|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
1-715 |
0e+00 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 1305.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 1 MGACVVSVMAKRNAAQVMPDPRAEELERRraecgGNFVQRVPGTESEHASAIYRIAGVTAEQHEAILAAAAAKPTFYTTL 80
Cdd:PTZ00216 1 MGGCVVSLMDKRNSRSEVPDPDIEEYRRY-----GPQNVPVPGTETENASAIYRIAGVTDEEHERLRNEWYYGPNFLQRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 81 MRHCAERTDQRVLGYRPVKCVTKEPAPSTSrgstsepaKKERLMSITHFDEVVYVTYSEMEERIFHFGAGLAALGVTANG 160
Cdd:PTZ00216 76 ERICKERGDRRALAYRPVERVEKEVVKDAD--------GKERTMEVTHFNETRYITYAELWERIVNFGRGLAELGLTKGS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 161 NVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGSANVANVLKLMKNGVMPQVPIIYVGTL 240
Cdd:PTZ00216 148 NVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGKNVPNLLRLMKSGGMPNTTIIYLDSL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 241 PASLDTHGVQVVSFKQVEMIGaaHLEGGAAKGTGPLNDDDLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLEPRVVDLLG 320
Cdd:PTZ00216 228 PASVDTEGCRLVAWTDVVAKG--HSAGSHHPLNIPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLNDLIG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 321 QPHSDDVYLSYLPMAHIMEFTITNLFIFRGAFIGFGTPRTLTDTTARPHGDLLTFNPSMLAGVPRIFDTLKKAVEAKLPP 400
Cdd:PTZ00216 306 PPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGFGSPRTLTDTFARPHGDLTEFRPVFLIGVPRIFDTIKKAVEAKLPP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 401 VGTLKRQVFDHAYQSRLAALKKGKDTPYWNEKVFAAPRAVLGNRLRIMLSGGGPLSAATHEFVNVVFGRVVIGYGLTETI 480
Cdd:PTZ00216 386 VGSLKRRVFDHAYQSRLRALKEGKDTPYWNEKVFSAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGMVIQGWGLTETV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 481 CVGAIQIPGDTETNVTGLMEPGQEIKLLDIDEYKHTDTPEPRGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGS 560
Cdd:PTZ00216 466 CCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEEYKHTDTPEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGS 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 561 FTADGKMRIVGRVKALAKNCLGEYIALEALEAVYSGNELLQPNGVCVLVHPDKPYITALALTDEARATSFAAKHGIEGTY 640
Cdd:PTZ00216 546 IAANGTLRIIGRVKALAKNCLGEYIALEALEALYGQNELVVPNGVCVLVHPARSYICALVLTDEAKAMAFAKEHGIEGEY 625
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398009334 641 PALLKDQRFQQAAAISMADTARASNRASFECVKRVRVIDDEWTPENEILTAAQKLKRRVIDAQYAQTIAELFTDD 715
Cdd:PTZ00216 626 PAILKDPEFQKKATESLQETARAAGRKSFEIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELFADE 700
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
130-700 |
0e+00 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 796.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 130 DEVVYVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQA 209
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 210 ILCGSanvanvlklmkngvmpqvpiiyvgtlpasldthgvqvvsfkqvemigaahleggaakgtgplNDDDLALIMYTSG 289
Cdd:cd17639 81 IFTDG--------------------------------------------------------------KPDDLACIMYTSG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 290 TTGDPKGVMHTHRTLAAGLHTLEPRVVDLLGqphSDDVYLSYLPMAHIMEFTITNLFIFRGAFIGFGTPRTLTD-TTARP 368
Cdd:cd17639 99 STGNPKGVMLTHGNLVAGIAGLGDRVPELLG---PDDRYLAYLPLAHIFELAAENVCLYRGGTIGYGSPRTLTDkSKRGC 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 369 HGDLLTFNPSMLAGVPRIFDTLKKAVEAKLPPVGTLKRQVFDHAYQSRLAALKKGKDTPYWNEKVFAAPRAVLGNRLRIM 448
Cdd:cd17639 176 KGDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALKEGPGTPLLDELVFKKVRAALGGRLRYM 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 449 LSGGGPLSAATHEFVNVVFGRVVIGYGLTETICVGAIQIPGDTETNVTGLMEPGQEIKLLDIDEYKH-TDTPEPRGEMLS 527
Cdd:cd17639 256 LSGGAPLSADTQEFLNIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYsTDKPPPRGEILI 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 528 RGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKALAKNCLGEYIALEALEAVYSGNELlqPNGVCV 607
Cdd:cd17639 336 RGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPL--VNNICV 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 608 LVHPDKPYITALALTDEARATSFAAKHG-IEGTYPALLKDQRFQQAAAISMADTARASNRASFECVKRVRVIDDEWTPEN 686
Cdd:cd17639 414 YADPDKSYPVAIVVPNEKHLTKLAEKHGvINSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEWTPEN 493
|
570
....*....|....
gi 398009334 687 EILTAAQKLKRRVI 700
Cdd:cd17639 494 GLVTAAQKLKRKEI 507
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
133-712 |
1.48e-133 |
|
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: 405.06 E-value: 1.48e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 133 VYVTYSEMEERIFHFGAGLAALGVTANGN--VSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAI 210
Cdd:cd05927 4 EWISYKEVAERADNIGSALRSLGGKPAPAsfVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 211 LCGSanvanvlklmkngvmpqvpiiyvgtlpasldthGVQVVSFKQVEMIGAAhleggaAKGTGPLND-DDLALIMYTSG 289
Cdd:cd05927 84 FCDA---------------------------------GVKVYSLEEFEKLGKK------NKVPPPPPKpEDLATICYTSG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 290 TTGDPKGVMHTHRTLAAGLHTLEpRVVDLLGQPHSDDVYLSYLPMAHIMEFTITNLFIFRGAFIGF--GTPRTLTDttar 367
Cdd:cd05927 125 TTGNPKGVMLTHGNIVSNVAGVF-KILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFysGDIRLLLD---- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 368 phgDLLTFNPSMLAGVPRIFDTLKKAVEAKLPPVGTLKRQVFDHAYQSRLAALKKGKDT--PYWNEKVFAAPRAVLGNRL 445
Cdd:cd05927 200 ---DIKALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALNYKLAELRSGVVRasPFWDKLVFNKIKQALGGNV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 446 RIMLSGGGPLSAATHEFVNVVFG-RVVIGYGLTETICVGAIQIPGDTETNVTGLMEPGQEIKLLDIDE--YKHTDtPEPR 522
Cdd:cd05927 277 RLMLTGSAPLSPEVLEFLRVALGcPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEmnYDAKD-PNPR 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 523 GEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKALAKNCLGEYIALEALEAVYSGNELLQP 602
Cdd:cd05927 356 GEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQ 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 603 ngvcVLVHPD--KPYITALALTDEARATSFAA-KHGIEGTYPALLKDQRFQQAAAISMADTARASNRASFECVKRVRVID 679
Cdd:cd05927 436 ----IFVYGDslKSFLVAIVVPDPDVLKEWAAsKGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEP 511
|
570 580 590
....*....|....*....|....*....|...
gi 398009334 680 DEWTPENEILTAAQKLKRRVIDAQYAQTIAELF 712
Cdd:cd05927 512 EPFSVENGLLTPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
128-715 |
2.68e-127 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 390.62 E-value: 2.68e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 128 HFDEVVYVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETES 207
Cdd:COG1022 34 EDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 208 QAILCGSANVANVLKlmknGVMPQVP----IIYVGTLPASLDThgvQVVSFKQVEMIGAAH-----LEGGAAKGTGplnd 278
Cdd:COG1022 114 KVLFVEDQEQLDKLL----EVRDELPslrhIVVLDPRGLRDDP---RLLSLDELLALGREVadpaeLEARRAAVKP---- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 279 DDLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLEPRVvdllgQPHSDDVYLSYLPMAHIMEFTITNLFIFRGAFIGFGT- 357
Cdd:COG1022 183 DDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERL-----PLGPGDRTLSFLPLAHVFERTVSYYALAAGATVAFAEs 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 358 PRTLTDttarphgDLLTFNPSMLAGVPRIFDTLKKAVEAKLPPVGTLKRQVFDHAY---QSRLAALKKGKDTPYW----- 429
Cdd:COG1022 258 PDTLAE-------DLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWALavgRRYARARLAGKSPSLLlrlkh 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 430 ---NEKVFAAPRAVLGNRLRIMLSGGGPLSAATHEFVNVVfG-RVVIGYGLTETICVGAIQIPGDTETNVTGLMEPGQEI 505
Cdd:COG1022 331 alaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFRAL-GiPVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGVEV 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 506 KlldIDEykhtdtpepRGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKALAKNCLGEYI 585
Cdd:COG1022 410 K---IAE---------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVTSGGKNV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 586 ALEALEAVYSGNELL-QpngvCVLVHPDKPYITALALTDEARATSFAAKHGIE-GTYPALLKDQRFQQA--AAIsmadtA 661
Cdd:COG1022 478 APQPIENALKASPLIeQ----AVVVGDGRPFLAALIVPDFEALGEWAEENGLPyTSYAELAQDPEVRALiqEEV-----D 548
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 398009334 662 RASNR-ASFECVKRVRVIDDEWTPENEILTAAQKLKRRVIDAQYAQTIAELFTDD 715
Cdd:COG1022 549 RANAGlSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYAGA 603
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
84-713 |
2.63e-124 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 386.01 E-value: 2.63e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 84 CAERTDQRVLGYRpvKCVTKEPapstsrgSTSEPAKK-ERLmsitHFDEVVYVTYSEMEERIFHFGAGLAALGVTANGNV 162
Cdd:PLN02387 68 CKKYSDKRLLGTR--KLISREF-------ETSSDGRKfEKL----HLGEYEWITYGQVFERVCNFASGLVALGHNKEERV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 163 SIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGS------ANVANVLKLMKNgvmpqvpIIY 236
Cdd:PLN02387 135 AIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSkqlkklIDISSQLETVKR-------VIY 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 237 VGTLPASLDTHGVQ-----VVSFKQVEMIGaahlEGGAAKGTGPLNdDDLALIMYTSGTTGDPKGVMHTHRTL---AAGL 308
Cdd:PLN02387 208 MDDEGVDSDSSLSGssnwtVSSFSEVEKLG----KENPVDPDLPSP-NDIAVIMYTSGSTGLPKGVMMTHGNIvatVAGV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 309 HTLEPRvvdlLGqphSDDVYLSYLPMAHIMEFTITNLFIFRGAFIGFGTPRTLTDTTAR----PHGDLLTFNPSMLAGVP 384
Cdd:PLN02387 283 MTVVPK----LG---KNDVYLAYLPLAHILELAAESVMAAVGAAIGYGSPLTLTDTSNKikkgTKGDASALKPTLMTAVP 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 385 RIFDTLKKAVEAKLPPVGTLKRQVFDHAYQSRLAALKK------GKDTPYWNEKVFAAPRAVLGNRLRIMLSGGGPLSAA 458
Cdd:PLN02387 356 AILDRVRDGVRKKVDAKGGLAKKLFDIAYKRRLAAIEGswfgawGLEKLLWDALVFKKIRAVLGGRIRFMLSGGAPLSGD 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 459 THEFVNVVFGR-VVIGYGLTETICVGAIQIPGDTETNVTGLMEPGQEIKLLDIDE--YKHTDTPEPRGEMLSRGPYLFKG 535
Cdd:PLN02387 436 TQRFINICLGApIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEggYLISDKPMPRGEIVIGGPSVTLG 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 536 YYKQPELTREV--LDEDG--WFHTGDVGSFTADGKMRIVGRVKALAKNCLGEYIALEALEAVYSGNELLQPngvcVLVHP 611
Cdd:PLN02387 516 YFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDN----IMVHA 591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 612 D--KPYITALALTDEARATSFAAKHGIEGTYPALL--KDQRFQQAAAiSMADTARASNRASFECVKRVRVIDDEWTPENE 687
Cdd:PLN02387 592 DpfHSYCVALVVPSQQALEKWAKKAGIDYSNFAELceKEEAVKEVQQ-SLSKAAKAARLEKFEIPAKIKLLPEPWTPESG 670
|
650 660
....*....|....*....|....*.
gi 398009334 688 ILTAAQKLKRRVIDAQYAQTIAELFT 713
Cdd:PLN02387 671 LVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
134-713 |
2.46e-112 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 353.63 E-value: 2.46e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 134 YVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCG 213
Cdd:PLN02736 78 WMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 214 SANVANVLKLMKNgvMPQVPIIYV-----GTLPASLDTHGVQVVSFKQVEMIGAAHLEGGAakgtgPLNDDDLALIMYTS 288
Cdd:PLN02736 158 PQTLNTLLSCLSE--IPSVRLIVVvggadEPLPSLPSGTGVEIVTYSKLLAQGRSSPQPFR-----PPKPEDVATICYTS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 289 GTTGDPKGVMHTHRTL---AAGlhtleprvVDLLGQPHSDDVYLSYLPMAHIMEFTITNLFIFRGAFIGF--GTPRTLTD 363
Cdd:PLN02736 231 GTTGTPKGVVLTHGNLianVAG--------SSLSTKFYPSDVHISYLPLAHIYERVNQIVMLHYGVAVGFyqGDNLKLMD 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 364 ttarphgDLLTFNPSMLAGVPRIFDTLKKAVEAKLPPVGTLKRQVFDHAYQSRLAALKKGKD-TPYWNEKVFAAPRAVLG 442
Cdd:PLN02736 303 -------DLAALRPTIFCSVPRLYNRIYDGITNAVKESGGLKERLFNAAYNAKKQALENGKNpSPMWDRLVFNKIKAKLG 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 443 NRLRIMLSGGGPLSAATHEFVNVVFGRVVI-GYGLTETICVGAIQIPGDTETNVTGLMEPGQEIKLLDIDEYKHT--DTP 519
Cdd:PLN02736 376 GRVRFMSSGASPLSPDVMEFLRICFGGRVLeGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNYTseDQP 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 520 EPRGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKALAKNCLGEYIALEALEAVYSGNEL 599
Cdd:PLN02736 456 YPRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKF 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 600 LqpnGVCvLVHPD--KPYITALALTDEARATSFAAKHGIE-GTYPALLKDQRFQQAAAISMADTARASNRASFECVKRVR 676
Cdd:PLN02736 536 V---AQC-FVYGDslNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRAAVLADMDAVGREAQLRGFEFAKAVT 611
|
570 580 590
....*....|....*....|....*....|....*..
gi 398009334 677 VIDDEWTPENEILTAAQKLKRRVIDAQYAQTIAELFT 713
Cdd:PLN02736 612 LVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYA 648
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
129-578 |
1.58e-98 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 310.01 E-value: 1.58e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 129 FDEVVYVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQ 208
Cdd:pfam00501 16 VGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 209 AILCGSANVA-NVLKLMKNGVMPQVPIIYVGTLPASLDthgvqvvsfkqvEMIGAAHLEGGAAKGTGPLNDDDLALIMYT 287
Cdd:pfam00501 96 VLITDDALKLeELLEALGKLEVVKLVLVLDRDPVLKEE------------PLPEEAKPADVPPPPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 288 SGTTGDPKGVMHTHRTLAAGLHTLEpRVVDLLGQPHSDDVYLSYLPMAHIMEFT-ITNLFIFRGAFIGFGTPRTLTDtTA 366
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNLVANVLSIK-RVRPRGFGLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATVVLPPGFPALD-PA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 367 RPHGDLLTFNPSMLAGVPRIFDTLKKAveaklppvGTLKRQVFDHayqsrlaalkkgkdtpywnekvfaapravlgnrLR 446
Cdd:pfam00501 242 ALLELIERYKVTVLYGVPTLLNMLLEA--------GAPKRALLSS---------------------------------LR 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 447 IMLSGGGPLSAATHEFVNVVFGRVVI-GYGLTETICVGAIQIPGDTETNV---TGLMEPGQEIKLLDID--EYKHTDTPe 520
Cdd:pfam00501 281 LVLSGGAPLPPELARRFRELFGGALVnGYGLTETTGVVTTPLPLDEDLRSlgsVGRPLPGTEVKIVDDEtgEPVPPGEP- 359
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 398009334 521 prGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKALAK 578
Cdd:pfam00501 360 --GELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIK 415
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
135-700 |
2.07e-95 |
|
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: 302.98 E-value: 2.07e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGS 214
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 AnvanvlklmkngvmpqvpiiyvgtlpasldthgvqvvsfkqvemigaahleggaakgtgplndDDLALIMYTSGTTGDP 294
Cdd:cd05907 86 P---------------------------------------------------------------DDLATIIYTSGTTGRP 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 295 KGVMHTHRTLAAGLHTLEPRVvdllgQPHSDDVYLSYLPMAHIMEFTITNLFIFR-GAFIGFGTP-RTLTDttarphgDL 372
Cdd:cd05907 103 KGVMLSHRNILSNALALAERL-----PATEGDRHLSFLPLAHVFERRAGLYVPLLaGARIYFASSaETLLD-------DL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 373 LTFNPSMLAGVPRIFDTLKKAVEAKLppVGTLKRQVFDhayqsrlaalkkgkdtpywnekvfaapRAVLGnRLRIMLSGG 452
Cdd:cd05907 171 SEVRPTVFLAVPRVWEKVYAAIKVKA--VPGLKRKLFD---------------------------LAVGG-RLRFAASGG 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 453 GPLSAATHEFVNVVFGRVVIGYGLTETICVGAIQIPGDTETNVTGLMEPGQEIKLLDideykhtdtpepRGEMLSRGPYL 532
Cdd:cd05907 221 APLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD------------DGEILVRGPNV 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 533 FKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKALAKNCLGEYIALEALEAVYSGNELLqpnGVCVLVHPD 612
Cdd:cd05907 289 MLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLI---SQAVVIGDG 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 613 KPYITALALTDEARATSFAAKHGIEGTYPALLKDQRFQQAAAISMADTARAsNRASFECVKRVRVIDDEWTPENEILTAA 692
Cdd:cd05907 366 RPFLVALIVPDPEALEAWAEEHGIAYTDVAELAANPAVRAEIEAAVEAANA-RLSRYEQIKKFLLLPEPFTIENGELTPT 444
|
....*...
gi 398009334 693 QKLKRRVI 700
Cdd:cd05907 445 LKLKRPVI 452
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
133-712 |
1.37e-85 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 283.24 E-value: 1.37e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 133 VYVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILC 212
Cdd:PLN02430 75 MWKTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFV 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 213 GSANVANVLKlMKNGVMPQVPIIYVGTLPASLDTHGVQVVSFKQVEMIGAAHLEGGAAKGTGPLNDDDLALIMYTSGTTG 292
Cdd:PLN02430 155 QDKKIKELLE-PDCKSAKRLKAIVSFTSVTEEESDKASQIGVKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 293 DPKGVMHTHRTLAAGLhtlepRVVDLLGQPHSD-----DVYLSYLPMAHIMEFTITNLFIFRGAFIGF--GTPRTLTDtt 365
Cdd:PLN02430 234 DPKGVVLTHEAVATFV-----RGVDLFMEQFEDkmthdDVYLSFLPLAHILDRMIEEYFFRKGASVGYyhGDLNALRD-- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 366 arphgDLLTFNPSMLAGVPRIFDTLKKAVEAKLPPVGTLKRQVFDHAYQSRLAALKKG----KDTPYWNEKVFAAPRAVL 441
Cdd:PLN02430 307 -----DLMELKPTLLAGVPRVFERIHEGIQKALQELNPRRRLIFNALYKYKLAWMNRGyshkKASPMADFLAFRKVKAKL 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 442 GNRLRIMLSGGGPLSAATHEFVNVVFGRVVI-GYGLTETICVGAIQIPGD-TETNVTGLMEPGQEIKLLDIDE--YKHTD 517
Cdd:PLN02430 382 GGRLRLLISGGAPLSTEIEEFLRVTSCAFVVqGYGLTETLGPTTLGFPDEmCMLGTVGAPAVYNELRLEEVPEmgYDPLG 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 518 TPePRGEMLSRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGRVKALAKNCLGEYIALEALEAVYSGN 597
Cdd:PLN02430 462 EP-PRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQN 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 598 ELLQPngvcVLVHPD--KPYITALALTDEARATSFAAKHGIEGTYPALLKDQRFQQAAAISMADTARASNRASFECVKRV 675
Cdd:PLN02430 540 PIVED----IWVYGDsfKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKEHILSELKSTAEKNKLRGFEYIKGV 615
|
570 580 590
....*....|....*....|....*....|....*..
gi 398009334 676 RVIDDEWTPENEILTAAQKLKRRVIDAQYAQTIAELF 712
Cdd:PLN02430 616 ILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMY 652
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
121-714 |
3.10e-81 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 271.72 E-value: 3.10e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 121 ERLMSITHFDEVVYVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAH 200
Cdd:PLN02861 64 RRQVTDSKVGPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 201 ALHETESQAILCGSANVANVLKLMKNGVMPQVPIIYVGTLPASL----DTHGVQVVSFKQVEMIGAAHLEggaakgTGPL 276
Cdd:PLN02861 144 IINHAEVSIAFVQESKISSILSCLPKCSSNLKTIVSFGDVSSEQkeeaEELGVSCFSWEEFSLMGSLDCE------LPPK 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 277 NDDDLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLE------PRVVDllgqphSDDVYLSYLPMAHIMEFTITNLFIFRG 350
Cdd:PLN02861 218 QKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDhllkvtDRVAT------EEDSYFSYLPLAHVYDQVIETYCISKG 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 351 AFIGF--GTPRTLTDttarphgDLLTFNPSMLAGVPRIFDTLKKAVEAKLPPVGTLKRQVFDHAYQSRLAALKKG----K 424
Cdd:PLN02861 292 ASIGFwqGDIRYLME-------DVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDFAYNYKLGNLRKGlkqeE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 425 DTPYWNEKVFAAPRAVLGNRLRIMLSGGGPLSAATHEFVNVVFGRVVI-GYGLTETiCVGAIQIPGDTETNV--TGLMEP 501
Cdd:PLN02861 365 ASPRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSqGYGLTES-CGGCFTSIANVFSMVgtVGVPMT 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 502 GQEIKLLDIDEYKHTDTPE-PRGEMLSRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGRVKALAKNC 580
Cdd:PLN02861 444 TIEARLESVPEMGYDALSDvPRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLS 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 581 LGEYIALEALEAVYSGNELLqpNGVCVLVHPDKPYITALALTDEARATSFAAKHGIEGTYPALLKDQRFQQAAAISMADT 660
Cdd:PLN02861 523 QGEYVAVENLENTYSRCPLI--ASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNST 600
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 398009334 661 ARASNRASFECVKRVRVIDDEWTPENEILTAAQKLKRRVIDAQYAQTIAELFTD 714
Cdd:PLN02861 601 GKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYSE 654
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
133-712 |
3.60e-78 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 263.80 E-value: 3.60e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 133 VYVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILC 212
Cdd:PLN02614 78 VWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 213 GSANVANVLKLMKNGVMPQVPIIYVGTLP----ASLDTHGVQVVSFKQVEMIGAAHLEGGAAKgtgplNDDDLALIMYTS 288
Cdd:PLN02614 158 EEKKISELFKTCPNSTEYMKTVVSFGGVSreqkEEAETFGLVIYAWDEFLKLGEGKQYDLPIK-----KKSDICTIMYTS 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 289 GTTGDPKGVMHTHRTLAaglhTLEPRVVDLLGQPHS----DDVYLSYLPMAHIMEFTITNLFIFRGAFIGF--GTPRTLT 362
Cdd:PLN02614 233 GTTGDPKGVMISNESIV----TLIAGVIRLLKSANAaltvKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFwrGDVKLLI 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 363 DttarphgDLLTFNPSMLAGVPRIFDTLKKAVEAKLPPVGTLKRQVFDHAYQSRLAALKKGKD----TPYWNEKVFAAPR 438
Cdd:PLN02614 309 E-------DLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAFSYKFGNMKKGQShveaSPLCDKLVFNKVK 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 439 AVLGNRLRIMLSGGGPLSAATHEFVNVVFG-RVVIGYGLTETiCVGA-IQIPGDTET-NVTGLMEPGQEIKLLDIDEYKH 515
Cdd:PLN02614 382 QGLGGNVRIILSGAAPLASHVESFLRVVACcHVLQGYGLTES-CAGTfVSLPDELDMlGTVGPPVPNVDIRLESVPEMEY 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 516 TD-TPEPRGEMLSRGPYLFKGYYKQPELTREVLDeDGWFHTGDVGSFTADGKMRIVGRVKALAKNCLGEYIALEALEAVY 594
Cdd:PLN02614 461 DAlASTPRGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIY 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 595 SGNELLQpnGVCVLVHPDKPYITALALTDEARATSFAAKHGIEGTYPALLKDQRFQQAAAISMADTARASNRASFECVKR 674
Cdd:PLN02614 540 GEVQAVD--SVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEKKMKGFEIIKA 617
|
570 580 590
....*....|....*....|....*....|....*...
gi 398009334 675 VRVIDDEWTPENEILTAAQKLKRRVIDAQYAQTIAELF 712
Cdd:PLN02614 618 IHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMY 655
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
135-700 |
4.38e-69 |
|
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: 233.79 E-value: 4.38e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILcgs 214
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 anvanvlklmkngvmpqvpiiyvgtlpasLDTHGvqvvsfkqvemigaahleggaakgtgplndDDLALIMYTSGTTGDP 294
Cdd:cd17640 83 -----------------------------VENDS------------------------------DDLATIIYTSGTTGNP 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 295 KGVMHTHRTLAAGLHTLEPRVvdllgQPHSDDVYLSYLPMAHIMEFTITNLFIFRGAFIGFGTPRTLTDttarphgDLLT 374
Cdd:cd17640 104 KGVMLTHANLLHQIRSLSDIV-----PPQPGDRFLSILPIWHSYERSAEYFIFACGCSQAYTSIRTLKD-------DLKR 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 375 FNPSMLAGVPRIFDTLKKAVEaklppvgtlkrqvfdhayqsrlaalKKGKDTPYWNEKVFAAprAVLGNRLRIMLSGGGP 454
Cdd:cd17640 172 VKPHYIVSVPRLWESLYSGIQ-------------------------KQVSKSSPIKQFLFLF--FLSGGIFKFGISGGGA 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 455 LSAATHEFVNVVFGRVVIGYGLTETICVGAIQIPGDTETNVTGLMEPGQEIKLLDIDEYKHTdTPEPRGEMLSRGPYLFK 534
Cdd:cd17640 225 LPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVL-PPGEKGIVWVRGPQVMK 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 535 GYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRvkalAKNCL----GEYIALEALEAVYSGNELLQPngvCVLVH 610
Cdd:cd17640 304 GYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGR----AKDTIvlsnGENVEPQPIEEALMRSPFIEQ---IMVVG 376
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 611 PDKPYITALALTDEARATSFAAKHGIEGTYPALLKDQRFQQAAAISMADTARASNRA---SFECVKRVRVIDDEWTpENE 687
Cdd:cd17640 377 QDQKRLGALIVPNFEELEKWAKESGVKLANDRSQLLASKKVLKLYKNEIKDEISNRPgfkSFEQIAPFALLEEPFI-ENG 455
|
570
....*....|...
gi 398009334 688 ILTAAQKLKRRVI 700
Cdd:cd17640 456 EMTQTMKIKRNVV 468
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
131-704 |
2.44e-67 |
|
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: 230.43 E-value: 2.44e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 131 EVVYVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAI 210
Cdd:cd05932 3 QVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 211 LCGsanvanvlKL-----MKNGVmPQVPIIYVGTLPASLDTHgvqvvsfKQVEMIGAAHlegGAAKGTGPLNDDDLALIM 285
Cdd:cd05932 83 FVG--------KLddwkaMAPGV-PEGLISISLPPPSAANCQ-------YQWDDLIAQH---PPLEERPTRFPEQLATLI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 286 YTSGTTGDPKGVMHTHRTLAAGLHtlepRVVDLLGQpHSDDVYLSYLPMAHIMEftitNLFIFRGAFIGfGTPRTLTDTT 365
Cdd:cd05932 144 YTSGTTGQPKGVMLTFGSFAWAAQ----AGIEHIGT-EENDRMLSYLPLAHVTE----RVFVEGGSLYG-GVLVAFAESL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 366 ARPHGDLLTFNPSMLAGVPRIFDTLKKAVEAKLPPvgtlkrqvfdhayqSRLAALKKgkdTPYWNEKVFAAPRAVLG-NR 444
Cdd:cd05932 214 DTFVEDVQRARPTLFFSVPRLWTKFQQGVQDKIPQ--------------QKLNLLLK---IPVVNSLVKRKVLKGLGlDQ 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 445 LRIMLSGGGPLSAATHEFVNVVFGRVVIGYGLTETICVGAIQIPGDTETNVTGLMEPGQEIKLldideykhtdtpEPRGE 524
Cdd:cd05932 277 CRLAGCGSAPVPPALLEWYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRI------------SEDGE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 525 MLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKALAKNCLGEYIA----------LEALEAV- 593
Cdd:cd05932 345 ILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVApapienklaeHDRVEMVc 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 594 YSGNELLQPNGVCVlvhpdkpyitalaLTDEARATSFAAKHG-IEGTYPALLKDQRfqqaaaismadtaraSNRASFECV 672
Cdd:cd05932 425 VIGSGLPAPLALVV-------------LSEEARLRADAFARAeLEASLRAHLARVN---------------STLDSHEQL 476
|
570 580 590
....*....|....*....|....*....|..
gi 398009334 673 KRVRVIDDEWTPENEILTAAQKLKRRVIDAQY 704
Cdd:cd05932 477 AGIVVVKDPWSIDNGILTPTLKIKRNVLEKAY 508
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
130-593 |
6.54e-57 |
|
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: 201.29 E-value: 6.54e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 130 DEVVYVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQA 209
Cdd:cd05911 6 DTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 210 ILCGSANVANVLKLMKNgVMPQVPIIyvgTLPASLDTHGvqvvsfkQVEMIGAAHLEGGAAKGTGPLND--DDLALIMYT 287
Cdd:cd05911 86 IFTDPDGLEKVKEAAKE-LGPKDKII---VLDDKPDGVL-------SIEDLLSPTLGEEDEDLPPPLKDgkDDTAAILYS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 288 SGTTGDPKGVMHTHRTLAAGL-HTLEPrvvdLLGQPHSDDVYLSYLPMAHIMEFTITNLFIFRGAfigfgtPRTLTdtta 366
Cdd:cd05911 155 SGTTGLPKGVCLSHRNLIANLsQVQTF----LYGNDGSNDVILGFLPLYHIYGLFTTLASLLNGA------TVIIM---- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 367 rPHGDLLTF-------NPSMLAGVPRIFDTLkkaveAKLPpvgtlkrqvfdhayqsrlaalkkgkdtpywnekvfAAPRA 439
Cdd:cd05911 221 -PKFDSELFldliekyKITFLYLVPPIAAAL-----AKSP-----------------------------------LLDKY 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 440 VLGNrLRIMLSGGGPLSAATHEFVNVVFGRVVI--GYGLTETICVGAIQIPGDTETNVTGLMEPGQEIKLLDIDEyKHTD 517
Cdd:cd05911 260 DLSS-LRVILSGGAPLSKELQELLAKRFPNATIkqGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDG-KDSL 337
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398009334 518 TPEPRGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKALAKnCLGEYIALEALEAV 593
Cdd:cd05911 338 GPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIK-YKGFQVAPAELEAV 412
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
135-704 |
1.24e-55 |
|
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: 199.96 E-value: 1.24e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGS 214
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAED 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 ANvaNVLKLMKngVMPQVP----IIYVGtlPASLDTHG-VQVVSFKQVEMIGAAH-------LEGGAAKGTGplndDDLA 282
Cdd:cd17641 92 EE--QVDKLLE--IADRIPsvryVIYCD--PRGMRKYDdPRLISFEDVVALGRALdrrdpglYEREVAAGKG----EDVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 283 LIMYTSGTTGDPKGVMHTHRTLA---AGLHTLEPRvvdllgqpHSDDVYLSYLPMAHIMEFTITnlfIFRGAFIGFGTPR 359
Cdd:cd17641 162 VLCTTSGTTGKPKLAMLSHGNFLghcAAYLAADPL--------GPGDEYVSVLPLPWIGEQMYS---VGQALVCGFIVNF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 360 TLTDTTARPhgDLLTFNPSMLAGVPRIFDTLKKAVEAKLPPVGTLKRQVFDHAYQSRLAAL---KKGKDTPYWNEK---- 432
Cdd:cd17641 231 PEEPETMME--DLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKLGLRALdrgKRGRPVSLWLRLaswl 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 433 ----VFAAPRAVLG-NRLRIMLSGGGPLSAATHEF-----VNVvfgRVVigYGLTETICVGAIQIPGDTETNVTGLMEPG 502
Cdd:cd17641 309 adalLFRPLRDRLGfSRLRSAATGGAALGPDTFRFfhaigVPL---KQL--YGQTELAGAYTVHRDGDVDPDTVGVPFPG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 503 QEIKlldIDEykhtdtpepRGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKALAKNCLG 582
Cdd:cd17641 384 TEVR---IDE---------VGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDG 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 583 E---------------YIAlealEAVYSGNellqpngvcvlvhpDKPYITALALTDEARATSFAAKHGIE-GTYPALlkD 646
Cdd:cd17641 452 TrfspqfienklkfspYIA----EAVVLGA--------------GRPYLTAFICIDYAIVGKWAEQRGIAfTTYTDL--A 511
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398009334 647 QRFQQAAAI---------SMADTARasnrasfecVKRVRVIDDEWTPENEILTAAQKLKRRVIDAQY 704
Cdd:cd17641 512 SRPEVYELIrkevekvnaSLPEAQR---------IRRFLLLYKELDADDGELTRTRKVRRGVIAEKY 569
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
135-593 |
2.35e-53 |
|
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: 190.79 E-value: 2.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCgs 214
Cdd:COG0318 25 LTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 anvanvlklmkngvmpqvpiiyvgtlpasldthgvqvvsfkqvemigaahleggaakgtgplndddlALIMYTSGTTGDP 294
Cdd:COG0318 103 -------------------------------------------------------------------ALILYTSGTTGRP 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 295 KGVMHTHRTLAAGLHTleprVVDLLGqPHSDDVYLSYLPMAHIMEFTI-TNLFIFRGA---FIGFGTPRTLTDTTARphg 370
Cdd:COG0318 116 KGVMLTHRNLLANAAA----IAAALG-LTPGDVVLVALPLFHVFGLTVgLLAPLLAGAtlvLLPRFDPERVLELIER--- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 371 dlltFNPSMLAGVPRIFDTLKKAVEAKlppvgtlkrqvfdhayqsrlaalkkGKDTPywnekvfaapravlgnRLRIMLS 450
Cdd:COG0318 188 ----ERVTVLFGVPTMLARLLRHPEFA-------------------------RYDLS----------------SLRLVVS 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 451 GGGPLSAATHEFVNVVFG-RVVIGYGLTETICVGAIQIPGDTETNVT--GLMEPGQEIKLLDIDeykhtDTPEPR---GE 524
Cdd:COG0318 223 GGAPLPPELLERFEERFGvRIVEGYGLTETSPVVTVNPEDPGERRPGsvGRPLPGVEVRIVDED-----GRELPPgevGE 297
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398009334 525 MLSRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGRVKALAKnCLGEYIALEALEAV 593
Cdd:COG0318 298 IVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMII-SGGENVYPAEVEEV 364
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
135-592 |
8.15e-53 |
|
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: 189.58 E-value: 8.15e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGs 214
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 anvanvlklmkngvmpqvpiiyvgtlpasldthgvqvvsfkqvemigaahleggaakgtgplNDDDLALIMYTSGTTGDP 294
Cdd:cd05914 87 --------------------------------------------------------------DEDDVALINYTSGTTGNS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 295 KGVMHTHRTLAAGLHTLepRVVDLLGQphsDDVYLSYLPMAHIMEFTITNLFIFRgafigFGTPRTLTDTTARPHGDLLT 374
Cdd:cd05914 105 KGVMLTYRNIVSNVDGV--KEVVLLGK---GDKILSILPLHHIYPLTFTLLLPLL-----NGAHVVFLDKIPSAKIIALA 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 375 FNP-SMLAGVPRIFDTLKKAVEAKLPPVgTLKRQVFdhayqsRLAalKKGKDTPYWNEkVFAAPRAVLGNRLRIMLSGGG 453
Cdd:cd05914 175 FAQvTPTLGVPVPLVIEKIFKMDIIPKL-TLKKFKF------KLA--KKINNRKIRKL-AFKKVHEAFGGNIKEFVIGGA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 454 PLSAATHEFVNVVFGRVVIGYGLTETICVGAIQIPGDTETNVTGLMEPGQEIKLLDIDEYKHTdtpeprGEMLSRGPYLF 533
Cdd:cd05914 245 KINPDVEEFLRTIGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDPATGE------GEIIVRGPNVM 318
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 398009334 534 KGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKALAKNCLGEYIALEALEA 592
Cdd:cd05914 319 KGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEA 377
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
136-574 |
1.34e-50 |
|
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: 183.53 E-value: 1.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 136 TYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCgsa 215
Cdd:cd05936 26 TYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIV--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 216 nvanvlklmkngvmpqvpiiyvgtlpasldthgvqVVSFKQVemigaahLEGGAAKGTGP-LNDDDLALIMYTSGTTGDP 294
Cdd:cd05936 103 -----------------------------------AVSFTDL-------LAAGAPLGERVaLTPEDVAVLQYTSGTTGVP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 295 KGVMHTHRTLAAGLHTLEPRVVDLLgqpHSDDVYLSYLPMAHIMEFTIT-NLFIFRGAFIgfgtprtLTDTTARPHG--- 370
Cdd:cd05936 141 KGAMLTHRNLVANALQIKAWLEDLL---EGDDVVLAALPLFHVFGLTVAlLLPLALGATI-------VLIPRFRPIGvlk 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 371 DLLTFNPSMLAGVPRIFDTLKKAVEaklppvgtlkrqvfdhayqsrlaalKKGKDTpywnekvfaapravlgNRLRIMLS 450
Cdd:cd05936 211 EIRKHRVTIFPGVPTMYIALLNAPE-------------------------FKKRDF----------------SSLRLCIS 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 451 GGGPLSAATHEFVNVVFG-RVVIGYGLTETICVGAIQIPGDTETNVT-GLMEPGQEIKLLDIDeykhtDTPEPR---GEM 525
Cdd:cd05936 250 GGAPLPVEVAERFEELTGvPIVEGYGLTETSPVVAVNPLDGPRKPGSiGIPLPGTEVKIVDDD-----GEELPPgevGEL 324
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 398009334 526 LSRGPYLFKGYYKQPELTREVLDeDGWFHTGDVGSFTADGKMRIVGRVK 574
Cdd:cd05936 325 WVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKK 372
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
126-574 |
3.42e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 178.07 E-value: 3.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 126 ITHFDEVVYvTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHET 205
Cdd:PRK06187 24 AVYFDGRRT-TYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 206 ESQAILCGSANVANVLKLmkNGVMPQVPIIYVGTlPASLDTHGVQVVSFkqVEMIGAAHLEGGAAkgtgPLNDDDLALIM 285
Cdd:PRK06187 103 EDRVVLVDSEFVPLLAAI--LPQLPTVRTVIVEG-DGPAAPLAPEVGEY--EELLAAASDTFDFP----DIDENDAAAML 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 286 YTSGTTGDPKGVMHTHRTLAagLHTLeprVVDLLGQPHSDDVYLSYLPMAHIMEFTITNLFIFRGA-------FIgfgtP 358
Cdd:PRK06187 174 YTSGTTGHPKGVVLSHRNLF--LHSL---AVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLALMAGAkqviprrFD----P 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 359 RTLTDTTarphgdlLTFNPSMLAGVPRIfdtlkkaveaklppvgtlkrqvfdhaYQSRLAALKkgkdtpywnekvfAAPR 438
Cdd:PRK06187 245 ENLLDLI-------ETERVTFFFAVPTI--------------------------WQMLLKAPR-------------AYFV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 439 AVlgNRLRIMLSGGGPLSAAT-HEFVNVVFGRVVIGYGLTETICVGAIQIPGDTETNV------TGLMEPGQEIKLLDID 511
Cdd:PRK06187 279 DF--SSLRLVIYGGAALPPALlREFKEKFGIDLVQGYGMTETSPVVSVLPPEDQLPGQwtkrrsAGRPLPGVEARIVDDD 356
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398009334 512 EykhtdTPEPR-----GEMLSRGPYLFKGYYKQPELTREVLDeDGWFHTGDVGSFTADGKMRIVGRVK 574
Cdd:PRK06187 357 G-----DELPPdggevGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIK 418
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
135-593 |
1.41e-44 |
|
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: 167.41 E-value: 1.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGS 214
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 ANVANVLKLmkngvmpQVPIIYVGTLPASLDTHGVqvvsfkqvemigAAHLEGGAAKGTGPLNDDDLALIMYTSGTTGDP 294
Cdd:cd05904 113 ELAEKLASL-------ALPVVLLDSAEFDSLSFSD------------LLFEADEAEPPVVVIKQDDVAALLYSSGTTGRS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 295 KGVMHTHRTLAAGLHTLEPRVVdllGQPHSDDVYLSYLPMAHIMEFT-ITNLFIFRGAFIgfgtprtltdtTARPHGDLl 373
Cdd:cd05904 174 KGVMLTHRNLIAMVAQFVAGEG---SNSDSEDVFLCVLPMFHIYGLSsFALGLLRLGATV-----------VVMPRFDL- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 374 tfnPSMLAGVPRIFDTLKKAVeaklPPVgtlkrqvfdhayqsrLAALKKgkdtpywNEKVFAAPRAvlgnRLRIMLSGGG 453
Cdd:cd05904 239 ---EELLAAIERYKVTHLPVV----PPI---------------VLALVK-------SPIVDKYDLS----SLRQIMSGAA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 454 PLSAATHEFVNVVFGRVVI--GYGLTETICVGAIqIPGDTETNV----TGLMEPGQEIKLLDIDeykhTDTPEP---RGE 524
Cdd:cd05904 286 PLGKELIEAFRAKFPNVDLgqGYGMTESTGVVAM-CFAPEKDRAkygsVGRLVPNVEAKIVDPE----TGESLPpnqTGE 360
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398009334 525 MLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKALAKnCLGEYIALEALEAV 593
Cdd:cd05904 361 LWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIK-YKGFQVAPAELEAL 428
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
280-613 |
2.18e-44 |
|
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: 162.45 E-value: 2.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 280 DLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLEPRvvdllGQPHSDDVYLSYLPMAHIMEFTITNLFIFRGA---FIGFG 356
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS-----GGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGtvvLLPKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 357 TPRTLTDTTARPHgdlltfnPSMLAGVPRIFDTLkkaveaklppvgtlkrqvfdhayqsRLAALKKGKDTPywnekvfaa 436
Cdd:cd04433 76 DPEAALELIEREK-------VTILLGVPTLLARL-------------------------LKAPESAGYDLS--------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 437 pravlgnRLRIMLSGGGPLSAATHEFVNVVFG-RVVIGYGLTETiCVGAIQIPGDTETNV---TGLMEPGQEIKLLDIDE 512
Cdd:cd04433 115 -------SLRALVSGGAPLPPELLERFEEAPGiKLVNGYGLTET-GGTVATGPPDDDARKpgsVGRPVPGVEVRIVDPDG 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 513 ykHTDTPEPRGEMLSRGPYLFKGYYKQPELTREVlDEDGWFHTGDVGSFTADGKMRIVGRVKALAKnCLGEYIALEALEA 592
Cdd:cd04433 187 --GELPPGEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEA 262
|
330 340
....*....|....*....|....
gi 398009334 593 VysgneLLQPNGV---CVLVHPDK 613
Cdd:cd04433 263 V-----LLGHPGVaeaAVVGVPDP 281
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
78-691 |
1.23e-43 |
|
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: 166.09 E-value: 1.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 78 TTLMRHCAERTdqrVLGYRPVKCVTKEPAPSTSrgstsepakkerLMSITHFDEVvyvTYSEMEERIFHFGAGLAALGVT 157
Cdd:cd17632 29 ATVMTGYADRP---ALGQRATELVTDPATGRTT------------LRLLPRFETI---TYAELWERVGAVAAAHDPEQPV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 158 ANGN-VSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGSANVANVLKLMKNGvmPQVPIIY 236
Cdd:cd17632 91 RPGDfVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAEHLDLAVEAVLEG--GTPPRLV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 237 VGTLPASLDTHGVQVVS--------FKQVEMIGAAHLEGGAAKGTGPL----NDDDLALIMYTSGTTGDPKGVMHTHRTL 304
Cdd:cd17632 169 VFDHRPEVDAHRAALESarerlaavGIPVTTLTLIAVRGRDLPPAPLFrpepDDDPLALLIYTSGSTGTPKGAMYTERLV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 305 AAGLHTLEPRVVDLlgQPHSddVYLSYLPMAHIMEFTITNLFIFRGA---FIGFGTPRTLTDttarphgDLLTFNPSMLA 381
Cdd:cd17632 249 ATFWLKVSSIQDIR--PPAS--ITLNFMPMSHIAGRISLYGTLARGGtayFAAASDMSTLFD-------DLALVRPTELF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 382 GVPRIFDTlkkaveaklppvgtlkrqVFDHaYQSRLAA-LKKGKDTPYWNEKVFAAPRA-VLGNRLRIMLSGGGPLSAAT 459
Cdd:cd17632 318 LVPRVCDM------------------LFQR-YQAELDRrSVAGADAETLAERVKAELRErVLGGRLLAAVCGSAPLSAEM 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 460 HEFVNVVFG-RVVIGYGLTETICV---GAIQIPgdtetnvtglmePGQEIKLLDIDE--YKHTDTPEPRGEMLSRGPYLF 533
Cdd:cd17632 379 KAFMESLLDlDLHDGYGSTEAGAVildGVIVRP------------PVLDYKLVDVPElgYFRTDRPHPRGELLVKTDTLF 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 534 KGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKALAKNCLGEYIALEALEAVYSGNELLQPngvcVLVH--P 611
Cdd:cd17632 447 PGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQ----IFVYgnS 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 612 DKPYITALAL-TDEARATsfaakhgiegtypalLKDQRFQQAAAISMADTARASNRASFECVKRVRVIDDEWTPENEILT 690
Cdd:cd17632 523 ERAYLLAVVVpTQDALAG---------------EDTARLRAALAESLQRIAREAGLQSYEIPRDFLIETEPFTIANGLLS 587
|
.
gi 398009334 691 A 691
Cdd:cd17632 588 G 588
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
130-574 |
6.67e-43 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 162.77 E-value: 6.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 130 DEVVYVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQA 209
Cdd:PRK07656 26 FGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 210 ILCgSANVANVLKLMKNGVmPQVPIIYVGTLPASlDTHGVQVVSFKQVemigaahLEGGAAKGTGP-LNDDDLALIMYTS 288
Cdd:PRK07656 106 LFV-LGLFLGVDYSATTRL-PALEHVVICETEED-DPHTEKMKTFTDF-------LAAGDPAERAPeVDPDDVADILFTS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 289 GTTGDPKGVMHTHRTLAAGLHTleprVVDLLGQpHSDDVYLSYLPMAHIMEFTIT-NLFIFRGAfigfgtprtltdtTAR 367
Cdd:PRK07656 176 GTTGRPKGAMLTHRQLLSNAAD----WAEYLGL-TEGDRYLAANPFFHVFGYKAGvNAPLMRGA-------------TIL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 368 PHgdlLTFNPSmlagvpRIFDTLKKAVEAKLPPVGTLkrqvfdhaYQSRLAALKKGKDTpywnekvFAApravlgnrLRI 447
Cdd:PRK07656 238 PL---PVFDPD------EVFRLIETERITVLPGPPTM--------YNSLLQHPDRSAED-------LSS--------LRL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 448 MLSGGGPLSAATHEFVNVVFG--RVVIGYGLTETICVGAIQIPGDTETNV---TGLMEPGQEIKLldIDEYKHTDTPEPR 522
Cdd:PRK07656 286 AVTGAASMPVALLERFESELGvdIVLTGYGLSEASGVTTFNRLDDDRKTVagtIGTAIAGVENKI--VNELGEEVPVGEV 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 398009334 523 GEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVK 574
Cdd:PRK07656 364 GELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKK 415
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
135-712 |
8.72e-40 |
|
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: 155.21 E-value: 8.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILcgs 214
Cdd:cd05933 9 LTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILV--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 anVANVLKLMK-NGVMPQVP-----IIYVGTLPASLDthgvQVVSFKQVEMIGAAHLEGGAAKGTGPLNDDDLALIMYTS 288
Cdd:cd05933 86 --VENQKQLQKiLQIQDKLPhlkaiIQYKEPLKEKEP----NLYSWDEFMELGRSIPDEQLDAIISSQKPNQCCTLIYTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 289 GTTGDPKGVMHTHRTL-----AAGLHtleprvVDLLGQPHSDDVYLSYLPMAHIMEfTITNLF--IFRGAFIGFGTPRTL 361
Cdd:cd05933 160 GTTGMPKGVMLSHDNItwtakAASQH------MDLRPATVGQESVVSYLPLSHIAA-QILDIWlpIKVGGQVYFAQPDAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 362 TDTTARphgDLLTFNPSMLAGVPRIFDTLK---KAVEAKlppVGTLKRQVFDHA----YQSRLAALKKGKDTPYW----N 430
Cdd:cd05933 233 KGTLVK---TLREVRPTAFMGVPRVWEKIQekmKAVGAK---SGTLKRKIASWAkgvgLETNLKLMGGESPSPLFyrlaK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 431 EKVFAAPRAVLG-NRLRIMLSGGGPLSAATHEFVNVVFGRVVIGYGLTETICVGAIQIPGDTETNVTGLMEPGQEIKLLD 509
Cdd:cd05933 307 KLVFKKVRKALGlDRCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 510 IDEYKHtdtpeprGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKALAKNCLGEYIALEA 589
Cdd:cd05933 387 PDADGI-------GEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVP 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 590 LEavysgnELLQPNGVCV----LVHPDKPYITAL----------------ALTDEarATSFAAKHGIEGTYPALL---KD 646
Cdd:cd05933 460 IE------DAVKKELPIIsnamLIGDKRKFLSMLltlkcevnpetgepldELTEE--AIEFCRKLGSQATRVSEIaggKD 531
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398009334 647 QRFQQA--AAISMADTARASNRASfecVKRVRVIDDEWTPENEILTAAQKLKRRVIDAQYAQTIAELF 712
Cdd:cd05933 532 PKVYEAieEGIKRVNKKAISNAQK---IQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
133-578 |
5.90e-37 |
|
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: 145.75 E-value: 5.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 133 VYVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILC 212
Cdd:cd17642 43 VNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFC 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 213 GSANVANVLKLMKNGVMPQVPII------YVG-----TLPASLDTHGVQVVSFKQVEMIgaahleggaakgtgplNDDDL 281
Cdd:cd17642 123 SKKGLQKVLNVQKKLKIIKTIIIldskedYKGyqclyTFITQNLPPGFNEYDFKPPSFD----------------RDEQV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 282 ALIMYTSGTTGDPKGVMHTHRTLAAGL-HTLEPRVVDllgQPHSDDVYLSYLPMAHimeftitnlfifrgafiGFGTPRT 360
Cdd:cd17642 187 ALIMNSSGSTGLPKGVQLTHKNIVARFsHARDPIFGN---QIIPDTAILTVIPFHH-----------------GFGMFTT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 361 LTDTTarphgdlltfnpsmlagvprifdtlkkaVEAKLPPVGTLKRQVFdhayqsrLAALKKgkdtpYWNEKVFAAP--- 437
Cdd:cd17642 247 LGYLI----------------------------CGFRVVLMYKFEEELF-------LRSLQD-----YKVQSALLVPtlf 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 438 ----RAVLGNR-----LRIMLSGGGPLSAATHEFVNVVFGRVVI--GYGLTETICVGAIQIPGDTETNVTGLMEPGQEIK 506
Cdd:cd17642 287 affaKSTLVDKydlsnLHEIASGGAPLSKEVGEAVAKRFKLPGIrqGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAK 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398009334 507 LLDIDEYKhTDTPEPRGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKALAK 578
Cdd:cd17642 367 VVDLDTGK-TLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIK 437
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
136-576 |
1.01e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 145.53 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 136 TYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAatVYANlgeaALAHAlHETESQAILCGSA 215
Cdd:PRK05605 59 TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVV--VEHN----PLYTA-HELEHPFEDHGAR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 216 ------NVANVLKLMKNGVmpQVPIIYVGTLPASLDTHG-------VQVVSFKQVEMIGAA-------HLEGGAAKGTGP 275
Cdd:PRK05605 132 vaivwdKVAPTVERLRRTT--PLETIVSVNMIAAMPLLQrlalrlpIPALRKARAALTGPApgtvpweTLVDAAIGGDGS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 276 LND------DDLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLEPRVVDLLGQPhsdDVYLSYLPMAHIMEFTITNLFifr 349
Cdd:PRK05605 210 DVShprptpDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPGLGDGP---ERVLAALPMFHAYGLTLCLTL--- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 350 GAFIGfgtprtltdttarphGDLLTFnPSMlaGVPRIFDTLKKAVEAKLPPVGTLKRQVFDhayqsrlAALKKGKDTpyw 429
Cdd:PRK05605 284 AVSIG---------------GELVLL-PAP--DIDLILDAMKKHPPTWLPGVPPLYEKIAE-------AAEERGVDL--- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 430 nekvfaapravlgNRLRIMLSGGGPLSAAT-HEFVNVVFGRVVIGYGLTET--ICVGAiQIPGDTETNVTGLMEPGQEIK 506
Cdd:PRK05605 336 -------------SGVRNAFSGAMALPVSTvELWEKLTGGLLVEGYGLTETspIIVGN-PMSDDRRPGYVGVPFPDTEVR 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 507 LLDIDEYKHTDTPEPRGEMLSRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGRVKAL 576
Cdd:PRK05605 402 IVDPEDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKEL 470
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
130-574 |
2.21e-35 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 141.34 E-value: 2.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 130 DEVVYVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQA 209
Cdd:PRK13295 51 GAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 210 ILcgsanVANVLK-----LMKNGVMPQVP----IIYVGtlpasldthGVQVVSFKQVEMIGAAHLEGGAAKG-----TGP 275
Cdd:PRK13295 131 LV-----VPKTFRgfdhaAMARRLRPELPalrhVVVVG---------GDGADSFEALLITPAWEQEPDAPAIlarlrPGP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 276 lndDDLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLEPRVVdlLGqphSDDVYLSYLPMAHIMEFTItnlfifrGAF--I 353
Cdd:PRK13295 197 ---DDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLG--LG---ADDVILMASPMAHQTGFMY-------GLMmpV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 354 GFGTPRTLTDT--------TARPHGdlLTFnpsMLAGVPRIFDtLKKAVEAKLPPVGTLkrqvfdhayqsrlaalkkgkd 425
Cdd:PRK13295 262 MLGATAVLQDIwdparaaeLIRTEG--VTF---TMASTPFLTD-LTRAVKESGRPVSSL--------------------- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 426 tpywnekvfaapravlgnrlRIMLSGGGPLSAATHEFVNVVFG-RVVIGYGLTETICVGAIqIPGDTE---TNVTGLMEP 501
Cdd:PRK13295 315 --------------------RTFLCAGAPIPGALVERARAALGaKIVSAWGMTENGAVTLT-KLDDPDeraSTTDGCPLP 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398009334 502 GQEIKLLDIDeykhtDTPEPRGE---MLSRGPYLFKGYYKQPELTREvlDEDGWFHTGDVGSFTADGKMRIVGRVK 574
Cdd:PRK13295 374 GVEVRVVDAD-----GAPLPAGQigrLQVRGCSNFGGYLKRPQLNGT--DADGWFDTGDLARIDADGYIRISGRSK 442
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
277-595 |
4.84e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 142.16 E-value: 4.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 277 NDDD--LALIMYTSGTTGDPKGVMHTHRTLAAGLHTLEPRVVDLLGQPhsdDVYLSYLPMAHIMEFTITNLFIFRGafig 354
Cdd:PTZ00342 300 NEDPdfITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKHSIFKKYNP---KTHLSYLPISHIYERVIAYLSFMLG---- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 355 fGTPRTLTDTTARPHGDLLTFNPSMLAGVPRIFDTLKKAVEA---KLPPvgtLKRQVFDhayqsRLAALKKG-KDTPYWN 430
Cdd:PTZ00342 373 -GTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTeinNLPP---LKRFLVK-----KILSLRKSnNNGGFSK 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 431 --EKVFAAPRAVLGN---RLRIMLSGGGPLSAATHE----FVNVVFGRvviGYGLTETicVGAI--QIPGDTETN-VTGL 498
Cdd:PTZ00342 444 flEGITHISSKIKDKvnpNLEVILNGGGKLSPKIAEelsvLLNVNYYQ---GYGLTET--TGPIfvQHADDNNTEsIGGP 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 499 MEPGQEIKLLDIDEYKHTDTPePRGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKALAK 578
Cdd:PTZ00342 519 ISPNTKYKVRTWETYKATDTL-PKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVK 597
|
330
....*....|....*..
gi 398009334 579 NCLGEYIALEALEAVYS 595
Cdd:PTZ00342 598 LSQGEYIETDMLNNLYS 614
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
280-615 |
3.36e-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: 135.88 E-value: 3.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 280 DLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLeprvVDLLgQPHSDDVYLSYLPMAHIME-FTITNLFIFRGAFIGFgTP 358
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRAL----VDAW-RWTEDDVLLHVLPLHHVHGlVNALLCPLFAGASVEF-LP 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 359 RtltDTTARPHGDLLTFNPSMLAGVPRIFDTLKKAVEAKLPPVGTLkrqvfdhayqsrlaalkkgkdtpywnekvfaapR 438
Cdd:cd05941 164 K---FDPKEVAISRLMPSITVFMGVPTIYTRLLQYYEAHFTDPQFA---------------------------------R 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 439 AVLGNRLRIMLSGGGPLSAATHEFVNVVFGRVVIG-YGLTETicVGAIQIP--GDTETNVTGLMEPGQEIKLLDIDEYKH 515
Cdd:cd05941 208 AAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLErYGMTEI--GMALSNPldGERRPGTVGMPLPGVQARIVDEETGEP 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 516 TDTPEPrGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKALAKNCLGEYI-ALEaLEAVy 594
Cdd:cd05941 286 LPRGEV-GEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSGGYKVsALE-IERV- 362
|
330 340
....*....|....*....|....
gi 398009334 595 sgneLLQPNGV---CVLVHPDKPY 615
Cdd:cd05941 363 ----LLAHPGVsecAVIGVPDPDW 382
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
135-574 |
1.04e-33 |
|
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: 134.27 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILcgs 214
Cdd:cd17631 21 LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 anvanvlklmkngvmpqvpiiyvgtlpasldthgvqvvsfkqvemigaahleggaakgtgplndDDLALIMYTSGTTGDP 294
Cdd:cd17631 98 ----------------------------------------------------------------DDLALLMYTSGTTGRP 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 295 KGVMHTHRTLAAGLHTLeprVVDLlgQPHSDDVYLSYLPMAHIMEF-TITNLFIFRGAFI----GFgTPRTLTDTTARpH 369
Cdd:cd17631 114 KGAMLTHRNLLWNAVNA---LAAL--DLGPDDVLLVVAPLFHIGGLgVFTLPTLLRGGTVvilrKF-DPETVLDLIER-H 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 370 GDLLTFnpsmlaGVPRIFDTLKkaveaklppvgtlkrqvfdhayqsrlaalkkgkDTPYWNEKVFAapravlgnRLRIML 449
Cdd:cd17631 187 RVTSFF------LVPTMIQALL---------------------------------QHPRFATTDLS--------SLRAVI 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 450 SGGGPLSAATHEFVNVVFGRVVIGYGLTETICVGAIQIPGDTETNV--TGLMEPGQEIKLLDIDeykhtDTPEP---RGE 524
Cdd:cd17631 220 YGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSPEDHRRKLgsAGRPVFFVEVRIVDPD-----GREVPpgeVGE 294
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 398009334 525 MLSRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGRVK 574
Cdd:cd17631 295 IVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKK 343
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
135-612 |
4.72e-33 |
|
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: 132.50 E-value: 4.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILcgs 214
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 anvanvlklmkngvmpqVPIIYVGTLPASLDthgvqvvsfkqvemigaahleggaakgtgplndDDLALIMYTSGTTGDP 294
Cdd:cd05903 79 -----------------VPERFRQFDPAAMP---------------------------------DAVALLLFTSGTTGEP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 295 KGVMHTHRTLAAGLHTLEPRVvdLLGQPhsdDVYLSYLPMAHIMEFtitnLFIFRGAFIgFGTPRTLTDT--------TA 366
Cdd:cd05903 109 KGVMHSHNTLSASIRQYAERL--GLGPG---DVFLVASPMAHQTGF----VYGFTLPLL-LGAPVVLQDIwdpdkalaLM 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 367 RPHGdlLTFnpsMLAGVPRIFDTLKkaveaklppvgtlkrqvfdhayqsrlAALKKGKDTPywnekvfaapravlgnRLR 446
Cdd:cd05903 179 REHG--VTF---MMGATPFLTDLLN--------------------------AVEEAGEPLS----------------RLR 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 447 IMLSGGGPLSAATHEFVNVVFGRVVIG-YGLTEtiCVGAIQIPGDTETN----VTGLMEPGQEIKLldIDEYKHTDTPEP 521
Cdd:cd05903 212 TFVCGGATVPRSLARRAAELLGAKVCSaYGSTE--CPGAVTSITPAPEDrrlyTDGRPLPGVEIKV--VDDTGATLAPGV 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 522 RGEMLSRGPYLFKGYYKQPELTREVlDEDGWFHTGDVGSFTADGKMRIVGRVKALAkNCLGEYIALEALEAVysgneLLQ 601
Cdd:cd05903 288 EGELLSRGPSVFLGYLDRPDLTADA-APEGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDL-----LLG 360
|
490
....*....|....
gi 398009334 602 PNGV---CVLVHPD 612
Cdd:cd05903 361 HPGVieaAVVALPD 374
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
135-612 |
5.49e-33 |
|
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: 132.22 E-value: 5.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGS 214
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 ANvanvlklmkngvmpqvpiiyvgtlpasldthgvqvvsfkqvemigaahleggaakgtgplndDDLALIMYTSGTTGDP 294
Cdd:cd05935 82 EL--------------------------------------------------------------DDLALIPYTSGTTGLP 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 295 KGVMHTHRTLAAglHTLEPRVVDLLGqphSDDVYLSYLPMAHIMEFT-ITNLFIFRGA---FIGFGTPRTLTDTTARPHG 370
Cdd:cd05935 100 KGCMHTHFSAAA--NALQSAVWTGLT---PSDVILACLPLFHVTGFVgSLNTAVYVGGtyvLMARWDRETALELIEKYKV 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 371 DLLTFNPSMLAGVprifdtlkkaveaklppVGTLKRQVFDHAYqsrlaalkkgkdtpywnekvfaapravlgnrLRIMLS 450
Cdd:cd05935 175 TFWTNIPTMLVDL-----------------LATPEFKTRDLSS-------------------------------LKVLTG 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 451 GGGPLSAATHEFVNVVFG-RVVIGYGLTETICVGAIQIPGDTETNVTGLMEPGQEIKLLDIDEYKHTDtPEPRGEMLSRG 529
Cdd:cd05935 207 GGAPMPPAVAEKLLKLTGlRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELP-PNEVGEIVVRG 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 530 PYLFKGYYKQPELTREVLDEDG---WFHTGDVGSFTADGKMRIVGRVKALAkNCLGEYIALEALEAVYSGNELLQPngVC 606
Cdd:cd05935 286 PQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMI-NVSGFKVWPAEVEAKLYKHPAI*E--VC 362
|
....*.
gi 398009334 607 VLVHPD 612
Cdd:cd05935 363 VISVPD 368
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
125-591 |
2.10e-32 |
|
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: 131.98 E-value: 2.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 125 SITHFDEVVYVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHE 204
Cdd:cd12119 16 SRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 205 TESQAILCGsanvANVLKLMKNgVMPQVP----IIYVGTLPASLDTHGVQVVSFKQVemigaahLEGGAAKGTGPLNDDD 280
Cdd:cd12119 96 AEDRVVFVD----RDFLPLLEA-IAPRLPtvehVVVMTDDAAMPEPAGVGVLAYEEL-------LAAESPEYDWPDFDEN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 281 LALIM-YTSGTTGDPKGVMHTHRTLAagLHTLEPRVVDLLGQPHSDdVYLSYLPMAHIMEFTItnlfifrgAFIGF--GT 357
Cdd:cd12119 164 TAAAIcYTSGTTGNPKGVVYSHRSLV--LHAMAALLTDGLGLSESD-VVLPVVPMFHVNAWGL--------PYAAAmvGA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 358 PRTLTDttARPHGDLL-----TFNPSMLAGVPRIFDTLKKAVEAKLPPVGTLKRQVFDHAyqsrlaalkkgkdtpywnek 432
Cdd:cd12119 233 KLVLPG--PYLDPASLaelieREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGS-------------------- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 433 vfAAPRAVLgnrlrimlsgggplSAATHEFVnvvfgRVVIGYGLTETICVGAIQIPGDTETN-----------VTGLMEP 501
Cdd:cd12119 291 --AVPRSLI--------------EAFEERGV-----RVIHAWGMTETSPLGTVARPPSEHSNlsedeqlalraKQGRPVP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 502 GQEIKLLDIDEYKHTDTPEPRGEMLSRGPYLFKGYYKQPELTREvLDEDGWFHTGDVGSFTADGKMRIVGRVKALAKNCl 581
Cdd:cd12119 350 GVELRIVDDDGRELPWDGKAVGELQVRGPWVTKSYYKNDEESEA-LTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSG- 427
|
490
....*....|
gi 398009334 582 GEYIALEALE 591
Cdd:cd12119 428 GEWISSVELE 437
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
135-700 |
3.68e-32 |
|
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: 130.90 E-value: 3.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGS 214
Cdd:cd05926 15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 ANVAnvlKLMKNGVMPQVPIIYVGTLPASLDTHGvqvvsfkQVEMIGAAHLEGGAAKGTGPLNDDDLALIMYTSGTTGDP 294
Cdd:cd05926 95 GELG---PASRAASKLGLAILELALDVGVLIRAP-------SAESLSNLLADKKNAKSEGVPLPDDLALILHTSGTTGRP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 295 KGVMHTHRTLAA------GLHTLEPrvvdllgqphsDDVYLSYLPMAHIMEFTITNLFIFR--GAFI---GFgtprtltd 363
Cdd:cd05926 165 KGVPLTHRNLAAsatnitNTYKLTP-----------DDRTLVVMPLFHVHGLVASLLSTLAagGSVVlppRF-------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 364 ttaRPH---GDLLTFNPSMLAGVPRIFDTLkkaveaklppvgtlkrqvfdhayqsrLAALKKGKDTPYwnekvfaaprav 440
Cdd:cd05926 226 ---SAStfwPDVRDYNATWYTAVPTIHQIL--------------------------LNRPEPNPESPP------------ 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 441 lgNRLRIMLSGGGPLSAATHEFVNVVFGRVVI-GYGLTETicvgAIQI---PGDTETNVTGLMEPGQEIKLLDIDEYKHT 516
Cdd:cd05926 265 --PKLRFIRSCSASLPPAVLEALEATFGAPVLeAYGMTEA----AHQMtsnPLPPGPRKPGSVGKPVGVEVRILDEDGEI 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 517 DTPEPRGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKALAkNCLGEYIALEALEAVYSG 596
Cdd:cd05926 339 LPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELI-NRGGEKISPLEVDGVLLS 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 597 NELLQpNGVCVLVhPDKPYitalaltDEARATSFAAKHGIEGTYPALLKDQRfqqaaaismadtaraSNRASFECVKRVR 676
Cdd:cd05926 418 HPAVL-EAVAFGV-PDEKY-------GEEVAAAVVLREGASVTEEELRAFCR---------------KHLAAFKVPKKVY 473
|
570 580
....*....|....*....|....*
gi 398009334 677 VIDdewtpenEIL-TAAQKLKRRVI 700
Cdd:cd05926 474 FVD-------ELPkTATGKIQRRKV 491
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
131-573 |
1.40e-31 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 130.23 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 131 EVVYVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAI 210
Cdd:COG0365 36 EERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 211 LC--GSANVANVLKLMKN--GVMPQVP----IIYVGTLPASLDTHGVqvVSFKQVEMIGAAHLEggaakgTGPLNDDDLA 282
Cdd:COG0365 116 ITadGGLRGGKVIDLKEKvdEALEELPslehVIVVGRTGADVPMEGD--LDWDELLAAASAEFE------PEPTDADDPL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 283 LIMYTSGTTGDPKGVMHTHRTLAAGLHTLEPRVVDLlgqpHSDDVY-----------LSYL---PMAHimEFTItnlFIF 348
Cdd:COG0365 188 FILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDL----KPGDVFwctadigwatgHSYIvygPLLN--GATV---VLY 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 349 RGAfIGFGTPRTLTDTTARphgdlltFNPSMLAGVPRIFDTLKKAVEAKLPpvgtlkrqvfdhayQSRLAAlkkgkdtpy 428
Cdd:COG0365 259 EGR-PDFPDPGRLWELIEK-------YGVTVFFTAPTAIRALMKAGDEPLK--------------KYDLSS--------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 429 wnekvfaapravlgnrLRIMLSGGGPLSAATHEFVNVVFGRVVI-GYGLTETICV------------GAIQIPGdtetnv 495
Cdd:COG0365 308 ----------------LRLLGSAGEPLNPEVWEWWYEAVGVPIVdGWGQTETGGIfisnlpglpvkpGSMGKPV------ 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 496 tglmePGQEIKLLDiDEYKHTDTPEPrGEMLSRGPY--LFKGYYKQPELTREVL--DEDGWFHTGDVGSFTADGKMRIVG 571
Cdd:COG0365 366 -----PGYDVAVVD-EDGNPVPPGEE-GELVIKGPWpgMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILG 438
|
..
gi 398009334 572 RV 573
Cdd:COG0365 439 RS 440
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
277-572 |
5.07e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 127.03 E-value: 5.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 277 NDDDLALIMYTSGTTGDPKGVMHTHRTLAAGLhtleprvvDLLGQP---HSDDVYLSYLPMAHIMEFTITNLFIFR--GA 351
Cdd:PRK07787 126 DPDAPALIVYTSGTTGPPKGVVLSRRAIAADL--------DALAEAwqwTADDVLVHGLPLFHVHGLVLGVLGPLRigNR 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 352 FIGFGTPrtltdtTARPHGDLLTFNPSMLAGVPRIFdtlkkaveaklppvgtlkrqvfdhayqSRLAAlkkgkDTpywne 431
Cdd:PRK07787 198 FVHTGRP------TPEAYAQALSEGGTLYFGVPTVW---------------------------SRIAA-----DP----- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 432 kvfAAPRAVLGNRLriMLSGGGPLSAATHEFVNVVFG-RVVIGYGLTETICVGAIQIPGDTETNVTGLMEPGQEIKLLDI 510
Cdd:PRK07787 235 ---EAARALRGARL--LVSGSAALPVPVFDRLAALTGhRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDE 309
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398009334 511 DEYKHTDTPEPRGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGR 572
Cdd:PRK07787 310 DGGPVPHDGETVGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGR 371
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
279-613 |
2.30e-30 |
|
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: 125.52 E-value: 2.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 279 DDLALIMYTSGTTGDPKGVMHTHRTLaagLHTLEP--RVVDllgqPHSDDVYLSYLPMAHIMEFTITNLFIFRGAFIGFg 356
Cdd:cd05909 147 DDPAVILFTSGSEGLPKGVVLSHKNL---LANVEQitAIFD----PNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVV- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 357 tprtltdttarphgdlLTFNPSMLAGVPRIFDTLKKAVEAKLPpvgtlkrqVFDHAYqsrlaalkkgkdTPYWNEKVFAa 436
Cdd:cd05909 219 ----------------FHPNPLDYKKIPELIYDKKATILLGTP--------TFLRGY------------ARAAHPEDFS- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 437 pravlgnRLRIMLSGGGPLSAATHEFVNVVFG-RVVIGYGLTETICVGAIQIPG-DTETNVTGLMEPGQEIKLLDIDEYK 514
Cdd:cd05909 262 -------SLRLVVAGAEKLKDTLRQEFQEKFGiRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHE 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 515 HTDTPEpRGEMLSRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGRVKALAKnCLGEYIALEALEAVY 594
Cdd:cd05909 335 EVPIGE-GGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAK-IAGEMVSLEAIEDIL 411
|
330
....*....|....*....
gi 398009334 595 SGNeLLQPNGVCVLVHPDK 613
Cdd:cd05909 412 SEI-LPEDNEVAVVSVPDG 429
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
105-574 |
2.51e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 126.43 E-value: 2.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 105 PAPSTSRGSTSEPAKKERLMSitHFDEVV----------------YVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDT 168
Cdd:PRK12583 2 PQPSYYQGGGDKPLLTQTIGD--AFDATVarfpdrealvvrhqalRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 169 CVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILC-----GSANVANVLKLMKNGVMPQVPIIYVGTLPas 243
Cdd:PRK12583 80 CAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICadafkTSDYHAMLQELLPGLAEGQPGALACERLP-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 244 ldtHGVQVVSFKQVEMIG--AAHLEGGAAKG---------TGPLNDDDLALIMYTSGTTGDPKGVMHTHRTLAAGLHTle 312
Cdd:PRK12583 158 ---ELRGVVSLAPAPPPGflAWHELQARGETvsrealaerQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYF-- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 313 prVVDLLGQPHSDDVYLSyLPMAHIMEFTITNL--------FIFRG-AFIGFGTPRTLTDTTArphgdlltfnpSMLAGV 383
Cdd:PRK12583 233 --VAESLGLTEHDRLCVP-VPLYHCFGMVLANLgcmtvgacLVYPNeAFDPLATLQAVEEERC-----------TALYGV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 384 PRIFdtlkkAVEAKLPpvgtlKRQVFDhayqsrLAALKKGkdtpywnekvfaapravlgnrlrIMLSGGGPLSAATHEFV 463
Cdd:PRK12583 299 PTMF-----IAELDHP-----QRGNFD------LSSLRTG-----------------------IMAGAPCPIEVMRRVMD 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 464 NVVFGRVVIGYGLTETICVGAIQIPGDT-ETNVT--GLMEPGQEIKLLDIDeyKHTDTPEPRGEMLSRGPYLFKGYYKQP 540
Cdd:PRK12583 340 EMHMAEVQIAYGMTETSPVSLQTTAADDlERRVEtvGRTQPHLEVKVVDPD--GATVPRGEIGELCTRGYSVMKGYWNNP 417
|
490 500 510
....*....|....*....|....*....|....
gi 398009334 541 ELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVK 574
Cdd:PRK12583 418 EATAESIDEDGWMHTGDLATMDEQGYVRIVGRSK 451
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
135-576 |
2.64e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 126.30 E-value: 2.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGS 214
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 ANVANVLKLMKNGVMPQVPIIYVGT---LPASLDTHGVQ------VVSFKQVEMIgaaHLEGGAAK----GTGPLND--D 279
Cdd:PRK06710 130 LVFPRVTNVQSATKIEHVIVTRIADflpFPKNLLYPFVQkkqsnlVVKVSESETI---HLWNSVEKevntGVEVPCDpeN 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 280 DLALIMYTSGTTGDPKGVMHTHRTLAA----GLHTLEPRVvdllgqpHSDDVYLSYLPMAHIMEFT-ITNLFIFRGAFIG 354
Cdd:PRK06710 207 DLALLQYTGGTTGFPKGVMLTHKNLVSntlmGVQWLYNCK-------EGEEVVLGVLPFFHVYGMTaVMNLSIMQGYKMV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 355 FgTPRtltdttarphgdlltFNPSMlagvprIFDTLKKAveaklppvgtlKRQVFDHAYQSRLAALkkgkDTPYWNEKVF 434
Cdd:PRK06710 280 L-IPK---------------FDMKM------VFEAIKKH-----------KVTLFPGAPTIYIALL----NSPLLKEYDI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 435 AAPRAVlgnrlrimLSGGGPLSAATHE-FVNVVFGRVVIGYGLTETICV------------GAIQIP-GDTETNVTGLmE 500
Cdd:PRK06710 323 SSIRAC--------ISGSAPLPVEVQEkFETVTGGKLVEGYGLTESSPVthsnflwekrvpGSIGVPwPDTEAMIMSL-E 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398009334 501 PGQEIKlldideykhtdtPEPRGEMLSRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGRVKAL 576
Cdd:PRK06710 394 TGEALP------------PGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDM 456
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
135-578 |
1.25e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 124.38 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILC-- 212
Cdd:PRK06178 59 ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLAld 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 213 ----------GSANVANVLKLMKNGVMPQVPIIyvgTLPASLDTHGVQVVSfkQVEMIGAAHLEGGAAKGTGPlNDDDLA 282
Cdd:PRK06178 139 qlapvveqvrAETSLRHVIVTSLADVLPAEPTL---PLPDSLRAPRLAAAG--AIDLLPALRACTAPVPLPPP-ALDALA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 283 LIMYTSGTTGDPKGVMHTHRTL---AAGLHTleprvVDLLGQphSDDVYLSYLPMAHIMEFTITNLF-IFRGAfigfgtp 358
Cdd:PRK06178 213 ALNYTGGTTGMPKGCEHTQRDMvytAAAAYA-----VAVVGG--EDSVFLSFLPEFWIAGENFGLLFpLFSGA------- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 359 rTLTdTTARphGDLLTFnpsMLA----GVPRIFDTLKKAVEaklppvgtlkrqVFDH--AYQSRLAALKkgkdtpywnek 432
Cdd:PRK06178 279 -TLV-LLAR--WDAVAF---MAAveryRVTRTVMLVDNAVE------------LMDHprFAEYDLSSLR----------- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 433 vfaAPRAV-----LGNRLRimlsggGPLSAAThefvnvvfGRVVI--GYGLTET-----ICVGaiQIPGD----TETNVT 496
Cdd:PRK06178 329 ---QVRVVsfvkkLNPDYR------QRWRALT--------GSVLAeaAWGMTEThtcdtFTAG--FQDDDfdllSQPVFV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 497 GLMEPGQEIKLLDIDeykhTDTPEP---RGEMLSRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGRV 573
Cdd:PRK06178 390 GLPVPGTEFKICDFE----TGELLPlgaEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRR 464
|
....*
gi 398009334 574 KALAK 578
Cdd:PRK06178 465 KEMLK 469
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
135-574 |
2.26e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 123.33 E-value: 2.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAAL-GVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCg 213
Cdd:PRK05677 50 LTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVC- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 214 SANVANVLK--LMKNGVmPQVPIIYVGTLPASLDTHGVQVVSFKQVEMIGAAHLEGGA------AKGTG-PLND-----D 279
Cdd:PRK05677 129 LANMAHLAEkvLPKTGV-KHVIVTEVADMLPPLKRLLINAVVKHVKKMVPAYHLPQAVkfndalAKGAGqPVTEanpqaD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 280 DLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLEPRVVDLLGQphSDDVYLSYLPMAHIMEFTITNLFIfrgafigfgtpr 359
Cdd:PRK05677 208 DVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNE--GCEILIAPLPLYHIYAFTFHCMAM------------ 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 360 tltdttarphgdLLTFNPSMLAGVPRIFDTLKKaveaklppvgTLKRQVFDH--AYQSRLAALkkgkdtpyWNEKVFaap 437
Cdd:PRK05677 274 ------------MLIGNHNILISNPRDLPAMVK----------ELGKWKFSGfvGLNTLFVAL--------CNNEAF--- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 438 RAVLGNRLRIMLSGGGPLSAATHEFVNVVFG-RVVIGYGLTETICVGAIQIPGDTETNVTGLMEPGQEIKLLDiDEYKHT 516
Cdd:PRK05677 321 RKLDFSALKLTLSGGMALQLATAERWKEVTGcAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVID-DDGNEL 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 398009334 517 DTPEPrGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVK 574
Cdd:PRK05677 400 PLGEV-GELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKK 456
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
183-576 |
1.12e-28 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 121.47 E-value: 1.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 183 SAVAATVYANLGEAALAHALHETESQAILcgSANVANVLKLMK----NGVMPQVPIIyvgtLPaslDTHGVQVVSFKQVE 258
Cdd:PRK12492 121 SGARALVYLNMFGKLVQEVLPDTGIEYLI--EAKMGDLLPAAKgwlvNTVVDKVKKM----VP---AYHLPQAVPFKQAL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 259 MIGAAHleggaAKGTGPLNDDDLALIMYTSGTTGDPKGVMHTHRTLAAGLHtlepRVVDLLGQPHSD---------DVYL 329
Cdd:PRK12492 192 RQGRGL-----SLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANML----QVRACLSQLGPDgqplmkegqEVMI 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 330 SYLPMAHIMEFTITNLFIFrgafigfgtprtltdtTARPHGDLLTfNPSMLAGvprIFDTLKKAVEAKLPPVGTLKRQVF 409
Cdd:PRK12492 263 APLPLYHIYAFTANCMCMM----------------VSGNHNVLIT-NPRDIPG---FIKELGKWRFSALLGLNTLFVALM 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 410 DHayqsrlaalkkgkdtPYWNEKVFAApravlgnrLRIMLSGGGPLSAATHEFVNVVFG-RVVIGYGLTETICVGAIQIP 488
Cdd:PRK12492 323 DH---------------PGFKDLDFSA--------LKLTNSGGTALVKATAERWEQLTGcTIVEGYGLTETSPVASTNPY 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 489 GD-TETNVTGLMEPGQEIKLLDiDEYKHTDTPEpRGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKM 567
Cdd:PRK12492 380 GElARLGTVGIPVPGTALKVID-DDGNELPLGE-RGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFV 457
|
....*....
gi 398009334 568 RIVGRVKAL 576
Cdd:PRK12492 458 RIVDRKKDL 466
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
136-615 |
1.48e-28 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 119.09 E-value: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 136 TYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCgsa 215
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLT--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 216 nvanvlklmkngvmpqvpiiyvgtlPASLDTHGVQVVSFKQVEMIGAAHLEGGAAkgtgpLNDDDLALIMYTSGTTGDPK 295
Cdd:TIGR01923 78 -------------------------DSLLEEKDFQADSLDRIEAAGRYETSLSAS-----FNMDQIATLMFTSGTTGKPK 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 296 GVMHTHRTlaaglHTLEPRVVDLLGQPHSDDVYLSYLPMAHIMEFTItnlfIFRGAFIGFGTprTLTDTTARPHGDLLTF 375
Cdd:TIGR01923 128 AVPHTFRN-----HYASAVGSKENLGFTEDDNWLLSLPLYHISGLSI----LFRWLIEGATL--RIVDKFNQLLEMIANE 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 376 NPSMLAGVPRifdTLKKAVEAKLPPVgtlkrqvfdhayqsrlaalkkgkdtpywnekvfaapravlgnRLRIMLSGGGPL 455
Cdd:TIGR01923 197 RVTHISLVPT---QLNRLLDEGGHNE------------------------------------------NLRKILLGGSAI 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 456 SAATHEFVNVVFGRVVIGYGLTETIC-VGAIQIPGDTETNVTGLMEPGQEIKLldideykHTDTPEPRGEMLSRGPYLFK 534
Cdd:TIGR01923 232 PAPLIEEAQQYGLPIYLSYGMTETCSqVTTATPEMLHARPDVGRPLAGREIKI-------KVDNKEGHGEIMVKGANLMK 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 535 GYYKQPELtREVLDEDGWFHTGDVGSFTADGKMRIVGRvkalAKNCL---GEYIALEALEAVysgneLLQPNGV--CVLV 609
Cdd:TIGR01923 305 GYLYQGEL-TPAFEQQGWFNTGDIGELDGEGFLYVLGR----RDDLIisgGENIYPEEIETV-----LYQHPGIqeAVVV 374
|
....*..
gi 398009334 610 -HPDKPY 615
Cdd:TIGR01923 375 pKPDAEW 381
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
135-572 |
2.02e-28 |
|
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: 119.78 E-value: 2.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAiLCGS 214
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARV-VVVS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 ANVANVLKLMKNGVMPQ-VPIIYVGtlPASLDThgvqvvSFKQVEMIGAAHLEGGAAKGTGPlndDDLALIMYTSGTTGD 293
Cdd:cd05959 109 GELAPVLAAALTKSEHTlVVLIVSG--GAGPEA------GALLLAELVAAEAEQLKPAATHA---DDPAFWLYSSGSTGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 294 PKGVMHTHRTLAaglHTLEPRVVDLLGQpHSDDVYLSylpmahimeftITNLFIfrgAFiGFGT----PRTLTDTT---- 365
Cdd:cd05959 178 PKGVVHLHADIY---WTAELYARNVLGI-REDDVCFS-----------AAKLFF---AY-GLGNsltfPLSVGATTvlmp 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 366 ARPHGD-----LLTFNPSMLAGVPrifdTLkkaveaklppvgtlkrqvfdhaYQSRLAAlkkgkdtPYWNEKVFAaprav 440
Cdd:cd05959 239 ERPTPAavfkrIRRYRPTVFFGVP----TL----------------------YAAMLAA-------PNLPSRDLS----- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 441 lgnRLRIMLSGGGPLSAATHEFVNVVFG-RVVIGYGLTETICVGAIQIPGDTETNVTGLMEPGQEIKLldIDEYKHTDTP 519
Cdd:cd05959 281 ---SLRLCVSAGEALPAEVGERWKARFGlDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVEL--RDEDGGDVAD 355
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 398009334 520 EPRGEMLSRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGR 572
Cdd:cd05959 356 GEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGR 407
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
118-574 |
2.09e-28 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 120.08 E-value: 2.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 118 AKKERLMSITHFDE---VVYVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDT---CVEWLigiygiWSC--------- 182
Cdd:cd05906 20 AERGPTKGITYIDAdgsEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDnedFIPAF------WACvlagfvpap 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 183 SAVAATvYANlGEAALAHALH--ET-ESQAILCGSANVANVLKLMKNGVMPQVPIIYVGTLPASL-DTHGVQVVSfkqve 258
Cdd:cd05906 94 LTVPPT-YDE-PNARLRKLRHiwQLlGSPVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAaDHDLPQSRP----- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 259 migaahleggaakgtgplndDDLALIMYTSGTTGDPKGVMHTHRTLaagLHTLEPRVVDLLGQPhsDDVYLSYLPMAHIM 338
Cdd:cd05906 167 --------------------DDLALLMLTSGSTGFPKAVPLTHRNI---LARSAGKIQHNGLTP--QDVFLNWVPLDHVG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 339 EFTITNLfifRGAFIGFGTPRTLTDTtarphgdlltfnpsMLAGVPRIFDTLKKaveaklppvgtlkRQV-------Fdh 411
Cdd:cd05906 222 GLVELHL---RAVYLGCQQVHVPTEE--------------ILADPLRWLDLIDR-------------YRVtitwapnF-- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 412 AYQSRLAALKKGKDTPyWNekvfaapravLGNrLRIMLSGGGPLSAATHEFVNVVFGR-------VVIGYGLTETiCVGA 484
Cdd:cd05906 270 AFALLNDLLEEIEDGT-WD----------LSS-LRYLVNAGEAVVAKTIRRLLRLLEPyglppdaIRPAFGMTET-CSGV 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 485 IQIPGDTETNVTGLME--------PGQEIKLLDIDEykhTDTPEPR-GEMLSRGPYLFKGYYKQPELTREVLDEDGWFHT 555
Cdd:cd05906 337 IYSRSFPTYDHSQALEfvslgrpiPGVSMRIVDDEG---QLLPEGEvGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRT 413
|
490
....*....|....*....
gi 398009334 556 GDVGsFTADGKMRIVGRVK 574
Cdd:cd05906 414 GDLG-FLDNGNLTITGRTK 431
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
136-594 |
2.60e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 119.65 E-value: 2.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 136 TYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGSA 215
Cdd:PRK08316 38 TYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 216 NVANVLKLMKNgvMPQVPIIYvgTLPASLDTHGVQVVSFkqvemigAAHLEGGAAKGTGP-LNDDDLALIMYTSGTTGDP 294
Cdd:PRK08316 118 LAPTAEAALAL--LPVDTLIL--SLVLGGREAPGGWLDF-------ADWAEAGSVAEPDVeLADDDLAQILYTSGTESLP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 295 KGVMHTHRTLaagLHTLEPRVVDllGQPHSDDVYLSYLPMAHIMEftitnLFIFRGAFIGFGTPRTLTDttaRPHGDLlt 374
Cdd:PRK08316 187 KGAMLTHRAL---IAEYVSCIVA--GDMSADDIPLHALPLYHCAQ-----LDVFLGPYLYVGATNVILD---APDPEL-- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 375 fnpsmlagvprIFDTLKKAVEAKL--PP---VGTLKRQVFDhayQSRLAALKKGkdtpYWNEKVFaaPRAVLgNRLRIML 449
Cdd:PRK08316 252 -----------ILRTIEAERITSFfaPPtvwISLLRHPDFD---TRDLSSLRKG----YYGASIM--PVEVL-KELRERL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 450 SGGGplsaatheFVNVvfgrvvigYGLTETICVGAIQIPGDTETNVTGLMEPG--QEIKLLDIDeykHTDTP--EPrGEM 525
Cdd:PRK08316 311 PGLR--------FYNC--------YGQTEIAPLATVLGPEEHLRRPGSAGRPVlnVETRVVDDD---GNDVApgEV-GEI 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 526 LSRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGRVKALAKNClGEYIA-LEALEAVY 594
Cdd:PRK08316 371 VHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVAsREVEEALY 438
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
136-578 |
4.55e-28 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 119.31 E-value: 4.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 136 TYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATvyANLgeaalAHALHETESQAILCGSa 215
Cdd:PLN02246 52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTT--ANP-----FYTPAEIAKQAKASGA- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 216 nvanvlKLmkngVMPQVPiiYVGTLPASLDTHGVQVVSFKQVEMiGAAHLEGGAAKGTGPL-----NDDDLALIMYTSGT 290
Cdd:PLN02246 124 ------KL----IITQSC--YVDKLKGLAEDDGVTVVTIDDPPE-GCLHFSELTQADENELpeveiSPDDVVALPYSSGT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 291 TGDPKGVMHTHRtlaaGLHTLEPRVVDllGQ-P----HSDDVYLSYLPMAHIMEFTITNLFIFR-GAFI----GFGTPRT 360
Cdd:PLN02246 191 TGLPKGVMLTHK----GLVTSVAQQVD--GEnPnlyfHSDDVILCVLPMFHIYSLNSVLLCGLRvGAAIlimpKFEIGAL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 361 LtdttarphgDLLT-FNPSMLAGVPRIFDTLkkaveAKLPPVGtlkrqvfDHAYQSrlaalkkgkdtpywnekvfaapra 439
Cdd:PLN02246 265 L---------ELIQrHKVTIAPFVPPIVLAI-----AKSPVVE-------KYDLSS------------------------ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 440 vlgnrLRIMLSGGGPL-----SAATHEFVNVVFGRvviGYGLTE-----TICVGAIQIPGDTETNVTGLMEPGQEIKLLD 509
Cdd:PLN02246 300 -----IRMVLSGAAPLgkeleDAFRAKLPNAVLGQ---GYGMTEagpvlAMCLAFAKEPFPVKSGSCGTVVRNAELKIVD 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398009334 510 IDeykhTDTPEPR---GEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKALAK 578
Cdd:PLN02246 372 PE----TGASLPRnqpGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIK 439
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
135-574 |
1.20e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 117.75 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGL-AALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCG 213
Cdd:PRK08314 36 ISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 214 SANVANVLKLMKNGVMPQVpII--YVGTLPaslDTHGVQVVSFKQVEmigaAHLEGGAAKGTGPLND------------- 278
Cdd:PRK08314 116 SELAPKVAPAVGNLRLRHV-IVaqYSDYLP---AEPEIAVPAWLRAE----PPLQALAPGGVVAWKEalaaglappphta 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 279 --DDLALIMYTSGTTGDPKGVMHTHRTLaagLHTLEPRVVdlLGQPHSDDVYLSYLPMAHI--MEFTItNLFIFRGAfig 354
Cdd:PRK08314 188 gpDDLAVLPYTSGTTGVPKGCMHTHRTV---MANAVGSVL--WSNSTPESVVLAVLPLFHVtgMVHSM-NAPIYAGA--- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 355 fgtprTLTdttarphgdLLTFNPSMLAGvpRIFDTLKKAVEAKLPPVgtlkrqVFDhayqsrlaalkkgkdtpywnekVF 434
Cdd:PRK08314 259 -----TVV---------LMPRWDREAAA--RLIERYRVTHWTNIPTM------VVD----------------------FL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 435 AAPRavLGNR----LRIMLSGGGPLSAATHEFVNVVFG-RVVIGYGLTETI--------------CVGaiqIPG-DTETN 494
Cdd:PRK08314 295 ASPG--LAERdlssLRYIGGGGAAMPEAVAERLKELTGlDYVEGYGLTETMaqthsnppdrpklqCLG---IPTfGVDAR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 495 VtglMEP--GQEiklLDIDEykhtdtpepRGEMLSRGPYLFKGYYKQPELTREVLDE-DG--WFHTGDVGSFTADGKMRI 569
Cdd:PRK08314 370 V---IDPetLEE---LPPGE---------VGEIVVHGPQVFKGYWNRPEATAEAFIEiDGkrFFRTGDLGRMDEEGYFFI 434
|
....*
gi 398009334 570 VGRVK 574
Cdd:PRK08314 435 TDRLK 439
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
134-576 |
5.51e-27 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 115.36 E-value: 5.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 134 YVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIgIYGiwSCSAVAAtVYANLG----EAALAHALHETESQA 209
Cdd:PRK07514 28 RYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALA-LYL--ATLRAGA-VFLPLNtaytLAELDYFIGDAEPAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 210 ILCGSANVANVLKLMKngvmpQVPIIYVGTLPAslDTHGvqvvSFKQvemiGAAHLegGAAKGTGPLNDDDLALIMYTSG 289
Cdd:PRK07514 104 VVCDPANFAWLSKIAA-----AAGAPHVETLDA--DGTG----SLLE----AAAAA--PDDFETVPRGADDLAAILYTSG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 290 TTGDPKGVMHTHRTLAAGLHTLeprvVDLLGQpHSDDVYLSYLPMAHImeftitnlfifrgafigfgtprtltdttarpH 369
Cdd:PRK07514 167 TTGRSKGAMLSHGNLLSNALTL----VDYWRF-TPDDVLIHALPIFHT-------------------------------H 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 370 GDLLTFNPSMLAGVPRIFdtLKK----AVEAKLPPvgtlkrqvfdhayqsrlAALKKGKDTPYwnEKVFAAPR----AVL 441
Cdd:PRK07514 211 GLFVATNVALLAGASMIF--LPKfdpdAVLALMPR-----------------ATVMMGVPTFY--TRLLQEPRltreAAA 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 442 GNRLRImlSGGGPLSAATH-EFVNVVFGRVVIGYGLTETI------CVGAiQIPGdtetnVTGLMEPGQEIKLLDIDeyk 514
Cdd:PRK07514 270 HMRLFI--SGSAPLLAETHrEFQERTGHAILERYGMTETNmntsnpYDGE-RRAG-----TVGFPLPGVSLRVTDPE--- 338
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398009334 515 hTDTPEPRGE--MLS-RGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKAL 576
Cdd:PRK07514 339 -TGAELPPGEigMIEvKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDL 402
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
136-626 |
6.55e-27 |
|
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: 113.93 E-value: 6.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 136 TYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCgsa 215
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 216 nvanvlklmkngvmpqvpiiyvgtlpasldthgvqvvsfkqvemigaahleggaakgtgplnddDLALIMYTSGTTGDPK 295
Cdd:cd05934 82 ----------------------------------------------------------------DPASILYTSGTTGPPK 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 296 GVMHTHRTLA-AGLHTLEPRVVdllgqpHSDDVYLSYLPMAHIMEFTITNLfifrGAFIGFGT--------PRTLTDTTA 366
Cdd:cd05934 98 GVVITHANLTfAGYYSARRFGL------GEDDVYLTVLPLFHINAQAVSVL----AALSVGATlvllprfsASRFWSDVR 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 367 RPHGDLLTFNPSMLagvprifDTLKKAveaklPPVgtlkrqvfdhayqsrlaalkkgkdtpywnekvfAAPRAvlgNRLR 446
Cdd:cd05934 168 RYGATVTNYLGAML-------SYLLAQ-----PPS---------------------------------PDDRA---HRLR 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 447 IMLSGGGPlsAATHEFVNVVFG-RVVIGYGLTETICVGAIQIPGDTETNVTGLMEPGQEIKLLDiDEYKHTDTPEPrGEM 525
Cdd:cd05934 200 AAYGAPNP--PELHEEFEERFGvRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVD-DDGQELPAGEP-GEL 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 526 L---SRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGRvkalAKNCL---GEYIALEALEAVysgnel 599
Cdd:cd05934 276 VirgLRGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDR----KKDMIrrrGENISSAEVERA------ 344
|
490 500
....*....|....*....|....*..
gi 398009334 600 lqpngvcVLVHPDKPYITALALTDEAR 626
Cdd:cd05934 345 -------ILRHPAVREAAVVAVPDEVG 364
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
275-593 |
1.67e-26 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 114.55 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 275 PLNDDDLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLEPRVVDLLGQPHSDDVYLSYLPMAHIMeftitNLFIFRGAFIG 354
Cdd:PLN02574 194 VIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEYPGSDNVYLAALPMFHIY-----GLSLFVVGLLS 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 355 FGTPRTLtdttarphgdLLTFNPSMLAGVPRIFDTLKKAVeakLPPVgtlkrqvfdhayqsrLAALKKgkdtpywnekvf 434
Cdd:PLN02574 269 LGSTIVV----------MRRFDASDMVKVIDRFKVTHFPV---VPPI---------------LMALTK------------ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 435 aAPRAVLGN---RLRIMLSGGGPLSAAT-HEFVNVvFGRV--VIGYGLTETICVGAIQIPGDTETNVT--GLMEPGQEIK 506
Cdd:PLN02574 309 -KAKGVCGEvlkSLKQVSCGAAPLSGKFiQDFVQT-LPHVdfIQGYGMTESTAVGTRGFNTEKLSKYSsvGLLAPNMQAK 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 507 LLDIdEYKHTDTPEPRGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKALAKNcLGEYIA 586
Cdd:PLN02574 387 VVDW-STGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIA 464
|
....*..
gi 398009334 587 LEALEAV 593
Cdd:PLN02574 465 PADLEAV 471
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
135-624 |
3.63e-25 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 110.45 E-value: 3.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGS 214
Cdd:PLN02330 56 VTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTND 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 ANVANVLKLmkngvmpQVPIIYVGtlpaslDTHGVQVVSFKQVemigaahLEGGAAKGTGPLNDD----DLALIMYTSGT 290
Cdd:PLN02330 136 TNYGKVKGL-------GLPVIVLG------EEKIEGAVNWKEL-------LEAADRAGDTSDNEEilqtDLCALPFSSGT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 291 TGDPKGVMHTHRTLAAGL-HTLEPRVVDLLGQPhsddVYLSYLPMAHImeFTITNlfifrgafIGFGTPRTLTDTTARPH 369
Cdd:PLN02330 196 TGISKGVMLTHRNLVANLcSSLFSVGPEMIGQV----VTLGLIPFFHI--YGITG--------ICCATLRNKGKVVVMSR 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 370 GDLLTFNPSMLAG-------VPRIFDTLkkaveAKLPPVgtlkrQVFDhayqsrLAALKkgkdtpywnekvfaapravlg 442
Cdd:PLN02330 262 FELRTFLNALITQevsfapiVPPIILNL-----VKNPIV-----EEFD------LSKLK--------------------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 443 nrLRIMLSGGGPL-----SAATHEFVNVvfgRVVIGYGLTETICVGAIQipGDTET-------NVTGLMEPGQEIKLLDI 510
Cdd:PLN02330 305 --LQAIMTAAAPLapellTAFEAKFPGV---QVQEAYGLTEHSCITLTH--GDPEKghgiakkNSVGFILPNLEVKFIDP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 511 DEYKHTDTPEPrGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKALAKNcLGEYIALEAL 590
Cdd:PLN02330 378 DTGRSLPKNTP-GELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAEL 455
|
490 500 510
....*....|....*....|....*....|....
gi 398009334 591 EAVysgnellqpngvcVLVHPDKPYITALALTDE 624
Cdd:PLN02330 456 EAI-------------LLTHPSVEDAAVVPLPDE 476
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
280-593 |
8.03e-25 |
|
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: 105.88 E-value: 8.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 280 DLALIMYTSGTTGDPKGVMHTHRTL---AAGLHTLEPrvvdllgqPHSDDVYLSYLPMAHIMEFTItnlfIFRGAfigfg 356
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLlasAAGLHSRLG--------FGGGDSWLLSLPLYHVGGLAI----LVRSL----- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 357 tprtltdttarphgdlltfnpsmLAGVPRIFDTLKKAVEAKLPPVGtlkrqvFDHAyqsRL--AALKKGKDTPywnekvf 434
Cdd:cd17630 64 -----------------------LAGAELVLLERNQALAEDLAPPG------VTHV---SLvpTQLQRLLDSG------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 435 AAPRAVLgnRLRIMLSGGGPLSAATHEFVNVVFGRVVIGYGLTET---ICVGAiqiPGDTETNVTGLMEPGQEIKLLDid 511
Cdd:cd17630 105 QGPAALK--SLRAVLLGGAPIPPELLERAADRGIPLYTTYGMTETasqVATKR---PDGFGRGGVGVLLPGRELRIVE-- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 512 eykhtdtpepRGEMLSRGPYLFKGYYKQPEltREVLDEDGWFHTGDVGSFTADGKMRIVGRVKALAkNCLGEYIALEALE 591
Cdd:cd17630 178 ----------DGEIWVGGASLAMGYLRGQL--VPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIE 244
|
..
gi 398009334 592 AV 593
Cdd:cd17630 245 AA 246
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
136-574 |
9.11e-25 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 109.07 E-value: 9.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 136 TYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGSA 215
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 216 NVANVLKLMKNGVMPQVP----IIYVGTL-PASLDthgvqvVSFKQVemigaahLEGGAAKGTG-PLNDDDLALIMYTSG 289
Cdd:PRK06087 131 FKQTRPVDLILPLQNQLPqlqqIVGVDKLaPATSS------LSLSQI-------IADYEPLTTAiTTHGDELAAVLFTSG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 290 TTGDPKGVMHTH-------RTLAAGLHTleprvvdllgqpHSDDVYLSYLPMAHIMEF--TITNLFIFRGafigfgtpRT 360
Cdd:PRK06087 198 TEGLPKGVMLTHnnilaseRAYCARLNL------------TWQDVFMMPAPLGHATGFlhGVTAPFLIGA--------RS 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 361 LTDTTARPHGDLLTFNPS----MLAGVPRIFDTLKkAVEAklppvgtlkrqvfDHAYQSRLaalkkgkdtpywnekvfaa 436
Cdd:PRK06087 258 VLLDIFTPDACLALLEQQrctcMLGATPFIYDLLN-LLEK-------------QPADLSAL------------------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 437 pravlgnrlRIMLSGGGPLSAathEFVNVVFGRVVI---GYGLTETiCVGAIQIPGD-TETNV--TGLMEPGQEIKLldI 510
Cdd:PRK06087 305 ---------RFFLCGGTTIPK---KVARECQQRGIKllsVYGSTES-SPHAVVNLDDpLSRFMhtDGYAAAGVEIKV--V 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398009334 511 DEYKHTDTPEPRGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVK 574
Cdd:PRK06087 370 DEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKK 433
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
136-573 |
1.42e-24 |
|
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: 106.97 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 136 TYSEMEERIFHFGAGL-AALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGS 214
Cdd:TIGR01733 1 TYRELDERANRLARHLrAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 ANVANVLKlmkngvMPQVPIIYVGTlpasldthgvqvvsfkQVEMIGAAHLEGGAAKGTGPlndDDLALIMYTSGTTGDP 294
Cdd:TIGR01733 81 ALASRLAG------LVLPVILLDPL----------------ELAALDDAPAPPPPDAPSGP---DDLAYVIYTSGSTGRP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 295 KGVMHTHRTLAAGLHTLEPRVVDLlgqphSDDVYLSYLPMAHimEFTITNLFifrGAFIGFGTPRTLTDTTARPHGDLL- 373
Cdd:TIGR01733 136 KGVVVTHRSLVNLLAWLARRYGLD-----PDDRVLQFASLSF--DASVEEIF---GALLAGATLVVPPEDEERDDAALLa 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 374 ----TFNPSMLAGVPRIFDTLKKAVEAKLPpvgtlkrqvfdhayqsrlaalkkgkdtpywnekvfaapravlgnRLRIML 449
Cdd:TIGR01733 206 aliaEHPVTVLNLTPSLLALLAAALPPALA--------------------------------------------SLRLVI 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 450 SGGGPLSAATHEFVNVVFGRVVI--GYGLTE-TICVGAIQIPGDTETNVT----GLMEPGQEIKLLDiDEYKHTDTPEPr 522
Cdd:TIGR01733 242 LGGEALTPALVDRWRARGPGARLinLYGPTEtTVWSTATLVDPDDAPRESpvpiGRPLANTRLYVLD-DDLRPVPVGVV- 319
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 398009334 523 GEMLSRGPYLFKGYYKQPELTREVL--------DEDGWFHTGDVGSFTADGKMRIVGRV 573
Cdd:TIGR01733 320 GELYIGGPGVARGYLNRPELTAERFvpdpfaggDGARLYRTGDLVRYLPDGNLEFLGRI 378
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
280-574 |
1.88e-24 |
|
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: 104.89 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 280 DLALIMYTSGTTGDPKGVMHTHR-TLAAGLHTLEprvvdlLGQPHSDDVYLSYLPMAHImeftitnlFIFRGAFIGfgtp 358
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRqTLRAAAAWAD------CADLTEDDRYLIINPFFHT--------FGYKAGIVA---- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 359 RTLTDTTARPHGdllTFNpsmlagVPRIFDTLKKAVEAKLPPVGTLKRQVFDHAYQSR--LAALKKGKDTPywnekvfAA 436
Cdd:cd17638 63 CLLTGATVVPVA---VFD------VDAILEAIERERITVLPGPPTLFQSLLDHPGRKKfdLSSLRAAVTGA-------AT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 437 PRAVLGNRLRIMLSgggplsaathefvnvvFGRVVIGYGLTETICVGAIQiPGDTETNV---TGLMEPGQEIKLLDidey 513
Cdd:cd17638 127 VPVELVRRMRSELG----------------FETVLTAYGLTEAGVATMCR-PGDDAETVattCGRACPGFEVRIAD---- 185
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398009334 514 khtdtpepRGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVK 574
Cdd:cd17638 186 --------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLK 238
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
135-572 |
8.79e-24 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 104.85 E-value: 8.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILcgs 214
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVV--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 anvanvlklmkngvmpqvpiiyvgtlpasldthgvqvvsfkqvemigaahleggaakgtgpLNDDDLALIMYTSGTTGDP 294
Cdd:cd05919 88 -------------------------------------------------------------TSADDIAYLLYSSGTTGPP 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 295 KGVMHTHRTLaagLHTLEPRVVDLLGQPHSDDVYlsylpMAHIMEFTI---TNLF--IFRGA----FIGFGTPRTLTDTT 365
Cdd:cd05919 107 KGVMHAHRDP---LLFADAMAREALGLTPGDRVF-----SSAKMFFGYglgNSLWfpLAVGAsavlNPGWPTAERVLATL 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 366 ARphgdlltFNPSMLAGVPRIFDTLKkaVEAKLPPvgtlkrqvfdHAYQSrlaalkkgkdtpywnekvfaapravlgnrL 445
Cdd:cd05919 179 AR-------FRPTVLYGVPTFYANLL--DSCAGSP----------DALRS-----------------------------L 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 446 RIMLSGGGPLSAATHEFVNVVFGRVVI-GYGLTETICVGAIQIPGDTETNVTGLMEPGQEIKLLDidEYKHTDTPEPRGE 524
Cdd:cd05919 211 RLCVSAGEALPRGLGERWMEHFGGPILdGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD--EEGHTIPPGEEGD 288
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 398009334 525 MLSRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGR 572
Cdd:cd05919 289 LLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGR 335
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
279-574 |
3.01e-23 |
|
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: 101.97 E-value: 3.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 279 DDLALIMYTSGTTGDPKGVMHTHRTLAAGLHTleprVVDLLGQPHSDDVYLSYlPMAHIMEFTITNLF-IFRGAFIGFGT 357
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNNGYF----IGERLGLTEQDRLCIPV-PLFHCFGSVLGVLAcLTHGATMVFPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 358 PrtltdttarphgdllTFNP------------SMLAGVPRIFdtlkkaveaklppVGTLKRQVFDhayQSRLAALKKGkd 425
Cdd:cd05917 77 P---------------SFDPlavleaiekekcTALHGVPTMF-------------IAELEHPDFD---KFDLSSLRTG-- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 426 tpywnekvfaapravlgnrlrIMlsGGGPLSAATHEFVNVVFG--RVVIGYGLTETICVGAIQIPGDT---ETNVTGLME 500
Cdd:cd05917 124 ---------------------IM--AGAPCPPELMKRVIEVMNmkDVTIAYGMTETSPVSTQTRTDDSiekRVNTVGRIM 180
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398009334 501 PGQEIKLLDIdeykhTDTPEP----RGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVK 574
Cdd:cd05917 181 PHTEAKIVDP-----EGGIVPpvgvPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIK 253
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
125-613 |
8.79e-23 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 102.94 E-value: 8.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 125 SITHFDEVVyVTY--SEMEERIF-HFGAGLAAL--------GVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANL 193
Cdd:PRK05620 20 STVHGDTTV-TTWggAEQEQTTFaAIGARAAALahalhdelGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 194 GEAALAHALHETESQAILCGSANVANVLKLMKNgvMPQV-PIIYVG----TLPASLDTHGVQVVSFKQVemigaahLEGG 268
Cdd:PRK05620 99 MNDQIVHIINHAEDEVIVADPRLAEQLGEILKE--CPCVrAVVFIGpsdaDSAAAHMPEGIKVYSYEAL-------LDGR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 269 AAKGTGP-LNDDDLALIMYTSGTTGDPKGVMHTHRTLAagLHTLEPRVVDLLGQPHsDDVYLSYLPMAHIMEFTITnlfi 347
Cdd:PRK05620 170 STVYDWPeLDETTAAAICYSTGTTGAPKGVVYSHRSLY--LQSLSLRTTDSLAVTH-GESFLCCVPIYHVLSWGVP---- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 348 fRGAFIGfGTPRTLTDTTARPhgdlltfnpsmlagvprifDTLKKAVEAKLPPVG----TLKRQVFDHAYQSrlaalkkg 423
Cdd:PRK05620 243 -LAAFMS-GTPLVFPGPDLSA-------------------PTLAKIIATAMPRVAhgvpTLWIQLMVHYLKN-------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 424 kdtpywnekvfaAPRAVlgnRLRIMLSGGGPLSAATHEFVNVVFG-RVVIGYGLTETICVGAIQIP-----GDTETNV-- 495
Cdd:PRK05620 294 ------------PPERM---SLQEIYVGGSAVPPILIKAWEERYGvDVVHVWGMTETSPVGTVARPpsgvsGEARWAYrv 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 496 -TGLMEPGQEIKLLDIDEYKHTdTPEPRGEMLSRGPYLFKGYYKQP----------------ELTREVLDEDGWFHTGDV 558
Cdd:PRK05620 359 sQGRFPASLEYRIVNDGQVMES-TDRNEGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDV 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 398009334 559 GSFTADGKMRIVGRVKALAKNClGEYIALEALEavysgNELLQPNGV---CVLVHPDK 613
Cdd:PRK05620 438 GSVTRDGFLTIHDRARDVIRSG-GEWIYSAQLE-----NYIMAAPEVvecAVIGYPDD 489
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
136-576 |
2.14e-22 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 101.48 E-value: 2.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 136 TYSEMEERIFHFGAGLA-ALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCgS 214
Cdd:PRK06839 29 TYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFV-E 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 ANVANVLKLMKnGVMPQVPIIYVGTLPASLDThgvqvvsfkqvEMIGAAhleggaakgtgPLNDDDLALIMYTSGTTGDP 294
Cdd:PRK06839 108 KTFQNMALSMQ-KVSYVQRVISITSLKEIEDR-----------KIDNFV-----------EKNESASFIICYTSGTTGKP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 295 KG-VMHTHRTLAAGLHTLepRVVDLlgqpHSDDVYLSYLPMAHIMEFtitNLFIFrgafigfgtprtltdttarphgdll 373
Cdd:PRK06839 165 KGaVLTQENMFWNALNNT--FAIDL----TMHDRSIVLLPLFHIGGI---GLFAF------------------------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 374 tfnPSMLAG----VPRIFDTLKKaveaklppvgtlkrqvfdhayqsrLAALKKGKDT-----PYWNEKVFAAPRAVLGN- 443
Cdd:PRK06839 211 ---PTLFAGgviiVPRKFEPTKA------------------------LSMIEKHKVTvvmgvPTIHQALINCSKFETTNl 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 444 -RLRIMLSGGGPLSAA-THEFVN--VVFGRvviGYGLTETICVGAIQIPGDTETNVTGLMEPGQEIKLLDIDEYKHTDTP 519
Cdd:PRK06839 264 qSVRWFYNGGAPCPEElMREFIDrgFLFGQ---GFGMTETSPTVFMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEV 340
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 398009334 520 EPRGEMLSRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGRVKAL 576
Cdd:PRK06839 341 GEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEM 396
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
136-596 |
5.23e-22 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 100.14 E-value: 5.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 136 TYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCgSA 215
Cdd:PRK08008 39 SYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVT-SA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 216 NVANVLKLMKNGVMPQVPIIYVgTLPASLDTHGVqvVSFKQVEMIGAAHLeggaaKGTGPLNDDDLALIMYTSGTTGDPK 295
Cdd:PRK08008 118 QFYPMYRQIQQEDATPLRHICL-TRVALPADDGV--SSFTQLKAQQPATL-----CYAPPLSTDDTAEILFTSGTTSRPK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 296 GVMHTHRTLA-AGLHTleprvvDLLGQPHSDDVYLSYLPMAHImEFTITNLFifrGAFIGFGTPRTLTDTTARPH-GDLL 373
Cdd:PRK08008 190 GVVITHYNLRfAGYYS------AWQCALRDDDVYLTVMPAFHI-DCQCTAAM---AAFSAGATFVLLEKYSARAFwGQVC 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 374 TFNPSMLAGVPRIFDTLkkaveaKLPPVGTLKRQvfdhayqsrlaalkkgkdtpywnekvfaapravlgNRLRIMLSgGG 453
Cdd:PRK08008 260 KYRATITECIPMMIRTL------MVQPPSANDRQ-----------------------------------HCLREVMF-YL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 454 PLSAATHEFVNVVFG-RVVIGYGLTETIcVGAIqipGDTetnvtglmePGQEIKLLDI------------DEYKHTDTPE 520
Cdd:PRK08008 298 NLSDQEKDAFEERFGvRLLTSYGMTETI-VGII---GDR---------PGDKRRWPSIgrpgfcyeaeirDDHNRPLPAG 364
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398009334 521 PRGEMLSR---GPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKALAKNClGEYIALEALEAVYSG 596
Cdd:PRK08008 365 EIGEICIKgvpGKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENIIAT 442
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
275-593 |
7.79e-22 |
|
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: 99.30 E-value: 7.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 275 PLNDDDLALIMYTSGTTGDPKGVMHTHR-----TLAAGLHTleprvvdllgQPHSDDVYLSYLPMAHIMEFTitnlFIFR 349
Cdd:cd12118 129 PADEWDPIALNYTSGTTGRPKGVVYHHRgaylnALANILEW----------EMKQHPVYLWTLPMFHCNGWC----FPWT 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 350 GAFIGfGTPRTLTDTTARPHGDLL-TFNPSMLAGVPRIFDTLKKAVEAKLPPvgtLKRQVFdhayqsrlaalkkgkdtpy 428
Cdd:cd12118 195 VAAVG-GTNVCLRKVDAKAIYDLIeKHKVTHFCGAPTVLNMLANAPPSDARP---LPHRVH------------------- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 429 wnekvfaapravlgnrlriMLSGGGPLSAATHEFVNVVFGRVVIGYGLTET---ICVGAIQ-----IPGDTETNV---TG 497
Cdd:cd12118 252 -------------------VMTAGAPPPAAVLAKMEELGFDVTHVYGLTETygpATVCAWKpewdeLPTEERARLkarQG 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 498 LMEPGQE-IKLLDideyKHTDTPEPR-----GEMLSRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVG 571
Cdd:cd12118 313 VRYVGLEeVDVLD----PETMKPVPRdgktiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKD 387
|
330 340
....*....|....*....|..
gi 398009334 572 RVKALAkNCLGEYIALEALEAV 593
Cdd:cd12118 388 RSKDII-ISGGENISSVEVEGV 408
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
280-641 |
1.15e-21 |
|
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: 96.95 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 280 DLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLEPRVVDLLgqphSDDVYLSYLPMAHI--MEFTITNLFiFRGAFIGFGT 357
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWV----VGDVTYLPLPATHIggLWWILTCLI-HGGLCVTGGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 358 PRTLTDTTarphgDLLTFNPSMLAG-VPrifDTLKKAVeaklppvgtlkrqvfdHAYQSRLAALKKGKDTPYWNEKVFAA 436
Cdd:cd17635 77 NTTYKSLF-----KILTTNAVTTTClVP---TLLSKLV----------------SELKSANATVPSLRLIGYGGSRAIAA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 437 PRAVlgnrlrIMLSGggplsaathefvnvvFGRVVIGYGLTETICVGAIQIPGDT-ETNVTGLMEPGQEIKLLDIDEYKH 515
Cdd:cd17635 133 DVRF------IEATG---------------LTNTAQVYGLSETGTALCLPTDDDSiEINAVGRPYPGVDVYLAATDGIAG 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 516 TDTPEprGEMLSRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGRVKaLAKNCLGEYIALEALEAVYS 595
Cdd:cd17635 192 PSASF--GTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSS-ESINCGGVKIAPDEVERIAE 267
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 398009334 596 GNELLQPNGVCVLvhPDKPY-------ITALALTDEARATsfAAKHGIEGTYP 641
Cdd:cd17635 268 GVSGVQECACYEI--SDEEFgelvglaVVASAELDENAIR--ALKHTIRRELE 316
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
279-613 |
1.18e-21 |
|
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: 98.19 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 279 DDLALIMYTSGTTGDPKGVMHThrtlaAGLHTLEPRVVDL-LGQpHSDDVYLSYLPMAHIMEFTItnlfIFRGAFigFGT 357
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQT-----FGNHWWSAIGSALnLGL-TEDDNWLCALPLFHISGLSI----LMRSVI--YGM 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 358 PRTLTD--TTARPHGDLLTFNPSMLAGVPRIFDTLKkaveaklppvgtlkrQVFDHAYQsrlaalkkgkdtpywnekvfa 435
Cdd:cd05912 145 TVYLVDkfDAEQVLHLINSGKVTIISVVPTMLQRLL---------------EILGEGYP--------------------- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 436 apravlgNRLRIMLSGGGPLSAATHEFVNVVFGRVVIGYGLTETicvgAIQI----PGDTETNV--TGLMEPGQEIKLLD 509
Cdd:cd05912 189 -------NNLRCILLGGGPAPKPLLEQCKEKGIPVYQSYGMTET----CSQIvtlsPEDALNKIgsAGKPLFPVELKIED 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 510 IDEYKHTDtpeprGEMLSRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGRVKALAKNClGEYIALEA 589
Cdd:cd05912 258 DGQPPYEV-----GEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLIISG-GENIYPAE 330
|
330 340
....*....|....*....|....*..
gi 398009334 590 LEAVysgneLLQPNGV--CVLV-HPDK 613
Cdd:cd05912 331 IEEV-----LLSHPAIkeAGVVgIPDD 352
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
130-578 |
1.79e-21 |
|
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: 98.37 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 130 DEVVYVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQA 209
Cdd:TIGR02262 26 DDISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 210 ILCGSAnVANVLKLMKNGVMPQVPIIYVGTLPASLDthgvqvvsfkQVEMIGAAHLEGGAAKGTGPlndDDLALIMYTSG 289
Cdd:TIGR02262 106 VFVSGA-LLPVIKAALGKSPHLEHRVVVGRPEAGEV----------QLAELLATESEQFKPAATQA---DDPAFWLYSSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 290 TTGDPKGVMHTHRTLaagLHTLEPRVVDLLGQPHSDDVylsylpmahimeFTITNLFIFRGAFIGFGTPRTLTDTTA--- 366
Cdd:TIGR02262 172 STGMPKGVVHTHSNP---YWTAELYARNTLGIREDDVC------------FSAAKLFFAYGLGNALTFPMSVGATTVlmg 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 367 -RPHGD-----LLTFNPSMLAGVPrifdTLkkaveaklppvgtlkrqvfdhaYQSRLAALKKGKDTPywnekvfaaprav 440
Cdd:TIGR02262 237 eRPTPDavfdrLRRHQPTIFYGVP----TL----------------------YAAMLADPNLPSEDQ------------- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 441 lgNRLRIMLSGGGPLSAATHEFVNVVFG-RVVIGYGLTETICVGAIQIPGDTETNVTGLMEPGQEIKLLDiDEYKHTDTP 519
Cdd:TIGR02262 278 --VRLRLCTSAGEALPAEVGQRWQARFGvDIVDGIGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVG-DGGQDVADG 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 398009334 520 EPrGEMLSRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGRVKALAK 578
Cdd:TIGR02262 355 EP-GELLISGPSSATMYWNNRAKSRDTF-QGEWTRSGDKYVRNDDGSYTYAGRTDDMLK 411
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
262-574 |
1.89e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 98.34 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 262 AAHLEGGAAKGTGPLNDDDLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLeprvvDLLGQPHSDDVYLSYLPMAHIMEFt 341
Cdd:PRK09088 118 IASADALEPADTPSIPPERVSLILFTSGTSGQPKGVMLSERNLQQTAHNF-----GVLGRVDAHSSFLCDAPMFHIIGL- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 342 ITNL--FIFRGAFI----GFGTPRTLtdttaRPHGDLlTFNPSMLAGVPRIFDTLKKaveaklppvgtlkRQVFDHAYQS 415
Cdd:PRK09088 192 ITSVrpVLAVGGSIlvsnGFEPKRTL-----GRLGDP-ALGITHYFCVPQMAQAFRA-------------QPGFDAAALR 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 416 RLAALKKGkdtpywnekvfAAPRAvlGNRLRIMLSGGGPlsaathefvnvvfgrVVIGYGLTETICVGAIQIPG---DTE 492
Cdd:PRK09088 253 HLTALFTG-----------GAPHA--AEDILGWLDDGIP---------------MVDGFGMSEAGTVFGMSVDCdviRAK 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 493 TNVTGLMEPGQEIKLLDIDEykhTDTP--EPrGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIV 570
Cdd:PRK09088 305 AGAAGIPTPTVQTRVVDDQG---NDCPagVP-GELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVV 380
|
....
gi 398009334 571 GRVK 574
Cdd:PRK09088 381 DRKK 384
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
265-592 |
4.19e-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: 341246 [Multi-domain] Cd Length: 457 Bit Score: 97.13 E-value: 4.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 265 LEGGAAKGTG----PLNDDDLALIMYTSGTTGDPKGVMHTHRTLAAGLHTleprVVDLLGQpHSDDVYLSYLPMAHIMEF 340
Cdd:cd05922 99 ADGIRAARASapahEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARS----IAEYLGI-TADDRALTVLPLSYDYGL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 341 TITNLFIFRGAFI----GFGTPRTLTDttarphgDLLTFNPSMLAGVPRIFdtlkkaveaklppvGTLKRQVFDHAyqsr 416
Cdd:cd05922 174 SVLNTHLLRGATLvltnDGVLDDAFWE-------DLREHGATGLAGVPSTY--------------AMLTRLGFDPA---- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 417 laalkkgkdtpywnekvfAAPravlgnRLRIMLSGGGPLSAATHEFVNVVF--GRVVIGYGLTETICVGAIQIPG--DTE 492
Cdd:cd05922 229 ------------------KLP------SLRYLTQAGGRLPQETIARLRELLpgAQVYVMYGQTEATRRMTYLPPEriLEK 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 493 TNVTGLMEPGQEIKLLDIDEYKhTDTPEPrGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGR 572
Cdd:cd05922 285 PGSIGLAIPGGEFEILDDDGTP-TPPGEP-GEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGR 362
|
330 340
....*....|....*....|
gi 398009334 573 VKALAKnCLGEYIALEALEA 592
Cdd:cd05922 363 RDRMIK-LFGNRISPTEIEA 381
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
130-572 |
5.30e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 97.51 E-value: 5.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 130 DEVVYVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGiwsCSAVAATVYA---NLGEAALAHALheTE 206
Cdd:PRK06164 31 DEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLA---CARLGATVIAvntRYRSHEVAHIL--GR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 207 SQAILCGSA------NVANVLKLMKNGVMPQVPIIYV-----GTLPASLDTHGVQVVSFKQvemiGAAHleggAAKGTGP 275
Cdd:PRK06164 106 GRARWLVVWpgfkgiDFAAILAAVPPDALPPLRAIAVvddaaDATPAPAPGARVQLFALPD----PAPP----AAAGERA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 276 LNDDDLALIMYTSGTTGDPKGVMHTHRTLAAGLHtlepRVVDLLGQpHSDDVYLSYLPMAHIMEFTITNLFIFRGAFI-- 353
Cdd:PRK06164 178 ADPDAGALLFTTSGTTSGPKLVLHRQATLLRHAR----AIARAYGY-DPGAVLLAALPFCGVFGFSTLLGALAGGAPLvc 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 354 --GFGTPRTLtdTTARPHGDLLTF-NPSMLAgvpRIFDTlkkavEAKLPPVGTLKRQVFdHAYQSR---LAALKKGKDTP 427
Cdd:PRK06164 253 epVFDAARTA--RALRRHRVTHTFgNDEMLR---RILDT-----AGERADFPSARLFGF-ASFAPAlgeLAALARARGVP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 428 ----YWNEKVFA---APRAVLGNRLRImLSGGGPLSAAthefvnvvfGRVVIgyglteticvgaiqipGDTETNvtGLME 500
Cdd:PRK06164 322 ltglYGSSEVQAlvaLQPATDPVSVRI-EGGGRPASPE---------ARVRA----------------RDPQDG--ALLP 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398009334 501 PGQEiklldideykhtdtpeprGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGR 572
Cdd:PRK06164 374 DGES------------------GEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTR 427
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
277-605 |
1.08e-20 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 95.80 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 277 NDDDLALIMYTSGTTGDPKGVMHTHR---------TLAAGLHtleprvvdllgqphSDDVYLSYLPMAHIMEFTItnlfI 347
Cdd:PRK03640 139 DLDEVATIMYTSGTTGKPKGVIQTYGnhwwsavgsALNLGLT--------------EDDCWLAAVPIFHISGLSI----L 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 348 FRGafIGFGTPRTLTDT--TARPHGDLLTFNPSMLAGVPRIFDTLkkaveaklppvgtlkrqvfdhayqsrLAALKKGkd 425
Cdd:PRK03640 201 MRS--VIYGMRVVLVEKfdAEKINKLLQTGGVTIISVVSTMLQRL--------------------------LERLGEG-- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 426 tPYwnekvfaapravlGNRLRIMLSGGGPLSAATHEFVNVVFGRVVIGYGLTETicvgAIQI----PGDTETNVTGLMEP 501
Cdd:PRK03640 251 -TY-------------PSSFRCMLLGGGPAPKPLLEQCKEKGIPVYQSYGMTET----ASQIvtlsPEDALTKLGSAGKP 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 502 --GQEIKLLDiDEykHTDTPEPRGEMLSRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGRVKALAkN 579
Cdd:PRK03640 313 lfPCELKIEK-DG--VVVPPFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLI-I 387
|
330 340
....*....|....*....|....*.
gi 398009334 580 CLGEYIALEALEAVYSGNELLQPNGV 605
Cdd:PRK03640 388 SGGENIYPAEIEEVLLSHPGVAEAGV 413
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
276-635 |
1.14e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 96.65 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 276 LNDDDLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLEPRVVDLLGQPHSddVYLSYLPMAHIMEFTItnlfIFRGAFIGF 355
Cdd:PRK12582 217 ITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPP--VSLDWMPWNHTMGGNA----NFNGLLWGG 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 356 GT---------PrTLTDTTARphgDLLTFNPSMLAGVPRIFDTLKKAVEAKlppvGTLKRQVFdhayqsrlaalkkgkdt 426
Cdd:PRK12582 291 GTlyiddgkplP-GMFEETIR---NLREISPTVYGNVPAGYAMLAEAMEKD----DALRRSFF----------------- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 427 pywnekvfaapravlgNRLRIMLSGGGPLSAATHE-----FVNVVFGRVVI--GYGLTET--ICVGAIQipgDTE-TNVT 496
Cdd:PRK12582 346 ----------------KNLRLMAYGGATLSDDLYErmqalAVRTTGHRIPFytGYGATETapTTTGTHW---DTErVGLI 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 497 GLMEPGQEIKLLDI-DEYkhtdtpeprgEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGK----MRIVG 571
Cdd:PRK12582 407 GLPLPGVELKLAPVgDKY----------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVDPDDpekgLIFDG 476
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398009334 572 RVKALAKNCLGEYIALEAL--EAVYSGNELLQPNGVCVLvhpDKPYITALALTDEARATSFAAKHG 635
Cdd:PRK12582 477 RVAEDFKLSTGTWVSVGTLrpDAVAACSPVIHDAVVAGQ---DRAFIGLLAWPNPAACRQLAGDPD 539
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
136-574 |
1.17e-20 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 96.28 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 136 TYSEMEERIFHFGAGLA-ALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGS 214
Cdd:PRK08974 50 TFRKLEERSRAFAAYLQnGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 aNVANVL-KLMKNGVMPQVPIIYVG-TLPASLDThgvqVVSF--KQVE-MIGAAHLEGGAA------KGTG-----P-LN 277
Cdd:PRK08974 130 -NFAHTLeKVVFKTPVKHVILTRMGdQLSTAKGT----LVNFvvKYIKrLVPKYHLPDAISfrsalhKGRRmqyvkPeLV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 278 DDDLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLEPRVVDLLgQPHSDDVYLSyLPMAHIMEFTITNL-FIFRGAfigfg 356
Cdd:PRK08974 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGPLL-HPGKELVVTA-LPLYHIFALTVNCLlFIELGG----- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 357 tprtltdttarphGDLLTFNPSmlaGVPRIFDTLKKAVEAKLPPVGTLkrqvFDhayqsrlaALKKGKDtpyWNEKVFAA 436
Cdd:PRK08974 278 -------------QNLLITNPR---DIPGFVKELKKYPFTAITGVNTL----FN--------ALLNNEE---FQELDFSS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 437 pravlgnrLRIMLSGGGPLSAATHE-FVNVVFGRVVIGYGLTEtiC---VGAIQIPGDTETNVTGLMEPGQEIKLLDiDE 512
Cdd:PRK08974 327 --------LKLSVGGGMAVQQAVAErWVKLTGQYLLEGYGLTE--CsplVSVNPYDLDYYSGSIGLPVPSTEIKLVD-DD 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398009334 513 YKHTDTPEPrGEMLSRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGRVK 574
Cdd:PRK08974 396 GNEVPPGEP-GELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKK 455
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
135-578 |
2.57e-20 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 94.85 E-value: 2.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQaILCGS 214
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVR-LLVTS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 ANVANVLKLMKNGVMPQVPIIYVGTL-PASLDTHGVQVVSFKQVEMIGaahlegGAAKGTgPLNDDDLALIMYTSGTTGD 293
Cdd:TIGR03098 105 SERLDLLHPALPGCHDLRTLIIVGDPaHASEGHPGEEPASWPKLLALG------DADPPH-PVIDSDMAAILYTSGSTGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 294 PKGVMHTHRTLAAGLHTLEPRVvdllgQPHSDDVYLSYLPMAHIMEFTITNLFIFRGA---FIGFGTPRTLTDTTARpHG 370
Cdd:TIGR03098 178 PKGVVLSHRNLVAGAQSVATYL-----ENRPDDRLLAVLPLSFDYGFNQLTTAFYVGAtvvLHDYLLPRDVLKALEK-HG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 371 dlltfnPSMLAGVPRIFdtlkkaveaklppvgtlkrqvfdhayqSRLAALKkgkdtpyWNEKVFAApravlgnrLRIMLS 450
Cdd:TIGR03098 252 ------ITGLAAVPPLW---------------------------AQLAQLD-------WPESAAPS--------LRYLTN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 451 GGGPLSAATHEFVNVVF--GRVVIGYGLTETIcvGAIQIPG---DTETNVTGLMEPGQEIKLLDIDeyKHTDTPEPRGEM 525
Cdd:TIGR03098 284 SGGAMPRATLSRLRSFLpnARLFLMYGLTEAF--RSTYLPPeevDRRPDSIGKAIPNAEVLVLRED--GSECAPGEEGEL 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398009334 526 LSRGPYLFKGYYKQPELTREVLDEDGWFH-----------TGDVGSFTADGKMRIVGRVKALAK 578
Cdd:TIGR03098 360 VHRGALVAMGYWNDPEKTAERFRPLPPFPgelhlpelavwSGDTVRRDEEGFLYFVGRRDEMIK 423
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
280-624 |
3.61e-20 |
|
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: 94.32 E-value: 3.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 280 DLALIMYTSGTTGDPKGVMHTHRTLAAGLHtlepRVVDLLGQPHsDDVYLSYLPMAHimEFTITNLFIFrGAFIGFGTPr 359
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTHNDYAYNVR----ASAEVCGLDQ-DTVYLAVLPAAH--NFPLACPGVL-GTLLAGGRV- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 360 tltdttarphgdLLTFNPSMLAGVPRIfDTLKKAVEAKLPPVGTLkrqvfdhayqsrlaalkkgkdtpyWNEKVfAAPRA 439
Cdd:cd05920 211 ------------VLAPDPSPDAAFPLI-EREGVTVTALVPALVSL------------------------WLDAA-ASRRA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 440 VLGNrLRIMLSGGGPLSAATHEFVNVVFG-RVVIGYGLTE-TICVGAIQIPGDTETNVTGL-MEPGQEIKLLDIDEykhT 516
Cdd:cd05920 253 DLSS-LRLLQVGGARLSPALARRVPPVLGcTLQQVFGMAEgLLNYTRLDDPDEVIIHTQGRpMSPDDEIRVVDEEG---N 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 517 DTPE-PRGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKALAkNCLGEYIALEALEavys 595
Cdd:cd05920 329 PVPPgEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQI-NRGGEKIAAEEVE---- 403
|
330 340
....*....|....*....|....*....
gi 398009334 596 gNELLQpngvcvlvHPDKPYITALALTDE 624
Cdd:cd05920 404 -NLLLR--------HPAVHDAAVVAMPDE 423
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
136-574 |
4.35e-20 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 94.44 E-value: 4.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 136 TYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGSA 215
Cdd:PRK06155 48 TYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 216 NVAnVLKLMKNGVMPQVPIIYVGTLPASLDTHGVQVVSFKQvemigaahleGGAAKGTGPLNDDDLALIMYTSGTTGDPK 295
Cdd:PRK06155 128 LLA-ALEAADPGDLPLPAVWLLDAPASVSVPAGWSTAPLPP----------LDAPAPAAAVQPGDTAAILYTSGTTGPSK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 296 GVMHTHrtlaAGLHTLEPRVVDLLGQpHSDDVYLSYLPMAHimeftitnlfifrgafigfgtprtltdTTArphgdLLTF 375
Cdd:PRK06155 197 GVCCPH----AQFYWWGRNSAEDLEI-GADDVLYTTLPLFH---------------------------TNA-----LNAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 376 NPSMLAGVPRIFDTLKKAveaklppvgtlkrqvfdhayqSRL-AALKKGKDTPYWnekVFAAPRAVL----------GNR 444
Cdd:PRK06155 240 FQALLAGATYVLEPRFSA---------------------SGFwPAVRRHGATVTY---LLGAMVSILlsqparesdrAHR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 445 LRIMLSGGGPlsAATHEFVNVVFG-RVVIGYGLTETICVGAIQIPGDtETNVTGLMEPGQEIKLldIDEYKHTDTPEPRG 523
Cdd:PRK06155 296 VRVALGPGVP--AALHAAFRERFGvDLLDGYGSTETNFVIAVTHGSQ-RPGSMGRLAPGFEARV--VDEHDQELPDGEPG 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 398009334 524 EMLSRG--PYLF-KGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGRVK 574
Cdd:PRK06155 371 ELLLRAdePFAFaTGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIK 423
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
185-626 |
6.70e-20 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 94.99 E-value: 6.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 185 VAATVYANL----GEAALAHALHETESQAILCGSANVAnvlKLMKNGVMPQVP----IIYVGTLPASLdtHGVQ-VVSFK 255
Cdd:PRK08633 687 LAGKVPVNLnytaSEAALKSAIEQAQIKTVITSRKFLE---KLKNKGFDLELPenvkVIYLEDLKAKI--SKVDkLTALL 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 256 QVEMIGAAHLEGGAAKGTGPlndDDLALIMYTSGTTGDPKGVMHTHRTLAAGLhtlepRVVDLLGQPHSDDVYLSYLPMA 335
Cdd:PRK08633 762 AARLLPARLLKRLYGPTFKP---DDTATIIFSSGSEGEPKGVMLSHHNILSNI-----EQISDVFNLRNDDVILSSLPFF 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 336 HIMEFTITnlfifrgafigfgtprtltdttarphgdllTFNPsMLAGVPRIF--DTLKKAVEAKLppvgTLKRQV----- 408
Cdd:PRK08633 834 HSFGLTVT------------------------------LWLP-LLEGIKVVYhpDPTDALGIAKL----VAKHRAtillg 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 409 ---FDHAYqsrlaaLKKGKDTPywneKVFAApravlgnrLRIMLSGGGPLSAATHEFVNVVFG-RVVIGYGLTETICVGA 484
Cdd:PRK08633 879 tptFLRLY------LRNKKLHP----LMFAS--------LRLVVAGAEKLKPEVADAFEEKFGiRILEGYGATETSPVAS 940
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 485 IQIPGDTETNVT----------GLMEPGQEIKLLDIDEYKHTDTPEPrGEMLSRGPYLFKGYYKQPELTREVL---DEDG 551
Cdd:PRK08633 941 VNLPDVLAADFKrqtgskegsvGMPLPGVAVRIVDPETFEELPPGED-GLILIGGPQVMKGYLGDPEKTAEVIkdiDGIG 1019
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398009334 552 WFHTGDVGSFTADGKMRIVGRVKALAKnCLGEYIALEALEavysgnELLQpngvcVLVHPDKPYITALALTDEAR 626
Cdd:PRK08633 1020 WYVTGDKGHLDEDGFLTITDRYSRFAK-IGGEMVPLGAVE------EELA-----KALGGEEVVFAVTAVPDEKK 1082
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
129-574 |
6.72e-20 |
|
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: 93.84 E-value: 6.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 129 FDEVVYVTYSEMEERIFHFGAGLAALGvTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYA-NLGEAA--LAHALHET 205
Cdd:cd05931 19 GGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPpTPGRHAerLAAILADA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 206 ESQAILCGSANVANVLKLMKNGVMPQVPIIYVGTLPASldthgvqvvsfkqvemigaahlEGGAAKGTGPLNDDDLALIM 285
Cdd:cd05931 98 GPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPD----------------------TSAADWPPPSPDPDDIAYLQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 286 YTSGTTGDPKGVMHTHRTLAAGLHTLeprvvDLLGQPHSDDVYLSYLPMAH---IMEFTITNLFifrgafigFGTPRTLT 362
Cdd:cd05931 156 YTSGSTGTPKGVVVTHRNLLANVRQI-----RRAYGLDPGDVVVSWLPLYHdmgLIGGLLTPLY--------SGGPSVLM 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 363 DTTA---RPHG--DLLTFNPSMLAGVPrifdtlkkaveaklppvgtlkrqvfDHAYQsrLAAlKKGKDTpywnekvfAAP 437
Cdd:cd05931 223 SPAAflrRPLRwlRLISRYRATISAAP-------------------------NFAYD--LCV-RRVRDE--------DLE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 438 RAVLGnRLRIMLSGGGPLSAAT-HEFVNvVFGR-------VVIGYGLTETIC--------------------------VG 483
Cdd:cd05931 267 GLDLS-SWRVALNGAEPVRPATlRRFAE-AFAPfgfrpeaFRPSYGLAEATLfvsggppgtgpvvlrvdrdalagravAV 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 484 AIQIPGDTETNVTGLMEPGQEIKLLDIDeykhTDTPEPR---GEMLSRGPYLFKGYYKQPELTREV------LDEDGWFH 554
Cdd:cd05931 345 AADDPAARELVSCGRPLPDQEVRIVDPE----TGRELPDgevGEIWVRGPSVASGYWGRPEATAETfgalaaTDEGGWLR 420
|
490 500
....*....|....*....|
gi 398009334 555 TGDVGsFTADGKMRIVGRVK 574
Cdd:cd05931 421 TGDLG-FLHDGELYITGRLK 439
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
135-574 |
7.13e-20 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 93.79 E-value: 7.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGL-AALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCG 213
Cdd:PRK08751 51 ITYREADQLVEQFAAYLlGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 214 SANVANVLKLMKNGVMPQVPIIYVGTL----PASL-------------DTHGVQVVSFKQVEMIGAAHleggaAKGTGPL 276
Cdd:PRK08751 131 DNFGTTVQQVIADTPVKQVITTGLGDMlgfpKAALvnfvvkyvkklvpEYRINGAIRFREALALGRKH-----SMPTLQI 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 277 NDDDLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLEPRVVDLLGQPHSDDVYLSYLPMAHIMEFTITNLfifrgAFIGFG 356
Cdd:PRK08751 206 EPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKLEEGCEVVITALPLYHIFALTANGL-----VFMKIG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 357 TPRTLTDttarphgdlltfNPSMLAGVPRifdTLKKAVEAKLPPVGTLKRQVFDhayqsrlaalkkgkdTPYWNEKVFAA 436
Cdd:PRK08751 281 GCNHLIS------------NPRDMPGFVK---ELKKTRFTAFTGVNTLFNGLLN---------------TPGFDQIDFSS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 437 pravlgnrLRIMLSGGGPLSAATHEFVNVVFGRVVI-GYGLTET---ICVGAIQIPgdtETNVT-GLMEPGQEIKLLDiD 511
Cdd:PRK08751 331 --------LKMTLGGGMAVQRSVAERWKQVTGLTLVeAYGLTETspaACINPLTLK---EYNGSiGLPIPSTDACIKD-D 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398009334 512 EYKHTDTPEpRGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVK 574
Cdd:PRK08751 399 AGTVLAIGE-IGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKK 460
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
134-620 |
7.64e-20 |
|
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: 93.08 E-value: 7.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 134 YVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWScsavaatvyanLGeaalahalhetesqailcg 213
Cdd:cd05945 16 TLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALK-----------AG------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 214 sanvanvlklmkngvMPQVPIiyvgtlpaslDTHgvqvVSFKQVEMIGAAhleggaAKGTGPLND-DDLALIMYTSGTTG 292
Cdd:cd05945 66 ---------------HAYVPL----------DAS----SPAERIREILDA------AKPALLIADgDDNAYIIFTSGSTG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 293 DPKGVMHTHRTLAAglhTLEPRVVDLLGQPHsdDVYLSYLPmahimeftitnlFIFrgafigfgtprtltdttarphgDL 372
Cdd:cd05945 111 RPKGVQISHDNLVS---FTNWMLSDFPLGPG--DVFLNQAP------------FSF----------------------DL 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 373 LTFN--PSMLAG-----VPRifDTLKKAVEaklpPVGTLKRQVFDHAYQsrlaalkkgkdTPYwnekvFAAPRAVLGN-- 443
Cdd:cd05945 152 SVMDlyPALASGatlvpVPR--DATADPKQ----LFRFLAEHGITVWVS-----------TPS-----FAAMCLLSPTft 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 444 -----RLRIMLSGGGPLSAATHEFVNVVF--GRVVIGYGLTE-TICVGAIQIPGDTETNVT----GLMEPGQEIKLldID 511
Cdd:cd05945 210 peslpSLRHFLFCGEVLPHKTARALQQRFpdARIYNTYGPTEaTVAVTYIEVTPEVLDGYDrlpiGYAKPGAKLVI--LD 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 512 EYKHTDTPEPRGEMLSRGPYLFKGYYKQPELTREVLDED---GWFHTGDVGSFTADGKMRIVGRVKALAK-NclGEYIAL 587
Cdd:cd05945 288 EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKlN--GYRIEL 365
|
490 500 510
....*....|....*....|....*....|...
gi 398009334 588 EALEAVYSGNELLQpnGVCVLVHPDKPYITALA 620
Cdd:cd05945 366 EEIEAALRQVPGVK--EAVVVPKYKGEKVTELI 396
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
470-574 |
8.90e-20 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 93.72 E-value: 8.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 470 VVIGYGLTETIcvgaiqiPGDTETNVT----------GLMEPGQEIKLLDIDeykhTDTPEPR---GEMLSRGPYLFKGY 536
Cdd:PRK08315 344 VTIAYGMTETS-------PVSTQTRTDdplekrvttvGRALPHLEVKIVDPE----TGETVPRgeqGELCTRGYSVMKGY 412
|
90 100 110
....*....|....*....|....*....|....*...
gi 398009334 537 YKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVK 574
Cdd:PRK08315 413 WNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIK 450
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
135-663 |
1.19e-19 |
|
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: 93.27 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVyanlgeaALAHALHETESqailcgs 214
Cdd:cd05921 26 VTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPV-------SPAYSLMSQDL------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 ANVANVLKLMKNG-VMPQVPIIYVGTLPASLDTHGVQVVSFKQVEMIGAAHLEGGAAK-----------GTGPlndDDLA 282
Cdd:cd05921 92 AKLKHLFELLKPGlVFAQDAAPFARALAAIFPLGTPLVVSRNAVAGRGAISFAELAATpptaavdaafaAVGP---DTVA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 283 LIMYTSGTTGDPKGVMHTHRTLAAGLHTLEPRVVDLLGQPhsdDVYLSYLPMAHIMEFTIT-NLFIFRGA--FIGFGTPR 359
Cdd:cd05921 169 KFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEP---PVLVDWLPWNHTFGGNHNfNLVLYNGGtlYIDDGKPM 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 360 T-LTDTTARphgDLLTFNPSMLAGVPRIFDTLKKAVEAKlppvGTLKRQVFDhayqsrlaalkkgkdtpywnekvfaapr 438
Cdd:cd05921 246 PgGFEETLR---NLREISPTVYFNVPAGWEMLVAALEKD----EALRRRFFK---------------------------- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 439 avlgnRLRIMLSGGGPLSAATHE-----FVNVVFGRVVI--GYGLTET-----ICVGAIQIPGdtetNVtGLMEPGQEIK 506
Cdd:cd05921 291 -----RLKLMFYAGAGLSQDVWDrlqalAVATVGERIPMmaGLGATETaptatFTHWPTERSG----LI-GLPAPGTELK 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 507 LLDIDEykhtdtpepRGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFT--ADGKMRIV--GRVKALAKNCLG 582
Cdd:cd05921 361 LVPSGG---------KYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpDDPAKGLVfdGRVAEDFKLASG 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 583 EYIALEAL--EAVYSGNELLQ------PNGVCV--LVHPDKPYITALALTDEARATSFAAKHGIEGTYPALLkdQRFQQA 652
Cdd:cd05921 432 TWVSVGPLraRAVAACAPLVHdavvagEDRAEVgaLVFPDLLACRRLVGLQEASDAEVLRHAKVRAAFRDRL--AALNGE 509
|
570
....*....|.
gi 398009334 653 AAISMADTARA 663
Cdd:cd05921 510 ATGSSSRIARA 520
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
278-611 |
1.22e-19 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 92.89 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 278 DDDLALIM-YTSGTTGDPKGVMHTHRTLAagLHTLEPRVVDLLGQpHSDDVYLSYLPMAHIMEFTItnlfifrgAFIGFG 356
Cdd:PRK06018 175 DENTAAGMcYTSGTTGDPKGVLYSHRSNV--LHALMANNGDALGT-SAADTMLPVVPLFHANSWGI--------AFSAPS 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 357 TPRTLTDTTARPHGdlltfnpsmlAGVPRIFDTLKKAVEAKLPPVGTLKRQVFDhayqsrlaalKKGKDTPYWNEKVF-- 434
Cdd:PRK06018 244 MGTKLVMPGAKLDG----------ASVYELLDTEKVTFTAGVPTVWLMLLQYME----------KEGLKLPHLKMVVCgg 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 435 -AAPRAVLgnrlrimlsgggplsAATHEF-VNVVFGrvvigYGLTETICVGAI--------QIPGDTETNV---TGLMEP 501
Cdd:PRK06018 304 sAMPRSMI---------------KAFEDMgVEVRHA-----WGMTEMSPLGTLaalkppfsKLPGDARLDVlqkQGYPPF 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 502 GQEIKLLDIDEYKHTDTPEPRGEMLSRGPYLFKGYYKqpeLTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKALAKNCl 581
Cdd:PRK06018 364 GVEMKITDDAGKELPWDGKTFGRLKVRGPAVAAAYYR---VDGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSG- 439
|
330 340 350
....*....|....*....|....*....|
gi 398009334 582 GEYIALEALEAVYSGNELLQPNGVCVLVHP 611
Cdd:PRK06018 440 GEWISSIDLENLAVGHPKVAEAAVIGVYHP 469
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
135-715 |
1.99e-19 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 92.63 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATV---YANLGE--AALAHALHETESQA 209
Cdd:PRK08180 70 LTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVspaYSLVSQdfGKLRHVLELLTPGL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 210 ILCGSANV-ANVLKLMkngVMPQVPIIYVGTLPAsldthGVQVVSFKQ-VEMIGAAHLEGGAAKgTGPlndDDLALIMYT 287
Cdd:PRK08180 150 VFADDGAAfARALAAV---VPADVEVVAVRGAVP-----GRAATPFAAlLATPPTAAVDAAHAA-VGP---DTIAKFLFT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 288 SGTTGDPKGVMHTHRTLAAGLHTLEPRVVDLLGQPhsdDVYLSYLPMAHImeF---TITNLFIFRGA--FIGFGTPRT-L 361
Cdd:PRK08180 218 SGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEP---PVLVDWLPWNHT--FggnHNLGIVLYNGGtlYIDDGKPTPgG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 362 TDTTARphgDLLTFNPSMLAGVPRIFDTLKKAVEAklppvgtlkrqvfDHAyqsrLAalkkgkdtpywnEKVFAapravl 441
Cdd:PRK08180 293 FDETLR---NLREISPTVYFNVPKGWEMLVPALER-------------DAA----LR------------RRFFS------ 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 442 gnRLRIMLSGGGPLSAAT----HEF-VNVVFGRVVI--GYGLTETicvgaiqipGDTETNVTGLME---------PGQEI 505
Cdd:PRK08180 335 --RLKLLFYAGAALSQDVwdrlDRVaEATCGERIRMmtGLGMTET---------APSATFTTGPLSragniglpaPGCEV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 506 KLLDIDEykhtdtpepRGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFtAD------GKM---RI------- 569
Cdd:PRK08180 404 KLVPVGG---------KLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRF-VDpadperGLMfdgRIaedfkls 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 570 ------VG--RVKALAKncLGEYIAlealEAVYSGNELlqpNGVCVLVHPDKPYITALALTDEARATSFAAKHgiegtyP 641
Cdd:PRK08180 474 sgtwvsVGplRARAVSA--GAPLVQ----DVVITGHDR---DEIGLLVFPNLDACRRLAGLLADASLAEVLAH------P 538
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398009334 642 ALLkdQRFQQAAAISMADTARASNRasfecVKRVRVIDDEWTPE-NEIlTAAQKLKRRVIDAQYAQTIAELFTDD 715
Cdd:PRK08180 539 AVR--AAFRERLARLNAQATGSSTR-----VARALLLDEPPSLDaGEI-TDKGYINQRAVLARRAALVEALYADE 605
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
279-591 |
4.21e-19 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 92.08 E-value: 4.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 279 DDLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLEPrVVDLLgqphSDDVYLSYLPMAHimEFTITnlfifrgafIGFGTP 358
Cdd:PRK08043 365 EDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKT-IADFT----PNDRFMSALPLFH--SFGLT---------VGLFTP 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 359 rtltdttarphgdLLTfnpsmlaGVpRIFdtlkkaveakLPPVGTLKRQVFDHAYQSRLAALKkGKDTPYWNEKVFAAPR 438
Cdd:PRK08043 429 -------------LLT-------GA-EVF----------LYPSPLHYRIVPELVYDRNCTVLF-GTSTFLGNYARFANPY 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 439 AVLgnRLRIMLSGGGPLSAATHEFVNVVFG-RVVIGYGLTETICVGAIQIPGDTETNVTGLMEPGQEIKLLDIDEYKHTd 517
Cdd:PRK08043 477 DFA--RLRYVVAGAEKLQESTKQLWQDKFGlRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEQG- 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 518 tpeprGEMLSRGPYLFKGYYK----------QPELTREVLdEDGWFHTGDVGSFTADGKMRIVGRVKALAKnCLGEYIAL 587
Cdd:PRK08043 554 -----GRLQLKGPNIMNGYLRvekpgvlevpTAENARGEM-ERGWYDTGDIVRFDEQGFVQIQGRAKRFAK-IAGEMVSL 626
|
....
gi 398009334 588 EALE 591
Cdd:PRK08043 627 EMVE 630
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
136-574 |
5.44e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 90.82 E-value: 5.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 136 TYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIgiygiwscsAVAATVYANLGEAALaHALHETESQAILCGSA 215
Cdd:PRK06188 39 TYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLM---------AIGAAQLAGLRRTAL-HPLGSLDDHAYVLEDA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 216 NVanvlklmkngvmpQVPIIYVGTLPASLDTHGVQVVSFKQVEMIGAAH-----LEGGAAKGTGPLND----DDLALIMY 286
Cdd:PRK06188 109 GI-------------STLIVDPAPFVERALALLARVPSLKHVLTLGPVPdgvdlLAAAAKFGPAPLVAaalpPDIAGLAY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 287 TSGTTGDPKGVMHTHRTLAAGLHTL--------EPRvvdllgqphsddvYLSYLPMAHIMEFTITNLfIFRGAFI----G 354
Cdd:PRK06188 176 TGGTTGKPKGVMGTHRSIATMAQIQlaewewpaDPR-------------FLMCTPLSHAGGAFFLPT-LLRGGTVivlaK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 355 FgTPRTLTDTTARPHGDLLTFNPSMLAGVprifdtlkkaveaklppvgtlkrqvFDHAYQSR--LAALkkgkdtpywnEK 432
Cdd:PRK06188 242 F-DPAEVLRAIEEQRITATFLVPTMIYAL-------------------------LDHPDLRTrdLSSL----------ET 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 433 VFAAPRAVLGNRLRIMLSGGGPlsaathefvnvVFGRVvigYGLTE---TICV--GAIQIPGDTETNVT-GLMEPGQEIK 506
Cdd:PRK06188 286 VYYGASPMSPVRLAEAIERFGP-----------IFAQY---YGQTEapmVITYlrKRDHDPDDPKRLTScGRPTPGLRVA 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398009334 507 LLDiDEYKHTDTPEPrGEMLSRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGRVK 574
Cdd:PRK06188 352 LLD-EDGREVAQGEV-GEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKK 416
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
135-574 |
7.15e-19 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 90.85 E-value: 7.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCgS 214
Cdd:PRK07059 49 ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVV-L 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 ANVANVLKlmknGVMPQVPI--IYVGTLPASLDTHGVQV-------------------VSFKQVemigaahLEGGAAKGT 273
Cdd:PRK07059 128 ENFATTVQ----QVLAKTAVkhVVVASMGDLLGFKGHIVnfvvrrvkkmvpawslpghVRFNDA-------LAEGARQTF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 274 GP--LNDDDLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLEPRVVDLLGQPHSDD--VYLSYLPMAHIMEFTITNLFIFR 349
Cdd:PRK07059 197 KPvkLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAFEKKPRPDqlNFVCALPLYHIFALTVCGLLGMR 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 350 GAFIGfgtprtltdttarphgdLLTFNPSMLAGVPRifdTLKKAVEAKLPPVGTLKRQVFDHAYQSRLAalkkgkdtpyw 429
Cdd:PRK07059 277 TGGRN-----------------ILIPNPRDIPGFIK---ELKKYQVHIFPAVNTLYNALLNNPDFDKLD----------- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 430 nekvFAapravlgnRLRIMLSGGGPLSAATHE-FVNVVFGRVVIGYGLTETICVGAIQIPGDTE-TNVTGLMEPGQEIKL 507
Cdd:PRK07059 326 ----FS--------KLIVANGGGMAVQRPVAErWLEMTGCPITEGYGLSETSPVATCNPVDATEfSGTIGLPLPSTEVSI 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398009334 508 LDiDEYKHTDTPEPrGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVK 574
Cdd:PRK07059 394 RD-DDGNDLPLGEP-GEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKK 458
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
135-634 |
1.07e-18 |
|
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: 89.29 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGS 214
Cdd:cd17653 23 LTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLLTTD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 AnvanvlklmkngvmpqvpiiyvgtlpasldthgvqvvsfkqvemigaahleggaakgtgplnDDDLALIMYTSGTTGDP 294
Cdd:cd17653 103 S--------------------------------------------------------------PDDLAYIIFTSGSTGIP 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 295 KGVMHTHRTLAAGLHTLEPRvvdLLGQPHSDdvylsylpMAHIMEFT----ITNLF--IFRGAFIGFGTPRTLTDTTARP 368
Cdd:cd17653 121 KGVMVPHRGVLNYVSQPPAR---LDVGPGSR--------VAQVLSIAfdacIGEIFstLCNGGTLVLADPSDPFAHVART 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 369 hGDLLTFNPSMLAgvprifdtlkkaveaklppvgTLKRQVFDhayqsrlaalkkgkdtpywnekvfaapravlgnRLRIM 448
Cdd:cd17653 190 -VDALMSTPSILS---------------------TLSPQDFP---------------------------------NLKTI 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 449 LSGGGPLSAathefvNVV----FGRVVI-GYGLTETICVGAIQIPGDTETNVTGLMEPGQEIKLLDIDEykhTDTPEPR- 522
Cdd:cd17653 215 FLGGEAVPP------SLLdrwsPGRRLYnAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCYILDADL---QPVPEGVv 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 523 GEMLSRGPYLFKGYYKQPELT----REVLDEDGW--FHTGDVGSFTADGKMRIVGRVKALAKNcLGEYIALEALEAVYsg 596
Cdd:cd17653 286 GEICISGVQVARGYLGNPALTaskfVPDPFWPGSrmYRTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEIEEVV-- 362
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 398009334 597 neLLQPNGV---CVLVHPDKpyITALALT---DEARATSFAAKH 634
Cdd:cd17653 363 --LQSQPEVtqaAAIVVNGR--LVAFVTPetvDVDGLRSELAKH 402
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
136-574 |
2.00e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 89.24 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 136 TYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCG-- 213
Cdd:PRK08162 45 TWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDte 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 214 -SANVANVLKLMKNgvmPQVPIIYVgTLPAsldthgvqvvsFKQVEMIGAAHLEGGAAKGtgplnDDDLALIM------- 285
Cdd:PRK08162 125 fAEVAREALALLPG---PKPLVIDV-DDPE-----------YPGGRFIGALDYEAFLASG-----DPDFAWTLpadewda 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 286 ----YTSGTTGDPKGVMHTHR---------TLAAGLhtleprvvdllgQPHSddVYLSYLPMAHI----MEFTI-----T 343
Cdd:PRK08162 185 ialnYTSGTTGNPKGVVYHHRgaylnalsnILAWGM------------PKHP--VYLWTLPMFHCngwcFPWTVaaragT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 344 NLFIFRGafigfgTPRTLTDTTARpHGdlltfnPSMLAGVPRIFDTLKKAVEAKlppvgtlkRQVFDHAYQSRLAALkkg 423
Cdd:PRK08162 251 NVCLRKV------DPKLIFDLIRE-HG------VTHYCGAPIVLSALINAPAEW--------RAGIDHPVHAMVAGA--- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 424 kdtpywnekvfAAPRAVLGNRLRIMLSgggplsaATHEfvnvvfgrvvigYGLTET---ICVGAIQ-----IPGDTETNV 495
Cdd:PRK08162 307 -----------APPAAVIAKMEEIGFD-------LTHV------------YGLTETygpATVCAWQpewdaLPLDERAQL 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 496 T---GLMEPGQE-IKLLDIDeykhTDTPEPR-----GEMLSRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGK 566
Cdd:PRK08162 357 KarqGVRYPLQEgVTVLDPD----TMQPVPAdgetiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGY 431
|
....*...
gi 398009334 567 MRIVGRVK 574
Cdd:PRK08162 432 IKIKDRSK 439
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
209-592 |
4.63e-18 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 89.25 E-value: 4.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 209 AILCGSANVANVLKLMKngvMPQVPIIY----------VGTLPASLDThGVQVVSFKQV-EMIGAAHLEGGAAKGTGPL- 276
Cdd:PRK06814 710 AMINFSAGIANILSACK---AAQVKTVLtsrafiekarLGPLIEALEF-GIRIIYLEDVrAQIGLADKIKGLLAGRFPLv 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 277 -----NDDDLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLEPRVvDLlgqpHSDDVYLSYLPMAHimeftitnlfifrga 351
Cdd:PRK06814 786 yfcnrDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARI-DF----SPEDKVFNALPVFH--------------- 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 352 fiGFGtprtLTDttarphGDLLTfnpsMLAGVPrIFdtlkkaveakLPPVGTLKRQVFDHAYQSRlAALKKGKDTpywne 431
Cdd:PRK06814 846 --SFG----LTG------GLVLP----LLSGVK-VF----------LYPSPLHYRIIPELIYDTN-ATILFGTDT----- 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 432 kvFAAPRAVLGN-----RLRIMLSGGGPLSAATHEFVNVVFG-RVVIGYGLTETICVGAIQIPGDTETNVTGLMEPGQEI 505
Cdd:PRK06814 893 --FLNGYARYAHpydfrSLRYVFAGAEKVKEETRQTWMEKFGiRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEY 970
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 506 KLLD---IDEykhtdtpepRGEMLSRGPYLFKGYYK-------QPEltrevldEDGWFHTGDVGSFTADGKMRIVGRVKA 575
Cdd:PRK06814 971 RLEPvpgIDE---------GGRLFVRGPNVMLGYLRaenpgvlEPP-------ADGWYDTGDIVTIDEEGFITIKGRAKR 1034
|
410
....*....|....*..
gi 398009334 576 LAKnCLGEYIALEALEA 592
Cdd:PRK06814 1035 FAK-IAGEMISLAAVEE 1050
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
130-576 |
8.64e-18 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 87.70 E-value: 8.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 130 DEVVYVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGiwscSAVAATVYA---NLGEAALAHALHETE 206
Cdd:PRK07529 54 DRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG----GEAAGIANPinpLLEPEQIAELLRAAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 207 SQAILCGSA--------NVANVLKLMKN-------GVMPQVPIIYVGTLPASLDTHGVQVVSFKQvEMigaAHLEGGAAK 271
Cdd:PRK07529 130 AKVLVTLGPfpgtdiwqKVAEVLAALPElrtvvevDLARYLPGPKRLAVPLIRRKAHARILDFDA-EL---ARQPGDRLF 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 272 GTGPLNDDDLALIMYTSGTTGDPKGVMHTHRTLAA---GLHTLeprvvdLLGQPhsDDVYLSYLPMAHIMEFTITNLF-I 347
Cdd:PRK07529 206 SGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVAnawLGALL------LGLGP--GDTVFCGLPLFHVNALLVTGLApL 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 348 FRGAFIGFGTPRTLTDTTARPH--GDLLTFNPSMLAGVPRIFDTLkkaveaklppvgtLKRQVFDHAYQSrlaalkkgkd 425
Cdd:PRK07529 278 ARGAHVVLATPQGYRGPGVIANfwKIVERYRINFLSGVPTVYAAL-------------LQVPVDGHDISS---------- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 426 tpywnekvfaapravlgnrLRIMLSGGGPLSAATHE-FVNVVFGRVVIGYGLTETICVGAIQIP-GDTETNVTGLMEPGQ 503
Cdd:PRK07529 335 -------------------LRYALCGAAPLPVEVFRrFEAATGVRIVEGYGLTEATCVSSVNPPdGERRIGSVGLRLPYQ 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398009334 504 EIKLLDIDE---YKHTDTPEPRGEMLSRGPYLFKGYYkQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKAL 576
Cdd:PRK07529 396 RVRVVILDDagrYLRDCAVDEVGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDL 470
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
135-573 |
9.53e-18 |
|
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: 86.43 E-value: 9.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGS 214
Cdd:cd05930 13 LTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLVLTDP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 anvanvlklmkngvmpqvpiiyvgtlpasldthgvqvvsfkqvemigaahleggaakgtgplndDDLALIMYTSGTTGDP 294
Cdd:cd05930 93 ----------------------------------------------------------------DDLAYVIYTSGSTGKP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 295 KGVMHTHRTLAAGLHTLEPRVvdllgQPHSDDVYLSYLPMAHIMefTITNLFifrGAFIGFGT-----------PRTLTD 363
Cdd:cd05930 109 KGVMVEHRGLVNLLLWMQEAY-----PLTPGDRVLQFTSFSFDV--SVWEIF---GALLAGATlvvlpeevrkdPEALAD 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 364 TTARPHGDLLTFNPSMLagvprifdtlkkaveaklppvgtlkRQVFDHAYQSRLAalkkgkdtpywnekvfaapravlgn 443
Cdd:cd05930 179 LLAEEGITVLHLTPSLL-------------------------RLLLQELELAALP------------------------- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 444 RLRIMLSGGGPLSAAT-HEFVNVVFGRVVI-GYGLTE-TICVGAIQIPGD--TETNVT-GLMEPGQEIKLLDiDEYKhtd 517
Cdd:cd05930 209 SLRLVLVGGEALPPDLvRRWRELLPGARLVnLYGPTEaTVDATYYRVPPDdeEDGRVPiGRPIPNTRVYVLD-ENLR--- 284
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398009334 518 tPEPRGEM----LSrGPYLFKGYYKQPELTREVLDEDGWFH------TGDVGSFTADGKMRIVGRV 573
Cdd:cd05930 285 -PVPPGVPgelyIG-GAGLARGYLNRPELTAERFVPNPFGPgermyrTGDLVRWLPDGNLEFLGRI 348
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
279-605 |
9.66e-18 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 87.16 E-value: 9.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 279 DDLALIMYTSGTTGDPKGVMHTHRTLAAglHTLEPrvVDLLGQpHSDDVYLSYLPMAHI--MEFTITNLFIfrGAfigfg 356
Cdd:PLN02860 172 DDAVLICFTSGTTGRPKGVTISHSALIV--QSLAK--IAIVGY-GEDDVYLHTAPLCHIggLSSALAMLMV--GA----- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 357 tprtltdttarPHGDLLTFNPSMlagvprIFDTLKKAVEAKLPPVGTLKRQVFdhayqsRLAALKKgkdtpywNEKVFAA 436
Cdd:PLN02860 240 -----------CHVLLPKFDAKA------ALQAIKQHNVTSMITVPAMMADLI------SLTRKSM-------TWKVFPS 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 437 pravlgnrLRIMLSGGGPLSAATHEFVNVVFGRVVI--GYGLTETiC----------------VGAIQIPGDTETNVTGL 498
Cdd:PLN02860 290 --------VRKILNGGGSLSSRLLPDAKKLFPNAKLfsAYGMTEA-CssltfmtlhdptlespKQTLQTVNQTKSSSVHQ 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 499 ME--------PGQEIKLldideykHTDTPEPRGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIV 570
Cdd:PLN02860 361 PQgvcvgkpaPHVELKI-------GLDESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLI 433
|
330 340 350
....*....|....*....|....*....|....*
gi 398009334 571 GRVKALAKNClGEYIALEALEAVysgneLLQPNGV 605
Cdd:PLN02860 434 GRSNDRIKTG-GENVYPEEVEAV-----LSQHPGV 462
|
|
| DHB_AMP_lig |
TIGR02275 |
2,3-dihydroxybenzoate-AMP ligase; Proteins in this family belong to the AMP-binding enzyme ... |
136-624 |
2.41e-17 |
|
2,3-dihydroxybenzoate-AMP ligase; Proteins in this family belong to the AMP-binding enzyme family (pfam00501). Members activate 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate; many are involved in synthesis of siderophores such as enterobactin, vibriobactin, vulnibactin, etc. The most closely related proteine believed to differ in function activates salicylate rather than DHB. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 274063 [Multi-domain] Cd Length: 526 Bit Score: 85.61 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 136 TYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIY-----GIWSCSAVAA------TVYANLGEAAL-----A 199
Cdd:TIGR02275 50 SYRELDQRADNLAAGLTKLGIKQGDTAVVQLPNIAEFYIVFFallklGVAPVLALFShrkselTAYASQIEPALyiidrA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 200 HALHETESQAilcgsanvanvLKLMKNGVMPQVpIIYVGTLPASLDTHgvqvvsfkqvemigaaHLEGGAAKGTGPLND- 278
Cdd:TIGR02275 130 HSLFDYDDFA-----------RQLQSKLPTLRN-IIVAGQTGEAELFL----------------WLESPAEPVKFPPTKs 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 279 DDLALIMYTSGTTGDPKGVMHTHRTLAAGLHtlepRVVDLLGQPHSDdVYLSYLPMAHIMEFTITNLFifrGAFIGFGTP 358
Cdd:TIGR02275 182 DEVAFFQLSGGSTGTPKLIPRTHNDYYYSVR----RSVEICWLTQQT-RYLCALPAAHNYPLSSPGAL---GVFYAGGCV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 359 rtltdttarphgdLLTFNPSMLAGVPRIfDTLKKAVEAKLPPVGTLKRQvfdhAYQSRLAALKKgkdtpywnekvfaapr 438
Cdd:TIGR02275 254 -------------VLAPDPSPTDCFPLI-ERHKVTVTALVPPAVALWMQ----AASKSRADLSS---------------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 439 avlgnrLRIMLSGGGPLSAATHEFVNVVFG-RVVIGYGLTE-TICVGAIQIPGDTETNVTGL-MEPGQEIKLLDIDeykh 515
Cdd:TIGR02275 300 ------LKLLQVGGAKFSAAAARRVPAVFGcQLQQVFGMAEgLVNYTRLDDPAEIIFTTQGRpMSPDDEVRVVDDH---- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 516 tDTPEPRGE---MLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKAlAKNCLGEYIALEALEa 592
Cdd:TIGR02275 370 -GNPVAPGEtgmLLTRGPYTFRGYYKAPEHNAAAFDAEGFYYTGDLVRLTPEGYIVVVGRAKD-QINRGGEKIAAEEIE- 446
|
490 500 510
....*....|....*....|....*....|..
gi 398009334 593 vysgNELLQpngvcvlvHPDKPYITALALTDE 624
Cdd:TIGR02275 447 ----NLLLA--------HPAVHDAALVSMPDE 466
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
135-572 |
4.18e-17 |
|
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: 84.31 E-value: 4.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCgs 214
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 anvanvlklmkngvmpqvpiiyvgtlpasldthgvqvvsfkqvemigaahleggaakgtgplNDDDLALIMYTSGTTGDP 294
Cdd:cd05972 79 --------------------------------------------------------------DAEDPALIYFTSGTTGLP 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 295 KGVMHTHRTLAAGLHTLEpRVVDLlgqpHSDDVYLSylpmahimeftitnlfifrgafigfgtprtlTDTTARPHGDLLT 374
Cdd:cd05972 97 KGVLHTHSYPLGHIPTAA-YWLGL----RPDDIHWN-------------------------------IADPGWAKGAWSS 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 375 FNPSMLAGVPRIFDTLKKAVEAKLppVGTLKRqvfdhayqsrlaalkkgkdtpyWNEKVFAAPRAVLG------------ 442
Cdd:cd05972 141 FFGPWLLGATVFVYEGPRFDAERI--LELLER----------------------YGVTSFCGPPTAYRmlikqdlssykf 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 443 NRLRIMLSGGGPLSAATHEFVNVVFGRVVI-GYGLTETICVGAIQIPGDTETNVTGLMEPGQEIKLLDiDEYKHTDTPEP 521
Cdd:cd05972 197 SHLRLVVSAGEPLNPEVIEWWRAATGLPIRdGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIID-DDGRELPPGEE 275
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 398009334 522 rGEM-LSRGPY-LFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGR 572
Cdd:cd05972 276 -GDIaIKLPPPgLFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGR 326
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
276-629 |
4.87e-17 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 84.94 E-value: 4.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 276 LNDDDlALIMYTSGTTGDPKGVMHTHRTLAAGLHT------LEPRvvdllgqphsdDVYLSYLPMAHimeftitnlfifr 349
Cdd:PRK05852 174 LRPDD-AMIMFTGGTTGLPKMVPWTHANIASSVRAiitgyrLSPR-----------DATVAVMPLYH------------- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 350 gafiGFGTPRTLTDTTARPHGDLLtfnPSMLAGVPRIF-DTLKKAVEAKLPPVGTLKRQVFDHAyqsrlaalkkgkdtpy 428
Cdd:PRK05852 229 ----GHGLIAALLATLASGGAVLL---PARGRFSAHTFwDDIKAVGATWYTAVPTIHQILLERA---------------- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 429 wNEKVFAAPRAvlgnRLRIMLSGGGPLSAATHEFVNVVFGR-VVIGYGLTET---ICVGAIQIPGDTETNV--TGLM--E 500
Cdd:PRK05852 286 -ATEPSGRKPA----ALRFIRSCSAPLTAETAQALQTEFAApVVCAFGMTEAthqVTTTQIEGIGQTENPVvsTGLVgrS 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 501 PGQEIKLLDIDeyKHTDTPEPRGEMLSRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGRVKALAkNC 580
Cdd:PRK05852 361 TGAQIRIVGSD--GLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELI-NR 436
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 398009334 581 LGEYIALEALEAVYSGNellqPN--GVCVLVHPDKPY---ITALALTDEARATS 629
Cdd:PRK05852 437 GGEKISPERVEGVLASH----PNvmEAAVFGVPDQLYgeaVAAVIVPRESAPPT 486
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
279-612 |
5.99e-17 |
|
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: 84.07 E-value: 5.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 279 DDLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLEPRVVdllgQPHSDDVYLSYLPMAHIMEFTITNLFIFR--GAFIGF- 355
Cdd:cd05958 97 DDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVL----RLREDDRFVGSPPLAFTFGLGGVLLFPFGvgASGVLLe 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 356 -GTPRTLTDTTARphgdlltFNPSMLAGVPrifdTLKKAVEAKLPpvgtlkrqvfdhayqsrlaalkkgkdtpywnekvF 434
Cdd:cd05958 173 eATPDLLLSAIAR-------YKPTVLFTAP----TAYRAMLAHPD----------------------------------A 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 435 AAPravLGNRLRIMLSGGGPLSAATHEFVNVVFGRVVI-GYGLTETICVGAIQIPGDTETNVTGLMEPGQEIKLLDiDEY 513
Cdd:cd05958 208 AGP---DLSSLRKCVSAGEALPAALHRAWKEATGIPIIdGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD-DEG 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 514 KhtdtPEPRGEM---LSRGPylfKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKALAKNClGEYIALEAL 590
Cdd:cd05958 284 N----PVPDGTIgrlAVRGP---TGCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEV 355
|
330 340
....*....|....*....|....*
gi 398009334 591 EAVysgneLLQPNGV--CVLV-HPD 612
Cdd:cd05958 356 EDV-----LLQHPAVaeCAVVgHPD 375
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
499-612 |
3.39e-16 |
|
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: 82.12 E-value: 3.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 499 MEPGQEIKLLDIDeykhtDTPEPRGE---MLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKA 575
Cdd:COG1021 359 ISPDDEVRIVDED-----GNPVPPGEvgeLLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKD 433
|
90 100 110
....*....|....*....|....*....|....*..
gi 398009334 576 LAkNCLGEYIALEALEavysgnELLqpngvcvLVHPD 612
Cdd:COG1021 434 QI-NRGGEKIAAEEVE------NLL-------LAHPA 456
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
499-624 |
3.48e-16 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 81.96 E-value: 3.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 499 MEPGQEIKLLDIDeykhtDTPEPRGE---MLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKA 575
Cdd:PRK10946 359 MSPDDEVWVADAD-----GNPLPQGEvgrLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD 433
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 398009334 576 lAKNCLGEYIALEALEavysgNELLQpngvcvlvHPDKPYITALALTDE 624
Cdd:PRK10946 434 -QINRGGEKIAAEEIE-----NLLLR--------HPAVIHAALVSMEDE 468
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
279-576 |
4.26e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 80.60 E-value: 4.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 279 DDLALIMYTSGTTGDPKGVMHTHRTLAAglhtlEPRVVDLLGQPHSDDVYLSYLPMAHIMEFTITNLF-IFRGAFIGFGT 357
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVY-----NAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTpLASGAHVVLAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 358 PRTLTDttarphgdlltfnpsmlagvPRIFDTLKKAVEaklppvgtlkrqvfdhayQSRLAALKKgkdTPywneKVFAAP 437
Cdd:cd05944 77 PAGYRN--------------------PGLFDNFWKLVE------------------RYRITSLST---VP----TVYAAL 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 438 RAVLGNR----LRIMLSGGGPLSAATHEFVNVVFG-RVVIGYGLTETICVGAIQIP-GDTETNVTGLMEPGQEIKLLDID 511
Cdd:cd05944 112 LQVPVNAdissLRFAMSGAAPLPVELRARFEDATGlPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKVLD 191
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398009334 512 EYKHTD---TPEPRGEMLSRGPYLFKGYYKQpELTREVLDEDGWFHTGDVGSFTADGKMRIVGRVKAL 576
Cdd:cd05944 192 GVGRLLrdcAPDEVGEICVAGPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDL 258
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
135-572 |
4.58e-16 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 81.32 E-value: 4.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGS 214
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 AnvanvlklmkngvmpqvpiiyvgtlpasldthgvqvvsfkqvemigaahleggaakgtgplndDDLALIMYTSGTTGDP 294
Cdd:cd05971 87 S---------------------------------------------------------------DDPALIIYTSGTTGPP 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 295 KGVMHTHRTLAAGLHTLEpRVVDLLgqPHSDDVYlsylpmahimeFTITNLfifrgAFIGfgtprtltdttarphGDLLT 374
Cdd:cd05971 104 KGALHAHRVLLGHLPGVQ-FPFNLF--PRDGDLY-----------WTPADW-----AWIG---------------GLLDV 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 375 FNPSMLAGVP------------RIFDTLK--KAVEAKLPPvgtlkrqvfdhayqsrlAALKKGKDTPywnekvfaAPRAV 440
Cdd:cd05971 150 LLPSLYFGVPvlahrmtkfdpkAALDLMSryGVTTAFLPP-----------------TALKMMRQQG--------EQLKH 204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 441 LGNRLRIMLSGGGPLSAathefVNVVFGRVVIG------YGLTET-ICVGAIQIPGDTETNVTGLMEPGQEIKLLDiDEy 513
Cdd:cd05971 205 AQVKLRAIATGGESLGE-----ELLGWAREQFGvevnefYGQTECnLVIGNCSALFPIKPGSMGKPIPGHRVAIVD-DN- 277
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398009334 514 khtDTPEPRGE-----MLSRGPYLFKGYYKQPELTREVLDEDgWFHTGDVGSFTADGKMRIVGR 572
Cdd:cd05971 278 ---GTPLPPGEvgeiaVELPDPVAFLGYWNNPSATEKKMAGD-WLLTGDLGRKDSDGYFWYVGR 337
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
135-573 |
1.98e-15 |
|
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: 80.67 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVaatvY----ANLGEAALAHALHETESQAI 210
Cdd:COG1020 502 LTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAA----YvpldPAYPAERLAYMLEDAGARLV 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 211 LCGSAnvanvlklmkngvmpqvpiiyvgtLPASLDTHGVQVVSFKQVEMIGAAhleggAAKGTGPLNDDDLALIMYTSGT 290
Cdd:COG1020 578 LTQSA------------------------LAARLPELGVPVLALDALALAAEP-----ATNPPVPVTPDDLAYVIYTSGS 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 291 TGDPKGVMHTHRTLAAGLHTLEPRVvdllgQPHSDDVYLSYLPMAhimeFTITNLFIFrGAFIGFGT-----------PR 359
Cdd:COG1020 629 TGRPKGVMVEHRALVNLLAWMQRRY-----GLGPGDRVLQFASLS----FDASVWEIF-GALLSGATlvlappearrdPA 698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 360 TLTDTTARPHGDLLTFNPSMLagvprifdtlkkaveaklppvgtlkrQVFDHAYQSRLAalkkgkdtpywnekvfaapra 439
Cdd:COG1020 699 ALAELLARHRVTVLNLTPSLL--------------------------RALLDAAPEALP--------------------- 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 440 vlgnRLRIMLSGGGPLSAAT-HEFVNVVFGRVVI-GYGLTE-TICVGAIQIPGDTETNVT---GLMEPGQEIKLLDidey 513
Cdd:COG1020 732 ----SLRLVLVGGEALPPELvRRWRARLPGARLVnLYGPTEtTVDSTYYEVTPPDADGGSvpiGRPIANTRVYVLD---- 803
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 514 kHTDTPEP---RGEMLSRGPYLFKGYYKQPELTREV-----LDEDG--WFHTGDVGSFTADGKMRIVGRV 573
Cdd:COG1020 804 -AHLQPVPvgvPGELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRA 872
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
135-593 |
3.29e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 78.77 E-value: 3.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGS 214
Cdd:PRK06145 28 ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 ANVANVLklmkngvmpqvpiiyVGTLPASLDTHGVQVVSfkqveMIGAAHLEGGAAKGTGPlndDDLALIMYTSGTTGDP 294
Cdd:PRK06145 108 EFDAIVA---------------LETPKIVIDAAAQADSR-----RLAQGGLEIPPQAAVAP---TDLVRLMYTSGTTDRP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 295 KGVMHTHRTLA--AGLHTLEprvvdlLGQPhSDDVYLSYLPMAHIMEFTITNLFIFRgafigfgtprtltdttarpHGDL 372
Cdd:PRK06145 165 KGVMHSYGNLHwkSIDHVIA------LGLT-ASERLLVVGPLYHVGAFDLPGIAVLW-------------------VGGT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 373 LTfnpsmlagVPRIFDTlkkaveaklppvgtlkrqvfdhayQSRLAALKKGKDTPYWNEKVFAAPRAVLGNRLRIMLS-- 450
Cdd:PRK06145 219 LR--------IHREFDP------------------------EAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDsl 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 451 ----GGGP------LSAATHEFVNvvfGRVVIGYGLTETIcvgaiqiPGDTetnvtgLMEPGQEI-------------KL 507
Cdd:PRK06145 267 awciGGGEktpesrIRDFTRVFTR---ARYIDAYGLTETC-------SGDT------LMEAGREIekigstgralahvEI 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 508 LDIDEYKHTDTPEPRGEMLSRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGRVKALAKNClGEYIAL 587
Cdd:PRK06145 331 RIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMIISG-GENIAS 408
|
....*.
gi 398009334 588 EALEAV 593
Cdd:PRK06145 409 SEVERV 414
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
135-573 |
4.05e-15 |
|
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: 78.49 E-value: 4.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGS 214
Cdd:cd12116 13 LSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTDD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 ANVAnvlklmkngvmpqvpiiyvgTLPASLDthgvqvvsfkqVEMIGAAHLEGGAAKGTGPLNDDDLALIMYTSGTTGDP 294
Cdd:cd12116 93 ALPD--------------------RLPAGLP-----------VLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 295 KGVMHTHRTLAAGLHTLEPRVvdllgQPHSDDVYLSYLPMAhimeFTITNLFIFrGAFIGFGTPRTLTDTTARPHGDLL- 373
Cdd:cd12116 142 KGVVVSHRNLVNFLHSMRERL-----GLGPGDRLLAVTTYA----FDISLLELL-LPLLAGARVVIAPRETQRDPEALAr 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 374 ---TFNPSMLAGVPrifdtlkkaveaklppvgTLKRQVFDHAYQSRlaalkkgkdtpywnekvfaapravlgNRLRiMLS 450
Cdd:cd12116 212 lieAHSITVMQATP------------------ATWRMLLDAGWQGR--------------------------AGLT-ALC 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 451 GGGPLSAATHEFVNVVFGRVVIGYGLTET--------ICVGAIQIPgdtetnvTGLMEPGQEIKLLDIDEykhtdTPEPR 522
Cdd:cd12116 247 GGEALPPDLAARLLSRVGSLWNLYGPTETtiwstaarVTAAAGPIP-------IGRPLANTQVYVLDAAL-----RPVPP 314
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398009334 523 ---GEMLSRGPYLFKGYYKQPELTREVLDEDG-------WFHTGDVGSFTADGKMRIVGRV 573
Cdd:cd12116 315 gvpGELYIGGDGVAQGYLGRPALTAERFVPDPfagpgsrLYRTGDLVRRRADGRLEYLGRA 375
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
277-611 |
4.27e-15 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 78.91 E-value: 4.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 277 NDDDLALIMYTSGTTGDPKGVMHTHRtlAAGLHTLEPRVVDLLGqphSDDVYLSYLPMAHIMEFTITNLFIFRGafigfG 356
Cdd:PLN03102 184 DEHDPISLNYTSGTTADPKGVVISHR--GAYLSTLSAIIGWEMG---TCPVYLWTLPMFHCNGWTFTWGTAARG-----G 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 357 TPRTLTDTTA-RPHGDLLTFNPSMLAGVPRIFDTLkkaveaklppvgtLKRQVFDHAYQSrlaalkkgkdtpywnekvfa 435
Cdd:PLN03102 254 TSVCMRHVTApEIYKNIEMHNVTHMCCVPTVFNIL-------------LKGNSLDLSPRS-------------------- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 436 APRAVLgnrlrimlSGGGPLSAATHEFVNVVFGRVVIGYGLTETicVGAI----------QIPGDTETNvtglMEPGQEI 505
Cdd:PLN03102 301 GPVHVL--------TGGSPPPAALVKKVQRLGFQVMHAYGLTEA--TGPVlfcewqdewnRLPENQQME----LKARQGV 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 506 KLL---DIDeYKHTDTPE--PR-----GEMLSRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGRVKA 575
Cdd:PLN03102 367 SILglaDVD-VKNKETQEsvPRdgktmGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKD 444
|
330 340 350
....*....|....*....|....*....|....*..
gi 398009334 576 LAKNClGEYI-ALEALEAVYSGNELLQpNGVCVLVHP 611
Cdd:PLN03102 445 IIISG-GENIsSVEVENVLYKYPKVLE-TAVVAMPHP 479
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
280-572 |
1.15e-14 |
|
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: 75.77 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 280 DLALIMYTSGTTGDPKGVMHTHRTL-AAGLHTleprvVDLLGQPHsDDVYLSYLPMAHIMEFTITNLFIFRGA------- 351
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLiAANLQL-----IHAMGLTE-ADVYLNMLPLFHIAGLNLALATFHAGGanvvmek 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 352 FigfgTPRTLTDTTARPHGDLLTFNPSMLAgvpRIFDtlkkAVEAKLPPVGTLkRQVFdhayqsrlaalkkGKDTPywnE 431
Cdd:cd17637 75 F----DPAEALELIEEEKVTLMGSFPPILS---NLLD----AAEKSGVDLSSL-RHVL-------------GLDAP---E 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 432 KVfaapravlgnrlrimlsgggplsAATHEFVNVVFgrvVIGYGLTETICVGAIQiPGDTETNVTGLMEPGQEIKLldID 511
Cdd:cd17637 127 TI-----------------------QRFEETTGATF---WSLYGQTETSGLVTLS-PYRERPGSAGRPGPLVRVRI--VD 177
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398009334 512 EYkhtDTPEPR---GEMLSRGPYLFKGYYKQPELTREVLDeDGWFHTGDVGSFTADGKMRIVGR 572
Cdd:cd17637 178 DN---DRPVPAgetGEIVVRGPLVFQGYWNLPELTAYTFR-NGWHHTGDLGRFDEDGYLWYAGR 237
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
130-574 |
1.73e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 76.96 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 130 DEVVYVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQA 209
Cdd:PRK07768 25 DAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWAEDTLRVI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 210 ILCGSANVanvlkLMKNGVMPQVPIiyvgtlpasLDTHGVQVVSFkqvemigaAHLEGGAAKGTGPLNDDDLALIMYTSG 289
Cdd:PRK07768 105 GMIGAKAV-----VVGEPFLAAAPV---------LEEKGIRVLTV--------ADLLAADPIDPVETGEDDLALMQLTSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 290 TTGDPKGVMHTHRTLAAGLHTLEPRV---VDllgqphsDDVYLSYLPMAHIME----FTITnlfIFRGAFIGFGTPrtlT 362
Cdd:PRK07768 163 STGSPKAVQITHGNLYANAEAMFVAAefdVE-------TDVMVSWLPLFHDMGmvgfLTVP---MYFGAELVKVTP---M 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 363 DTTARPhgdLL------TFNPSMLAGvPrifdTLKKAVEAKLppvgtLKRQVFDHAYQsrLAAlkkgkdtpywnekvfaa 436
Cdd:PRK07768 230 DFLRDP---LLwaelisKYRGTMTAA-P----NFAYALLARR-----LRRQAKPGAFD--LSS----------------- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 437 pravlgnrLRIMLSGGGPLSAATHEFVNVVFGR-------VVIGYGLTET-----------------ICVGAIQI----- 487
Cdd:PRK07768 278 --------LRFALNGAEPIDPADVEDLLDAGARfglrpeaILPAYGMAEAtlavsfspcgaglvvdeVDADLLAAlrrav 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 488 ---PGDTETNVT-GLMEPGQEIKLLDIDeykHTDTPEPR-GEMLSRGPYLFKGyYKQPELTREVLDEDGWFHTGDVGSFT 562
Cdd:PRK07768 350 patKGNTRRLATlGPPLPGLEVRVVDED---GQVLPPRGvGVIELRGESVTPG-YLTMDGFIPAQDADGWLDTGDLGYLT 425
|
490
....*....|..
gi 398009334 563 ADGKMRIVGRVK 574
Cdd:PRK07768 426 EEGEVVVCGRVK 437
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
275-634 |
2.11e-14 |
|
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: 76.21 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 275 PLNDDDLALIMYTSGTTGDPKGVMHTHRtlaaGLHTLEPRVVDLLGQPHSDDVYLsYLPMAhiMEFTITNLFifrgafig 354
Cdd:cd17655 133 VSKSDDLAYVIYTSGSTGKPKGVMIEHR----GVVNLVEWANKVIYQGEHLRVAL-FASIS--FDASVTEIF-------- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 355 fgtprtltdttarphgdlltfnPSMLAGvPRIFDTLKKAVEAKLPPVGTLKRQVFDHAyqsrlaalkkgKDTPYwNEKVF 434
Cdd:cd17655 198 ----------------------ASLLSG-NTLYIVRKETVLDGQALTQYIRQNRITII-----------DLTPA-HLKLL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 435 AAPRAVLGNRLRIMLSGGGPLSAathEFVNVVFGRVVIG------YGLTETiCVGA---IQIPGDTETNVTGLMEPGQEI 505
Cdd:cd17655 243 DAADDSEGLSLKHLIVGGEALST---ELAKKIIELFGTNptitnaYGPTET-TVDAsiyQYEPETDQQVSVPIGKPLGNT 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 506 KLLDIDEYKHtdtPEP---RGEMLSRGPYLFKGYYKQPELTREVLDEDGW------FHTGDVGSFTADGKMRIVGRVKAL 576
Cdd:cd17655 319 RIYILDQYGR---PQPvgvAGELYIGGEGVARGYLNRPELTAEKFVDDPFvpgermYRTGDLARWLPDGNIEFLGRIDHQ 395
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398009334 577 AKnCLGEYIALEALEAVysgneLLQPNGV---CVLVHPDK---PYITALALTDEARATS----FAAKH 634
Cdd:cd17655 396 VK-IRGYRIELGEIEAR-----LLQHPDIkeaVVIARKDEqgqNYLCAYIVSEKELPVAqlreFLARE 457
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
135-698 |
2.99e-14 |
|
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: 76.01 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVsiyldtcvewligiygiwscsavaATVYANLGEAALAH-ALHETES-QAILC 212
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRPGQRV------------------------AVVLPNSVEAVIALlALHRLGAvPALIN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 213 GSANVANVLKLMKNGVMPQVpIIYVGTLPASLD-THGVQVVSFKQVEMIGAAHLEGGAAKGTGPLNDDDlALIMYTSGTT 291
Cdd:cd05923 85 PRLKAAELAELIERGEMTAA-VIAVDAQVMDAIfQSGVRVLALSDLVGLGEPESAGPLIEDPPREPEQP-AFVFYTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 292 GDPKGVMHTHRTLaaglhtlEPRVVDLLGQPH----SDDVYLSYLPMAHIMEFtitnLFIFRGAFIGFGTPRTLTDTTAR 367
Cdd:cd05923 163 GLPKGAVIPQRAA-------ESRVLFMSTQAGlrhgRHNVVLGLMPLYHVIGF----FAVLVAALALDGTYVVVEEFDPA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 368 PHGDLL-TFNPSMLAGVPRIFDTLKKAVEAKLPPVGTLKRQVFDHAyqsrlaalkkgkdtpywnekvfAAPRAVLgNRLR 446
Cdd:cd05923 232 DALKLIeQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGA----------------------TMPDAVL-ERVN 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 447 IMLSGggplsaathEFVNVvfgrvvigYGLTETIcvGAIQIPGDTETNVtglMEPG--QEIKLLDIDEY-KHTDTPEPRG 523
Cdd:cd05923 289 QHLPG---------EKVNI--------YGTTEAM--NSLYMRDARTGTE---MRPGffSEVRIVRIGGSpDEALANGEEG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 524 EML--SRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGRVKalaknclgeyialealEAVYSGNELLQ 601
Cdd:cd05923 347 ELIvaAAADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVD----------------DMIISGGENIH 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 602 PNGV--CVLVHPDKPYITALALTDE---ARATSFAAKHgiEGTYPALLKDQrfqqaaaismadTARASNRASFECVKRVR 676
Cdd:cd05923 410 PSEIerVLSRHPGVTEVVVIGVADErwgQSVTACVVPR--EGTLSADELDQ------------FCRASELADFKRPRRYF 475
|
570 580
....*....|....*....|..
gi 398009334 677 VIDDewTPENeiltAAQKLKRR 698
Cdd:cd05923 476 FLDE--LPKN----AMNKVLRR 491
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
223-572 |
3.82e-14 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 75.42 E-value: 3.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 223 LMKNGVMPQVPIIYvgTLPASLDthgvQVVSFKQVEMIGAAHL----EGGAAKGTGPLND----------DDLALIMYTS 288
Cdd:cd17643 29 LRAEGVGPGDRVAL--ALPRSAE----LIVALLAILKAGGAYVpidpAYPVERIAFILADsgpsllltdpDDLAYVIYTS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 289 GTTGDPKGVMHTHRTLAAgLHTLEPRVVDLlgqpHSDDVYLSYLPMAhiMEFTITNLFifrGAFIgfgtprtltdttarp 368
Cdd:cd17643 103 GSTGRPKGVVVSHANVLA-LFAATQRWFGF----NEDDVWTLFHSYA--FDFSVWEIW---GALL--------------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 369 HGDLLTFNPSMLAGVPRIFDTLKKavEAKLppvgTLKRQVFDHAYQSRLAALKKGKDTPywnekvfaapravlgnRLRIM 448
Cdd:cd17643 158 HGGRLVVVPYEVARSPEDFARLLR--DEGV----TVLNQTPSAFYQLVEAADRDGRDPL----------------ALRYV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 449 LSGGGPLSAATHEFVNVVFG----RVVIGYGLTETiCV-------GAIQIPGDTETNVTGLMePGQEIKLLDIDeykhtD 517
Cdd:cd17643 216 IFGGEALEAAMLRPWAGRFGldrpQLVNMYGITET-TVhvtfrplDAADLPAAAASPIGRPL-PGLRVYVLDAD-----G 288
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398009334 518 TPEPR---GEMLSRGPYLFKGYYKQPELT--REVLDEDG-----WFHTGDVGSFTADGKMRIVGR 572
Cdd:cd17643 289 RPVPPgvvGELYVSGAGVARGYLGRPELTaeRFVANPFGgpgsrMYRTGDLARRLPDGELEYLGR 353
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
136-572 |
4.32e-14 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 74.86 E-value: 4.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 136 TYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCgsa 215
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 216 NVANVLKLmkngvmpqvpiiyvgtlpasldthgvqvvsfkqvemigaahleggaakgtgplnDDDLALIMYTSGTTGDPK 295
Cdd:cd05973 79 DAANRHKL------------------------------------------------------DSDPFVMMFTSGTTGLPK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 296 GVMHTHRTLAAgLHTLEPRVVDLlgqpHSDDVY--LSYLPMAHIMEFTITnlfifrgAFIGFGTPRTLTdttarpHGDLl 373
Cdd:cd05973 105 GVPVPLRALAA-FGAYLRDAVDL----RPEDSFwnAADPGWAYGLYYAIT-------GPLALGHPTILL------EGGF- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 374 tfnpsmlaGVPRIFDTLKKAVEAKLPPVGTlkrqvfdhAYQSRLAAlkkGKDTPywnekvfaaprAVLGNRLRIMLSGGG 453
Cdd:cd05973 166 --------SVESTWRVIERLGVTNLAGSPT--------AYRLLMAA---GAEVP-----------ARPKGRLRRVSSAGE 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 454 PLSAATHEFVNVVFGRVVIG-YGLTET-ICVGAIQIPGD-TETNVTGLMEPGQEIKLLDIDeykhTDTPEPrGEM----- 525
Cdd:cd05973 216 PLTPEVIRWFDAALGVPIHDhYGQTELgMVLANHHALEHpVHAGSAGRAMPGWRVAVLDDD----GDELGP-GEPgrlai 290
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 398009334 526 -LSRGPYL-FKGYYKQPELTRevldEDGWFHTGDVGSFTADGKMRIVGR 572
Cdd:cd05973 291 dIANSPLMwFRGYQLPDTPAI----DGGYYLTGDTVEFDPDGSFSFIGR 335
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
122-572 |
7.86e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 74.69 E-value: 7.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 122 RLMSITHF---------DEVVYV------TYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVA 186
Cdd:PRK07470 5 RVMNLAHFlrqaarrfpDRIALVwgdrswTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 187 ATVYANLGEAALAHALHETESQAILCGSANVANVlKLMKNGVMPQVPIIYVGTLPASLDthgvqvvsfkqVEMIGAAHLe 266
Cdd:PRK07470 85 VPTNFRQTPDEVAYLAEASGARAMICHADFPEHA-AAVRAASPDLTHVVAIGGARAGLD-----------YEALVARHL- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 267 gGAAKGTGPLNDDDLALIMYTSGTTGDPKGVMHTHRTLAaglHTLEPRVVDLL-GQPHsDDVYLSYLPMAHimeftitnl 345
Cdd:PRK07470 152 -GARVANAAVDHDDPCWFFFTSGTTGRPKAAVLTHGQMA---FVITNHLADLMpGTTE-QDASLVVAPLSH--------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 346 fifrGAFIgfgtpRTLTDTtARPHGDLLT----FNP------------SMLAGVPRIfdtLKKAVEAklPPVGTlkrqvF 409
Cdd:PRK07470 218 ----GAGI-----HQLCQV-ARGAATVLLpserFDPaevwalverhrvTNLFTVPTI---LKMLVEH--PAVDR-----Y 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 410 DHAyqsrlaalkkgkdtpywnekvfaapravlgnRLRIMLSGGGPLSAATHEFVNVVFGRVVIGY-GLTEtiCVGAIQI- 487
Cdd:PRK07470 278 DHS-------------------------------SLRYVIYAGAPMYRADQKRALAKLGKVLVQYfGLGE--VTGNITVl 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 488 ------PGD-TETNV--TGLMEPGQEIKLLDiDEYKHTDTPEpRGEMLSRGPYLFKGYYKQPELTREVLdEDGWFHTGDV 558
Cdd:PRK07470 325 ppalhdAEDgPDARIgtCGFERTGMEVQIQD-DEGRELPPGE-TGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDL 401
|
490
....*....|....
gi 398009334 559 GSFTADGKMRIVGR 572
Cdd:PRK07470 402 GHLDARGFLYITGR 415
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
209-613 |
1.74e-13 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 73.37 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 209 AILCGsanvANVLklmknGVMPQVPIIYVGTLPASLD-THGVQVVSFKQVEMIGAAHLEGGAAKGTGPLNDDDLALIMYT 287
Cdd:PRK09029 73 LLQCG----ARVL-----PLNPQLPQPLLEELLPSLTlDFALVLEGENTFSALTSLHLQLVEGAHAVAWQPQRLATMTLT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 288 SGTTGDPKGVMHTHRtlaAGLHTLEPrVVDLLGQPHSDDVYLSyLPMAHIMEFTITNLFIFRGAfigfgtprTLTdttAR 367
Cdd:PRK09029 144 SGSTGLPKAAVHTAQ---AHLASAEG-VLSLMPFTAQDSWLLS-LPLFHVSGQGIVWRWLYAGA--------TLV---VR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 368 PHGDLLtfnpSMLAGVprifdtlkkaVEAKLPPvgT-LKRQVfdhAYQSRLAALKkgkdtpywnekvfaaprAVLgnrlr 446
Cdd:PRK09029 208 DKQPLE----QALAGC----------THASLVP--TqLWRLL---DNRSEPLSLK-----------------AVL----- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 447 imLSGggplSAATHEFVNVVFGRVV---IGYGLTE---TICvgAIQIpgDTETNVtGLMEPGQEIKLLDideykhtdtpe 520
Cdd:PRK09029 247 --LGG----AAIPVELTEQAEQQGIrcwCGYGLTEmasTVC--AKRA--DGLAGV-GSPLPGREVKLVD----------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 521 prGEMLSRGPYLFKGYYKQPELTrEVLDEDGWFHTGDVGSFtADGKMRIVGRvkalAKN---CLGEYIALEALEAVYSGN 597
Cdd:PRK09029 305 --GEIWLRGASLALGYWRQGQLV-PLVNDEGWFATRDRGEW-QNGELTILGR----LDNlffSGGEGIQPEEIERVINQH 376
|
410
....*....|....*.
gi 398009334 598 ELLQPngVCVLVHPDK 613
Cdd:PRK09029 377 PLVQQ--VFVVPVADA 390
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
277-593 |
4.59e-13 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 72.16 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 277 NDDDLALIMYTSGTTGDPKGVMHTHRTLAAGlhtlEPRVVDLLgQPHSDDVYLSYLPMAHIMEFTITNLFifrgafigfg 356
Cdd:PRK06334 181 DPEDVAVILFTSGTEKLPKGVPLTHANLLAN----QRACLKFF-SPKEDDVMMSFLPPFHAYGFNSCTLF---------- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 357 tprtltdttarphgdlltfnpSMLAGVPRIFDT----LKKAVE----AKLPPVGTLKrQVFDHAYQsrlAALKKGKDTPy 428
Cdd:PRK06334 246 ---------------------PLLSGVPVVFAYnplyPKKIVEmideAKVTFLGSTP-VFFDYILK---TAKKQESCLP- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 429 wnekvfaapravlgnRLRIMLSGGGPLSAATHEFVNVVFGRVVI--GYGLTE---TICVGAIQIPGDTEtnVTGLMEPGQ 503
Cdd:PRK06334 300 ---------------SLRFVVIGGDAFKDSLYQEALKTFPHIQLrqGYGTTEcspVITINTVNSPKHES--CVGMPIRGM 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 504 EIKLLDideyKHTDTPEPRGE---MLSRGPYLFKGYYKQPELTREV-LDEDGWFHTGDVGSFTADGKMRIVGRVKALAKn 579
Cdd:PRK06334 363 DVLIVS----EETKVPVSSGEtglVLTRGTSLFSGYLGEDFGQGFVeLGGETWYVTGDLGYVDRHGELFLKGRLSRFVK- 437
|
330
....*....|....
gi 398009334 580 CLGEYIALEALEAV 593
Cdd:PRK06334 438 IGAEMVSLEALESI 451
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
279-634 |
4.91e-13 |
|
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: 71.73 E-value: 4.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 279 DDLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLEpRVVDLLGQPHsddvylSYLPMAHImeftitNLFIFRGAFIgfgtp 358
Cdd:cd17650 93 EDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWR-REYELDSFPV------RLLQMASF------SFDVFAGDFA----- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 359 RTLTD-TTARPHGDLLTFNPSmlagvpRIFDTLKKAVEAKLPPVGTLKRQVFDHAY--QSRLAALK---KGKDTPYWNEK 432
Cdd:cd17650 155 RSLLNgGTLVICPDEVKLDPA------ALYDLILKSRITLMESTPALIRPVMAYVYrnGLDLSAMRlliVGSDGCKAQDF 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 433 VFAAPRavLGNRLRIMLSgggplsaathefvnvvfgrvvigYGLTETiCVGAIQIPGDTETNVTGLMEP-GQEIKLLDID 511
Cdd:cd17650 229 KTLAAR--FGQGMRIINS-----------------------YGVTEA-TIDSTYYEEGRDPLGDSANVPiGRPLPNTAMY 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 512 EYKHTDTPEP---RGEMLSRGPYLFKGYYKQPELTREVLDEDGW------FHTGDVGSFTADGKMRIVGRVKALAKnCLG 582
Cdd:cd17650 283 VLDERLQPQPvgvAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVK-IRG 361
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398009334 583 EYIALEALEAVysgneLLQPNGV---CVLVHPDK-------PYITALALTDEARATSFAAKH 634
Cdd:cd17650 362 FRIELGEIESQ-----LARHPAIdeaVVAVREDKggearlcAYVVAAATLNTAELRAFLAKE 418
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
136-573 |
5.66e-13 |
|
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: 71.76 E-value: 5.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 136 TYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCgsa 215
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 216 nvanvlklmkngvmpqVPIIYVGTLPasldthgvqvvsfkqvemigaahleggaakgtgplndDDLALIMYTSGTTGDPK 295
Cdd:cd05969 79 ----------------TEELYERTDP-------------------------------------EDPTLLHYTSGTTGTPK 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 296 GVMHTHRTLAAGLHTLEpRVVDLlgqpHSDDVYLSYLPMAHIMeftitnlfifrGAFIGFGTPrtltdttarphgdlltf 375
Cdd:cd05969 106 GVLHVHDAMIFYYFTGK-YVLDL----HPDDIYWCTADPGWVT-----------GTVYGIWAP----------------- 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 376 npsMLAGVPRIFDtlkkavEAKLPP---VGTLKRQVFDHAYQSRLA--ALKKGKDTPywnekvfaaPRAVLGNRLRIMLS 450
Cdd:cd05969 153 ---WLNGVTNVVY------EGRFDAeswYGIIERVKVTVWYTAPTAirMLMKEGDEL---------ARKYDLSSLRFIHS 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 451 GGGPLSAATHEFVNVVFG-RVVIGYGLTETicvGAIQI---PG-DTETNVTGLMEPGqeIKLLDIDEYKHTDTPEPRGEM 525
Cdd:cd05969 215 VGEPLNPEAIRWGMEVFGvPIHDTWWQTET---GSIMIanyPCmPIKPGSMGKPLPG--VKAAVVDENGNELPPGTKGIL 289
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 398009334 526 -LSRG-PYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGRV 573
Cdd:cd05969 290 aLKPGwPSMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRA 338
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
136-593 |
6.20e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 71.66 E-value: 6.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 136 TYSEMEERIFHFGAGLAALGVTA---------NG--NVSIYldtcvewligiYGIWSCSAVAATVYANLGEAALAHALHE 204
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPgdrvgtlawNGyrHLEAY-----------YGVSGSGAVCHTINPRLFPEQIAYIVNH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 205 TESQaILCGSANVANVLKlmknGVMPQVPII--YVG-TLPASLDTHGVQVVSFKQVemigaahLEGGAAKGTGPLNDDDL 281
Cdd:PRK07008 110 AEDR-YVLFDLTFLPLVD----ALAPQCPNVkgWVAmTDAAHLPAGSTPLLCYETL-------VGAQDGDYDWPRFDENQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 282 ALIM-YTSGTTGDPKGVMHTHRTLAagLHTLEPRVVDLLGQPHSDDVyLSYLPMAHIMEFTITNLFIFRGAFIGFGTP-- 358
Cdd:PRK07008 178 ASSLcYTSGTTGNPKGALYSHRSTV--LHAYGAALPDAMGLSARDAV-LPVVPMFHVNAWGLPYSAPLTGAKLVLPGPdl 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 359 --RTLTDTTArphGDLLTFNpsmlAGVPRIFDTLKKAVEAKLPPVGTLKRQVFDHAyqsrlaalkkgkdtpywnekvfAA 436
Cdd:PRK07008 255 dgKSLYELIE---AERVTFS----AGVPTVWLGLLNHMREAGLRFSTLRRTVIGGS----------------------AC 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 437 PRAVLgnrlrimlsgggplsaatHEFVNVVFGRVVIGYGLTE-----TICV---GAIQIPGDTETNV---TGLMEPGQEI 505
Cdd:PRK07008 306 PPAMI------------------RTFEDEYGVEVIHAWGMTEmsplgTLCKlkwKHSQLPLDEQRKLlekQGRVIYGVDM 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 506 KLLDIDEYKHTDTPEPRGEMLSRGPYLFKGYYKQPEltrEVLDeDGWFHTGDVGSFTADGKMRIVGRVKALAKNClGEYI 585
Cdd:PRK07008 368 KIVGDDGRELPWDGKAFGDLQVRGPWVIDRYFRGDA---SPLV-DGWFPTGDVATIDADGFMQITDRSKDVIKSG-GEWI 442
|
....*...
gi 398009334 586 ALEALEAV 593
Cdd:PRK07008 443 SSIDIENV 450
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
277-574 |
6.24e-13 |
|
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: 71.75 E-value: 6.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 277 NDDDLALIMYTSGTTGDPKGVMHTHrtlaaglHTLEPRVVDLLGQPH--SDDVYLSYLPMAHIMeftitNLFIFRGAFIG 354
Cdd:cd05908 104 LADELAFIQFSSGSTGDPKGVMLTH-------ENLVHNMFAILNSTEwkTKDRILSWMPLTHDM-----GLIAFHLAPLI 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 355 FGTPRTLTDTTarphgdLLTFNPSMLagvprifdtLKKAVEAKL-----PPVG------TLKRQVFDHAYQSRLAALKKG 423
Cdd:cd05908 172 AGMNQYLMPTR------LFIRRPILW---------LKKASEHKAtivssPNFGykyflkTLKPEKANDWDLSSIRMILNG 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 424 KDtPYWNE--KVFAAPRAVLGNRLRIML--------SGGGPLSAATHEFVNVVFGR--VVIGYGLTETIcvgaiqipgDT 491
Cdd:cd05908 237 AE-PIDYElcHEFLDHMSKYGLKRNAILpvyglaeaSVGASLPKAQSPFKTITLGRrhVTHGEPEPEVD---------KK 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 492 ETNVTGLMEPGQEIKLLDI---DEYKHTDTPEPRGEMLSRGPYLFKGYYKQPELTREVLDEDGWFHTGDVGsFTADGKMR 568
Cdd:cd05908 307 DSECLTFVEVGKPIDETDIricDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRNGRLV 385
|
....*.
gi 398009334 569 IVGRVK 574
Cdd:cd05908 386 ITGREK 391
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
135-572 |
6.51e-13 |
|
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: 71.61 E-value: 6.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALhetesqailcgs 214
Cdd:cd17651 21 LTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFML------------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 ANVANVLKLMKNGVMPQVPIIYVGtlpasldthGVQVVSFKQVEMIGAAHleggaakgTGPLNDDDLALIMYTSGTTGDP 294
Cdd:cd17651 89 ADAGPVLVLTHPALAGELAVELVA---------VTLLDQPGAAAGADAEP--------DPALDADDLAYVIYTSGSTGRP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 295 KGVMHTHRTLA--AGLHTlepRVVDLlgqpHSDDVYLSYLPMAhimeFTITNLFIF----RGAFIGFGTPRTLTDTTArp 368
Cdd:cd17651 152 KGVVMPHRSLAnlVAWQA---RASSL----GPGARTLQFAGLG----FDVSVQEIFstlcAGATLVLPPEEVRTDPPA-- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 369 hgdLLTFnpsmLA--GVPRIFdtlkkaveakLPPVgtLKRQVFDHAyqsrlaalkkgkdtpywnekvfaAPRAVLGNRLR 446
Cdd:cd17651 219 ---LAAW----LDeqRISRVF----------LPTV--ALRALAEHG-----------------------RPLGVRLAALR 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 447 IMLSGGGPLSAAT---HEFVNVVFGRVVIGYGLTETICVGAIQIPGDT----ETNVTGLMEPGQEIKLLDIDeykhtDTP 519
Cdd:cd17651 257 YLLTGGEQLVLTEdlrEFCAGLPGLRLHNHYGPTETHVVTALSLPGDPaawpAPPPIGRPIDNTRVYVLDAA-----LRP 331
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398009334 520 EPR---GEMLSRGPYLFKGYYKQPELTREVLDEDGW------FHTGDVGSFTADGKMRIVGR 572
Cdd:cd17651 332 VPPgvpGELYIGGAGLARGYLNRPELTAERFVPDPFvpgarmYRTGDLARWLPDGELEFLGR 393
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
136-574 |
8.87e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 71.35 E-value: 8.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 136 TYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGSA 215
Cdd:PRK07786 44 TWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 216 nVANVLKLMKNGVMPQVPIIYVGTlpASLDThgvqVVSFKQVEMigaahlEGGAAKGTGPLNDDDLALIMYTSGTTGDPK 295
Cdd:PRK07786 124 -LAPVATAVRDIVPLLSTVVVAGG--SSDDS----VLGYEDLLA------EAGPAHAPVDIPNDSPALIMYTSGTTGRPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 296 GVMHTHRTLAAGLHTLeprvVDLLGQPHSDDVYLSYLPMAHIMefTITNLfifrGAFIGFGTPRTLTDTTArphgdlltF 375
Cdd:PRK07786 191 GAVLTHANLTGQAMTC----LRTNGADINSDVGFVGVPLFHIA--GIGSM----LPGLLLGAPTVIYPLGA--------F 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 376 NPSMLagvpriFDTL--KKAVEAKLPPVgtlkrqvfdhAYQSRLAALKkgkdtpywnekvfAAPRAVlgnRLRIMLSGGG 453
Cdd:PRK07786 253 DPGQL------LDVLeaEKVTGIFLVPA----------QWQAVCAEQQ-------------ARPRDL---ALRVLSWGAA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 454 PLSAATHEFVNVVF--GRVVIGYGLTETICVGAIQIPGDTETNVTGLMEPGQEIKLLDIDEYKHTDTPEPRGEMLSRGPY 531
Cdd:PRK07786 301 PASDTLLRQMAATFpeAQILAAFGQTEMSPVTCMLLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPT 380
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 398009334 532 LFKGYYKQPELTREVLDeDGWFHTGDVGSFTADGKMRIVGRVK 574
Cdd:PRK07786 381 LMSGYWNNPEATAEAFA-GGWFHSGDLVRQDEEGYVWVVDRKK 422
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
136-613 |
2.25e-12 |
|
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: 70.30 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 136 TYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGSA 215
Cdd:cd17634 86 SYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 216 NV-----ANVLKLMKNGVMPQVP----IIYVGTLPASLDTHGVQVVSFKqvEMIGAAhlegGAAKGTGPLNDDDLALIMY 286
Cdd:cd17634 166 GVragrsVPLKKNVDDALNPNVTsvehVIVLKRTGSDIDWQEGRDLWWR--DLIAKA----SPEHQPEAMNAEDPLFILY 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 287 TSGTTGDPKGVMHTHRTLAAGLHTLEPRVVDLlgqpHSDDVYLSYLPMAHIMEftitnlfifrGAFIGFGtPRTLTDTTA 366
Cdd:cd17634 240 TSGTTGKPKGVLHTTGGYLVYAATTMKYVFDY----GPGDIYWCTADVGWVTG----------HSYLLYG-PLACGATTL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 367 rphgdlltfnpsMLAGVPrifdtlkkaveaKLPPVGTLKRQVFDHA----YQSRLA--ALKKgkdtpywnekvfAAPRAV 440
Cdd:cd17634 305 ------------LYEGVP------------NWPTPARMWQVVDKHGvnilYTAPTAirALMA------------AGDDAI 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 441 LG---NRLRIMLSGGGPLSAATHE-FVNVVFGR---VVIGYGLTET---ICV---GAIQIPGDTETNVTglmePGQEIKL 507
Cdd:cd17634 349 EGtdrSSLRILGSVGEPINPEAYEwYWKKIGKEkcpVVDTWWQTETggfMITplpGAIELKAGSATRPV----FGVQPAV 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 508 LdiDEYKHTDTPEPRGEM---LSRGPYLFKGYYKQPELTREVLDE-DGWFHTGDVGSFTADGKMRIVGRVKALAkNCLGE 583
Cdd:cd17634 425 V--DNEGHPQPGGTEGNLvitDPWPGQTRTLFGDHERFEQTYFSTfKGMYFSGDGARRDEDGYYWITGRSDDVI-NVAGH 501
|
490 500 510
....*....|....*....|....*....|
gi 398009334 584 YIALEALEAVYSGNELLQPNGVCVLVHPDK 613
Cdd:cd17634 502 RLGTAEIESVLVAHPKVAEAAVVGIPHAIK 531
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
130-593 |
3.00e-12 |
|
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: 69.43 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 130 DEVVYVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQA 209
Cdd:cd17656 9 FENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 210 ILCgSANVANVLKLMKNGVMPQVPIIYVGtlpaslDTHGVQVVSfkqvemigaahleggaakgtgplNDDDLALIMYTSG 289
Cdd:cd17656 89 VLT-QRHLKSKLSFNKSTILLEDPSISQE------DTSNIDYIN-----------------------NSDDLLYIIYTSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 290 TTGDPKGVMHTHRTLAAGLHtlepRVVDLLGQPHSDDVyLSYLPMAhimeFTITNLFIFRGAFIGfGTPRTLTDTTARPh 369
Cdd:cd17656 139 TTGKPKGVQLEHKNMVNLLH----FEREKTNINFSDKV-LQFATCS----FDVCYQEIFSTLLSG-GTLYIIREETKRD- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 370 gdlltfnpsmlagVPRIFDTLKK-AVEAKLPPVGTLKRQVFDHAYQSRLAALKKgkdtpywnEKVFAAPRAVLGNRLRIM 448
Cdd:cd17656 208 -------------VEQLFDLVKRhNIEVVFLPVAFLKFIFSEREFINRFPTCVK--------HIITAGEQLVITNEFKEM 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 449 LSGGGplsAATHEFvnvvfgrvvigYGLTETICVGAIQI-PGDTETNVTGLMEPGQEIKLLDIDEYKhtdTPEPR---GE 524
Cdd:cd17656 267 LHEHN---VHLHNH-----------YGPSETHVVTTYTInPEAEIPELPPIGKPISNTWIYILDQEQ---QLQPQgivGE 329
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398009334 525 MLSRGPYLFKGYYKQPELTREVLDEDGW------FHTGDVGSFTADGKMRIVGRVKALAKnCLGEYIALEALEAV 593
Cdd:cd17656 330 LYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVK-IRGYRIELGEIEAQ 403
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
135-614 |
3.37e-12 |
|
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: 69.39 E-value: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILcgs 214
Cdd:cd17644 26 LTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYILEDAQISVLL--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 anvanvlklmkngvmpqvpiiyvgtlpasldthgvqvvsfkqvemigaahleggaakgTGPLNdddLALIMYTSGTTGDP 294
Cdd:cd17644 103 ----------------------------------------------------------TQPEN---LAYVIYTSGSTGKP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 295 KGVMHTHRTLAAGLHTLEpRVVDLlgqPHSDdvylsylpmaHIMEFtitnlfifrgAFIGFgtprtltDTTARP------ 368
Cdd:cd17644 122 KGVMIEHQSLVNLSHGLI-KEYGI---TSSD----------RVLQF----------ASIAF-------DVAAEEiyvtll 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 369 HGDLLTFNPSMLagVPRIFDTLKKAVEAKLppvgtlkrQVFD--HAYQSRLAA--LKKGKDTPYWNEKVFAAPRAVLGNR 444
Cdd:cd17644 171 SGATLVLRPEEM--RSSLEDFVQYIQQWQL--------TVLSlpPAYWHLLVLelLLSTIDLPSSLRLVIVGGEAVQPEL 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 445 LRIMLSGGGPLSaathEFVNVvfgrvvigYGLTE-TICVGAIQIPGDTETNVTGLM--EPGQEIKLLDIDEYKHTDTPEP 521
Cdd:cd17644 241 VRQWQKNVGNFI----QLINV--------YGPTEaTIAATVCRLTQLTERNITSVPigRPIANTQVYILDENLQPVPVGV 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 522 RGEMLSRGPYLFKGYYKQPELTREVLDEDGWFH--------TGDVGSFTADGKMRIVGRVKALAKnCLGEYIALEALEAV 593
Cdd:cd17644 309 PGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVK-IRGFRIELGEIEAV 387
|
490 500
....*....|....*....|.
gi 398009334 594 YSGNELLQPngVCVLVHPDKP 614
Cdd:cd17644 388 LSQHNDVKT--AVVIVREDQP 406
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
135-572 |
1.00e-11 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 68.11 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGS 214
Cdd:PRK05857 42 LRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 ANVANVLKLMKngVMPQVPIIYVGTLPASLDTHGVQVVSFKqvemigAAHLEGGAakgtgplnDDDLALImYTSGTTGDP 294
Cdd:PRK05857 122 GSKMASSAVPE--ALHSIPVIAVDIAAVTRESEHSLDAASL------AGNADQGS--------EDPLAMI-FTSGTTGEP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 295 KGVMHTHRTLAAGLHTLEPRVVDLLGQPHSDDVYlSYLPMAHI--MEFTITNLFifRGAFIGFGTPRTLTDTtarphgDL 372
Cdd:PRK05857 185 KAVLLANRTFFAVPDILQKEGLNWVTWVVGETTY-SPLPATHIggLWWILTCLM--HGGLCVTGGENTTSLL------EI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 373 LTFNpsmlagvprifdtlkKAVEAKLPPVgTLKRQVfdhaYQSRLAalkkGKDTPywnekvfaapravlgnRLRIMLSGG 452
Cdd:PRK05857 256 LTTN---------------AVATTCLVPT-LLSKLV----SELKSA----NATVP----------------SLRLVGYGG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 453 GPLSAATHEFVNVVFGRVVIGYGLTETICVgAIQIPGDT------ETNVTGLMEPGQEIKLLDIDEYKHT--DTPEPR-- 522
Cdd:PRK05857 296 SRAIAADVRFIEATGVRTAQVYGLSETGCT-ALCLPTDDgsivkiEAGAVGRPYPGVDVYLAATDGIGPTapGAGPSAsf 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 398009334 523 GEMLSRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGR 572
Cdd:PRK05857 375 GTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGR 423
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
275-574 |
1.69e-11 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 67.23 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 275 PLNDDDLALIMYTSGTTGDPKGVMHTHRTLAAGLHTL------EPRVVDLLGQPhsddVYLSYLP---MAHI---MEFTi 342
Cdd:PRK09274 170 DLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALredygiEPGEIDLPTFP----LFALFGPalgMTSVipdMDPT- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 343 tnlfifRGAFIgfgTPRTLTDTTARphgdlltFNPSMLAGVPRIFDTLKKAVEAKLPPVGTLKRqvfdhayqsrlaalkk 422
Cdd:PRK09274 245 ------RPATV---DPAKLFAAIER-------YGVTNLFGSPALLERLGRYGEANGIKLPSLRR---------------- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 423 gkdtpywnekvfaapravlgnrlriMLSGGGPLSAATHEFVNVVF---GRVVIGYGLTET--IC-VGAIQIPGDTeTNVT 496
Cdd:PRK09274 293 -------------------------VISAGAPVPIAVIERFRAMLppdAEILTPYGATEAlpISsIESREILFAT-RAAT 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 497 --------GLMEPGQEIKLLDIdeykhTDTPEPR------------GEMLSRGPYLFKGYYKQPELTRE--VLDEDG--W 552
Cdd:PRK09274 347 dngagicvGRPVDGVEVRIIAI-----SDAPIPEwddalrlatgeiGEIVVAGPMVTRSYYNRPEATRLakIPDGQGdvW 421
|
330 340
....*....|....*....|..
gi 398009334 553 FHTGDVGSFTADGKMRIVGRVK 574
Cdd:PRK09274 422 HRMGDLGYLDAQGRLWFCGRKA 443
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
196-572 |
2.21e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 67.01 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 196 AALAHALHETESQAILCGSANVAnvlklMKNGVMPQVPIIYVGTLP--ASLDTHGvqvvsfkqvemigaahlegGAAKGT 273
Cdd:PRK07867 91 AALARDIAHADCQLVLTESAHAE-----LLDGLDPGVRVINVDSPAwaDELAAHR-------------------DAEPPF 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 274 GPLNDDDLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLEPRvvdlLGQPHSDDVYLSyLPMAHimeftitnlfifRGAFI 353
Cdd:PRK07867 147 RVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQR----FGLGPDDVCYVS-MPLFH------------SNAVM 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 354 GfgtprtltdttarphgdllTFNPSMLAG----VPRIFdtlkkAVEAKLPPVgtlKRqvFDHAYQSRLaalkkGKDTPYw 429
Cdd:PRK07867 210 A-------------------GWAVALAAGasiaLRRKF-----SASGFLPDV---RR--YGATYANYV-----GKPLSY- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 430 nekVFAAPRAV--LGNRLRIMLSG-GGPlsAATHEFVNVvFG-RVVIGYGLTEticvGAIQIPG--DTETNVTGLMEPGq 503
Cdd:PRK07867 255 ---VLATPERPddADNPLRIVYGNeGAP--GDIARFARR-FGcVVVDGFGSTE----GGVAITRtpDTPPGALGPLPPG- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 504 eIKLLD-----------IDEYKHTDTPEPRGEML-SRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVG 571
Cdd:PRK07867 324 -VAIVDpdtgtecppaeDADGRLLNADEAIGELVnTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAG 401
|
.
gi 398009334 572 R 572
Cdd:PRK07867 402 R 402
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
134-336 |
3.52e-11 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 66.44 E-value: 3.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 134 YVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCG 213
Cdd:PRK08279 62 SISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 214 SANVANVlklmkNGVMPQV---PIIYVGTLPASLDTHGVQVVSfkqvEMIGAAHLEGGAAkgTGPLNDDDLALIMYTSGT 290
Cdd:PRK08279 142 EELVEAF-----EEARADLarpPRLWVAGGDTLDDPEGYEDLA----AAAAGAPTTNPAS--RSGVTAKDTAFYIYTSGT 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 398009334 291 TGDPK-GVMHTHRTLAAG---LHTLEPRvvdllgqphSDDVYLSYLPMAH 336
Cdd:PRK08279 211 TGLPKaAVMSHMRWLKAMggfGGLLRLT---------PDDVLYCCLPLYH 251
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
130-328 |
5.93e-11 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 65.69 E-value: 5.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 130 DEVVYVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQA 209
Cdd:PRK04319 69 SRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 210 ILCGSAnvanvlkLMKNGVMPQVP----IIYVGtlpaSLDTHGVQVVSFKQvEMIGAA-HLEggaakgTGPLNDDDLALI 284
Cdd:PRK04319 149 LITTPA-------LLERKPADDLPslkhVLLVG----EDVEEGPGTLDFNA-LMEQASdEFD------IEWTDREDGAIL 210
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 398009334 285 MYTSGTTGDPKGVMHTHRtlAAGLHTLEPR-VVDLlgqpHSDDVY 328
Cdd:PRK04319 211 HYTSGSTGKPKGVLHVHN--AMLQHYQTGKyVLDL----HEDDVY 249
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
278-573 |
7.45e-11 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 64.30 E-value: 7.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 278 DDDLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLEPRvvdlLGQPHSddvYLSYLPMAHIMEFTItnlfIFRGAFIGFgT 357
Cdd:PRK07824 34 DDDVALVVATSGTTGTPKGAMLTAAALTASADATHDR----LGGPGQ---WLLALPAHHIAGLQV----LVRSVIAGS-E 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 358 PRTLtDTTArphgdllTFNPSMLAGVprifdtlkkaveaklppVGTLKRqvfDHAYQSRLAA-LKKGKDTPywnekvfAA 436
Cdd:PRK07824 102 PVEL-DVSA-------GFDPTALPRA-----------------VAELGG---GRRYTSLVPMqLAKALDDP-------AA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 437 PRAVlgNRLRIMLSGGGPLSAATHEFVNVVFGRVVIGYGLTETI--CVgaiqipgdtetnVTGLMEPGQEIKLLDideyk 514
Cdd:PRK07824 147 TAAL--AELDAVLVGGGPAPAPVLDAAAAAGINVVRTYGMSETSggCV------------YDGVPLDGVRVRVED----- 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 398009334 515 htdtpeprGEMLSRGPYLFKGYYKQPEltREVLDEDGWFHTGDVGSFTaDGKMRIVGRV 573
Cdd:PRK07824 208 --------GRIALGGPTLAKGYRNPVD--PDPFAEPGWFRTDDLGALD-DGVLTVLGRA 255
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
136-592 |
2.51e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 64.21 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 136 TYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGSA 215
Cdd:PRK12316 3084 SYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSH 3163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 216 nvanvLKLmkngvmPQvpiiyvgtlpasldTHGVQVVsfkqveMIGAAHLEGGAAKGTGPLNDDDLALIMYTSGTTGDPK 295
Cdd:PRK12316 3164 -----LRL------PL--------------AQGVQVL------DLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPK 3212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 296 GVMHTHRTLAAGLHTleprVVDLLGQPHSDDVyLSYLPmahimeftitnlFIFRGAFIGFGTPrtltdttarphgdlLTF 375
Cdd:PRK12316 3213 GVGIRHSALSNHLCW----MQQAYGLGVGDRV-LQFTT------------FSFDVFVEELFWP--------------LMS 3261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 376 NPSMLAGVPRIFDTLKKAVEaklppvgTLKRQVFD--HAYQSRLAALkkgkdtpywnekvFAAPRAVLGNRLRIMLSGGG 453
Cdd:PRK12316 3262 GARVVLAGPEDWRDPALLVE-------LINSEGVDvlHAYPSMLQAF-------------LEEEDAHRCTSLKRIVCGGE 3321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 454 PLSAATHEFVNVVfGRVVIGYGLTET-ICVGAIQIPGDTETNV-TGLMEPGQEIKLLDIdeykhTDTPEPRG---EMLSR 528
Cdd:PRK12316 3322 ALPADLQQQVFAG-LPLYNLYGPTEAtITVTHWQCVEEGKDAVpIGRPIANRACYILDG-----SLEPVPVGalgELYLG 3395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 529 GPYLFKGYYKQPELTREVLDEDGW------FHTGDVGSFTADGKMRIVGRVKALAKnCLGEYIALEALEA 592
Cdd:PRK12316 3396 GEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVK-IRGFRIELGEIEA 3464
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
275-572 |
3.07e-10 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 62.86 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 275 PLNDDDlALIMYTSGTTGDPKGVMHTHRTLAAGLHTLEprvvDLLGqPHSDDVYLSYLPmahimeftitnLFIFRGAFIG 354
Cdd:cd05910 82 PKADEP-AAILFTSGSTGTPKGVVYRHGTFAAQIDALR----QLYG-IRPGEVDLATFP-----------LFALFGPALG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 355 FGTPRTLTDTTaRP--------HGDLLTFNPSMLAGVPRIFDTLKKAVEAKLPPVGTLKRQVfdhayqsrlaalkkgkdt 426
Cdd:cd05910 145 LTSVIPDMDPT-RParadpqklVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVL------------------ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 427 pywnekVFAAP-RAVLGNRLRIMLSGGGPlsaathefvnvvfgrVVIGYGLTETICVGAIqipGDTETNVT--------- 496
Cdd:cd05910 206 ------SAGAPvPIALAARLRKMLSDEAE---------------ILTPYGATEALPVSSI---GSRELLATttaatsgga 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 497 ----GLMEPGQEIKLLDIDEykhTDTPE-------PR---GEMLSRGPYLFKGYYKQPELTR--EVLDEDG--WFHTGDV 558
Cdd:cd05910 262 gtcvGRPIPGVRVRIIEIDD---EPIAEwddtlelPRgeiGEITVTGPTVTPTYVNRPVATAlaKIDDNSEgfWHRMGDL 338
|
330
....*....|....
gi 398009334 559 GSFTADGKMRIVGR 572
Cdd:cd05910 339 GYLDDEGRLWFCGR 352
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
135-634 |
3.44e-10 |
|
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: 62.99 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGS 214
Cdd:cd12117 23 LTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLTDR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 ANVANVLKLmkngvmpqvpiiyvgtlpasldthgvqvvsfkQVEMIGAAHLEGGAAKGTGPLND-DDLALIMYTSGTTGD 293
Cdd:cd12117 103 SLAGRAGGL--------------------------------EVAVVIDEALDAGPAGNPAVPVSpDDLAYVMYTSGSTGR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 294 PKGVMHTHRTLAAGLHtlEPRVVDLLGQphsdDVYLSYLPMAhimeFTITNLFIFrGAFIgfgtprtltdttarpHGDLL 373
Cdd:cd12117 151 PKGVAVTHRGVVRLVK--NTNYVTLGPD----DRVLQTSPLA----FDASTFEIW-GALL---------------NGARL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 374 TFNPSmlaGVPRIFDTLKKAVEAKLPPVGTLKRQVFDHAYQSRLAALKkgkdtpywnekvfaapravlgnRLRIMLSGGG 453
Cdd:cd12117 205 VLAPK---GTLLDPDALGALIAEEGVTVLWLTAALFNQLADEDPECFA----------------------GLRELLTGGE 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 454 PLSAAtheFVNVVF-----GRVVIGYGLTE-TICVGAIQIPGDTETNVT---GLMEPGQEIKLLdiDEYKHTDTPEPRGE 524
Cdd:cd12117 260 VVSPP---HVRRVLaacpgLRLVNGYGPTEnTTFTTSHVVTELDEVAGSipiGRPIANTRVYVL--DEDGRPVPPGVPGE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 525 MLSRGPYLFKGYYKQPELTREVLDEDGW------FHTGDVGSFTADGKMRIVGRVKALAKnCLGEYIALEALEAVysgne 598
Cdd:cd12117 335 LYVGGDGLALGYLNRPALTAERFVADPFgpgerlYRTGDLARWLPDGRLEFLGRIDDQVK-IRGFRIELGEIEAA----- 408
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 398009334 599 LLQPNGV---CVLVHPDKP-------YITALALTDEARATSFAAKH 634
Cdd:cd12117 409 LRAHPGVreaVVVVREDAGgdkrlvaYVVAEGALDAAELRAFLRER 454
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
279-574 |
4.43e-10 |
|
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: 62.56 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 279 DDLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLEPRvvdlLGQPHSDDVYL--SYLPMAHIMEFtitnlfifrgafigFG 356
Cdd:cd05918 106 SDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRA----LGLTSESRVLQfaSYTFDVSILEI--------------FT 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 357 TprtltdttarphgdlLTFN-----PS---MLAGVPRIFDTLkKAVEAKLPPvgtlkrqvfdhayqsRLAALKKGKDTPy 428
Cdd:cd05918 168 T---------------LAAGgclciPSeedRLNDLAGFINRL-RVTWAFLTP---------------SVARLLDPEDVP- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 429 wnekvfaapravlgnRLRIMLSGGGPLSAA-THEFVNVVfgRVVIGYGLTE-TICVGAIQIPGDTETNVTG--------L 498
Cdd:cd05918 216 ---------------SLRTLVLGGEALTQSdVDTWADRV--RLINAYGPAEcTIAATVSPVVPSTDPRNIGrplgatcwV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 499 MEPGQEIKLLdideykhtdtpePR---GEMLSRGPYLFKGYYKQPELTREVLDED-GW------------FHTGDVGSFT 562
Cdd:cd05918 279 VDPDNHDRLV------------PIgavGELLIEGPILARGYLNDPEKTAAAFIEDpAWlkqegsgrgrrlYRTGDLVRYN 346
|
330
....*....|....*.
gi 398009334 563 ADGKMRIVGR----VK 574
Cdd:cd05918 347 PDGSLEYVGRkdtqVK 362
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
286-613 |
6.96e-10 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 62.17 E-value: 6.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 286 YTSGTTGDPKGVMHTHRtlAAGLHTLEPRVVdlLGQPHSDdVYLSYLPMAHimeftiTNLFIFRGAFIGF-GTPRTLTDT 364
Cdd:PLN02479 202 YTSGTTASPKGVVLHHR--GAYLMALSNALI--WGMNEGA-VYLWTLPMFH------CNGWCFTWTLAALcGTNICLRQV 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 365 TARP-HGDLLTFNPSMLAGVPRIFDTLKKAveaklPPvgtlkrqvfdhayqsrlaalkkgkdtpywNEKVFAAPRAVlgn 443
Cdd:PLN02479 271 TAKAiYSAIANYGVTHFCAAPVVLNTIVNA-----PK-----------------------------SETILPLPRVV--- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 444 rlRIMLSGGGPLSAATHEFVNVVFgRVVIGYGLTET-----ICVGAIQ---IPGDTETNVT---GLMEPGQEikLLDIDE 512
Cdd:PLN02479 314 --HVMTAGAAPPPSVLFAMSEKGF-RVTHTYGLSETygpstVCAWKPEwdsLPPEEQARLNarqGVRYIGLE--GLDVVD 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 513 YKhTDTPEPR-----GEMLSRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGRVKALAKNClGEYI-A 586
Cdd:PLN02479 389 TK-TMKPVPAdgktmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISG-GENIsS 465
|
330 340
....*....|....*....|....*..
gi 398009334 587 LEALEAVYSGNELLQpngVCVLVHPDK 613
Cdd:PLN02479 466 LEVENVVYTHPAVLE---ASVVARPDE 489
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
136-641 |
7.89e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 62.67 E-value: 7.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 136 TYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGSA 215
Cdd:PRK12316 538 DYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSH 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 216 nvanvlklmkngVMPQVPIiyvgtlpasldTHGVQVVSFKQVEMIGAAHLEGGAAKGTGPLNdddLALIMYTSGTTGDPK 295
Cdd:PRK12316 618 ------------LGRKLPL-----------AAGVQVLDLDRPAAWLEGYSEENPGTELNPEN---LAYVIYTSGSTGKPK 671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 296 GVMHTHRTLAAGLHTLEPRvvdlLGQPHSDDVyLSYLPMAhiMEFTITNLF--IFRGAFI-----GFGT-PRTLTDTTAR 367
Cdd:PRK12316 672 GAGNRHRALSNRLCWMQQA----YGLGVGDTV-LQKTPFS--FDVSVWEFFwpLMSGARLvvaapGDHRdPAKLVELINR 744
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 368 PHGDLLTFNPSML------AGVPRIfDTLKKAVEAKLPPVGTLKRQVFDHAYQSRLAALkkgkdtpYwnekvfaapravl 441
Cdd:PRK12316 745 EGVDTLHFVPSMLqaflqdEDVASC-TSLRRIVCSGEALPADAQEQVFAKLPQAGLYNL-------Y------------- 803
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 442 gnrlrimlsggGPLSAA---THE-FVNVVFGRVVIGYGLTETICvgaiqipgdtetnvtglmepgqeiKLLDIDEykhtd 517
Cdd:PRK12316 804 -----------GPTEAAidvTHWtCVEEGGDSVPIGRPIANLAC------------------------YILDANL----- 843
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 518 TPEP---RGEMLSRGPYLFKGYYKQPELTRE--VLDEDG----WFHTGDVGSFTADGKMRIVGRVKALAKnCLGEYIALE 588
Cdd:PRK12316 844 EPVPvgvLGELYLAGRGLARGYHGRPGLTAErfVPSPFVagerMYRTGDLARYRADGVIEYAGRIDHQVK-LRGLRIELG 922
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 398009334 589 ALEAvysgnELLQPNGV---CVLVHPDKPYITALALTDEARATSFAAKHGIEGTYP 641
Cdd:PRK12316 923 EIEA-----RLLEHPWVreaAVLAVDGKQLVGYVVLESEGGDWREALKAHLAASLP 973
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
135-593 |
1.96e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 60.67 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAIL--- 211
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVyer 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 212 CGSANVANVLklmkngvmPQVP----IIYVGTlpASLDTHGVQVVSFkqvEMIGAAhleGGAAKGTGPLNDDDLaLIMYT 287
Cdd:PRK07798 109 EFAPRVAEVL--------PRLPklrtLVVVED--GSGNDLLPGAVDY---EDALAA---GSPERDFGERSPDDL-YLLYT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 288 SGTTGDPKGVMHTH----RTLAAGlhtleprvVDLL-GQPHSDDVYLS----------YLPMAHIMEFTITNlfifrGAF 352
Cdd:PRK07798 172 GGTTGMPKGVMWRQedifRVLLGG--------RDFAtGEPIEDEEELAkraaagpgmrRFPAPPLMHGAGQW-----AAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 353 IGF---GTPRTLTDTTARPHgdlltfnpsmlagvprifDTLKKAVEAK---LPPVGtlkrqvfDhAYQSRLAAlkkgkdt 426
Cdd:PRK07798 239 AALfsgQTVVLLPDVRFDAD------------------EVWRTIEREKvnvITIVG-------D-AMARPLLD------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 427 pywnekVFAAPRAVLGNRLRIMLSGGGPLSAATHE-FVNVVFGRVVI-GYGLTETICVGAIQIPGDTETNVTGLMEPGQE 504
Cdd:PRK07798 286 ------ALEARGPYDLSSLFAIASGGALFSPSVKEaLLELLPNVVLTdSIGSSETGFGGSGTVAKGAVHTGGPRFTIGPR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 505 IKLLDIDEYKHTDTPEPRGeMLSRGPYLFKGYYKQPELTREVLDE-DG--WFHTGDVGSFTADGKMRIVGRvKALAKNCL 581
Cdd:PRK07798 360 TVVLDEDGNPVEPGSGEIG-WIARRGHIPLGYYKDPEKTAETFPTiDGvrYAIPGDRARVEADGTITLLGR-GSVCINTG 437
|
490
....*....|..
gi 398009334 582 GEYIALEALEAV 593
Cdd:PRK07798 438 GEKVFPEEVEEA 449
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
136-573 |
2.32e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 61.33 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 136 TYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGSA 215
Cdd:PRK12467 1601 TYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSH 1680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 216 nvanvlklmkngVMPQVPIIyvgtlpasldtHGVQVVSFKQVEMIGAAHLEGGAAKGTGPlndDDLALIMYTSGTTGDPK 295
Cdd:PRK12467 1681 ------------LQARLPLP-----------DGLRSLVLDQEDDWLEGYSDSNPAVNLAP---QNLAYVIYTSGSTGRPK 1734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 296 GVMHTHRTLAAGLHTLEPRVvdllgQPHSDDVYLSYLPMAhiMEFTITNLF--IFRGA---FIGFGT---PRTLTDTTAR 367
Cdd:PRK12467 1735 GAGNRHGALVNRLCATQEAY-----QLSAADVVLQFTSFA--FDVSVWELFwpLINGArlvIAPPGAhrdPEQLIQLIER 1807
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 368 PHGDLLTFNPSMLagvprifdtlkkaveaklppvgtlkRQVFDHAYQsrlaalkkgkdtpywnekvFAAPRAvlgnrLRI 447
Cdd:PRK12467 1808 QQVTTLHFVPSML-------------------------QQLLQMDEQ-------------------VEHPLS-----LRR 1838
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 448 MLSGGGPLSAATHEFVNVVFGRVVI--GYGLTET---ICVGAIQIPGDTETNVTGLMEPGQEIKLLDIDEYKHtdtPEPR 522
Cdd:PRK12467 1839 VVCGGEALEVEALRPWLERLPDTGLfnLYGPTETavdVTHWTCRRKDLEGRDSVPIGQPIANLSTYILDASLN---PVPI 1915
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398009334 523 ---GEMLSRGPYLFKGYYKQPELTRE--VLDEDG-----WFHTGDVGSFTADGKMRIVGRV 573
Cdd:PRK12467 1916 gvaGELYLGGVGLARGYLNRPALTAErfVADPFGtvgsrLYRTGDLARYRADGVIEYLGRI 1976
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
473-578 |
4.49e-09 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 59.43 E-value: 4.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 473 GYGLTE-TICVGAIqiPG-DTETNVTGLMEPGQEIKLLDiDEYKHTDTPEpRGEM---LSRG-PY-LFKGYYKQPELTRE 545
Cdd:cd05970 332 GFGQTEtTLTIATF--PWmEPKPGSMGKPAPGYEIDLID-REGRSCEAGE-EGEIvirTSKGkPVgLFGGYYKDAEKTAE 407
|
90 100 110
....*....|....*....|....*....|...
gi 398009334 546 VLdEDGWFHTGDVGSFTADGKMRIVGRVKALAK 578
Cdd:cd05970 408 VW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIK 439
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
279-573 |
8.59e-09 |
|
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: 58.42 E-value: 8.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 279 DDLALIMYTSGTTGDPKGVMHTHRtlaaGLHTLEPRVVDLLGQPHSDDV--YLSYLPMAHIMEFTIT-----NLFIFRGA 351
Cdd:cd17652 93 DNLAYVIYTSGSTGRPKGVVVTHR----GLANLAAAQIAAFDVGPGSRVlqFASPSFDASVWELLMAllagaTLVLAPAE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 352 FIGFGTPrtLTDTTARPHGDLLTFNPSMLAGVPrifdtlkkavEAKLPPVGTLkrqvfdhayqsrlaalkkgkdtpywne 431
Cdd:cd17652 169 ELLPGEP--LADLLREHRITHVTLPPAALAALP----------PDDLPDLRTL--------------------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 432 kvfaapravlgnrlrimLSGGGPLSAATHEFVNVvfGRVVI-GYGLTE-TICVGAIQIPGDTETNVTGLMEPGQEIKLLD 509
Cdd:cd17652 210 -----------------VVAGEACPAELVDRWAP--GRRMInAYGPTEtTVCATMAGPLPGGGVPPIGRPVPGTRVYVLD 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398009334 510 ideykHTDTPEP---RGEMLSRGPYLFKGYYKQPELTRE--VLDEDG-----WFHTGDVGSFTADGKMRIVGRV 573
Cdd:cd17652 271 -----ARLRPVPpgvPGELYIAGAGLARGYLNRPGLTAErfVADPFGapgsrMYRTGDLARWRADGQLEFLGRA 339
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
129-573 |
9.97e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 59.02 E-value: 9.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 129 FDEVVyVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWScsavAATVYANLGEAA----LAHALHE 204
Cdd:PRK12467 533 FGEQV-LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLK----AGGAYVPLDPEYpqdrLAYMLDD 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 205 TESQAILCGSanvaNVLKLMKngvmpqvpiiyvgtLPAsldthGVQVVSFKQVemigAAHLEGGAAKGTGP-LNDDDLAL 283
Cdd:PRK12467 608 SGVRLLLTQS----HLLAQLP--------------VPA-----GLRSLCLDEP----ADLLCGYSGHNPEVaLDPDNLAY 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 284 IMYTSGTTGDPKGVMHTHRTLAAGLHTLEPRVvdllgQPHSDDVYLSYLPMAhiMEFTITNLFifrgafigfgtprtltd 363
Cdd:PRK12467 661 VIYTSGSTGQPKGVAISHGALANYVCVIAERL-----QLAADDSMLMVSTFA--FDLGVTELF----------------- 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 364 tTARPHGDLLTFNPsmlagvpriFDTLKKAVEaklppvgtLKRQVFDHayqsRLAALKKgkdTPYWNEKVFAAPRAVLGN 443
Cdd:PRK12467 717 -GALASGATLHLLP---------PDCARDAEA--------FAALMADQ----GVTVLKI---VPSHLQALLQASRVALPR 771
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 444 RLRIMLSGGG--PLSAATHEFVNVVFGRVVIGYGLTETiCVGAIQIPGDTETNVTGLMEPGQEIKLLDIDEYKHTDTPEP 521
Cdd:PRK12467 772 PQRALVCGGEalQVDLLARVRALGPGARLINHYGPTET-TVGVSTYELSDEERDFGNVPIGQPLANLGLYILDHYLNPVP 850
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398009334 522 ---RGEMLSRGPYLFKGYYKQPELTRE--VLDEDG-----WFHTGDVGSFTADGKMRIVGRV 573
Cdd:PRK12467 851 vgvVGELYIGGAGLARGYHRRPALTAErfVPDPFGadggrLYRTGDLARYRADGVIEYLGRM 912
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
147-596 |
1.03e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 58.59 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 147 FGAGLAALG-----VTANGN-VSIYLDTCVEWLIGIYGIWSCSAVAATVYA--NLGEAALAHA-LHETESQAILCGSANV 217
Cdd:PRK07769 61 FGARNRAVGarlqqVTKPGDrVAILAPQNLDYLIAFFGALYAGRIAVPLFDpaEPGHVGRLHAvLDDCTPSAILTTTDSA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 218 ANVLKLMKNGVMPQVP-IIYVGTLPASLDTHGVQVvsfkqvemigaahleggaakgtgPLNDDDLALIMYTSGTTGDPKG 296
Cdd:PRK07769 141 EGVRKFFRARPAKERPrVIAVDAVPDEVGATWVPP-----------------------EANEDTIAYLQYTSGSTRIPAG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 297 VMHTHRTLAAGLhtlePRVVDLLGQpHSDDVYLSYLPMAHIMEFTITNLFIFRGAFIGFGTP--------RTLTDTTARP 368
Cdd:PRK07769 198 VQITHLNLPTNV----LQVIDALEG-QEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPaafvrrpgRWIRELARKP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 369 HGDLLTFnpsmlAGVPRIfdtlkkaveaklppvgtlkrqVFDHAYQSRLAalKKGKdtPYWNekvfaapravLGNrLRIM 448
Cdd:PRK07769 273 GGTGGTF-----SAAPNF---------------------AFEHAAARGLP--KDGE--PPLD----------LSN-VKGL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 449 LSGGGPLSAATHEFVNVVFG-------RVVIGYGLTE-TICVGAI----------------------QIPGDTETNVT-- 496
Cdd:PRK07769 312 LNGSEPVSPASMRKFNEAFApyglpptAIKPSYGMAEaTLFVSTTpmdeeptviyvdrdelnagrfvEVPADAPNAVAqv 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 497 --GLMEPGQEIKLLDIDeykhTDTPEPR---GEMLSRGPYLFKGYYKQPELTREVL-----------------DEDGWFH 554
Cdd:PRK07769 392 saGKVGVSEWAVIVDPE----TASELPDgqiGEIWLHGNNIGTGYWGKPEETAATFqnilksrlseshaegapDDALWVR 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 398009334 555 TGDVGSFTaDGKMRIVGRVKAL----AKNCLG---EYIALEALEAVYSG 596
Cdd:PRK07769 468 TGDYGVYF-DGELYITGRVKDLviidGRNHYPqdlEYTAQEATKALRTG 515
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
234-573 |
1.36e-08 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 57.98 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 234 IIYVGTLPASLDthGVQVVSFKQVEMIGAahlEGGAAKGTGPLNDDDLALIMYTSGTTGDPKGVMHTHRTLaaglhtlep 313
Cdd:PRK04813 103 IIATEELPLEIL--GIPVITLDELKDIFA---TGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGVQISHDNL--------- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 314 rvvdllgqphsddvylsylpmahiMEFT--ITNLFifrgafigfGTPRtltdttarphgdlltfNPSMLAGVPRIFD--- 388
Cdd:PRK04813 169 ------------------------VSFTnwMLEDF---------ALPE----------------GPQFLNQAPYSFDlsv 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 389 --------------TLKKAVEAKLppvgtlkRQVFDHAYQSRLAALKKgkdTPYWNEKVFAAPR--AVLGNRLRIMLSGG 452
Cdd:PRK04813 200 mdlyptlasggtlvALPKDMTANF-------KQLFETLPQLPINVWVS---TPSFADMCLLDPSfnEEHLPNLTHFLFCG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 453 GPLSAATHEFVNVVF--GRVVIGYGLTE-TICVGAIQIPGDTETNVT----GLMEPGQEIKLLDIDEYKHTDTPEprGEM 525
Cdd:PRK04813 270 EELPHKTAKKLLERFpsATIYNTYGPTEaTVAVTSIEITDEMLDQYKrlpiGYAKPDSPLLIIDEEGTKLPDGEQ--GEI 347
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 398009334 526 LSRGPYLFKGYYKQPELTREVL-DEDGW--FHTGDVGSFtADGKMRIVGRV 573
Cdd:PRK04813 348 VISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGYL-EDGLLFYQGRI 397
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
130-573 |
1.70e-08 |
|
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: 57.67 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 130 DEVVYVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALhetesqa 209
Cdd:cd17646 19 DEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYML------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 210 ilcGSANVANVLklmknGVMPQVPIIYVGTLPASLdthgvqvvsfkqVEMIGAAHLEGGAAKGTGPlndDDLALIMYTSG 289
Cdd:cd17646 92 ---ADAGPAVVL-----TTADLAARLPAGGDVALL------------GDEALAAPPATPPLVPPRP---DNLAYVIYTSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 290 TTGDPKGVMHTHRTLAAGL------HTLEPRVVDLLGQPHSDDVYLS--YLPMAHimeftitnlfifrGAFIGFGTPRTL 361
Cdd:cd17646 149 STGRPKGVMVTHAGIVNRLlwmqdeYPLGPGDRVLQKTPLSFDVSVWelFWPLVA-------------GARLVVARPGGH 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 362 TDTTA-----RPHG-DLLTFNPSMLagvprifdtlkkaveaklppvgtlkrQVFdhayqsrlaalkkgkdtpywnekvFA 435
Cdd:cd17646 216 RDPAYlaaliREHGvTTCHFVPSML--------------------------RVF------------------------LA 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 436 APRAVLGNRLRIMLSGGGPLSAATHEFVNVVFG-RVVIGYGLTE-TICVGAIQIPGDTETNVTGLMEPGQEIKLLDIDEY 513
Cdd:cd17646 246 EPAAGSCASLRRVFCSGEALPPELAARFLALPGaELHNLYGPTEaAIDVTHWPVRGPAETPSVPIGRPVPNTRLYVLDDA 325
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 514 KHtdtPEPR---GEMLSRGPYLFKGYYKQPELTREVLDEDgWF-------HTGDVGSFTADGKMRIVGRV 573
Cdd:cd17646 326 LR---PVPVgvpGELYLGGVQLARGYLGRPALTAERFVPD-PFgpgsrmyRTGDLARWRPDGALEFLGRS 391
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
136-301 |
1.84e-08 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 57.50 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 136 TYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILC--G 213
Cdd:cd05968 93 TYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITadG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 214 SANVANVLKLMKN-----GVMPQVP-IIYVGTLPASLDTHGVQVVSFKQVEMIGAAHLEggaakGTGPlndDDLALIMYT 287
Cdd:cd05968 173 FTRRGREVNLKEEadkacAQCPTVEkVVVVRHLGNDFTPAKGRDLSYDEEKETAGDGAE-----RTES---EDPLMIIYT 244
|
170
....*....|....
gi 398009334 288 SGTTGDPKGVMHTH 301
Cdd:cd05968 245 SGTTGKPKGTVHVH 258
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
136-593 |
2.39e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 58.04 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 136 TYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHEtesqailCGSA 215
Cdd:PRK12316 2030 SYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLED-------SGAA 2102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 216 nvanvLKLMKNGVMPQVPIiyvgtlpasldTHGVQVVSFKQvemigAAHLEGGAAkgTGPLND---DDLALIMYTSGTTG 292
Cdd:PRK12316 2103 -----LLLTQRHLLERLPL-----------PAGVARLPLDR-----DAEWADYPD--TAPAVQlagENLAYVIYTSGSTG 2159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 293 DPKGVMHTHRTLAAGLHTLEPRvvdlLGQPHSDDVYlsylpmaHIMEFTitnlfiFRGAFIGFGTPRTltdttarpHGDL 372
Cdd:PRK12316 2160 LPKGVAVSHGALVAHCQAAGER----YELSPADCEL-------QFMSFS------FDGAHEQWFHPLL--------NGAR 2214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 373 LTFNPSMLAGVPRIFDTLKK--AVEAKLPPVgtlkrqvfdhayqsrlaalkkgkdtpYWNEkvFAAPRAVLGNR--LRIM 448
Cdd:PRK12316 2215 VLIRDDELWDPEQLYDEMERhgVTILDFPPV--------------------------YLQQ--LAEHAERDGRPpaVRVY 2266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 449 LSGGGPLSAATHEFVNVVFG--RVVIGYGLTETICVGAIQIPGDTETNVTGLMEPGQEI---KLLDIDEYKHTDTPEPRG 523
Cdd:PRK12316 2267 CFGGEAVPAASLRLAWEALRpvYLFNGYGPTEAVVTPLLWKCRPQDPCGAAYVPIGRALgnrRAYILDADLNLLAPGMAG 2346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 524 EMLSRGPYLFKGYYKQPELTREVLDEDGW-------FHTGDVGSFTADGKMRIVGRVKALAKNC-----LGEYIA-LEAL 590
Cdd:PRK12316 2347 ELYLGGEGLARGYLNRPGLTAERFVPDPFsasgerlYRTGDLARYRADGVVEYLGRIDHQVKIRgfrieLGEIEArLQAH 2426
|
...
gi 398009334 591 EAV 593
Cdd:PRK12316 2427 PAV 2429
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
275-576 |
2.67e-08 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 57.08 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 275 PLNDDDLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLEPRVvdLLGQPHsdDVYLSYLPMAHIMEFTitnlFIFRGAFIG 354
Cdd:PRK05851 148 PPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARV--GLDAAT--DVGCSWLPLYHDMGLA----FLLTAALAG 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 355 fgTPRTLTDTTArphgdlltFNPSMLAGVPRIFD---TLKKAVEAKLPPVGTLKRQVFDhayqsrlaalkkgkdtpywne 431
Cdd:PRK05851 220 --APLWLAPTTA--------FSASPFRWLSWLSDsraTLTAAPNFAYNLIGKYARRVSD--------------------- 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 432 kvfaaprAVLGNrLRIMLSGGGPLSAA-----THEFVNVVF--GRVVIGYGLTETICVGAIQIPG-----------DTET 493
Cdd:PRK05851 269 -------VDLGA-LRVALNGGEPVDCDgferfATAMAPFGFdaGAAAPSYGLAESTCAVTVPVPGiglrvdevttdDGSG 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 494 N----VTGLMEPGQEIKLLDIDEYKHTDTPEPrGEMLSRGPYLFKGYykqpeLTREVLDEDGWFHTGDVGSFTADGkMRI 569
Cdd:PRK05851 341 ArrhaVLGNPIPGMEVRISPGDGAAGVAGREI-GEIEIRGASMMSGY-----LGQAPIDPDDWFPTGDLGYLVDGG-LVV 413
|
....*..
gi 398009334 570 VGRVKAL 576
Cdd:PRK05851 414 CGRAKEL 420
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
279-629 |
2.91e-08 |
|
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: 56.81 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 279 DDLALIMYTSGTTGDPKGVMHTHRTLAAGlhtleprvvdllgqpHSDDVYLSYLPMAHImEFTITNLFIFRGAFIGFGTP 358
Cdd:cd05974 85 DDPMLLYFTSGTTSKPKLVEHTHRSYPVG---------------HLSTMYWIGLKPGDV-HWNISSPGWAKHAWSCFFAP 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 359 RTLTDTtarphgdLLTFNPSMLAGvPRIFDTLKKAVEAKL--PPVgtlkrqVFDHAYQSRLAALKkgkdtpywnekvfAA 436
Cdd:cd05974 149 WNAGAT-------VFLFNYARFDA-KRVLAALVRYGVTTLcaPPT------VWRMLIQQDLASFD-------------VK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 437 PRAVLGnrlrimlsGGGPLSAATHEFVNVVFGRVVI-GYGLTETICVgAIQIPGdtETNVTGLM---EPGQEIKLLDIDe 512
Cdd:cd05974 202 LREVVG--------AGEPLNPEVIEQVRRAWGLTIRdGYGQTETTAL-VGNSPG--QPVKAGSMgrpLPGYRVALLDPD- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 513 ykhtDTPEPRGEML-----SRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGRVKALAKNclGEY-IA 586
Cdd:cd05974 270 ----GAPATEGEVAldlgdTRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFKS--SDYrIS 342
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 398009334 587 LEALEAVYSGNELLQPNGVCVLVHPD-----KPYITALALTDEARATS 629
Cdd:cd05974 343 PFELESVLIEHPAVAEAAVVPSPDPVrlsvpKAFIVLRAGYEPSPETA 390
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
135-573 |
3.24e-08 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 56.94 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGS 214
Cdd:cd05967 83 YTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLIVTAS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 ANVAnvlklmKNGVMPQVPIIYVGTLPASLDTHGVQVVSFKQVEMIGAAH---------LEGGAAKGTGPLNDDDLALIM 285
Cdd:cd05967 163 CGIE------PGKVVPYKPLLDKALELSGHKPHHVLVLNRPQVPADLTKPgrdldwselLAKAEPVDCVPVAATDPLYIL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 286 YTSGTTGDPKGVMHTHRTLAAGLHTLEPRVVDLlgqpHSDDVYlsylpmahimeFTITNLfifrGAFIGfgtprtltdtt 365
Cdd:cd05967 237 YTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGI----KPGDVW-----------WAASDV----GWVVG----------- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 366 arpHgDLLTFNPsMLAGVPRIFdtlkkaVEAKlpPVGTLKRQVF-----DHayqsRLAALkkgkdtpywnekvFAAPRAV 440
Cdd:cd05967 287 ---H-SYIVYGP-LLHGATTVL------YEGK--PVGTPDPGAFwrvieKY----QVNAL-------------FTAPTAI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 441 LG----------------NRLRIMLSGGGPLSAATHEFVNVVFGRVVIG-YGLTET------ICVGAIQIPgdTETNVTG 497
Cdd:cd05967 337 RAirkedpdgkyikkydlSSLRTLFLAGERLDPPTLEWAENTLGVPVIDhWWQTETgwpitaNPVGLEPLP--IKAGSPG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 498 LMEPGQEIKLLDideykhtDTPEP-----RGEMLSRGPY---LFKGYYKQPELTREVL--DEDGWFHTGDVGSFTADGKM 567
Cdd:cd05967 415 KPVPGYQVQVLD-------EDGEPvgpneLGNIVIKLPLppgCLLTLWKNDERFKKLYlsKFPGYYDTGDAGYKDEDGYL 487
|
....*.
gi 398009334 568 RIVGRV 573
Cdd:cd05967 488 FIMGRT 493
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
283-571 |
3.35e-08 |
|
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: 55.77 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 283 LIMYTSGTTGDPKGVMHTHRTL-AAGLHTLeprvvdLLGQPHSDDVYLSYLPMAHI-MEFTITNLFIFRGA--FIGFGTP 358
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALlAQALVLA------VLQAIDEGTVFLNSGPLFHIgTLMFTLATFHAGGTnvFVRRVDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 359 RTLTDTTARPHGDLltfnpSMLagVPRIFDTLKKAVEAKLPPVGTLKRQVFDHAYQSRLAAlkkgkDTPYWnekvfaapr 438
Cdd:cd17636 78 EEVLELIEAERCTH-----AFL--LPPTIDQIVELNADGLYDLSSLRSSPAAPEWNDMATV-----DTSPW--------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 439 avlgnrlrimlsgggplsaathefvnvvfGRVVIGYGLTETicVGAIQIP--GDTETNVTGLMEPGQEIKLLDID--EYK 514
Cdd:cd17636 137 -----------------------------GRKPGGYGQTEV--MGLATFAalGGGAIGGAGRPSPLVQVRILDEDgrEVP 185
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 398009334 515 HTDTpeprGEMLSRGPYLFKGYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVG 571
Cdd:cd17636 186 DGEV----GEIVARGPTVMAGYWNRPEVNARRT-RGGWHHTNDLGRREPDGSLSFVG 237
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
501-576 |
4.02e-08 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 56.55 E-value: 4.02e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398009334 501 PGQEIKLLDIDEykhTDTPEPR-GEMLSRGPYLFKGYYKQPELTReVLDEDGWFHTGDVGsFTADGKMRIVGRVKAL 576
Cdd:PRK09192 392 PGHEIEIRNEAG---MPLPERVvGHICVRGPSLMSGYFRDEESQD-VLAADGWLDTGDLG-YLLDGYLYITGRAKDL 463
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
279-573 |
7.25e-08 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 55.45 E-value: 7.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 279 DDLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLEpRVVDLlgqpHSDDVYLSYLPMAhimeftitnlfiFRGAfigfgtp 358
Cdd:cd17649 94 RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATA-ERYGL----TPGDRELQFASFN------------FDGA------- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 359 rtltdttarpHGDLLtfnPSMLAGVPRIFDTlkkavEAKLPPVGTLKRQVFDHAYQsrLAALKkgkdTPYWNEKVFAAPR 438
Cdd:cd17649 150 ----------HEQLL---PPLICGACVVLRP-----DELWASADELAEMVRELGVT--VLDLP----PAYLQQLAEEADR 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 439 AVLGN--RLRIMLSGGGPLSAathEFVNVVFG---RVVIGYGLTETICVGAIQIPGDTETNVTGLME-----PGQEIKLL 508
Cdd:cd17649 206 TGDGRppSLRLYIFGGEALSP---ELLRRWLKapvRLFNAYGPTEATVTPLVWKCEAGAARAGASMPigrplGGRSAYIL 282
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398009334 509 DIDeyKHTDTPEPRGEMLSRGPYLFKGYYKQPELTRE--VLDEDG-----WFHTGDVGSFTADGKMRIVGRV 573
Cdd:cd17649 283 DAD--LNPVPVGVTGELYIGGEGLARGYLGRPELTAErfVPDPFGapgsrLYRTGDLARWRDDGVIEYLGRV 352
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
275-573 |
1.58e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 55.35 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 275 PLNDDDLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLEPRVvdllgQPHSDDVYLSYLPmahimeftitnlFIFRGAFIG 354
Cdd:PRK12316 4690 RLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERY-----ELTPDDRVLQFMS------------FSFDGSHEG 4752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 355 FGTPrtltdttarphgdlLTFNPSMLAGVPRIFDTlkkaveaklppvGTLKRQVFDHayqsRLAALKKgkdTP-YWNEKV 433
Cdd:PRK12316 4753 LYHP--------------LINGASVVIRDDSLWDP------------ERLYAEIHEH----RVTVLVF---PPvYLQQLA 4799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 434 FAAPRAVLGNRLRIMLSGGGPLSAATHEFVNVVFGRVVI--GYGLTETICVGAIQ--IPGDTETNVT---GLMEPGQEIK 506
Cdd:PRK12316 4800 EHAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLfnGYGPTETTVTVLLWkaRDGDACGAAYmpiGTPLGNRSGY 4879
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398009334 507 LLDideykhtDTPEPR-----GEMLSRGPYLFKGYYKQPELTRE-----VLDEDG--WFHTGDVGSFTADGKMRIVGRV 573
Cdd:PRK12316 4880 VLD-------GQLNPLpvgvaGELYLGGEGVARGYLERPALTAErfvpdPFGAPGgrLYRTGDLARYRADGVIDYLGRV 4951
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
136-573 |
2.40e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 54.78 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 136 TYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIwsCSAVAATVYANLGeaalahalHETESQAILCGSA 215
Cdd:PRK12467 3122 SYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAV--LKAGGAYVPLDPE--------YPRERLAYMIEDS 3191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 216 NVAnvLKLMKNGVMPQVPIIyvgtlpasldtHGVQVVSFKQVEMIG------AAHLEGgaakgtgplndDDLALIMYTSG 289
Cdd:PRK12467 3192 GVK--LLLTQAHLLEQLPAP-----------AGDTALTLDRLDLNGysennpSTRVMG-----------ENLAYVIYTSG 3247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 290 TTGDPKGVMHTHRTLAAGLHTLEprvvDLLGQPHSDDVyLSYLPMAhiMEFTITNLF---IFRGAFIGFG----TPRTLT 362
Cdd:PRK12467 3248 STGKPKGVGVRHGALANHLCWIA----EAYELDANDRV-LLFMSFS--FDGAQERFLwtlICGGCLVVRDndlwDPEELW 3320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 363 DTTARPHGDLLTFNPSMLagvprifdtlkkaveaklppvgtlkrqvfdhayqSRLAALKKGKDTPywnekvfaapravlg 442
Cdd:PRK12467 3321 QAIHAHRISIACFPPAYL----------------------------------QQFAEDAGGADCA--------------- 3351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 443 nRLRIMLSGGGPLSAATHEFVNVVFGRVVI--GYGLTET-ICVGAIQIPGDTETNVT----GLMEPGQEIKLLDideykH 515
Cdd:PRK12467 3352 -SLDIYVFGGEAVPPAAFEQVKRKLKPRGLtnGYGPTEAvVTVTLWKCGGDAVCEAPyapiGRPVAGRSIYVLD-----G 3425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398009334 516 TDTPEPR---GEMLSRGPYLFKGYYKQPELTREVLDEDGW-------FHTGDVGSFTADGKMRIVGRV 573
Cdd:PRK12467 3426 QLNPVPVgvaGELYIGGVGLARGYHQRPSLTAERFVADPFsgsggrlYRTGDLARYRADGVIEYLGRI 3493
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
283-572 |
2.90e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 53.78 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 283 LIMYTSGTTGDPKGVMHTHRTLAAGLHTLEPRVvdllgqP-HSDDVYLSYLPMAHIMEFTITNLFIFRGAFI----GFGT 357
Cdd:PRK07788 211 IVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRV------PfRAGETTLLPAPMFHATGWAHLTLAMALGSTVvlrrRFDP 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 358 PRTLTDTtARPHGDLLTFNPSMLAgvpRIFDTLKKAVEAKlppvgtlkrqvfdhayqsrlaalkkgkDTpywnekvfaap 437
Cdd:PRK07788 285 EATLEDI-AKHKATALVVVPVMLS---RILDLGPEVLAKY---------------------------DT----------- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 438 ravlgNRLRIMLSGGGPLSAATHEFVNVVFGRVVIG-YGLTEtICVGAIQIPGDTETNVT--GLMEPGQEIKLLDIDeyk 514
Cdd:PRK07788 323 -----SSLKIIFVSGSALSPELATRALEAFGPVLYNlYGSTE-VAFATIATPEDLAEAPGtvGRPPKGVTVKILDEN--- 393
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398009334 515 htDTPEPRGE---MLSRGPYLFKGYY--KQPELtrevldEDGWFHTGDVGSFTADGKMRIVGR 572
Cdd:PRK07788 394 --GNEVPRGVvgrIFVGNGFPFEGYTdgRDKQI------IDGLLSSGDVGYFDEDGLLFVDGR 448
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
276-574 |
3.04e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.40 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 276 LNDDDLALIMYTSGTTGDPKGVMHTHRTLAAGlHTLEPRVVDLLGQPhsDDVYLSYLPMAHIMEFTitnlfifrgafigf 355
Cdd:PRK05691 163 LQPDDIAFLQYTSGSTALPKGVQVSHGNLVAN-EQLIRHGFGIDLNP--DDVIVSWLPLYHDMGLI-------------- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 356 gtprtltdttarphGDLLTfnpSMLAGVPRIFdtlkkaveakLPPVGTLKRQV-FDHAYQSRLAALKKGKDTPY--WNEK 432
Cdd:PRK05691 226 --------------GGLLQ---PIFSGVPCVL----------MSPAYFLERPLrWLEAISEYGGTISGGPDFAYrlCSER 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 433 VFAAPRAVLG-NRLRIMLSGGGP-----LSAATHEFVNVVF--GRVVIGYGLTE-TICV---------GAIQI------- 487
Cdd:PRK05691 279 VSESALERLDlSRWRVAYSGSEPirqdsLERFAEKFAACGFdpDSFFASYGLAEaTLFVsggrrgqgiPALELdaealar 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 488 ----PGDTETNVT-GLMEPGQEIKLldIDEYKHTDTPEPR-GEMLSRGPYLFKGYYKQPELT-REVLDEDG--WFHTGDV 558
Cdd:PRK05691 359 nraePGTGSVLMScGRSQPGHAVLI--VDPQSLEVLGDNRvGEIWASGPSIAHGYWRNPEASaKTFVEHDGrtWLRTGDL 436
|
330
....*....|....*.
gi 398009334 559 GsFTADGKMRIVGRVK 574
Cdd:PRK05691 437 G-FLRDGELFVTGRLK 451
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
137-574 |
4.46e-07 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 53.16 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 137 YSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGsan 216
Cdd:PRK12406 14 FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAH--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 217 vANVLKLMKNGVMPQVPIIYVGTLPASLDTHGVQVVSFKQVEmiGAAHLEGGAAKG---TGPLNDDDLALImYTSGTTGD 293
Cdd:PRK12406 91 -ADLLHGLASALPAGVTVLSVPTPPEIAAAYRISPALLTPPA--GAIDWEGWLAQQepyDGPPVPQPQSMI-YTSGTTGH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 294 PKGVMHTHRT---------LAAGLHTLEPRVVDLLGQP--HSddvylsyLPMAH-IMEFTITNLFIFRGAFigfgTPRTL 361
Cdd:PRK12406 167 PKGVRRAAPTpeqaaaaeqMRALIYGLKPGIRALLTGPlyHS-------APNAYgLRAGRLGGVLVLQPRF----DPEEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 362 TDTTARPHGDLLTFNPSMLAgvpRIFDtLKKAVEAKLpPVGTLKRQVfdHAyqsrlAAlkkgkdtpywnekvfAAPRAVl 441
Cdd:PRK12406 236 LQLIERHRITHMHMVPTMFI---RLLK-LPEEVRAKY-DVSSLRHVI--HA-----AA---------------PCPADV- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 442 gnrLRIMLSGGGPLsaaTHEFvnvvfgrvvigYGLTETICVG------AIQIPGdtetnVTGLMEPGQEIKLLDiDEYKH 515
Cdd:PRK12406 288 ---KRAMIEWWGPV---IYEY-----------YGSTESGAVTfatsedALSHPG-----TVGKAAPGAELRFVD-EDGRP 344
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398009334 516 TDTPEPrGEMLSR--GPYLFKgYYKQPELTREVlDEDGWFHTGDVGSFTADGKMRIVGRVK 574
Cdd:PRK12406 345 LPQGEI-GEIYSRiaGNPDFT-YHNKPEKRAEI-DRGGFITSGDVGYLDADGYLFLCDRKR 402
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
135-655 |
1.38e-06 |
|
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: 51.50 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILCGS 214
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLTDG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 ANVANVlklmkngvmpqVPIIYVGTLPASLDTHGVQVVSfkqvemigaahleggaakgtGPLNDDDLALIMYTSGTTGDP 294
Cdd:cd12114 93 PDAQLD-----------VAVFDVLILDLDALAAPAPPPP--------------------VDVAPDDLAYVIFTSGSTGTP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 295 KGVMHTHRtlaAGLHTLEprvvDLLGQPH--SDDVYLSYLPMAHIMefTITNLFifrGAFiGFGTPRTLTDTTARPHGD- 371
Cdd:cd12114 142 KGVMISHR---AALNTIL----DINRRFAvgPDDRVLALSSLSFDL--SVYDIF---GAL-SAGATLVLPDEARRRDPAh 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 372 ----LLTFNPSMLAGVPRIFDTLKKAVEAKLPPVGTLkRQVF---DHAYQSRLAALKKgkdtpywnekvfAAPRAVLgnr 444
Cdd:cd12114 209 waelIERHGVTLWNSVPALLEMLLDVLEAAQALLPSL-RLVLlsgDWIPLDLPARLRA------------LAPDARL--- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 445 lrimLSGGGPLSAA----THEFVNVVFGRVVIGYGLteticvgaiqiPgdtetnvtglmEPGQEIKLLDIDEykhTDTPE 520
Cdd:cd12114 273 ----ISLGGATEASiwsiYHPIDEVPPDWRSIPYGR-----------P-----------LANQRYRVLDPRG---RDCPD 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 521 -PRGEMLSRGPYLFKGYYKQPELTRE--VLDEDG--WFHTGDVGSFTADGKMRIVGRVKALAKNC-----LGEyI--ALE 588
Cdd:cd12114 324 wVPGELWIGGRGVALGYLGDPELTAArfVTHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRgyrieLGE-IeaALQ 402
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398009334 589 ALEAVYSgnellqpngVCVLVHPDkPYITALAL-----TDEARATSFAAKHGIEGTYPALLKDQRFQQAAAI 655
Cdd:cd12114 403 AHPGVAR---------AVVVVLGD-PGGKRLAAfvvpdNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEAL 464
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
276-612 |
2.71e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 51.32 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 276 LNDDDLALIMYTSGTTGDPKGVMHTHRTLAAGLH----TLEPRVVDLLGQ--PHSDD--VYLSYLPMahimeftITNLfi 347
Cdd:PRK05691 1270 LHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQwmqaTYALDDSDVLMQkaPISFDvsVWECFWPL-------ITGC-- 1340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 348 fRGAFIGFGT---PRTLTDTTARPHGDLLTFNPSMLagvprifdtlkkaveaklppvgtlkrQVFdhayqsrlaalkkgk 424
Cdd:PRK05691 1341 -RLVLAGPGEhrdPQRIAELVQQYGVTTLHFVPPLL--------------------------QLF--------------- 1378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 425 dtpywnekvFAAPRAVLGNRLRIMLSGGGPLSAATHEFVNVVFGRVVIG--YGLTET-ICVGAIQIPG-DTETNVTGLME 500
Cdd:PRK05691 1379 ---------IDEPLAAACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHnrYGPTETaINVTHWQCQAeDGERSPIGRPL 1449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 501 PGQEIKLLDiDEYKHTDTPEPrGEMLSRGPYLFKGYYKQPELTRE--VLDEDG-----WFHTGDVGSFTADGKMRIVGRV 573
Cdd:PRK05691 1450 GNVLCRVLD-AELNLLPPGVA-GELCIGGAGLARGYLGRPALTAErfVPDPLGedgarLYRTGDRARWNADGALEYLGRL 1527
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 398009334 574 KALAKnCLGEYIALEALEAVysgneLLQPNGV---CVLVHPD 612
Cdd:PRK05691 1528 DQQVK-LRGFRVEPEEIQAR-----LLAQPGVaqaAVLVREG 1563
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
130-328 |
3.05e-06 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 50.64 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 130 DEVVYVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQA 209
Cdd:cd05966 80 DQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 210 ILCGSANV---------ANVLKLMKNGVMPQVPIIYvgtlpasldTHGVQVVSFKQ------VEMIGAAHLEGGAAkgtg 274
Cdd:cd05966 160 VITADGGYrggkviplkEIVDEALEKCPSVEKVLVV---------KRTGGEVPMTEgrdlwwHDLMAKQSPECEPE---- 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 398009334 275 PLNDDDLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLEPRVVDLlgqpHSDDVY 328
Cdd:cd05966 227 WMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDY----HPDDIY 276
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
130-328 |
5.02e-06 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 49.94 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 130 DEVVYVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALA---------- 199
Cdd:TIGR02188 84 GEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALAdrindagakl 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 200 -------------HALHETESQAILCGSANVANVLKLMKNG--VMPQVPiiyvgtlpaSLDTHGVQVVSFKQVEMIGAah 264
Cdd:TIGR02188 164 vitadeglrggkvIPLKAIVDEALEKCPVSVEHVLVVRRTGnpVVPWVE---------GRDVWWHDLMAKASAYCEPE-- 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398009334 265 leggaakgtgPLNDDDLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLEPRVVDLlgqpHSDDVY 328
Cdd:TIGR02188 233 ----------PMDSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDI----KDGDIF 282
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
277-578 |
6.43e-06 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 49.09 E-value: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 277 NDDDLALIMYTSGTTGDPKGVMHTHRTLaaglhtleprvVDLLGQPHSddvYLSYLPMAHIMEFtitnlfifrgAFIGFg 356
Cdd:cd17645 102 NPDDLAYVIYTSGSTGLPKGVMIEHHNL-----------VNLCEWHRP---YFGVTPADKSLVY----------ASFSF- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 357 tprtltdttarpHGDLLTFNPSMLAGVprifdTLKKAVEAKLPPVGTLKRQVFDHayqsrlaalkkGKDTPYWNEKVFAA 436
Cdd:cd17645 157 ------------DASAWEIFPHLTAGA-----ALHVVPSERRLDLDALNDYFNQE-----------GITISFLPTGAAEQ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 437 PRAVLGNRLRIMLSGGGPLSAA---THEFVNvvfgrvviGYGLTETICVgAIQIPGDTETNVTGLMEPGQEIKLLDIDEY 513
Cdd:cd17645 209 FMQLDNQSLRVLLTGGDKLKKIerkGYKLVN--------NYGPTENTVV-ATSFEIDKPYANIPIGKPIDNTRVYILDEA 279
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398009334 514 KHTDTPEPRGEMLSRGPYLFKGYYKQPELTREVLDEDGW------FHTGDVGSFTADGKMRIVGRVKALAK 578
Cdd:cd17645 280 LQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFvpgermYRTGDLAKFLPDGNIEFLGRLDQQVK 350
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
136-336 |
8.39e-06 |
|
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: 48.97 E-value: 8.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 136 TYSEMEERIFHFGAGL-AALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALHETESQAILcgs 214
Cdd:cd05937 7 TYSETYDLVLRYAHWLhDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVI--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 215 anvanvlklmkngvmpqvpiiyvgtlpasldthgvqvvsfkqvemigaahleggaakgtgpLNDDDLALIMYTSGTTGDP 294
Cdd:cd05937 84 -------------------------------------------------------------VDPDDPAILIYTSGTTGLP 102
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 398009334 295 KGV-MHTHRTLAAGlhTLEPRVvdlLGQPHSDDVYlSYLPMAH 336
Cdd:cd05937 103 KAAaISWRRTLVTS--NLLSHD---LNLKNGDRTY-TCMPLYH 139
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
136-336 |
1.19e-05 |
|
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: 48.50 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 136 TYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIWSCSAVAATVYANLGEAALAHALhetesqailcgsa 215
Cdd:cd05940 5 TYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCL------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 216 NVANvlklmkngvmPQVPIIyvgtlpasldthgvqvvsfkqvemigaahleggaakgtgplnddDLALIMYTSGTTGDPK 295
Cdd:cd05940 72 NVSS----------AKHLVV--------------------------------------------DAALYIYTSGTTGLPK 97
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 398009334 296 GVMHTHRTLAAGLhtlepRVVDLLGQPHSDDVYLSYLPMAH 336
Cdd:cd05940 98 AAIISHRRAWRGG-----AFFAGSGGALPSDVLYTCLPLYH 133
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
444-613 |
2.08e-05 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 47.68 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 444 RLRIMLSGGGPL------SAATHEFvnvvfgRVVIGYGLTETicvgAIQI----PGD--TETNVTGLMEPGQEIKLldid 511
Cdd:PRK07445 231 QFRTILLGGAPAwpslleQARQLQL------RLAPTYGMTET----ASQIatlkPDDflAGNNSSGQVLPHAQITI---- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 512 eykhtdTPEPRGEMLSRGPYLFKGYYKQpeltreVLDEDGWFHTGDVGSFTADGKMRIVGRV--KALAKnclGEYIALEA 589
Cdd:PRK07445 297 ------PANQTGNITIQAQSLALGYYPQ------ILDSQGIFETDDLGYLDAQGYLHILGRNsqKIITG---GENVYPAE 361
|
170 180
....*....|....*....|....
gi 398009334 590 LEAVYSGNELLQpnGVCVLVHPDK 613
Cdd:PRK07445 362 VEAAILATGLVQ--DVCVLGLPDP 383
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
132-565 |
2.82e-05 |
|
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: 47.37 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 132 VVYVTYSEMEERIFHFGAGLAALGVTangnvsIYLDTCVEWLIGIYGIWSCSAVAAtvyanlgeaALAHALHETESQAIL 211
Cdd:cd05929 21 DVYSIALNRNARAAAAEGVWIADGVY------IYLINSILTVFAAAAAWKCGACPA---------YKSSRAPRAEACAII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 212 cGSANVANVLKLMKNGVMPQVPIIYvgtlpasldthgvqvvsfkqvemigaAHLEGGAAKgtgPLNDDDLA--LIMYTSG 289
Cdd:cd05929 86 -EIKAAALVCGLFTGGGALDGLEDY--------------------------EAAEGGSPE---TPIEDEAAgwKMLYSGG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 290 TTGDPKGVMhthRTLAAGLHTLEPRVVDLLGQPHS-DDVYLSYLPMAHIMEFTITNLFIFRGafigfGT--------PRT 360
Cdd:cd05929 136 TTGRPKGIK---RGLPGGPPDNDTLMAAALGFGPGaDSVYLSPAPLYHAAPFRWSMTALFMG-----GTlvlmekfdPEE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 361 LTDTTARPHGDLLTFnpsmlagVPRIFDTLkkaveAKLPpvgtlkrQVFDHAYQsrLAALKKGKDTpywnekvfAAPRAV 440
Cdd:cd05929 208 FLRLIERYRVTFAQF-------VPTMFVRL-----LKLP-------EAVRNAYD--LSSLKRVIHA--------AAPCPP 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 441 LGNrlRIMLSGGGPLsaaTHEFvnvvfgrvvigYGLTE----TICVGA--IQIPGDTETNVTGlmepgqEIKLLDIDEyK 514
Cdd:cd05929 259 WVK--EQWIDWGGPI---IWEY-----------YGGTEgqglTIINGEewLTHPGSVGRAVLG------KVHILDEDG-N 315
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 398009334 515 HTDTPEPrGEMLSRGPYLFKgYYKQPELTREVLDEDGWFHTGDVGSFTADG 565
Cdd:cd05929 316 EVPPGEI-GEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDG 364
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
280-596 |
2.87e-05 |
|
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: 47.01 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 280 DLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLEPRvvdLLGQPHSDDVYLSYlpMAHIMEFTItnlfifrgafigfgtpR 359
Cdd:cd17648 95 DLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSER---YFGRDNGDEAVLFF--SNYVFDFFV----------------E 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 360 TLTDTTARPHgDLLTFNPSMLAGVPRIFDTLKKAVEAKLPPVGTLkRQVFDHayqSRLaalkkgkdtpywnekvfaapra 439
Cdd:cd17648 154 QMTLALLNGQ-KLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSV-LQQYDL---ARL---------------------- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 440 vlgNRLRIMLSGGGPLSAATHEFVNVVF-GRVVIGYGLTETiCVGAIQI---PGDTETNVTGLMEPGQEIKLLDideykH 515
Cdd:cd17648 207 ---PHLKRVDAAGEEFTAPVFEKLRSRFaGLIINAYGPTET-TVTNHKRffpGDQRFDKSLGRPVRNTKCYVLN-----D 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 516 TDTPEP---RGEMLSRGPYLFKGYYKQPELTREVLDEDGW--------------FHTGDVGSFTADGKMRIVGRVKALAK 578
Cdd:cd17648 278 AMKRVPvgaVGELYLGGDGVARGYLNRPELTAERFLPNPFqteqerargrnarlYKTGDLVRWLPSGELEYLGRNDFQVK 357
|
330 340
....*....|....*....|.
gi 398009334 579 nCLGEYIALEALEAV---YSG 596
Cdd:cd17648 358 -IRGQRIEPGEVEAAlasYPG 377
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
135-336 |
1.84e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 44.51 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEwLIGIYgiWSCSaVAATVYA----NLGEAALAHALHETESQAI 210
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPE-FFEVY--WAAR-RSGLYYTpinwHLTAAEIAYIVDDSGAKVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 211 LcGSANVANVLKLMKNGVMPQVPIIYVGTLPASldthGVQvvSFKqvemigaahlEGGAAKGTGPLNDDDL-ALIMYTSG 289
Cdd:PRK08276 88 I-VSAALADTAAELAAELPAGVPLLLVVAGPVP----GFR--SYE----------EALAAQPDTPIADETAgADMLYSSG 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 398009334 290 TTGDPKGVmhthRTLAAGLHTLEP-----RVVDLLGQPHSDDVYLSYLPMAH 336
Cdd:PRK08276 151 TTGRPKGI----KRPLPGLDPDEApgmmlALLGFGMYGGPDSVYLSPAPLYH 198
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
131-301 |
2.41e-04 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 44.57 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 131 EVVYVTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIG------IYGIW-SCS-------------------- 183
Cdd:cd05943 95 ERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAmlatasIGAIWsSCSpdfgvpgvldrfgqiepkvl 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 184 -AVAATVYAnlgeaALAHAlHETESQAILCGSANVANVLKLMKNGVMPQV---PIIYVGTLPASLDTHGVQVVSFKQVEm 259
Cdd:cd05943 175 fAVDAYTYN-----GKRHD-VREKVAELVKGLPSLLAVVVVPYTVAAGQPdlsKIAKALTLEDFLATGAAGELEFEPLP- 247
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 398009334 260 igAAHleggaakgtgPLndddlaLIMYTSGTTGDPKGVMHTH 301
Cdd:cd05943 248 --FDH----------PL------YILYSSGTTGLPKCIVHGA 271
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
275-300 |
2.85e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 44.36 E-value: 2.85e-04
10 20
....*....|....*....|....*.
gi 398009334 275 PLNDDDLALIMYTSGTTGDPKGVMHT 300
Cdd:PRK00174 241 PMDAEDPLFILYTSGSTGKPKGVLHT 266
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
135-302 |
3.10e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 44.26 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 135 VTYSEMEERIFHFGAGLAALGVTANGNVSIYLDTCVEWLIGIYGIwsCSAVAATVYANLG--EAALAHALHETESQAILC 212
Cdd:PRK10252 484 FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAI--VEAGAAWLPLDTGypDDRLKMMLEDARPSLLIT 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 213 GSANVANvlklmkngvMPQVPIIYVGTLPASLDTHGVQVVSFKQvemigaahleggaakgtgPlndDDLALIMYTSGTTG 292
Cdd:PRK10252 562 TADQLPR---------FADVPDLTSLCYNAPLAPQGAAPLQLSQ------------------P---HHTAYIIFTSGSTG 611
|
170
....*....|
gi 398009334 293 DPKGVMHTHR 302
Cdd:PRK10252 612 RPKGVMVGQT 621
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
279-306 |
3.29e-04 |
|
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: 43.85 E-value: 3.29e-04
10 20
....*....|....*....|....*...
gi 398009334 279 DDLALIMYTSGTTGDPKGVMHTHRTLAA 306
Cdd:cd12115 105 DDLAYVIYTSGSTGRPKGVAIEHRNAAA 132
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
131-576 |
7.15e-04 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 42.81 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 131 EVVYVTYSEMEERIFHFGAGLAAlgVTANGN-VSIYLDTCVEWLIGIYGIWSCSAVAATVYA-NL-GEAA-LAHALHETE 206
Cdd:PRK12476 65 CAVELTWTQLGVRLRAVGARLQQ--VAGPGDrVAILAPQGIDYVAGFFAAIKAGTIAVPLFApELpGHAErLDTALRDAE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 207 SQAILCGSANVANVLKLMKNGVMPQVP-IIYVGTLPASLdthgvqvvsfkqvemigaahlegGAAKGTGPLNDDDLALIM 285
Cdd:PRK12476 143 PTVVLTTTAAAEAVEGFLRNLPRLRRPrVIAIDAIPDSA-----------------------GESFVPVELDTDDVSHLQ 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 286 YTSGTTGDPKGVMHTHRtlAAGLHTLEPRV-VDLLGQ-PHSddvyLSYLPMAHIMEFTItnlfifrgafIGF----GTPR 359
Cdd:PRK12476 200 YTSGSTRPPVGVEITHR--AVGTNLVQMILsIDLLDRnTHG----VSWLPLYHDMGLSM----------IGFpavyGGHS 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 360 TLTDTTA---RPH------GDLLTFNPsMLAGVPRIFDTLkkAVEAKLPPVGtlkrqvfdhayqsrlaalkKGKDtpywn 430
Cdd:PRK12476 264 TLMSPTAfvrRPQrwikalSEGSRTGR-VVTAAPNFAYEW--AAQRGLPAEG-------------------DDID----- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 431 ekvfaapravLGNrlRIMLSGGGPLSAATHEFVNVVFG-----RVVI--GYGLTE-TICVG------------------- 483
Cdd:PRK12476 317 ----------LSN--VVLIIGSEPVSIDAVTTFNKAFApyglpRTAFkpSYGIAEaTLFVAtiapdaepsvvyldreqlg 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 484 ---AIQIPGDTEtNVTGLMEPGQEIKLL---DIDEYKHTDTPEPR-GEMLSRGPYLFKGYYKQPELTREVL--------- 547
Cdd:PRK12476 385 agrAVRVAADAP-NAVAHVSCGQVARSQwavIVDPDTGAELPDGEvGEIWLHGDNIGRGYWGRPEETERTFgaklqsrla 463
|
490 500 510
....*....|....*....|....*....|....*...
gi 398009334 548 ---------DEDGWFHTGDVGsFTADGKMRIVGRVKAL 576
Cdd:PRK12476 464 egshadgaaDDGTWLRTGDLG-VYLDGELYITGRIADL 500
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
467-572 |
1.03e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 42.32 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 467 FG-RVVIGYGLTETicVGAIQIPGDTETNVTGLMEPGQEIKLLD---------IDEYKHTDTP-EPRGEMLSR-GPYLFK 534
Cdd:PRK13388 287 FGcQVEDGYGSSEG--AVIVVREPGTPPGSIGRGAPGVAIYNPEtltecavarFDAHGALLNAdEAIGELVNTaGAGFFE 364
|
90 100 110
....*....|....*....|....*....|....*...
gi 398009334 535 GYYKQPELTREVLdEDGWFHTGDVGSFTADGKMRIVGR 572
Cdd:PRK13388 365 GYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGR 401
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
443-572 |
1.36e-03 |
|
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: 41.62 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398009334 443 NRLRIMLSGGGPLSAATHEFVNVVFGRVVI--GYGLTETICVgAIQIPGDTET-NVTGLMEPGQEIKLLDIDEYKhtdtp 519
Cdd:cd17633 110 SKIKSIFSSGQKLFESTKKKLKNIFPKANLieFYGTSELSFI-TYNFNQESRPpNSVGRPFPNVEIEIRNADGGE----- 183
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 398009334 520 epRGEMLSRGPYLFKGYykqpeLTREVLDEDGWFHTGDVGSFTADGKMRIVGR 572
Cdd:cd17633 184 --IGKIFVKSEMVFSGY-----VRGGFSNPDGWMSVGDIGYVDEEGYLYLVGR 229
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
280-342 |
1.51e-03 |
|
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: 41.89 E-value: 1.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398009334 280 DLALIMYTSGTTGDPKGVMHTHRTLAAGLHTLEPRVVdllgqpHSDDVYLSYLPMAHIMEFTI 342
Cdd:cd05938 145 SPALYIYTSGTTGLPKAARISHLRVLQCSGFLSLCGV------TADDVIYITLPLYHSSGFLL 201
|
|
| |
