGIPdeVSGE 434
|
....*..
gi 327412329 517 SLKAFLV 523
Cdd:cd05911 435 LPRAYVV 441
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
234-531 |
1.01e-50 |
|
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: 178.63 E-value: 1.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 234 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLK---VTEGDIRLLSDDM----------KALC---------------- 284
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAsggLTEGDVFLSTLPLfhigglfgllGALLaggtvvllpkfdpeaa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 285 --------PTIFPVVPRLLNRMydkifsqantplkrwllefaakRKQAEVRSgiiRNDSiwdelffnkiqaslggCVRMI 356
Cdd:cd04433 81 lelierekVTILLGVPTLLARL----------------------LKAPESAG---YDLS----------------SLRAL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 357 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT--SGHVGAPLPCNHIKLVDVEElNYWACKGEGEIC 434
Cdd:cd04433 120 VSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPDG-GELPPGEIGELV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 435 VRGPNVFKGYLKDPDRTkEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYVH 514
Cdd:cd04433 199 VRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPGVAEAAVV 276
|
330
....*....|....*..
gi 327412329 515 GdslkaflvgivVPDPE 531
Cdd:cd04433 277 G-----------VPDPE 282
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
51-530 |
1.87e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 160.35 E-value: 1.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 51 YDDARTMYQVFRRGLSISGNGPCLGFRKPKqpyqwLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVEL 130
Cdd:PRK06187 2 QDYPLTIGRILRHGARKHPDKEAVYFDGRR-----TTYAELDERVNRLANALRALGVKK--GDRVAVFDWNSHEYLEAYF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 131 ACytySM---VVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlLLEHVE--RKETPGLKLIILMDPFEEALkergqk 205
Cdd:PRK06187 75 AV---PKigaVLHPINIRLKPEEIAYILNDAEDRVVLVDSE-----FVPLLAaiLPQLPTVRTVIVEGDGPAAP------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 206 CGVVIKSMQAVEDCGQENHQAPvPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD---FSGFLKVTEGDI--------- 273
Cdd:PRK06187 141 LAPEVGEYEELLAAASDTFDFP-DIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHslaVCAWLKLSRDDVylvivpmfh 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 274 -------------------------RLLSDDMKALCPTIFPVVPRLLNRMydkifSQANTPLKRWLlefaakrkqaevrS 328
Cdd:PRK06187 220 vhawglpylalmagakqviprrfdpENLLDLIETERVTFFFAVPTIWQML-----LKAPRAYFVDF-------------S 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 329 GIirndsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGH---- 404
Cdd:PRK06187 282 SL-----------------------RLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVLPPEDQLPGQwtkr 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 405 --VGAPLPCNHIKLVDvEELNYWACKGE--GEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDR 480
Cdd:PRK06187 339 rsAGRPLPGVEARIVD-DDGDELPPDGGevGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDR 416
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 327412329 481 KKHIFKLAqGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDP 530
Cdd:PRK06187 417 IKDVIISG-GENIYPRELEDA---------LYGHPAVAEVAVIG--VPDE 454
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
61-530 |
1.58e-37 |
|
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: 144.68 E-value: 1.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 61 FRRGLSISGNGPCLGFRKpkqpyQWLSYQEVADRAEFLGSGLlQHNCKACTDQfIGVFAQNRPEWIIVELACYTYSMVVV 140
Cdd:cd17631 1 LRRRARRHPDRTALVFGG-----RSLTYAELDERVNRLAHAL-RALGVAKGDR-VAVLSKNSPEFLELLFAAARLGAVFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 141 PLYDTLGPGAIRYIINTADiSTVIVDkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcg 220
Cdd:cd17631 74 PLNFRLTPPEVAYILADSG-AKVLFD------------------------------------------------------ 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 221 qenhqapvppqpdDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTEGDIRLLSDDMKALCPTIFPVVPRLLNr 297
Cdd:cd17631 99 -------------DLALLMYTSGTTGRPKGAMLTHRNLLWNAVNalaALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLR- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 298 mydkifSQANTPLKRwlleFAAKRKQAEVRSGIIRN----DSIWDELF----FNKIQASlggCVRMIVTGAAPASPTVLG 369
Cdd:cd17631 165 ------GGTVVILRK----FDPETVLDLIERHRVTSfflvPTMIQALLqhprFATTDLS---SLRAVIYGGAPMPERLLR 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 370 FLRAAlGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKD 447
Cdd:cd17631 232 ALQAR-GVKFVQGYGMTETSPGVTFLSPEDHRRklGSAGRPVFFVEVRIVD-PDGREVPPGEVGEIVVRGPHVMAGYWNR 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 448 PDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivV 527
Cdd:cd17631 310 PEATAAAFR-DGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDV---------LYEHPAVAEVAVIG--V 376
|
...
gi 327412329 528 PDP 530
Cdd:cd17631 377 PDE 379
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
86-501 |
1.85e-37 |
|
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: 145.55 E-value: 1.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLGSgLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 165
Cdd:cd05909 8 LTYRKLLTGAIALAR-KLAKMTKE--GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 166 DKPQKAVLLLEHVERKETPgLKLIILmdpfeEALKER---GQKCGVVIKSMQAVEDCGQENHQAPVppQPDDLSIVCFTS 242
Cdd:cd05909 85 SKQFIEKLKLHHLFDVEYD-ARIVYL-----EDLRAKiskADKCKAFLAGKFPPKWLLRIFGVAPV--QPDDPAVILFTS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 243 GTTGNPKGAMLTHGNVVADFSGFLKVtegdIRLLSDD--MKALCP---------TIFPvvprLLNRMYdkIFSQANtPLK 311
Cdd:cd05909 157 GSEGLPKGVVLSHKNLLANVEQITAI----FDPNPEDvvFGALPFfhsfgltgcLWLP----LLSGIK--VVFHPN-PLD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 312 -RWLLEFAAKRKqaevrSGIIRNDSIWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTA 390
Cdd:cd05909 226 yKKIPELIYDKK-----ATILLGTPTFLRGYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 391 GCTFTTPG-DWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKW 469
Cdd:cd05909 301 VISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKI 379
|
410 420 430
....*....|....*....|....*....|..
gi 327412329 470 LPAGTLKIIDRKKHIFKLAqGEYVAPEKIENI 501
Cdd:cd05909 380 DGEGFLTITGRLSRFAKIA-GEMVSLEAIEDI 410
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
85-608 |
1.86e-34 |
|
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: 137.06 E-value: 1.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 85 WLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVI 164
Cdd:cd05926 14 ALTYADLAELVDDLARQLAALGIKK--GDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 165 VDKpqkaVLLLEHVERKETPGLkliilmdpfeeALKERGQKCGVVIKSMQAVE----DCGQENHQAPVPPQPDDLSIVCF 240
Cdd:cd05926 92 TPK----GELGPASRAASKLGL-----------AILELALDVGVLIRAPSAESlsnlLADKKNAKSEGVPLPDDLALILH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 241 TSGTTGNPKGAMLTHGNVVA---DFSGFLKVTEGD---------------IRLLS--------------------DDMKA 282
Cdd:cd05926 157 TSGTTGRPKGVPLTHRNLAAsatNITNTYKLTPDDrtlvvmplfhvhglvASLLStlaaggsvvlpprfsastfwPDVRD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 283 LCPTIFPVVPRLLnrmydKIfsqantplkrwLLEFAAKRKQAEvrsgiirndsiwdelfFNKIqaslggcvRMIVTGAAP 362
Cdd:cd05926 237 YNATWYTAVPTIH-----QI-----------LLNRPEPNPESP----------------PPKL--------RFIRSCSAS 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 363 ASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTP---GDWTSGHVGAPlpcNHIKLVDVEElnywacKGE-------GE 432
Cdd:cd05926 277 LPPAVLEALEATFGAPVLEAYGMTE-AAHQMTSNPlppGPRKPGSVGKP---VGVEVRILDE------DGEilppgvvGE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 433 ICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIY 512
Cdd:cd05926 347 ICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVLLSHPAVLEAV 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 513 VHGdslkaflvgivVPDP---EVMPSWAQKRgiEGTYADlctnkdlKKAILEDMvrlgkESGLHSFEQVKAIHIhsdmfs 589
Cdd:cd05926 426 AFG-----------VPDEkygEEVAAAVVLR--EGASVT-------EEELRAFC-----RKHLAAFKVPKKVYF------ 474
|
570
....*....|....*....
gi 327412329 590 VQNGLLTPTLKAKRPELRE 608
Cdd:cd05926 475 VDELPKTATGKIQRRKVAE 493
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
86-534 |
2.73e-34 |
|
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: 135.50 E-value: 2.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLgSGLLQHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIv 165
Cdd:cd05941 12 ITYADLVARAARL-ANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 166 dkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhqapvppqpdDLSIVCFTSGTT 245
Cdd:cd05941 90 --------------------------------------------------------------------DPALILYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 246 GNPKGAMLTHGNVVADFSGFLKV---TEGDiRLLsddmkaLCPTIFPVvprllnrmyDKIFSQANTPLK-----RWLLEF 317
Cdd:cd05941 102 GRPKGVVLTHANLAANVRALVDAwrwTEDD-VLL------HVLPLHHV---------HGLVNALLCPLFagasvEFLPKF 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 318 AAKRkqaevRSGIIRNDSI---------------WDELFFNKIQASLGGC---VRMIVTGAAPASPTVLGFLRAALGCQV 379
Cdd:cd05941 166 DPKE-----VAISRLMPSItvfmgvptiytrllqYYEAHFTDPQFARAAAaerLRLMVSGSAALPVPTLEEWEAITGHTL 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 380 YEGYGQTEctAGCTFTTP--GDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDS 457
Cdd:cd05941 241 LERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTD 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 458 DGWLHTGDIGKWLPAGTLKIIDRKK-HIFKlAQGEYVAPEKIENIyIRSQP-VAQIYVHGDSLKAF---LVGIVVPDPEV 532
Cdd:cd05941 319 DGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIERV-LLAHPgVSECAVIGVPDPDWgerVVAVVVLRAGA 396
|
..
gi 327412329 533 MP 534
Cdd:cd05941 397 AA 398
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
234-524 |
3.42e-33 |
|
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: 129.93 E-value: 3.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 234 DLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTEGDIRLLSDDM------KALC-------PTIFPV----VPR 293
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLraaAAWADCADLTEDDRYLIINPFfhtfgyKAGIvaclltgATVVPVavfdVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 294 LLNRMYDKIFSQANTP--LKRWLLEFAAkRKQAEVRSgiirndsiwdelffnkiqaslggcVRMIVTGAAPASPTVLGFL 371
Cdd:cd17638 81 ILEAIERERITVLPGPptLFQSLLDHPG-RKKFDLSS------------------------LRAAVTGAATVPVELVRRM 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 372 RAALGCQ-VYEGYGQTECTAGcTFTTPGD---WTSGHVGAPLPCNHIKLVDveelnywackgEGEICVRGPNVFKGYLKD 447
Cdd:cd17638 136 RSELGFEtVLTAYGLTEAGVA-TMCRPGDdaeTVATTCGRACPGFEVRIAD-----------DGEVLVRGYNVMQGYLDD 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 448 PDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKA 520
Cdd:cd17638 204 PEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGALAEHPGVAQVAVigvpderMGEVGKA 282
|
....
gi 327412329 521 FLVG 524
Cdd:cd17638 283 FVVA 286
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
212-501 |
1.36e-32 |
|
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: 131.59 E-value: 1.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 212 SMQAVEDCGQENHQAPVPPQ--PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFL----KVTEGDIRLLsddmkALCP 285
Cdd:cd05904 135 SLSFSDLLFEADEAEPPVVVikQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVagegSNSDSEDVFL-----CVLP 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 286 -----------------------------------------TIFPVVPrllnrmydkifsqantPLkrwlleFAAKRKQA 324
Cdd:cd05904 210 mfhiyglssfalgllrlgatvvvmprfdleellaaierykvTHLPVVP----------------PI------VLALVKSP 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 325 EVRSGIIRndsiwdelffnkiqaSLggcvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTTP---GDW 400
Cdd:cd05904 268 IVDKYDLS---------------SL----RQIMSGAAPLGKELIeAFRAKFPNVDLGQGYGMTESTGVVAMCFApekDRA 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 401 TSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDR 480
Cdd:cd05904 329 KYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDR 408
|
330 340
....*....|....*....|.
gi 327412329 481 KKHIFKLaQGEYVAPEKIENI 501
Cdd:cd05904 409 LKELIKY-KGFQVAPAELEAL 428
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
86-513 |
2.37e-32 |
|
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: 129.81 E-value: 2.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADIstviv 165
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGP--GDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 166 dkpqkavlllehverketpglKLIILMDPFeealkergqkcgvviksmqavedcGQENHQApvppQPDDLSIVCFTSGTT 245
Cdd:cd05903 75 ---------------------KVFVVPERF------------------------RQFDPAA----MPDAVALLLFTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 246 GNPKGAMLTHGNVVADFSGF---LKVTEGDIRLLSDDMK--------ALCPTIFPVvPRLLNRMYDK------------I 302
Cdd:cd05903 106 GEPKGVMHSHNTLSASIRQYaerLGLGPGDVFLVASPMAhqtgfvygFTLPLLLGA-PVVLQDIWDPdkalalmrehgvT 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 303 FSQANTPLKRWLLEfaAKRKQAEVRSGIirndsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEG 382
Cdd:cd05903 185 FMMGATPFLTDLLN--AVEEAGEPLSRL-----------------------RTFVCGGATVPRSLARRAAELLGAKVCSA 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 383 YGQTECTAGCTFTTPGD----WTSGhvGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDsD 458
Cdd:cd05903 240 YGSTECPGAVTSITPAPedrrLYTD--GRPLPGVEIKVVD-DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAP-E 315
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 327412329 459 GWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYV 513
Cdd:cd05903 316 GWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAV 369
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
87-507 |
5.72e-32 |
|
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: 128.15 E-value: 5.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 87 SYQEVADRAEFLGSGLLQHnCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLyDTLGPGA-IRYIINTADISTVIV 165
Cdd:TIGR01733 1 TYRELDERANRLARHLRAA-GGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPL-DPAYPAErLAFILEDAGARLLLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 166 DKPqkavllleHVERKETPGLKLIILMDPFEEALkergqkcgvviksmqavEDCGQENHqAPVPPQPDDLSIVCFTSGTT 245
Cdd:TIGR01733 79 DSA--------LASRLAGLVLPVILLDPLELAAL-----------------DDAPAPPP-PDAPSGPDDLAYVIYTSGST 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 246 GNPKGAMLTHGNVV---ADFSGFLKVTEGDIRL----LSDDMKALcpTIFP---------VVPRllnrmydkifsqanTP 309
Cdd:TIGR01733 133 GRPKGVVVTHRSLVnllAWLARRYGLDPDDRVLqfasLSFDASVE--EIFGallagatlvVPPE--------------DE 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 310 LKRWLLEFAAKRKQAEVrsgiirndSIWDEL--FFNKIQASLGGC---VRMIVTGAAPASPTVLGFLRAALG-CQVYEGY 383
Cdd:TIGR01733 197 ERDDAALLAALIAEHPV--------TVLNLTpsLLALLAAALPPAlasLRLVILGGEALTPALVDRWRARGPgARLINLY 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 384 GQTECTAGCT-FTTPGDWTSGHV----GAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEA-LDS 457
Cdd:TIGR01733 269 GPTETTVWSTaTLVDPDDAPRESpvpiGRPLANTRLYVLD-DDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERfVPD 347
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 327412329 458 DGWL-------HTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIyIRSQP 507
Cdd:TIGR01733 348 PFAGgdgarlyRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAA-LLRHP 402
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
220-523 |
6.34e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 130.65 E-value: 6.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 220 GQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFsgfLKVTEgdirLLSDDMKALCPTIfpVVPRLLNRMY 299
Cdd:PRK05677 194 GAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANM---LQCRA----LMGSNLNEGCEIL--IAPLPLYHIY 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 300 DKIFSQANT----------PLKRWLLEFAAKRKQAEVrSGIIR---------NDSIWDELFFNKIQASLGGcvRMIVTGA 360
Cdd:PRK05677 265 AFTFHCMAMmlignhniliSNPRDLPAMVKELGKWKF-SGFVGlntlfvalcNNEAFRKLDFSALKLTLSG--GMALQLA 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 361 APASptvlgfLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNV 440
Cdd:PRK05677 342 TAER------WKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVID-DDGNELPLGEVGELCVKGPQV 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 441 FKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIyIRSQP----VAQIYV--- 513
Cdd:PRK05677 415 MKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVSGFNVYPNELEDV-LAALPgvlqCAAIGVpde 492
|
330
....*....|.
gi 327412329 514 -HGDSLKAFLV 523
Cdd:PRK05677 493 kSGEAIKVFVV 503
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
84-540 |
3.05e-31 |
|
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: 127.02 E-value: 3.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 84 QWLSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLyDTLGPGA-IRYIINTADIST 162
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARG--VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPL-DPDYPADrLRYILEDAEPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 163 VIVDkpqkavlllehverketpglkliilmdpfeEALKERGQKCGVVIksMQAVEDCGQENHQAPVPPQPDDLSIVCFTS 242
Cdd:cd12116 88 VLTD------------------------------DALPDRLPAGLPVL--LLALAAAAAAPAAPRTPVSPDDLAYVIYTS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 243 GTTGNPKGAMLTHGNVVADFSGF---LKVTEGDiRLLsddmkALCPTIFPV-VPRLLnrmydkifsqanTPL---KRWLL 315
Cdd:cd12116 136 GSTGRPKGVVVSHRNLVNFLHSMrerLGLGPGD-RLL-----AVTTYAFDIsLLELL------------LPLlagARVVI 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 316 EFAAKRKQAEVRSGIIRNDSI---------WDELFFNKIQASLGgcVRMIVTGAApaSPTVLGFLRAALGCQVYEGYGQT 386
Cdd:cd12116 198 APRETQRDPEALARLIEAHSItvmqatpatWRMLLDAGWQGRAG--LTALCGGEA--LPPDLAARLLSRVGSLWNLYGPT 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 387 ECT--AGCTFTTPGDwTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH-- 462
Cdd:cd12116 274 ETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLD-AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpg 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 463 -----TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQ--IYVHGDSLKAFLVGIVVPDPEVMPS 535
Cdd:cd12116 352 srlyrTGDLVRRRADGRLEYLGRADGQVKI-RGHRIELGEIEAALAAHPGVAQaaVVVREDGGDRRLVAYVVLKAGAAPD 430
|
....*
gi 327412329 536 WAQKR 540
Cdd:cd12116 431 AAALR 435
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
220-529 |
7.94e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 127.42 E-value: 7.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 220 GQENHQAPVP-PQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD------------------------FSGF-------LK 267
Cdd:PRK05605 205 GGDGSDVSHPrPTPDDVALILYTSGTTGKPKGAQLTHRNLFANaaqgkawvpglgdgpervlaalpmFHAYgltlcltLA 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 268 VTEG---------DIRLLSDDMKALCPTIFPVVPRLlnrmYDKIfsqantplkrwlLEFAAKRkqaevrsGIirndsiwd 338
Cdd:PRK05605 285 VSIGgelvllpapDIDLILDAMKKHPPTWLPGVPPL----YEKI------------AEAAEER-------GV-------- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 339 elffnkiqaSLGGcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECT---AGCTFTTpgDWTSGHVGAPLPCNHIK 415
Cdd:PRK05605 334 ---------DLSG-VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpiiVGNPMSD--DRRPGYVGVPFPDTEVR 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 416 LVDVEELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVA 494
Cdd:PRK05605 402 IVDPEDPDETMPDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELI-ITGGFNVY 479
|
330 340 350
....*....|....*....|....*....|....*
gi 327412329 495 PEKIENIyirsqpVAQiyvHGDSLKAFLVGIVVPD 529
Cdd:PRK05605 480 PAEVEEV------LRE---HPGVEDAAVVGLPRED 505
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
86-538 |
1.80e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 125.48 E-value: 1.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAE-----FLGSGLLQHNCkactdqfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADI 160
Cdd:PRK06188 38 LTYGQLADRISryiqaFEALGLGTGDA-------VALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 161 STVIVDK---PQKAVLLLEHVerketPGLKLIILMDPFEEAlkergqkcgvviksmqavEDCGQENHQAPVPP-----QP 232
Cdd:PRK06188 111 STLIVDPapfVERALALLARV-----PSLKHVLTLGPVPDG------------------VDLLAAAAKFGPAPlvaaaLP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 233 DDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLkvTEGDIRllsDDMKALCPTIF------PVVPRLLnrmydkifsqa 306
Cdd:PRK06188 168 PDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQL--AEWEWP---ADPRFLMCTPLshaggaFFLPTLL----------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 307 ntplKRWLLEFAAKRKQAEVRSgIIRNDSI-WDELFFNKIQASL--GGCVR-------MIVTGAAPASPTVLGFLRAALG 376
Cdd:PRK06188 232 ----RGGTVIVLAKFDPAEVLR-AIEEQRItATFLVPTMIYALLdhPDLRTrdlssleTVYYGASPMSPVRLAEAIERFG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 377 CQVYEGYGQTECTAGCTFTTPGDWTSGHV------GAPLPCNHIKLVDvEELNYWAcKGE-GEICVRGPNVFKGYLKDPD 449
Cdd:PRK06188 307 PIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRVALLD-EDGREVA-QGEvGEICVRGPLVMDGYWNRPE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 450 RTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAfl 522
Cdd:PRK06188 385 ETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMI-VTGGFNVFPREVEDVLAEHPAVAQVAVigvpdekWGEAVTA-- 460
|
490
....*....|....*.
gi 327412329 523 vgIVVPDPEVMPSWAQ 538
Cdd:PRK06188 461 --VVVLRPGAAVDAAE 474
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
87-531 |
2.16e-30 |
|
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: 125.72 E-value: 2.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 87 SYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLgpgAIRYIINTADIST-VIV 165
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLK--QNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIY---NERELDHSLNISKpTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 166 DKPQKAVLLLEHVERKeTPGLKLIILMDPFEEAlkeRGQKCGVVIKSMQAVEDCGQENHQAPVPPQPDDLSIVCFTSGTT 245
Cdd:cd17642 121 FCSKKGLQKVLNVQKK-LKIIKTIIILDSKEDY---KGYQCLYTFITQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGST 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 246 GNPKGAMLTHGNVVADFSGFLKVTEGDirllsddmkALCP--TIFPVVP--------------------RLLNRMYDKIF 303
Cdd:cd17642 197 GLPKGVQLTHKNIVARFSHARDPIFGN---------QIIPdtAILTVIPfhhgfgmfttlgylicgfrvVLMYKFEEELF 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 304 SQA-------NTPLKRWLLEFAAKrkqaevrSGIIrndsiwdelffNKIQASlggCVRMIVTGAAPASPTVLGFLRAALG 376
Cdd:cd17642 268 LRSlqdykvqSALLVPTLFAFFAK-------STLV-----------DKYDLS---NLHEIASGGAPLSKEVGEAVAKRFK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 377 CQ-VYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL 455
Cdd:cd17642 327 LPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALI 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 327412329 456 DSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRsqpvaqiyvHGDSLKAFLVGIvvPDPE 531
Cdd:cd17642 407 DKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQ---------HPKIFDAGVAGI--PDED 470
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
181-619 |
4.22e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 125.99 E-value: 4.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 181 KETPGLKLIILMDPFE---------EALKERGQKCGvvIKSMQAVEDCGQENHQAPVPPQ-PDDLSIVCFTSGTTGNPKG 250
Cdd:PTZ00342 244 NDLSNELEDISLGPLEydkeklekiKDLKEKAKKLG--ISIILFDDMTKNKTTNYKIQNEdPDFITSIVYTSGTSGKPKG 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 251 AMLTHGNV------VADFSGFLK--------------VTE-----------GDIRLLSDDMKALCPTIFPV-------VP 292
Cdd:PTZ00342 322 VMLSNKNLyntvvpLCKHSIFKKynpkthlsylpishIYErviaylsfmlgGTINIWSKDINYFSKDIYNSkgnilagVP 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 293 RLLNRMYDKIFSQAN--TPLKRWLlefaAKRKQAEVRSGIIRNDSIWDELFFN---KIQASLGGCVRMIVTGAAPASPTV 367
Cdd:PTZ00342 402 KVFNRIYTNIMTEINnlPPLKRFL----VKKILSLRKSNNNGGFSKFLEGITHissKIKDKVNPNLEVILNGGGKLSPKI 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 368 LGFLRAALGCQVYEGYGQTEcTAGCTFTTPG-DWTSGHVGAPL-PCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYL 445
Cdd:PTZ00342 478 AEELSVLLNVNYYQGYGLTE-TTGPIFVQHAdDNNTESIGGPIsPNTKYKVRTWETYKATDTLPKGELLIKSDSIFSGYF 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 446 KDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHG-DSLKAFLvG 524
Cdd:PTZ00342 557 LEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGdDSMDGPL-A 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 525 IVVPDPEVM------PSWAQKRGI-EGTYADLCTNKDLKKAILEDMVR-----LGKESGLHSFEQVKAIHIHSDMFSVQN 592
Cdd:PTZ00342 636 IISVDKYLLfkclkdDNMLESTGInEKNYLEKLTDETINNNIYVDYVKgkmleVYKKTNLNRYNIINDIYLTSKVWDTNN 715
|
490 500 510
....*....|....*....|....*....|
gi 327412329 593 gLLTPTLKAKRPEL-REY--FKKQIEELYS 619
Cdd:PTZ00342 716 -YLTPTFKVKRFYVfKDYafFIDQVKKIYK 744
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
86-535 |
8.00e-30 |
|
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: 122.64 E-value: 8.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACY----TYsmvvVPLYDTLGPGAIRYIINTADIS 161
Cdd:cd05930 13 LTYAELDARANRLARYLRERGVGP--GDLVAVLLERSLEMVVAILAVLkagaAY----VPLDPSYPAERLAYILEDSGAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 162 TVIVDkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhqapvppqPDDLSIVCFT 241
Cdd:cd05930 87 LVLTD-----------------------------------------------------------------PDDLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 242 SGTTGNPKGAMLTHGNVV---ADFSGFLKVTEGDIRL----LSDDMkalcpTIFPVVPRLLN--RMYdkifsqantplkr 312
Cdd:cd05930 102 SGSTGKPKGVMVEHRGLVnllLWMQEAYPLTPGDRVLqftsFSFDV-----SVWEIFGALLAgaTLV------------- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 313 wLLEFAAKRKQAEVRSGIIRND--------SIWDELFFNKIQASLGgCVRMIVTGAAPASPTVL-GFLRAALGCQVYEGY 383
Cdd:cd05930 164 -VLPEEVRKDPEALADLLAEEGitvlhltpSLLRLLLQELELAALP-SLRLVLVGGEALPPDLVrRWRELLPGARLVNLY 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 384 GQTECTAGCTFT--TPGDWTSGHV--GAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEA----- 454
Cdd:cd05930 242 GPTEATVDATYYrvPPDDEEDGRVpiGRPIPNTRVYVLD-ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERfvpnp 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 455 LDSDGWLH-TGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYV---HGDSLKAFLVGIVVPDP 530
Cdd:cd05930 321 FGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIELGEIEAALLAHPGVREAAVvarEDGDGEKRLVAYVVPDE 399
|
....*
gi 327412329 531 EVMPS 535
Cdd:cd05930 400 GGELD 404
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
115-568 |
9.32e-30 |
|
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: 122.17 E-value: 9.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 115 IGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlllehVERKETPGLKLIILMDP 194
Cdd:TIGR01923 27 VALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL---------LEEKDFQADSLDRIEAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 195 FEEALKERGQKcgvviksmqavedcgqenhqapvppQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF---LKVTEG 271
Cdd:TIGR01923 98 GRYETSLSASF-------------------------NMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSkenLGFTED 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 272 DIRLLSddmkalcptifpvVPrllnrMYdKIFSQAntPLKRWLLEFAAKR---KQAEVRSGIIRNDSIWDELF---FNKI 345
Cdd:TIGR01923 153 DNWLLS-------------LP-----LY-HISGLS--ILFRWLIEGATLRivdKFNQLLEMIANERVTHISLVptqLNRL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 346 QASLGGC--VRMIVTGAAPASPTVLgflRAAL--GCQVYEGYGQTE-CTAGCTFTTPGDWTSGHVGAPLPCNHIKL-VDV 419
Cdd:TIGR01923 212 LDEGGHNenLRKILLGGSAIPAPLI---EEAQqyGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIkVDN 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 420 EElnywackGEGEICVRGPNVFKGYLkDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIE 499
Cdd:TIGR01923 289 KE-------GHGEIMVKGANLMKGYL-YQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIE 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 327412329 500 NIYIRSQPVAQiyvhgdslkAFLVGivVPDPEvmpsWAQKrgiegTYADLCTNKDLKKAILEDMV--RLGK 568
Cdd:TIGR01923 360 TVLYQHPGIQE---------AVVVP--KPDAE----WGQV-----PVAYIVSESDISQAKLIAYLteKLAK 410
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
234-531 |
1.91e-29 |
|
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: 121.24 E-value: 1.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 234 DLSIVCFTSGTTGNPKGAMLTHGNVVadFSG-----FLKVTEGDIRLLSD---DMKALCPTIFPVvprllnrmydkIFSQ 305
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLT--FAGyysarRFGLGEDDVYLTVLplfHINAQAVSVLAA-----------LSVG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 306 AN-TPLKRwlleFAAKRKQAEVRsgiiRNDSIWdelfFNkiqaSLGGCVRMI---------------VTGAAPASPTVLG 369
Cdd:cd05934 149 ATlVLLPR----FSASRFWSDVR----RYGATV----TN----YLGAMLSYLlaqppspddrahrlrAAYGAPNPPELHE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 370 FLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEelNYWACKGE-GEICVR---GPNVFKGYL 445
Cdd:cd05934 213 EFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDD--GQELPAGEpGELVIRglrGWGFFKGYY 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 446 KDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYVHG-------DSL 518
Cdd:cd05934 291 NMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVERAILRHPAVREAAVVAvpdevgeDEV 368
|
330
....*....|...
gi 327412329 519 KAFlvgIVVPDPE 531
Cdd:cd05934 369 KAV---VVLRPGE 378
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
115-531 |
2.18e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 121.84 E-value: 2.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 115 IGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAvlllehverketpglkliilmdp 194
Cdd:PRK09088 50 LAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDDAVAA----------------------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 195 feealkerGQKCGVVIKSMQAVEDCGQENHQAPVPPqpDDLSIVCFTSGTTGNPKGAMLTHGN---VVADFSGFLKVTEG 271
Cdd:PRK09088 107 --------GRTDVEDLAAFIASADALEPADTPSIPP--ERVSLILFTSGTSGQPKGVMLSERNlqqTAHNFGVLGRVDAH 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 272 DIRLLSDDMKALCPTIFPVVPRLLNRMYDKI---FSQANTplKRWLLE--------FAAKRKQAEVRSGIIRNDSIWDEL 340
Cdd:PRK09088 177 SSFLCDAPMFHIIGLITSVRPVLAVGGSILVsngFEPKRT--LGRLGDpalgithyFCVPQMAQAFRAQPGFDAAALRHL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 341 ffnkiqaslggcvRMIVTGAAP-ASPTVLGFLraALGCQVYEGYGQTEctAGCTFTTPGDWT-----SGHVGAPLPCNHI 414
Cdd:PRK09088 255 -------------TALFTGGAPhAAEDILGWL--DDGIPMVDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 415 KLVDVEELNYWAckGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYV 493
Cdd:PRK09088 318 RVVDDQGNDCPA--GVpGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENV 394
|
410 420 430
....*....|....*....|....*....|....*...
gi 327412329 494 APEKIEniyirsqpvAQIYVHGDSLKAFLVGivVPDPE 531
Cdd:PRK09088 395 YPAEIE---------AVLADHPGIRECAVVG--MADAQ 421
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
232-515 |
4.48e-29 |
|
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: 118.53 E-value: 4.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 232 PDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSGF-LKVTEGDirllsddmKALCPT----IFPVVPRLLNR------- 297
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVnnGYFIGErLGLTEQD--------RLCIPVplfhCFGSVLGVLAClthgatm 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 298 -MYDKIFSQANTplkrwlLEfAAKRKQAEVRSGI----IrndsiwDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLR 372
Cdd:cd05917 73 vFPSPSFDPLAV------LE-AIEKEKCTALHGVptmfI------AELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 373 AALGC-QVYEGYGQTECTAGCTFTTPGDWTS---GHVGAPLPCNHIKLVDvEELNYWACKGE-GEICVRGPNVFKGYLKD 447
Cdd:cd05917 140 EVMNMkDVTIAYGMTETSPVSTQTRTDDSIEkrvNTVGRIMPHTEAKIVD-PEGGIVPPVGVpGELCIRGYSVMKGYWND 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 327412329 448 PDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYVHG 515
Cdd:cd05917 219 PEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGENIYPREIEEFLHTHPKVSDVQVVG 285
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
121-523 |
7.18e-29 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 119.36 E-value: 7.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 121 NRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKpqkavlllehverketpglkliilmdpfeealk 200
Cdd:cd05972 34 RVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA--------------------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 201 ergqkcgvviksmqavedcgqenhqapvppqpDDLSIVCFTSGTTGNPKGAMLTHG---NVVADFSGFLKVTEGDIRLLS 277
Cdd:cd05972 81 --------------------------------EDPALIYFTSGTTGLPKGVLHTHSyplGHIPTAAYWLGLRPDDIHWNI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 278 DD----MKALCPTIFPV---VPRLLN--------RMYDKI-------FSQANTPLKRWLLEFAAKRKQAEVRSgiirnds 335
Cdd:cd05972 129 ADpgwaKGAWSSFFGPWllgATVFVYegprfdaeRILELLerygvtsFCGPPTAYRMLIKQDLSSYKFSHLRL------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 336 iwdelffnkiqaslggcvrmIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIK 415
Cdd:cd05972 202 --------------------VVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 416 LVDvEELNYWACKGEGEICVRGPNV--FKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYV 493
Cdd:cd05972 262 IID-DDGRELPPGEEGDIAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRI 338
|
410 420 430
....*....|....*....|....*....|....*..
gi 327412329 494 APEKIENIYIRSQPVAQIYV-------HGDSLKAFLV 523
Cdd:cd05972 339 GPFEVESALLEHPAVAEAAVvgspdpvRGEVVKAFVV 375
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
138-535 |
1.85e-28 |
|
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: 118.70 E-value: 1.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 138 VVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlLLEHVErketpgLKLIILMDPfeealkergqkcGVVIKsmqaVE 217
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGGRIVLADAG-----AADRLR------DALPASPDP------------GTVLD----AD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 218 DCGQENHQAP-VPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTEGDIrllsddmkalcptifpvVPR 293
Cdd:cd05922 101 GIRAARASAPaHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSiaeYLGITADDR-----------------ALT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 294 LLNRMYDKIFSQANTPLKRwllefaakrkQAEVrsgIIRNDSIWDELFFNKIQA----SLGGC----------------- 352
Cdd:cd05922 164 VLPLSYDYGLSVLNTHLLR----------GATL---VLTNDGVLDDAFWEDLREhgatGLAGVpstyamltrlgfdpakl 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 353 --VRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFTTPG--DWTSGHVGAPLPCNHIklvDVEELNYWAC 427
Cdd:cd05922 231 psLRYLTQAGGRLPQETIARLRELLpGAQVYVMYGQTEATRRMTYLPPEriLEKPGSIGLAIPGGEF---EILDDDGTPT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 428 K-GE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkWLPA-GTLKIIDRKKHIFKLAqGEYVAPEKIENIyIR 504
Cdd:cd05922 308 PpGEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLA-RRDEdGFLFIVGRRDRMIKLF-GNRISPTEIEAA-AR 384
|
410 420 430
....*....|....*....|....*....|....
gi 327412329 505 SQP---VAQIYVHGDSLKAFLVGIVVPDPEVMPS 535
Cdd:cd05922 385 SIGliiEAAAVGLPDPLGEKLALFVTAPDKIDPK 418
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
87-501 |
2.23e-28 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 119.47 E-value: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 87 SYQEVADRAEFLGSGLLQHNCKACTdqfigVFAQNRPEW---IIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTV 163
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGD-----RVAFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 164 IVDKPQKAV--LLLEHVERKETPGLKLIILMDPFEEALKErgqkcgvvIKSMQAVEDcgQENHQAPVPPQPDDLSIVCFT 241
Cdd:PRK06087 126 FAPTLFKQTrpVDLILPLQNQLPQLQQIVGVDKLAPATSS--------LSLSQIIAD--YEPLTTAITTHGDELAAVLFT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 242 SGTTGNPKGAMLTHGNVVADFSGFLKVTEgdirLLSDDmkalcpTIFpvVPRLLNRMyDKIFSQANTPL---KRWLLEFA 318
Cdd:PRK06087 196 SGTEGLPKGVMLTHNNILASERAYCARLN----LTWQD------VFM--MPAPLGHA-TGFLHGVTAPFligARSVLLDI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 319 AKRKQAevrSGIIRNDS----------IWDELFFNKIQASLGGCVRMIVTGAAPASPTVLgflRAAL--GCQVYEGYGQT 386
Cdd:PRK06087 263 FTPDAC---LALLEQQRctcmlgatpfIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVA---RECQqrGIKLLSVYGST 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 387 ECTAGcTFTTPGD---WTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHT 463
Cdd:PRK06087 337 ESSPH-AVVNLDDplsRFMHTDGYAAAGVEIKVVD-EARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYS 414
|
410 420 430
....*....|....*....|....*....|....*...
gi 327412329 464 GDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENI 501
Cdd:PRK06087 415 GDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDI 451
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
86-531 |
2.47e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 119.29 E-value: 2.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLgSGLLQHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 165
Cdd:PRK08314 36 ISYRELLEEAERL-AGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 166 -----DKPQKAV--LLLEHV-------ERKETPGLKLIILMDpfEEALKERGQKCGVViksmqAVEDCGQENHQA-PVPP 230
Cdd:PRK08314 115 gselaPKVAPAVgnLRLRHVivaqysdYLPAEPEIAVPAWLR--AEPPLQALAPGGVV-----AWKEALAAGLAPpPHTA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 231 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTEGDIRLlsddmkALCPtIFPVVPrLLNRMYDKIFSQAN 307
Cdd:PRK08314 188 GPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGsvlWSNSTPESVVL------AVLP-LFHVTG-MVHSMNAPIYAGAT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 308 TPL-KRWLLEFAAkrkQAEVRSGIirndSIWD-------ELFFN-KIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQ 378
Cdd:PRK08314 260 VVLmPRWDREAAA---RLIERYRV----THWTniptmvvDFLASpGLAERDLSSLRYIGGGGAAMPEAVAERLKELTGLD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 379 VYEGYGQTEcTAGCTFTTPGDWT-SGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEA--- 454
Cdd:PRK08314 333 YVEGYGLTE-TMAQTHSNPPDRPkLQCLGIPTFGVDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfie 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 455 LDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFlvgiVV 527
Cdd:PRK08314 412 IDGKRFFRTGDLGRMDEEGYFFITDRLKRMIN-ASGFKVWPAEVENLLYKHPAIQEACViatpdprRGETVKAV----VV 486
|
....
gi 327412329 528 PDPE 531
Cdd:PRK08314 487 LRPE 490
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
234-513 |
3.32e-28 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 119.31 E-value: 3.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 234 DLSIVCFTSGTTGNPKGAMLTHGNVVADfsgflkvtegdirllsddmkaLCPTIFPVVPRLLN----------------- 296
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNLVAN---------------------LCSSLFSVGPEMIGqvvtlglipffhiygit 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 297 -------RMYDKIFSQANTPLKRWLLEFAAKRKQ-AEVRSGIIRN---DSIWDELFFNKIQaslggcVRMIVTGAAPASP 365
Cdd:PLN02330 244 giccatlRNKGKVVVMSRFELRTFLNALITQEVSfAPIVPPIILNlvkNPIVEEFDLSKLK------LQAIMTAAAPLAP 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 366 TVL-GFLRAALGCQVYEGYGQTECTagCTFTTPGDWTSGH-------VGAPLPCNHIKLVDVEELNYWACKGEGEICVRG 437
Cdd:PLN02330 318 ELLtAFEAKFPGVQVQEAYGLTEHS--CITLTHGDPEKGHgiakknsVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRS 395
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 327412329 438 PNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYV 513
Cdd:PLN02330 396 QCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAILLTHPSVEDAAV 470
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
86-515 |
4.16e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 119.11 E-value: 4.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVV---PLYDT------LGPGAIRYII- 155
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQP--GDRVGIWAPNCAEWLLTQFATARIGAILVninPAYRAseleyaLGQSGVRWVIc 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 156 ----NTADISTVIVD-KPQKAVLLLEHVERKETPGLKLIILMDPFE-------EALKERGQkcGVvikSMQAVEDcgqen 223
Cdd:PRK12583 124 adafKTSDYHAMLQElLPGLAEGQPGALACERLPELRGVVSLAPAPppgflawHELQARGE--TV---SREALAE----- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 224 HQAPVppQPDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSG-FLKVTEGDiRLlsddmkalcptifpVVPRLLNRMYD 300
Cdd:PRK12583 194 RQASL--DRDDPINIQYTSGTTGFPKGATLSHHNILnnGYFVAeSLGLTEHD-RL--------------CVPVPLYHCFG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 301 KIFS---------------QANTPLKrwLLEFAAKRKQAEVRSGIIRNDSIWDELFFNKIQASlggCVRMIVTGAAPASP 365
Cdd:PRK12583 257 MVLAnlgcmtvgaclvypnEAFDPLA--TLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLS---SLRTGIMAGAPCPI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 366 TVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGD-----WTSghVGAPLPCNHIKLVDVEELNywACKGE-GEICVRGP 438
Cdd:PRK12583 332 EVMRRVMDEMHMaEVQIAYGMTETSPVSLQTTAADdlerrVET--VGRTQPHLEVKVVDPDGAT--VPRGEiGELCTRGY 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 327412329 439 NVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYVHG 515
Cdd:PRK12583 408 SVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMI-IRGGENIYPREIEEFLFTHPAVADVQVFG 483
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
58-469 |
5.98e-28 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 118.29 E-value: 5.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 58 YQVFRRGLSISGNGPCLGFRKPKQPYQWLSYQEVADRAEFLGSGLLQHnckactdqfiGV--------FAQNRPEWIIVE 129
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRAL----------GVkkgdrvaiYLPNIPEAVIAM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 130 LACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVD----KPQKAVLLLEHVE--RKETPGLKLIILMD---------- 193
Cdd:COG0365 82 LACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITAdgglRGGKVIDLKEKVDeaLEELPSLEHVIVVGrtgadvpmeg 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 194 --PFEEALKERGQKCgvviksmqavedcgqenhqAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLK---- 267
Cdd:COG0365 162 dlDWDELLAAASAEF-------------------EPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKyvld 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 268 VTEGDIrllsddmkALCPT------------IFPvvprLLNR----MYDkifSQANTPLKRWLLEFAAKRK-------QA 324
Cdd:COG0365 223 LKPGDV--------FWCTAdigwatghsyivYGP----LLNGatvvLYE---GRPDFPDPGRLWELIEKYGvtvfftaPT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 325 EVRSgIIRndsiWDELFFNKIQASlggCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECtaGCTFTTPGDWTS-- 402
Cdd:COG0365 288 AIRA-LMK----AGDEPLKKYDLS---SLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTET--GGIFISNLPGLPvk 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 327412329 403 -GHVGAPLPCNHIKLVDvEELNywACKG--EGEICVRG--PNVFKGYLKDPDRTKEAL--DSDGWLHTGDIGKW 469
Cdd:COG0365 358 pGSMGKPVPGYDVAVVD-EDGN--PVPPgeEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGARR 428
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
54-482 |
6.52e-28 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 118.90 E-value: 6.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 54 ARTMYQVFRRGLSISGNGPCLgfrkpkqpyqwlSYQEVADR---------AEFLG-----SGLLqHNCKACTDQFIGVFA 119
Cdd:PRK07529 24 PASTYELLSRAAARHPDAPAL------------SFLLDADPldrpetwtyAELLAdvtrtANLL-HSLGVGPGDVVAFLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 120 QNRPEWIIVELACYTYSmVVVPLYDTLGPGAIRYIINTADISTVIVDKP-------QKAVLLLEHVerketPGLKLIILM 192
Cdd:PRK07529 91 PNLPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGAKVLVTLGPfpgtdiwQKVAEVLAAL-----PELRTVVEV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 193 D-------PFEEALKERGQKCGVVIKSMQA-VEDCGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD--- 261
Cdd:PRK07529 165 DlarylpgPKRLAVPLIRRKAHARILDFDAeLARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANawl 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 262 FSGFLKVTEGDIRLlsddmkalCPT----IFPVVPRLLnrmydkifsqanTPLKRwllefaakrkQAEVRSGII---RND 334
Cdd:PRK07529 245 GALLLGLGPGDTVF--------CGLplfhVNALLVTGL------------APLAR----------GAHVVLATPqgyRGP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 335 SIWDEL----------FFN--------KIQASLGG----CVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGC 392
Cdd:PRK07529 295 GVIANFwkiveryrinFLSgvptvyaaLLQVPVDGhdisSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVS 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 393 TFTTP-GDWTSGHVGAPLPCNHIKLVDVEEL-NYW--ACKGE-GEICVRGPNVFKGYLkDPDRTKEALDSDGWLHTGDIG 467
Cdd:PRK07529 375 SVNPPdGERRIGSVGLRLPYQRVRVVILDDAgRYLrdCAVDEvGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLG 453
|
490
....*....|....*
gi 327412329 468 KWLPAGTLKIIDRKK 482
Cdd:PRK07529 454 RIDADGYFWLTGRAK 468
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
228-523 |
7.02e-28 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 118.23 E-value: 7.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 228 VPPQ--PDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgfLKVTEGDIRLLSDDMKALCPTIFPVV-------------- 291
Cdd:PRK08974 199 VKPElvPEDLAFLQYTGGTTGVAKGAMLTHRNMLAN----LEQAKAAYGPLLHPGKELVVTALPLYhifaltvncllfie 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 292 ----------PRLLNRMYDKI-------FSQANTPLKRWLlefaakrkqaevrsgiirNDSIWDELFFNKIQASLGGcvr 354
Cdd:PRK08974 275 lggqnllitnPRDIPGFVKELkkypftaITGVNTLFNALL------------------NNEEFQELDFSSLKLSVGG--- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 355 mivtgAAPASPTVLGFLRAALGCQVYEGYGQTECT---AGCTFTTPGdwTSGHVGAPLPCNHIKLVDvEELNYWACKGEG 431
Cdd:PRK08974 334 -----GMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVNPYDLDY--YSGSIGLPVPSTEIKLVD-DDGNEVPPGEPG 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 432 EICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQI 511
Cdd:PRK08974 406 ELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVYPNEIEDVVMLHPKVLEV 483
|
330
....*....|....*....
gi 327412329 512 Y-------VHGDSLKAFLV 523
Cdd:PRK08974 484 AavgvpseVSGEAVKIFVV 502
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
220-523 |
8.03e-28 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 118.00 E-value: 8.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 220 GQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD-------FSGFLKVTEGDIRLLSDDMKALCPtIFPVVP 292
Cdd:PRK12492 194 GRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANmlqvracLSQLGPDGQPLMKEGQEVMIAPLP-LYHIYA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 293 RLLNRMYDKIFSQANT-------------PLKRWLLE--------FAAKRKQAEVRSgiirndsiwdeLFFNKIQASLGG 351
Cdd:PRK12492 273 FTANCMCMMVSGNHNVlitnprdipgfikELGKWRFSallglntlFVALMDHPGFKD-----------LDFSALKLTNSG 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 352 cvrmivtGAAPASPTVLGFlRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDvEELNYWACKGE 430
Cdd:PRK12492 342 -------GTALVKATAERW-EQLTGCTIVEGYGLTETSPVASTNPYGELARlGTVGIPVPGTALKVID-DDGNELPLGER 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 431 GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQ 510
Cdd:PRK12492 413 GELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLI-IVSGFNVYPNEIEDVVMAHPKVAN 491
|
330 340
....*....|....*....|
gi 327412329 511 IYV-------HGDSLKAFLV 523
Cdd:PRK12492 492 CAAigvpderSGEAVKLFVV 511
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
220-530 |
1.42e-27 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 117.29 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 220 GQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD-------FSGFLKVTEGDIRLLSddmkALCPT-IFPVV 291
Cdd:PRK08751 195 GRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANmqqahqwLAGTGKLEEGCEVVIT----ALPLYhIFALT 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 292 PRLLNRMY-----DKIFSQANTP-----LKRwlLEFAAKRKQAEVRSGIIrNDSIWDELFFNKIQASLGGcvRMIVTGAa 361
Cdd:PRK08751 271 ANGLVFMKiggcnHLISNPRDMPgfvkeLKK--TRFTAFTGVNTLFNGLL-NTPGFDQIDFSSLKMTLGG--GMAVQRS- 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 362 pasptVLGFLRAALGCQVYEGYGQTECT-AGCTFTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNV 440
Cdd:PRK08751 345 -----VAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDACIKD-DAGTVLAIGEIGELCIKGPQV 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 441 FKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYVHG----D 516
Cdd:PRK08751 419 MKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-LVSGFNVYPNEIEDVIAMMPGVLEVAAVGvpdeK 497
|
330
....*....|....
gi 327412329 517 SLKAFLVGIVVPDP 530
Cdd:PRK08751 498 SGEIVKVVIVKKDP 511
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
87-530 |
2.20e-27 |
|
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: 116.19 E-value: 2.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 87 SYQEVADRAEFLGSGLlqHNCKACTDQFIGVFAQNRpewiIVELACYtY-----SMVVVPLYDTLGPGAIRYIINTADIS 161
Cdd:cd12119 27 TYAEVAERARRLANAL--RRLGVKPGDRVATLAWNT----HRHLELY-YavpgmGAVLHTINPRLFPEQIAYIINHAEDR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 162 TVIVDK---PQKAVLL--LEHVERketpglklIILMDPFEEALKERGQKcgvVIKSMQAVEDcgqenhQAPVPPQPD--- 233
Cdd:cd12119 100 VVFVDRdflPLLEAIAprLPTVEH--------VVVMTDDAAMPEPAGVG---VLAYEELLAA------ESPEYDWPDfde 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 234 -DLSIVCFTSGTTGNPKGAMLTHGNVV-----ADFSGFLKVTEGDirllsddmkalcpTIFPVVPrllnrMYdkifsQAN 307
Cdd:cd12119 163 nTAAAICYTSGTTGNPKGVVYSHRSLVlhamaALLTDGLGLSESD-------------VVLPVVP-----MF-----HVN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 308 TplkrWLLEFAA-----------KRKQAEVRSGIIRND---------SIWDELF--FNKIQASLGGCVRMIVTGAAPASP 365
Cdd:cd12119 220 A----WGLPYAAamvgaklvlpgPYLDPASLAELIEREgvtfaagvpTVWQGLLdhLEANGRDLSSLRRVVIGGSAVPRS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 366 TVLGFlrAALGCQVYEGYGQTECTAGCTFTTPgdwTSGHV--------------GAPLPCNHIKLVDVE--ELNyWACKG 429
Cdd:cd12119 296 LIEAF--EERGVRVIHAWGMTETSPLGTVARP---PSEHSnlsedeqlalrakqGRPVPGVELRIVDDDgrELP-WDGKA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 430 EGEICVRGPNVFKGYLKDPDRTkEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVA 509
Cdd:cd12119 370 VGELQVRGPWVTKSYYKNDEES-EALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSG-GEWISSVELENAIMAHPAVA 447
|
490 500
....*....|....*....|.
gi 327412329 510 QIYVhgdslkaflvgIVVPDP 530
Cdd:cd12119 448 EAAV-----------IGVPHP 457
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
82-482 |
2.23e-27 |
|
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: 116.61 E-value: 2.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 82 PYQWLSYQEVADRAEFLGSGLLQHNCKAcTDQFIGVFAQNRpEWIIVELACYTYSMVVVPLydtlGPGAIRyiintadis 161
Cdd:cd05906 36 SEEFQSYQDLLEDARRLAAGLRQLGLRP-GDSVILQFDDNE-DFIPAFWACVLAGFVPAPL----TVPPTY--------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 162 tvivDKPQKAVLLLEHVerKETPGLKLII----LMDPFEEALKERGQkCGVVIKSMQAVEDCGqENHQAPvPPQPDDLSI 237
Cdd:cd05906 101 ----DEPNARLRKLRHI--WQLLGSPVVLtdaeLVAEFAGLETLSGL-PGIRVLSIEELLDTA-ADHDLP-QSRPDDLAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 238 VCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEG------------------------DIRLLSDDMKALCPTIFPVVPR 293
Cdd:cd05906 172 LMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLtpqdvflnwvpldhvgglvelhlrAVYLGCQQVHVPTEEILADPLR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 294 LLNRMyDKiFSQANTplkrWLLEFA-AK-RKQAEVRSgiirnDSIWDelffnkiqasLGGCVRMIVTGAAPASPTVLGFL 371
Cdd:cd05906 252 WLDLI-DR-YRVTIT----WAPNFAfALlNDLLEEIE-----DGTWD----------LSSLRYLVNAGEAVVAKTIRRLL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 372 RAALGCQVYE-----GYGQTECTAGCTFTTP---GDWTSGH----VGAPLPCNHIKLVDVEElnywACKGEGEIC---VR 436
Cdd:cd05906 311 RLLEPYGLPPdairpAFGMTETCSGVIYSRSfptYDHSQALefvsLGRPIPGVSMRIVDDEG----QLLPEGEVGrlqVR 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 327412329 437 GPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkWLPAGTLKIIDRKK 482
Cdd:cd05906 387 GPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
226-532 |
2.56e-27 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 116.66 E-value: 2.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 226 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD--------------------------------FS----GFLKVT 269
Cdd:PRK07059 197 KPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANvlqmeawlqpafekkprpdqlnfvcalplyhiFAltvcGLLGMR 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 270 EG----------DIRLLSDDMKALCPTIFPVVPRLLNRMYdkifsqaNTPlkrwllEFaakrkqaevrsgiirndsiwDE 339
Cdd:PRK07059 277 TGgrnilipnprDIPGFIKELKKYQVHIFPAVNTLYNALL-------NNP------DF--------------------DK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 340 LFFNKIQASLGGcvrmivtGAAPASPTVLGFLRAAlGCQVYEGYG--QTECTAGCTFTTPGDWTsGHVGAPLPCNHIKLV 417
Cdd:PRK07059 324 LDFSKLIVANGG-------GMAVQRPVAERWLEMT-GCPITEGYGlsETSPVATCNPVDATEFS-GTIGLPLPSTEVSIR 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 418 DvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEK 497
Cdd:PRK07059 395 D-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMI-LVSGFNVYPNE 472
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 327412329 498 IENIyIRSQP----VAQIYVH----GDSLKAFlvgIVVPDPEV 532
Cdd:PRK07059 473 IEEV-VASHPgvleVAAVGVPdehsGEAVKLF---VVKKDPAL 511
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
54-619 |
4.26e-27 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 117.65 E-value: 4.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 54 ARTMYQVFRRGLSISGNGPCLGFRKPKQPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACY 133
Cdd:PTZ00297 426 VRSLGEMWERSVTRHSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGVRP--GDVIGVDCEASRNIVILEVACA 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 134 TYSMVVVPLydtLGPG-AIRYIINTADISTVIVDKPQKAVLLLEHVERKETpglklIILMDPFEEALKERGQK-CGVVIK 211
Cdd:PTZ00297 504 LYGFTTLPL---VGKGsTMRTLIDEHKIKVVFADRNSVAAILTCRSRKLET-----VVYTHSFYDEDDHAVARdLNITLI 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 212 SMQAVEdcgQENHQAPVPPQP--DDLSIVCFTSGTTGNPKGAML-----THGNVVADFSGFL------------------ 266
Cdd:PTZ00297 576 PYEFVE---QKGRLCPVPLKEhvTTDTVFTYVVDNTTSASGDGLavvrvTHADVLRDISTLVmtgvlpssfkkhlmvhft 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 267 -------------------KVTEGDIRLLSDDMKALCPTIFPVVPRLlnrmydkiFSQANTPLKR----------WLLEf 317
Cdd:PTZ00297 653 pfamlfnrvfvlglfahgsAVATVDAAHLQRAFVKFQPTILVAAPSL--------FSTSRLQLSRanerysavysWLFE- 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 318 aakrKQAEVRSGII----RNDSIWDELFFNKIQASLGGCVRMIVTGAAPASPTV-----LGFLRAALGCQVYegygQTEC 388
Cdd:PTZ00297 724 ----RAFQLRSRLInihrRDSSLLRFIFFRATQELLGGCVEKIVLCVSEESTSFsllehISVCYVPCLREVF----FLPS 795
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 389 TAGCTFTtpgdwtsghvGAPLPCNHIKLVDVEELNYWACKGEGEICVRGpnvfkgylkDPDRTKEAldsdgwlhtgdIGK 468
Cdd:PTZ00297 796 EGVFCVD----------GTPAPSLQVDLEPFDEPSDGAGIGQLVLAKKG---------EPRRTLPI-----------AAQ 845
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 469 WLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAfLVGIVVPDPEVMP-SWAQKRGIE--GT 545
Cdd:PTZ00297 846 WKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfEWRQSHCMGegGG 924
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 327412329 546 YADLCTNKDLKK----AILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 619
Cdd:PTZ00297 925 PARQLGWTELVAyassLLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERFYS 1002
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
86-540 |
1.03e-26 |
|
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: 113.34 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLGSGLlqHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 165
Cdd:cd05935 2 LTYLELLEVVKKLASFL--SNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 166 DKPQkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhqapvppqpDDLSIVCFTSGTT 245
Cdd:cd05935 80 GSEL---------------------------------------------------------------DDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 246 GNPKGAMLTHGNVVADFSGFLKVTEGDirlLSDDMKALCPTIFpvVPRLLNRMYDKIFSQANTPL-KRWLLEFAakRKQA 324
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSAVWTGLT---PSDVILACLPLFH--VTGFVGSLNTAVYVGGTYVLmARWDRETA--LELI 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 325 EVRSGIIRNDS---IWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT 401
Cdd:cd05935 170 EKYKVTFWTNIptmLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPK 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 402 SGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDG---WLHTGDIGKWLPAGTLKII 478
Cdd:cd05935 250 LQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFV 329
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 327412329 479 DRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLVgiVVP------DPEVMPSWAQKR 540
Cdd:cd05935 330 DRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVisvpderVGEEVKAFIV--LRPeyrgkvTEEDIIEWAREQ 401
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
123-530 |
1.11e-26 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 114.20 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 123 PEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDkPQKAVLLLEHVERKETPGLkliilmdpfeEALKER 202
Cdd:PRK07514 64 PEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCD-PANFAWLSKIAAAAGAPHV----------ETLDAD 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 203 GQkcGVViksMQAVEDCGQEnhQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGN------VVADFSGFlkvTEGDiRLL 276
Cdd:PRK07514 133 GT--GSL---LEAAAAAPDD--FETVPRGADDLAAILYTSGTTGRSKGAMLSHGNllsnalTLVDYWRF---TPDD-VLI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 277 sddmKALcPtIFPVvprllnrmyDKIFSQANTPLKR-----WLLEFAAKR-----KQAEVRSGI----IRndsIWDELFF 342
Cdd:PRK07514 202 ----HAL-P-IFHT---------HGLFVATNVALLAgasmiFLPKFDPDAvlalmPRATVMMGVptfyTR---LLQEPRL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 343 NKIQASlggCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTfTTP--GDWTSGHVGAPLPCNHIKLVDVE 420
Cdd:PRK07514 264 TREAAA---HMRLFISGSAPLLAETHREFQERTGHAILERYGMTE-TNMNT-SNPydGERRAGTVGFPLPGVSLRVTDPE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 421 ---ELNywacKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIfkLAQGEY-VAP 495
Cdd:PRK07514 339 tgaELP----PGEiGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDL--IISGGYnVYP 412
|
410 420 430
....*....|....*....|....*....|....*....
gi 327412329 496 EKIENiYIRSQP-VAQIYVHGDSLKAF---LVGIVVPDP 530
Cdd:PRK07514 413 KEVEG-EIDELPgVVESAVIGVPHPDFgegVTAVVVPKP 450
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
121-523 |
3.75e-26 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 112.47 E-value: 3.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 121 NRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDkpQKAVLLLEHVERKETPGLKLIILMDPFEEALK 200
Cdd:PRK08008 71 NCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTS--AQFYPMYRQIQQEDATPLRHICLTRVALPADD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 201 ergqkcGVV----IKSMQAVEDCGQenhqapVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVTEGDIRll 276
Cdd:PRK08008 149 ------GVSsftqLKAQQPATLCYA------PPLSTDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYYSAWQCALR-- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 277 SDDMKALCPTIFPVVPRLLNRMydKIFSQANTPLkrwLLE-FAAKRKQAEVRsgiirndsiwdelffnKIQASLGGCVRM 355
Cdd:PRK08008 213 DDDVYLTVMPAFHIDCQCTAAM--AAFSAGATFV---LLEkYSARAFWGQVC----------------KYRATITECIPM 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 356 IVTG--AAPASPT--------VLGFLRAA----------LGCQVYEGYGQTECTAGCTFTTPGD---WTSghVGAPLPCN 412
Cdd:PRK08008 272 MIRTlmVQPPSANdrqhclreVMFYLNLSdqekdafeerFGVRLLTSYGMTETIVGIIGDRPGDkrrWPS--IGRPGFCY 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 413 HIKLVDveELNYWACKGE-GEICVRG---PNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLA 488
Cdd:PRK08008 350 EAEIRD--DHNRPLPAGEiGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG 427
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 327412329 489 qGEYVAPEKIENIyIRSQP-VAQIYVHG--DSL-----KAFLV 523
Cdd:PRK08008 428 -GENVSCVELENI-IATHPkIQDIVVVGikDSIrdeaiKAFVV 468
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
230-530 |
6.15e-26 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 112.07 E-value: 6.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 230 PQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD---FSGFLKVTEGDIRLLSDDMKALCPTIFPV-VPRLLN--------- 296
Cdd:PRK13295 194 PGPDDVTQLIYTSGTTGEPKGVMHTANTLMANivpYAERLGLGADDVILMASPMAHQTGFMYGLmMPVMLGatavlqdiw 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 297 ---RMYDKI------FSQANTPlkrWLLEFAakRKQAEVRSGIirndsiwdelffnkiqASLggcvRMIVTGAAPASPTV 367
Cdd:PRK13295 274 dpaRAAELIrtegvtFTMASTP---FLTDLT--RAVKESGRPV----------------SSL----RTFLCAGAPIPGAL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 368 LGFLRAALGCQVYEGYGQTECTAgCTFTTPGD---WTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGY 444
Cdd:PRK13295 329 VERARAALGAKIVSAWGMTENGA-VTLTKLDDpdeRASTTDGCPLPGVEVRVVD-ADGAPLPAGQIGRLQVRGCSNFGGY 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 445 LKDPDRTkeALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQiyvhgdslkaflVG 524
Cdd:PRK13295 407 LKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEALLYRHPAIAQ------------VA 471
|
....*..
gi 327412329 525 IV-VPDP 530
Cdd:PRK13295 472 IVaYPDE 478
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
84-540 |
6.33e-26 |
|
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: 113.80 E-value: 6.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 84 QWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELA------CYtysmvvVPLyDTLGPGA-IRYIIN 156
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALGVGP--GDLVGVCLERSLEMVVALLAvlkagaAY------VPL-DPAYPAErLAYMLE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 157 TADISTVIVDkpqkavlllehverketpglkliilmdpfeEALKERGQKCGVVIKSMQAVEDCGQENHQAPVPPQPDDLS 236
Cdd:COG1020 571 DAGARLVLTQ------------------------------SALAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLA 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 237 IVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTEGDiRLLsddMKA-LC--PTIFPVVPRLLN--RMYdkIFSQANT 308
Cdd:COG1020 621 YVIYTSGSTGRPKGVMVEHRALVnllAWMQRRYGLGPGD-RVL---QFAsLSfdASVWEIFGALLSgaTLV--LAPPEAR 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 309 P----LKRWLlefaakrkqaeVRSGIirndSIWD------ELFfnkIQASLGGC--VRMIVTGAAPASPTVLGFLRAAL- 375
Cdd:COG1020 695 RdpaaLAELL-----------ARHRV----TVLNltpsllRAL---LDAAPEALpsLRLVLVGGEALPPELVRRWRARLp 756
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 376 GCQVYEGYGQTECTAGCTF--TTPGDWTSGHV--GAPLPCNHIKLVDvEELN---YWACkgeGEICVRGPNVFKGYLKDP 448
Cdd:COG1020 757 GARLVNLYGPTETTVDSTYyeVTPPDADGGSVpiGRPIANTRVYVLD-AHLQpvpVGVP---GELYIGGAGLARGYLNRP 832
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 449 DRTKEA-----LDSDG--WLHTGDIGKWLPAGTLKIIDRKKHifklaQ----------GEyvapekIENIyIRSQP-VAQ 510
Cdd:COG1020 833 ELTAERfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRADD-----QvkirgfrielGE------IEAA-LLQHPgVRE 900
|
490 500 510
....*....|....*....|....*....|...
gi 327412329 511 IYV--HGDSL-KAFLVGIVVPDPEVMPSWAQKR 540
Cdd:COG1020 901 AVVvaREDAPgDKRLVAYVVPEAGAAAAAALLR 933
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
121-501 |
8.01e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 111.79 E-value: 8.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 121 NRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADiSTVIVDKPQKAVLLLEhvERKETPGLKLIILMDPFEEAlk 200
Cdd:PRK07786 76 NRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCG-AHVVVTEAALAPVATA--VRDIVPLLSTVVVAGGSSDD-- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 201 ergqkcGVViksmqAVEDCGQENHQAPVPPQ-PDDL-SIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEGDIrllSD 278
Cdd:PRK07786 151 ------SVL-----GYEDLLAEAGPAHAPVDiPNDSpALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADI---NS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 279 DMKALCPTIF------PVVPRLLNRMYDKIFsqantPLKRW----LLEFAAkrkqAEVRSGIIRNDSIWDELFFNKIQAS 348
Cdd:PRK07786 217 DVGFVGVPLFhiagigSMLPGLLLGAPTVIY-----PLGAFdpgqLLDVLE----AEKVTGIFLVPAQWQAVCAEQQARP 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 349 LGGCVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAgCTFTTPGD---WTSGHVGAPLPCNHIKLVDvEELNY 424
Cdd:PRK07786 288 RDLALRVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEMSP-VTCMLLGEdaiRKLGSVGKVIPTVAARVVD-ENMND 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 327412329 425 WACKGEGEICVRGPNVFKGYLKDPDRTKEALDSdGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENI 501
Cdd:PRK07786 366 VPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENV 440
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
86-532 |
8.42e-26 |
|
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: 110.80 E-value: 8.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLyDTLGPGA-IRYIINTADISTVI 164
Cdd:cd05945 17 LTYRELKERADALAAALASLGLDA--GDPVVVYGHKSPDAIAAFLAALKAGHAYVPL-DASSPAErIREILDAAKPALLI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 165 VDkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhqapvppqPDDLSIVCFTSGT 244
Cdd:cd05945 94 AD-----------------------------------------------------------------GDDNAYIIFTSGS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 245 TGNPKGAMLTHGNVVAdFS----GFLKVTEGDIRL----LSDDMKALcpTIFP---------VVPRLLNRMYDKIFSQ-A 306
Cdd:cd05945 109 TGRPKGVQISHDNLVS-FTnwmlSDFPLGPGDVFLnqapFSFDLSVM--DLYPalasgatlvPVPRDATADPKQLFRFlA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 307 NTPLKRWLlefaakrkqaevrsgiiRNDSIWDELF----FNkiQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEG 382
Cdd:cd05945 186 EHGITVWV-----------------STPSFAAMCLlsptFT--PESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNT 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 383 YGQTECTAGCTFT--TP---GDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDS 457
Cdd:cd05945 247 YGPTEATVAVTYIevTPevlDGYDRLPIGYAKPGAKLVILD-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFP 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 458 D---GWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYV----HGDSlKAFLVGIVVPDP 530
Cdd:cd05945 326 DegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIELEEIEAALRQVPGVKEAVVvpkyKGEK-VTELIAFVVPKP 403
|
..
gi 327412329 531 EV 532
Cdd:cd05945 404 GA 405
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
230-538 |
1.95e-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: 108.97 E-value: 1.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 230 PQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF---LKVTEGD----------IRLLSDDMKALcptI--FPVvprl 294
Cdd:cd05912 74 VKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSalnLGLTEDDnwlcalplfhISGLSILMRSV---IygMTV---- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 295 lnRMYDKifsqantplkrwlleFAAKRKQAEVRSGIIRNDSIWDELFFNKIQASLGGC---VRMIVTGAAPASPTVLGFL 371
Cdd:cd05912 147 --YLVDK---------------FDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYpnnLRCILLGGGPAPKPLLEQC 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 372 RAaLGCQVYEGYGQTE-CTAGCTFTtPGDWTS--GHVGAPLPCNHIKLVDVEELNYwackGEGEICVRGPNVFKGYLKDP 448
Cdd:cd05912 210 KE-KGIPVYQSYGMTEtCSQIVTLS-PEDALNkiGSAGKPLFPVELKIEDDGQPPY----EVGEILLKGPNVTKGYLNRP 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 449 DRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYVhgdslkaflVGIvvP 528
Cdd:cd05912 284 DATEESFE-NGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPAIKEAGV---------VGI--P 350
|
330
....*....|
gi 327412329 529 DPEvmpsWAQ 538
Cdd:cd05912 351 DDK----WGQ 356
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
185-503 |
2.73e-25 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 110.07 E-value: 2.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 185 GLKLIILMDPFEEALKERGQKCGVVIKSM-QAVEDC--------GQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTH 255
Cdd:PLN02246 122 GAKLIITQSCYVDKLKGLAEDDGVTVVTIdDPPEGClhfseltqADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTH 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 256 GNVVadfSGFLKVTEGD---IRLLSDDMkALCptIFP----------------------VVPRL-LNRMYDKIFSQANT- 308
Cdd:PLN02246 202 KGLV---TSVAQQVDGEnpnLYFHSDDV-ILC--VLPmfhiyslnsvllcglrvgaailIMPKFeIGALLELIQRHKVTi 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 309 -----PLkrwLLEFAakrKQAEVRSgiirndsiwDELffnkiqASlggcVRMIVTGAAPASPTVLGFLRAALGCQVY-EG 382
Cdd:PLN02246 276 apfvpPI---VLAIA---KSPVVEK---------YDL------SS----IRMVLSGAAPLGKELEDAFRAKLPNAVLgQG 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 383 YGQTE-------CTAgctFT-TPGDWTSGHVGAPLPCNHIKLVDVE---ELNYWACkgeGEICVRGPNVFKGYLKDPDRT 451
Cdd:PLN02246 331 YGMTEagpvlamCLA---FAkEPFPVKSGSCGTVVRNAELKIVDPEtgaSLPRNQP---GEICIRGPQIMKGYLNDPEAT 404
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 327412329 452 KEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYI 503
Cdd:PLN02246 405 ANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAELEALLI 455
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
84-531 |
7.91e-25 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 108.41 E-value: 7.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 84 QWLSYQEVADRAEFLgSGLLQHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTV 163
Cdd:PRK06839 26 EEMTYKQLHEYVSKV-AAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 164 IVDKP-QKAVLLLEHVERKETPglkliilmdpfeealkergqkcgVVIKSMQAVEDCGQENHqapVPPQPDDLSIVCFTS 242
Cdd:PRK06839 105 FVEKTfQNMALSMQKVSYVQRV-----------------------ISITSLKEIEDRKIDNF---VEKNESASFIICYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 243 GTTGNPKGAMLTHGNVVadFSGFLKVTEGDIRllSDDMKALC--------------PTIFP----VVPRLLNRmyDKIFS 304
Cdd:PRK06839 159 GTTGKPKGAVLTQENMF--WNALNNTFAIDLT--MHDRSIVLlplfhiggiglfafPTLFAggviIVPRKFEP--TKALS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 305 QANTplKRWLLEFAAKRKQAEVRSGIIRNDSIWDElffnkiqaslggcVRMIVTGAAPAS-PTVLGFLRAalGCQVYEGY 383
Cdd:PRK06839 233 MIEK--HKVTVVMGVPTIHQALINCSKFETTNLQS-------------VRWFYNGGAPCPeELMREFIDR--GFLFGQGF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 384 GQTEcTAGCTFTTPGD---WTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGW 460
Cdd:PRK06839 296 GMTE-TSPTVFMLSEEdarRKVGSIGKPVLFCDYELID-ENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGW 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 327412329 461 LHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDPE 531
Cdd:PRK06839 373 LCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQV---------INKLSDVYEVAVVG--RQHVK 431
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
86-515 |
1.33e-24 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 107.36 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 165
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLAALGVK--KGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLIT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 166 DkpqkavlllehverketpglkliilmDPFEEALKERGQkcgVVIKSMQAvedcGQENHQAPVPPQP-DDLSIVCFTSGT 244
Cdd:PRK03640 106 D--------------------------DDFEAKLIPGIS---VKFAELMN----GPKEEAEIQEEFDlDEVATIMYTSGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 245 TGNPKGAMLTHGNVVADFSGF---LKVTEGD----------IRLLSDDMKALcptIF--PVVprlLNRMYDK-------- 301
Cdd:PRK03640 153 TGKPKGVIQTYGNHWWSAVGSalnLGLTEDDcwlaavpifhISGLSILMRSV---IYgmRVV---LVEKFDAekinkllq 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 302 -----IFSQANTPLKRWLLEFAAKRkqaevrsgiiRNDSiwdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAAlG 376
Cdd:PRK03640 227 tggvtIISVVSTMLQRLLERLGEGT----------YPSS-----------------FRCMLLGGGPAPKPLLEQCKEK-G 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 377 CQVYEGYGQTEcTAGCTFTTPGDWTS---GHVGAPL-PCNhIKLVDveELNYWACKGEGEICVRGPNVFKGYLKDPDRTK 452
Cdd:PRK03640 279 IPVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCE-LKIEK--DGVVVPPFEEGEIVVKGPNVTKGYLNREDATR 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 327412329 453 EALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYVHG 515
Cdd:PRK03640 355 ETFQ-DGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPGVAEAGVVG 415
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
229-529 |
1.85e-24 |
|
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: 106.62 E-value: 1.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 229 PPQPDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSGF-LKVTEGDIRLLsddmkaLCPTIFPVVprlLNRMYDKIFSQ 305
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLnyVSQPPArLDVGPGSRVAQ------VLSIAFDAC---IGEIFSTLCNG 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 306 ANTPLKRWLLEFAAKRKQAEVrsgIIRNDSIWDEL----FFNkiqaslggcVRMIVTGAAPASPTVLGflRAALGCQVYE 381
Cdd:cd17653 172 GTLVLADPSDPFAHVARTVDA---LMSTPSILSTLspqdFPN---------LKTIFLGGEAVPPSLLD--RWSPGRRLYN 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 382 GYGQTECTAGCTFT--TPGDWTsgHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDG 459
Cdd:cd17653 238 AYGPTECTISSTMTelLPGQPV--TIGKPIPNSTCYILD-ADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDP 314
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 327412329 460 WLH------TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQ---IYVHGDSLKAFlvgiVVPD 529
Cdd:cd17653 315 FWPgsrmyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEIEEVVLQSQPEVTqaaAIVVNGRLVAF----VTPE 388
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
231-531 |
2.73e-24 |
|
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: 106.47 E-value: 2.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 231 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEGDirllSDDmkalcptifpvvpRLL---NRMYD----KIF 303
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLT----SES-------------RVLqfaSYTFDvsilEIF 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 304 sqanTPLkrwllefaakrkqaevRSG----IIRNDSIWDEL--FFNKIQASLGG---------------CVRMIVTGAAP 362
Cdd:cd05918 167 ----TTL----------------AAGgclcIPSEEDRLNDLagFINRLRVTWAFltpsvarlldpedvpSLRTLVLGGEA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 363 ASPTVLGflRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPC--------NHIKLVDVeelnywackGE-GE 432
Cdd:cd05918 227 LTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLGAtcwvvdpdNHDRLVPI---------GAvGE 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 433 ICVRGPNVFKGYLKDPDRTKEA-LDSDGWLH------------TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIE 499
Cdd:cd05918 296 LLIEGPILARGYLNDPEKTAAAfIEDPAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKI-RGQRVELGEIE 374
|
330 340 350
....*....|....*....|....*....|....*....
gi 327412329 500 NiYIRSQP------VAQIYVH-GDSLKAFLVGIVVPDPE 531
Cdd:cd05918 375 H-HLRQSLpgakevVVEVVKPkDGSSSPQLVAFVVLDGS 412
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
86-531 |
8.27e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 105.89 E-value: 8.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 165
Cdd:PRK06178 59 ITYAELDELSDRFAALLRQRGVGA-GDR-VAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 166 dkpQKAVL-LLEHVeRKETPgLKLII---LMD--------PFEEALKERGQKCGVVIKSMQAVEDCGQENHQAPvpPQPD 233
Cdd:PRK06178 137 ---LDQLApVVEQV-RAETS-LRHVIvtsLADvlpaeptlPLPDSLRAPRLAAAGAIDLLPALRACTAPVPLPP--PALD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 234 DLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTEGDIRLLS---------DDMKALCPTIF--PVVprLLNRmy 299
Cdd:PRK06178 210 ALAALNYTGGTTGMPKGCEHTQRDMVytaAAAYAVAVVGGEDSVFLSflpefwiagENFGLLFPLFSgaTLV--LLAR-- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 300 dkifsqantplkrW-LLEFAAKRKQAEVRSGIIRNDSIwDELF---------FNKIQASlgGCVRMIvtgaAPASPTVLG 369
Cdd:PRK06178 286 -------------WdAVAFMAAVERYRVTRTVMLVDNA-VELMdhprfaeydLSSLRQV--RVVSFV----KKLNPDYRQ 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 370 FLRAALGCQVYEG-YGQTECTAGCTFTTpGDWTSGH--------VGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNV 440
Cdd:PRK06178 346 RWRALTGSVLAEAaWGMTETHTCDTFTA-GFQDDDFdllsqpvfVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 441 FKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRsqpvaqiyvHGDSLKA 520
Cdd:PRK06178 425 LKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV-NGMSVFPSEVEALLGQ---------HPAVLGS 493
|
490
....*....|.
gi 327412329 521 FLVGivVPDPE 531
Cdd:PRK06178 494 AVVG--RPDPD 502
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
84-540 |
8.64e-24 |
|
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: 105.10 E-value: 8.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 84 QWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLyDTLGPGA-IRYIINTADIST 162
Cdd:cd17655 21 QTLTYRELNERANQLARTLREKGVGP--DTIVGIMAERSLEMIVGILGILKAGGAYLPI-DPDYPEErIQYILEDSGADI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 163 VIVDKPQKAVLLlehverketpGLKLIILMDpfEEALKErgqkcgvviksmqavedcgQENHQAPVPPQPDDLSIVCFTS 242
Cdd:cd17655 98 LLTQSHLQPPIA----------FIGLIDLLD--EDTIYH-------------------EESENLEPVSKSDDLAYVIYTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 243 GTTGNPKGAMLTHGNVVADFSGFLKV---TEGD--IRLLSDDMKALCPTIFPvvPRLL-NRMYdkIFSQANTPLKRWLLE 316
Cdd:cd17655 147 GSTGKPKGVMIEHRGVVNLVEWANKViyqGEHLrvALFASISFDASVTEIFA--SLLSgNTLY--IVRKETVLDGQALTQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 317 FAAKRkqaevRSGIIR-NDSIWDELffNKIQASLGGCVRMIVTGAAPASPTVLGFL--RAALGCQVYEGYGQTECTAGCT 393
Cdd:cd17655 223 YIRQN-----RITIIDlTPAHLKLL--DAADDSEGLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETTVDAS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 394 F--TTPGDWTSGHV--GAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWL------HT 463
Cdd:cd17655 296 IyqYEPETDQQVSVpiGKPLGNTRIYILD-QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRT 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 464 GDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQ---IYVHGDSLKAFLVGIVVPDPEVMPSWAQKR 540
Cdd:cd17655 375 GDLARWLPDGNIEFLGRIDHQVKI-RGYRIELGEIEARLLQHPDIKEavvIARKDEQGQNYLCAYIVSEKELPVAQLREF 453
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
86-533 |
1.17e-23 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 105.28 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIVELACYTYSMVVV---PLYDTlgpGAIRYIINTADIST 162
Cdd:PRK08315 44 WTYREFNEEVDALAKGLLALGIEK-GDR-VGIWAPNVPEWVLTQFATAKIGAILVtinPAYRL---SELEYALNQSGCKA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 163 -VIVDK--------------PQKAVLLLEHVERKETPGLKLIILMDpfeeALKERGqkcgvvIKSMQAVEDCGQENHQAP 227
Cdd:PRK08315 119 lIAADGfkdsdyvamlyelaPELATCEPGQLQSARLPELRRVIFLG----DEKHPG------MLNFDELLALGRAVDDAE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 228 VPP-----QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsGFLkVTEGdIRLLSDDmkALC---P-------------- 285
Cdd:PRK08315 189 LAArqatlDPDDPINIQYTSGTTGFPKGATLTHRNILNN--GYF-IGEA-MKLTEED--RLCipvPlyhcfgmvlgnlac 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 286 ------TIFPVvprllnrmydkifsQANTPLKrwLLEFAAKRKQ-----------AEVrsgiirndsiwDELFFNKIQAS 348
Cdd:PRK08315 263 vthgatMVYPG--------------EGFDPLA--TLAAVEEERCtalygvptmfiAEL-----------DHPDFARFDLS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 349 lggCVRmivTGAAPASPtvlgflraalgC------QVYE---------GYGQTECTAGCTFTTPGD------WTsghVGA 407
Cdd:PRK08315 316 ---SLR---TGIMAGSP-----------CpievmkRVIDkmhmsevtiAYGMTETSPVSTQTRTDDplekrvTT---VGR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 408 PLPCNHIKLVDVEelnywacKGE-------GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDR 480
Cdd:PRK08315 376 ALPHLEVKIVDPE-------TGEtvprgeqGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGR 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 327412329 481 KKHIFkLAQGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDP----EVM 533
Cdd:PRK08315 449 IKDMI-IRGGENIYPREIEEF---------LYTHPKIQDVQVVG--VPDEkygeEVC 493
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
86-530 |
1.36e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 104.63 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 165
Cdd:PRK08316 37 WTYAELDAAVNRVAAALLDLGLKK-GDR-VAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 166 DkpqkaVLLLEHVErketPGLKLIiLMDPFEEALKERGQkcgVVIKSMQAVEDCGQEnhQAPVPPQP----DDLSIVCFT 241
Cdd:PRK08316 115 D-----PALAPTAE----AALALL-PVDTLILSLVLGGR---EAPGGWLDFADWAEA--GSVAEPDVeladDDLAQILYT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 242 SGTTGNPKGAMLTHGNVVADFSGF---LKVTEGDIRLL------SDDMKALCPTIF-----------PVVPRLLnrmyDK 301
Cdd:PRK08316 180 SGTESLPKGAMLTHRALIAEYVSCivaGDMSADDIPLHalplyhCAQLDVFLGPYLyvgatnvildaPDPELIL----RT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 302 IFSQANTPLkrwlleFAAKrkqaevrsgiirndSIWDELF----FNKIQASlggCVRMIVTGAAPASPTVLGFLRAAL-G 376
Cdd:PRK08316 256 IEAERITSF------FAPP--------------TVWISLLrhpdFDTRDLS---SLRKGYYGASIMPVEVLKELRERLpG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 377 CQVYEGYGQTECTAGCTFTTPGDwtsgHVGAP----LPCNHI--KLVDvEELNYWAcKGE-GEICVRGPNVFKGYLKDPD 449
Cdd:PRK08316 313 LRFYNCYGQTEIAPLATVLGPEE----HLRRPgsagRPVLNVetRVVD-DDGNDVA-PGEvGEIVHRSPQLMLGYWDDPE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 450 RTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPD 529
Cdd:PRK08316 387 KTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEA---------LYTHPAVAEVAVIG--LPD 453
|
.
gi 327412329 530 P 530
Cdd:PRK08316 454 P 454
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
127-499 |
1.46e-23 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 106.16 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 127 IVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKpqkavlllEHVERKETPGLKLIILMDP---FEEALKER- 202
Cdd:PRK08633 680 LANLALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVITSR--------KFLEKLKNKGFDLELPENVkviYLEDLKAKi 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 203 --GQKC--GVVIKSMQAVEDCGQENHqapvPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD---FSGFLKVTEGDiRL 275
Cdd:PRK08633 752 skVDKLtaLLAARLLPARLLKRLYGP----TFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNieqISDVFNLRNDD-VI 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 276 LSddmkALCP---------TIFPvvprLLNRMydKIFSQANtPLKRWLLEFAAKRKQAEVRSGI-------IRNDSIWDE 339
Cdd:PRK08633 827 LS----SLPFfhsfgltvtLWLP----LLEGI--KVVYHPD-PTDALGIAKLVAKHRATILLGTptflrlyLRNKKLHPL 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 340 LFfnkiqASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-----GDWT-----SGHVGAPL 409
Cdd:PRK08633 896 MF-----ASL----RLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNLPdvlaaDFKRqtgskEGSVGMPL 966
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 410 PCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL---DSDGWLHTGDIGKWLPAGTLKIIDRKKHIFK 486
Cdd:PRK08633 967 PGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFAK 1046
|
410
....*....|...
gi 327412329 487 LAqGEYVAPEKIE 499
Cdd:PRK08633 1047 IG-GEMVPLGAVE 1058
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
234-531 |
2.34e-23 |
|
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: 101.58 E-value: 2.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 234 DLSIVCFTSGTTGNPKGAMLTHGNVVA---DFSGFLKVTEGDIRLlsddmkALCPtIFPVVPrlLNrMYDKIFSQ--ANT 308
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAanlQLIHAMGLTEADVYL------NMLP-LFHIAG--LN-LALATFHAggANV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 309 PLKRWLLEFAAKRKQAEvrsgiirNDSIWDElfFNKIQASLggcvrmivTGAAPASPTVLGFLRAALG------------ 376
Cdd:cd17637 71 VMEKFDPAEALELIEEE-------KVTLMGS--FPPILSNL--------LDAAEKSGVDLSSLRHVLGldapetiqrfee 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 377 ---CQVYEGYGQTEcTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveELNYWACKGE-GEICVRGPNVFKGYLKDPDRTK 452
Cdd:cd17637 134 ttgATFWSLYGQTE-TSGLVTLSPYRERPGSAGRPGPLVRVRIVD--DNDRPVPAGEtGEIVVRGPLVFQGYWNLPELTA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 453 EALDsDGWLHTGDIGKWLPAGTLKIIDRK--KHIFKlAQGEYVAPEKIENIyIRSQP-VAQIYVHGdslkaflvgivVPD 529
Cdd:cd17637 211 YTFR-NGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKV-ILEHPaIAEVCVIG-----------VPD 276
|
..
gi 327412329 530 PE 531
Cdd:cd17637 277 PK 278
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
224-535 |
2.57e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 103.53 E-value: 2.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 224 HQAPVPPqPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEgdirLLSDDMKALCPTIFPV---VPRLLNrmyd 300
Cdd:PRK07787 120 HRYPEPD-PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQ----WTADDVLVHGLPLFHVhglVLGVLG---- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 301 kifsqantPLKR-----WLLEFAAKRKQAEVRSGiirndsiwDELFFN------------KIQASLGGcVRMIVTGAAPA 363
Cdd:PRK07787 191 --------PLRIgnrfvHTGRPTPEAYAQALSEG--------GTLYFGvptvwsriaadpEAARALRG-ARLLVSGSAAL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 364 SPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGE--GEICVRGPNVF 441
Cdd:PRK07787 254 PVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVD-EDGGPVPHDGEtvGELQVRGPTLF 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 442 KGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDR------KKHIFKLAQGEyvapekIENIYIRSQPVAQIYVHG 515
Cdd:PRK07787 333 DGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGGYRIGAGE------IETALLGHPGVREAAVVG 406
|
330 340
....*....|....*....|...
gi 327412329 516 ---DSLKAFLVGIVVPDPEVMPS 535
Cdd:PRK07787 407 vpdDDLGQRIVAYVVGADDVAAD 429
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
117-530 |
6.50e-23 |
|
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: 102.96 E-value: 6.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 117 VFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKavlLLEHVE--RKETPGL-KLIILMD 193
Cdd:cd05970 77 LTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDN---IPEEIEkaAPECPSKpKLVWVGD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 194 PFEEALKERGQKCgvviksMQAVEDCgqENHQAPVPPQPDDLSIVCFTSGTTGNPKgaMLTHGN-------VVADFsgFL 266
Cdd:cd05970 154 PVPEGWIDFRKLI------KNASPDF--ERPTANSYPCGEDILLVYFSSGTTGMPK--MVEHDFtyplghiVTAKY--WQ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 267 KVTEGDIRLLSDDM---KALCPTIF-------PVVprllnrMYD-KIFSQANtplkrwLLEFAAKRKQAE------VRSG 329
Cdd:cd05970 222 NVREGGLHLTVADTgwgKAVWGKIYgqwiagaAVF------VYDyDKFDPKA------LLEKLSKYGVTTfcapptIYRF 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 330 IIRND-SIWDelfFNKIqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPG-DWTSGHVGA 407
Cdd:cd05970 290 LIREDlSRYD---LSSL--------RYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTL-TIATFPWmEPKPGSMGK 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 408 PLPCNHIKLVDVEELnywACKG--EGEICVRGPN-----VFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDR 480
Cdd:cd05970 358 PAPGYEIDLIDREGR---SCEAgeEGEIVIRTSKgkpvgLFGGYYKDAEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGR 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 327412329 481 KKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYVHGdslkaflvgivVPDP 530
Cdd:cd05970 434 TDDLIK-SSGYRIGPFEVESALIQHPAVLECAVTG-----------VPDP 471
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
234-610 |
6.63e-23 |
|
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: 100.10 E-value: 6.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 234 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTEGDIRLLSddmkalcptiFPVVprllnrmydKIFSQAntPL 310
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGlhsRLGFGGGDSWLLS----------LPLY---------HVGGLA--IL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 311 KRWLL---EFAAKRKQAEVRSGIIRND------------SIWDELFFNKIQASLggcvRMIVTGAAPASPtvlGFLRAA- 374
Cdd:cd17630 60 VRSLLagaELVLLERNQALAEDLAPPGvthvslvptqlqRLLDSGQGPAALKSL----RAVLLGGAPIPP---ELLERAa 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 375 -LGCQVYEGYGQTEcTAGCTFT-TPGDWTSGHVGAPLPCNHIKLVDveelnywackgEGEICVRGPNVFKGYLKDPdrTK 452
Cdd:cd17630 133 dRGIPLYTTYGMTE-TASQVATkRPDGFGRGGVGVLLPGRELRIVE-----------DGEIWVGGASLAMGYLRGQ--LV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 453 EALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIyIRSQP-VAQIYVHGdslkaflvgivVPDPE 531
Cdd:cd17630 199 PEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAA-LAAHPaVRDAFVVG-----------VPDEE 265
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 327412329 532 vmpsWAQKrgiegTYADLCTNKDLKKAILEDMVRlgkeSGLHSFEQVKAIHIhsdmfsVQNGLLTPTLKAKRPELREYF 610
Cdd:cd17630 266 ----LGQR-----PVAVIVGRGPADPAELRAWLK----DKLARFKLPKRIYP------VPELPRTGGGKVDRRALRAWL 325
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
85-467 |
1.50e-22 |
|
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: 101.93 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 85 WLSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNrPEWIIVELACYTYSMVVVPLYDTLGPGA---IRYIINTADIS 161
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAVG--KPGDRVLLLAPPG-LDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 162 TVIVDKPQKAvLLLEHVERKETPGLKLIILMDPFEEALKERGQkcgvviksmqavedcgqenhqaPVPPQPDDLSIVCFT 241
Cdd:cd05931 101 VVLTTAAALA-AVRAFAASRPAAGTPRLLVVDLLPDTSAADWP----------------------PPSPDPDDIAYLQYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 242 SGTTGNPKGAMLTHGNVVADFSGFLKVTEGD--IRLLS-----DDM---KALCPTIF---PVVprLLNRMYdkiFSQAnt 308
Cdd:cd05931 158 SGSTGTPKGVVVTHRNLLANVRQIRRAYGLDpgDVVVSwlplyHDMgliGGLLTPLYsggPSV--LMSPAA---FLRR-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 309 PLkRWL-----------------LEFAAKRKQAEVRSGIirndsiwdELffnkiqaslgGCVRMIVTGAAPASPTVL--- 368
Cdd:cd05931 231 PL-RWLrlisryratisaapnfaYDLCVRRVRDEDLEGL--------DL----------SSWRVALNGAEPVRPATLrrf 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 369 -------GFLRAAlgcqVYEGYGQTECTAGCTFTTPG----------DWTSGHV----------------GAPLPCNHIK 415
Cdd:cd05931 292 aeafapfGFRPEA----FRPSYGLAEATLFVSGGPPGtgpvvlrvdrDALAGRAvavaaddpaarelvscGRPLPDQEVR 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 327412329 416 LVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKE------ALDSDGWLHTGDIG 467
Cdd:cd05931 368 IVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaATDEGGWLRTGDLG 425
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
86-532 |
3.77e-22 |
|
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: 99.97 E-value: 3.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELA------CYtysmvvVPLYDTLGPGAIRYIINTAD 159
Cdd:cd12117 23 LTYAELNERANRLARRLRAAGVGP--GDVVGVLAERSPELVVALLAvlkagaAY------VPLDPELPAERLAFMLADAG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 160 ISTVIVDKPQKAVLLLehverketPGLKLIILMDPFEEALKErgqkcgvviksmqavedcgqenhqAPVPPQPDDLSIVC 239
Cdd:cd12117 95 AKVLLTDRSLAGRAGG--------LEVAVVIDEALDAGPAGN------------------------PAVPVSPDDLAYVM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 240 FTSGTTGNPKGAMLTHGNVV--ADFSGFLKVTEGDIRL----LSDDmkALCPTIFpvVPrLLN----RMYDKifsqaNTP 309
Cdd:cd12117 143 YTSGSTGRPKGVAVTHRGVVrlVKNTNYVTLGPDDRVLqtspLAFD--ASTFEIW--GA-LLNgarlVLAPK-----GTL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 310 LKrwllefaAKRKQAEVRSGIIrnDSIWdeL---FFNKI----QASLGGcVRMIVTGAAPASPT-VLGFLRAALGCQVYE 381
Cdd:cd12117 213 LD-------PDALGALIAEEGV--TVLW--LtaaLFNQLadedPECFAG-LRELLTGGEVVSPPhVRRVLAACPGLRLVN 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 382 GYGQTECTagcTFTT-----PGDWTSGHV--GAPLPCNHIKLVDveELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKE 453
Cdd:cd12117 281 GYGPTENT---TFTTshvvtELDEVAGSIpiGRPIANTRVYVLD--EDGRPVPPGVpGELYVGGDGLALGYLNRPALTAE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 454 ALDSDGWL------HTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIyIRSQP-VAQIYV---HGDSLKAFLV 523
Cdd:cd12117 356 RFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRIELGEIEAA-LRAHPgVREAVVvvrEDAGGDKRLV 433
|
....*....
gi 327412329 524 GIVVPDPEV 532
Cdd:cd12117 434 AYVVAEGAL 442
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
86-534 |
4.60e-22 |
|
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: 99.65 E-value: 4.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 165
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVR--PGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 166 DKPQkavlllehvERKETPGLKLIILMDPFEEALKErgqkcgvviksmqavedcgqenhQAPVPPQPDDLSIVCFTSGTT 245
Cdd:cd12114 91 DGPD---------AQLDVAVFDVLILDLDALAAPAP-----------------------PPPVDVAPDDLAYVIFTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 246 GNPKGAMLTHG---NVVADFSGFLKVTEGDIRL----LSDDMKAlcptifpvvprllnrmYDkIF--------------S 304
Cdd:cd12114 139 GTPKGVMISHRaalNTILDINRRFAVGPDDRVLalssLSFDLSV----------------YD-IFgalsagatlvlpdeA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 305 QANTPlKRWllefaakrKQAEVRSGIirndSIWdelffNKIQASLGgcvrMIVTgAAPASPTVLGFLRAAL--------- 375
Cdd:cd12114 202 RRRDP-AHW--------AELIERHGV----TLW-----NSVPALLE----MLLD-VLEAAQALLPSLRLVLlsgdwipld 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 376 ----------GCQVYEGYGQTECTAGCTF----TTPGDWTSGHVGAPLPCNHIKLVD--VEELNYWackGEGEICVRGPN 439
Cdd:cd12114 259 lparlralapDARLISLGGATEASIWSIYhpidEVPPDWRSIPYGRPLANQRYRVLDprGRDCPDW---VPGELWIGGRG 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 440 VFKGYLKDPDRTKEAL--DSDG--WLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQ--IYV 513
Cdd:cd12114 336 VALGYLGDPELTAARFvtHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKV-RGYRIELGEIEAALQAHPGVARavVVV 414
|
490 500
....*....|....*....|.
gi 327412329 514 HGDSLKAFLVGIVVPDPEVMP 534
Cdd:cd12114 415 LGDPGGKRLAAFVVPDNDGTP 435
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
77-494 |
7.73e-22 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 99.95 E-value: 7.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 77 RKPKQPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPL---YDTLG--PGAI 151
Cdd:PRK08180 61 RGADGGWRRLTYAEALERVRAIAQALLDRGLSA--ERPLMILSGNSIEHALLALAAMYAGVPYAPVspaYSLVSqdFGKL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 152 RYIINTADISTVIVDKPQK-----AVLLLEHVE----RKETPGLKLIilmdPFEEALKERGQkcGVVIKSMQAVedcgqe 222
Cdd:PRK08180 139 RHVLELLTPGLVFADDGAAfaralAAVVPADVEvvavRGAVPGRAAT----PFAALLATPPT--AAVDAAHAAV------ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 223 nhqapvppQPDDLSIVCFTSGTTGNPKGAMLTHG---------------------------------------NVVADFS 263
Cdd:PRK08180 207 --------GPDTIAKFLFTSGSTGLPKAVINTHRmlcanqqmlaqtfpflaeeppvlvdwlpwnhtfggnhnlGIVLYNG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 264 GFL-----KVTEGDIRLLSDDMKALCPTIFPVVPRLlnrmydkifsqantplkrWLLEFAAKRKQAEVRsgiirndsiwd 338
Cdd:PRK08180 279 GTLyiddgKPTPGGFDETLRNLREISPTVYFNVPKG------------------WEMLVPALERDAALR----------- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 339 ELFFNKiqaslggcVRMIVTGAAPASPTVLGFL----RAALGCQVY--EGYGQTECTAGCTFTTPGDWTSGHVGAPLPCN 412
Cdd:PRK08180 330 RRFFSR--------LKLLFYAGAALSQDVWDRLdrvaEATCGERIRmmTGLGMTETAPSATFTTGPLSRAGNIGLPAPGC 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 413 HIKLVDVEelnywackGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWL----PAGTLKIIDRKKHIFKLA 488
Cdd:PRK08180 402 EVKLVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVdpadPERGLMFDGRIAEDFKLS 473
|
....*.
gi 327412329 489 QGEYVA 494
Cdd:PRK08180 474 SGTWVS 479
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
231-540 |
5.30e-21 |
|
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: 96.00 E-value: 5.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 231 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEGD---IRLLS-----------DDMKALCP--TIFPVVPRL 294
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDsfpVRLLQmasfsfdvfagDFARSLLNggTLVICPDEV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 295 L---NRMYDKIFSQ-----ANTP-LKRWLLEFAAKRKQ--AEVRSGIIRNDSIWDElFFNKIQASLGGCVRMIvtgaapa 363
Cdd:cd17650 171 KldpAALYDLILKSritlmESTPaLIRPVMAYVYRNGLdlSAMRLLIVGSDGCKAQ-DFKTLAARFGQGMRII------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 364 spTVLGFLRAALGCQVYEGYGQTECTAGctfTTPgdwtsghVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKG 443
Cdd:cd17650 243 --NSYGVTEATIDSTYYEEGRDPLGDSA---NVP-------IGRPLPNTAMYVLD-ERLQPQPVGVAGELYIGGAGVARG 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 444 YLKDPDRTKEALDSDGW------LHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYV---H 514
Cdd:cd17650 310 YLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RGFRIELGEIESQLARHPAIDEAVVavrE 388
|
330 340
....*....|....*....|....*.
gi 327412329 515 GDSLKAFLVGIVVPDPEvmPSWAQKR 540
Cdd:cd17650 389 DKGGEARLCAYVVAAAT--LNTAELR 412
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
226-538 |
5.79e-21 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 96.83 E-value: 5.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 226 APVPPQpDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTE-----------------------------GDIRL- 275
Cdd:PLN02574 192 KPVIKQ-DDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEAsqyeypgsdnvylaalpmfhiyglslfvvGLLSLg 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 276 ----------LSDDMKAL---CPTIFPVVPRLLNRMYDKIFSQANTPLKrwllefaakrkqaevrsgiirndsiwdelff 342
Cdd:PLN02574 271 stivvmrrfdASDMVKVIdrfKVTHFPVVPPILMALTKKAKGVCGEVLK------------------------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 343 nkiqaslggCVRMIVTGAAPAS-PTVLGFLRAALGCQVYEGYGQTECTAGCT--FTTPGDWTSGHVGAPLPCNHIKLVDV 419
Cdd:PLN02574 320 ---------SLKQVSCGAAPLSgKFIQDFVQTLPHVDFIQGYGMTESTAVGTrgFNTEKLSKYSSVGLLAPNMQAKVVDW 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 420 EELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIE 499
Cdd:PLN02574 391 STGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIAPADLE 469
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 327412329 500 NIYIrSQP----VAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQ 538
Cdd:PLN02574 470 AVLI-SHPeiidAAVTAVPDKECGEIPVAFVVRRQGSTLSQEA 511
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
232-540 |
8.67e-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: 341266 [Multi-domain] Cd Length: 359 Bit Score: 94.47 E-value: 8.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 232 PDDLSIVCFTSGTTGNPKGAMLTHGNVVAD---FSGFLKVTEGDIrllsddmkALCPT----IFPVVPRLLNrmydKIFS 304
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNawmLALNSLFDPDDV--------LLCGLplfhVNGSVVTLLT----PLAS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 305 QAN----TPL---------KRWLLefaAKRKQAEVRSGIirnDSIWDELFFNKIQASLGGcVRMIVTGAAPASPTVLGFL 371
Cdd:cd05944 69 GAHvvlaGPAgyrnpglfdNFWKL---VERYRITSLSTV---PTVYAALLQVPVNADISS-LRFAMSGAAPLPVELRARF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 372 RAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLV--DVEELNYWACKGE--GEICVRGPNVFKGYLK 446
Cdd:cd05944 142 EDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKvlDGVGRLLRDCAPDevGEICVAGPGVFGGYLY 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 447 DpDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYVHG--DSLKAFL-V 523
Cdd:cd05944 222 T-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRHPAVAFAGAVGqpDAHAGELpV 299
|
330 340
....*....|....*....|...
gi 327412329 524 GIV--VPDPEVMP----SWAQKR 540
Cdd:cd05944 300 AYVqlKPGAVVEEeellAWARDH 322
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
86-501 |
1.30e-20 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 96.96 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLGsGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 165
Cdd:PRK06814 659 LTYRKLLTGAFVLG-RKLKKNTPP--GENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 166 DKP--QKAVL--LLEHVERketpGLKLIILMDPFEE---ALKERGqkcgVVIKSMQAVEDCGqenhqapvpPQPDDLSIV 238
Cdd:PRK06814 736 SRAfiEKARLgpLIEALEF----GIRIIYLEDVRAQiglADKIKG----LLAGRFPLVYFCN---------RDPDDPAVI 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 239 CFTSGTTGNPKGAMLTHGNVVA---------DFSGFLKV------------TEGDIRLLSDDMKAL---CPTIFPVVPRL 294
Cdd:PRK06814 799 LFTSGSEGTPKGVVLSHRNLLAnraqvaariDFSPEDKVfnalpvfhsfglTGGLVLPLLSGVKVFlypSPLHYRIIPEL 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 295 LnrmYDK----IFSqANTPLkrwllefaakrkqaevrSGIIRNDSIWDelFFNkiqaslggcVRMIVTGAAPASPTVLGF 370
Cdd:PRK06814 879 I---YDTnatiLFG-TDTFL-----------------NGYARYAHPYD--FRS---------LRYVFAGAEKVKEETRQT 926
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 371 LRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNywacKGeGEICVRGPNVFKGYLK-DPD 449
Cdd:PRK06814 927 WMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGID----EG-GRLFVRGPNVMLGYLRaENP 1001
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 327412329 450 RTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENI 501
Cdd:PRK06814 1002 GVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVEEL 1051
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
221-523 |
1.99e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 95.10 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 221 QENHQAPVPPQPD-DLSIVCFTSGTTGNPKGAMLTHGNVVAD------------------------FSGF-------LKV 268
Cdd:PRK06710 193 EVNTGVEVPCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSNtlmgvqwlynckegeevvlgvlpfFHVYgmtavmnLSI 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 269 TEG---------DIRLLSDDMKALCPTIFPVVPRLLnrmydkiFSQANTPLkrwllefaakRKQAEVRSgiirndsiwde 339
Cdd:PRK06710 273 MQGykmvlipkfDMKMVFEAIKKHKVTLFPGAPTIY-------IALLNSPL----------LKEYDISS----------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 340 lffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgctfTTPGDW-----TSGHVGAPLPCNHI 414
Cdd:PRK06710 325 -------------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSP----VTHSNFlwekrVPGSIGVPWPDTEA 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 415 KLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVA 494
Cdd:PRK06710 388 MIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVY 465
|
330 340 350
....*....|....*....|....*....|....*.
gi 327412329 495 PEKIENIYIRSQPVAQIYV-------HGDSLKAFLV 523
Cdd:PRK06710 466 PREVEEVLYEHEKVQEVVTigvpdpyRGETVKAFVV 501
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
115-543 |
2.17e-20 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 94.04 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 115 IGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDkpqkavlllehverketpglkliilmdp 194
Cdd:cd05971 34 VGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTD---------------------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 195 feealkergqkcgvviksmqavedcgqenhqapvppQPDDLSIVCFTSGTTGNPKGAMLTH----GNVVADFSGF-LKVT 269
Cdd:cd05971 86 ------------------------------------GSDDPALIIYTSGTTGPPKGALHAHrvllGHLPGVQFPFnLFPR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 270 EGDIRLLSDD-------MKALCPTIFPVVPRLLNRMydKIFS--QANTPLKRW------LLEFAAK--RKQAEVRSGIIR 332
Cdd:cd05971 130 DGDLYWTPADwawigglLDVLLPSLYFGVPVLAHRM--TKFDpkAALDLMSRYgvttafLPPTALKmmRQQGEQLKHAQV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 333 NdsiwdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEC---TAGCTFTTPGDwtSGHVGAPL 409
Cdd:cd05971 208 K-------------------LRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECnlvIGNCSALFPIK--PGSMGKPI 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 410 PCNHIKLVDvEELNYWACKGEGEICVRGPN--VFKGYLKDPDRTKEALDSDgWLHTGDIGKWLPAGTLKIIDRKKHIFKL 487
Cdd:cd05971 267 PGHRVAIVD-DNGTPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDDVITS 344
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 327412329 488 AqGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFlvgiVVPDPEVMPSWAQKRGIE 543
Cdd:cd05971 345 S-GYRIGPAEIEECLLKHPAVLMAAVvgipdpiRGEIVKAF----VVLNPGETPSDALAREIQ 402
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
72-530 |
2.51e-20 |
|
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: 94.81 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 72 PCLGFRKPKQPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTY---SMVVVPLYDTLGp 148
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLSA--ERPLLILSGNSIEHALMALAAMYAgvpAAPVSPAYSLMS- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 149 gairyiintADISTvivdkpqkavllLEHVERKETPGLKLIILMDPFEEALKERGQKCGVVIKSMQAVEDCGQEN----- 223
Cdd:cd05921 89 ---------QDLAK------------LKHLFELLKPGLVFAQDAAPFARALAAIFPLGTPLVVSRNAVAGRGAISfaela 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 224 HQAP---VPP-----QPDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgflkvtegdirllSDDMKALCPTIF-PVVPRL 294
Cdd:cd05921 148 ATPPtaaVDAafaavGPDTVAKFLFTSGSTGLPKAVINTQRMLCA----------------NQAMLEQTYPFFgEEPPVL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 295 LNRM-YDKIFS-----------------QANTPLK-------RWLLE-----FAAKRKQAEVRSGIIRNDSIWDELFFNK 344
Cdd:cd05921 212 VDWLpWNHTFGgnhnfnlvlynggtlyiDDGKPMPggfeetlRNLREisptvYFNVPAGWEMLVAALEKDEALRRRFFKR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 345 iqaslggcVRMIVTGAAPASPTVLGFLRA----ALGCQV--YEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVd 418
Cdd:cd05921 292 --------LKLMFYAGAGLSQDVWDRLQAlavaTVGERIpmMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKLV- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 419 veelnywACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWL----PAGTLKIIDRKKHIFKLAQGEYVA 494
Cdd:cd05921 363 -------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpddPAKGLVFDGRVAEDFKLASGTWVS 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 327412329 495 --PekieniyIRSQPVAQI--YVHgDSL-----KAFLVGIVVPDP 530
Cdd:cd05921 436 vgP-------LRARAVAACapLVH-DAVvagedRAEVGALVFPDL 472
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
115-530 |
8.35e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 93.03 E-value: 8.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 115 IGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAVLLLEHVerketpglklIILMDP 194
Cdd:PRK06145 55 VALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDEEFDAIVALETP----------KIVIDA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 195 FEEALKERGQKCGVVIKSMQAVedcgqenhqapvppQPDDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTEG 271
Cdd:PRK06145 125 AAQADSRRLAQGGLEIPPQAAV--------------APTDLVRLMYTSGTTDRPKGVMHSYGNLHwksIDHVIALGLTAS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 272 DIRLLSDDMKALCPTIFPVVPRL-------LNRMYDKIFSQANTPLKR----WLlefaakrkqAEVRSGIIRNDSIWDEL 340
Cdd:PRK06145 191 ERLLVVGPLYHVGAFDLPGIAVLwvggtlrIHREFDPEAVLAAIERHRltcaWM---------APVMLSRVLTVPDRDRF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 341 FFNKIQASLGGcvrmivtGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPCNHIKLVD 418
Cdd:PRK06145 262 DLDSLAWCIGG-------GEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREIEkiGSTGRALAHVEIRIAD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 419 vEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKI 498
Cdd:PRK06145 335 -GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEV 411
|
410 420 430
....*....|....*....|....*....|....*
gi 327412329 499 EN-IYIRSQ--PVAQIYVHGDSLKAFLVGIVVPDP 530
Cdd:PRK06145 412 ERvIYELPEvaEAAVIGVHDDRWGERITAVVVLNP 446
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
185-499 |
1.06e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 92.75 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 185 GLKLIILMDPFEEA---LKERGQKcgvviksMQAVEDCGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD 261
Cdd:PRK07768 108 GAKAVVVGEPFLAAapvLEEKGIR-------VLTVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYAN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 262 FSGFLKVTEGDIRL--------LSDDMK---ALC-------------PTIFPVVPRLLNRMYDKiFSQANTPLKRWLLEF 317
Cdd:PRK07768 181 AEAMFVAAEFDVETdvmvswlpLFHDMGmvgFLTvpmyfgaelvkvtPMDFLRDPLLWAELISK-YRGTMTAAPNFAYAL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 318 AAKR--KQAEvrsgiirnDSIWDElffnkiqaslgGCVRMIVTGAAPASPTVL----------GFLRAALGCqvyeGYGQ 385
Cdd:PRK07768 260 LARRlrRQAK--------PGAFDL-----------SSLRFALNGAEPIDPADVedlldagarfGLRPEAILP----AYGM 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 386 TECTAGCTFTTPGD--------------------WTSGHV------GAPLPCNHIKLVDvEELNYWACKGEGEICVRGPN 439
Cdd:PRK07768 317 AEATLAVSFSPCGAglvvdevdadllaalrravpATKGNTrrlatlGPPLPGLEVRVVD-EDGQVLPPRGVGVIELRGES 395
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 440 VFKGYLkDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIE 499
Cdd:PRK07768 396 VTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPTDIE 453
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
214-548 |
2.21e-19 |
|
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: 90.98 E-value: 2.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 214 QAVEDCGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSG--FLKVTEGDiRLLSddmkalcptifp 289
Cdd:cd05919 72 DDYAYIARDCEARLVVTSADDIAYLLYSSGTTGPPKGVMHAHRDPLlfADAMAreALGLTPGD-RVFS------------ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 290 vVPRLL------NRMYDKIFSQANTPL-KRWLLEFAAKRKQAEVRSGIIRNDSIwdelFFNKIQASLGGCVRM-----IV 357
Cdd:cd05919 139 -SAKMFfgyglgNSLWFPLAVGASAVLnPGWPTAERVLATLARFRPTVLYGVPT----FYANLLDSCAGSPDAlrslrLC 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 358 TGAAPASPTVLG-FLRAALGCQVYEGYGQTEctAGCTFTT--PGDWTSGHVGAPLPCNHIKLVDveELNYWACKGE-GEI 433
Cdd:cd05919 214 VSAGEALPRGLGeRWMEHFGGPILDGIGATE--VGHIFLSnrPGAWRLGSTGRPVPGYEIRLVD--EEGHTIPPGEeGDL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 434 CVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYV 513
Cdd:cd05919 290 LVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLIIQHPAVAEAAV 367
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 327412329 514 ----HGDSL---KAFlvgiVVPDPEVMPSWAQKRGIEGTYAD 548
Cdd:cd05919 368 vavpESTGLsrlTAF----VVLKSPAAPQESLARDIHRHLLE 405
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
35-513 |
2.55e-19 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 91.74 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 35 ARRSVIGSGPQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRKpkqpyQWLSYQEVADRAEFLGSGLLQHNCKAcTDQf 114
Cdd:PRK06155 1 GEPLGAGLAARAVDPLPPSERTLPAMLARQAERYPDRPLLVFGG-----TRWTYAEAARAAAAAAHALAAAGVKR-GDR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 115 IGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlLLEHVERKETPGLKL--IILM 192
Cdd:PRK06155 74 VALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAA-----LLAALEAADPGDLPLpaVWLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 193 DPFEEALKERGQKCGVVIKSMQAVedcgqenhqAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHG-------NVVADfsgf 265
Cdd:PRK06155 149 DAPASVSVPAGWSTAPLPPLDAPA---------PAAAVQPGDTAAILYTSGTTGPSKGVCCPHAqfywwgrNSAED---- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 266 LKVTEGDIRLlsddmkalcpTIFPvvprLLNRMYDKIFSQANTPLKRWLLE--FAAKRkqaevrsgiirndsIWDELFFN 343
Cdd:PRK06155 216 LEIGADDVLY----------TTLP----LFHTNALNAFFQALLAGATYVLEprFSASG--------------FWPAVRRH 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 344 KIQAS--LGGCVRMIVT--------------GAAPASPTVLGF-LRAALGCQVYEGYGQTECTAGCtFTTPGDWTSGHVG 406
Cdd:PRK06155 268 GATVTylLGAMVSILLSqparesdrahrvrvALGPGVPAALHAaFRERFGVDLLDGYGSTETNFVI-AVTHGSQRPGSMG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 407 APLPCNHIKLVDVEELNYWAckGE-GEICVRG--PNVF-KGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKK 482
Cdd:PRK06155 347 RLAPGFEARVVDEHDQELPD--GEpGELLLRAdePFAFaTGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIK 423
|
490 500 510
....*....|....*....|....*....|..
gi 327412329 483 HIFKlAQGEYVAPEKIENIyIRSQP-VAQIYV 513
Cdd:PRK06155 424 DAIR-RRGENISSFEVEQV-LLSHPaVAAAAV 453
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
227-530 |
1.84e-18 |
|
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: 88.51 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 227 PVPPQPDDLSIVC-FTSGTTGNPKGAMLTHGnvvadfSGFLKVTEGdirLLSDDMKaLCPTIFPVVPrllnrMYdkifsQ 305
Cdd:cd12118 126 WIPPADEWDPIALnYTSGTTGRPKGVVYHHR------GAYLNALAN---ILEWEMK-QHPVYLWTLP-----MF-----H 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 306 ANTplkrWLLEFAAKrkqaeVRSGI------IRNDSIWDELFFNKI--------------------QASLGGCVRMIVTG 359
Cdd:cd12118 186 CNG----WCFPWTVA-----AVGGTnvclrkVDAKAIYDLIEKHKVthfcgaptvlnmlanappsdARPLPHRVHVMTAG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 360 AAPaSPTVLgFLRAALGCQVYEGYGQTEcTAG----CTFTTPGDWTSGHVGAPLPC----NHIKL--VDVEELNY----- 424
Cdd:cd12118 257 APP-PAAVL-AKMEELGFDVTHVYGLTE-TYGpatvCAWKPEWDELPTEERARLKArqgvRYVGLeeVDVLDPETmkpvp 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 425 WACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIyir 504
Cdd:cd12118 334 RDGKTIGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENISSVEVEGV--- 408
|
330 340
....*....|....*....|....*.
gi 327412329 505 sqpvaqIYVHGDSLKAFLVGivVPDP 530
Cdd:cd12118 409 ------LYKHPAVLEAAVVA--RPDE 426
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
232-607 |
9.64e-18 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 86.78 E-value: 9.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 232 PDDLSIVCFTSGTTGNPKGAMLTHGNVVAD------FSGFlkvTEGDIRL----------LSDDMKAL----CPTIFPvv 291
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALIVQslakiaIVGY---GEDDVYLhtaplchiggLSSALAMLmvgaCHVLLP-- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 292 prllnrmydkifsqantplkrwllEFAAKR-----KQAEVRSGIIRNDSIWDELFFN--KIQASLGGCVRMIVTGAAPAS 364
Cdd:PLN02860 246 ------------------------KFDAKAalqaiKQHNVTSMITVPAMMADLISLTrkSMTWKVFPSVRKILNGGGSLS 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 365 P-----TVLGFLRAALgcqvYEGYGQTECTAGCTFTTPGDWT-----------------SGH------VGAPLPcnHIKL 416
Cdd:PLN02860 302 SrllpdAKKLFPNAKL----FSAYGMTEACSSLTFMTLHDPTlespkqtlqtvnqtkssSVHqpqgvcVGKPAP--HVEL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 417 vdveELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPE 496
Cdd:PLN02860 376 ----KIGLDESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIK-TGGENVYPE 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 497 KIENIYIRSQPVAQIYVHGdSLKAFLVGIVVPDPEVMPSWaqkRGIEGTYADLCTNKDLKKAILEDMVRlgkESGLHSFE 576
Cdd:PLN02860 451 EVEAVLSQHPGVASVVVVG-VPDSRLTEMVVACVRLRDGW---IWSDNEKENAKKNLTLSSETLRHHCR---EKNLSRFK 523
|
410 420 430
....*....|....*....|....*....|.
gi 327412329 577 QVKAIHIHSDMFSvqnglLTPTLKAKRPELR 607
Cdd:PLN02860 524 IPKLFVQWRKPFP-----LTTTGKIRRDEVR 549
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
231-531 |
1.22e-17 |
|
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: 85.82 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 231 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkvTEGDIRLLSDDMKALCPTI---FPV---------------VP 292
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA----TQRWFGFNEDDVWTLFHSYafdFSVweiwgallhggrlvvVP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 293 RLLNRmydkifsqanTPLKRWLLefaakrkqaeVRSGIIRNDSIWDELFFNKIQASLGG-----CVRMIVTGAAPASPTV 367
Cdd:cd17643 167 YEVAR----------SPEDFARL----------LRDEGVTVLNQTPSAFYQLVEAADRDgrdplALRYVIFGGEALEAAM 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 368 LGFLRAALGC---QVYEGYGQTECTAGCTFT--TPGDW---TSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPN 439
Cdd:cd17643 227 LRPWAGRFGLdrpQLVNMYGITETTVHVTFRplDAADLpaaAASPIGRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 440 VFKGYLKDPDRTKE-------ALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIY 512
Cdd:cd17643 306 VARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI-RGFRIELGEIEAALATHPSVRDAA 384
|
330 340
....*....|....*....|..
gi 327412329 513 V---HGDSLKAFLVGIVVPDPE 531
Cdd:cd17643 385 VivrEDEPGDTRLVAYVVADDG 406
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
30-529 |
1.30e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 87.52 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 30 LDSGGARRSVIGSGPqllTHYYDDARTMYQVFRRGLSISGNGPCLGFRKpkqpyQWLSYQEVADRAEFLGSGLLQHNckA 109
Cdd:PRK12467 490 LDAEERARELVRWNA---PATEYAPDCVHQLIEAQARQHPERPALVFGE-----QVLSYAELNRQANRLAHVLIAAG--V 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 110 CTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAVLLLehverkeTPGLKLI 189
Cdd:PRK12467 560 GPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPV-------PAGLRSL 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 190 ILMDPfeealkergqkcgvviksmqAVEDCGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVvadfSGFLKVT 269
Cdd:PRK12467 633 CLDEP--------------------ADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGAL----ANYVCVI 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 270 EGDIRLLSDDMKALCPT---------IFPVV---PRLLNRMYDKIFSQAntplkrwllEFAAkrKQAEVRSGIIR-NDSI 336
Cdd:PRK12467 689 AERLQLAADDSMLMVSTfafdlgvteLFGALasgATLHLLPPDCARDAE---------AFAA--LMADQGVTVLKiVPSH 757
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 337 WDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTT----PGDWTSGHVGAPLPCN 412
Cdd:PRK12467 758 LQALLQASRVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYElsdeERDFGNVPIGQPLANL 837
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 413 HIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSD------GWLH-TGDIGKWLPAGTLKIIDRKKHIF 485
Cdd:PRK12467 838 GLYILD-HYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDpfgadgGRLYrTGDLARYRADGVIEYLGRMDHQV 916
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 327412329 486 KLaQGEYVAPEKIENIyIRSQP-------VAQIYVHGDSLKAFLVGIVVPD 529
Cdd:PRK12467 917 KI-RGFRIELGEIEAR-LLAQPgvreavvLAQPGDAGLQLVAYLVPAAVAD 965
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
115-535 |
3.62e-17 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 84.94 E-value: 3.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 115 IGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKpqkavlLLEHVERKET-PGLKLIILMD 193
Cdd:PRK05852 71 VALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDA------DGPHDRAEPTtRWWPLTVNVG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 194 PfeealkERGQKCGVVIKSMQAVedcGQENHQAPVPP--QPDDLSIVcFTSGTTGNPKGAMLTHGNVVADFSGFL---KV 268
Cdd:PRK05852 145 G------DSGPSGGTLSVHLDAA---TEPTPATSTPEglRPDDAMIM-FTGGTTGLPKMVPWTHANIASSVRAIItgyRL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 269 TEGDIR---------------LLS----------------------DDMKALCPTIFPVVPrllnrmydkifsqantPLK 311
Cdd:PRK05852 215 SPRDATvavmplyhghgliaaLLAtlasggavllpargrfsahtfwDDIKAVGATWYTAVP----------------TIH 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 312 RWLLEFAAKRKQAEVRSGIirndsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAG 391
Cdd:PRK05852 279 QILLERAATEPSGRKPAAL-----------------------RFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 392 CTfTTPGDWtSGHVGAPLPCN---------HIKLV--DVEELNYWACkgeGEICVRGPNVFKGYLKDPDRTKEALdSDGW 460
Cdd:PRK05852 336 VT-TTQIEG-IGQTENPVVSTglvgrstgaQIRIVgsDGLPLPAGAV---GEVWLRGTTVVRGYLGDPTITAANF-TDGW 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 327412329 461 LHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAF---LVGIVVPDPEVMPS 535
Cdd:PRK05852 410 LRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLASHPNVMEAAVFGVPDQLYgeaVAAVIVPRESAPPT 486
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
227-541 |
4.45e-17 |
|
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: 84.32 E-value: 4.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 227 PVPPQPDDLSIVCFTSGTTGNPKGAMLTHG---NVVADFSGFLKVTEGDIRL----LSDDMKALcpTIFP--------VV 291
Cdd:cd17651 130 DPALDADDLAYVIYTSGSTGRPKGVVMPHRslaNLVAWQARASSLGPGARTLqfagLGFDVSVQ--EIFStlcagatlVL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 292 PR-------------LLNRMYDKIFsqANTPLKRWLLEfAAKRKQAEvrsgiirndsiwdelffnkiqaslGGCVRMIVT 358
Cdd:cd17651 208 PPeevrtdppalaawLDEQRISRVF--LPTVALRALAE-HGRPLGVR------------------------LAALRYLLT 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 359 G--AAPASPTVLGFLRAALGCQVYEGYGQTE---CTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDvEELNYWACKGEGE 432
Cdd:cd17651 261 GgeQLVLTEDLREFCAGLPGLRLHNHYGPTEthvVTALSLPGDPAAWPApPPIGRPIDNTRVYVLD-AALRPVPPGVPGE 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 433 ICVRGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQ 506
Cdd:cd17651 340 LYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFRIELGEIEAALARHP 418
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 327412329 507 PVAQIYV------HGDslkAFLVGIVVPDPEVMPSWAQKRG 541
Cdd:cd17651 419 GVREAVVlaredrPGE---KRLVAYVVGDPEAPVDAAELRA 456
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
86-539 |
5.41e-17 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 84.45 E-value: 5.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLGSGLlQHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 165
Cdd:PRK05620 39 TTFAAIGARAAALAHAL-HDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 166 D---KPQKAVLLlehverKETPGLKLIILMDPFEEALKERGQKCGVVIKSMQAVEDCGQENHQAPVPPQpDDLSIVCFTS 242
Cdd:PRK05620 118 DprlAEQLGEIL------KECPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALLDGRSTVYDWPELDE-TTAAAICYST 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 243 GTTGNPKGAMLTHGNVVADFSGF-----LKVTEGDIRLlsddmkaLCPTIFPV----VPrLLNRMydkifsqANTPLKrw 313
Cdd:PRK05620 191 GTTGAPKGVVYSHRSLYLQSLSLrttdsLAVTHGESFL-------CCVPIYHVlswgVP-LAAFM-------SGTPLV-- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 314 lleFAAKRKQAEVRSGIIRN---------DSIWDELFFNKIQ-----ASLggcvRMIVTGAAPASPTVLGFLRAALGCQV 379
Cdd:PRK05620 254 ---FPGPDLSAPTLAKIIATamprvahgvPTLWIQLMVHYLKnpperMSL----QEIYVGGSAVPPILIKAWEERYGVDV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 380 YEGYGQTECTAGCTFTTPGDWTSGHVGA---------PLPCNHiKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDP-- 448
Cdd:PRK05620 327 VHVWGMTETSPVGTVARPPSGVSGEARWayrvsqgrfPASLEY-RIVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPte 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 449 --------------DRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVaqiyvh 514
Cdd:PRK05620 406 egggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIR-SGGEWIYSAQLENYIMAAPEV------ 478
|
490 500
....*....|....*....|....*
gi 327412329 515 gdsLKAFLVGIvvPDPEvmpsWAQK 539
Cdd:PRK05620 479 ---VECAVIGY--PDDK----WGER 494
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
86-534 |
6.27e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 84.02 E-value: 6.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 165
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQG--VRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 166 DKPQKAVLL---LEHVERKETPGLKLIILMDPFEEALKERGQKCGVviksmQAVEDCGQENHQAPVPPQ-PDDLSIVCFT 241
Cdd:PRK06164 114 WPGFKGIDFaaiLAAVPPDALPPLRAIAVVDDAADATPAPAPGARV-----QLFALPDPAPPAAAGERAaDPDAGALLFT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 242 -SGTTGNPK------GAMLTHGNVVADFSGflkVTEGDIRLLSD------DMKALCPTIFPVVPRLLNRMYDkifsqant 308
Cdd:PRK06164 189 tSGTTSGPKlvlhrqATLLRHARAIARAYG---YDPGAVLLAALpfcgvfGFSTLLGALAGGAPLVCEPVFD-------- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 309 plkrwllefaAKRKQAEVRSGIIRNDSIWDELFfnkiqaslggcVRMIVTGAAPA---SPTVLGFLR--------AALGC 377
Cdd:PRK06164 258 ----------AARTARALRRHRVTHTFGNDEML-----------RRILDTAGERAdfpSARLFGFASfapalgelAALAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 378 Q----VYEGYGQTECTA---GCTFTTPgdWTSGHVGAPLPCN---HIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKD 447
Cdd:PRK06164 317 ArgvpLTGLYGSSEVQAlvaLQPATDP--VSVRIEGGGRPASpeaRVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 448 PDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVHGDSL--KAFLVGI 525
Cdd:PRK06164 395 PDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPAEIEHALEALPGVAAAQVVGATRdgKTVPVAF 473
|
....*....
gi 327412329 526 VVPDPEVMP 534
Cdd:PRK06164 474 VIPTDGASP 482
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
86-534 |
7.57e-17 |
|
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: 83.52 E-value: 7.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 165
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVG--PESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 166 DkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhqapvppqPDDLSIVCFTSGTT 245
Cdd:cd12115 103 D-----------------------------------------------------------------PDDLAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 246 GNPKGAMLTHGNVVA-------DFSG---------------------FLKVTEGDIRLLSDDMKALcptifPVVPRLLNr 297
Cdd:cd12115 118 GRPKGVAIEHRNAAAflqwaaaAFSAeelagvlastsicfdlsvfelFGPLATGGKVVLADNVLAL-----PDLPAAAE- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 298 mydkiFSQANTplkrwllefaakrkqaeVRSGIirndsiwDELF-FNKIQASlggcVRMIVTGAAPASPTVLGFLRAAL- 375
Cdd:cd12115 192 -----VTLINT-----------------VPSAA-------AELLrHDALPAS----VRVVNLAGEPLPRDLVQRLYARLq 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 376 GCQVYEGYGQTECTAGCTFT--TPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKE 453
Cdd:cd12115 239 VERVVNLYGPSEDTTYSTVApvPPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 454 ALDSDGWL------HTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIyIRSQP-VAQ--IYVHGDSL-KAFLV 523
Cdd:cd12115 318 RFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAA-LRSIPgVREavVVAIGDAAgERRLV 395
|
490
....*....|.
gi 327412329 524 GIVVPDPEVMP 534
Cdd:cd12115 396 AYIVAEPGAAG 406
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
86-530 |
1.29e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 83.14 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 165
Cdd:PLN03102 40 FTWPQTYDRCCRLAASLISLNIT--KNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 166 DKP-----QKAVLLLEHVERKETPGLKLIILMD----PFE-----EALKERGQKCGVVIKSMQAVEDcgqenhqapvppQ 231
Cdd:PLN03102 118 DRSfeplaREVLHLLSSEDSNLNLPVIFIHEIDfpkrPSSeeldyECLIQRGEPTPSLVARMFRIQD------------E 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 232 PDDLSIvCFTSGTTGNPKGAMLTH-GNVVADFSGFLKVTEGdirllsddmkaLCPTIFPVVPrllnrmydkIFSqantpL 310
Cdd:PLN03102 186 HDPISL-NYTSGTTADPKGVVISHrGAYLSTLSAIIGWEMG-----------TCPVYLWTLP---------MFH-----C 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 311 KRWLLEFA-AKRKQAEVRSGIIRNDSIWDELFFNKI--------------------QASLGGCVRMIVTGAAPasPTVLG 369
Cdd:PLN03102 240 NGWTFTWGtAARGGTSVCMRHVTAPEIYKNIEMHNVthmccvptvfnillkgnsldLSPRSGPVHVLTGGSPP--PAALV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 370 FLRAALGCQVYEGYGQTECTAGCTFTTPGD-WTSghvgapLPCN------------HIKLVDVEELNYWAC-------KG 429
Cdd:PLN03102 318 KKVQRLGFQVMHAYGLTEATGPVLFCEWQDeWNR------LPENqqmelkarqgvsILGLADVDVKNKETQesvprdgKT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 430 EGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIyirsqpva 509
Cdd:PLN03102 392 MGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENV-------- 461
|
490 500
....*....|....*....|.
gi 327412329 510 qIYVHGDSLKAFLVGIvvPDP 530
Cdd:PLN03102 462 -LYKYPKVLETAVVAM--PHP 479
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
123-523 |
4.55e-16 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 81.36 E-value: 4.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 123 PEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlLLEHVER--KETPGLKLIILMDP------ 194
Cdd:cd05928 78 PEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDE-----LAPEVDSvaSECPSLKTKLLVSEksrdgw 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 195 --FEEALKERGQKcgvviksmqavEDCGQENHQAPvppqpddlSIVCFTSGTTGNPKGAMLTHGN----VVADFSGFLKV 268
Cdd:cd05928 153 lnFKELLNEASTE-----------HHCVETGSQEP--------MAIYFTSGTTGSPKMAEHSHSSlglgLKVNGRYWLDL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 269 TEGDIRL-LSDD--MKALCPTIFP-------VVPRLLNRMYDKIFSQANT--PLKRWLLEFAAKRKqaevrsgIIRNDsi 336
Cdd:cd05928 214 TASDIMWnTSDTgwIKSAWSSLFEpwiqgacVFVHHLPRFDPLVILKTLSsyPITTFCGAPTVYRM-------LVQQD-- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 337 wdelfFNKIQ-ASLGGCVrmivTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIK 415
Cdd:cd05928 285 -----LSSYKfPSLQHCV----TGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQ 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 416 LVDvEELNYWACKGEGEICVR-GPN----VFKGYLKDPDRTKEALDSDGWLhTGDIGKWLPAGTLKIIDRKKHIFkLAQG 490
Cdd:cd05928 356 IID-DNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSG 432
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 327412329 491 EYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLV 523
Cdd:cd05928 433 YRIGPFEVESALIEHPAVVESAVvsspdpiRGEVVKAFVV 472
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
382-538 |
7.81e-16 |
|
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: 78.88 E-value: 7.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 382 GYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVE--ELNywacKGE-GEICVRGPNVFKGYLKDPDRTKEALdSD 458
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDgrEVP----DGEvGEIVARGPTVMAGYWNRPEVNARRT-RG 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 459 GWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqgeyvapekIENIY-------IRSQP-VAQIYVhgdslkaflvgIVVPDp 530
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSG---------AENIYpaevercLRQHPaVADAAV-----------IGVPD- 275
|
....*...
gi 327412329 531 evmPSWAQ 538
Cdd:cd17636 276 ---PRWAQ 280
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
86-542 |
9.69e-16 |
|
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: 80.11 E-value: 9.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLGSGLLQhnckactdqfIGVFAQNR--------PEWIIVELACYTYSMVVVPLYDTLGPGAIRYIInt 157
Cdd:cd05959 30 LTYAELEAEARRVAGALRA----------LGVKREERvllimldtVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 158 ADI-STVIVDKPQKAVLLLEHVERKEtPGLKLIILMDPFEEALKErgqkcgvviksMQAVEDCGQENHQ-APVPPQPDDL 235
Cdd:cd05959 98 EDSrARVVVVSGELAPVLAAALTKSE-HTLVVLIVSGGAGPEAGA-----------LLLAELVAAEAEQlKPAATHADDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 236 SIVCFTSGTTGNPKGAMLTHGN--VVADFSG--FLKVTEGDIrLLS---------------------------------- 277
Cdd:cd05959 166 AFWLYSSGSTGRPKGVVHLHADiyWTAELYArnVLGIREDDV-CFSaaklffayglgnsltfplsvgattvlmperptpa 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 278 ---DDMKALCPTIFPVVPRLLNRMydkifsqantplkrwlleFAAKRKQAEVRSGIirndsiwdelffnkiqaslggcvR 354
Cdd:cd05959 245 avfKRIRRYRPTVFFGVPTLYAAM------------------LAAPNLPSRDLSSL-----------------------R 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 355 MIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTF--TTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGE 432
Cdd:cd05959 284 LCVSAGEALPAEVGERWKARFGLDILDGIGSTE--MLHIFlsNRPGRVRYGTTGKPVPGYEVELRD-EDGGDVADGEPGE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 433 ICVRGPNVFKGYLKDPDRTKEALDSdGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIY 512
Cdd:cd05959 361 LYVRGPSSATMYWNNRDKTRDTFQG-EWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSPFEVESALVQHPAVLEAA 438
|
490 500 510
....*....|....*....|....*....|....*..
gi 327412329 513 VHG-------DSLKAFlvgiVVPDPEVMPSWAQKRGI 542
Cdd:cd05959 439 VVGvededglTKPKAF----VVLRPGYEDSEALEEEL 471
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
115-532 |
1.59e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 79.72 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 115 IGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAVL--LLEHVERKETPGLKLIILM 192
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLdgLDPGVRVINVDSPAWADEL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 193 DPFEEALKErgqkcgvviksmqavedcgqenhqaPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVTEGD 272
Cdd:PRK07867 137 AAHRDAEPP-------------------------FRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVA--SAGVMLAQRFG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 273 IRllSDDMKALCPTIF----------PVVPrllnrmydkifSQANTPLKRwllEFAAKRKQAEVRS-GIIrndsiwdelF 341
Cdd:PRK07867 190 LG--PDDVCYVSMPLFhsnavmagwaVALA-----------AGASIALRR---KFSASGFLPDVRRyGAT---------Y 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 342 FNKIqaslGGCVRMIVtgAAP-----------------ASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTTPGDWTSGH 404
Cdd:PRK07867 245 ANYV----GKPLSYVL--ATPerpddadnplrivygneGAPGDIARFARRFGCVVVDGFGSTE--GGVAITRTPDTPPGA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 405 VGaPLPCNhIKLVDVE--------------ELNYWACKGEgEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWL 470
Cdd:PRK07867 317 LG-PLPPG-VAIVDPDtgtecppaedadgrLLNADEAIGE-LVNTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRD 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 327412329 471 PAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYVHGdslkaflvgivVPDPEV 532
Cdd:PRK07867 393 ADGYAYFAGRLGDWMRV-DGENLGTAPIERILLRYPDATEVAVYA-----------VPDPVV 442
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
228-531 |
1.59e-15 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 79.63 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 228 VPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkvtEGDIRLLSDD---MKAlcPTIFPV-VPRLLnrmydkif 303
Cdd:cd17646 133 VPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWM----QDEYPLGPGDrvlQKT--PLSFDVsVWELF-------- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 304 sqantplkrWLLEFAAK--------RKQAEVRSGIIRNDSIWD--------ELFFNKIQASLGGCVRMIVTGAAPASPTV 367
Cdd:cd17646 199 ---------WPLVAGARlvvarpggHRDPAYLAALIREHGVTTchfvpsmlRVFLAEPAAGSCASLRRVFCSGEALPPEL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 368 LGFLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHV--GAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGY 444
Cdd:cd17646 270 AARFLALPGAELHNLYGPTEAAIDVThWPVRGPAETPSVpiGRPVPNTRLYVLD-DALRPVPVGVPGELYLGGVQLARGY 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 445 LKDPDRTKEALDSDGWLH------TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIyIRSQP-VAQIYV---H 514
Cdd:cd17646 349 LGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKI-RGFRVEPGEIEAA-LAAHPaVTHAVVvarA 426
|
330
....*....|....*..
gi 327412329 515 GDSLKAFLVGIVVPDPE 531
Cdd:cd17646 427 APAGAARLVGYVVPAAG 443
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
117-530 |
1.74e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 79.70 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 117 VFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV--DKPqkavlllEHVE--RKETPGLKLIILM 192
Cdd:PRK07470 62 VHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMIChaDFP-------EHAAavRAASPDLTHVVAI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 193 D--PFEEAlkergqkcgvviksmqaVEDCGQENHQAPVPPQP---DDLSIVCFTSGTTGNPKGAMLTHG-------NVVA 260
Cdd:PRK07470 135 GgaRAGLD-----------------YEALVARHLGARVANAAvdhDDPCWFFFTSGTTGRPKAAVLTHGqmafvitNHLA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 261 DFsgFLKVTEGDIRL----LSDD--MKALC------PTIFPVVPRLlnrmydkIFSQANTPLKRW--------------L 314
Cdd:PRK07470 198 DL--MPGTTEQDASLvvapLSHGagIHQLCqvargaATVLLPSERF-------DPAEVWALVERHrvtnlftvptilkmL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 315 LEFAAkrkqaevrsgIIRNDsiwdelffnkiQASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF 394
Cdd:PRK07470 269 VEHPA----------VDRYD-----------HSSL----RYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVTGNITV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 395 TTP-----GDWTSGHVGaplPCNH--------IKLVDVEELNywacKGE-GEICVRGPNVFKGYLKDPDRTKEALdSDGW 460
Cdd:PRK07470 324 LPPalhdaEDGPDARIG---TCGFertgmevqIQDDEGRELP----PGEtGEICVIGPAVFAGYYNNPEANAKAF-RDGW 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 461 LHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENiyirsqpvaQIYVHGDSLKAFLVGivVPDP 530
Cdd:PRK07470 396 FRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREIEE---------KLLTHPAVSEVAVLG--VPDP 453
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
224-519 |
1.75e-15 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 80.14 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 224 HQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTH----GNV-----VADFSG---FLK---------VTEGdirLLSDDMKA 282
Cdd:PRK08043 356 RLAQVKQQPEDAALILFTSGSEGHPKGVVHSHksllANVeqiktIADFTPndrFMSalplfhsfgLTVG---LFTPLLTG 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 283 LCPTIFP------VVPRLLnrmYDK----IFSQANtplkrWLLEFAakrkqaevrsgiiRNDSIWDelFFNkiqaslggc 352
Cdd:PRK08043 433 AEVFLYPsplhyrIVPELV---YDRnctvLFGTST-----FLGNYA-------------RFANPYD--FAR--------- 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 353 VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNywacKGeGE 432
Cdd:PRK08043 481 LRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIE----QG-GR 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 433 ICVRGPNVFKGYLK--DPDRTK-------EALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYI 503
Cdd:PRK08043 556 LQLKGPNIMNGYLRveKPGVLEvptaenaRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIA-GEMVSLEMVEQLAL 634
|
330
....*....|....*.
gi 327412329 504 RSQPVAQiyvHGDSLK 519
Cdd:PRK08043 635 GVSPDKQ---HATAIK 647
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
226-492 |
1.98e-15 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 79.56 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 226 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFS---GFLKVTEGDIRLlsddmkalcPTiFPVV----PRLLNRM 298
Cdd:PRK09274 167 PMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEalrEDYGIEPGEIDL---------PT-FPLFalfgPALGMTS 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 299 Y--------------DKIFSQ----------ANTPLKRWLLEFAAKRKQaevrsgiirndsiwdelffnkiqaSLGGCVR 354
Cdd:PRK09274 237 VipdmdptrpatvdpAKLFAAierygvtnlfGSPALLERLGRYGEANGI------------------------KLPSLRR 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 355 MIVTGAaPASPTVLGFLRAAL--GCQVYEGYGQTECTAGCT-------FTTPGDWTSGH---VGAPLPCNHIKLVDV--E 420
Cdd:PRK09274 293 VISAGA-PVPIAVIERFRAMLppDAEILTPYGATEALPISSiesreilFATRAATDNGAgicVGRPVDGVEVRIIAIsdA 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 421 ELNYWA-----CKGE-GEICVRGPNVFKGYLKDPDRTKEA--LDSDG--WLHTGDIGkWL-PAGTLKIIDRKKHIFKLAQ 489
Cdd:PRK09274 372 PIPEWDdalrlATGEiGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLG-YLdAQGRLWFCGRKAHRVETAG 450
|
...
gi 327412329 490 GEY 492
Cdd:PRK09274 451 GTL 453
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
232-508 |
2.65e-15 |
|
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: 78.68 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 232 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEGDI--RLLS-----DDMKALCPTIFPVVPRL-LNRMYDKIF 303
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTkdRILSwmpltHDMGLIAFHLAPLIAGMnQYLMPTRLF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 304 SQANTplkRWLLEfAAKRKQAEVRSGIIRNDSIWDELFFNKIQASLGGCVRMIVTGAAPASP----------TVLGFLRA 373
Cdd:cd05908 185 IRRPI---LWLKK-ASEHKATIVSSPNFGYKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYelchefldhmSKYGLKRN 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 374 AlgcqVYEGYGQTECTAGCTF----------------------------TTPGDWTSGHVGAPLPCNHIKLVDveELNYW 425
Cdd:cd05908 261 A----ILPVYGLAEASVGASLpkaqspfktitlgrrhvthgepepevdkKDSECLTFVEVGKPIDETDIRICD--EDNKI 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 426 ACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIR 504
Cdd:cd05908 335 LPDGYiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRNGRLVITGREKDII-FVNGQNVYPHDIERIAEE 412
|
....
gi 327412329 505 SQPV 508
Cdd:cd05908 413 LEGV 416
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
86-531 |
3.18e-15 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 78.31 E-value: 3.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLGSGLLQHNCKACTDQFigVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYiintadistviv 165
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVF--VLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRD------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 166 dkpqkavlllehveRKETPGLKLIILmdpfEEALKERgqkcgvviksmqavedcgqenhqapvpPQPDDLSIVCFTSGTT 245
Cdd:cd05969 67 --------------RLENSEAKVLIT----TEELYER---------------------------TDPEDPTLLHYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 246 GNPKGAMLTHGNVVAD-FSG--FLKVTEGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTPlKRWLlefaakrk 322
Cdd:cd05969 102 GTPKGVLHVHDAMIFYyFTGkyVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRFDA-ESWY-------- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 323 qaevrsGIIRND--SIW--------------DELFFNKIQASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQT 386
Cdd:cd05969 173 ------GIIERVkvTVWytaptairmlmkegDELARKYDLSSL----RFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 387 ECTAGCTFTTPG-DWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRG--PNVFKGYLKDPDRTKEALdSDGWLHT 463
Cdd:cd05969 243 ETGSIMIANYPCmPIKPGSMGKPLPGVKAAVVD-ENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSF-IDGWYLT 320
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 327412329 464 GDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVHGdslkaflvgivVPDPE 531
Cdd:cd05969 321 GDLAYRDEDGYFWFVGRADDIIKTS-GHRVGPFEVESALMEHPAVAEAGVIG-----------KPDPL 376
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
86-515 |
5.42e-15 |
|
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: 77.93 E-value: 5.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 165
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRP--GQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 166 dkpqkavllleHVERKETPGLKLIILMDPFEEALKERGQKC--GVVIKsmqavedcgqenhqaPVPPQPDDLSIVCFTSG 243
Cdd:cd05923 107 -----------AVDAQVMDAIFQSGVRVLALSDLVGLGEPEsaGPLIE---------------DPPREPEQPAFVFYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 244 TTGNPKGAMLTH--------------------GNVVADFS------GFLKVTEGDIrllsddmkALCPTIFPVvprllnr 297
Cdd:cd05923 161 TTGLPKGAVIPQraaesrvlfmstqaglrhgrHNVVLGLMplyhviGFFAVLVAAL--------ALDGTYVVV------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 298 mydKIFSQANtplkrwllefAAKRKQAEVRSGIIRNDSIWDELFFNKIQASLG-GCVRMIVTGAAPASPTVLGFLRAALG 376
Cdd:cd05923 226 ---EEFDPAD----------ALKLIEQERVTSLFATPTHLDALAAAAEFAGLKlSSLRHVTFAGATMPDAVLERVNQHLP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 377 CQVYEGYGQTECTagcTFTTPGDWTSGHVGAPLPCNHIKLVDV-EELNYWACKG-EGEICVR--GPNVFKGYLKDPDRTK 452
Cdd:cd05923 293 GEKVNIYGTTEAM---NSLYMRDARTGTEMRPGFFSEVRIVRIgGSPDEALANGeEGELIVAaaADAAFTGYLNQPEATA 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 327412329 453 EALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYVHG 515
Cdd:cd05923 370 KKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIG 430
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
229-523 |
7.88e-15 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 77.58 E-value: 7.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 229 PPQPDDLSIVC-FTSGTTGNPKGAMLTH-GNVVADFSGFL--KVTEGDIRLLSDDM------------KALCPTIFPVVP 292
Cdd:PLN02479 190 PPADEWQSIALgYTSGTTASPKGVVLHHrGAYLMALSNALiwGMNEGAVYLWTLPMfhcngwcftwtlAALCGTNICLRQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 293 RLLNRMYDKIFSQANTplkrwllEFAAkrkqAEVRSGIIRNDSIWDELFfnkiqaSLGGCVRMIVTGAAPaSPTVLgFLR 372
Cdd:PLN02479 270 VTAKAIYSAIANYGVT-------HFCA----APVVLNTIVNAPKSETIL------PLPRVVHVMTAGAAP-PPSVL-FAM 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 373 AALGCQVYEGYGQTEcTAG----CTFTTPGDWTSGHVGAPLPCNH---------IKLVDVEELNYWACKGE--GEICVRG 437
Cdd:PLN02479 331 SEKGFRVTHTYGLSE-TYGpstvCAWKPEWDSLPPEEQARLNARQgvryiglegLDVVDTKTMKPVPADGKtmGEIVMRG 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 438 PNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIyirsqpvaqIYVHGDS 517
Cdd:PLN02479 410 NMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGGENISSLEVENV---------VYTHPAV 478
|
....*.
gi 327412329 518 LKAFLV 523
Cdd:PLN02479 479 LEASVV 484
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
354-531 |
2.14e-14 |
|
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: 75.95 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 354 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctaG-CTFTTPGD--WTSGH-VGAPL-PCNHIKLVD-----VEEln 423
Cdd:COG1021 303 RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---GlVNYTRLDDpeEVILTtQGRPIsPDDEVRIVDedgnpVPP-- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 424 ywackGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKK-HIFKlaQGEYVAPEKIENi 501
Cdd:COG1021 378 -----GEvGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKdQINR--GGEKIAAEEVEN- 449
|
170 180 190
....*....|....*....|....*....|
gi 327412329 502 yirsqpvaQIYVHGDSLKAFLVGivVPDPE 531
Cdd:COG1021 450 --------LLLAHPAVHDAAVVA--MPDEY 469
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
233-513 |
2.68e-14 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 75.30 E-value: 2.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 233 DDLSIVCFTSGTTGNPKGAMLTHGNV-VADFSG--FLKVTEGDIRL-LSDdmkalcptifpvvPRLLNRMYDKIFSQANT 308
Cdd:cd05974 85 DDPMLLYFTSGTTSKPKLVEHTHRSYpVGHLSTmyWIGLKPGDVHWnISS-------------PGWAKHAWSCFFAPWNA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 309 PLKRWLL---EFAAKRKQAE-VRSGIIR---NDSIWdELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYE 381
Cdd:cd05974 152 GATVFLFnyaRFDAKRVLAAlVRYGVTTlcaPPTVW-RMLIQQDLASFDVKLREVVGAGEPLNPEVIEQVRRAWGLTIRD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 382 GYGQTECTAGCTfTTPGD-WTSGHVGAPLPCNHIKLVDVEElnywACKGEGEICV-----RGPNVFKGYLKDPDRTKEAL 455
Cdd:cd05974 231 GYGQTETTALVG-NSPGQpVKAGSMGRPLPGYRVALLDPDG----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM 305
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 327412329 456 dSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYV 513
Cdd:cd05974 306 -RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSDYRISPFELESVLIEHPAVAEAAV 361
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
354-531 |
3.31e-14 |
|
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: 75.44 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 354 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPL-PCNHIKLVDvEELNYWACKGEG 431
Cdd:cd05920 258 RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTrLDDPDEVIIHTQGRPMsPDDEIRVVD-EEGNPVPPGEEG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 432 EICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENiyirsqpvaQI 511
Cdd:cd05920 337 ELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVEN---------LL 406
|
170 180
....*....|....*....|
gi 327412329 512 YVHGDSLKAFLVGivVPDPE 531
Cdd:cd05920 407 LRHPAVHDAAVVA--MPDEL 424
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
230-528 |
1.06e-13 |
|
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: 73.65 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 230 PQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGfLKVTEGdIRLLSDDMKALCP-TIFPVVPRLLNRMYDKIFSQANT 308
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDA-LRQLYG-IRPGEVDLATFPLfALFGPALGLTSVIPDMDPTRPAR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 309 PLKRWLLEFAAkrkQAEVrSGIIRNDSIWDEL--FFNKIQASLGGcVRMIVTGAAPASPTVLGFLRAAL--GCQVYEGYG 384
Cdd:cd05910 160 ADPQKLVGAIR---QYGV-SIVFGSPALLERVarYCAQHGITLPS-LRRVLSAGAPVPIALAARLRKMLsdEAEILTPYG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 385 QTECTAGCT------FTTPGDWTSGH----VGAPLPCNHIKLV--DVEELNYWACKGE------GEICVRGPNVFKGYLK 446
Cdd:cd05910 235 ATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVRVRIIeiDDEPIAEWDDTLElprgeiGEITVTGPTVTPTYVN 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 447 DPDRTKEALDSDG----WLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVapekieniyirSQPVAQIY-VHGDSLKAF 521
Cdd:cd05910 315 RPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLY-----------TEPVERVFnTHPGVRRSA 383
|
....*..
gi 327412329 522 LVGIVVP 528
Cdd:cd05910 384 LVGVGKP 390
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
232-503 |
1.19e-13 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 73.70 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 232 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKV---TEGDIrllsddMKALCP----------TIFPVVPRLlnrm 298
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFfspKEDDV------MMSFLPpfhaygfnscTLFPLLSGV---- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 299 yDKIFsqANTPLK-RWLLEFAAKRKQAEVRSGIIRNDSIwdeLFFNKIQASLGGCVRMIVTGAAPASPTVL-GFLRAALG 376
Cdd:PRK06334 252 -PVVF--AYNPLYpKKIVEMIDEAKVTFLGSTPVFFDYI---LKTAKKQESCLPSLRFVVIGGDAFKDSLYqEALKTFPH 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 377 CQVYEGYGQTECTAGCTFTT---PGDwtSGHVGAPLPCNHIKLVDvEELNYWACKGE-GEICVRGPNVFKGYL-KDPDRT 451
Cdd:PRK06334 326 IQLRQGYGTTECSPVITINTvnsPKH--ESCVGMPIRGMDVLIVS-EETKVPVSSGEtGLVLTRGTSLFSGYLgEDFGQG 402
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 327412329 452 KEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYI 503
Cdd:PRK06334 403 FVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSLEALESILM 453
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
86-530 |
1.37e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 73.38 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 165
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGP--GDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 166 DK---PQKAVLLlehverKETPGLKLIILMD------------PFEEALKErgqkcgvviksmqavedcgQENHQAPVPP 230
Cdd:PRK07798 107 ERefaPRVAEVL------PRLPKLRTLVVVEdgsgndllpgavDYEDALAA-------------------GSPERDFGER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 231 QPDDLSIVCfTSGTTGNPKGAMLTHGNV-VADFSGFLKVTEGDIR---LLSDDMKALCPTIFPVVPRL-----LNRMYDK 301
Cdd:PRK07798 162 SPDDLYLLY-TGGTTGMPKGVMWRQEDIfRVLLGGRDFATGEPIEdeeELAKRAAAGPGMRRFPAPPLmhgagQWAAFAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 302 IFSQANTPLKRW-------LLEFAAKRKqaeVRSGIIRNDS----IWDELffnkiqASLGG----CVRMIVTGAAPASPT 366
Cdd:PRK07798 241 LFSGQTVVLLPDvrfdadeVWRTIEREK---VNVITIVGDAmarpLLDAL------EARGPydlsSLFAIASGGALFSPS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 367 V-LGFLRAALGCQVYEGYGQTECTAGCTFTTPGDwtSGHVGAPL--PCNHIKLVDvEELNYWAcKGEGEICV--RGPNVF 441
Cdd:PRK07798 312 VkEALLELLPNVVLTDSIGSSETGFGGSGTVAKG--AVHTGGPRftIGPRTVVLD-EDGNPVE-PGSGEIGWiaRRGHIP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 442 KGYLKDPDRTKEALDS-DG--WLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIyIRSQPvaqiyvhgDSL 518
Cdd:PRK07798 388 LGYYKDPEKTAETFPTiDGvrYAIPGDRARVEADGTITLLGRGSVCINTG-GEKVFPEEVEEA-LKAHP--------DVA 457
|
490
....*....|..
gi 327412329 519 KAFLVGivVPDP 530
Cdd:PRK07798 458 DALVVG--VPDE 467
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
51-523 |
2.09e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 74.22 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 51 YDDARTMYQVFRRGLSISGNGPCLGFRKpkqpyQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVEL 130
Cdd:PRK12316 3053 YPLERGVHRLFEEQVERTPDAVALAFGE-----QRLSYAELNRRANRLAHRLIERGVGP--DVLVGVAVERSLEMVVGLL 3125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 131 ACYTYSMVVVPLyDTLGPGAiryiintaDISTVIVDKPQKAVLLLEHVERKETPGLKlIILMDPFEEALKErgqkcgvvi 210
Cdd:PRK12316 3126 AILKAGGAYVPL-DPEYPEE--------RLAYMLEDSGAQLLLSQSHLRLPLAQGVQ-VLDLDRGDENYAE--------- 3186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 211 ksmqavedcgqenHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNvvadFSGFLKVTEGDIRLLSDD-MKALCPTIFP 289
Cdd:PRK12316 3187 -------------ANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSA----LSNHLCWMQQAYGLGVGDrVLQFTTFSFD 3249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 290 VVPRLLNRMYDKIFSQANTPLKRWLLEfaAKRKQAEVRSGIIRNDSIWDEL--FFNKIQASLGGCVRMIVTGAAPASPTV 367
Cdd:PRK12316 3250 VFVEELFWPLMSGARVVLAGPEDWRDP--ALLVELINSEGVDVLHAYPSMLqaFLEEEDAHRCTSLKRIVCGGEALPADL 3327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 368 LGflRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGH--VGAPLPCNHIKLVDVeELNYWACKGEGEICVRGPNVFKGYL 445
Cdd:PRK12316 3328 QQ--QVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILDG-SLEPVPVGALGELYLGGEGLARGYH 3404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 446 KDPDRTKEALDSDGW------LHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPV---AQIYVHGD 516
Cdd:PRK12316 3405 NRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVKI-RGFRIELGEIEARLLEHPWVreaVVLAVDGR 3483
|
....*..
gi 327412329 517 SLKAFLV 523
Cdd:PRK12316 3484 QLVAYVV 3490
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
231-540 |
2.73e-13 |
|
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: 72.29 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 231 QPDDLSIVCFTSGTTGNPKGAMLTH---GNVVADFSGFLKVTEGDiRLL-----SDD-------MKALCPTIFPVVPRLL 295
Cdd:cd17652 91 TPDNLAYVIYTSGSTGRPKGVVVTHrglANLAAAQIAAFDVGPGS-RVLqfaspSFDasvwellMALLAGATLVLAPAEE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 296 nrmydkifSQANTPLKRWLlefaakrkQAEVRSGIIRNDSIWDELffnkIQASLGGCVRMIVTGAAPASPTVLgflRAAL 375
Cdd:cd17652 170 --------LLPGEPLADLL--------REHRITHVTLPPAALAAL----PPDDLPDLRTLVVAGEACPAELVD---RWAP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 376 GCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEA 454
Cdd:cd17652 227 GRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYVLD-ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAER 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 455 LDSD------GWLH-TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQ--IYVHGDSL-KAFLVG 524
Cdd:cd17652 306 FVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKI-RGFRIELGEVEAALTEHPGVAEavVVVRDDRPgDKRLVA 384
|
330
....*....|....*.
gi 327412329 525 IVVPDPEVMPSWAQKR 540
Cdd:cd17652 385 YVVPAPGAAPTAAELR 400
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
236-509 |
3.26e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 72.43 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 236 SIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVTEGDIRLLSDDmkalcpTIFPVVPRLLNRMYDKIFSQANTPLKrwlL 315
Cdd:PRK07008 179 SSLCYTSGTTGNPKGALYSHRSTV--LHAYGAALPDAMGLSARD------AVLPVVPMFHVNAWGLPYSAPLTGAK---L 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 316 EFAAKRKQAEVRSGIIRND---------SIWDELFFNKIQASLG-GCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQ 385
Cdd:PRK07008 248 VLPGPDLDGKSLYELIEAErvtfsagvpTVWLGLLNHMREAGLRfSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGM 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 386 TECTAGCTFTTPgdwTSGHVGAPLPCNH--------------IKLVDVE--ELNyWACKGEGEICVRGPNVFKGYLKdpd 449
Cdd:PRK07008 328 TEMSPLGTLCKL---KWKHSQLPLDEQRkllekqgrviygvdMKIVGDDgrELP-WDGKAFGDLQVRGPWVIDRYFR--- 400
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 450 RTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVA 509
Cdd:PRK07008 401 GDASPLV-DGWFPTGDVATIDADGFMQITDRSKDVIK-SGGEWISSIDIENVAVAHPAVA 458
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
239-515 |
3.83e-13 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 72.09 E-value: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 239 CFTSGTTGNPKGAMLTH-GNVVADFsgflkvtegdIRLLSDDMKALCP-TIFPVVPrllnrMYdkifsQANTplkrWLLE 316
Cdd:PRK06018 183 CYTSGTTGDPKGVLYSHrSNVLHAL----------MANNGDALGTSAAdTMLPVVP-----LF-----HANS----WGIA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 317 FAAKRKQAEVRSGIIRND--SIWDELFFNKIQASLG-------------------GCVRMIVTGAApASPTvlGFLRA-- 373
Cdd:PRK06018 239 FSAPSMGTKLVMPGAKLDgaSVYELLDTEKVTFTAGvptvwlmllqymekeglklPHLKMVVCGGS-AMPR--SMIKAfe 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 374 ALGCQVYEGYGQTECTAGCTFTT--------PGDWTSGHV---GAPLPCNHIKLVDVE--ELNyWACKGEGEICVRGPNV 440
Cdd:PRK06018 316 DMGVEVRHAWGMTEMSPLGTLAAlkppfsklPGDARLDVLqkqGYPPFGVEMKITDDAgkELP-WDGKTFGRLKVRGPAV 394
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 327412329 441 FKGYLKDPDrtkEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYVHG 515
Cdd:PRK06018 395 AAAYYRVDG---EILDDDGFFDTGDVATIDAYGYMRITDRSKDVIK-SGGEWISSIDLENLAVGHPKVAEAAVIG 465
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
429-484 |
4.35e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 71.90 E-value: 4.35e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 327412329 429 GE--GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHI 484
Cdd:PRK08162 385 GEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDI 441
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
231-540 |
4.38e-13 |
|
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: 71.70 E-value: 4.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 231 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKV---TEGDIRLL--SDDMKALCPTIFPVVPR--LLNRMYDKIF 303
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEygiTSSDRVLQfaSIAFDVAAEEIYVTLLSgaTLVLRPEEMR 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 304 SQantplkrwLLEFAAK--RKQAEVRSgiiRNDSIWDELFFNKIQASLGG--CVRMIVTGAAPASPTVLGFLRAALG--C 377
Cdd:cd17644 184 SS--------LEDFVQYiqQWQLTVLS---LPPAYWHLLVLELLLSTIDLpsSLRLVIVGGEAVQPELVRQWQKNVGnfI 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 378 QVYEGYGQTECTAGCTFTTPGDWTSGH-----VGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTK 452
Cdd:cd17644 253 QLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANTQVYILD-ENLQPVPVGVPGELHIGGVGLARGYLNRPELTA 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 453 EALDSDGWLH--------TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQ--IYVHGDSL-KAF 521
Cdd:cd17644 332 EKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKI-RGFRIELGEIEAVLSQHNDVKTavVIVREDQPgNKR 410
|
330
....*....|....*....
gi 327412329 522 LVGIVVPDPEVMPSWAQKR 540
Cdd:cd17644 411 LVAYIVPHYEESPSTVELR 429
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
379-493 |
6.46e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 71.62 E-value: 6.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 379 VYEGYGQTEcTAGCTFTTpgDWTS---GHVGAPLPCNHIKLVDVEElNYwackgegEICVRGPNVFKGYLKDPDRTKEAL 455
Cdd:PRK12582 380 FYTGYGATE-TAPTTTGT--HWDTervGLIGLPLPGVELKLAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAF 448
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 327412329 456 DSDGWLHTGDIGKWL----PAGTLKIIDRKKHIFKLAQGEYV 493
Cdd:PRK12582 449 DEEGFYRLGDAARFVdpddPEKGLIFDGRVAEDFKLSTGTWV 490
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
233-535 |
1.34e-12 |
|
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: 70.20 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 233 DDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTegdIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTplkr 312
Cdd:cd05958 97 DDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNV---LRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGV---- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 313 wLLEfaaKRKQAEVRSGIIRNDSIwdeLFFN------------KIQASLGGCVRMIVTgAAPASPTVLGFL-RAALGCQV 379
Cdd:cd05958 170 -LLE---EATPDLLLSAIARYKPT---VLFTaptayramlahpDAAGPDLSSLRKCVS-AGEALPAALHRAwKEATGIPI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 380 YEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveELNYWACKGE-GEICVRGPNVFKgYLKDPDRTKEAldSD 458
Cdd:cd05958 242 IDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD--DEGNPVPDGTiGRLAVRGPTGCR-YLADKRQRTYV--QG 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 459 GWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLV---GIVVPDPEVMPS 535
Cdd:cd05958 317 GWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVvvkAFVVLRPGVIPG 395
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
223-513 |
1.75e-12 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 69.90 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 223 NHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKV---TEGDIRLLS---------------------- 277
Cdd:PRK09029 125 EGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLmpfTAQDSWLLSlplfhvsgqgivwrwlyagatl 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 278 --------DDMKALCpTIFPVVP----RLLNRmydkifSQANTPLKRWLLefaakrkqaevrsgiirndsiwdelffnki 345
Cdd:PRK09029 205 vvrdkqplEQALAGC-THASLVPtqlwRLLDN------RSEPLSLKAVLL------------------------------ 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 346 qaslGGCvrMIvtgaapasPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTSGhVGAPLPCNHIKLVDveelnyw 425
Cdd:PRK09029 248 ----GGA--AI--------PVELTEQAEQQGIRCWCGYGLTE-MASTVCAKRADGLAG-VGSPLPGREVKLVD------- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 426 ackgeGEICVRGPNVFKGYLKDpDRTKEALDSDGWLHTGDIGKWLpAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRS 505
Cdd:PRK09029 305 -----GEIWLRGASLALGYWRQ-GQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQH 376
|
....*...
gi 327412329 506 QPVAQIYV 513
Cdd:PRK09029 377 PLVQQVFV 384
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
234-501 |
2.91e-12 |
|
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: 68.44 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 234 DLSIVCFTSGTTGNPKGAMLTHGNVVAD----FSGFLKVTEGDIRLLsddmkaLCPTIFPVvpRLLNRMYDKIFSQA--- 306
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVpdilQKEGLNWVVGDVTYL------PLPATHIG--GLWWILTCLIHGGLcvt 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 307 ---NTPLKRWLlefaaKRKQAEVRSGIIRNDSIWDELFfNKIQASLGGC--VRMIVTGAAPASPTVLGFLRAALGCQVYE 381
Cdd:cd17635 74 ggeNTTYKSLF-----KILTTNAVTTTCLVPTLLSKLV-SELKSANATVpsLRLIGYGGSRAIAADVRFIEATGLTNTAQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 382 GYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDVEELNYWAcKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGW 460
Cdd:cd17635 148 VYGLSETGTALCLPTDDDSIEiNAVGRPYPGVDVYLAATDGIAGPS-ASFGTIWIKSPANMLGYWNNPERTAEVL-IDGW 225
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 327412329 461 LHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENI 501
Cdd:cd17635 226 VNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERI 265
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
232-538 |
4.05e-12 |
|
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: 68.55 E-value: 4.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 232 PDDLSIVCFTSGTTGNPKGAMLTHGNVVA---DFSGFLKVTEGDIRL----LSDDMKALCptIFP-------VVPRllnr 297
Cdd:cd17649 93 PRQLAYVIYTSGSTGTPKGVAVSHGPLAAhcqATAERYGLTPGDRELqfasFNFDGAHEQ--LLPplicgacVVLR---- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 298 mydkifsqantPLKRWLlefAAKRKQAEVRSGIIRNDSI----WDELF--FNKIQASLGGCVRMIVTGAAPASPTvlgFL 371
Cdd:cd17649 167 -----------PDELWA---SADELAEMVRELGVTVLDLppayLQQLAeeADRTGDGRPPSLRLYIFGGEALSPE---LL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 372 RAALGCQVY--EGYGQTECTAGCT-FTTPGD----WTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGY 444
Cdd:cd17649 230 RRWLKAPVRlfNAYGPTEATVTPLvWKCEAGaaraGASMPIGRPLGGRSAYILD-ADLNPVPVGVTGELYIGGEGLARGY 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 445 LKDPDRTKEAL--DSDG-----WLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENiYIRSQP----VAQIYV 513
Cdd:cd17649 309 LGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RGFRIELGEIEA-ALLEHPgvreAAVVAL 386
|
330 340
....*....|....*....|....*.
gi 327412329 514 HGDSLKAfLVGIVVP-DPEVMPSWAQ 538
Cdd:cd17649 387 DGAGGKQ-LVAYVVLrAAAAQPELRA 411
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
231-539 |
4.77e-12 |
|
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: 68.35 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 231 QPDDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTEGDIRLL--SDDMKALCPTIFPvvprllnrmydkifsq 305
Cdd:cd17645 102 NPDDLAYVIYTSGSTGLPKGVMIEHHNLVnlcEWHRPYFGVTPADKSLVyaSFSFDASAWEIFP---------------- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 306 antplkRWLLEFAAKRKQAEVRSGIIR-NDSIWD-------------ELFFNKIQASLggcvRMIVTGAapaspTVLGFL 371
Cdd:cd17645 166 ------HLTAGAALHVVPSERRLDLDAlNDYFNQegitisflptgaaEQFMQLDNQSL----RVLLTGG-----DKLKKI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 372 RAAlGCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDR 450
Cdd:cd17645 231 ERK-GYKLVNNYGPTENTVVATsFEIDKPYANIPIGKPIDNTRVYILD-EALQLQPIGVAGELCIAGEGLARGYLNRPEL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 451 TKEALDSDGWL------HTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENI---YIRSQPVAQIYVHGDSLKAF 521
Cdd:cd17645 309 TAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIEPFlmnHPLIELAAVLAKEDADGRKY 387
|
330 340
....*....|....*....|..
gi 327412329 522 LVGIVVP----DPEVMPSWAQK 539
Cdd:cd17645 388 LVAYVTApeeiPHEELREWLKN 409
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
84-524 |
6.22e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 69.22 E-value: 6.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 84 QWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLyDTLGPGA-IRYIINTADIST 162
Cdd:PRK12316 2027 QHLSYAELDSRANRLAHRLRARGVGP--EVRVAIAAERSFELVVALLAVLKAGGAYVPL-DPNYPAErLAYMLEDSGAAL 2103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 163 VIVDKPQKAVLLLehverkeTPGLKLIILMDPfeEALKERGQKcgvviksmqavedcgqenhqAPVPP-QPDDLSIVCFT 241
Cdd:PRK12316 2104 LLTQRHLLERLPL-------PAGVARLPLDRD--AEWADYPDT--------------------APAVQlAGENLAYVIYT 2154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 242 SGTTGNPKGAMLTHGNVVAdfsgFLKVTEGDIRLLSDDmkalcptifpvvpRLLNRM---YDKIFSQANTPLKrwllefa 318
Cdd:PRK12316 2155 SGSTGLPKGVAVSHGALVA----HCQAAGERYELSPAD-------------CELQFMsfsFDGAHEQWFHPLL------- 2210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 319 akrKQAEVrsgIIRNDSIWD-ELFFNKIQ--------------------ASLGGC---VRMIVTGAAPASPTVLGFLRAA 374
Cdd:PRK12316 2211 ---NGARV---LIRDDELWDpEQLYDEMErhgvtildfppvylqqlaehAERDGRppaVRVYCFGGEAVPAASLRLAWEA 2284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 375 LGCQ-VYEGYGQTEctagcTFTTPGDWTSGH----------VGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKG 443
Cdd:PRK12316 2285 LRPVyLFNGYGPTE-----AVVTPLLWKCRPqdpcgaayvpIGRALGNRRAYILD-ADLNLLAPGMAGELYLGGEGLARG 2358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 444 YLKDPDRTKEALDSDGWLH-------TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENiYIRSQP-------VA 509
Cdd:PRK12316 2359 YLNRPGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKI-RGFRIELGEIEA-RLQAHPavreavvVA 2436
|
490
....*....|....*
gi 327412329 510 QIYVHGDSLKAFLVG 524
Cdd:PRK12316 2437 QDGASGKQLVAYVVP 2451
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
360-531 |
1.12e-11 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 67.40 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 360 AAPASPTVLGFLRAALGCQVYEGYGQTECTaGCTFTTPGDWTS--GHVGAPLPcNHIKLVDvEELNYWACKGEGEICVRG 437
Cdd:cd05929 253 AAPCPPWVKEQWIDWGGPIIWEYYGGTEGQ-GLTIINGEEWLThpGSVGRAVL-GKVHILD-EDGNEVPPGEIGEVYFAN 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 438 PNVFKgYLKDPDRTKEALDSDGWLHTGDIGkWLPA-GTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRsqpvaqiyvHGD 516
Cdd:cd05929 330 GPGFE-YTNDPEKTAAARNEGGWSTLGDVG-YLDEdGYLYLTDRRSDMI-ISGGVNIYPQEIENALIA---------HPK 397
|
170
....*....|....*
gi 327412329 517 SLKAFLVGivVPDPE 531
Cdd:cd05929 398 VLDAAVVG--VPDEE 410
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
233-499 |
2.68e-11 |
|
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: 65.96 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 233 DDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVT-EGDIRLLSDDMKALCPTIFPVVprllnrmYDKIFSqanTPLK 311
Cdd:cd17656 128 DDLLYIIYTSGTTGKPKGVQLEHKNMV----NLLHFErEKTNINFSDKVLQFATCSFDVC-------YQEIFS---TLLS 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 312 RWLLEFAAKRKQAEVRS--GIIRNDSI--------WDELFFNKIQA--SLGGCVRMIVTGAAP--ASPTVLGFLRAAlGC 377
Cdd:cd17656 194 GGTLYIIREETKRDVEQlfDLVKRHNIevvflpvaFLKFIFSEREFinRFPTCVKHIITAGEQlvITNEFKEMLHEH-NV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 378 QVYEGYG--QTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEA 454
Cdd:cd17656 273 HLHNHYGpsETHVVTTYTINPEAEIPElPPIGKPISNTWIYILD-QEQQLQPQGIVGELYISGASVARGYLNRQELTAEK 351
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 327412329 455 LDSDGW------LHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIE 499
Cdd:cd17656 352 FFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIELGEIE 401
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
220-544 |
3.99e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 66.52 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 220 GQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgFLKVTEGDIRLLSDDmkalcptifpvvpRLLNRM- 298
Cdd:PRK12316 4681 GFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVN----HLHATGERYELTPDD-------------RVLQFMs 4743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 299 --YDKIFSQANTPLKRwllefaakrkQAEVrsgIIRNDSIWD-ELFFNKI---QASLGGCV----RMIVTGAA----PAS 364
Cdd:PRK12316 4744 fsFDGSHEGLYHPLIN----------GASV---VIRDDSLWDpERLYAEIhehRVTVLVFPpvylQQLAEHAErdgePPS 4810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 365 PTVLGF-------------LRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSG----HVGAPLPCNHIKLVDVEeLNYWA 426
Cdd:PRK12316 4811 LRVYCFggeavaqasydlaWRALKPVYLFNGYGPTETTVTVLlWKARDGDACGaaymPIGTPLGNRSGYVLDGQ-LNPLP 4889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 427 CKGEGEICVRGPNVFKGYLKDPDRTKEALDSD------GWLH-TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIE 499
Cdd:PRK12316 4890 VGVAGELYLGGEGVARGYLERPALTAERFVPDpfgapgGRLYrTGDLARYRADGVIDYLGRVDHQVKI-RGFRIELGEIE 4968
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 327412329 500 nIYIRSQP-------VAQIYVHGdslkAFLVGIVVP-DPEVMPSWAQKRGIEG 544
Cdd:PRK12316 4969 -ARLREHPavreavvIAQEGAVG----KQLVGYVVPqDPALADADEAQAELRD 5016
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
354-535 |
4.36e-11 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 65.49 E-value: 4.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 354 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCNHIKLVDvEELNYWACKGEG 431
Cdd:PRK12406 274 RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE-SGAVTFATSEDALShpGTVGKAAPGAELRFVD-EDGRPLPQGEIG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 432 EICVRGPNV--FKgYLKDPDRTKEaLDSDGWLHTGDIGkWLPA-GTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPV 508
Cdd:PRK12406 352 EIYSRIAGNpdFT-YHNKPEKRAE-IDRGGFITSGDVG-YLDAdGYLFLCDRKRDMV-ISGGVNIYPAEIEAVLHAVPGV 427
|
170 180 190
....*....|....*....|....*....|
gi 327412329 509 AQIYVHGDSLKAF---LVGIVVPDPEVMPS 535
Cdd:PRK12406 428 HDCAVFGIPDAEFgeaLMAVVEPQPGATLD 457
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
232-534 |
7.42e-11 |
|
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: 64.73 E-value: 7.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 232 PDDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSG-FLKVTEGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQAN 307
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVnlrTSLSErYFGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEM 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 308 TPLKRWLLEFAaKRKQAEVRSGiirNDSIWDELFFnkiqASLGGCVRMIVTGAAPASPtVLGFLRAALGCQVYEGYGQTE 387
Cdd:cd17648 173 RFDPDRFYAYI-NREKVTYLSG---TPSVLQQYDL----ARLPHLKRVDAAGEEFTAP-VFEKLRSRFAGLIINAYGPTE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 388 C--TAGCTFTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKE------------ 453
Cdd:cd17648 244 TtvTNHKRFFPGDQRFDKSLGRPVRNTKCYVLN-DAMKRVPVGAVGELYLGGDGVARGYLNRPELTAErflpnpfqteqe 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 454 -ALDSDGWLH-TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIY-----IRSQPVAQIYVHGDSLKA---FLV 523
Cdd:cd17648 323 rARGRNARLYkTGDLVRWLPSGELEYLGRNDFQVKI-RGQRIEPGEVEAALasypgVRECAVVAKEDASQAQSRiqkYLV 401
|
330
....*....|.
gi 327412329 524 GIVVPDPEVMP 534
Cdd:cd17648 402 GYYLPEPGHVP 412
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
166-523 |
1.42e-10 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 64.28 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 166 DKPQKAVLLLEHVERketpGLkLIILMDPF----EEALKERGQKCGVVIKS------------MQAVEDCGQENHQAPVP 229
Cdd:PRK06060 64 DSPDLVQLLLACLAR----GV-MAFLANPElhrdDHALAARNTEPALVVTSdalrdrfqpsrvAEAAELMSEAARVAPGG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 230 PQP---DDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF----LKVTEGDIRLLSDDMK---ALCPTI-FPVV---PRLL 295
Cdd:PRK06060 139 YEPmggDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMcrkaLRLTPEDTGLCSARMYfayGLGNSVwFPLAtggSAVI 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 296 NRMydkifsqantPLKRWLLEFAAKRKQAEVRSGIIRndsiwdelFFNKIqasLGGC-------VRMIVTGAAPASPTVL 368
Cdd:PRK06060 219 NSA----------PVTPEAAAILSARFGPSVLYGVPN--------FFARV---IDSCspdsfrsLRCVVSAGEALELGLA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 369 GFLRAALG-CQVYEGYGQTEctAGCTFT--TPGDWTSGHVGAPLPCNHIKLVDVEELNYwACKGEGEICVRGPNVFKGYL 445
Cdd:PRK06060 278 ERLMEFFGgIPILDGIGSTE--VGQTFVsnRVDEWRLGTLGRVLPPYEIRVVAPDGTTA-GPGVEGDLWVRGPAIAKGYW 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 446 KDPDrtkEALDSDGWLHTGDIGK-----WLPAGTlkiidrKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHG----- 515
Cdd:PRK06060 355 NRPD---SPVANEGWLDTRDRVCidsdgWVTYRC------RADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAvrest 425
|
410
....*....|
gi 327412329 516 --DSLKAFLV 523
Cdd:PRK06060 426 gaSTLQAFLV 435
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
117-465 |
2.63e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 63.38 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 117 VFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADiSTVIVDKPQkavlLLEHVERKETPGLKLIILMDPFE 196
Cdd:PRK04319 103 IFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSE-AKVLITTPA----LLERKPADDLPSLKHVLLVGEDV 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 197 EAlkerGQKCGVVIKSM-QAVEDCgqenhqAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADF-SGF--LKVTEGD 272
Cdd:PRK04319 178 EE----GPGTLDFNALMeQASDEF------DIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYqTGKyvLDLHEDD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 273 IRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTPlKRWLlefaakrkqaevrsGIIRND--SIW------------- 337
Cdd:PRK04319 248 VYWCTADPGWVTGTSYGIFAPWLNGATNVIDGGRFSP-ERWY--------------RILEDYkvTVWytaptairmlmga 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 338 -DELfFNKIQASlggCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPCNHIK 415
Cdd:PRK04319 313 gDDL-VKKYDLS---SLRHILSVGEPLNPEVVRWGMKVFGLPIHDNWWMTETGGIMIANYPAmDIKPGSMGKPLPGIEAA 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 327412329 416 LVDVEElNYWACKGEGEICVRG--PNVFKGYLKDPDRTKEALdSDGWLHTGD 465
Cdd:PRK04319 389 IVDDQG-NELPPNRMGNLAIKKgwPSMMRGIWNNPEKYESYF-AGDWYVSGD 438
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
115-532 |
5.93e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 61.97 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 115 IGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAvlLLEHVErkeTPGLKLIILMDP 194
Cdd:PRK13388 55 VGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLVTDAEHRP--LLDGLD---LPGVRVLDVDTP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 195 -FEEALKERGqkcgvviksmqavedcgqENHQAPvPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVTEGDi 273
Cdd:PRK13388 130 aYAELVAAAG------------------ALTPHR-EVDAMDPFMLIFTSGTTGAPKAVRCSHGRLA--FAGRALTERFG- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 274 rLLSDDMKALCPTIF----------PVVPrllnrmydkifSQANTPLKRwllEFAAKRKQAEVRSgiirndsiWDELFFN 343
Cdd:PRK13388 188 -LTRDDVCYVSMPLFhsnavmagwaPAVA-----------SGAAVALPA---KFSASGFLDDVRR--------YGATYFN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 344 KIQASLGgcvRMIVTGAAP---ASPTVLGFLRAA-----------LGCQVYEGYGQTEctAGCTFTTPGDWTSGHVGAPL 409
Cdd:PRK13388 245 YVGKPLA---YILATPERPddaDNPLRVAFGNEAsprdiaefsrrFGCQVEDGYGSSE--GAVIVVREPGTPPGSIGRGA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 410 PcnHIKLVDVEE---------------LNywACKGEGEICVR-GPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAG 473
Cdd:PRK13388 320 P--GVAIYNPETltecavarfdahgalLN--ADEAIGELVNTaGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 327412329 474 TLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYVHGdslkaflvgivVPDPEV 532
Cdd:PRK13388 395 WIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYA-----------VPDERV 441
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
226-523 |
7.40e-10 |
|
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: 61.78 E-value: 7.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 226 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGN--VVADFSG--FLKVTEGDIRLLSDDM-------KALcptIFPVVPRL 294
Cdd:TIGR02262 154 KPAATQADDPAFWLYSSGSTGMPKGVVHTHSNpyWTAELYArnTLGIREDDVCFSAAKLffayglgNAL---TFPMSVGA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 295 LNRMYdkifSQANTP---LKRWLlefaakRKQAEVRSGIirnDSIWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGF- 370
Cdd:TIGR02262 231 TTVLM----GERPTPdavFDRLR------RHQPTIFYGV---PTLYAAMLADPNLPSEDQVRLRLCTSAGEALPAEVGQr 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 371 LRAALGCQVYEGYGQTEctAGCTFTT--PGDWTSGHVGAPLPCNHIKLVDveELNYWACKGE-GEICVRGPNVFKGYLKD 447
Cdd:TIGR02262 298 WQARFGVDIVDGIGSTE--MLHIFLSnlPGDVRYGTSGKPVPGYRLRLVG--DGGQDVADGEpGELLISGPSSATMYWNN 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 448 PDRTKEALDSdGWLHTGDigKWL--PAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVHG----DSL--- 518
Cdd:TIGR02262 374 RAKSRDTFQG-EWTRSGD--KYVrnDDGSYTYAGRTDDMLKVS-GIYVSPFEIESALIQHPAVLEAAVVGvadeDGLikp 449
|
....*
gi 327412329 519 KAFLV 523
Cdd:TIGR02262 450 KAFVV 454
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
51-564 |
7.75e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 62.49 E-value: 7.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 51 YDDARTMYQVFRRGLSISGNGPCLGFRKpkqpyQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVEL 130
Cdd:PRK12467 1570 YPLARLVHQLIEDQAAATPEAVALVFGE-----QELTYGELNRRANRLAHRLIALGVGP--EVLVGIAVERSLEMVVGLL 1642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 131 ACYTYSMVVVPLYDTLGPGAIRYIINTADIStvivdkpqkavLLLEHveRKETPGLKLIilmdpfeealkeRGQKCGVVI 210
Cdd:PRK12467 1643 AILKAGGAYVPLDPEYPRERLAYMIEDSGIE-----------LLLTQ--SHLQARLPLP------------DGLRSLVLD 1697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 211 KSMQAVEDCGQENHQapVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFsgflKVTEGDIRLLSDD----------- 279
Cdd:PRK12467 1698 QEDDWLEGYSDSNPA--VNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRL----CATQEAYQLSAADvvlqftsfafd 1771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 280 ------MKALCP-----TIFPVVPRLLNRMYDKIFSQANTplkrwLLEFAAKRKQAevrsgiirndsiwdelfFNKIQAS 348
Cdd:PRK12467 1772 vsvwelFWPLINgarlvIAPPGAHRDPEQLIQLIERQQVT-----TLHFVPSMLQQ-----------------LLQMDEQ 1829
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 349 LGGC--VRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAG-----CTFTTPGDWTSGHVGAPLPCNHIKLVDvE 420
Cdd:PRK12467 1830 VEHPlsLRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPTETAVDvthwtCRRKDLEGRDSVPIGQPIANLSTYILD-A 1908
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 421 ELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL------DSDGWLH-TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYV 493
Cdd:PRK12467 1909 SLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLYrTGDLARYRADGVIEYLGRIDHQVKI-RGFRI 1987
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 327412329 494 APEKIENiYIRSQP----VAQIYVHGDSLKAfLVGIVVPDPEVMPSWAQKRgieGTYADlcTNKDLKKAILED-MV 564
Cdd:PRK12467 1988 ELGEIEA-RLREQGgvreAVVIAQDGANGKQ-LVAYVVPTDPGLVDDDEAQ---VALRA--ILKNHLKASLPEyMV 2056
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
86-531 |
8.07e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 61.48 E-value: 8.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRpEWIIVELACYTYSmvvvplydtlgpGAIRYIINTAdistviV 165
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRA--GDGVAVLARNH-RGFVLALYAAGKV------------GARIILLNTG------F 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 166 DKPQkavlLLEHVERKetpGLKLIILMDPFEE---ALKERGQKCGVVIKSMQAVEDC------------GQENHQAPVPP 230
Cdd:PRK07788 134 SGPQ----LAEVAARE---GVKALVYDDEFTDllsALPPDLGRLRAWGGNPDDDEPSgstdetlddliaGSSTAPLPKPP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 231 QPDdlSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtegdIRLLSDDMKALCPTIF----------------PVVPRl 294
Cdd:PRK07788 207 KPG--GIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSR----VPFRAGETTLLPAPMFhatgwahltlamalgsTVVLR- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 295 lnrmydKIFSQANTplkrwlLEFAAKRK-QAEVRSGIirndsiwdelFFNKIQAsLGGCVR----------MIVTGAAPA 363
Cdd:PRK07788 280 ------RRFDPEAT------LEDIAKHKaTALVVVPV----------MLSRILD-LGPEVLakydtsslkiIFVSGSALS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 364 SPTVLGFLrAALGCQVYEGYGQTECtAGCTFTTPGDWT--SGHVGAPLPCNHIKLVD-----VEElnywackGE-GEICV 435
Cdd:PRK07788 337 PELATRAL-EAFGPVLYNLYGSTEV-AFATIATPEDLAeaPGTVGRPPKGVTVKILDengneVPR-------GVvGRIFV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 436 RGPNVFKGYlKDPdRTKEALdsDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIyirsqpvaqIYVHG 515
Cdd:PRK07788 408 GNGFPFEGY-TDG-RDKQII--DGLLSSGDVGYFDEDGLLFVDGRDDDMI-VSGGENVFPAEVEDL---------LAGHP 473
|
490
....*....|....*.
gi 327412329 516 DSLKAFLVGivVPDPE 531
Cdd:PRK07788 474 DVVEAAVIG--VDDEE 487
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
353-531 |
1.00e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 61.07 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 353 VRMIVTGAAPASPTVLgflRAAL---GCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCNhIKLVDvEELNYWAC 427
Cdd:PRK08276 264 LRVAIHAAAPCPVEVK---RAMIdwwGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGE-VRILD-EDGNELPP 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 428 KGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkWLPA-GTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQ 506
Cdd:PRK08276 338 GEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVG-YLDEdGYLYLTDRKSDMI-ISGGVNIYPQEIENLLVTHP 415
|
170 180
....*....|....*....|....*
gi 327412329 507 PVAQIYVHGdslkaflvgivVPDPE 531
Cdd:PRK08276 416 KVADVAVFG-----------VPDEE 429
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
354-530 |
5.68e-09 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 58.85 E-value: 5.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 354 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT---------FTT------PGD--WTSGHVGAPLPCNHIkl 416
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAEGLVNYTrlddsderiFTTqgrpmsPDDevWVADADGNPLPQGEV-- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 417 vdveelnywackgeGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHifklaQ----GEY 492
Cdd:PRK10946 381 --------------GRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEK 441
|
170 180 190
....*....|....*....|....*....|....*...
gi 327412329 493 VAPEKIENIYIRsqpvaqiyvHGDSLKAFLVGIvvPDP 530
Cdd:PRK10946 442 IAAEEIENLLLR---------HPAVIHAALVSM--EDE 468
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
51-540 |
6.36e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 59.59 E-value: 6.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 51 YDDARTMYQVFRRGLSISGNGPCLGFRKpkqpyQWLSYQEVADRAEFLGSGLLQhnCKACTDQFIGVFAQNRPEWIIVEL 130
Cdd:PRK12316 507 YPLQRGVHRLFEEQVERTPEAPALAFGE-----ETLDYAELNRRANRLAHALIE--RGVGPDVLVGVAMERSIEMVVALL 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 131 ACYTYSMVVVPLYDTLGPGAIRYIINTADIstvivdkpqkAVLLLEHVERKETP---GLKLIILMDP--FEEALKERGQK 205
Cdd:PRK12316 580 AILKAGGAYVPLDPEYPAERLAYMLEDSGV----------QLLLSQSHLGRKLPlaaGVQVLDLDRPaaWLEGYSEENPG 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 206 CGVViksmqavedcgqenhqapvppqPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEGDirlLSDDMKALCP 285
Cdd:PRK12316 650 TELN----------------------PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLG---VGDTVLQKTP 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 286 TIFPV------VPrLLN--RMYDKIFSQANTPLKRW---------LLEFAAKRKQAEVRSGIIrndsiwdelffnkiqAS 348
Cdd:PRK12316 705 FSFDVsvweffWP-LMSgaRLVVAAPGDHRDPAKLVelinregvdTLHFVPSMLQAFLQDEDV---------------AS 768
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 349 LGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHV--GAPLPCNHIKLVDVeELNYWA 426
Cdd:PRK12316 769 CTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGGDSVpiGRPIANLACYILDA-NLEPVP 847
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 427 CKGEGEICVRGPNVFKGYLKDPDRTKEAL------DSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIEN 500
Cdd:PRK12316 848 VGVLGELYLAGRGLARGYHGRPGLTAERFvpspfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEA 926
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 327412329 501 IYIRSQPVAQIYVHGDSLKAfLVGIVVPD------PEVMPSWAQKR 540
Cdd:PRK12316 927 RLLEHPWVREAAVLAVDGKQ-LVGYVVLEseggdwREALKAHLAAS 971
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
86-531 |
8.28e-09 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 58.30 E-value: 8.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLGSGLLQHNCKAcTDQFIGVFAQNrPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 165
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGP-GDVVAGLLPRT-PELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 166 DKPQKAVLllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhqapvppqPDDLSIVCFTSGTT 245
Cdd:cd05973 79 DAANRHKL----------------------------------------------------------DSDPFVMMFTSGTT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 246 GNPKGAMLTHgNVVADFSGFLK----VTEGDIRLLSDD-------MKALCPTIFPVVPRLLnrmYDKIFSQANT--PLKR 312
Cdd:cd05973 101 GLPKGVPVPL-RALAAFGAYLRdavdLRPEDSFWNAADpgwayglYYAITGPLALGHPTIL---LEGGFSVESTwrVIER 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 313 W-LLEFAAkrkqAEVRSGIIRNDSIwdelffnKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEC-TA 390
Cdd:cd05973 177 LgVTNLAG----SPTAYRLLMAAGA-------EVPARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELgMV 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 391 GCTFTTPGDWT-SGHVGAPLPCNHIKLVDvEELNYWACKGEGEICV---RGPNV-FKGYLKDPDRTKealdSDGWLHTGD 465
Cdd:cd05973 246 LANHHALEHPVhAGSAGRAMPGWRVAVLD-DDGDELGPGEPGRLAIdiaNSPLMwFRGYQLPDTPAI----DGGYYLTGD 320
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 327412329 466 IGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVhgdslkaflvgIVVPDPE 531
Cdd:cd05973 321 TVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVESALIEHPAVAEAAV-----------IGVPDPE 374
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
86-532 |
9.78e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 58.10 E-value: 9.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLGSGLlqHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIv 165
Cdd:PRK13390 25 VSYRQLDDDSAALARVL--YDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLV- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 166 dkpqkAVLLLEHVERKETPGLKLIILMD-------PFEEALKERGQKCgvviksmqAVEDCGqenhqapvppqpddlSIV 238
Cdd:PRK13390 102 -----ASAALDGLAAKVGADLPLRLSFGgeidgfgSFEAALAGAGPRL--------TEQPCG---------------AVM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 239 CFTSGTTGNPKG--------AMLTHGN-VVADFSGFLKVTEGDIRLLSDDMKALCPTIFPVVPRLL--NRMYDKIFSQAN 307
Cdd:PRK13390 154 LYSSGTTGFPKGiqpdlpgrDVDAPGDpIVAIARAFYDISESDIYYSSAPIYHAAPLRWCSMVHALggTVVLAKRFDAQA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 308 TplKRWLLEFAAKRKQAeVRSGIIRNDSIWDELFFNKIQASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTE 387
Cdd:PRK13390 234 T--LGHVERYRITVTQM-VPTMFVRLLKLDADVRTRYDVSSL----RAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 388 cTAGCTFTTPGDWTS--GHVG-APLPCNHIKLVDVEELNywackgEGEIcvrGPNVFK------GYLKDPDRTKEALDSD 458
Cdd:PRK13390 307 -AHGMTFIDSPDWLAhpGSVGrSVLGDLHICDDDGNELP------AGRI---GTVYFErdrlpfRYLNDPEKTAAAQHPA 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 327412329 459 G--WLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYVHGdslkaflvgivVPDPEV 532
Cdd:PRK13390 377 HpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETENALTMHPAVHDVAVIG-----------VPDPEM 440
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
229-482 |
1.50e-08 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 57.71 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 229 PPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF----LKVTEGDiRLLS-----DDMKALCPTIFPVVPRL-LNRM 298
Cdd:PRK09192 172 RPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAIshdgLKVRPGD-RCVSwlpfyHDMGLVGFLLTPVATQLsVDYL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 299 YDKIFsqANTPLKrWL-----------------LEFAAKRkqAEVRSGIIRNDSIWdelffnkiqaslggcvRMIVTGAA 361
Cdd:PRK09192 251 PTRDF--ARRPLQ-WLdlisrnrgtisysppfgYELCARR--VNSKDLAELDLSCW----------------RVAGIGAD 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 362 PASPTVL----------GF-LRAALGCqvyegYGQTECTAGCTFTTPG----------DWTSGH---------------- 404
Cdd:PRK09192 310 MIRPDVLhqfaeafapaGFdDKAFMPS-----YGLAEATLAVSFSPLGsgivveevdrDRLEYQgkavapgaetrrvrtf 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 405 --VGAPLPCNHIKLVDV--EELNYwacKGEGEICVRGPNVFKGYLKDPDRTKeALDSDGWLHTGDIGkWLPAGTLKIIDR 480
Cdd:PRK09192 385 vnCGKALPGHEIEIRNEagMPLPE---RVVGHICVRGPSLMSGYFRDEESQD-VLAADGWLDTGDLG-YLLDGYLYITGR 459
|
..
gi 327412329 481 KK 482
Cdd:PRK09192 460 AK 461
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
230-539 |
3.06e-08 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 55.85 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 230 PQPDDLSIVCfTSGTTGNPKGAMLTHGNV-VADFSGFLKVTEGDIRL-LSDDMKALCP--TIFPVVP-----RLLNRMYD 300
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQEDIfRMLMGGADFGTGEFTPSeDAHKAAAAAAgtVMFPAPPlmhgtGSWTAFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 301 KIFSQA-NTPLKRW----LLEFAAKRKqaeVRSGIIRNDSIWDELffnkIQASLGG------CVRMIVTGAAPASPTVL- 368
Cdd:cd05924 80 LLGGQTvVLPDDRFdpeeVWRTIEKHK---VTSMTIVGDAMARPL----IDALRDAgpydlsSLFAISSGGALLSPEVKq 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 369 GFLRAALGCQVYEGYGQTECTAGCTFTTPGdwtSGHVGAPL-PCNHIKLVDVEELNYWACK--GEGEICVRGpNVFKGYL 445
Cdd:cd05924 153 GLLELVPNITLVDAFGSSETGFTGSGHSAG---SGPETGPFtRANPDTVVLDDDGRVVPPGsgGVGWIARRG-HIPLGYY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 446 KDPDRTKEA---LDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIyIRSQP-VAQIYVHGdslkaf 521
Cdd:cd05924 229 GDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTG-GEKVFPEEVEEA-LKSHPaVYDVLVVG------ 300
|
330
....*....|....*...
gi 327412329 522 lvgivVPDPEvmpsWAQK 539
Cdd:cd05924 301 -----RPDER----WGQE 309
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
353-546 |
5.33e-08 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 55.78 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 353 VRMIVTGAAPASPTVLGFLRAA--LGCQVYeGYGQTECTAGCTFTTPGDWT---SGHVGAPLPCNHIKLVDVEELNYWAC 427
Cdd:PRK05857 288 LRLVGYGGSRAIAADVRFIEATgvRTAQVY-GLSETGCTALCLPTDDGSIVkieAGAVGRPYPGVDVYLAATDGIGPTAP 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 428 KGE-----GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIY 502
Cdd:PRK05857 367 GAGpsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGGVNIAPDEVDRIA 444
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 327412329 503 IRSQPV--AQIYVHGDSLKAFLVGI-VVPDPEVMPSWAQ--KRGIEGTY 546
Cdd:PRK05857 445 EGVSGVreAACYEIPDEEFGALVGLaVVASAELDESAARalKHTIAARF 493
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
223-540 |
8.76e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 54.67 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 223 NHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVA------DFSGflkvTEGdirllsddmkalcptifpvvprlln 296
Cdd:PRK07824 25 DALRVGEPIDDDVALVVATSGTTGTPKGAMLTAAALTAsadathDRLG----GPG------------------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 297 rmydkifsqantplkRWLLEFAAKR---KQAEVRSGIIRNDSI-------WDELFFNKIQASLGGCVR------------ 354
Cdd:PRK07824 76 ---------------QWLLALPAHHiagLQVLVRSVIAGSEPVeldvsagFDPTALPRAVAELGGGRRytslvpmqlaka 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 355 --------------MIVTGAAPASPTVlgfLRAA--LGCQVYEGYGQTECTAGCTFTtpgdwtsghvGAPLPCNHIKLVD 418
Cdd:PRK07824 141 lddpaataalaeldAVLVGGGPAPAPV---LDAAaaAGINVVRTYGMSETSGGCVYD----------GVPLDGVRVRVED 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 419 veelnywackgeGEICVRGPNVFKGY--LKDPDrtkeALDSDGWLHTGDIGKwLPAGTLKIIDRKKHIFKLAqGEYVAPE 496
Cdd:PRK07824 208 ------------GRIALGGPTLAKGYrnPVDPD----PFAEPGWFRTDDLGA-LDDGVLTVLGRADDAISTG-GLTVLPQ 269
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 327412329 497 KIENIYIRSQPVAQIYVHG---DSLKAFLVGIVVPDPEVMPSWAQKR 540
Cdd:PRK07824 270 VVEAALATHPAVADCAVFGlpdDRLGQRVVAAVVGDGGPAPTLEALR 316
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
222-510 |
1.80e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.79 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 222 ENHQAPVPpQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFS----GF-LKVTEGDIRL----LSDDM---KALCPTIFP 289
Cdd:PRK05691 156 EAWQEPAL-QPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQlirhGFgIDLNPDDVIVswlpLYHDMgliGGLLQPIFS 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 290 VVPRLLnrMYDKIFSQanTPLkRWLL-------------EFAAKRKQAEVR------------------SGIIRNDSIwd 338
Cdd:PRK05691 235 GVPCVL--MSPAYFLE--RPL-RWLEaiseyggtisggpDFAYRLCSERVSesalerldlsrwrvaysgSEPIRQDSL-- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 339 ELFFNKIQ----------ASLG-GCVRMIVTGAAPA-SPTVLGFLRAALGCQVYEGyGQTECTAGCTFTTPGdwtsghvg 406
Cdd:PRK05691 308 ERFAEKFAacgfdpdsffASYGlAEATLFVSGGRRGqGIPALELDAEALARNRAEP-GTGSVLMSCGRSQPG-------- 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 407 aplpcNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEA---LDSDGWLHTGDIGkWLPAGTLKIIDRKKH 483
Cdd:PRK05691 379 -----HAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfveHDGRTWLRTGDLG-FLRDGELFVTGRLKD 452
|
330 340
....*....|....*....|....*..
gi 327412329 484 IFkLAQGEYVAPEKIENIYIRSQPVAQ 510
Cdd:PRK05691 453 ML-IVRGHNLYPQDIEKTVEREVEVVR 478
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
383-501 |
2.52e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 53.62 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 383 YGQTECTAGCTFTTPG-----------DWTSGH----VGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKD 447
Cdd:PRK05851 310 YGLAESTCAVTVPVPGiglrvdevttdDGSGARrhavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQ 389
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 327412329 448 PdrtkeALDSDGWLHTGDIGkWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENI 501
Cdd:PRK05851 390 A-----PIDPDDWFPTGDLG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERV 436
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
408-468 |
2.05e-06 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 50.66 E-value: 2.05e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 327412329 408 PLPCNHIK-----LVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL-DSDGW--LHTGDIGK 468
Cdd:PRK04813 317 RLPIGYAKpdsplLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGY 385
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
353-500 |
4.72e-06 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 48.94 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 353 VRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTEcTAGCTFTTPGD-WTSGHVGAPLPCNHIKLVDVEElnywacKGE 430
Cdd:cd17633 112 IKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSE-LSFITYNFNQEsRPPNSVGRPFPNVEIEIRNADG------GEI 184
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 431 GEICVRGPNVFKGYLKDPDRTKealdsDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIEN 500
Cdd:cd17633 185 GKIFVKSEMVFSGYVRGGFSNP-----DGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIES 248
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
227-535 |
6.81e-06 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 49.11 E-value: 6.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 227 PVPPQPDDLSIVCFTSGTTGNPKGAMLTHGN----VVADFSGFLKVTEGDIRLLSDDMK-------------ALCPTIF- 288
Cdd:cd17634 226 PEAMNAEDPLFILYTSGTTGKPKGVLHTTGGylvyAATTMKYVFDYGPGDIYWCTADVGwvtghsyllygplACGATTLl 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 289 ----PVVPRlLNRMYDKIFSQANTPLkrWLLEFAAKRKQAEVRSGIIRNDsiwdelffnkiQASLggcvRMIVTGAAPAS 364
Cdd:cd17634 306 yegvPNWPT-PARMWQVVDKHGVNIL--YTAPTAIRALMAAGDDAIEGTD-----------RSSL----RILGSVGEPIN 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 365 PTVLGFLRAALG---CQVYEGYGQTECTAGCTFTTPG--DWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRG-- 437
Cdd:cd17634 368 PEAYEWYWKKIGkekCPVVDTWWQTETGGFMITPLPGaiELKAGSATRPVFGVQPAVVD-NEGHPQPGGTEGNLVITDpw 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 438 PNVFKGYLKDPDRTKEALDS--DGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVHG 515
Cdd:cd17634 447 PGQTRTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVA-GHRLGTAEIESVLVAHPKVAEAAVVG 525
|
330 340
....*....|....*....|...
gi 327412329 516 --DSLKA-FLVGIVVPDPEVMPS 535
Cdd:cd17634 526 ipHAIKGqAPYAYVVLNHGVEPS 548
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
240-620 |
1.42e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 47.85 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 240 FTSGTTGNPKGAMLTHGNVVADFSgflkVTEGDIRLLSDDmKALCPTIFpVVPRLLNRMYDKIFSQANTPLKRWLLEFAA 319
Cdd:PRK07638 150 FTSGSTGKPKAFLRAQQSWLHSFD----CNVHDFHMKRED-SVLIAGTL-VHSLFLYGAISTLYVGQTVHLMRKFIPNQV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 320 KRK-QAEVRSGIIRNDSIWDELFfnKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPG 398
Cdd:PRK07638 224 LDKlETENISVMYTVPTMLESLY--KENRVIENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF-VTALVDE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 399 DWTSGHVGAPLPCNHIKLVDVEELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEaLDSDGWLHTGDIGKWLPAGTLKI 477
Cdd:PRK07638 301 ESERRPNSVGRPFHNVQVRICNEAGEEVQKGEiGTVYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVGYEDEEGFIYI 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 478 IDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYVHGdslkaflvgivVPDpevmPSWAQKRG--IEGTyadlCTNKDL 555
Cdd:PRK07638 380 VGREKNMI-LFGGINIFPEEIESVLHEHPAVDEIVVIG-----------VPD----SYWGEKPVaiIKGS----ATKQQL 439
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 327412329 556 KKAILEDmvrlgkesgLHSFEQVKAIHIhsdmfsVQNGLLTPTLKAKRPELreyfKKQIEELYSI 620
Cdd:PRK07638 440 KSFCLQR---------LSSFKIPKEWHF------VDEIPYTNSGKIARMEA----KSWIENQEKI 485
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
232-515 |
1.82e-05 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 47.43 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 232 PDDLSIVCFTSGTTGNPKGAMLTHG-NVVAD--FSGFLKVTEGDiRLLSddmkalCPTIFPVVPRLLNRMYDkIFSQANT 308
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWRrTLVTSnlLSHDLNLKNGD-RTYT------CMPLYHGTAAFLGACNC-LMSGGTL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 309 PLKRwllEFAAKRKQAEVR---SGIIR------------NDSIWDELffNKIQASLGGCVRmivtgaapasPTVLGFLRA 373
Cdd:cd05937 158 ALSR---KFSASQFWKDVRdsgATIIQyvgelcryllstPPSPYDRD--HKVRVAWGNGLR----------PDIWERFRE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 374 ALGC-QVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKL--------VDVEELNYW----------ACKGE-GEI 433
Cdd:cd05937 223 RFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKFenqvvlvkMDPETDDPIrdpktgfcvrAPVGEpGEM 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 434 CVRGPNV----FKGYLKDPDRTKEAL------DSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYI 503
Cdd:cd05937 303 LGRVPFKnreaFQGYLHNEDATESKLvrdvfrKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRW-KSENVSTTEVADVLG 381
|
330
....*....|..
gi 327412329 504 RSQPVAQIYVHG 515
Cdd:cd05937 382 AHPDIAEANVYG 393
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
229-532 |
2.76e-05 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 47.06 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 229 PPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEgdirllsddMKALCPTIFpVVPrllnrMYDKI-FSQan 307
Cdd:PRK13382 192 EPTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKAILDRTP---------WRAEEPTVI-VAP-----MFHAWgFSQ-- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 308 tplkrwlLEFAA--------KRK---QAEVR-------SGIIRNDSIWDELF------FNKIQaslGGCVRMIVTGAAPA 363
Cdd:PRK13382 255 -------LVLAAslactivtRRRfdpEATLDlidrhraTGLAVVPVMFDRIMdlpaevRNRYS---GRSLRFAAASGSRM 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 364 SPTVLGFLRAALGCQVYEGYGQTEctAGCTFT-TPGDWTSG--HVGAPLPCNHIKLVDVE--ELNywacKGE-GEICVRG 437
Cdd:PRK13382 325 RPDVVIAFMDQFGDVIYNNYNATE--AGMIATaTPADLRAApdTAGRPAEGTEIRILDQDfrEVP----TGEvGTIFVRN 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 438 PNVFKGYlkDPDRTKEAldSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIyIRSQP-VAQIYV--- 513
Cdd:PRK13382 399 DTQFDGY--TSGSTKDF--HDGFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENVYPIEVEKT-LATHPdVAEAAVigv 472
|
330 340
....*....|....*....|...
gi 327412329 514 ----HGDSLKAFlvgiVVPDPEV 532
Cdd:PRK13382 473 ddeqYGQRLAAF----VVLKPGA 491
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
232-523 |
3.28e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 47.47 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 232 PDDLSIVCFTSGTTGNPKGAMLT-HGNVVADFSG--FLKVTEGDI----RLLSDDMKA---LCPTIF----PVVPRLLnr 297
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEqRGMLNNQLSKvpYLALSEADViaqtASQSFDISVwqfLAAPLFgarvEIVPNAI-- 3945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 298 mydkifsqANTPlkRWLLEFAAKRKQAEVRS------GIIRNDsiwdelffnkiQASLGGCVRMIVTGAAPASPTVLGFL 371
Cdd:PRK05691 3946 --------AHDP--QGLLAHVQAQGITVLESvpsliqGMLAED-----------RQALDGLRWMLPTGEAMPPELARQWL 4004
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 372 RAALGCQVYEGYGQTECTAGCTF------TTPGDWTSghVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYL 445
Cdd:PRK05691 4005 QRYPQIGLVNAYGPAECSDDVAFfrvdlaSTRGSYLP--IGSPTDNNRLYLLD-EALELVPLGAVGELCVAGTGVGRGYV 4081
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 446 KDPDRTKEAL-------DSDGWLHTGDIGKWLPAGTLKIIDRKKHI-----FKLAQGEYVApEKIENIYIRSQPVA-QIY 512
Cdd:PRK05691 4082 GDPLRTALAFvphpfgaPGERLYRTGDLARRRSDGVLEYVGRIDHQvkirgYRIELGEIEA-RLHEQAEVREAAVAvQEG 4160
|
330
....*....|.
gi 327412329 513 VHGDSLKAFLV 523
Cdd:PRK05691 4161 VNGKHLVGYLV 4171
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
343-507 |
9.70e-05 |
|
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: 45.50 E-value: 9.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 343 NKIQASLGGCVRMIVTGAAPASPTV----LGFLRA--ALGCQVYEGYGqTECTAGCTFTTPGDWTSGHVGAPLPCNHI-K 415
Cdd:cd05915 263 ESTGHRLKTLRRLVVGGSAAPRSLIarfeRMGVEVrqGYGLTETSPVV-VQNFVKSHLESLSEEEKLTLKAKTGLPIPlV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 416 LVDVEELNYWACKGEGE----ICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGE 491
Cdd:cd05915 342 RLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG-GE 420
|
170
....*....|....*.
gi 327412329 492 YVAPEKIENIyIRSQP 507
Cdd:cd05915 421 WISSVDLENA-LMGHP 435
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
86-523 |
1.09e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 44.99 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 165
Cdd:PRK13383 61 LSYRELQRATESLARRLTRDGVAP--GRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 166 DkpqkavlllehverketpglkliilmDPFEEALKERGQKCGVVIKSMQAVEDCGQENHQAPVPpqpddlSIVCFTSGTT 245
Cdd:PRK13383 139 D--------------------------NEFAERIAGADDAVAVIDPATAGAEESGGRPAVAAPG------RIVLLTSGTT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 246 GNPKGamLTHGNVVADFSGFLKVTEGDIRLLSDDMKALCptiFPVVPRLLNRMYDKIFSQANTPLKRWLLEFAAKRKQAE 325
Cdd:PRK13383 187 GKPKG--VPRAPQLRSAVGVWVTILDRTRLRTGSRISVA---MPMFHGLGLGMLMLTIALGGTVLTHRHFDAEAALAQAS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 326 VRsgiiRNDSiwdelfFNKIQASLG---------------GCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTA 390
Cdd:PRK13383 262 LH----RADA------FTAVPVVLArilelpprvrarnplPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 391 GcTFTTPG---DWTSGhVGAPLPCNHIKLVDVEELNYwACKGEGEICVRGPNVFKGYlkdPDRTKEALdSDGWLHTGDIG 467
Cdd:PRK13383 332 G-ALATPAdlrDAPET-VGKPVAGCPVRILDRNNRPV-GPRVTGRIFVGGELAGTRY---TDGGGKAV-VDGMTSTGDMG 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 327412329 468 KWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLV 523
Cdd:PRK13383 405 YLDNAGRLFIVGREDDMI-ISGGENVYPRAVENALAAHPAVADNAVigvpderFGHRLAAFVV 466
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
86-273 |
1.46e-04 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 44.87 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 86 LSYQEVADRAE-----FLGSGLLQHNCkactdqfIGVFAQNRPEWIIVELACyTYSMVVVPLYDT-LGPGAIRYIINTAD 159
Cdd:PRK08279 63 ISYAELNARANryahwAAARGVGKGDV-------VALLMENRPEYLAAWLGL-AKLGAVVALLNTqQRGAVLAHSLNLVD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 160 ISTVIVDKPqkavlLLEHVE--RKETPGLKLIILMDPFEEALKERgqkcgvVIKSMQAVEDCGQENHQAPVPPQPDDLSI 237
Cdd:PRK08279 135 AKHLIVGEE-----LVEAFEeaRADLARPPRLWVAGGDTLDDPEG------YEDLAAAAAGAPTTNPASRSGVTAKDTAF 203
|
170 180 190
....*....|....*....|....*....|....*....
gi 327412329 238 VCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTEGDI 273
Cdd:PRK08279 204 YIYTSGTTGLPKAAVMSHMRWLkamGGFGGLLRLTPDDV 242
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
191-273 |
2.20e-04 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 44.20 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 191 LMDPFEE---ALKERGQKCGVVIKSM--QAVEDCGQENHQAPVPPQPDDLS---------IVCFTSGTTGNPKGAMLTHG 256
Cdd:cd05938 88 LQEAVEEvlpALRADGVSVWYLSHTSntEGVISLLDKVDAASDEPVPASLRahvtikspaLYIYTSGTTGLPKAARISHL 167
|
90 100
....*....|....*....|
gi 327412329 257 NVVAdFSGFL---KVTEGDI 273
Cdd:cd05938 168 RVLQ-CSGFLslcGVTADDV 186
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
228-259 |
4.87e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 43.49 E-value: 4.87e-04
10 20 30
....*....|....*....|....*....|..
gi 327412329 228 VPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVV 259
Cdd:PRK10252 593 QLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIV 624
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
339-524 |
7.84e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.85 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 339 ELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTF--TTPGDWTSGHVGAPLPCNHIK 415
Cdd:PRK05691 1376 QLFIDEPLAAACTSLRRLFSGGEALPAELRNRVLQRLpQVQLHNRYGPTETAINVTHwqCQAEDGERSPIGRPLGNVLCR 1455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 416 LVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKE-----ALDSDG--WLHTGDIGKWLPAGTLKIIDRKKHIFKLa 488
Cdd:PRK05691 1456 VLD-AELNLLPPGVAGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL- 1533
|
170 180 190
....*....|....*....|....*....|....*...
gi 327412329 489 QGEYVAPEKIENIYIRSQPVAQ--IYVHGDSLKAFLVG 524
Cdd:PRK05691 1534 RGFRVEPEEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
234-531 |
9.25e-04 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 41.96 E-value: 9.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 234 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTegdIRLLSDdmkalcpTIFPVVP-----RLLNRMYDKIFSQANT 308
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSG---GALPSD-------VLYTCLPlyhstALIVGWSACLASGATL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 309 PLKRwllEFAAKRkqaevrsgiirndsIWDELffNKIQASL----GGCVRMIVtgAAPASPTVLGF-LRAALG------- 376
Cdd:cd05940 152 VIRK---KFSASN--------------FWDDI--RKYQATIfqyiGELCRYLL--NQPPKPTERKHkVRMIFGnglrpdi 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 377 ----------CQVYEGYGQTECTAGCT--FTTPGdwTSGHVGAPLPCNH-IKLV--DVEELNYW---------ACKGE-- 430
Cdd:cd05940 211 weefkerfgvPRIAEFYAATEGNSGFInfFGKPG--AIGRNPSLLRKVApLALVkyDLESGEPIrdaegrcikVPRGEpg 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 431 ---GEICVRGPnvFKGYLKDPDRTKEAL-----DSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIY 502
Cdd:cd05940 289 lliSRINPLEP--FDGYTDPAATEKKILrdvfkKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRW-KGENVSTTEVAAVL 365
|
330 340 350
....*....|....*....|....*....|....
gi 327412329 503 IRSQPVAQIYVHGDSL-----KAFLVGIVVPDPE 531
Cdd:cd05940 366 GAFPGVEEANVYGVQVpgtdgRAGMAAIVLQPNE 399
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
226-482 |
1.65e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 41.47 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 226 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADF----SGFLKVTEGDIRL---------LSDDMKAL--------- 283
Cdd:PRK05850 153 DARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFeqlmSDYFGDTGGVPPPdttvvswlpFYHDMGLVlgvcapilg 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 284 -CPTIF--PVV----P----RLLNRmYDKIFSQAntPlkRWLLEFAAKRKQAEVRSGIirndsiwdelffnkiqaSLGGc 352
Cdd:PRK05850 233 gCPAVLtsPVAflqrParwmQLLAS-NPHAFSAA--P--NFAFELAVRKTSDDDMAGL-----------------DLGG- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 353 VRMIVTGAAPASP-TVLGFLR--AALGCQ---VYEGYGQTECTAGCTFTTPGD-----------WTSGHV-------GAP 408
Cdd:PRK05850 290 VLGIISGSERVHPaTLKRFADrfAPFNLRetaIRPSYGLAEATVYVATREPGQppesvrfdyekLSAGHAkrcetggGTP 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 409 LPCNH------IKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALD------SDG-----WLHTGDIGkWLP 471
Cdd:PRK05850 370 LVSYGsprsptVRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGatlvdpSPGtpegpWLRTGDLG-FIS 448
|
330
....*....|.
gi 327412329 472 AGTLKIIDRKK 482
Cdd:PRK05850 449 EGELFIVGRIK 459
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
442-530 |
1.99e-03 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 41.57 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327412329 442 KGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIyIRSQP-VAQIYVH 514
Cdd:PRK10252 814 QGYLGRPDLTASRFIADPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKI-RGQRIELGEIDRA-MQALPdVEQAVTH 891
|
90 100
....*....|....*....|....*..
gi 327412329 515 -----------GDSLKafLVGIVVPDP 530
Cdd:PRK10252 892 acvinqaaatgGDARQ--LVGYLVSQS 916
|
|
| |
