|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
10-561 |
0e+00 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 869.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 10 RPWLAHYPPGVPHDINPDSYTSLAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMP 89
Cdd:PRK07059 3 KIWLKSYPPGVPAEIDASQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQS-RGLAKGARVAIMMP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 90 NLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIVILANFAGNLEKILSQTAIEHVIVTQIGDLLGFpKKL 169
Cdd:PRK07059 82 NVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQQVLAKTAVKHVVVASMGDLLGF-KGH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 170 IVNAVVKYVKKMVPAYHLPGAISFGDALSRGSRQPLKPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWM 249
Cdd:PRK07059 161 IVNFVVRRVKKMVPAWSLPGHVRFNDALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 250 KPA----GVPDgQGIIVAALPLYHVYALTTNALASLKSGSMNLLITNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHP 325
Cdd:PRK07059 241 QPAfekkPRPD-QLNFVCALPLYHIFALTVCGLLGMRTGGRNILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 326 RINEVDFSELRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETSPVLCSNTVTEeGNRVGTIGIPWPSTYMKCVTEDG 405
Cdd:PRK07059 320 DFDKLDFSKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSPVATCNPVDA-TEFSGTIGLPLPSTEVSIRDDDG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 406 TEAALGEPGEIWAKGPQVFGGYYNRPDESAKVL-EDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVS 484
Cdd:PRK07059 399 NDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMtADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVA 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518832993 485 QCPGVLEVACVGVPNEKSGETVKIFVVKKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREE 561
Cdd:PRK07059 479 SHPGVLEVAAVGVPDEHSGEAVKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRDG 555
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
10-568 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 867.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 10 RPWLAHYPPGVPHDINPDSYTSLAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQNDLKLQKGDRIAIQMP 89
Cdd:PRK08974 3 KVWLNRYPADVPAEINPDRYQSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGLGLKKGDRVALMMP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 90 NLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIVILANFAGNLEKILSQTAIEHVIVTQIGDLLGFPKKL 169
Cdd:PRK08974 83 NLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKTPVKHVILTRMGDQLSTAKGT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 170 IVNAVVKYVKKMVPAYHLPGAISFGDALSRGSR-QPLKPVaIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVIcQDEW 248
Cdd:PRK08974 163 LVNFVVKYIKRLVPKYHLPDAISFRSALHKGRRmQYVKPE-LVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLE-QAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 249 MKPAGVPDGQGIIVAALPLYHVYALTTNALASLKSGSMNLLITNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRIN 328
Cdd:PRK08974 241 AYGPLLHPGKELVVTALPLYHIFALTVNCLLFIELGGQNLLITNPRDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 329 EVDFSELRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETSPVLCSNTVTEEGNRvGTIGIPWPSTYMKCVTEDGTEA 408
Cdd:PRK08974 321 ELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSVNPYDLDYYS-GSIGLPVPSTEIKLVDDDGNEV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 409 ALGEPGEIWAKGPQVFGGYYNRPDESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPG 488
Cdd:PRK08974 400 PPGEPGELWVKGPQVMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 489 VLEVACVGVPNEKSGETVKIFVVKKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREEELAKLKK 568
Cdd:PRK08974 480 VLEVAAVGVPSEVSGEAVKIFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAKVDN 559
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
12-567 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 798.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 12 WLAHYPPGVPHDINPDSYTSLAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQNDLKLQKGDRIAIQMPNL 91
Cdd:PRK05677 6 WKDKYPAGIAAEINPDEYPNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 92 LQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIVILANFAGNLEKILSQTAIEHVIVTQIGDLLGFPKKLIV 171
Cdd:PRK05677 86 LQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAEKVLPKTGVKHVIVTEVADMLPPLKRLLI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 172 NAVVKYVKKMVPAYHLPGAISFGDALSRGSRQPLKPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVIcQDEWMKP 251
Cdd:PRK05677 166 NAVVKHVKKMVPAYHLPQAVKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANML-QCRALMG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 252 AGVPDGQGIIVAALPLYHVYALTTNALASLKSGSMNLLITNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVD 331
Cdd:PRK05677 245 SNLNEGCEILIAPLPLYHIYAFTFHCMAMMLIGNHNILISNPRDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 332 FSELRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETSPVLCSNTVteEGNRVGTIGIPWPSTYMKCVTEDGTEAALG 411
Cdd:PRK05677 325 FSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPS--QAIQVGTIGIPVPSTLCKVIDDDGNELPLG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 412 EPGEIWAKGPQVFGGYYNRPDESAKVL-EDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVL 490
Cdd:PRK05677 403 EVGELCVKGPQVMKGYWQRPEATDEILdSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVL 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518832993 491 EVACVGVPNEKSGETVKIFVV-KKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREEELAKLK 567
Cdd:PRK05677 483 QCAAIGVPDEKSGEAIKVFVVvKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEELKKAG 560
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
7-560 |
0e+00 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 715.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 7 TQTRPWLAHYPPGVPHDINPDSYTSLAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQNDLKLQKGDRIAI 86
Cdd:PRK08751 2 SQARPWLQSYPAGVAAEIDLEQFRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGELQLKKGDRVAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 87 QMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIVILANFAGNLEKILSQTAIEHVIVTQIGDLLGFP 166
Cdd:PRK08751 82 MMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQVIADTPVKQVITTGLGDMLGFP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 167 KKLIVNAVVKYVKKMVPAYHLPGAISFGDALSRGSRQPLKPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVICQD 246
Cdd:PRK08751 162 KAALVNFVVKYVKKLVPEYRINGAIRFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 247 EWMKPAG-VPDGQGIIVAALPLYHVYALTTNALASLKSGSMNLLITNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHP 325
Cdd:PRK08751 242 QWLAGTGkLEEGCEVVITALPLYHIFALTANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 326 RINEVDFSELRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETSPVLCSNTVT-EEGNrvGTIGIPWPSTYMkCVTED 404
Cdd:PRK08751 322 GFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSPAACINPLTlKEYN--GSIGLPIPSTDA-CIKDD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 405 -GTEAALGEPGEIWAKGPQVFGGYYNRPDESAKVLE-DGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEV 482
Cdd:PRK08751 399 aGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDaDGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDV 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518832993 483 VSQCPGVLEVACVGVPNEKSGETVKIFVVKKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLRE 560
Cdd:PRK08751 479 IAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRD 556
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
12-560 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 691.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 12 WLAHYPPGVPHDINPDSYTSLAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQNDLKLQKGDRIAIQMPNL 91
Cdd:PRK12492 6 WNDKRPAGVPSTIDLAAYKSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 92 LQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIVILANFAGNLEKILSQTAIEHVIVTQIGDLLGFPKKLIV 171
Cdd:PRK12492 86 LQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLNMFGKLVQEVLPDTGIEYLIEAKMGDLLPAAKGWLV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 172 NAVVKYVKKMVPAYHLPGAISFGDALSRGSRQPLKPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMK- 250
Cdd:PRK12492 166 NTVVDKVKKMVPAYHLPQAVPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSq 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 251 --PAGVP---DGQGIIVAALPLYHVYALTTNALASLKSGSMNLLITNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHP 325
Cdd:PRK12492 246 lgPDGQPlmkEGQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMDHP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 326 RINEVDFSELRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETSPVLCSNTVTEEGnRVGTIGIPWPSTYMKCVTEDG 405
Cdd:PRK12492 326 GFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELA-RLGTVGIPVPGTALKVIDDDG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 406 TEAALGEPGEIWAKGPQVFGGYYNRPDESAKVLE-DGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVS 484
Cdd:PRK12492 405 NELPLGERGELCIKGPQVMKGYWQQPEATAEALDaEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVM 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518832993 485 QCPGVLEVACVGVPNEKSGETVKIFVVKKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLRE 560
Cdd:PRK12492 485 AHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRD 560
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
32-559 |
0e+00 |
|
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: 651.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 32 LAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNT 111
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQN-LGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 112 NPLYTPREMQHQFNDSGAKAIVIlanfagnlekilsqtaiehvivtqigdllgfpkklivnavvkyvkkmvpayhlpgAI 191
Cdd:cd05936 80 NPLYTPRELEHILNDSGAKALIV-------------------------------------------------------AV 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 192 SFGDALSRGSRqPLKPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMKPAGVPDGqgIIVAALPLYHVY 271
Cdd:cd05936 105 SFTDLLAAGAP-LGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEGDD--VVLAALPLFHVF 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 272 ALTTNALASLKSGSMNLLITNPRDLNAfIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSVAD 351
Cdd:cd05936 182 GLTVALLLPLALGATIVLIPRFRPIGV-LKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAE 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 352 RWQKLTGNKPAEGYGLSETSPVLCSNTVTEEgNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRP 431
Cdd:cd05936 261 RFEELTGVPIVEGYGLTETSPVVAVNPLDGP-RKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRP 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 432 DESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVV 511
Cdd:cd05936 340 EETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVV 419
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 518832993 512 KKDEA-LTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLR 559
Cdd:cd05936 420 LKEGAsLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
32-565 |
0e+00 |
|
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: 529.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 32 LAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNT 111
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALR-ALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 112 NPLYTPREMQHQFNDSGAKAIVIlanfagnlekilsqtaiehvivtqigdllgfpkklivnavvkyvkkmvpayhlpgai 191
Cdd:COG0318 80 NPRLTAEELAYILEDSGARALVT--------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 192 sfgdalsrgsrqplkpvaikntdlAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMKPagvpDGQGIIVAALPLYHVY 271
Cdd:COG0318 103 ------------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGL----TPGDVVLVALPLFHVF 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 272 ALTTNALASLKSGSMNLLITNpRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSVAD 351
Cdd:COG0318 155 GLTVGLLAPLLAGATLVLLPR-FDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLE 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 352 RWQKLTGNKPAEGYGLSETSPVLCSNTVTEEGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRP 431
Cdd:COG0318 234 RFEERFGVRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDP 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 432 DESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVV 511
Cdd:COG0318 314 EATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVV 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 518832993 512 KKDEA-LTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREEELAK 565
Cdd:COG0318 394 LRPGAeLDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAG 448
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
5-568 |
6.58e-175 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 506.85 E-value: 6.58e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 5 TPTQTRPWLAHYPPGVPHDINPDSyTSLAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRI 84
Cdd:PRK05605 8 SAFADKPWLQSYAPWTPHDLDYGD-TTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLR-ALGVRPGDRV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 85 AIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIVILANFAGNLEKILSQTAIEHVIVTQIGDLLG 164
Cdd:PRK05605 86 AIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTPLETIVSVNMIAAMP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 165 FPKKLIVNAVVKYVKKMVPAYH--LPGAISFgDALSRGSRQPLKPVA----IKNTDLAFVQYTGGTTGVSKGAALTHRNI 238
Cdd:PRK05605 166 LLQRLALRLPIPALRKARAALTgpAPGTVPW-ETLVDAAIGGDGSDVshprPTPDDVALILYTSGTTGKPKGAQLTHRNL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 239 ISNVICQDEWMKpaGVPDGQGIIVAALPLYHVYALTTN-ALASLKSGSMNLLitnPR-DLNAFIDDLKKYKITAFTGLNT 316
Cdd:PRK05605 245 FANAAQGKAWVP--GLGDGPERVLAALPMFHAYGLTLClTLAVSIGGELVLL---PApDIDLILDAMKKHPPTWLPGVPP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 317 LYNGLLNHPRINEVDFSELRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETSPVLCSNTVTEEgNRVGTIGIPWPST 396
Cdd:PRK05605 320 LYEKIAEAAEERGVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVGNPMSDD-RRPGYVGVPFPDT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 397 YMKCVT-EDGTEA-ALGEPGEIWAKGPQVFGGYYNRPDESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNV 474
Cdd:PRK05605 399 EVRIVDpEDPDETmPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 475 YPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKD-EALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKI 553
Cdd:PRK05605 479 YPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPgAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKV 558
|
570
....*....|....*
gi 518832993 554 LRRPLREEELAKLKK 568
Cdd:PRK05605 559 RRREVREELLEKLGA 573
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
10-565 |
7.80e-158 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 462.97 E-value: 7.80e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 10 RPWLAHYPPGVPHDINPDSyTSLAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMP 89
Cdd:PRK06710 5 KPWLKSYPEEIPSTISYDI-QPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQK-LGVEKGDRVAIMLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 90 NLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIVILANFAGNLEKILSQTAIEHVIVTQIGDLLGFPKKL 169
Cdd:PRK06710 83 NCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSATKIEHVIVTRIADFLPFPKNL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 170 IVNAVVKYVKKMVPAYHLPGAISFGDALSRGSRQPLKPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWM 249
Cdd:PRK06710 163 LYPFVQKKQSNLVVKVSESETIHLWNSVEKEVNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 250 kpAGVPDGQGIIVAALPLYHVYALTTNALASLKSGSMNLLItnPR-DLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRIN 328
Cdd:PRK06710 243 --YNCKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLI--PKfDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 329 EVDFSELRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETSPVLCSNTVTEEgnRV-GTIGIPWPSTYMKCVT-EDGT 406
Cdd:PRK06710 319 EYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEK--RVpGSIGVPWPDTEAMIMSlETGE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 407 EAALGEPGEIWAKGPQVFGGYYNRPDESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQC 486
Cdd:PRK06710 397 ALPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEH 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 487 PGVLEVACVGVPNEKSGETVKIFVV-KKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREEELAK 565
Cdd:PRK06710 477 EKVQEVVTIGVPDPYRGETVKAFVVlKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEKRK 556
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
31-561 |
4.56e-148 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 435.87 E-value: 4.56e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 31 SLAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVN 110
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALA-ALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 111 TNPLYTPREMQHQFNDSGAKAIVILANFAGNLEKILSQT-AIEHVIVTQIGDLLGFPKKLIvnavvkyvkkmvpayhlpg 189
Cdd:PRK07656 85 LNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLpALEHVVICETEEDDPHTEKMK------------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 190 aiSFGDALSRGSrQPLKPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVicqDEWMKPAGVPDGQGIIvAALPLYH 269
Cdd:PRK07656 146 --TFTDFLAAGD-PAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNA---ADWAEYLGLTEGDRYL-AANPFFH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 270 VYALTTNALASLKSGSmNLLITNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSV 349
Cdd:PRK07656 219 VFGYKAGVNAPLMRGA-TILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVAL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 350 ADRWQKLTG-NKPAEGYGLSETSPVLCSNTVTEEGNRV-GTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGY 427
Cdd:PRK07656 298 LERFESELGvDIVLTGYGLSEASGVTTFNRLDDDRKTVaGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 428 YNRPDESAKVL-EDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETV 506
Cdd:PRK07656 378 YDDPEATAAAIdADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVG 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 518832993 507 KIFVVKKDEA-LTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREE 561
Cdd:PRK07656 458 KAYVVLKPGAeLTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
30-568 |
1.67e-127 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 384.31 E-value: 1.67e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 30 TSLAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQNDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVV 109
Cdd:PRK08314 10 TSLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 110 NTNPLYTPREMQHQFNDSGAKAIVILANFAGNLEKILSQTAIEHVIVTQIGDLLGFPKKLIVNAVVKyVKKMVPAYHLPG 189
Cdd:PRK08314 90 PVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHVIVAQYSDYLPAEPEIAVPAWLR-AEPPLQALAPGG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 190 AISFGDALSRGSRQPlkPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMKpaGVPDgqGIIVAALPLYH 269
Cdd:PRK08314 169 VVAWKEALAAGLAPP--PHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSN--STPE--SVVLAVLPLFH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 270 VYALTTNALASLKSGSMNLLItnPR-DLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTS 348
Cdd:PRK08314 243 VTGMVHSMNAPIYAGATVVLM--PRwDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMPEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 349 VADRWQKLTGNKPAEGYGLSETSPVLCSNtvTEEGNRVGTIGIPWPSTYMKCVT-EDGTEAALGEPGEIWAKGPQVFGGY 427
Cdd:PRK08314 321 VAERLKELTGLDYVEGYGLTETMAQTHSN--PPDRPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFKGY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 428 YNRPDESAKV-LE-DG--WFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSG 503
Cdd:PRK08314 399 WNRPEATAEAfIEiDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRG 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518832993 504 ETVKIFVVKKDEA---LTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREEELAKLKK 568
Cdd:PRK08314 479 ETVKAVVVLRPEArgkTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKARAAK 546
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
27-560 |
2.06e-126 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 380.69 E-value: 2.06e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 27 DSYTSLAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGl 106
Cdd:PRK06187 3 DYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALR-ALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 107 TVVNT-NPLYTPREMQHQFNDSGAKAIVILANFAGNLEKILSQ-TAIEHVIVTQIGDLLGFPKklivnavvkyvkkMVPA 184
Cdd:PRK06187 81 AVLHPiNIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQlPTVRTVIVEGDGPAAPLAP-------------EVGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 185 YHlpgaisfgDALSRGSRQPLKPvAIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMK--PAGVpdgqgiIV 262
Cdd:PRK06187 148 YE--------ELLAAASDTFDFP-DIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKlsRDDV------YL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 263 AALPLYHVYALTTnALASLKSGSMNLLitnPR--DLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSA 340
Cdd:PRK06187 213 VIVPMFHVHAWGL-PYLALMAGAKQVI---PRrfDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIY 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 341 GGMALQTSVADRWQKLTGNKPAEGYGLSETSPVLCSNT----VTEEGNRVGTIGIPWPSTYMKCVTEDGTE--AALGEPG 414
Cdd:PRK06187 289 GGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVLPpedqLPGQWTKRRSAGRPLPGVEARIVDDDGDElpPDGGEVG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 415 EIWAKGPQVFGGYYNRPDESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVAC 494
Cdd:PRK06187 369 EIIVRGPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAV 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518832993 495 VGVPNEKSGETVKIFVV-KKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLRE 560
Cdd:PRK06187 449 IGVPDEKWGERPVAVVVlKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLRE 515
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
36-470 |
7.30e-121 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 362.79 E-value: 7.30e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 36 IEEGVKRFSSAPAYACM-GKQITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPL 114
Cdd:pfam00501 1 LERQAARTPDKTALEVGeGRRLTYRELDERANRLAAGLRA-LGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 115 YTPREMQHQFNDSGAKAIVILANFAgnLEKILS-QTAIEHVIVTQIGDLLGFPKKLIVNAVVKYVKKmvpayhlpgaisf 193
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDALK--LEELLEaLGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADV------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 194 gdalsrgsrQPLKPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMKPAGVPDGQGIIVAALPLYHVYAL 273
Cdd:pfam00501 145 ---------PPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 274 TTNALASLKSGSMNLLI--TNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSVAD 351
Cdd:pfam00501 216 SLGLLGPLLAGATVVLPpgFPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELAR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 352 RWQKLTGNKPAEGYGLSETSPVLCSN-TVTEEGNRVGTIGIPWPSTYMKCV-TEDGTEAALGEPGEIWAKGPQVFGGYYN 429
Cdd:pfam00501 296 RFRELFGGALVNGYGLTETTGVVTTPlPLDEDLRSLGSVGRPLPGTEVKIVdDETGEPVPPGEPGELCVRGPGVMKGYLN 375
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 518832993 430 RPDESAKVL-EDGWFKTGDIGVMTADGYFKIVDRKKDMILVS 470
Cdd:pfam00501 376 DPELTAEAFdEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
46-555 |
2.51e-119 |
|
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: 359.62 E-value: 2.51e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 46 APAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFN 125
Cdd:cd17631 11 RTALVFGGRSLTYAELDERVNRLAHALR-ALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 126 DSGAKAIVilanfagnlekilsqtaiehvivtqigdllgfpkklivnavvkyvkkmvpayhlpgaisfgdalsrgsrqpl 205
Cdd:cd17631 90 DSGAKVLF------------------------------------------------------------------------ 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 206 kpvaiknTDLAFVQYTGGTTGVSKGAALTHRNIISNVIcqdEWMKPAGVPDGQGIIVAAlPLYHVYALTTNALASLKSGS 285
Cdd:cd17631 98 -------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAV---NALAALDLGPDDVLLVVA-PLFHIGGLGVFTLPTLLRGG 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 286 MNLLITNPrDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSVADRWQKlTGNKPAEGY 365
Cdd:cd17631 167 TVVILRKF-DPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQA-RGVKFVQGY 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 366 GLSETSPVLCSNTVTEEGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRPDESAKVLEDGWFKT 445
Cdd:cd17631 245 GMTETSPGVTFLSPEDHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWFHT 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 446 GDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKDEA-LTEDSITR 524
Cdd:cd17631 325 GDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAeLDEDELIA 404
|
490 500 510
....*....|....*....|....*....|.
gi 518832993 525 YCRENLTAYKVPKHIEFRTELPKSNVGKILR 555
Cdd:cd17631 405 HCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
53-554 |
3.09e-119 |
|
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: 361.15 E-value: 3.09e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 53 GKQITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAI 132
Cdd:cd05911 8 GKELTYAQLRTLSRRLAAGLRK-LGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 133 VILANFagnLEKILSQTAIehvivtqigdlLGFPKKLIVnavvkyVKKMVPAYHLPGAISFGDALSRGSRQPLkPVAIKN 212
Cdd:cd05911 87 FTDPDG---LEKVKEAAKE-----------LGPKDKIIV------LDDKPDGVLSIEDLLSPTLGEEDEDLPP-PLKDGK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 213 TDLAFVQYTGGTTGVSKGAALTHRNIISNV-ICQDEWMKPAGVPDgqgIIVAALPLYHVYALTTnALASLKSGsMNLLIT 291
Cdd:cd05911 146 DDTAAILYSSGTTGLPKGVCLSHRNLIANLsQVQTFLYGNDGSND---VILGFLPLYHIYGLFT-TLASLLNG-ATVIIM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 292 NPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSVADRWQKLTGNKPA-EGYGLSET 370
Cdd:cd05911 221 PKFDSELFLDLIEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIkQGYGMTET 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 371 SPVLCSNTVTEegNRVGTIGIPWPSTYMKCVTEDGTEA-ALGEPGEIWAKGPQVFGGYYNRPDESAKVL-EDGWFKTGDI 448
Cdd:cd05911 301 GGILTVNPDGD--DKPGSVGRLLPNVEAKIVDDDGKDSlGPNEPGEICVRGPQVMKGYYNNPEATKETFdEDGWLHTGDI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 449 GVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKD-EALTEDSITRYCR 527
Cdd:cd05911 379 GYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPgEKLTEKEVKDYVA 458
|
490 500 510
....*....|....*....|....*....|
gi 518832993 528 ENLTAYKvpKH---IEFRTELPKSNVGKIL 554
Cdd:cd05911 459 KKVASYK--QLrggVVFVDEIPKSASGKIL 486
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
214-554 |
3.36e-115 |
|
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: 345.42 E-value: 3.36e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 214 DLAFVQYTGGTTGVSKGAALTHRNIISNVIcqdeWMKPAGVPDGQGIIVAALPLYHVyALTTNALASLKSGSMNLLITnP 293
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAA----ALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLP-K 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 294 RDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETSPV 373
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 374 LCSNTVTEEGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRPDESAKVLEDGWFKTGDIGVMTA 453
Cdd:cd04433 155 VATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 454 DGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKDEA-LTEDSITRYCRENLTA 532
Cdd:cd04433 235 DGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGAdLDAEELRAHVRERLAP 314
|
330 340
....*....|....*....|..
gi 518832993 533 YKVPKHIEFRTELPKSNVGKIL 554
Cdd:cd04433 315 YKVPRRVVFVDALPRTASGKID 336
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
12-566 |
1.96e-102 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 320.45 E-value: 1.96e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 12 WLAHYPPGVPHDIN-PDSYTSLAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPN 90
Cdd:PRK06178 14 QQAAWPAGIPREPEyPHGERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQ-RGVGAGDRVAVFLPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 91 LLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIVILANFAGNLEKILSQTAIEHVIVTQIGDLLGFPKKLI 170
Cdd:PRK06178 93 CPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHVIVTSLADVLPAEPTLP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 171 VNAVVKyvkkmVPAYHLPGAISFGDALSRGSRQ-PLKPVAIKntDLAFVQYTGGTTGVSKGAALTHRNII----SNVicq 245
Cdd:PRK06178 173 LPDSLR-----APRLAAAGAIDLLPALRACTAPvPLPPPALD--ALAALNYTGGTTGMPKGCEHTQRDMVytaaAAY--- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 246 dewmkPAGVPDGQG-IIVAALPLYHVYALTTNALASLKSGSMNLLITnpR-DLNAFIDDLKKYKITAFTGLNTLYNGLLN 323
Cdd:PRK06178 243 -----AVAVVGGEDsVFLSFLPEFWIAGENFGLLFPLFSGATLVLLA--RwDAVAFMAAVERYRVTRTVMLVDNAVELMD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 324 HPRINEVDFSELRITSAGGMALQTSVA--DRWQKLTGNKPAEG-YGLSETSpvlCSNTVTEeGNRVGT---------IGI 391
Cdd:PRK06178 316 HPRFAEYDLSSLRQVRVVSFVKKLNPDyrQRWRALTGSVLAEAaWGMTETH---TCDTFTA-GFQDDDfdllsqpvfVGL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 392 PWPSTYMK-CVTEDGTEAALGEPGEIWAKGPQVFGGYYNRPDESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVS 470
Cdd:PRK06178 392 PVPGTEFKiCDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVN 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 471 GFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKDEA-LTEDSITRYCRENLTAYKVPKhIEFRTELPKSN 549
Cdd:PRK06178 472 GMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGAdLTAAALQAWCRENMAVYKVPE-IRIVDALPMTA 550
|
570
....*....|....*..
gi 518832993 550 VGKIlrrplREEELAKL 566
Cdd:PRK06178 551 TGKV-----RKQDLQAL 562
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
55-558 |
1.97e-101 |
|
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: 313.26 E-value: 1.97e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 55 QITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIVI 134
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSN-KGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 135 LANfagnLEkilsqtaiehvivtqigdllgfpkklivnavvkyvkkmvpayhlpgaisfgdalsrgsrqplkpvaikntD 214
Cdd:cd05935 80 GSE----LD----------------------------------------------------------------------D 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 215 LAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWmkpAGVpDGQGIIVAALPLYHVYALTTNALASLKSGSMNLLITNpR 294
Cdd:cd05935 86 LALIPYTSGTTGLPKGCMHTHFSAAANALQSAVW---TGL-TPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMAR-W 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 295 DLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETSPVL 374
Cdd:cd05935 161 DRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQT 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 375 CSNTVTEEgnRVGTIGIPWPSTYMKCVT-EDGTEAALGEPGEIWAKGPQVFGGYYNRPDESAKV-LEDG---WFKTGDIG 449
Cdd:cd05935 241 HTNPPLRP--KLQCLGIP*FGVDARVIDiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESfIEIKgrrFFRTGDLG 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 450 VMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKDE---ALTEDSITRYC 526
Cdd:cd05935 319 YMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEyrgKVTEEDIIEWA 398
|
490 500 510
....*....|....*....|....*....|..
gi 518832993 527 RENLTAYKVPKHIEFRTELPKSNVGKILRRPL 558
Cdd:cd05935 399 REQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
31-561 |
3.98e-99 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 310.33 E-value: 3.98e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 31 SLAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVN 110
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALL-DLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 111 TNPLYTPREMQHQFNDSGAKAIVILANFAGNLEKILSQTAIEHVIVTQIGDLLGFPKklivnavvkyvkkmvpayhlpGA 190
Cdd:PRK08316 91 VNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPG---------------------GW 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 191 ISFGDALSRGSRQPLkPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNII----SNVICQDewMKPAGVPdgqgiiVAALP 266
Cdd:PRK08316 150 LDFADWAEAGSVAEP-DVELADDDLAQILYTSGTESLPKGAMLTHRALIaeyvSCIVAGD--MSADDIP------LHALP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 267 LYHVYALTTNALASLKSGSMNLLITNPrDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQ 346
Cdd:PRK08316 221 LYHCAQLDVFLGPYLYVGATNVILDAP-DPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 347 TSVADRWQ-KLTGNKPAEGYGLSETSPVlcsNTV---TEEGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQ 422
Cdd:PRK08316 300 VEVLKELReRLPGLRFYNCYGQTEIAPL---ATVlgpEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 423 VFGGYYNRPDESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKS 502
Cdd:PRK08316 377 LMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKW 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 503 GETVKIFVVKKDEA-LTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREE 561
Cdd:PRK08316 457 IEAVTAVVVPKAGAtVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRER 516
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
20-558 |
4.37e-97 |
|
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: 304.54 E-value: 4.37e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 20 VPHDINPDSYTSLAALieegvkRFSSAPAY--ACMGKQITFSELDTLSQQFASFLQNDLkLQKGDRIAIQMPNLLQYPIA 97
Cdd:cd05904 1 LPTDLPLDSVSFLFAS------AHPSRPALidAATGRALTYAELERRVRRLAAGLAKRG-GRKGDVVLLLSPNSIEFPVA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 98 MFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIVILANfagNLEKILSqtaiehvivtqigdlLGFPkklivnaVVky 177
Cdd:cd05904 74 FLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAE---LAEKLAS---------------LALP-------VV-- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 178 vkkMVPAYHLPGAiSFGDALSRGSRQPLKPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNViCQDEWMKpAGVPDG 257
Cdd:cd05904 127 ---LLDSAEFDSL-SFSDLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMV-AQFVAGE-GSNSDS 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 258 QGIIVAALPLYHVYALTTNALASLKSGSMnLLITNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRI 337
Cdd:cd05904 201 EDVFLCVLPMFHIYGLSSFALGLLRLGAT-VVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQ 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 338 TSAGGMALQTSVADRW-QKLTGNKPAEGYGLSETSPVLCSNTVTEEGN-RVGTIGIPWPSTYMKCV-TEDGTEAALGEPG 414
Cdd:cd05904 280 IMSGAAPLGKELIEAFrAKFPNVDLGQGYGMTESTGVVAMCFAPEKDRaKYGSVGRLVPNVEAKIVdPETGESLPPNQTG 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 415 EIWAKGPQVFGGYYNRPDESAK-VLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVA 493
Cdd:cd05904 360 ELWIRGPSIMKGYLNNPEATAAtIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAA 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518832993 494 CVGVPNEKSGETVKIFVVKKDEA-LTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPL 558
Cdd:cd05904 440 VIPYPDEEAGEVPMAFVVRKPGSsLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
53-560 |
5.06e-93 |
|
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: 293.83 E-value: 5.06e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 53 GKQITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAI 132
Cdd:cd05926 12 TPALTYADLAELVDDLARQLAA-LGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 133 VILANFAGNLEKILSQTAIEHVivtqigdLLGFPKKLIVNAVVKyvkkmvpayhlpGAISFGDALSRGSRQPLKPvaiKN 212
Cdd:cd05926 91 LTPKGELGPASRAASKLGLAIL-------ELALDVGVLIRAPSA------------ESLSNLLADKKNAKSEGVP---LP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 213 TDLAFVQYTGGTTGVSKGAALTHRNIISNV--ICQDEWMKPAgvpDgqgIIVAALPLYHVYALTTNALASLKSGSmNLLI 290
Cdd:cd05926 149 DDLALILHTSGTTGRPKGVPLTHRNLAASAtnITNTYKLTPD---D---RTLVVMPLFHVHGLVASLLSTLAAGG-SVVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 291 TNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHP-RINEVDFSELRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSE 369
Cdd:cd05926 222 PPRFSASTFWPDVRDYNATWYTAVPTIHQILLNRPePNPESPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 370 TSPVLCSNTVTEEGNRVGTIGIPwPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRPDESAKV-LEDGWFKTGDI 448
Cdd:cd05926 302 AAHQMTSNPLPPGPRKPGSVGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAaFKDGWFRTGDL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 449 GVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVV-KKDEALTEDSITRYCR 527
Cdd:cd05926 381 GYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVlREGASVTEEELRAFCR 460
|
490 500 510
....*....|....*....|....*....|...
gi 518832993 528 ENLTAYKVPKHIEFRTELPKSNVGKILRRPLRE 560
Cdd:cd05926 461 KHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
54-565 |
3.58e-91 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 290.86 E-value: 3.58e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 54 KQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIV 133
Cdd:COG0365 38 RTLTYAELRREVNRFANALR-ALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 134 ILANFAGNLEKILSQTAIEhvivtQIGDLLGFPKKLIVnavvkyVKKMVPAYHLPGAISFGDALSRGSrQPLKPVAIKNT 213
Cdd:COG0365 117 TADGGLRGGKVIDLKEKVD-----EALEELPSLEHVIV------VGRTGADVPMEGDLDWDELLAAAS-AEFEPEPTDAD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 214 DLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEW---MKPAGVpdgqgiIVAALPLYHVYALTTNALASLKSGSMNLL- 289
Cdd:COG0365 185 DPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYvldLKPGDV------FWCTADIGWATGHSYIVYGPLLNGATVVLy 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 290 --ITNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHP--RINEVDFSELRITSAGGMALQTSVADRWQKLTGNKPAEGY 365
Cdd:COG0365 259 egRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGdePLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGW 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 366 GLSETSPVLCSNTVTEEgNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQ--VFGGYYNRPDESAKV---LED 440
Cdd:COG0365 339 GQTETGGIFISNLPGLP-VKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPWpgMFRGYWNDPERYRETyfgRFP 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 441 GWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKK-----DE 515
Cdd:COG0365 418 GWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKpgvepSD 497
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 518832993 516 ALTEDsITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREEELAK 565
Cdd:COG0365 498 ELAKE-LQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGR 546
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
30-564 |
1.93e-87 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 283.38 E-value: 1.93e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 30 TSLAALIEEGVKRFSSAPAYAC--------MGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGA 101
Cdd:PRK07529 25 ASTYELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLH-SLGVGPGDVVAFLLPNLPETHFALWGG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 102 LRAGLtVVNTNPLYTPREMQHQFNDSGAKAIVILANFAG-----NLEKILSQ-TAIEHVIVTQIGDLLGFPKKLIVnavv 175
Cdd:PRK07529 104 EAAGI-ANPINPLLEPEQIAELLRAAGAKVLVTLGPFPGtdiwqKVAEVLAAlPELRTVVEVDLARYLPGPKRLAV---- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 176 kyvkKMVPAYHLPGAISFGDALSRGSRQPL-KPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVicqdeWMKPAGV 254
Cdd:PRK07529 179 ----PLIRRKAHARILDFDAELARQPGDRLfSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANA-----WLGALLL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 255 PDGQG-IIVAALPLYHVYALTTNALASLKSGSMNLLIT-----NPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPrIN 328
Cdd:PRK07529 250 GLGPGdTVFCGLPLFHVNALLVTGLAPLARGAHVVLATpqgyrGPGVIANFWKIVERYRINFLSGVPTVYAALLQVP-VD 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 329 EVDFSELRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETSPVLCSNTVTEEgNRVGTIGIPWPSTYMKCV--TEDGT 406
Cdd:PRK07529 329 GHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPDGE-RRIGSVGLRLPYQRVRVVilDDAGR 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 407 ---EAALGEPGEIWAKGPQVFGGYYNRPDESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVV 483
Cdd:PRK07529 408 ylrDCAVDEVGVLCIAGPNVFSGYLEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEAL 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 484 SQCPGVLEVACVGVPNEKSGETVKIFV-VKKDEALTEDSITRYCRENL---TAykVPKHIEFRTELPKSNVGKILRRPLR 559
Cdd:PRK07529 488 LRHPAVALAAAVGRPDAHAGELPVAYVqLKPGASATEAELLAFARDHIaerAA--VPKHVRILDALPKTAVGKIFKPALR 565
|
....*
gi 518832993 560 EEELA 564
Cdd:PRK07529 566 RDAIR 570
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
56-559 |
1.59e-85 |
|
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: 274.63 E-value: 1.59e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 56 ITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIVIL 135
Cdd:cd05959 30 LTYAELEAEARRVAGALRA-LGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 136 ANFAGNLEKIL--SQTAIEHVIVTQigdllgfpkklivnavvkyvkkmvPAYHLPGAISFGDALSRGSRQpLKPVAIKNT 213
Cdd:cd05959 109 GELAPVLAAALtkSEHTLVVLIVSG------------------------GAGPEAGALLLAELVAAEAEQ-LKPAATHAD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 214 DLAFVQYTGGTTGVSKGAALTHRNIIsnVICqDEWMKPAGVPDGQGIIVAALPLYHVYALTTNALASLKSGSMNLLITNP 293
Cdd:cd05959 164 DPAFWLYSSGSTGRPKGVVHLHADIY--WTA-ELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 294 RDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETSPV 373
Cdd:cd05959 241 PTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 374 LCSNTvtEEGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRPDESAKVLEDGWFKTGDIGVMTA 453
Cdd:cd05959 321 FLSNR--PGRVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGEWTRTGDKYVRDD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 454 DGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKD-----EALTEDsITRYCRE 528
Cdd:cd05959 399 DGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPgyedsEALEEE-LKEFVKD 477
|
490 500 510
....*....|....*....|....*....|.
gi 518832993 529 NLTAYKVPKHIEFRTELPKSNVGKILRRPLR 559
Cdd:cd05959 478 RLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
53-560 |
1.10e-84 |
|
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: 270.32 E-value: 1.10e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 53 GKQITFSELDTLSQQFASFLQNDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAI 132
Cdd:cd05941 9 GDSITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 133 Vilanfagnlekilsqtaiehvivtqigdllgfpkklivnavvkyvkkmvpayhlpgaisfgdalsrgsrqplkpvaikn 212
Cdd:cd05941 89 L------------------------------------------------------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 213 tDLAFVQYTGGTTGVSKGAALTHRNIISNVIC-QDEW-MKPAGVpdgqgiIVAALPLYHVYALTTNALASLKSGSMNLLI 290
Cdd:cd05941 90 -DPALILYTSGTTGRPKGVVLTHANLAANVRAlVDAWrWTEDDV------LLHVLPLHHVHGLVNALLCPLFAGASVEFL 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 291 TNPRDLNAFIDDLKKyKITAFTGLNTLYNGLLNHPRINEVD--------FSELRITSAGGMALQTSVADRWQKLTGNKPA 362
Cdd:cd05941 163 PKFDPKEVAISRLMP-SITVFMGVPTIYTRLLQYYEAHFTDpqfaraaaAERLRLMVSGSAALPVPTLEEWEAITGHTLL 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 363 EGYGLSETSPVLcSNTVTEEgNRVGTIGIPWPSTYMKCVTEDGTEAAL-GEPGEIWAKGPQVFGGYYNRPDESAK-VLED 440
Cdd:cd05941 242 ERYGMTEIGMAL-SNPLDGE-RRPGTVGMPLPGVQARIVDEETGEPLPrGEVGEIQVRGPSVFKEYWNKPEATKEeFTDD 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 441 GWFKTGDIGVMTADGYFKIVDRKKDMILVS-GFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKDE--AL 517
Cdd:cd05941 320 GWFKTGDLGVVDEDGYYWILGRSSVDIIKSgGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGaaAL 399
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 518832993 518 TEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLRE 560
Cdd:cd05941 400 SLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
32-567 |
1.58e-84 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 273.57 E-value: 1.58e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 32 LAALIEEGVKRFSSAPA--YACMGKQITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVV 109
Cdd:PRK12583 20 IGDAFDATVARFPDREAlvVRHQALRYTWRQLADAVDRLARGLLA-LGVQPGDRVGIWAPNCAEWLLTQFATARIGAILV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 110 NTNPLYTPREMQHQFNDSGAKAIVILANFAGNLEKILSQTAIEHVIVTQIGDLLG--FPKklivnavVKYVKKMVPAyHL 187
Cdd:PRK12583 99 NINPAYRASELEYALGQSGVRWVICADAFKTSDYHAMLQELLPGLAEGQPGALACerLPE-------LRGVVSLAPA-PP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 188 PGAISFGDALSRG---SRQPLKPV--AIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVicqdeWMkpagVPDGQGI-- 260
Cdd:PRK12583 171 PGFLAWHELQARGetvSREALAERqaSLDRDDPINIQYTSGTTGFPKGATLSHHNILNNG-----YF----VAESLGLte 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 261 ---IVAALPLYHVYALTTNALASLKSGSMNLLITNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRi 337
Cdd:PRK12583 242 hdrLCVPVPLYHCFGMVLANLGCMTVGACLVYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLR- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 338 tsAGGMALQTSVADRWQKLTGN-KPAE---GYGLSETSPVLCSNTVTEE-GNRVGTIGIPWPSTYMKCVTEDGTEAALGE 412
Cdd:PRK12583 321 --TGIMAGAPCPIEVMRRVMDEmHMAEvqiAYGMTETSPVSLQTTAADDlERRVETVGRTQPHLEVKVVDPDGATVPRGE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 413 PGEIWAKGPQVFGGYYNRPDESAKVL-EDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLE 491
Cdd:PRK12583 399 IGELCTRGYSVMKGYWNNPEATAESIdEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVAD 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518832993 492 VACVGVPNEKSGETVKIFVV-KKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREEELAKLK 567
Cdd:PRK12583 479 VQVFGVPDEKYGEEIVAWVRlHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREISIEELA 555
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
32-568 |
4.41e-83 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 269.76 E-value: 4.41e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 32 LAALIEEGVKRFSSAPA--YACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVV 109
Cdd:PRK08315 18 IGQLLDRTAARYPDREAlvYRDQGLRWTYREFNEEVDALAKGLL-ALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 110 NTNPLYTPREMQHQFNDSGAKAIVILANF-----AGNLEKILSQTAiehviVTQIGDL--LGFPKklivnavVKYVKKMV 182
Cdd:PRK08315 97 TINPAYRLSELEYALNQSGCKALIAADGFkdsdyVAMLYELAPELA-----TCEPGQLqsARLPE-------LRRVIFLG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 183 PAYHlPGAISFGDALSRGSRQPLKPVA-----IKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMKpAGVPDG 257
Cdd:PRK08315 165 DEKH-PGMLNFDELLALGRAVDDAELAarqatLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMK-LTEEDR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 258 QGIIVaalPLYHVYALTTNALASLKSGSmNLLITNPrdlnAFiDDLK------KYKITAFTGLNTLYNGLLNHPRINEVD 331
Cdd:PRK08315 243 LCIPV---PLYHCFGMVLGNLACVTHGA-TMVYPGE----GF-DPLAtlaaveEERCTALYGVPTMFIAELDHPDFARFD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 332 FSELRitsAGGMALQTSvadrwqkltgnkPAE----------------GYGLSETSPVLC-SNTVTEEGNRVGTIGIPWP 394
Cdd:PRK08315 314 LSSLR---TGIMAGSPC------------PIEvmkrvidkmhmsevtiAYGMTETSPVSTqTRTDDPLEKRVTTVGRALP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 395 STYMKCV-TEDGTEAALGEPGEIWAKGPQVFGGYYNRPDESAKVL-EDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGF 472
Cdd:PRK08315 379 HLEVKIVdPETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGE 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 473 NVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVV-KKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVG 551
Cdd:PRK08315 459 NIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIIlRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTG 538
|
570
....*....|....*..
gi 518832993 552 KILRRPLREEELAKLKK 568
Cdd:PRK08315 539 KIQKFKMREMMIEELGL 555
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
26-496 |
8.57e-83 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 270.05 E-value: 8.57e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 26 PDSYTSLAALIEEGVKRFSSAPAYACMG----KQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGA 101
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLL-ALGVKPGDRVAILSDNRPEWVIADLAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 102 LRAGLTVVntnPLY---TPREMQHQFNDSGAKAIvilanFAGN---LEKILSQ----TAIEHVIVTQIGDLLGFPKKLIV 171
Cdd:COG1022 86 LAAGAVTV---PIYptsSAEEVAYILNDSGAKVL-----FVEDqeqLDKLLEVrdelPSLRHIVVLDPRGLRDDPRLLSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 172 NAVVKyvkkmvpayhlpgaisFGDALSRGSRQPLKPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMKP 251
Cdd:COG1022 158 DELLA----------------LGREVADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 252 agvpDGQGIIVAALPLYHVYALTTnALASLKSGSMnllITNPRDLNAFIDDLKKYKITAFTG----LNTLYNGLLNhpRI 327
Cdd:COG1022 222 ----GPGDRTLSFLPLAHVFERTV-SYYALAAGAT---VAFAESPDTLAEDLREVKPTFMLAvprvWEKVYAGIQA--KA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 328 NE----------------VDFSELRITS---AGGMALQTSVADR-----WQKLTGNK-----------PA---------- 362
Cdd:COG1022 292 EEagglkrklfrwalavgRRYARARLAGkspSLLLRLKHALADKlvfskLREALGGRlrfavsggaalGPelarffralg 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 363 ----EGYGLSETSPVLCSNTvtEEGNRVGTIGIPWPstymkcvtedGTEAALGEPGEIWAKGPQVFGGYYNRPDESAKVL 438
Cdd:COG1022 372 ipvlEGYGLTETSPVITVNR--PGDNRIGTVGPPLP----------GVEVKIAEDGEILVRGPNVMKGYYKNPEATAEAF 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 439 -EDGWFKTGDIGVMTADGYFKIVDRKKDMI-LVSGFNVYPNEIEEVVSQCPGVLEVACVG 496
Cdd:COG1022 440 dADGWLHTGDIGELDEDGFLRITGRKKDLIvTSGGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
30-561 |
2.03e-82 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 266.85 E-value: 2.03e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 30 TSLAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVV 109
Cdd:PRK06188 12 ATYGHLLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFE-ALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 110 NTNPLYTPREMQHQFNDSGAKAIVILAN-FAGNLEKILSQ-TAIEHVIvtQIGDLlgfpkklivnavvkyvkkmvpayhl 187
Cdd:PRK06188 91 ALHPLGSLDDHAYVLEDAGISTLIVDPApFVERALALLARvPSLKHVL--TLGPV------------------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 188 PGAISFGDALSRGSRQPLKPVAIKnTDLAFVQYTGGTTGVSKGAALTHRNIIS-NVICQDEWMKPAGVPdgqgiIVAALP 266
Cdd:PRK06188 144 PDGVDLLAAAAKFGPAPLVAAALP-PDIAGLAYTGGTTGKPKGVMGTHRSIATmAQIQLAEWEWPADPR-----FLMCTP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 267 LYHVYALTTnALASLKSGSMNLLitNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQ 346
Cdd:PRK06188 218 LSHAGGAFF-LPTLLRGGTVIVL--AKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMS 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 347 tsvADRWQ---KLTGNKPAEGYGLSEtspvlCSNTVT---------EEGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPG 414
Cdd:PRK06188 295 ---PVRLAeaiERFGPIFAQYYGQTE-----APMVITylrkrdhdpDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 415 EIWAKGPQVFGGYYNRPDESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVAC 494
Cdd:PRK06188 367 EICVRGPLVMDGYWNRPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAV 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518832993 495 VGVPNEKSGETVKIFVV-KKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREE 561
Cdd:PRK06188 447 IGVPDEKWGEAVTAVVVlRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRAR 514
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
54-560 |
8.44e-82 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 264.41 E-value: 8.44e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 54 KQITFSELDTLSQQFASFLQNDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIV 133
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 134 ILANFAGNLEKILSQTAIEHVIvtQIGDLLGFPKKLIVNAVVKyvkkmvpayhlpgaisfgdalsrGSRQPLkpvaiknt 213
Cdd:PRK06839 106 VEKTFQNMALSMQKVSYVQRVI--SITSLKEIEDRKIDNFVEK-----------------------NESASF-------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 214 dlaFVQYTGGTTGVSKGAALTHRNI----ISNVICQDEWMkpagvpDGQGIIVaaLPLYHVYALTTNALASLKSGSMnLL 289
Cdd:PRK06839 153 ---IICYTSGTTGKPKGAVLTQENMfwnaLNNTFAIDLTM------HDRSIVL--LPLFHIGGIGLFAFPTLFAGGV-II 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 290 ITNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGG----MALQTSVADRwqkltGNKPAEGY 365
Cdd:PRK06839 221 VPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGapcpEELMREFIDR-----GFLFGQGF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 366 GLSETSPVLCSNTVTEEGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRPDESAKVLEDGWFKT 445
Cdd:PRK06839 296 GMTETSPTVFMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWLCT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 446 GDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKDEA-LTEDSITR 524
Cdd:PRK06839 376 GDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSvLIEKDVIE 455
|
490 500 510
....*....|....*....|....*....|....*.
gi 518832993 525 YCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLRE 560
Cdd:PRK06839 456 HCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVN 491
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
53-561 |
5.65e-80 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 259.81 E-value: 5.65e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 53 GKQITFSELDTLSQQFASFLQNdLKLQKGDRIAIQM----PNLLQYpiamFGALRAGLTVVNTNPLYTPREMQHQFNDSG 128
Cdd:PRK07514 26 GLRYTYGDLDAASARLANLLVA-LGVKPGDRVAVQVekspEALALY----LATLRAGAVFLPLNTAYTLAELDYFIGDAE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 129 AKAIVIL-ANFAGnLEKILSQTAIEHVIVTqigdllgfpkklivnavvkyvkkmvpayhlpGAISFGDALSRGSRQP--L 205
Cdd:PRK07514 101 PALVVCDpANFAW-LSKIAAAAGAPHVETL-------------------------------DADGTGSLLEAAAAAPddF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 206 KPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNIISN-VICQDEW-MKPAGVpdgqgiIVAALPLYHVYAL--TTN-ALAS 280
Cdd:PRK07514 149 ETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNaLTLVDYWrFTPDDV------LIHALPIFHTHGLfvATNvALLA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 281 lkSGSMNLLitnPR-DLNAFIDDLKKykITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSVADRWQKLTGN 359
Cdd:PRK07514 223 --GASMIFL---PKfDPDAVLALMPR--ATVMMGVPTFYTRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGH 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 360 KPAEGYGLSETSpVLCSNTVteEGNRV-GTIGIPWPSTYMKCV-TEDGTEAALGEPGEIWAKGPQVFGGYYNRPDESAKV 437
Cdd:PRK07514 296 AILERYGMTETN-MNTSNPY--DGERRaGTVGFPLPGVSLRVTdPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 438 L-EDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVV-KKDE 515
Cdd:PRK07514 373 FrADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVpKPGA 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 518832993 516 ALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREE 561
Cdd:PRK07514 453 ALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
53-559 |
2.85e-78 |
|
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: 252.98 E-value: 2.85e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 53 GKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAI 132
Cdd:cd05934 1 GRRWTYAELLRESARIAAALA-ALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 133 Vilanfagnlekilsqtaiehvivtqigdllgfpkklivnavvkyvkkmvpayhlpgaisfgdalsrgsrqplkpvaikn 212
Cdd:cd05934 80 V------------------------------------------------------------------------------- 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 213 TDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMkpaGVPDGQgIIVAALPLYHVYALTTNALASLKSGSMNLLItn 292
Cdd:cd05934 81 VDPASILYTSGTTGPPKGVVITHANLTFAGYYSARRF---GLGEDD-VYLTVLPLFHINAQAVSVLAALSVGATLVLL-- 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 293 PR-DLNAFIDDLKKYKITAFTGLNTLYNGLLNHP-RINEVDfSELRITSAGGMALQTSvaDRWQKLTGNKPAEGYGLSET 370
Cdd:cd05934 155 PRfSASRFWSDVRRYGATVTNYLGAMLSYLLAQPpSPDDRA-HRLRAAYGAPNPPELH--EEFEERFGVRLLEGYGMTET 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 371 S-PVLCSNtvtEEGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAK---GPQVFGGYYNRPDESAKVLEDGWFKTG 446
Cdd:cd05934 232 IvGVIGPR---DEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAMRNGWFHTG 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 447 DIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVV-KKDEALTEDSITRY 525
Cdd:cd05934 309 DLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVlRPGETLDPEELFAF 388
|
490 500 510
....*....|....*....|....*....|....
gi 518832993 526 CRENLTAYKVPKHIEFRTELPKSNVGKILRRPLR 559
Cdd:cd05934 389 CEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
32-565 |
1.16e-76 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 251.88 E-value: 1.16e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 32 LAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNT 111
Cdd:PRK07470 9 LAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALA-ARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 112 NPLYTPREMQHQFNDSGAKAIVILANFAGNLEKILSQT-AIEHVIVtqIGDLlgfpkklivnavvkyvkkmvpayhlPGA 190
Cdd:PRK07470 88 NFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASpDLTHVVA--IGGA-------------------------RAG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 191 ISFGDALSRGSRQPLKPVAIKNTDLAFVQYTGGTTGVSKGAALTHRN---IISNVICQdewMKPAGVPDGQGIIVAalPL 267
Cdd:PRK07470 141 LDYEALVARHLGARVANAAVDHDDPCWFFFTSGTTGRPKAAVLTHGQmafVITNHLAD---LMPGTTEQDASLVVA--PL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 268 YHvyALTTNALASLKSGSMNLLITNPR-DLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELR-ITSAGGmal 345
Cdd:PRK07470 216 SH--GAGIHQLCQVARGAATVLLPSERfDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRyVIYAGA--- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 346 QTSVADRWQKLT--GNKPAEGYGLSETS---PVLCSNTVTEE---GNRVGTIGIPwpSTYMKCVTED--GTEAALGEPGE 415
Cdd:PRK07470 291 PMYRADQKRALAklGKVLVQYFGLGEVTgniTVLPPALHDAEdgpDARIGTCGFE--RTGMEVQIQDdeGRELPPGETGE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 416 IWAKGPQVFGGYYNRPDESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACV 495
Cdd:PRK07470 369 ICVIGPAVFAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVL 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518832993 496 GVPNEKSGET-VKIFVVKKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREEELAK 565
Cdd:PRK07470 449 GVPDPVWGEVgVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREELEER 519
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
218-559 |
7.97e-76 |
|
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: 244.11 E-value: 7.97e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 218 VQYTGGTTGVSKGAALTHRNIISNVICQDEWMKPAGvpdgQGIIVAALPLYHVYALTTNALASLKSGSMNLLITNPRDLN 297
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTE----QDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSPSFDPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 298 AFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSVADRWQKLTGNKPAE-GYGLSETSPVlCS 376
Cdd:cd05917 83 AVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTiAYGMTETSPV-ST 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 377 NTVTEEG--NRVGTIGIPWPSTYMKCV-TEDGTEAALGEPGEIWAKGPQVFGGYYNRPDESAKVL-EDGWFKTGDIGVMT 452
Cdd:cd05917 162 QTRTDDSieKRVNTVGRIMPHTEAKIVdPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIdGDGWLHTGDLAVMD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 453 ADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKDEA-LTEDSITRYCRENLT 531
Cdd:cd05917 242 EDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAeLTEEDIKAYCKGKIA 321
|
330 340
....*....|....*....|....*...
gi 518832993 532 AYKVPKHIEFRTELPKSNVGKILRRPLR 559
Cdd:cd05917 322 HYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
32-561 |
1.61e-74 |
|
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: 246.60 E-value: 1.61e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 32 LAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNT 111
Cdd:COG1021 27 LGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLL-ALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVFA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 112 NPLYTPREMQHQFNDSGAKAIVILANFAGN-----LEKILSQT-AIEHVIVtqIGDLLGFpkklivnavvkyvkkmvpay 185
Cdd:COG1021 106 LPAHRRAEISHFAEQSEAVAYIIPDRHRGFdyralARELQAEVpSLRHVLV--VGDAGEF-------------------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 186 hlpgaISFgDALSRGSRQPLKPvAIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNV-----ICqdewmkpaGVpDGQGI 260
Cdd:COG1021 164 -----TSL-DALLAAPADLSEP-RPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVrasaeIC--------GL-DADTV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 261 IVAALPLYHVYALTTN-ALASLKSGSMNLLITNPRDLNAF--IDdlkKYKITaFTGL-NTLYNGLLNHPRINEVDFSELR 336
Cdd:COG1021 228 YLAALPAAHNFPLSSPgVLGVLYAGGTVVLAPDPSPDTAFplIE---RERVT-VTALvPPLALLWLDAAERSRYDLSSLR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 337 ITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETspvLCSNT---VTEEgNRVGTIGIPwpstyM------KCVTEDGTE 407
Cdd:COG1021 304 VLQVGGAKLSPELARRVRPALGCTLQQVFGMAEG---LVNYTrldDPEE-VILTTQGRP-----IspddevRIVDEDGNP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 408 AALGEPGEIWAKGPQVFGGYYNRPDESAKVL-EDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQC 486
Cdd:COG1021 375 VPPGEVGELLTRGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAH 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518832993 487 PGVLEVACVGVPNEKSGETVKIFVVKKDEALTEDSITRYCRE-NLTAYKVPKHIEFRTELPKSNVGKILRRPLREE 561
Cdd:COG1021 455 PAVHDAAVVAMPDEYLGERSCAFVVPRGEPLTLAELRRFLRErGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAA 530
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
57-560 |
1.44e-71 |
|
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: 238.30 E-value: 1.44e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 57 TFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGlTVVNT-NPLYTPREMQHQFNDSGAKAIVIL 135
Cdd:cd12119 27 TYAEVAERARRLANALR-RLGVKPGDRVATLAWNTHRHLELYYAVPGMG-AVLHTiNPRLFPEQIAYIINHAEDRVVFVD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 136 ANFAGNLEKILSQ-TAIEHVIVTQIGDLLGFPkklivnavvkyvkkmvpayHLPGAISFGDALSRGSrqplkPVA----I 210
Cdd:cd12119 105 RDFLPLLEAIAPRlPTVEHVVVMTDDAAMPEP-------------------AGVGVLAYEELLAAES-----PEYdwpdF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 211 KNTDLAFVQYTGGTTGVSKGAALTHRNII--SNVICQdewmkpagvPDGQGI-----IVAALPLYHVYALTTnALASLKS 283
Cdd:cd12119 161 DENTAAAICYTSGTTGNPKGVVYSHRSLVlhAMAALL---------TDGLGLsesdvVLPVVPMFHVNAWGL-PYAAAMV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 284 GSmNLLITNPRDLNAFIDDL-KKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSVADRWQKLtGNKPA 362
Cdd:cd12119 231 GA-KLVLPGPYLDPASLAELiEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 363 EGYGLSETSPVLCSNTVT---------EEGNRVGTIGIPWPSTYMKCVTEDGTEAAL--GEPGEIWAKGPQVFGGYYNRP 431
Cdd:cd12119 309 HAWGMTETSPLGTVARPPsehsnlsedEQLALRAKQGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKND 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 432 DESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVV 511
Cdd:cd12119 389 EESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVV 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 518832993 512 KKDEA-LTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLRE 560
Cdd:cd12119 469 LKEGAtVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
57-560 |
1.23e-70 |
|
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: 233.43 E-value: 1.23e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 57 TFSELDTLSQQFASFLqNDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIVILA 136
Cdd:cd05903 3 TYSELDTRADRLAAGL-AALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 137 NFagnlekilsqtaiehvivtqigdllgfpkklivnavvkyvKKMVPAyHLPGAIsfgdalsrgsrqplkpvaikntdlA 216
Cdd:cd05903 82 RF----------------------------------------RQFDPA-AMPDAV------------------------A 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 217 FVQYTGGTTGVSKGAALTHRNIISNVICQDE-WMKPagvpdGQGIIVAALPLYH----VYALTTNALasLKSGSMNLLIT 291
Cdd:cd05903 97 LLLFTSGTTGEPKGVMHSHNTLSASIRQYAErLGLG-----PGDVFLVASPMAHqtgfVYGFTLPLL--LGAPVVLQDIW 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 292 NPRDLNAFiddLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETS 371
Cdd:cd05903 170 DPDKALAL---MREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECP 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 372 PVLCSNTVTEEGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRPDESAKVLEDGWFKTGDIGVM 451
Cdd:cd05903 247 GAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARL 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 452 TADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKDEA-LTEDSITRYC-REN 529
Cdd:cd05903 327 DEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGAlLTFDELVAYLdRQG 406
|
490 500 510
....*....|....*....|....*....|.
gi 518832993 530 LTAYKVPKHIEFRTELPKSNVGKILRRPLRE 560
Cdd:cd05903 407 VAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
23-560 |
6.16e-70 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 234.49 E-value: 6.16e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 23 DINPDSYTSLAALIEEgvkRFSSAPAYACM-----GKQITFSELDTLSQQFASFLqNDLKLQKGDRIAIQMPNLLQYPIA 97
Cdd:PLN02246 16 DIYIPNHLPLHDYCFE---RLSEFSDRPCLidgatGRVYTYADVELLSRRVAAGL-HKLGIRQGDVVMLLLPNCPEFVLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 98 MFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIVILANFAgnlEKILSQTAIEHVIVTQIGDllgfpkklivnavvky 177
Cdd:PLN02246 92 FLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYV---DKLKGLAEDDGVTVVTIDD---------------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 178 vkkmvpayHLPGAISFGDaLSRGSRQPLKPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMKPAGVPDG 257
Cdd:PLN02246 153 --------PPEGCLHFSE-LTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFHS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 258 QGIIVAALPLYHVYALTTNALASLKSGSMnLLITNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRI 337
Cdd:PLN02246 224 DDVILCVLPMFHIYSLNSVLLCGLRVGAA-ILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRM 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 338 TSAG----GMALQTSVADrwqKLTGNKPAEGYGLSETSPVL--C---SNTVTEEgnRVGTIGIPWPSTYMKCV-TEDGTE 407
Cdd:PLN02246 303 VLSGaaplGKELEDAFRA---KLPNAVLGQGYGMTEAGPVLamClafAKEPFPV--KSGSCGTVVRNAELKIVdPETGAS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 408 AALGEPGEIWAKGPQVFGGYYNRPDESAKVL-EDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQC 486
Cdd:PLN02246 378 LPRNQPGEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISH 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518832993 487 PGVLEVACVGVPNEKSGETVKIFVVK-KDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLRE 560
Cdd:PLN02246 458 PSIADAAVVPMKDEVAGEVPVAFVVRsNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRA 532
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
47-559 |
1.43e-69 |
|
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: 230.81 E-value: 1.43e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 47 PAYACMGKQITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFND 126
Cdd:cd05919 2 TAFYAADRSVTYGQLHDGANRLGSALRN-LGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 127 SGAKAIVILANfagnlekilsqtaiehvivtqigdllgfpkklivnavvkyvkkmvpayhlpgaisfgdalsrgsrqplk 206
Cdd:cd05919 81 CEARLVVTSAD--------------------------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 207 pvaikntDLAFVQYTGGTTGVSKGAALTHRNIISNVicqDEWMKPA-GVPDGQGIIVAAlPLYHVYALTTNALASLKSGS 285
Cdd:cd05919 92 -------DIAYLLYSSGTTGPPKGVMHAHRDPLLFA---DAMAREAlGLTPGDRVFSSA-KMFFGYGLGNSLWFPLAVGA 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 286 MNLLITNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSVADRWQKLTGNKPAEGY 365
Cdd:cd05919 161 SAVLNPGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGI 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 366 GLSETSPVLCSNTVTEEgnRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRPDESAKVLEDGWFKT 445
Cdd:cd05919 241 GATEVGHIFLSNRPGAW--RLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGGWYRT 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 446 GDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKK-----DEALTED 520
Cdd:cd05919 319 GDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKspaapQESLARD 398
|
490 500 510
....*....|....*....|....*....|....*....
gi 518832993 521 sITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLR 559
Cdd:cd05919 399 -IHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
57-559 |
1.01e-68 |
|
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: 227.99 E-value: 1.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 57 TFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIVILA 136
Cdd:cd05972 2 SFRELKRESAKAANVLA-KLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 137 NfagnlekilsqtaiehvivtqigdllgfpkklivnavvkyvkkmvpayhlpgaisfgdalsrgsrqplkpvaikntDLA 216
Cdd:cd05972 81 E----------------------------------------------------------------------------DPA 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 217 FVQYTGGTTGVSKGAALTHRNIISNVICQDEWMkpaGVPDGQGIIVAALPLYhVYALTTNALASLKSGSMNLLITNPR-D 295
Cdd:cd05972 85 LIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWL---GLRPDDIHWNIADPGW-AKGAWSSFFGPWLLGATVFVYEGPRfD 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 296 LNAFIDDLKKYKITAFTGLNTLYNgLLNHPRINEVDFSELRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETSpVLC 375
Cdd:cd05972 161 AERILELLERYGVTSFCGPPTAYR-MLIKQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETG-LTV 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 376 SNTVTEEgNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAK--GPQVFGGYYNRPDESAKVLEDGWFKTGDIGVMTA 453
Cdd:cd05972 239 GNFPDMP-VKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKlpPPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 454 DGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKD-----EALTEDsITRYCRE 528
Cdd:cd05972 318 DGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSgyepsEELAEE-LQGHVKK 396
|
490 500 510
....*....|....*....|....*....|.
gi 518832993 529 NLTAYKVPKHIEFRTELPKSNVGKILRRPLR 559
Cdd:cd05972 397 VLAPYKYPREIEFVEELPKTISGKIRRVELR 427
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
53-562 |
2.93e-68 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 228.69 E-value: 2.93e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 53 GKQITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNllqyPIAMFGALRA----GLTVVNTNPLYTPREMQHQFNDSG 128
Cdd:PRK03640 25 EKKVTFMELHEAVVSVAGKLAA-LGVKKGDRVALLMKN----GMEMILVIHAlqqlGAVAVLLNTRLSREELLWQLDDAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 129 AKaivilanfagnlekilsqtaieHVIVTQIgdllgFPKKLIVNAVVKYvkkmvpayhlpgaisfgDALSRGsrqPLKPV 208
Cdd:PRK03640 100 VK----------------------CLITDDD-----FEAKLIPGISVKF-----------------AELMNG---PKEEA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 209 AIKNT-DLAFV---QYTGGTTGVSKGAALTHRN----IISNVI-----CQDEWMkpagvpdgqgiivAALPLYHVYALTT 275
Cdd:PRK03640 133 EIQEEfDLDEVatiMYTSGTTGKPKGVIQTYGNhwwsAVGSALnlgltEDDCWL-------------AAVPIFHISGLSI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 276 nALASLKSGsMNLLITNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNhpRINEVDFSE-LR-ITSAGGMALQTSVADRW 353
Cdd:PRK03640 200 -LMRSVIYG-MRVVLVEKFDAEKINKLLQTGGVTIISVVSTMLQRLLE--RLGEGTYPSsFRcMLLGGGPAPKPLLEQCK 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 354 QKltgNKPA-EGYGLSETspvlCSNTVT----EEGNRVGTIGIPWPSTYMKcVTEDGTEAALGEPGEIWAKGPQVFGGYY 428
Cdd:PRK03640 276 EK---GIPVyQSYGMTET----ASQIVTlspeDALTKLGSAGKPLFPCELK-IEKDGVVVPPFEEGEIVVKGPNVTKGYL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 429 NRPDESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKI 508
Cdd:PRK03640 348 NREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVA 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 518832993 509 FVVkKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREEE 562
Cdd:PRK03640 428 FVV-KSGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLV 480
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
56-560 |
5.27e-68 |
|
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: 225.69 E-value: 5.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 56 ITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKaivil 135
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAA-LGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVK----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 136 anfagnLEKILSqtaiehvivtqigdllgfpkklivnavvkyvkkmvpayhlpgaisfgdalsrgsrqplkpvaikntdl 215
Cdd:cd05912 76 ------LDDIAT-------------------------------------------------------------------- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 216 afVQYTGGTTGVSKGAALTHRNIISNVIC---------QDEWMkpagvpdgqgiivAALPLYHVYALTTnALASLKSGsM 286
Cdd:cd05912 82 --IMYTSGTTGKPKGVQQTFGNHWWSAIGsalnlglteDDNWL-------------CALPLFHISGLSI-LMRSVIYG-M 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 287 NLLITNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNhpRINEVDFSELR-ITSAGGMALQTSVADRWQKltgNKPA-EG 364
Cdd:cd05912 145 TVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRLLE--ILGEGYPNNLRcILLGGGPAPKPLLEQCKEK---GIPVyQS 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 365 YGLSETSPVLCSNTVTEEGNRVGTIGIPWPSTYMKCVTEDGteaALGEPGEIWAKGPQVFGGYYNRPDESAKVLEDGWFK 444
Cdd:cd05912 220 YGMTETCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQ---PPYEVGEILLKGPNVTKGYLNRPDATEESFENGWFK 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 445 TGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKDEaLTEDSITR 524
Cdd:cd05912 297 TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERP-ISEEELIA 375
|
490 500 510
....*....|....*....|....*....|....*.
gi 518832993 525 YCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLRE 560
Cdd:cd05912 376 YCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
18-568 |
6.37e-67 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 226.78 E-value: 6.37e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 18 PGVPhdiNPDSYTsLAALIEEGVKRFSSAPAY--ACMGKQITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYP 95
Cdd:PLN02330 20 PSVP---VPDKLT-LPDFVLQDAELYADKVAFveAVTGKAVTYGEVVRDTRRFAKALRS-LGLRKGQVVVVVLPNVAEYG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 96 IAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIVilaNFAGNLEKILSqtaiehvivtqigdlLGFPkkLIVNAVV 175
Cdd:PLN02330 95 IVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIV---TNDTNYGKVKG---------------LGLP--VIVLGEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 176 KyvkkmvpayhLPGAISFGDALSRGSRQPLKPV--AIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMKPAG 253
Cdd:PLN02330 155 K----------IEGAVNWKELLEAADRAGDTSDneEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEM 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 254 VpdGQGIIVAALPLYHVYALTTNALASLKSGSmNLLITNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFS 333
Cdd:PLN02330 225 I--GQVVTLGLIPFFHIYGITGICCATLRNKG-KVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 334 ELRI----TSAGGMALQTSVADRwQKLTGNKPAEGYGLSETSPVLCSNTVTEEGNRVG---TIGIPWPSTYMKCVTED-G 405
Cdd:PLN02330 302 KLKLqaimTAAAPLAPELLTAFE-AKFPGVQVQEAYGLTEHSCITLTHGDPEKGHGIAkknSVGFILPNLEVKFIDPDtG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 406 TEAALGEPGEIWAKGPQVFGGYYNRPDESAKVL-EDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVS 484
Cdd:PLN02330 381 RSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIdEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 485 QCPGVLEVACVGVPNEKSGETVKIFVVKKDEAL-TEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREEEL 563
Cdd:PLN02330 461 THPSVEDAAVVPLPDEEAGEIPAACVVINPKAKeSEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKML 540
|
....*
gi 518832993 564 AKLKK 568
Cdd:PLN02330 541 SINKA 545
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
53-568 |
1.50e-66 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 225.78 E-value: 1.50e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 53 GKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAI 132
Cdd:PRK06087 47 GASYTYSALDHAASRLANWLL-AKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 133 vilanFAGNLEKILSQTAIEHVIVTQIGDLLGfpkklivnavVKYVKKMVPAYhlpGAISFGDALSRGsrQPLK-PVAIK 211
Cdd:PRK06087 126 -----FAPTLFKQTRPVDLILPLQNQLPQLQQ----------IVGVDKLAPAT---SSLSLSQIIADY--EPLTtAITTH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 212 NTDLAFVQYTGGTTGVSKGAALTHRNIIS---------NVICQDEWMKPAgvpdgqgiivaalPLYHVYALTTNALASLK 282
Cdd:PRK06087 186 GDELAAVLFTSGTEGLPKGVMLTHNNILAseraycarlNLTWQDVFMMPA-------------PLGHATGFLHGVTAPFL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 283 SGSMNLL--ITNPrdlNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSVADRWQKlTGNK 360
Cdd:PRK06087 253 IGARSVLldIFTP---DACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVARECQQ-RGIK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 361 PAEGYGLSETSPVLCSNTVTEEGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRPDESAKVL-E 439
Cdd:PRK06087 329 LLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALdE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 440 DGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKDEALT- 518
Cdd:PRK06087 409 EGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSl 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 518832993 519 --EDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREEELAKLKK 568
Cdd:PRK06087 489 tlEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDIMRRLTQ 540
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
214-555 |
5.11e-66 |
|
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: 218.14 E-value: 5.11e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 214 DLAFVQYTGGTTGVSKGAALTHRNIISnviCQDEWMKPAGVPDGQGIIVAAlPLYHVYALTTNALASLKSGSmNLLITNP 293
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLR---AAAAWADCADLTEDDRYLIIN-PFFHTFGYKAGIVACLLTGA-TVVPVAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 294 RDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSVADRWQ-KLTGNKPAEGYGLSETSP 372
Cdd:cd17638 76 FDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRsELGFETVLTAYGLTEAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 373 VlcsnTVTEEGNRVGTIGipwpSTYMKCVteDGTEAALGEPGEIWAKGPQVFGGYYNRPDESAKVL-EDGWFKTGDIGVM 451
Cdd:cd17638 156 A----TMCRPGDDAETVA----TTCGRAC--PGFEVRIADDGEVLVRGYNVMQGYLDDPEATAEAIdADGWLHTGDVGEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 452 TADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKD-EALTEDSITRYCRENL 530
Cdd:cd17638 226 DERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPgVTLTEEDVIAWCRERL 305
|
330 340
....*....|....*....|....*
gi 518832993 531 TAYKVPKHIEFRTELPKSNVGKILR 555
Cdd:cd17638 306 ANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
75-559 |
2.31e-64 |
|
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: 217.69 E-value: 2.31e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 75 DLKLQKGDRIAIQMPNLLQYPIAMFGALRAG----LTVVNTNPLYTPREMQHQFNDSGAKaIVILANFAGNLekilsqta 150
Cdd:cd05922 12 EAGGVRGERVVLILPNRFTYIELSFAVAYAGgrlgLVFVPLNPTLKESVLRYLVADAGGR-IVLADAGAADR-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 151 iehvivtqigdllgfpkklivnavvkyVKKMVPAYHLPGAISFGDALsRGSRQPLKPVAIKNTDLAFVQYTGGTTGVSKG 230
Cdd:cd05922 83 ---------------------------LRDALPASPDPGTVLDADGI-RAARASAPAHEVSHEDLALLLYTSGSTGSPKL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 231 AALTHRNIISNVICQDEWMKPagvpDGQGIIVAALPLYHVYALTTNALASLKSGSmnlLITNPRDL--NAFIDDLKKYKI 308
Cdd:cd05922 135 VRLSHQNLLANARSIAEYLGI----TADDRALTVLPLSYDYGLSVLNTHLLRGAT---LVLTNDGVldDAFWEDLREHGA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 309 TAFTGLNTLYnGLLNHPRINEVDFSELR-ITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETSPVLCSNTVTEEGNRVG 387
Cdd:cd05922 208 TGLAGVPSTY-AMLTRLGFDPAKLPSLRyLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPERILEKPG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 388 TIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRP-DESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDM 466
Cdd:cd05922 287 SIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPpYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRM 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 467 ILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEkSGETVKIFVVKKDEaLTEDSITRYCRENLTAYKVPKHIEFRTELP 546
Cdd:cd05922 367 IKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDP-LGEKLALFVTAPDK-IDPKDVLRSLAERLPPYKVPATVRVVDELP 444
|
490
....*....|...
gi 518832993 547 KSNVGKILRRPLR 559
Cdd:cd05922 445 LTASGKVDYAALR 457
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
53-567 |
3.36e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 215.44 E-value: 3.36e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 53 GKQITFSELDTLSQQFASFLQNDlKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAI 132
Cdd:PRK09088 20 GRRWTYAELDALVGRLAAVLRRR-GCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 133 VILANFAGNlekilsqtaiehviVTQIGDLLGFpkklivnavvkyvkkmvpayhlpgaISFGDALSRGSRQPLKPVAIkn 212
Cdd:PRK09088 99 LGDDAVAAG--------------RTDVEDLAAF-------------------------IASADALEPADTPSIPPERV-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 213 tdlAFVQYTGGTTGVSKGAALTHRNIISNVICqdewMKPAGVPDGQGIIVAALPLYHVYALTTNALASLKSGSmNLLITN 292
Cdd:PRK09088 138 ---SLILFTSGTSGQPKGVMLSERNLQQTAHN----FGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGG-SILVSN 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 293 ---PRDLNAFIDDLKkYKITAFTGLNTLYNGLLNHPrinEVDFSELRITSA--GGMALQTSVADRWQKLTGNKPAEGYGL 367
Cdd:PRK09088 210 gfePKRTLGRLGDPA-LGITHYFCVPQMAQAFRAQP---GFDAAALRHLTAlfTGGAPHAAEDILGWLDDGIPMVDGFGM 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 368 SETSPVL-CSNTVTEEGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRPDESAKVL-EDGWFKT 445
Cdd:PRK09088 286 SEAGTVFgMSVDCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFtGDGWFRT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 446 GDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKDEALTE-DSITR 524
Cdd:PRK09088 366 GDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDlERIRS 445
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 518832993 525 YCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREEELAKLK 567
Cdd:PRK09088 446 HLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDALAAGRK 488
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
50-560 |
6.27e-63 |
|
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: 215.85 E-value: 6.27e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 50 ACMGKQITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNdsga 129
Cdd:cd17642 39 AHTGVNYSYAEYLEMSVRLAEALKK-YGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLN---- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 130 kaivilanfagnlekiLSQTAIehVIVTQIGdllgFPKKLIVNAVVKYVKKMV---PAYHLPGAISFGDALSRGSRQPL- 205
Cdd:cd17642 114 ----------------ISKPTI--VFCSKKG----LQKVLNVQKKLKIIKTIIildSKEDYKGYQCLYTFITQNLPPGFn 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 206 ----KPVAI-KNTDLAFVQYTGGTTGVSKGAALTHRNIISNVI-CQDEWMKPAGVPDGQgiIVAALPLYHVYALTTnALA 279
Cdd:cd17642 172 eydfKPPSFdRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFShARDPIFGNQIIPDTA--ILTVIPFHHGFGMFT-TLG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 280 SLKSGSMNLLITNpRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSVADRWQKLTG- 358
Cdd:cd17642 249 YLICGFRVVLMYK-FEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKl 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 359 NKPAEGYGLSE-TSPVLCSNtvtEEGNRVGTIGIPWPSTYMKCVTEDgTEAALG--EPGEIWAKGPQVFGGYYNRPDE-S 434
Cdd:cd17642 328 PGIRQGYGLTEtTSAILITP---EGDDKPGAVGKVVPFFYAKVVDLD-TGKTLGpnERGELCVKGPMIMKGYVNNPEAtK 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 435 AKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKK- 513
Cdd:cd17642 404 ALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEa 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 518832993 514 DEALTEDSITRYCRENLT-AYKVPKHIEFRTELPKSNVGKILRRPLRE 560
Cdd:cd17642 484 GKTMTEKEVMDYVASQVStAKRLRGGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
46-559 |
1.53e-62 |
|
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: 212.34 E-value: 1.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 46 APAYACMGKQITFSELDTLSQQFASFLQNDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREmqhqfn 125
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKE------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 126 dsgakaivilanfagnLEKILSQTAIEHVIvtqigdllgfpkklivnavvkyvkkmvpayhLPGAISFGDalsrgsrqpl 205
Cdd:cd05958 75 ----------------LAYILDKARITVAL-------------------------------CAHALTASD---------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 206 kpvaikntDLAFVQYTGGTTGVSKGAALTHRNIISnvICqDEWMKPAGVPDGQGIIVAALPLYHVYALTTNALASLKSGS 285
Cdd:cd05958 98 --------DICILAFTSGTTGAPKATMHFHRDPLA--SA-DRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGA 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 286 MNLLI--TNPRDLnafIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSVADRWQKLTGNKPAE 363
Cdd:cd05958 167 SGVLLeeATPDLL---LSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIID 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 364 GYGLSETSPVLCSNTvtEEGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQvfgGYYNRPDESA-KVLEDGW 442
Cdd:cd05958 244 GIGSTEMFHIFISAR--PGDARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGPT---GCRYLADKRQrTYVQGGW 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 443 FKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKK-----DEAL 517
Cdd:cd05958 319 NITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRpgvipGPVL 398
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 518832993 518 TEDsITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLR 559
Cdd:cd05958 399 ARE-LQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
54-496 |
5.42e-61 |
|
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: 208.22 E-value: 5.42e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 54 KQITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVntnPLY---TPREMQHQFNDSGAK 130
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIA-LGVEPGDRVAILSRNRPEWTIADLAILAIGAVPV---PIYptsSAEQIAYILNDSEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 131 AIvilanFAGNLEkilsqtaiehvivtqigdllgfpkklivnavvkyvkkmvpayhlpgaisfgdalsrgsrqplkpvai 210
Cdd:cd05907 80 AL-----FVEDPD------------------------------------------------------------------- 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 211 kntDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMKPagvpDGQGIIVAALPLYHVYALTTNALASLKSGSMNLLI 290
Cdd:cd05907 88 ---DLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPA----TEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFA 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 291 TNPRDLnafIDDLKKYKITAFTG----LNTLYNGLLNH--PRINEVDF-----SELRITSAGGMALQTSVADRWQKLtgN 359
Cdd:cd05907 161 SSAETL---LDDLSEVRPTVFLAvprvWEKVYAAIKVKavPGLKRKLFdlavgGRLRFAASGGAPLPAELLHFFRAL--G 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 360 KPA-EGYGLSETSPVLCSNTVteEGNRVGTIGIPWPstymkcvtedGTEAALGEPGEIWAKGPQVFGGYYNRPDESAKVL 438
Cdd:cd05907 236 IPVyEGYGLTETSAVVTLNPP--GDNRIGTVGKPLP----------GVEVRIADDGEILVRGPNVMLGYYKNPEATAEAL 303
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 439 -EDGWFKTGDIGVMTADGYFKIVDRKKDMILVS-GFNVYPNEIEEVVSQCPGVLEVACVG 496
Cdd:cd05907 304 dADGWLHTGDLGEIDEDGFLHITGRKKDLIITSgGKNISPEPIENALKASPLISQAVVIG 363
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
58-560 |
6.20e-61 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 209.94 E-value: 6.20e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 58 FSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIVILAN 137
Cdd:PRK12406 14 FDELAQRAARAAGGLAA-LGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 138 FAGNLEKILSQTAIEHVIVTqigdllgfPKKLIVNAVVKYVKKMVPayhlPGAISFGDALSRGSRQPLKPVAIKNTDLaf 217
Cdd:PRK12406 93 LLHGLASALPAGVTVLSVPT--------PPEIAAAYRISPALLTPP----AGAIDWEGWLAQQEPYDGPPVPQPQSMI-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 218 vqYTGGTTGVSKG----------AALTHRNIISNVicqdewmkpaGVPDGqgiIVAAL--PLYHVyALTTNALASLKSGS 285
Cdd:PRK12406 159 --YTSGTTGHPKGvrraaptpeqAAAAEQMRALIY----------GLKPG---IRALLtgPLYHS-APNAYGLRAGRLGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 286 mnLLITNPR-DLNAFIDDLKKYKITAFTGLNTLYNGLLNHPriNEV----DFSELR-ITSAGGMA---LQTSVADRWqkl 356
Cdd:PRK12406 223 --VLVLQPRfDPEELLQLIERHRITHMHMVPTMFIRLLKLP--EEVrakyDVSSLRhVIHAAAPCpadVKRAMIEWW--- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 357 tGNKPAEGYGLSETSPV-LCsnTVTEEGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQV--FGgYYNRPDE 433
Cdd:PRK12406 296 -GPVIYEYYGSTESGAVtFA--TSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNpdFT-YHNKPEK 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 434 SAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKK 513
Cdd:PRK12406 372 RAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQ 451
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 518832993 514 DEA-LTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLRE 560
Cdd:PRK12406 452 PGAtLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRD 499
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
53-559 |
1.30e-60 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 210.08 E-value: 1.30e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 53 GKQITFSELDTLSQQFASFLQNDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAkAI 132
Cdd:PLN02574 64 GFSISYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSV-GL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 133 VILAnfAGNLEKiLSQTAIEHVIVTQIGDllgFPKKLIVNAvvkyvkkmvpayhlpgaiSFGDALSRGSRQPLKPVaIKN 212
Cdd:PLN02574 143 AFTS--PENVEK-LSPLGVPVIGVPENYD---FDSKRIEFP------------------KFYELIKEDFDFVPKPV-IKQ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 213 TDLAFVQYTGGTTGVSKGAALTHRNIISNV-------ICQDEWmkpagvPDGQGIIVAALPLYHVYALTTNALASLKSGS 285
Cdd:PLN02574 198 DDVAAIMYSSGTTGASKGVVLTHRNLIAMVelfvrfeASQYEY------PGSDNVYLAALPMFHIYGLSLFVVGLLSLGS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 286 mNLLITNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPR-INEVDFSELRITSAGGMAL-QTSVADRWQKLTGNKPAE 363
Cdd:PLN02574 272 -TIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKgVCGEVLKSLKQVSCGAAPLsGKFIQDFVQTLPHVDFIQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 364 GYGLSETSPVLCSNTVTEEGNRVGTIGIPWPSTYMKCVT-EDGTEAALGEPGEIWAKGPQVFGGYYNRPDESA-KVLEDG 441
Cdd:PLN02574 351 GYGMTESTAVGTRGFNTEKLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQsTIDKDG 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 442 WFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKDE-ALTED 520
Cdd:PLN02574 431 WLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGsTLSQE 510
|
490 500 510
....*....|....*....|....*....|....*....
gi 518832993 521 SITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLR 559
Cdd:PLN02574 511 AVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
79-553 |
2.79e-60 |
|
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: 207.57 E-value: 2.79e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 79 QKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIvilanfagnlekILSQTAIEHVIVTQ 158
Cdd:cd05909 29 KEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTV------------LTSKQFIEKLKLHH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 159 IGDLLgFPKKLI----VNAVVKYVKKMVPAyhLPGAISFGDALSRGSRQPLKPvaiknTDLAFVQYTGGTTGVSKGAALT 234
Cdd:cd05909 97 LFDVE-YDARIVyledLRAKISKADKCKAF--LAGKFPPKWLLRIFGVAPVQP-----DDPAVILFTSGSEGLPKGVVLS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 235 HRNIISNVicqdEWMKPAGVPDGQGIIVAALPLYHVYALTTNALASLKSGSMNLLITNP---RDLNAFIDDlkkYKITAF 311
Cdd:cd05909 169 HKNLLANV----EQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNPldyKKIPELIYD---KKATIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 312 TGLNTLYNGLLNhpRINEVDFSELRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETSPVLCSNTVtEEGNRVGTIGI 391
Cdd:cd05909 242 LGTPTFLRGYAR--AAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTP-QSPNKEGTVGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 392 PWPSTYMKCVT-EDGTEAALGEPGEIWAKGPQVFGGYYNRPDESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVS 470
Cdd:cd05909 319 PLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 471 GFNVYPNEIEEVVSQ-CPGVLEVACVGVPNEKSGEtvKIFVVKKDEALTEDSITRYCRE----NLTaykVPKHIEFRTEL 545
Cdd:cd05909 399 GEMVSLEAIEDILSEiLPEDNEVAVVSVPDGRKGE--KIVLLTTTTDTDPSSLNDILKNagisNLA---KPSYIHQVEEI 473
|
....*...
gi 518832993 546 PKSNVGKI 553
Cdd:cd05909 474 PLLGTGKP 481
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
31-561 |
1.94e-59 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 205.50 E-value: 1.94e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 31 SLAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQNDlKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVN 110
Cdd:PRK06145 3 NLSASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHAR-GIGQGDVVALLMKNSAAFLELAFAASYLGAVFLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 111 TNPLYTPREMQHQFNDSGAKAIVILANFAGNlekilsqTAIEHvivtqigdllgfpKKLIVNAVVKYVKKMVPAYHLPGA 190
Cdd:PRK06145 82 INYRLAADEVAYILGDAGAKLLLVDEEFDAI-------VALET-------------PKIVIDAAAQADSRRLAQGGLEIP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 191 isfgdalsrgsrqPLKPVAikNTDLAFVQYTGGTTGVSKGAALTHRNIISNVICQdewMKPAGVPDGQGIIVAAlPLYHV 270
Cdd:PRK06145 142 -------------PQAAVA--PTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDH---VIALGLTASERLLVVG-PLYHV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 271 YALTTNALASLKSGSMnLLITNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMAL-QTSV 349
Cdd:PRK06145 203 GAFDLPGIAVLWVGGT-LRIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTpESRI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 350 ADRWQKLTGNKPAEGYGLSETspvlCS-NTVTEEG---NRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFG 425
Cdd:PRK06145 282 RDFTRVFTRARYIDAYGLTET----CSgDTLMEAGreiEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTK 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 426 GYYNRPDESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGE- 504
Cdd:PRK06145 358 GYWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGEr 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 518832993 505 TVKIFVVKKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREE 561
Cdd:PRK06145 438 ITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
53-565 |
3.84e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 204.75 E-value: 3.84e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 53 GKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAI 132
Cdd:PRK08276 9 GEVVTYGELEARSNRLAHGLR-ALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 133 VILANFAGNLEKILSQTAiehvivtqigdlLGFPKKLIVNAVVkyvkkmvpayhlPGAISFGDALSRGSRQPLKPVaikn 212
Cdd:PRK08276 88 IVSAALADTAAELAAELP------------AGVPLLLVVAGPV------------PGFRSYEEALAAQPDTPIADE---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 213 TDLAFVQYTGGTTGVSKG--AALTHRNIISN------VICQDEWmkpaGVPDGQGIIVAalPLYH----VYALTTNALAs 280
Cdd:PRK08276 140 TAGADMLYSSGTTGRPKGikRPLPGLDPDEApgmmlaLLGFGMY----GGPDSVYLSPA--PLYHtaplRFGMSALALG- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 281 lksgsmNLLITNPR-DLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRinEV----DFSELRitSAGGMALQTSVADRWQK 355
Cdd:PRK08276 213 ------GTVVVMEKfDAEEALALIERYRVTHSQLVPTMFVRMLKLPE--EVraryDVSSLR--VAIHAAAPCPVEVKRAM 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 356 LTGNKPA--EGYGLSETSPVLCSNTVtEEGNRVGTIGIPWPSTyMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRPDE 433
Cdd:PRK08276 283 IDWWGPIihEYYASSEGGGVTVITSE-DWLAHPGSVGKAVLGE-VRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEK 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 434 SAKV-LEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFV-- 510
Cdd:PRK08276 361 TAAArNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVqp 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 518832993 511 ---VKKDEALTEDSITrYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREEELAK 565
Cdd:PRK08276 441 adgADAGDALAAELIA-WLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEG 497
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
220-555 |
5.07e-59 |
|
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: 199.42 E-value: 5.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 220 YTGGTTGVSKGAALTHRNIISNVIcqdEWMKPAGVpDGQGIIVAALPLYHVYALTTnALASLKSGSMNLLITNpRDLNAF 299
Cdd:cd17637 7 HTAAVAGRPRGAVLSHGNLIAANL---QLIHAMGL-TEADVYLNMLPLFHIAGLNL-ALATFHAGGANVVMEK-FDPAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 300 IDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAggmaLQT-SVADRWQKLTGNKPAEGYGLSETSPVLCSNT 378
Cdd:cd17637 81 LELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLG----LDApETIQRFEETTGATFWSLYGQTETSGLVTLSP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 379 VTEegnRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRPDESAKVLEDGWFKTGDIGVMTADGYFK 458
Cdd:cd17637 157 YRE---RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLW 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 459 IVDRK--KDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVK-IFVVKKDEALTEDSITRYCRENLTAYKV 535
Cdd:cd17637 234 YAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKaVCVLKPGATLTADELIEFVGSRIARYKK 313
|
330 340
....*....|....*....|
gi 518832993 536 PKHIEFRTELPKSNVGKILR 555
Cdd:cd17637 314 PRYVVFVEALPKTADGSIDR 333
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
26-561 |
6.18e-59 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 205.38 E-value: 6.18e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 26 PDSYTSLAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAG 105
Cdd:PRK06155 17 PPSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALA-AAGVKRGDRVALMCGNRIEFLDVFLGCAWLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 106 LTVVNTNPLYTPREMQHQFNDSGAKAIVILANFAGNLEKILSqtaiehvivtqigDLLGFPKKLIVNAVvkyvkkmvPAY 185
Cdd:PRK06155 96 AIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAADP-------------GDLPLPAVWLLDAP--------ASV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 186 HLPGAISFGDALSRGsrQPLKPVAIKNTDLAFVQYTGGTTGVSKGAALTHrniisnviCQDEWM-----KPAGVPDGQgI 260
Cdd:PRK06155 155 SVPAGWSTAPLPPLD--APAPAAAVQPGDTAAILYTSGTTGPSKGVCCPH--------AQFYWWgrnsaEDLEIGADD-V 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 261 IVAALPLYHVYALTTNALASLKSGSMNLLitnPR-DLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITS 339
Cdd:PRK06155 224 LYTTLPLFHTNALNAFFQALLAGATYVLE---PRfSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVAL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 340 AGGMALQtsVADRWQKLTGNKPAEGYGLSETSPVLcsnTVTEEGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIW-- 417
Cdd:PRK06155 301 GPGVPAA--LHAAFRERFGVDLLDGYGSTETNFVI---AVTHGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLlr 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 418 AKGPQVFG-GYYNRPDESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVG 496
Cdd:PRK06155 376 ADEPFAFAtGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFP 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518832993 497 VPNEKSGETVKIFVVKKD-EALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREE 561
Cdd:PRK06155 456 VPSELGEDEVMAAVVLRDgTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
82-562 |
1.04e-58 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 202.91 E-value: 1.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 82 DRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAivilanfagnlekilsqtaiehVIVTQIGD 161
Cdd:PRK07787 46 RRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQA----------------------WLGPAPDD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 162 LLGFPKklivnavvkyvkkmVPAyhlpgaisfgDALSRGSRQPLKPVAiknTDLAFVQYTGGTTGVSKGAALTHRNIISN 241
Cdd:PRK07787 104 PAGLPH--------------VPV----------RLHARSWHRYPEPDP---DAPALIVYTSGTTGPPKGVVLSRRAIAAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 242 V-ICQDEWmkpAGVPDGqgIIVAALPLYHVYALTTNALASLKSGSMNLLITNP------RDLNAfiddlkkyKITAFTGL 314
Cdd:PRK07787 157 LdALAEAW---QWTADD--VLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPtpeayaQALSE--------GGTLYFGV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 315 NTLYNGLLNHPRINEVdFSELRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETspvLCSNTVTEEGN-RVGTIGIPW 393
Cdd:PRK07787 224 PTVWSRIAADPEAARA-LRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTET---LITLSTRADGErRPGWVGLPL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 394 PSTYMKCVTEDGTEAAL-GEP-GEIWAKGPQVFGGYYNRPDESAKVL-EDGWFKTGDIGVMTADGYFKIVDRKK-DMILV 469
Cdd:PRK07787 300 AGVETRLVDEDGGPVPHdGETvGELQVRGPTLFDGYLNRPDATAAAFtADGWFRTGDVAVVDPDGMHRIVGREStDLIKS 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 470 SGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKDEAlTEDSITRYCRENLTAYKVPKHIEFRTELPKSN 549
Cdd:PRK07787 380 GGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDV-AADELIDFVAQQLSVHKRPREVRFVDALPRNA 458
|
490
....*....|...
gi 518832993 550 VGKILRRPLREEE 562
Cdd:PRK07787 459 MGKVLKKQLLSEG 471
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
46-560 |
1.21e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 204.24 E-value: 1.21e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 46 APAYACMGKQITFSELDTLSQQFASFLqNDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFN 125
Cdd:PRK07786 33 APALRFLGNTTTWRELDDRVAALAGAL-SRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 126 DSGAKAIV---ILANFAGNLEKIlsQTAIEHVIV---TQIGDLLGFpkklivnavvkyvkkmvpayhlpgaisfgDALSR 199
Cdd:PRK07786 112 DCGAHVVVteaALAPVATAVRDI--VPLLSTVVVaggSSDDSVLGY-----------------------------EDLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 200 GSRQPLKPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMKpAGVPDGQGIIvaALPLYHVYALTTNALA 279
Cdd:PRK07786 161 EAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNG-ADINSDVGFV--GVPLFHIAGIGSMLPG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 280 SLKSGSMNLLITNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSeLRITSAGGMALQTSVADR-WQKLTG 358
Cdd:PRK07786 238 LLLGAPTVIYPLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLA-LRVLSWGAAPASDTLLRQmAATFPE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 359 NKPAEGYGLSETSPVLCSNTVTEEGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRPDESAKVL 438
Cdd:PRK07786 317 AQILAAFGQTEMSPVTCMLLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 439 EDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGET-VKIFVVKKDEA- 516
Cdd:PRK07786 397 AGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVpVAVAAVRNDDAa 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 518832993 517 LTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLRE 560
Cdd:PRK07786 477 LTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRE 520
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
54-562 |
7.36e-58 |
|
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: 202.34 E-value: 7.36e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 54 KQITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIV 133
Cdd:cd05970 46 RIFTFAELADYSDKTANFFKA-MGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 134 ILAnfagnlEKILSQtaiehVIVTQIGDLLGFPKKLIVNAVVkyvkkmvpayhLPGAISFGDALSRGS---RQPLKPVAI 210
Cdd:cd05970 125 AIA------EDNIPE-----EIEKAAPECPSKPKLVWVGDPV-----------PEGWIDFRKLIKNASpdfERPTANSYP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 211 KNTDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEW--MKPAG----VPD------------GQGIIVAALPLYHVYA 272
Cdd:cd05970 183 CGEDILLVYFSSGTTGMPKMVEHDFTYPLGHIVTAKYWqnVREGGlhltVADtgwgkavwgkiyGQWIAGAAVFVYDYDK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 273 LTTNALaslksgsmnllitnprdlnafIDDLKKYKITAFTGLNTLYNGLLnHPRINEVDFSELRITSAGGMALQTSVADR 352
Cdd:cd05970 263 FDPKAL---------------------LEKLSKYGVTTFCAPPTIYRFLI-REDLSRYDLSSLRYCTTAGEALNPEVFNT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 353 WQKLTGNKPAEGYGLSETspVLCSNTVTEEGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEI---WAKGPQV--FGGY 427
Cdd:cd05970 321 FKEKTGIKLMEGFGQTET--TLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIvirTSKGKPVglFGGY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 428 YNRPDESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVK 507
Cdd:cd05970 399 YKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVK 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 508 IFVV-----KKDEALTEDsITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREEE 562
Cdd:cd05970 479 ATIVlakgyEPSEELKKE-LQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRERD 537
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
31-561 |
1.11e-57 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 201.65 E-value: 1.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 31 SLAALIEEGVKRFSSAPAYACMGKQI--TFSELDTLSQQFASFLQNDlKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTV 108
Cdd:PRK05852 17 RIADLVEVAATRLPEAPALVVTADRIaiSYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASRADLVV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 109 VNTNPLYTPREMQHQFNDSGAKAIVILANfaGNLEKILSQTAIEHVIVTQIGDLLGFPKKLIVnavvkyvkkmvpayHLP 188
Cdd:PRK05852 96 VPLDPALPIAEQRVRSQAAGARVVLIDAD--GPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSV--------------HLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 189 GAISFGDALSrgSRQPLKPvaikntDLAFVQYTGGTTGVSKGAALTHRNIISNV--ICQDEWMKPagvpdgQGIIVAALP 266
Cdd:PRK05852 160 AATEPTPATS--TPEGLRP------DDAMIMFTGGTTGLPKMVPWTHANIASSVraIITGYRLSP------RDATVAVMP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 267 LYHVYALTTNALASLKSGSMNLLITNPR-DLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSE--LRITSAGGM 343
Cdd:PRK05852 226 LYHGHGLIAALLATLASGGAVLLPARGRfSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPaaLRFIRSCSA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 344 ALQTSVADRWQKLTGNKPAEGYGLSETSPVLCSNTVTEEG---NRVGTIGIPWPST--YMKCVTEDGTEAALGEPGEIWA 418
Cdd:PRK05852 306 PLTAETAQALQTEFAAPVVCAFGMTEATHQVTTTQIEGIGqteNPVVSTGLVGRSTgaQIRIVGSDGLPLPAGAVGEVWL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 419 KGPQVFGGYYNRPDESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVP 498
Cdd:PRK05852 386 RGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVP 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518832993 499 NEKSGETVKIFVVKKDEA-LTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREE 561
Cdd:PRK05852 466 DQLYGEAVAAVIVPRESApPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQ 529
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
53-558 |
2.43e-57 |
|
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: 199.66 E-value: 2.43e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 53 GKQITFSEL-DTLSQQFASFLQndLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQhQFNDSGAKA 131
Cdd:cd05923 26 GLRLTYSELrARIEAVAARLHA--RGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELA-ELIERGEMT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 132 IVILANFAGNLEKIlsqtAIEHVIVTQIGDLLGfpkklivnavvkyvkkmvpayhLPGAISFGDALSRGSRQPLKPvaik 211
Cdd:cd05923 103 AAVIAVDAQVMDAI----FQSGVRVLALSDLVG----------------------LGEPESAGPLIEDPPREPEQP---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 212 ntdlAFVQYTGGTTGVSKGAALTHRNIISNVIcqdeWMKP-AGVPDGQGIIVAAL-PLYHVYALTTNALASLKSGSMNLL 289
Cdd:cd05923 153 ----AFVFYTSGTTGLPKGAVIPQRAAESRVL----FMSTqAGLRHGRHNVVLGLmPLYHVIGFFAVLVAALALDGTYVV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 290 IT--NPRDLNAFIDdlkKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSVADRWQKLTGNKPAEGYGL 367
Cdd:cd05923 225 VEefDPADALKLIE---QERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 368 SETSpvlcsNTVTEEGNRVGTIGIPWPSTYMKCVTEDGTE---AALGEPGEIWAK--GPQVFGGYYNRPDESAKVLEDGW 442
Cdd:cd05923 302 TEAM-----NSLYMRDARTGTEMRPGFFSEVRIVRIGGSPdeaLANGEEGELIVAaaADAAFTGYLNQPEATAKKLQDGW 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 443 FKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKDEALTEDSI 522
Cdd:cd05923 377 YRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADEL 456
|
490 500 510
....*....|....*....|....*....|....*..
gi 518832993 523 TRYCREN-LTAYKVPKHIEFRTELPKSNVGKILRRPL 558
Cdd:cd05923 457 DQFCRASeLADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
214-559 |
2.70e-57 |
|
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: 195.78 E-value: 2.70e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 214 DLAFVQYTGGTTGVSKGAALTHRNIISNVicqdeWMKPAGVPDGQG-IIVAALPLYHVYALTTNALASLKSGSmNLLITN 292
Cdd:cd05944 3 DVAAYFHTGGTTGTPKLAQHTHSNEVYNA-----WMLALNSLFDPDdVLLCGLPLFHVNGSVVTLLTPLASGA-HVVLAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 293 P---RDLNAFIDDLK---KYKITAFTGLNTLYNGLLNHPriNEVDFSELRITSAGGMALQTSVADRWQKLTGNKPAEGYG 366
Cdd:cd05944 77 PagyRNPGLFDNFWKlveRYRITSLSTVPTVYAALLQVP--VNADISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 367 LSETSpvlCSNTVTEEGN--RVGTIGIPWPSTYMKCVTEDGT-----EAALGEPGEIWAKGPQVFGGYYNRPDESAKVLE 439
Cdd:cd05944 155 LTEAT---CLVAVNPPDGpkRPGSVGLRLPYARVRIKVLDGVgrllrDCAPDEVGEICVAGPGVFGGYLYTEGNKNAFVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 440 DGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFV-VKKDEALT 518
Cdd:cd05944 232 DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVqLKPGAVVE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 518832993 519 EDSITRYCRENLTAY-KVPKHIEFRTELPKSNVGKILRRPLR 559
Cdd:cd05944 312 EEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
67-560 |
2.85e-57 |
|
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: 199.45 E-value: 2.85e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 67 QFASFLQnDLKLQKGDRIAIQMPN-----LLQYPIAMFGALragLTVVNTNplYTPREMQHQFNDSGAKAIVILANFAGN 141
Cdd:cd12118 41 RLASALA-ALGISRGDTVAVLAPNtpamyELHFGVPMAGAV---LNALNTR--LDAEEIAFILRHSEAKVLFVDREFEYE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 142 lekilsqtaiehvivtqigdllgfpkklivnavvkyvkkmvpayhlpgaisfgDALSRGSRQPLKPVAIKNTDLAFVQYT 221
Cdd:cd12118 115 -----------------------------------------------------DLLAEGDPDFEWIPPADEWDPIALNYT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 222 GGTTGVSKGAALTHR----NIISNVIcqdEW-MKPAGVpdgqgiIVAALPLYHV----YALTTNALaslksGSMNLLITN 292
Cdd:cd12118 142 SGTTGRPKGVVYHHRgaylNALANIL---EWeMKQHPV------YLWTLPMFHCngwcFPWTVAAV-----GGTNVCLRK 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 293 PRDLNAFiDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSE-LRITSAGGmALQTSVADRWQKLtGNKPAEGYGLSETS 371
Cdd:cd12118 208 VDAKAIY-DLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHrVHVMTAGA-PPPAAVLAKMEEL-GFDVTHVYGLTETY 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 372 P--VLCS----------------------NTVTEEGNRVGTigipwPSTyMKCVTEDGTEAalgepGEIWAKGPQVFGGY 427
Cdd:cd12118 285 GpaTVCAwkpewdelpteerarlkarqgvRYVGLEEVDVLD-----PET-MKPVPRDGKTI-----GEIVFRGNIVMKGY 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 428 YNRPDESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVK 507
Cdd:cd12118 354 LKNPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPC 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 518832993 508 IFV-VKKDEALTEDSITRYCRENLTAYKVPKHIEFRtELPKSNVGKILRRPLRE 560
Cdd:cd12118 434 AFVeLKEGAKVTEEEIIAFCREHLAGFMVPKTVVFG-ELPKTSTGKIQKFVLRD 486
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
75-559 |
8.22e-56 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 196.06 E-value: 8.22e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 75 DLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIVILANFAGNLEKILSQ--TAIE 152
Cdd:PRK08008 56 SLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEdaTPLR 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 153 HVIVTQIGDllgfpkklivnavvkyvkkmvPAyhLPGAISFGDALSRGSRQPLKPVAIKNTDLAFVQYTGGTTGVSKGAA 232
Cdd:PRK08008 136 HICLTRVAL---------------------PA--DDGVSSFTQLKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 233 LTHRNII---------SNVICQDEWMKPagvpdgqgiivaaLPLYHVYALTTNALASLKSGSmNLLITNPRDLNAFIDDL 303
Cdd:PRK08008 193 ITHYNLRfagyysawqCALRDDDVYLTV-------------MPAFHIDCQCTAAMAAFSAGA-TFVLLEKYSARAFWGQV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 304 KKYKITAFTGLNTLYNGLLNHP--------RINEVDFSeLRITSAGGMALQTSVADRWqkLTGnkpaegYGLSETSPVLC 375
Cdd:PRK08008 259 CKYRATITECIPMMIRTLMVQPpsandrqhCLREVMFY-LNLSDQEKDAFEERFGVRL--LTS------YGMTETIVGII 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 376 SNTVTEEgNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKG---PQVFGGYYNRPDESAKVLE-DGWFKTGDIGVM 451
Cdd:PRK08008 330 GDRPGDK-RRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEaDGWLHTGDTGYV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 452 TADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKD-EALTEDSITRYCRENL 530
Cdd:PRK08008 409 DEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEgETLSEEEFFAFCEQNM 488
|
490 500
....*....|....*....|....*....
gi 518832993 531 TAYKVPKHIEFRTELPKSNVGKILRRPLR 559
Cdd:PRK08008 489 AKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
31-552 |
7.90e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 193.95 E-value: 7.90e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 31 SLAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVN 110
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLI-AQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 111 TNPLYTPREMQHQFNDSGAKAIVILANFAGNLEKILSQTA-IEHVIvtQIGDLLGfpkklivnavvkyvkkmvPAYhLPG 189
Cdd:PRK07798 83 VNYRYVEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLPkLRTLV--VVEDGSG------------------NDL-LPG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 190 AISFGDALSRGSRQPLkPVAIKNTDLaFVQYTGGTTGVSKG----------AALTHRNIISNVICQDEWMKPAGVPDGQG 259
Cdd:PRK07798 142 AVDYEDALAAGSPERD-FGERSPDDL-YLLYTGGTTGMPKGvmwrqedifrVLLGGRDFATGEPIEDEEELAKRAAAGPG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 260 IIV-AALPLYHVYALTTnALASLKSGSMNLLITNPR-DLNAFIDDLKKYKIT--AFTG-------LNTLYNGllnhpriN 328
Cdd:PRK07798 220 MRRfPAPPLMHGAGQWA-AFAALFSGQTVVLLPDVRfDADEVWRTIEREKVNviTIVGdamarplLDALEAR-------G 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 329 EVDFSELRITSAGGMALQTSVADRWQKLtgnKP----AEGYGLSET----SPVLCSNTVTEEGNRVgTIGipwPSTymKC 400
Cdd:PRK07798 292 PYDLSSLFAIASGGALFSPSVKEALLEL---LPnvvlTDSIGSSETgfggSGTVAKGAVHTGGPRF-TIG---PRT--VV 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 401 VTEDGTEAALGEPGEIW-AKGPQVFGGYYNRPDESAKVLE--DG--WFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVY 475
Cdd:PRK07798 363 LDEDGNPVEPGSGEIGWiARRGHIPLGYYKDPEKTAETFPtiDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVF 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518832993 476 PNEIEEVVSQCPGVLEVACVGVPNEKSGETVkIFVVKKDE--ALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGK 552
Cdd:PRK07798 443 PEEVEEALKAHPDVADALVVGVPDERWGQEV-VAVVQLREgaRPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
40-560 |
1.74e-53 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 189.90 E-value: 1.74e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 40 VKRFSSAPAY--ACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTP 117
Cdd:PRK13391 7 AQTTPDKPAVimASTGEVVTYRELDERSNRLAHLFR-SLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 118 REMQHQFNDSGAKAIVILANFAGNLEKILSQT-AIEHVIVTQIGDllgfpkklivnavvkyvkkmvpayHLPGAISFGDA 196
Cdd:PRK13391 86 AEAAYIVDDSGARALITSAAKLDVARALLKQCpGVRHRLVLDGDG------------------------ELEGFVGYAEA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 197 LSRgsrQPLKPVA--IKNTDLafvQYTGGTTGVSKG--AALTHRNIISNVICQDEWMKPAGVPDGQgIIVAALPLYHVYA 272
Cdd:PRK13391 142 VAG---LPATPIAdeSLGTDM---LYSSGTTGRPKGikRPLPEQPPDTPLPLTAFLQRLWGFRSDM-VYLSPAPLYHSAP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 273 LTTNALASLKSGSMnlLITNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPriNEV----DFSELRITSAGGMALQTS 348
Cdd:PRK13391 215 QRAVMLVIRLGGTV--IVMEHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLP--EEVrdkyDLSSLEVAIHAAAPCPPQ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 349 VADRWQKLTGNKPAEGYGLSETSPVLCSNTvTEEGNRVGTIGIPWPSTYMKCvTEDGTEAALGEPGEIWAKGPQVFGgYY 428
Cdd:PRK13391 291 VKEQMIDWWGPIIHEYYAATEGLGFTACDS-EEWLAHPGTVGRAMFGDLHIL-DDDGAELPPGEPGTIWFEGGRPFE-YL 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 429 NRPDESAKVL--EDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETV 506
Cdd:PRK13391 368 NDPAKTAEARhpDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEV 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 518832993 507 KIFV-----VKKDEALTEDSITrYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLRE 560
Cdd:PRK13391 448 KAVVqpvdgVDPGPALAAELIA-FCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRD 505
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
31-558 |
3.76e-53 |
|
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: 188.31 E-value: 3.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 31 SLAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVN 110
Cdd:cd05920 16 PLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLR-GLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 111 TNPLYTPREMQHQFNDSGAKAIVIlanfagnlekilsqtaiehvivtqigdllgfpkklivnavvkyvkkmvpayhlPGA 190
Cdd:cd05920 95 ALPSHRRSELSAFCAHAEAVAYIV-----------------------------------------------------PDR 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 191 ISFGD--ALSRgsrqplkPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMkpaGVpDGQGIIVAALPLY 268
Cdd:cd05920 122 HAGFDhrALAR-------ELAESIPEVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVC---GL-DQDTVYLAVLPAA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 269 HVYALTT-NALASLKSGSMNLLITNPRDLNAFiDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQT 347
Cdd:cd05920 191 HNFPLACpGVLGTLLAGGRVVLAPDPSPDAAF-PLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 348 SVADRWQKLTGNKPAEGYGLSETspVLCSNTVTEEGNRV-GTIGIPW-PSTYMKCVTEDGTEAALGEPGEIWAKGPQVFG 425
Cdd:cd05920 270 ALARRVPPVLGCTLQQVFGMAEG--LLNYTRLDDPDEVIiHTQGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIR 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 426 GYYNRPDESAKVL-EDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGE 504
Cdd:cd05920 348 GYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGE 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 518832993 505 TVKIFVVKKDEALTEDSITRYCRE-NLTAYKVPKHIEFRTELPKSNVGKILRRPL 558
Cdd:cd05920 428 RSCAFVVLRDPPPSAAQLRRFLRErGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
29-562 |
1.31e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 188.21 E-value: 1.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 29 YTSLAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTV 108
Cdd:PRK07788 48 YGPFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLA-LGVRAGDGVAVLARNHRGFVLALYAAGKVGARI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 109 VNTNPLYTPREMQHQFNDSGAKAIVILANFAGNLEKILsqtaiehvivTQIGDLLgfpkklivnAVVKYVKKMVPAyhLP 188
Cdd:PRK07788 127 ILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALP----------PDLGRLR---------AWGGNPDDDEPS--GS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 189 GAISFGDALSRGSRQPLkPVAIKNTdlAFVQYTGGTTGVSKGAALTHRNIISNVicqdewmkpAGVPD------GQGIIV 262
Cdd:PRK07788 186 TDETLDDLIAGSSTAPL-PKPPKPG--GIVILTSGTTGTPKGAPRPEPSPLAPL---------AGLLSrvpfraGETTLL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 263 AAlPLYHVYALttnALASLKSGSMNLLITNPR-DLNAFIDDLKKYKITAFTGLNTLYNGLLNHP--RINEVDFSELRITS 339
Cdd:PRK07788 254 PA-PMFHATGW---AHLTLAMALGSTVVLRRRfDPEATLEDIAKHKATALVVVPVMLSRILDLGpeVLAKYDTSSLKIIF 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 340 AGGMALQTSVADRWQKLTGNKPAEGYGLSETSpvLCSNTVTEEGNRV-GTIGIPWPSTYMKCVTEDGTEAALGEPGEIWA 418
Cdd:PRK07788 330 VSGSALSPELATRALEAFGPVLYNLYGSTEVA--FATIATPEDLAEApGTVGRPPKGVTVKILDENGNEVPRGVVGRIFV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 419 KGPQVFGGYYNRPDesaKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVP 498
Cdd:PRK07788 408 GNGFPFEGYTDGRD---KQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVD 484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518832993 499 NEKSGETVKIFVVKKD-EALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREEE 562
Cdd:PRK07788 485 DEEFGQRLRAFVVKAPgAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
53-555 |
1.50e-52 |
|
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: 186.11 E-value: 1.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 53 GKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAI 132
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLK-INGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 133 vilanFAGNlekilsqtaiehvivtqigdllgfpkklivnavvkyvkkmvpayhlpgaisfgdalsrgsrqplkpvaikN 212
Cdd:cd05914 84 -----FVSD----------------------------------------------------------------------E 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 213 TDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEwMKPAGVPDgqgIIVAALPLYHVYALTTNALASLKSGSMNLLITN 292
Cdd:cd05914 89 DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKE-VVLLGKGD---KILSILPLHHIYPLTFTLLLPLLNGAHVVFLDK 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 293 PRdlNAFIDDLKKYKITAFTGLNTLY-----------------------NGLLNHPRINEVDFSEL--------RITSAG 341
Cdd:cd05914 165 IP--SAKIIALAFAQVTPTLGVPVPLviekifkmdiipkltlkkfkfklAKKINNRKIRKLAFKKVheafggniKEFVIG 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 342 GMALQTSVADRWQKLtGNKPAEGYGLSETSPVLCSNTVTEEgnRVGTIGIPWPSTYMKCVTEDGTEAAlgepGEIWAKGP 421
Cdd:cd05914 243 GAKINPDVEEFLRTI-GFPYTIGYGMTETAPIISYSPPNRI--RLGSAGKVIDGVEVRIDSPDPATGE----GEIIVRGP 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 422 QVFGGYYNRPDESAKVL-EDGWFKTGDIGVMTADGYFKIVDRKKDMILV-SGFNVYPNEIEEVVSQCPGVLEvACVGVPN 499
Cdd:cd05914 316 NVMKGYYKNPEATAEAFdKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLE-SLVVVQE 394
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518832993 500 EKSGETVKIF----------VVKKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILR 555
Cdd:cd05914 395 KKLVALAYIDpdfldvkalkQRNIIDAIKWEVRDKVNQKVPNYKKISKVKIVKEEFEKTPKGKIKR 460
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
54-559 |
2.35e-52 |
|
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: 184.94 E-value: 2.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 54 KQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIV 133
Cdd:cd05971 5 EKVTFKELKTASNRFANVLK-EIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 134 ilanfagnlekilsqtaiehvivTQIGDllgfpkklivnavvkyvkkmvpayhlpgaisfgdalsrgsrqplkpvaiknt 213
Cdd:cd05971 84 -----------------------TDGSD---------------------------------------------------- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 214 DLAFVQYTGGTTGVSKGAALTHRNIISNV----ICQDEWMKPAGV---PDGQGIIVAALPLYhvyalttnaLASLKSGsM 286
Cdd:cd05971 89 DPALIIYTSGTTGPPKGALHAHRVLLGHLpgvqFPFNLFPRDGDLywtPADWAWIGGLLDVL---------LPSLYFG-V 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 287 NLLITNPR--DLNAFIDDLKKYKIT-AF---TGLNTL--YNGLLNHPRINevdfseLRITSAGGMALQTSVAdRWQKLT- 357
Cdd:cd05971 159 PVLAHRMTkfDPKAALDLMSRYGVTtAFlppTALKMMrqQGEQLKHAQVK------LRAIATGGESLGEELL-GWAREQf 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 358 GNKPAEGYGLSETSPVLCSNTVTEEGnRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQ--VFGGYYNRPDESA 435
Cdd:cd05971 232 GVEVNEFYGQTECNLVIGNCSALFPI-KPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDpvAFLGYWNNPSATE 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 436 KVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKDE 515
Cdd:cd05971 311 KKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPG 390
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 518832993 516 ALTEDSITR----YCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLR 559
Cdd:cd05971 391 ETPSDALAReiqeLVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
31-560 |
4.17e-52 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 192.45 E-value: 4.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 31 SLAALIEEGVKRFSSAPAYA-CMGKQITFSELDTLSQQFASFLQNDLKLQKgdRIAIQMPNLLQYPIAMFGALRAGLTVV 109
Cdd:PRK08633 616 PLAEAWIDTAKRNWSRLAVAdSTGGELSYGKALTGALALARLLKRELKDEE--NVGILLPPSVAGALANLALLLAGKVPV 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 110 NTNplYTpremqhqfndSGAKAivilanfagnLEKILSQTAIEHVI-----VTQIGdLLGFPKKLIVNAVVKYVKKMVPA 184
Cdd:PRK08633 694 NLN--YT----------ASEAA----------LKSAIEQAQIKTVItsrkfLEKLK-NKGFDLELPENVKVIYLEDLKAK 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 185 yhlpgaISFGDALSRGSRQPLKPVA---------IKNTDLAFVQYTGGTTGVSKGAALTHRNIISN------VICQDEwm 249
Cdd:PRK08633 751 ------ISKVDKLTALLAARLLPARllkrlygptFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNieqisdVFNLRN-- 822
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 250 kpagvpdgQGIIVAALPLYHVYALTTNALASLKSGSMNLLITNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINE 329
Cdd:PRK08633 823 --------DDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYHPDPTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHP 894
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 330 VDFSELRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETSPVLCSNTVTEE--------GNRVGTIGIPWPSTYMKCV 401
Cdd:PRK08633 895 LMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNLPDVLaadfkrqtGSKEGSVGMPLPGVAVRIV 974
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 402 T-EDGTEAALGEPGEIWAKGPQVFGGYYNRPDESAKVLED----GWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYP 476
Cdd:PRK08633 975 DpETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIKDidgiGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPL 1054
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 477 NEIEEVVSQ--CPGVLEVACVGVPNEKSGEtvKIFVVKKDEALTEDSITRYCRE-NLTAYKVPKHIEFRTELPKSNVGKI 553
Cdd:PRK08633 1055 GAVEEELAKalGGEEVVFAVTAVPDEKKGE--KLVVLHTCGAEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKL 1132
|
....*..
gi 518832993 554 LRRPLRE 560
Cdd:PRK08633 1133 DLKGLKE 1139
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
53-562 |
4.43e-52 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 186.52 E-value: 4.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 53 GKQI--TFSELDTLSQQFASFLQNDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAK 130
Cdd:cd05928 37 GDEVkwSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 131 AIVILANFAGNLEKILSQTAIEHVivtqigdllgfpkklivnavvkyvKKMVPAYHLPGAISFGDALSRGSRQPlKPVAI 210
Cdd:cd05928 117 CIVTSDELAPEVDSVASECPSLKT------------------------KLLVSEKSRDGWLNFKELLNEASTEH-HCVET 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 211 KNTDLAFVQYTGGTTGVSKGAALTHRNI-ISNVICQDEWM--KPAGV---PDGQGIIVAALplyhvyaltTNALASLKSG 284
Cdd:cd05928 172 GSQEPMAIYFTSGTTGSPKMAEHSHSSLgLGLKVNGRYWLdlTASDImwnTSDTGWIKSAW---------SSLFEPWIQG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 285 SMNLLITNPR-DLNAFIDDLKKYKITAFTGLNTLYNGLLNHpRINEVDFSELRITSAGGMALQTSVADRWQKLTGNKPAE 363
Cdd:cd05928 243 ACVFVHHLPRfDPLVILKTLSSYPITTFCGAPTVYRMLVQQ-DLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 364 GYGLSETSpVLCSNTVTEEgNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAK-GPQ----VFGGYYNRPDESAKVL 438
Cdd:cd05928 322 GYGQTETG-LICANFKGMK-IKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 439 EDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKDEALT 518
Cdd:cd05928 400 RGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLS 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 518832993 519 ED--SITRYCRE---NLTA-YKVPKHIEFRTELPKSNVGKILRRPLREEE 562
Cdd:cd05928 480 HDpeQLTKELQQhvkSVTApYKYPRKVEFVQELPKTVTGKIQRNELRDKE 529
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
57-558 |
8.17e-52 |
|
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: 183.42 E-value: 8.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 57 TFSELDTLSQQFASFLQNDlKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGakaivila 136
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQ-GIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLD-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 137 nfagnlekilsqtaIEHVIVTQIgdllgFPKKLIVnavvkyvkkmvpayhlpgAISFgDALSRGSRQPLKPVAIKNTD-L 215
Cdd:TIGR01923 72 --------------VQLLLTDSL-----LEEKDFQ------------------ADSL-DRIEAAGRYETSLSASFNMDqI 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 216 AFVQYTGGTTGVSKGAALTHRNIISNVIC---------QDEWMkpagvpdgqgiivAALPLYHV--YALTTNALAslksG 284
Cdd:TIGR01923 114 ATLMFTSGTTGKPKAVPHTFRNHYASAVGskenlgfteDDNWL-------------LSLPLYHIsgLSILFRWLI----E 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 285 SMNLLITNPrdLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEvdfsELRITSAGGMALQTSVADRWQKLtGNKPAEG 364
Cdd:TIGR01923 177 GATLRIVDK--FNQLLEMIANERVTHISLVPTQLNRLLDEGGHNE----NLRKILLGGSAIPAPLIEEAQQY-GLPIYLS 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 365 YGLSETSPVLCSNTvTEEGNRVGTIGIPWPSTYMKCVTEDgteaaLGEPGEIWAKGPQVFGGYYNRPDESAKVLEDGWFK 444
Cdd:TIGR01923 250 YGMTETCSQVTTAT-PEMLHARPDVGRPLAGREIKIKVDN-----KEGHGEIMVKGANLMKGYLYQGELTPAFEQQGWFN 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 445 TGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGET-VKIFVVKKDEALTEdsIT 523
Cdd:TIGR01923 324 TGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVpVAYIVSESDISQAK--LI 401
|
490 500 510
....*....|....*....|....*....|....*
gi 518832993 524 RYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPL 558
Cdd:TIGR01923 402 AYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
219-560 |
3.60e-51 |
|
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: 182.58 E-value: 3.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 219 QYTGGTTGVSKG--AALTHRNIISNVIcqdewMKPAGV--PDGQGIIVAALPLYHVYALTTNALASLKSGSmnLLITNPR 294
Cdd:cd05929 131 LYSGGTTGRPKGikRGLPGGPPDNDTL-----MAAALGfgPGADSVYLSPAPLYHAAPFRWSMTALFMGGT--LVLMEKF 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 295 DLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRI--NEVDFSELRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETSP 372
Cdd:cd05929 204 DPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAvrNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQG 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 373 VLCSNTvTEEGNRVGTIGIPWPSTyMKCVTEDGTEAALGEPGEIWAKGPQVFGgYYNRPD-ESAKVLEDGWFKTGDIGVM 451
Cdd:cd05929 284 LTIING-EEWLTHPGSVGRAVLGK-VHILDEDGNEVPPGEIGEVYFANGPGFE-YTNDPEkTAAARNEGGWSTLGDVGYL 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 452 TADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFV-----VKKDEALTEDSITrYC 526
Cdd:cd05929 361 DEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVqpapgADAGTALAEELIA-FL 439
|
330 340 350
....*....|....*....|....*....|....
gi 518832993 527 RENLTAYKVPKHIEFRTELPKSNVGKILRRPLRE 560
Cdd:cd05929 440 RDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
55-563 |
3.77e-51 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 184.10 E-value: 3.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 55 QITFSELDTLSQQFASFLqNDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTvvnTNPL---YTPREMQHQFNDSGAKA 131
Cdd:PRK13295 55 RFTYRELAALVDRVAVGL-ARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAV---LNPLmpiFRERELSFMLKHAESKV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 132 IVILANFAG--------NLEKILSqtAIEHVIVTQIGDLLGFPKKLIVnavvkyvkkmvPAYHL-PGAisfgDALSRGSR 202
Cdd:PRK13295 131 LVVPKTFRGfdhaamarRLRPELP--ALRHVVVVGGDGADSFEALLIT-----------PAWEQePDA----PAILARLR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 203 qpLKPvaiknTDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMKpAGVPDgqgIIVAALPLYHVYALTTNALASLK 282
Cdd:PRK13295 194 --PGP-----DDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLG-LGADD---VILMASPMAHQTGFMYGLMMPVM 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 283 SGSMNLL--ITNPRDlnaFIDDLKKYKITaFTGLNTLY-NGLLNHPRINEVDFSELRITSAGGMALQTSVADRWQKLTGN 359
Cdd:PRK13295 263 LGATAVLqdIWDPAR---AAELIRTEGVT-FTMASTPFlTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 360 KPAEGYGLSETSPVlcsnTVTEEGNR----VGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRPDESA 435
Cdd:PRK13295 339 KIVSAWGMTENGAV----TLTKLDDPderaSTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 436 kVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVV-KKD 514
Cdd:PRK13295 415 -TDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVpRPG 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 518832993 515 EALTEDSITRYCRENLTAYK-VPKHIEFRTELPKSNVGKI----LRRPLREEEL 563
Cdd:PRK13295 494 QSLDFEEMVEFLKAQKVAKQyIPERLVVRDALPRTPSGKIqkfrLREMLRGEDA 547
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
54-522 |
1.73e-49 |
|
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: 177.94 E-value: 1.73e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 54 KQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIV 133
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLR-SLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 134 IlanfaGNLEKilsqtaiehvivtqigdllgfpkklivnavvkyvkkmvpayhlpgaisfgdalsrgsrqplkpvaiknt 213
Cdd:cd17640 83 V-----ENDSD--------------------------------------------------------------------- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 214 DLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEwMKPAGVPDgqgIIVAALPLYHVY--ALTTNALAslKSGSMnlLIT 291
Cdd:cd17640 89 DLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSD-IVPPQPGD---RFLSILPIWHSYerSAEYFIFA--CGCSQ--AYT 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 292 NPRdlnAFIDDLKKYKITAFTGL----NTLYNG----LLNHPRINEVDF------SELRITSAGGMALQTSVaDRWQKLT 357
Cdd:cd17640 161 SIR---TLKDDLKRVKPHYIVSVprlwESLYSGiqkqVSKSSPIKQFLFlfflsgGIFKFGISGGGALPPHV-DTFFEAI 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 358 GNKPAEGYGLSETSPVLCSNTVteEGNRVGTIGIPWPSTYMKCVTEDGTEA-ALGEPGEIWAKGPQVFGGYYNRPDESAK 436
Cdd:cd17640 237 GIEVLNGYGLTETSPVVSARRL--KCNVRGSVGRPLPGTEIKIVDPEGNVVlPPGEKGIVWVRGPQVMKGYYKNPEATSK 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 437 VL-EDGWFKTGDIGVMTADGYFKIVDRKKDMILVS-GFNVYPNEIEEVVSQCPGVLEVACVG----------VPN----E 500
Cdd:cd17640 315 VLdSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVGqdqkrlgaliVPNfeelE 394
|
490 500
....*....|....*....|..
gi 518832993 501 KSGETVKIFVVKKDEALTEDSI 522
Cdd:cd17640 395 KWAKESGVKLANDRSQLLASKK 416
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
214-555 |
4.00e-49 |
|
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: 172.98 E-value: 4.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 214 DLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMKPagvpDGQGIIVAALPLYHVYALTTnALASLKSGSMNLLITNp 293
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNI----SGEDAILAPGPLSHSLFLYG-AISALYLGGTFIGQRK- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 294 RDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINevdfSELRITSAGGMALQTSVADRWQKLTGN-KPAEGYGLSETSP 372
Cdd:cd17633 75 FNPKSWIRKINQYNATVIYLVPTMLQALARTLEPE----SKIKSIFSSGQKLFESTKKKLKNIFPKaNLIEFYGTSELSF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 373 VlcSNTVTEEGNRVGTIGIPWPSTYMKCVTEDGteaalGEPGEIWAKGPQVFGGYYNRPDESakvlEDGWFKTGDIGVMT 452
Cdd:cd17633 151 I--TYNFNQESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSN----PDGWMSVGDIGYVD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 453 ADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVkIFVVKKDEaLTEDSITRYCRENLTA 532
Cdd:cd17633 220 EEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIA-VALYSGDK-LTYKQLKRFLKQKLSR 297
|
330 340
....*....|....*....|...
gi 518832993 533 YKVPKHIEFRTELPKSNVGKILR 555
Cdd:cd17633 298 YEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
46-558 |
4.16e-49 |
|
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: 176.18 E-value: 4.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 46 APAYACMGKQITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYtPRE-MQHQF 124
Cdd:cd05930 3 AVAVVDGDQSLTYAELDARANRLARYLRE-RGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSY-PAErLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 125 NDSGAKaivilanfagnlekilsqtaiehVIVTQIGDLlgfpkklivnavvkyvkkmvpayhlpgaisfgdalsrgsrqp 204
Cdd:cd05930 81 EDSGAK-----------------------LVLTDPDDL------------------------------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 205 lkpvaikntdlAFVQYTGGTTGVSKGAALTHRNIISNVicqdEWMKPAGVPDGQGIIVAALPLYHVYALTtNALASLKSG 284
Cdd:cd05930 96 -----------AYVIYTSGSTGKPKGVMVEHRGLVNLL----LWMQEAYPLTPGDRVLQFTSFSFDVSVW-EIFGALLAG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 285 SMNLLITN--PRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINevDFSELRITSAGGMALQTSVADRWQKLtgNKPA 362
Cdd:cd05930 160 ATLVVLPEevRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELA--ALPSLRLVLVGGEALPPDLVRRWREL--LPGA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 363 E---GYGLSETSPVLCSNTVTEEGNRVG--TIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRPDESA-K 436
Cdd:cd05930 236 RlvnLYGPTEATVDATYYRVPPDDEEDGrvPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAeR 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 437 VLEDGWF------KTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFV 510
Cdd:cd05930 316 FVPNPFGpgermyRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYV 395
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 518832993 511 V-KKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPL 558
Cdd:cd05930 396 VpDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
46-558 |
3.39e-48 |
|
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: 173.97 E-value: 3.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 46 APAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPlYTPremqhqfn 125
Cdd:cd05945 7 RPAVVEGGRTLTYRELKERADALAAALA-SLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDA-SSP-------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 126 dsgakaivilanfAGNLEKILSQTAIEHVIVTQigdllgfpkklivnavvkyvkkmvpayhlpgaisfgdalsrgsrqpl 205
Cdd:cd05945 77 -------------AERIREILDAAKPALLIADG----------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 206 kpvaiknTDLAFVQYTGGTTGVSKGAALTHRNIISNVicqdEWMKPAGvPDGQGIIVAALPLYH----VYALttnaLASL 281
Cdd:cd05945 97 -------DDNAYIIFTSGSTGRPKGVQISHDNLVSFT----NWMLSDF-PLGPGDVFLNQAPFSfdlsVMDL----YPAL 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 282 KSGSM-----NLLITNPRDLNAFiddLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSVADRWQKL 356
Cdd:cd05945 161 ASGATlvpvpRDATADPKQLFRF---LAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQR 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 357 TGNKPAE-GYGLSETSpVLCS-NTVTEE---GNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRP 431
Cdd:cd05945 238 FPDARIYnTYGPTEAT-VAVTyIEVTPEvldGYDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNP 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 432 DESAKVL--EDG--WFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNeKSGETVK 507
Cdd:cd05945 317 EKTAAAFfpDEGqrAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYK-GEKVTEL 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 518832993 508 I-FVVKK--DEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPL 558
Cdd:cd05945 396 IaFVVPKpgAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
56-559 |
6.49e-48 |
|
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: 172.70 E-value: 6.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 56 ITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVntnPLYT---PREMQHQFNDSGAKAI 132
Cdd:cd05973 1 LTFGELRALSARFANALQ-ELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQ---PLFTafgPKAIEHRLRTSGARLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 133 VILANfagNLEKIlsqtaiehvivtqigdllgfpkklivnavvkyvkkmvpayhlpgaisfgdalsrgsrqplkpvaikN 212
Cdd:cd05973 77 VTDAA---NRHKL------------------------------------------------------------------D 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 213 TDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMkpaGVPDGQGIIVAALPLYhVYALTTNALASLKSGSMNLLITN 292
Cdd:cd05973 88 SDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAV---DLRPEDSFWNAADPGW-AYGLYYAITGPLALGHPTILLEG 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 293 PRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFS-ELRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETS 371
Cdd:cd05973 164 GFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPKgRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 372 PVLCSNTVTEEGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIW---AKGPQV-FGGYYNRPDESAkvlEDGWFKTGD 447
Cdd:cd05973 244 MVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAidiANSPLMwFRGYQLPDTPAI---DGGYYLTGD 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 448 IGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVV-----KKDEALtEDSI 522
Cdd:cd05973 321 TVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVlrgghEGTPAL-ADEL 399
|
490 500 510
....*....|....*....|....*....|....*..
gi 518832993 523 TRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLR 559
Cdd:cd05973 400 QLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
56-545 |
1.88e-47 |
|
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: 173.94 E-value: 1.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 56 ITFSELDTLSQQFAS-FLQNDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVntnPLYtpremqhqfNDSGAKAIvi 134
Cdd:cd05927 6 ISYKEVAERADNIGSaLRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTV---PLY---------DTLGPEAI-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 135 lanfagnlEKILSQTAIEHVIVTqigdllgfpKKLIVnavvkyvkkmvpayhlpgaISFGDALSRGSRQPLKPVAIKNTD 214
Cdd:cd05927 72 --------EYILNHAEISIVFCD---------AGVKV-------------------YSLEEFEKLGKKNKVPPPPPKPED 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 215 LAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMKPAGVPDGQGIIVAALPLYHVYALTTNALASLKSGSMNLLITNPR 294
Cdd:cd05927 116 LATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIR 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 295 DLnafIDDLKKYKITAFTG--------------------------LNTLYN---------GLLNHPRINEVDFS------ 333
Cdd:cd05927 196 LL---LDDIKALKPTVFPGvprvlnriydkifnkvqakgplkrklFNFALNyklaelrsgVVRASPFWDKLVFNkikqal 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 334 --ELRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETSpvlCSNTVTEEG-NRVGTIGIPWPSTYMKC--VTEDGTEA 408
Cdd:cd05927 273 ggNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECT---AGATLTLPGdTSVGHVGGPLPCAEVKLvdVPEMNYDA 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 409 ALGEP-GEIWAKGPQVFGGYYNRPDESAKVL-EDGWFKTGDIGVMTADGYFKIVDRKKDMI-LVSGFNVYPNEIEEVVSQ 485
Cdd:cd05927 350 KDPNPrGEVCIRGPNVFSGYYKDPEKTAEALdEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIENIYAR 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 486 CPGV---------LEVACVG--VPN---------EKSGETVKIFVVKKDEALTE---DSITRYCREN-LTAYKVPKHIEF 541
Cdd:cd05927 430 SPFVaqifvygdsLKSFLVAivVPDpdvlkewaaSKGGGTGSFEELCKNPEVKKailEDLVRLGKENgLKGFEQVKAIHL 509
|
....
gi 518832993 542 RTEL 545
Cdd:cd05927 510 EPEP 513
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
56-556 |
4.13e-47 |
|
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: 172.81 E-value: 4.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 56 ITFSELDTLSQQFASFLQNDLKlqKGDRIAIQMPNLLQYPIAMFGALRAGLTVVntnPLYTPREMQHqfndsgakaivil 135
Cdd:cd05931 25 LTYAELDRRARAIAARLQAVGK--PGDRVLLLAPPGLDFVAAFLGCLYAGAIAV---PLPPPTPGRH------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 136 anfAGNLEKILSQTAIEHVIVTqiGDLLGFPKKLIVNavvkyvkkmvPAYHLPGAISFGDALSRGSRQPLKPVAIKNTDL 215
Cdd:cd05931 87 ---AERLAAILADAGPRVVLTT--AAALAAVRAFAAS----------RPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 216 AFVQYTGGTTGVSKGAALTHRNIISNVicqdEWMKPAGVPDGQGIIVAALPLYHVYALTTNALASLKSGSMNLLITnPRd 295
Cdd:cd05931 152 AYLQYTSGSTGTPKGVVVTHRNLLANV----RQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMS-PA- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 296 lnAFIDD-------LKKYKIT-------AF-----------------TGLNTLYNGllNHP-RINEVD-FSE------LR 336
Cdd:cd05931 226 --AFLRRplrwlrlISRYRATisaapnfAYdlcvrrvrdedlegldlSSWRVALNG--AEPvRPATLRrFAEafapfgFR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 337 ---ITSAGGMAlQTSVAdrwqkLTGNKPAEGYGLSETSPVLCSNTV------TEEGNRVGTIGIPWPSTYMKCV-TEDGT 406
Cdd:cd05931 302 peaFRPSYGLA-EATLF-----VSGGPPGTGPVVLRVDRDALAGRAvavaadDPAARELVSCGRPLPDQEVRIVdPETGR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 407 EAALGEPGEIWAKGPQVFGGYYNRPDESAKVL-------EDGWFKTGDIGVMtADGYFKIVDRKKDMILVSGFNVYPNEI 479
Cdd:cd05931 376 ELPDGEVGEIWVRGPSVASGYWGRPEATAETFgalaatdEGGWLRTGDLGFL-HDGELYITGRLKDLIIVRGRNHYPQDI 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 480 EEVVSQCPGVLE---VACVGVPNEKSGETVKIFVVKKD-EALTEDSITRYCRENL-TAYKVPKH----IEFRTeLPKSNV 550
Cdd:cd05931 455 EATAEEAHPALRpgcVAAFSVPDDGEERLVVVAEVERGaDPADLAAIAAAIRAAVaREHGVAPAdvvlVRPGS-IPRTSS 533
|
....*.
gi 518832993 551 GKILRR 556
Cdd:cd05931 534 GKIQRR 539
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
220-547 |
7.64e-47 |
|
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: 167.09 E-value: 7.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 220 YTGGTTGVSKGAALTHRNIISnvicQDEWMKPAGVPDGQGIIVAALPLYHVYALTTnALASLKSGSMNLLI--TNPRDLN 297
Cdd:cd17636 7 YTAAFSGRPNGALLSHQALLA----QALVLAVLQAIDEGTVFLNSGPLFHIGTLMF-TLATFHAGGTNVFVrrVDAEEVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 298 AFIDDLKkykitaftglntLYNGLLNHPRINEV---------DFSELRITSAggMALQTSVADRWQKLTGNKPAeGYGLS 368
Cdd:cd17636 82 ELIEAER------------CTHAFLLPPTIDQIvelnadglyDLSSLRSSPA--APEWNDMATVDTSPWGRKPG-GYGQT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 369 ETSPVLCSNTVTEEGnrVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRPDESAKVLEDGWFKTGDI 448
Cdd:cd17636 147 EVMGLATFAALGGGA--IGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRGGWHHTNDL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 449 GVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVK-IFVVKKDEALTEDSITRYCR 527
Cdd:cd17636 225 GRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKaIVVLKPGASVTEAELIEHCR 304
|
330 340
....*....|....*....|
gi 518832993 528 ENLTAYKVPKHIEFRTELPK 547
Cdd:cd17636 305 ARIASYKKPKSVEFADALPR 324
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
214-560 |
7.38e-46 |
|
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: 164.04 E-value: 7.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 214 DLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMKPagvpDGQGIIVAALPLYHVYALTTnALASLKSGSMnLLITNP 293
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGF----GGGDSWLLSLPLYHVGGLAI-LVRSLLAGAE-LVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 294 RDLNAfiDDLKKYKITaFTGL--NTLYNGLLNHPRINEVDfsELRITSAGGMALQTSVADRWQKLtGNKPAEGYGLSETS 371
Cdd:cd17630 75 NQALA--EDLAPPGVT-HVSLvpTQLQRLLDSGQGPAALK--SLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTETA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 372 PVLCSNTVTEEGNrvGTIGIPWPstymkcvtedGTEAALGEPGEIWAKGPQVFGGYYNRPDESAkVLEDGWFKTGDIGVM 451
Cdd:cd17630 149 SQVATKRPDGFGR--GGVGVLLP----------GRELRIVEDGEIWVGGASLAMGYLRGQLVPE-FNEDGWFTTKDLGEL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 452 TADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVkIFVVKKDEALTEDSITRYCRENLT 531
Cdd:cd17630 216 HADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRP-VAVIVGRGPADPAELRAWLKDKLA 294
|
330 340
....*....|....*....|....*....
gi 518832993 532 AYKVPKHIEFRTELPKSNVGKILRRPLRE 560
Cdd:cd17630 295 RFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
57-495 |
1.71e-45 |
|
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: 165.52 E-value: 1.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 57 TFSELDTLSQQFASFLQNDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIVILA 136
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 137 NFAGNLekilSQTAIEHVIVTQigdllgfpkklivnavvkyvkkmvpayhlpgaiSFGDALSRGSRQPLKPVAIKNTDLA 216
Cdd:TIGR01733 81 ALASRL----AGLVLPVILLDP---------------------------------LELAALDDAPAPPPPDAPSGPDDLA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 217 FVQYTGGTTGVSKGAALTHRNIISNVicqdEWMKPAgVPDGQGIIVAALPLYHVYALTTNALASLKSGsMNLLITNPRDL 296
Cdd:TIGR01733 124 YVIYTSGSTGRPKGVVVTHRSLVNLL----AWLARR-YGLDPDDRVLQFASLSFDASVEEIFGALLAG-ATLVVPPEDEE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 297 NAFIDDL----KKYKITAFTGLNTLYNGLLNHPRInevDFSELRITSAGGMALQTSVADRWQKLTGNKP-AEGYGLSETS 371
Cdd:TIGR01733 198 RDDAALLaaliAEHPVTVLNLTPSLLALLAAALPP---ALASLRLVILGGEALTPALVDRWRARGPGARlINLYGPTETT 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 372 PVLCSNTVTEEGNRVG---TIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRPDESAKVL---------E 439
Cdd:TIGR01733 275 VWSTATLVDPDDAPREspvPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFvpdpfaggdG 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 518832993 440 DGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVlEVACV 495
Cdd:TIGR01733 355 ARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGV-REAVV 409
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
55-561 |
2.69e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 167.82 E-value: 2.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 55 QITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNL-----LQYPIAMFGAlragltVVNT-NPLYTPREMQHQFNDSG 128
Cdd:PRK08162 43 RRTWAETYARCRRLASALAR-RGIGRGDTVAVLLPNIpamveAHFGVPMAGA------VLNTlNTRLDAASIAFMLRHGE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 129 AKAIVILANFAGnlekiLSQTAIEhvivtqigdLLGFPKKLivnaVVKYVKKMVPAYHLPGAISFGDALSRG--SRQPLK 206
Cdd:PRK08162 116 AKVLIVDTEFAE-----VAREALA---------LLPGPKPL----VIDVDDPEYPGGRFIGALDYEAFLASGdpDFAWTL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 207 PV----AIKntdlafVQYTGGTTGVSKGAALTHR----NIISNVIcqdEW-MKPAGVpdgqgiIVAALPLYHV----YAL 273
Cdd:PRK08162 178 PAdewdAIA------LNYTSGTTGNPKGVVYHHRgaylNALSNIL---AWgMPKHPV------YLWTLPMFHCngwcFPW 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 274 TTNALAslksGSMNLLitnpRDLNA--FIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFS-ELRITSAGG---MALQT 347
Cdd:PRK08162 243 TVAARA----GTNVCL----RKVDPklIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDhPVHAMVAGAappAAVIA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 348 SVADRWQKLTgnkpaEGYGLSET-SPV-LCSN-------TVTEEGNRVGTIGIPWP---------STYMKCVTEDGTEAa 409
Cdd:PRK08162 315 KMEEIGFDLT-----HVYGLTETyGPAtVCAWqpewdalPLDERAQLKARQGVRYPlqegvtvldPDTMQPVPADGETI- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 410 lgepGEIWAKGPQVFGGYYNRPDESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGV 489
Cdd:PRK08162 389 ----GEIMFRGNIVMKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAV 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518832993 490 LEVACVGVPNEKSGETVKIFVVKKDEA-LTEDSITRYCRENLTAYKVPKHIEFrTELPKSNVGKILRRPLREE 561
Cdd:PRK08162 465 LVAAVVAKPDPKWGEVPCAFVELKDGAsATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQ 536
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
21-566 |
4.55e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 161.45 E-value: 4.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 21 PHDINPDSyTSLAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFG 100
Cdd:PRK06164 2 PHDAAPRA-DTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLA-AQGVRRGDRVAVWLPNCIEWVVLFLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 101 ALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIVILANFAG-NLEKILSQTAIEhvivtqigDLLGFPKKlivnAVVKYVK 179
Cdd:PRK06164 80 CARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPGFKGiDFAAILAAVPPD--------ALPPLRAI----AVVDDAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 180 KMVPAyHLPGAISFGDAL-SRGSRQPLKPVAIKNTDLAFVQYTGGTTGVSK------GAALTHRNIISNVIcqdewmkpa 252
Cdd:PRK06164 148 DATPA-PAPGARVQLFALpDPAPPAAAGERAADPDAGALLFTTSGTTSGPKlvlhrqATLLRHARAIARAY--------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 253 GVPDGQgIIVAALPLYHVYALTTnALASLKSGS---MNLLITNPRDLNAfiddLKKYKITAFTGLNTLYNGLLNHPRiNE 329
Cdd:PRK06164 218 GYDPGA-VLLAALPFCGVFGFST-LLGALAGGAplvCEPVFDAARTARA----LRRHRVTHTFGNDEMLRRILDTAG-ER 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 330 VDFSELRITsagGMAlqtSVADRWQKLTGNKPAEG------YGLSET-SPVLCSNTVTEEGNRVGTIGIP-WPSTYMKCV 401
Cdd:PRK06164 291 ADFPSARLF---GFA---SFAPALGELAALARARGvpltglYGSSEVqALVALQPATDPVSVRIEGGGRPaSPEARVRAR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 402 -TEDGTEAALGEPGEIWAKGPQVFGGYYNRPDESAKVL-EDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEI 479
Cdd:PRK06164 365 dPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALtDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEI 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 480 EEVVSQCPGVLEVACVGVpnEKSGETVKI-FVVKKD-EALTEDSITRYCRENLTAYKVPKHIEFRTELP---KSNVGKIL 554
Cdd:PRK06164 445 EHALEALPGVAAAQVVGA--TRDGKTVPVaFVIPTDgASPDEAGLMAACREALAGFKVPARVQVVEAFPvteSANGAKIQ 522
|
570
....*....|..
gi 518832993 555 RRPLREEELAKL 566
Cdd:PRK06164 523 KHRLREMAQARL 534
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
57-563 |
7.77e-43 |
|
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: 158.82 E-value: 7.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 57 TFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVntnPLYT---PREMQHQFNDSGAKAIV 133
Cdd:cd05969 2 TFAQLKVLSARFANVLK-SLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVIC---PLFSafgPEAIRDRLENSEAKVLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 134 ILanfagnlEKILSQTAIEhvivtqigdllgfpkklivnavvkyvkkmvpayhlpgaisfgdalsrgsrqplkpvaiknt 213
Cdd:cd05969 78 TT-------EELYERTDPE------------------------------------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 214 DLAFVQYTGGTTGVSKGAALTHRNIISnvicqdEWMKPAGVPD--GQGII-VAALPLY---HVYALttnaLASLKSGSMN 287
Cdd:cd05969 90 DPTLLHYTSGTTGTPKGVLHVHDAMIF------YYFTGKYVLDlhPDDIYwCTADPGWvtgTVYGI----WAPWLNGVTN 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 288 LLITNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNH--PRINEVDFSELRITSAGGMALQTSVAdRWQKLTGNKPA-EG 364
Cdd:cd05969 160 VVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEgdELARKYDLSSLRFIHSVGEPLNPEAI-RWGMEVFGVPIhDT 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 365 YGLSETSPVLCSNTVTEEGnRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKG--PQVFGGYYNRPDESAKVLEDGW 442
Cdd:cd05969 239 WWQTETGSIMIANYPCMPI-KPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSFIDGW 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 443 FKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKD-----EAL 517
Cdd:cd05969 318 YLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEgfepsDEL 397
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 518832993 518 TEDSITrYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREEEL 563
Cdd:cd05969 398 KEEIIN-FVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKEL 442
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
54-568 |
1.03e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 156.86 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 54 KQITFSELDTLSQQFASFLQNDLKLQKgdRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIV 133
Cdd:PRK07638 25 RVLTYKDWFESVCKVANWLNEKESKNK--TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 134 ILANFAGNLEKilSQTAIehvivtqigdllgfpkkLIVNAVVKYVKKMVPAYHlpgaisfgdalsrgsrqplkpvAIKNT 213
Cdd:PRK07638 103 TERYKLNDLPD--EEGRV-----------------IEIDEWKRMIEKYLPTYA----------------------PIENV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 214 DLA--FVQYTGGTTGVSKGAALTHRNIISNVIC--QDEWMKPAG---VPdgqGIIVAALPLYhvyalttNALASLKSG-S 285
Cdd:PRK07638 142 QNApfYMGFTSGSTGKPKAFLRAQQSWLHSFDCnvHDFHMKREDsvlIA---GTLVHSLFLY-------GAISTLYVGqT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 286 MNLLIT-NPrdlNAFIDDLKKYKITAFTGLNTLYNGLLnhpRINEVDFSELRITSAGgmalqtsvADrW-----QKLTGN 359
Cdd:PRK07638 212 VHLMRKfIP---NQVLDKLETENISVMYTVPTMLESLY---KENRVIENKMKIISSG--------AK-WeaeakEKIKNI 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 360 KPA----EGYGLSETSPVlcSNTVTEEGNRVGT-IGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRPDES 434
Cdd:PRK07638 277 FPYaklyEFYGASELSFV--TALVDEESERRPNsVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 435 AKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGEtVKIFVVKKD 514
Cdd:PRK07638 355 RELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGE-KPVAIIKGS 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 518832993 515 EalTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLRE--EELAKLKK 568
Cdd:PRK07638 434 A--TKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSwiENQEKIYE 487
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
214-555 |
1.99e-41 |
|
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: 152.41 E-value: 1.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 214 DLAFVQYTGGTTGVSKGAALTHRniiSNVICQDEWMKPAGVPDGQGIIVAALPLYHVYALTTnALASLKSGSMNLLITNP 293
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANK---TFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWW-ILTCLIHGGLCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 294 RDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGG-MALQTSVAD-RWQKLTgnKPAEGYGLSETS 371
Cdd:cd17635 78 TTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGsRAIAADVRFiEATGLT--NTAQVYGLSETG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 372 PVLCSNTVTEEGNrVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRPDESAKVLEDGWFKTGDIGVM 451
Cdd:cd17635 156 TALCLPTDDDSIE-INAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGER 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 452 TADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKDEaLTEDSIT---RYCRE 528
Cdd:cd17635 235 REDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAE-LDENAIRalkHTIRR 313
|
330 340
....*....|....*....|....*..
gi 518832993 529 NLTAYKVPKHIEFRTELPKSNVGKILR 555
Cdd:cd17635 314 ELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
35-560 |
7.84e-41 |
|
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: 153.23 E-value: 7.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 35 LIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPL 114
Cdd:cd17653 2 AFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLL-QLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 115 YTPREMQHQFNDSGAKaiVILANFAGNlekilsqtaiehvivtqigdllgfpkklivnavvkyvkkmvpayhlpgaisfg 194
Cdd:cd17653 81 LPSARIQAILRTSGAT--LLLTTDSPD----------------------------------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 195 dalsrgsrqplkpvaikntDLAFVQYTGGTTGVSKGAALTHRNIISNVicqdeWMKPAGVPDGQGIIVAalplyHVYALT 274
Cdd:cd17653 106 -------------------DLAYIIFTSGSTGIPKGVMVPHRGVLNYV-----SQPPARLDVGPGSRVA-----QVLSIA 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 275 TNA-----LASLKSGSmNLLITNPRDlnAFIDDLKKYKITAFTG--LNTLyngllnhpriNEVDFSELRITSAGGMALQT 347
Cdd:cd17653 157 FDAcigeiFSTLCNGG-TLVLADPSD--PFAHVARTVDALMSTPsiLSTL----------SPQDFPNLKTIFLGGEAVPP 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 348 SVADRWQKltGNKPAEGYGLSETSpVLCSNTVTEEGNRVgTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGY 427
Cdd:cd17653 224 SLLDRWSP--GRRLYNAYGPTECT-ISSTMTELLPGQPV-TIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGY 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 428 YNRPDESA-KVLEDGW------FKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVpne 500
Cdd:cd17653 300 LGNPALTAsKFVPDPFwpgsrmYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIV--- 376
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 501 kSGETVKIFVVKkdEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLRE 560
Cdd:cd17653 377 -VNGRLVAFVTP--ETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
34-558 |
2.26e-40 |
|
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: 153.13 E-value: 2.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 34 ALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNP 113
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLR-AAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 114 LYTPREMQHQFNDSGAKAIVILANFAGNLEKilsqtaiehvivtqigdllgfpkklivnavvkyvkkmvpayhLPGAISF 193
Cdd:cd12117 80 ELPAERLAFMLADAGAKVLLTDRSLAGRAGG------------------------------------------LEVAVVI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 194 GDALSRGSRQPLkPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVicqdewMKPAGVPDGQGIIVAALPLYHVYAL 273
Cdd:cd12117 118 DEALDAGPAGNP-AVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLV------KNTNYVTLGPDDRVLQTSPLAFDAS 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 274 TTNALASLKSGSMNLLIT--NPRDLNAFIDDLKKYKITAFTGLNTLYNGLLN-HPRInevdFSELRITSAGGMALQTSVA 350
Cdd:cd12117 191 TFEIWGALLNGARLVLAPkgTLLDPDALGALIAEEGVTVLWLTAALFNQLADeDPEC----FAGLRELLTGGEVVSPPHV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 351 DRW-QKLTGNKPAEGYGLSETSPVLCSNTVTEEGNRVGTIGIPWPSTYMKC--VTEDGTEAALGEPGEIWAKGPQVFGGY 427
Cdd:cd12117 267 RRVlAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAGSIPIGRPIANTRVyvLDEDGRPVPPGVPGELYVGGDGLALGY 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 428 YNRPDESA-KVLEDGW------FKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNE 500
Cdd:cd12117 347 LNRPALTAeRFVADPFgpgerlYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDA 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 518832993 501 KSGETVKIFVVkKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPL 558
Cdd:cd12117 427 GGDKRLVAYVV-AEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
25-568 |
2.30e-40 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 154.62 E-value: 2.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 25 NPDSYTSLAAL--IEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLqNDLKLQKGDRIAIQMPNLLQYPIAMFGAL 102
Cdd:PLN02479 13 NAANYTALTPLwfLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASAL-AKRSIGPGSTVAVIAPNIPAMYEAHFGVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 103 RAGLTVVNTNPLYTPREMQHQFNDSGAKAIVILANFAGNLE---KILSQ---TAIEHVIVTQIGDLLGFPKKLivnavvk 176
Cdd:PLN02479 92 MAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQEFFTLAEealKILAEkkkSSFKPPLLIVIGDPTCDPKSL------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 177 yvkkmvpAYHLP-GAISFGDALSRGSRQ-PLKPVAIKNTDLAfVQYTGGTTGVSKGAALTHRNI----ISNVICqdeWmk 250
Cdd:PLN02479 165 -------QYALGkGAIEYEKFLETGDPEfAWKPPADEWQSIA-LGYTSGTTASPKGVVLHHRGAylmaLSNALI---W-- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 251 paGVPDGqGIIVAALPLYHVYALT-TNALASLKSGSMNLLITNPRdlnAFIDDLKKYKITAFTGLNTLYNGLLNHPRINE 329
Cdd:PLN02479 232 --GMNEG-AVYLWTLPMFHCNGWCfTWTLAALCGTNICLRQVTAK---AIYSAIANYGVTHFCAAPVVLNTIVNAPKSET 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 330 V-DFSELRITSAGGMALQTSVADRWQKLtGNKPAEGYGLSET----------------SPVLCSNTVTEEGNR-VGTIGI 391
Cdd:PLN02479 306 IlPLPRVVHVMTAGAAPPPSVLFAMSEK-GFRVTHTYGLSETygpstvcawkpewdslPPEEQARLNARQGVRyIGLEGL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 392 PWPSTY-MKCVTEDGTEAalgepGEIWAKGPQVFGGYYNRPDESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVS 470
Cdd:PLN02479 385 DVVDTKtMKPVPADGKTM-----GEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISG 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 471 GFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKK------DEALTEDSITRYCRENLTAYKVPKHIEFrTE 544
Cdd:PLN02479 460 GENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKpgvdksDEAALAEDIMKFCRERLPAYWVPKSVVF-GP 538
|
570 580
....*....|....*....|....*.
gi 518832993 545 LPKSNVGKILRRPLRE--EELAKLKK 568
Cdd:PLN02479 539 LPKTATGKIQKHVLRAkaKEMGPVKK 564
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
56-560 |
2.46e-39 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 151.06 E-value: 2.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 56 ITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIVIL 135
Cdd:PRK13382 69 LTWRELDERSDALAAALQA-LPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 136 ANFAGNLEKILSQTAIehviVTQIGDLLGFPKKLIVNAVVkyvkkmvpayhlpgaisfgdALSRGSRQPLKPVAIKNTDL 215
Cdd:PRK13382 148 EEFSATVDRALADCPQ----ATRIVAWTDEDHDLTVEVLI--------------------AAHAGQRPEPTGRKGRVILL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 216 afvqyTGGTTGVSKGA---ALTHRNIISNVICQDEWMkpAGVPdgqgiIVAALPLYHVYALTTNALASLKSGSMnllITN 292
Cdd:PRK13382 204 -----TSGTTGTPKGArrsGPGGIGTLKAILDRTPWR--AEEP-----TVIVAPMFHAWGFSQLVLAASLACTI---VTR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 293 PR-DLNAFIDDLKKYKITAFTGLNTLYNGLLNHPR--INEVDFSELRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSE 369
Cdd:PRK13382 269 RRfDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAevRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 370 TSPVlcsNTVTEEGNRVG--TIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNrpdESAKVLEDGWFKTGD 447
Cdd:PRK13382 349 AGMI---ATATPADLRAApdTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTS---GSTKDFHDGFMASGD 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 448 IGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKDEA-LTEDSITRYC 526
Cdd:PRK13382 423 VGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGAsATPETLKQHV 502
|
490 500 510
....*....|....*....|....*....|....
gi 518832993 527 RENLTAYKVPKHIEFRTELPKSNVGKILRRPLRE 560
Cdd:PRK13382 503 RDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
55-563 |
6.82e-39 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 150.05 E-value: 6.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 55 QITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGlTVVNtnPLYT---PREMQHQFNDSGAKA 131
Cdd:PRK04319 73 KYTYKELKELSNKFANVLK-ELGVEKGDRVFIFMPRIPELYFALLGALKNG-AIVG--PLFEafmEEAVRDRLEDSEAKV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 132 IVILANFagnLEKILSQ--TAIEHVivtqigdllgfpkkLIVNAVVKYVkkmvpayhlPGAISFGDALSRGSRQpLKPVA 209
Cdd:PRK04319 149 LITTPAL---LERKPADdlPSLKHV--------------LLVGEDVEEG---------PGTLDFNALMEQASDE-FDIEW 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 210 IKNTDLAFVQYTGGTTGVSKG------AALTHRniISNVICQDewMKPAGV------P-----DGQGIIVaalPLYHvya 272
Cdd:PRK04319 202 TDREDGAILHYTSGSTGKPKGvlhvhnAMLQHY--QTGKYVLD--LHEDDVywctadPgwvtgTSYGIFA---PWLN--- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 273 lttnalaslksGSMNLLITNPRDLNAFIDDLKKYKI----TAFTGLNTLYNGLLNHprINEVDFSELR-ITSAGgMALQT 347
Cdd:PRK04319 272 -----------GATNVIDGGRFSPERWYRILEDYKVtvwyTAPTAIRMLMGAGDDL--VKKYDLSSLRhILSVG-EPLNP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 348 SVAdRW-QKLTGNKPAEGYGLSETSPVLCSNTVTEEgNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEI-----WakgP 421
Cdd:PRK04319 338 EVV-RWgMKVFGLPIHDNWWMTETGGIMIANYPAMD-IKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLaikkgW---P 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 422 QVFGGYYNRPDESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEK 501
Cdd:PRK04319 413 SMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPV 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518832993 502 SGETVKIFVVKK-----DEALTEDsITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREEEL 563
Cdd:PRK04319 493 RGEIIKAFVALRpgyepSEELKEE-IRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAWEL 558
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
56-568 |
1.09e-38 |
|
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: 149.35 E-value: 1.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 56 ITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQfndsgakaivil 135
Cdd:cd05906 40 QSYQDLLEDARRLAAGLRQ-LGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPNAR------------ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 136 anfagnLEKILsqtaiehvivtQIGDLLGFPKKLIVNAVVKYVKKMVPAYHLPG-AISFGDALSRGSRQPLKPVAiKNTD 214
Cdd:cd05906 107 ------LRKLR-----------HIWQLLGSPVVLTDAELVAEFAGLETLSGLPGiRVLSIEELLDTAADHDLPQS-RPDD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 215 LAFVQYTGGTTGVSKGAALTHRNIISNVICQdEWMKPAGVPDgqgIIVAALPLYHVYALTTNALASLKSGS------MNL 288
Cdd:cd05906 169 LALLMLTSGSTGFPKAVPLTHRNILARSAGK-IQHNGLTPQD---VFLNWVPLDHVGGLVELHLRAVYLGCqqvhvpTEE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 289 LITNPRDlnaFIDDLKKYKITAFTGLNTLYNGLLNHPRINEV---DFSELRITSAGGMALQTSVADRWQKLTG------N 359
Cdd:cd05906 245 ILADPLR---WLDLIDRYRVTITWAPNFAFALLNDLLEEIEDgtwDLSSLRYLVNAGEAVVAKTIRRLLRLLEpyglppD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 360 KPAEGYGLSETSPVLCSNTVTEEGNRVGT-----IGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRPDES 434
Cdd:cd05906 322 AIRPAFGMTETCSGVIYSRSFPTYDHSQAlefvsLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEAN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 435 AKVL-EDGWFKTGDIGVMTaDGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLE--VACVGVPNEKSG-ETVKIFV 510
Cdd:cd05906 402 AEAFtEDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVRDPGAEtEELAIFF 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518832993 511 V---KKDEALTE--DSITRYCRENLT---AYKVPkhIEfRTELPKSNVGKILRrplreeelAKLKK 568
Cdd:cd05906 481 VpeyDLQDALSEtlRAIRSVVSREVGvspAYLIP--LP-KEEIPKTSLGKIQR--------SKLKA 535
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
24-536 |
2.64e-38 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 148.87 E-value: 2.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 24 INPDSYTSLAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALR 103
Cdd:PRK08279 31 ITPDSKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAA-ARGVGKGDVVALLMENRPEYLAAWLGLAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 104 AGLTV--VNTN----PLytpremQHQFNDSGAKAIVILANFAGNLEKILSQTAIEHVIVTQIGDLLGFPkklivnavvky 177
Cdd:PRK08279 110 LGAVValLNTQqrgaVL------AHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDDP----------- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 178 vkkmvpayhlPGAISFgDALSRGSRQPLKPV--AIKNTDLAFVQYTGGTTGVSKGAALTHRniisnvicqdEWMKPAGvp 255
Cdd:PRK08279 173 ----------EGYEDL-AAAAAGAPTTNPASrsGVTAKDTAFYIYTSGTTGLPKAAVMSHM----------RWLKAMG-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 256 dGQGIIVAA---------LPLYHVYALTTnALASLKSGSMNLLITNPRDLNAFIDDLKKYKITAFTglntlYNG-----L 321
Cdd:PRK08279 230 -GFGGLLRLtpddvlyccLPLYHNTGGTV-AWSSVLAAGATLALRRKFSASRFWDDVRRYRATAFQ-----YIGelcryL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 322 LNHP-----RINevdfselRITSAGGMALQTSVADRWQKLTG-NKPAEGYGLSEtspvlcSNTV-TEEGNRVGTIGI--P 392
Cdd:PRK08279 303 LNQPpkptdRDH-------RLRLMIGNGLRPDIWDEFQQRFGiPRILEFYAASE------GNVGfINVFNFDGTVGRvpL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 393 WPSTYMKCV-----------TEDG--TEAALGEPGE----IWAKGPqvFGGYyNRPDESAK-----VLEDG--WFKTGDi 448
Cdd:PRK08279 370 WLAHPYAIVkydvdtgepvrDADGrcIKVKPGEVGLligrITDRGP--FDGY-TDPEASEKkilrdVFKKGdaWFNTGD- 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 449 gVMTAD--GYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVP----NEKSGeTVKIfVVKKDEALTEDSI 522
Cdd:PRK08279 446 -LMRDDgfGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVEvpgtDGRAG-MAAI-VLADGAEFDLAAL 522
|
570
....*....|....
gi 518832993 523 TRYCRENLTAYKVP 536
Cdd:PRK08279 523 AAHLYERLPAYAVP 536
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
31-565 |
5.57e-38 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 149.03 E-value: 5.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 31 SLAALIEEGVKR--FSSAPAYACmGKQITFSELDTLSQQFASFLQNDlKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTV 108
Cdd:PRK06060 5 NLAGLLAEQASEagWYDRPAFYA-ADVVTHGQIHDGAARLGEVLRNR-GLSSGDRVLLCLPDSPDLVQLLLACLARGVMA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 109 VNTNPLYTPREMQHQFNDSGAkAIVILAnfaGNL-EKILSQTAIEhvivtqigdllgfPKKLIVNAVvkyvkKMVPAYHL 187
Cdd:PRK06060 83 FLANPELHRDDHALAARNTEP-ALVVTS---DALrDRFQPSRVAE-------------AAELMSEAA-----RVAPGGYE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 188 PGAisfGDALsrgsrqplkpvaikntdlAFVQYTGGTTGVSKGAALTHRNIISNV---ICQDEWMKPagvpdgQGIIVAA 264
Cdd:PRK06060 141 PMG---GDAL------------------AYATYTSGTTGPPKAAIHRHADPLTFVdamCRKALRLTP------EDTGLCS 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 265 LPLYHVYALTTNALASLKSGSMNLLITNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEvdFSELRITSAGGMA 344
Cdd:PRK06060 194 ARMYFAYGLGNSVWFPLATGGSAVINSAPVTPEAAAILSARFGPSVLYGVPNFFARVIDSCSPDS--FRSLRCVVSAGEA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 345 LQTSVADRWQKLTGNKPA-EGYGLSETSPVLCSNTVTEEgnRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQV 423
Cdd:PRK06060 272 LELGLAERLMEFFGGIPIlDGIGSTEVGQTFVSNRVDEW--RLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAI 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 424 FGGYYNRPDesaKVLED-GWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKS 502
Cdd:PRK06060 350 AKGYWNRPD---SPVANeGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTG 426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518832993 503 GETVKIFVVKKDEALTEDSITRYCRE----NLTAYKVPKHIEFRTELPKSNVGKILRRPLREEELAK 565
Cdd:PRK06060 427 ASTLQAFLVATSGATIDGSVMRDLHRgllnRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQSPTK 493
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
35-562 |
2.53e-37 |
|
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: 144.39 E-value: 2.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 35 LIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQndlklQKG---DRI-AIQMPNLLQYPIAMFGALRAGLTVVN 110
Cdd:cd17655 2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLR-----EKGvgpDTIvGIMAERSLEMIVGILGILKAGGAYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 111 TNPLYTPREMQHQFNDSGAKAIVILANFAGNLEKIlsqtaiEHVIVTQIGDLlgfpkklivnavvkyvkkmvpaYHlpga 190
Cdd:cd17655 77 IDPDYPEERIQYILEDSGADILLTQSHLQPPIAFI------GLIDLLDEDTI----------------------YH---- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 191 isfgdalsrGSRQPLKPVaIKNTDLAFVQYTGGTTGVSKGAALTHRNiISNVIcqdEWMKPAgVPDGQGIIVAALPLYHV 270
Cdd:cd17655 125 ---------EESENLEPV-SKSDDLAYVIYTSGSTGKPKGVMIEHRG-VVNLV---EWANKV-IYQGEHLRVALFASISF 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 271 YALTTNALASLKSGsmNLLITNPR----DLNAFIDDLKKYKITAFTGLNTLYNgLLNHPRINEvdFSELRITSAGGMALQ 346
Cdd:cd17655 190 DASVTEIFASLLSG--NTLYIVRKetvlDGQALTQYIRQNRITIIDLTPAHLK-LLDAADDSE--GLSLKHLIVGGEALS 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 347 TSVADRWQKLTGNKPA--EGYGLSETSpVLCSNTVTEEGNRVGT---IGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGP 421
Cdd:cd17655 265 TELAKKIIELFGTNPTitNAYGPTETT-VDASIYQYEPETDQQVsvpIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGE 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 422 QVFGGYYNRPD-ESAKVLEDGW------FKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVAC 494
Cdd:cd17655 344 GVARGYLNRPElTAEKFVDDPFvpgermYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVV 423
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518832993 495 VGVPNEKSGETVKIFVVKKDEALTEDSITRYCREnLTAYKVPKHIEFRTELPKSNVGKILRRPLREEE 562
Cdd:cd17655 424 IARKDEQGQNYLCAYIVSEKELPVAQLREFLARE-LPDYMIPSYFIKLDEIPLTPNGKVDRKALPEPD 490
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
53-559 |
1.59e-36 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 142.45 E-value: 1.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 53 GKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAI 132
Cdd:PRK13390 22 GEQVSYRQLDDDSAALARVLY-DAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 133 VilanfagnlekilSQTAIEHVIVTQIGDLlgfPKKLIVNAvvkyvkkmvpayHLPGAISFGDALS-RGSRQPLKPVAik 211
Cdd:PRK13390 101 V-------------ASAALDGLAAKVGADL---PLRLSFGG------------EIDGFGSFEAALAgAGPRLTEQPCG-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 212 ntdlAFVQYTGGTTGVSKGAA--LTHRNIISNvicQDEWMKPAGVPDG---QGIIVAALPLYHVYALTTNALASLKSGSm 286
Cdd:PRK13390 151 ----AVMLYSSGTTGFPKGIQpdLPGRDVDAP---GDPIVAIARAFYDiseSDIYYSSAPIYHAAPLRWCSMVHALGGT- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 287 nLLITNPRDLNAFIDDLKKYKITAFTGLNTLYNGLL--NHPRINEVDFSELRITSAGGMALQTSVADRWQKLTGNKPAEG 364
Cdd:PRK13390 223 -VVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLklDADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 365 YGLSETSPVlcsnTVTEEGNRV---GTIGIPWPSTYMKCvTEDGTEAALGEPGEIWAKGPQVFGGYYNRPDESAKVLEDG 441
Cdd:PRK13390 302 YSSTEAHGM----TFIDSPDWLahpGSVGRSVLGDLHIC-DDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 442 ---WFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFV-----VKK 513
Cdd:PRK13390 377 hpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIqlvegIRG 456
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 518832993 514 DEALTEDSITrYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLR 559
Cdd:PRK13390 457 SDELARELID-YTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
44-559 |
3.34e-36 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 142.05 E-value: 3.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 44 SSAPAYACMGKQITFSELDTLSQQFASFLQNDlKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTnpLYTpremqHQ 123
Cdd:PRK10946 37 SDAIAVICGERQFSYRELNQASDNLACSLRRQ-GIKPGDTALVQLGNVAEFYITFFALLKLGVAPVNA--LFS-----HQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 124 FNDSGAKA------IVILAN----FAGN--LEKILSQ-TAIEHVIVtqigdllgfpkklivnavvkyvkkmvpaYHLPGA 190
Cdd:PRK10946 109 RSELNAYAsqiepaLLIADRqhalFSDDdfLNTLVAEhSSLRVVLL----------------------------LNDDGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 191 ISFGDALSRGSrQPLKPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNII-----SNVICQdewmkpagvPDGQGIIVAAL 265
Cdd:PRK10946 161 HSLDDAINHPA-EDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYYysvrrSVEICG---------FTPQTRYLCAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 266 PLYHVYALTT-NALASLKSGSMNLLITNPRDLNAFiDDLKKYKITAfTGL----NTLYNGLLNHPRINEvDFSELRITSA 340
Cdd:PRK10946 231 PAAHNYPMSSpGALGVFLAGGTVVLAPDPSATLCF-PLIEKHQVNV-TALvppaVSLWLQAIAEGGSRA-QLASLKLLQV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 341 GGMALQTSVADRWQKLTGNKPAEGYGLSETspvLCSNTVTEEGNRV--GTIGIPW-PSTYMKCVTEDGTEAALGEPGEIW 417
Cdd:PRK10946 308 GGARLSETLARRIPAELGCQLQQVFGMAEG---LVNYTRLDDSDERifTTQGRPMsPDDEVWVADADGNPLPQGEVGRLM 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 418 AKGPQVFGGYYNRPDESAKVL-EDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVG 496
Cdd:PRK10946 385 TRGPYTFRGYYKSPQHNASAFdANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVS 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518832993 497 VPNEKSGETVKIFVVKKdEALTEDSITRYCRENLTA-YKVPKHIEFRTELPKSNVGKILRRPLR 559
Cdd:PRK10946 465 MEDELMGEKSCAFLVVK-EPLKAVQLRRFLREQGIAeFKLPDRVECVDSLPLTAVGKVDKKQLR 527
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
15-491 |
3.43e-36 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 143.32 E-value: 3.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 15 HYPPgvphdiNPDSYTsLAALIEEGVKRFSSapaYACMGKQI------------TFSELDTLSQQFASFLQNdLKLQKGD 82
Cdd:PLN02736 36 RFPD------HPEIGT-LHDNFVYAVETFRD---YKYLGTRIrvdgtvgeykwmTYGEAGTARTAIGSGLVQ-HGIPKGA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 83 RIAIQMPNLLQYPIAMFGALRAGLTVVntnPLYtpremqhqfnDS-GAKAIVILANFAgNLEKILSQTAIEHVIVTQIGD 161
Cdd:PLN02736 105 CVGLYFINRPEWLIVDHACSAYSYVSV---PLY----------DTlGPDAVKFIVNHA-EVAAIFCVPQTLNTLLSCLSE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 162 LLGFpkKLIVnaVVKYVKKMVPAyhLPGA-----ISFGDALSRGSRQPLKPVAIKNTDLAFVQYTGGTTGVSKGAALTHR 236
Cdd:PLN02736 171 IPSV--RLIV--VVGGADEPLPS--LPSGtgveiVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 237 NIISNV--ICQDEWMKPAGVpdgqgiIVAALPLYHVYAlTTNALASLKSGSMNLLITNprDLNAFIDDLKKYKITAFTGL 314
Cdd:PLN02736 245 NLIANVagSSLSTKFYPSDV------HISYLPLAHIYE-RVNQIVMLHYGVAVGFYQG--DNLKLMDDLAALRPTIFCSV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 315 NTLYN------------------------------GLLN----HPRINEVDFS--------ELRITSAGGMALQTSVADR 352
Cdd:PLN02736 316 PRLYNriydgitnavkesgglkerlfnaaynakkqALENgknpSPMWDRLVFNkikaklggRVRFMSSGASPLSPDVMEF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 353 WQKLTGNKPAEGYGLSETSpvlCSNTVTEEGNR-VGTIGIPWPSTYMKCV--------TEDgteaalgEP---GEIWAKG 420
Cdd:PLN02736 396 LRICFGGRVLEGYGMTETS---CVISGMDEGDNlSGHVGSPNPACEVKLVdvpemnytSED-------QPyprGEICVRG 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518832993 421 PQVFGGYYNRPDESAKVL-EDGWFKTGDIGVMTADGYFKIVDRKKDMI-LVSGFNVYPNEIEEVVSQCPGVLE 491
Cdd:PLN02736 466 PIIFKGYYKDEVQTREVIdEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYAKCKFVAQ 538
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
211-561 |
1.01e-35 |
|
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: 139.93 E-value: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 211 KNTD-LAFVQYTGGTTGVSKGAALTHRNIISNVIC---QDEWmkpagvpDGQGIIVAALPLYHVYALTTNALASLKSGSM 286
Cdd:cd05908 103 ELADeLAFIQFSSGSTGDPKGVMLTHENLVHNMFAilnSTEW-------KTKDRILSWMPLTHDMGLIAFHLAPLIAGMN 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 287 NLLITNPRDLNAFIDDLKK---YKITAFTGLNTLYNGLL---NHPRINEVDFSELRITSAGGMALQTSVADRW------Q 354
Cdd:cd05908 176 QYLMPTRLFIRRPILWLKKaseHKATIVSSPNFGYKYFLktlKPEKANDWDLSSIRMILNGAEPIDYELCHEFldhmskY 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 355 KLTGNKPAEGYGLSE-----TSPVLCSNTVT---------------------EEGNRVGTIGIPWPSTYMKCVTEDGTEA 408
Cdd:cd05908 256 GLKRNAILPVYGLAEasvgaSLPKAQSPFKTitlgrrhvthgepepevdkkdSECLTFVEVGKPIDETDIRICDEDNKIL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 409 ALGEPGEIWAKGPQVFGGYYNRPDESAKVL-EDGWFKTGDIGVMTaDGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCP 487
Cdd:cd05908 336 PDGYIGHIQIRGKNVTPGYYNNPEATAKVFtDDGWLKTGDLGFIR-NGRLVITGREKDIIFVNGQNVYPHDIERIAEELE 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 488 GVL--EVACVGVPNEKS-GETVKIFVVKKDealTEDSITRYcrenltAYKVPKHIEFRT-----------ELPKSNVGKI 553
Cdd:cd05908 415 GVElgRVVACGVNNSNTrNEEIFCFIEHRK---SEDDFYPL------GKKIKKHLNKRGgwqinevlpirRIPKTTSGKV 485
|
....*...
gi 518832993 554 LRRPLREE 561
Cdd:cd05908 486 KRYELAQR 493
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
45-558 |
1.06e-35 |
|
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: 139.35 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 45 SAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYtPRE-MQHQ 123
Cdd:cd12116 2 DATAVRDDDRSLSYAELDERANRLAARLR-ARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDY-PADrLRYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 124 FNDSGAKAIVIlanfagnlekilsQTAIEHvivtqigdllgfpkKLIVNAVVkyVKKMVPAYHLPGAisfgdalsrGSRQ 203
Cdd:cd12116 80 LEDAEPALVLT-------------DDALPD--------------RLPAGLPV--LLLALAAAAAAPA---------APRT 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 204 PLKPvaiknTDLAFVQYTGGTTGVSKGAALTHRNIISNVIC--QDEWMKPAGvpdgqgiivaalplyHVYALTTNA---- 277
Cdd:cd12116 122 PVSP-----DDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSmrERLGLGPGD---------------RLLAVTTYAfdis 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 278 -----LASLKSGSMNLL----ITNPRDLNAFIDDlkkYKITAFTGLNTLYNGLLnhprinEVDFSELRITSA--GGMALQ 346
Cdd:cd12116 182 llellLPLLAGARVVIApretQRDPEALARLIEA---HSITVMQATPATWRMLL------DAGWQGRAGLTAlcGGEALP 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 347 TSVADRWQKLTG---NKpaegYGLSETSpVLCSNTVTEEGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQV 423
Cdd:cd12116 253 PDLAARLLSRVGslwNL----YGPTETT-IWSTAARVTAAAGPIPIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGV 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 424 FGGYYNRPDESAKVLEDG--------WFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACV 495
Cdd:cd12116 328 AQGYLGRPALTAERFVPDpfagpgsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVV 407
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518832993 496 GVPNEKSGETVKIFVVKKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPL 558
Cdd:cd12116 408 VREDGGDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
46-558 |
1.37e-35 |
|
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: 138.98 E-value: 1.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 46 APAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFN 125
Cdd:cd17643 3 AVAVVDEDRRLTYGELDARANRLARTLR-AEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 126 DSGAKAIVILANfagnlekilsqtaiehvivtqigdllgfpkklivnavvkyvkkmvpayhlpgaisfgdalsrgsrqpl 205
Cdd:cd17643 82 DSGPSLLLTDPD-------------------------------------------------------------------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 206 kpvaikntDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMKPagvpDGQGIIVaalpLYHVYALTTN------ALA 279
Cdd:cd17643 94 --------DLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGF----NEDDVWT----LFHSYAFDFSvweiwgALL 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 280 SlksGSmNLLITNP---RDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSVADRWQKL 356
Cdd:cd17643 158 H---GG-RLVVVPYevaRSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGR 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 357 TGNKPAE---GYGLSETSpVLcsNTVTE------EGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGY 427
Cdd:cd17643 234 FGLDRPQlvnMYGITETT-VH--VTFRPldaadlPAAAASPIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGY 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 428 YNRPDESAKVLEDGWF--------KTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVAcVGVPN 499
Cdd:cd17643 311 LGRPELTAERFVANPFggpgsrmyRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAA-VIVRE 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518832993 500 EKSGETVKI-FVVKKDE-ALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPL 558
Cdd:cd17643 390 DEPGDTRLVaYVVADDGaAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
220-561 |
1.54e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 137.15 E-value: 1.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 220 YTGGTTGVSKGAALTHRNIISNVICqdewmkpAGVPDGQGI-----IVAALPLYHVyalttNALASLKSGSMN---LLIT 291
Cdd:PRK07008 183 YTSGTTGNPKGALYSHRSTVLHAYG-------AALPDAMGLsardaVLPVVPMFHV-----NAWGLPYSAPLTgakLVLP 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 292 NPR-DLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSET 370
Cdd:PRK07008 251 GPDlDGKSLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEM 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 371 SPV--LCS-------------NTVTEEGNRVgTIGIPwpstyMKCVTEDGTEAalgeP------GEIWAKGPQVFGGYYn 429
Cdd:PRK07008 331 SPLgtLCKlkwkhsqlpldeqRKLLEKQGRV-IYGVD-----MKIVGDDGREL----PwdgkafGDLQVRGPWVIDRYF- 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 430 RPDESAkvLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIF 509
Cdd:PRK07008 400 RGDASP--LVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLV 477
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 518832993 510 VVKKDEA-LTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREE 561
Cdd:PRK07008 478 VVKRPGAeVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQ 530
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
34-558 |
1.99e-34 |
|
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: 136.25 E-value: 1.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 34 ALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNP 113
Cdd:cd17646 2 ALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLR-ARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 114 LYTPREMQHQFNDSGAKaivilanfagnlekilsqtaiehVIVTQiGDLLGFPKKLIVNAVVKYVKKMVPAYHLPGAISF 193
Cdd:cd17646 81 GYPADRLAYMLADAGPA-----------------------VVLTT-ADLAARLPAGGDVALLGDEALAAPPATPPLVPPR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 194 GDalsrgsrqplkpvaikntDLAFVQYTGGTTGVSKGAALTHRNIISNVIcqdeWMKpAGVPDGQGIIVA-ALPL---YH 269
Cdd:cd17646 137 PD------------------NLAYVIYTSGSTGRPKGVMVTHAGIVNRLL----WMQ-DEYPLGPGDRVLqKTPLsfdVS 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 270 VYALttnaLASLKSGSmNLLITNP---RD---LNAFIDDlkkYKITAFTGLNTLYNGLLNHPRINEVDfsELRITSAGGM 343
Cdd:cd17646 194 VWEL----FWPLVAGA-RLVVARPgghRDpayLAALIRE---HGVTTCHFVPSMLRVFLAEPAAGSCA--SLRRVFCSGE 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 344 ALQTSVADRWQKLTGNKPAEGYGLSETSPVLCSNTVTEEGNRVGT-IGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQ 422
Cdd:cd17646 264 ALPPELAARFLALPGAELHNLYGPTEAAIDVTHWPVRGPAETPSVpIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQ 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 423 VFGGYYNRPDESAKVLEDGWF-------KTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACV 495
Cdd:cd17646 344 LARGYLGRPALTAERFVPDPFgpgsrmyRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVV 423
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518832993 496 GVPNEKSGETVKIFVVKKDEALTEDS--ITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPL 558
Cdd:cd17646 424 ARAAPAGAARLVGYVVPAAGAAGPDTaaLRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
218-568 |
3.40e-34 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 136.69 E-value: 3.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 218 VQYTGGTTGVSKGAALTHR----NIISNVICQDEWMKPagvpdgqgIIVAALPLYHVYALTTNALASLKSGSMNLL--IT 291
Cdd:PLN03102 191 LNYTSGTTADPKGVVISHRgaylSTLSAIIGWEMGTCP--------VYLWTLPMFHCNGWTFTWGTAARGGTSVCMrhVT 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 292 NPRdlnaFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSVADRWQKLtGNKPAEGYGLSE-T 370
Cdd:PLN03102 263 APE----IYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRL-GFQVMHAYGLTEaT 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 371 SPVL-CS-----NTVTE---------EGNRVGTIG---IPWPSTyMKCVTEDGTEAalgepGEIWAKGPQVFGGYYNRPD 432
Cdd:PLN03102 338 GPVLfCEwqdewNRLPEnqqmelkarQGVSILGLAdvdVKNKET-QESVPRDGKTM-----GEIVIKGSSIMKGYLKNPK 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 433 ESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVV- 511
Cdd:PLN03102 412 ATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVl 491
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518832993 512 KKDEALTED----------SITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLR--------EEELAKLKK 568
Cdd:PLN03102 492 EKGETTKEDrvdklvtrerDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRdiakglvvEDEDNVIKK 566
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
211-501 |
6.41e-34 |
|
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: 135.04 E-value: 6.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 211 KNTDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMkpAGVPDGQGIIVAALPLYHVYALTTNALASLKSGSMNLli 290
Cdd:cd17639 86 KPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRV--PELLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY-- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 291 TNPRDLNAFI-----DDLKKYKITAFTG----LNTLYNGLLNH-----------------------------PRINEVDF 332
Cdd:cd17639 162 GSPRTLTDKSkrgckGDLTEFKPTLMVGvpaiWDTIRKGVLAKlnpmgglkrtlfwtayqsklkalkegpgtPLLDELVF 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 333 S--------ELRITSAGGMALQTSvADRWQKLTGNKPAEGYGLSETSpvlCSNTVTEEGN-RVGTIGIPWPSTYMKCV-T 402
Cdd:cd17639 242 KkvraalggRLRYMLSGGAPLSAD-TQEFLNIVLCPVIQGYGLTETC---AGGTVQDPGDlETGRVGPPLPCCEIKLVdW 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 403 EDG---TEAalGEP-GEIWAKGPQVFGGYYNRPDESAKVL-EDGWFKTGDIGVMTADGYFKIVDRKKDMI-LVSGFNVYP 476
Cdd:cd17639 318 EEGgysTDK--PPPrGEILIRGPNVFKGYYKNPEKTKEAFdGDGWFHTGDIGEFHPDGTLKIIDRKKDLVkLQNGEYIAL 395
|
330 340 350
....*....|....*....|....*....|....*..
gi 518832993 477 NEIEEVVSQCPGVLEVaCV------------GVPNEK 501
Cdd:cd17639 396 EKLESIYRSNPLVNNI-CVyadpdksypvaiVVPNEK 431
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
55-563 |
1.49e-33 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 134.91 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 55 QITFSELDTLSQQFASFLQNDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIVI 134
Cdd:PRK05620 38 QTTFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 135 LANFAGNLEKILSQT-AIEHVIVTQIGDLlgfpkklivnavvkyvkkMVPAYHLPGAISFGD--ALSRGSRQPLKPVAIK 211
Cdd:PRK05620 118 DPRLAEQLGEILKECpCVRAVVFIGPSDA------------------DSAAAHMPEGIKVYSyeALLDGRSTVYDWPELD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 212 NTDLAFVQYTGGTTGVSKGAALTHRNII---SNVICQDEWmkpaGVPDGQGIIVAaLPLYHVYALTTnALASLKSGSMnl 288
Cdd:PRK05620 180 ETTAAAICYSTGTTGAPKGVVYSHRSLYlqsLSLRTTDSL----AVTHGESFLCC-VPIYHVLSWGV-PLAAFMSGTP-- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 289 LITNPRDLNAfiDDLKKYKITAFT----GLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSVADRWQKLTGNKPAEG 364
Cdd:PRK05620 252 LVFPGPDLSA--PTLAKIIATAMPrvahGVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 365 YGLSETSPVlcsntvteegnrvGTIGIP------------------WPSTYMKCVTEDG--TEAALGEPGEIWAKGPQVF 424
Cdd:PRK05620 330 WGMTETSPV-------------GTVARPpsgvsgearwayrvsqgrFPASLEYRIVNDGqvMESTDRNEGEIQVRGNWVT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 425 GGYYNRP-----------------DESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCP 487
Cdd:PRK05620 397 ASYYHSPteegggaastfrgedveDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 488 GVLEVACVGVPNEKSGE-TVKIFVVKKDEALTEDSITRY---CRENLTAYKVPKHIEFRTELPKSNVGKI----LRRPLR 559
Cdd:PRK05620 477 EVVECAVIGYPDDKWGErPLAVTVLAPGIEPTRETAERLrdqLRDRLPNWMLPEYWTFVDEIDKTSVGKFdkkdLRQHLA 556
|
....
gi 518832993 560 EEEL 563
Cdd:PRK05620 557 DGDF 560
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
30-564 |
3.46e-33 |
|
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: 135.75 E-value: 3.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 30 TSLAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVV 109
Cdd:COG1020 476 ATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLR-ALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYV 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 110 ntnPL---YtPRE-MQHQFNDSGAKAIVILANFAGNLekilSQTAIEHVIVTQigdllgfpkklivnavvkyvkkmvpay 185
Cdd:COG1020 555 ---PLdpaY-PAErLAYMLEDAGARLVLTQSALAARL----PELGVPVLALDA--------------------------- 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 186 hlpgaisfgDALSRGSRQPLkPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVicqdEWMKpagvpdgqgiivaal 265
Cdd:COG1020 600 ---------LALAAEPATNP-PVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLL----AWMQ--------------- 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 266 plyHVYALTTN----ALAS-------------LKSGSMnLLITNP---RDLNAFIDDLKKYKITAFTGLNTLYNGLLNHP 325
Cdd:COG1020 651 ---RRYGLGPGdrvlQFASlsfdasvweifgaLLSGAT-LVLAPPearRDPAALAELLARHRVTVLNLTPSLLRALLDAA 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 326 RInevDFSELRITSAGGMALQTSVADRWQKLTGNkpAE---GYGLSETSPVLCSNTVTEEGNRVGT--IGIPWPSTYMKC 400
Cdd:COG1020 727 PE---ALPSLRLVLVGGEALPPELVRRWRARLPG--ARlvnLYGPTETTVDSTYYEVTPPDADGGSvpIGRPIANTRVYV 801
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 401 VTEDGTEAALGEPGEIWAKGPQVFGGYYNRPDESAK------VLEDG--WFKTGDIGVMTADGYFKIVDRKKDMILVSGF 472
Cdd:COG1020 802 LDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAErfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRADDQVKIRGF 881
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 473 NVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKDEALTEDSITRYC-RENLTAYKVPKHIEFRTELPKSNVG 551
Cdd:COG1020 882 RIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLAlALLLPPYMVPAAVVLLLPLPLTGNG 961
|
570
....*....|...
gi 518832993 552 KILRRPLREEELA 564
Cdd:COG1020 962 KLDRLALPAPAAA 974
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
214-566 |
3.65e-33 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 133.39 E-value: 3.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 214 DLAFVQYTGGTTGVSKGAALTHRNIISNVICqdewmKPAGVPDGQG-IIVAALPLYHVYALTTnALASLKSGSMNLLItn 292
Cdd:PLN02860 173 DAVLICFTSGTTGRPKGVTISHSALIVQSLA-----KIAIVGYGEDdVYLHTAPLCHIGGLSS-ALAMLMVGACHVLL-- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 293 PR-DLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVD--FSELRITSAGGMALQTSVADRWQKLTGN-KPAEGYGLS 368
Cdd:PLN02860 245 PKfDAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWkvFPSVRKILNGGGSLSSRLLPDAKKLFPNaKLFSAYGMT 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 369 ET----------SPVLCSNTVTEE----------GNRVGT-IGIPWPSTYMK-CVTEDGTEaalgepGEIWAKGPQVFGG 426
Cdd:PLN02860 325 EAcssltfmtlhDPTLESPKQTLQtvnqtksssvHQPQGVcVGKPAPHVELKiGLDESSRV------GRILTRGPHVMLG 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 427 YYNRPDESAKVL-EDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGET 505
Cdd:PLN02860 399 YWGQNSETASVLsNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEM 478
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518832993 506 VKIFV---------------VKKDEALTEDSITRYCRE-NLTAYKVPK-HIEFRTELPKSNVGKILRRPLREEELAKL 566
Cdd:PLN02860 479 VVACVrlrdgwiwsdnekenAKKNLTLSSETLRHHCREkNLSRFKIPKlFVQWRKPFPLTTTGKIRRDEVRREVLSHL 556
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
220-558 |
5.39e-33 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 132.82 E-value: 5.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 220 YTGGTTGVSKGAALTHRNIIS-NVICQDEWMKPAGVPDGQgIIVAALPLYHVYALTTnALASLKSGSmnLLITNPRDLNA 298
Cdd:PRK05857 176 FTSGTTGEPKAVLLANRTFFAvPDILQKEGLNWVTWVVGE-TTYSPLPATHIGGLWW-ILTCLMHGG--LCVTGGENTTS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 299 FIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMalQTSVAD-RWQKLTGNKPAEGYGLSETS-PVLCS 376
Cdd:PRK05857 252 LLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGS--RAIAADvRFIEATGVRTAQVYGLSETGcTALCL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 377 NTVTEEGNRV--GTIGIPWP--STYMKCVTEDGTEAALGEP----GEIWAKGPQVFGGYYNRPDESAKVLEDGWFKTGDI 448
Cdd:PRK05857 330 PTDDGSIVKIeaGAVGRPYPgvDVYLAATDGIGPTAPGAGPsasfGTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 449 GVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKDE-------ALTEDS 521
Cdd:PRK05857 410 LERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAEldesaarALKHTI 489
|
330 340 350
....*....|....*....|....*....|....*..
gi 518832993 522 ITRYCRENLTAYKvPKHIEFRTELPKSNVGKILRRPL 558
Cdd:PRK05857 490 AARFRRESEPMAR-PSTIVIVTDIPRTQSGKVMRASL 525
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
46-558 |
1.04e-32 |
|
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: 130.85 E-value: 1.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 46 APAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVntnPLytpremqhqfn 125
Cdd:cd12114 3 ATAVICGDGTLTYGELAERARRVAGALK-AAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYV---PV----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 126 DSGAKAivilanfaGNLEKILSQTAIeHVIVTQIGDLLGFPKKLIVNAVVkyvkkmvpayhlpgaisfGDALSRGSRQPl 205
Cdd:cd12114 68 DIDQPA--------ARREAILADAGA-RLVLTDGPDAQLDVAVFDVLILD------------------LDALAAPAPPP- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 206 kPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNIIsNVICQdewMKPAGVPDGQGIIVAALPLYH---VYALttnaLASLK 282
Cdd:cd12114 120 -PVDVAPDDLAYVIFTSGSTGTPKGVMISHRAAL-NTILD---INRRFAVGPDDRVLALSSLSFdlsVYDI----FGALS 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 283 SGSmNLLITNP---RDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSVADRWQKLTGN 359
Cdd:cd12114 191 AGA-TLVLPDEarrRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPD 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 360 kpAE----GyGLSETSpvLCSN--TVTEEGNRVGTI--GIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRP 431
Cdd:cd12114 270 --ARlislG-GATEAS--IWSIyhPIDEVPPDWRSIpyGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 432 DESA-KVLEDG----WFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVpNEKSGETV 506
Cdd:cd12114 345 ELTAaRFVTHPdgerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVL-GDPGGKRL 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 518832993 507 KIFVVKKDEA--LTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPL 558
Cdd:cd12114 424 AAFVVPDNDGtpIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
57-561 |
8.62e-32 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 129.10 E-value: 8.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 57 TFSELDTLSQQFASFLQND-LKLqkGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIVIL 135
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDgIKL--GDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 136 ANFAGNLEKILSQ-TAIEHVIVtqIGDllgfpkklivnavvkyvKKMVPAYHLPGAISFGDALSRGSrqplKPVAIKNTD 214
Cdd:PRK06018 119 LTFVPILEKIADKlPSVERYVV--LTD-----------------AAHMPQTTLKNAVAYEEWIAEAD----GDFAWKTFD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 215 ---LAFVQYTGGTTGVSKGAALTHR-NIISNVIcqdewmkpAGVPDGQG-----IIVAALPLYHVYALTTnALASLKSGS 285
Cdd:PRK06018 176 entAAGMCYTSGTTGDPKGVLYSHRsNVLHALM--------ANNGDALGtsaadTMLPVVPLFHANSWGI-AFSAPSMGT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 286 mNLLITNPR-DLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSVADRWQKLtGNKPAEG 364
Cdd:PRK06018 247 -KLVMPGAKlDGASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDM-GVEVRHA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 365 YGLSETSPV---------LCSNTVTEEGNRVGTIGIPWPSTYMKCVTEDGTEAALG--EPGEIWAKGPQVFGGYYNrpdE 433
Cdd:PRK06018 325 WGMTEMSPLgtlaalkppFSKLPGDARLDVLQKQGYPPFGVEMKITDDAGKELPWDgkTFGRLKVRGPAVAAAYYR---V 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 434 SAKVL-EDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGE-TVKIFVV 511
Cdd:PRK06018 402 DGEILdDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDErPLLIVQL 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 518832993 512 KKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREE 561
Cdd:PRK06018 482 KPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQ 531
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
57-495 |
3.74e-31 |
|
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: 126.81 E-value: 3.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 57 TFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIvila 136
Cdd:cd05932 8 TWGEVADKARRLAAALRA-LGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKAL---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 137 nFAGNLEKILSQTAiehvivtqigdllGFPKKLIVNAvvkyvkkMVPAYHLPGAISFGDALSRGsrQPLKPVAIKNTD-L 215
Cdd:cd05932 83 -FVGKLDDWKAMAP-------------GVPEGLISIS-------LPPPSAANCQYQWDDLIAQH--PPLEERPTRFPEqL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 216 AFVQYTGGTTGVSKGAALTHRNIisnvicqdEWMKPAGVPD----GQGIIVAALPLYHVYALTTNALASLKSGSmnlLIT 291
Cdd:cd05932 140 ATLIYTSGTTGQPKGVMLTFGSF--------AWAAQAGIEHigteENDRMLSYLPLAHVTERVFVEGGSLYGGV---LVA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 292 NPRDLNAFIDDLKKYKITAFTGLNTLY----------------NGLLNHPRINEV---------DFSELRITSAGGMALQ 346
Cdd:cd05932 209 FAESLDTFVEDVQRARPTLFFSVPRLWtkfqqgvqdkipqqklNLLLKIPVVNSLvkrkvlkglGLDQCRLAGCGSAPVP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 347 TSVADrWQKLTGNKPAEGYGLSETSPVlcsNTVTEEG-NRVGTIGIPWPstymkcvtedGTEAALGEPGEIWAKGPQVFG 425
Cdd:cd05932 289 PALLE-WYRSLGLNILEAYGMTENFAY---SHLNYPGrDKIGTVGNAGP----------GVEVRISEDGEILVRSPALMM 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518832993 426 GYYNRPDESAKVL-EDGWFKTGDIGVMTADGYFKIVDRKKDMILVS-GFNVYPNEIEEVVSQCPGVlEVACV 495
Cdd:cd05932 355 GYYKDPEATAEAFtADGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRV-EMVCV 425
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
35-558 |
5.45e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 129.31 E-value: 5.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 35 LIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPL 114
Cdd:PRK12316 516 LFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALI-ERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPE 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 115 YTPREMQHQFNDSGAKAIvilanfagnlekiLSQTAIehvivtqiGDLLGFPKKLIVNAVVKyvkkmvPAYHLPGAisfg 194
Cdd:PRK12316 595 YPAERLAYMLEDSGVQLL-------------LSQSHL--------GRKLPLAAGVQVLDLDR------PAAWLEGY---- 643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 195 dalsrgSRQPLKpVAIKNTDLAFVQYTGGTTGVSKGAALTHRNiISNVICqdeWMKPA-GVPDGQGiiVAALPLYHVYAL 273
Cdd:PRK12316 644 ------SEENPG-TELNPENLAYVIYTSGSTGKPKGAGNRHRA-LSNRLC---WMQQAyGLGVGDT--VLQKTPFSFDVS 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 274 TTNALASLKSGSmNLLITNP---RDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDfsELRITSAGGMALQtsvA 350
Cdd:PRK12316 711 VWEFFWPLMSGA-RLVVAAPgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCT--SLRRIVCSGEALP---A 784
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 351 DRWQKLTGNKPAEG----YGLSETSPVLCSNTVTEEGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGG 426
Cdd:PRK12316 785 DAQEQVFAKLPQAGlynlYGPTEAAIDVTHWTCVEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARG 864
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 427 YYNRPDESAK-----VLEDG--WFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVpn 499
Cdd:PRK12316 865 YHGRPGLTAErfvpsPFVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-- 942
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 500 ekSGETVKIFVVKKDEA-LTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPL 558
Cdd:PRK12316 943 --DGKQLVGYVVLESEGgDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
54-559 |
5.89e-31 |
|
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: 127.43 E-value: 5.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 54 KQITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLT--VVNTNplYTPREMQHQFNDSGAKa 131
Cdd:cd05967 81 RTYTYAELLDEVSRLAGVLRK-LGVVKGDRVIIYMPMIPEAAIAMLACARIGAIhsVVFGG--FAAKELASRIDDAKPK- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 132 IVILANFAGNLEKI------------LSQTAIEHVIVTQIGDllgfpkklivnavvkyvKKMVPAYHLpGAISFGDALSr 199
Cdd:cd05967 157 LIVTASCGIEPGKVvpykplldkaleLSGHKPHHVLVLNRPQ-----------------VPADLTKPG-RDLDWSELLA- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 200 gSRQPLKPVAIKNTDLAFVQYTGGTTGVSKG---------AAL--THRNIISnvicqdewMKPAGV----PD-----GQG 259
Cdd:cd05967 218 -KAEPVDCVPVAATDPLYILYTSGTTGKPKGvvrdngghaVALnwSMRNIYG--------IKPGDVwwaaSDvgwvvGHS 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 260 IIVAAlPLYHvyALTTNALASLKSGSmnllitnPrDLNAFIDDLKKYKITAF----TGLNTLYNGLLNHPRINEVDFSEL 335
Cdd:cd05967 289 YIVYG-PLLH--GATTVLYEGKPVGT-------P-DPGAFWRVIEKYQVNALftapTAIRAIRKEDPDGKYIKKYDLSSL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 336 RITSAGGMALQTSVADrWQKLTGNKPA-EGYGLSETSPVLCSNTVTEEGN--RVGTIGIPWPSTYMKCVTEDGTEAALGE 412
Cdd:cd05967 358 RTLFLAGERLDPPTLE-WAENTLGVPViDHWWQTETGWPITANPVGLEPLpiKAGSPGKPVPGYQVQVLDEDGEPVGPNE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 413 PGEIWAKGPQVFG---GYYNRPD---ESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQC 486
Cdd:cd05967 437 LGNIVIKLPLPPGcllTLWKNDErfkKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSH 516
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518832993 487 PGVLEVACVGVPNEKSGETVKIFVV-KKDEALTEDSITRYC----RENLTAYKVPKHIEFRTELPKSNVGKILRRPLR 559
Cdd:cd05967 517 PAVAECAVVGVRDELKGQVPLGLVVlKEGVKITAEELEKELvalvREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLR 594
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
81-524 |
7.47e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 126.98 E-value: 7.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 81 GDRIAIQMPNLLQYPIAMFGALRAGLTVVntnPLYTPREMQHQ------FNDSgaKAIVILANFAgnlekilsqtaiehv 154
Cdd:PRK05850 59 GDRAVILAPQGLEYIVAFLGALQAGLIAV---PLSVPQGGAHDervsavLRDT--SPSVVLTTSA--------------- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 155 ivtqigdllgfpkklIVNAVVKYVKKMvPAYHLPGAISFgDALSRGSRQPLKPVAIKNTDLAFVQYTGGTTGVSKGAALT 234
Cdd:PRK05850 119 ---------------VVDDVTEYVAPQ-PGQSAPPVIEV-DLLDLDSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 235 HRNIISNV--ICQDEWMKPAGVPDGQGIIVAALPLYH---------------VYALTTNALASLKSGS--MNLLITNPRD 295
Cdd:PRK05850 182 HRNVIANFeqLMSDYFGDTGGVPPPDTTVVSWLPFYHdmglvlgvcapilggCPAVLTSPVAFLQRPArwMQLLASNPHA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 296 LNA---FIDDLKKYKITA--FTGLNtLYN--GLLN-----HP----RINE----VDFSELRITSAGGMALQTS-VADRwq 354
Cdd:PRK05850 262 FSAapnFAFELAVRKTSDddMAGLD-LGGvlGIISgservHPatlkRFADrfapFNLRETAIRPSYGLAEATVyVATR-- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 355 kLTGNKPAEGY----GLSETSPVLCSntvTEEGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNR 430
Cdd:PRK05850 339 -EPGQPPESVRfdyeKLSAGHAKRCE---TGGGTPLVSYGSPRSPTVRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQK 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 431 PDESAKVL------------EDGWFKTGDIGVMTADGYFkIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVlEVACVGVP 498
Cdd:PRK05850 415 PEETERTFgatlvdpspgtpEGPWLRTGDLGFISEGELF-IVGRIKDLLIVDGRNHYPDDIEATIQEITGG-RVAAISVP 492
|
490 500
....*....|....*....|....*.
gi 518832993 499 NEKSGETVKIFVVKKDEALTEDSITR 524
Cdd:PRK05850 493 DDGTEKLVAIIELKKRGDSDEEAMDR 518
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
33-554 |
2.54e-30 |
|
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: 125.38 E-value: 2.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 33 AALIEEGvkrfssapAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAG--LTVVN 110
Cdd:cd17634 70 TAIIYEG--------DDTSQSRTISYRELHREVCRFAGTLL-DLGVKKGDRVAIYMPMIPEAAVAMLACARIGavHSVIF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 111 TNplYTPREMQHQFNDSGAKAIVI---------LANFAGNLEKIL--SQTAIEHVIVTQigdllgfpkklivnavvkyvK 179
Cdd:cd17634 141 GG--FAPEAVAGRIIDSSSRLLITadggvragrSVPLKKNVDDALnpNVTSVEHVIVLK--------------------R 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 180 KMVPAYHLPGAISFGDALSRGSRQPLKPVAIKNTDLAFVQYTGGTTGVSKG-----------AALTHRNIIsNVICQDEW 248
Cdd:cd17634 199 TGSDIDWQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGvlhttggylvyAATTMKYVF-DYGPGDIY 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 249 MKPAGVpdgqGIIVAALplYHVYA-LTTNALASLKSGSMNllitNPrDLNAFIDDLKKYKITAFTGLNTLYNGLL--NHP 325
Cdd:cd17634 278 WCTADV----GWVTGHS--YLLYGpLACGATTLLYEGVPN----WP-TPARMWQVVDKHGVNILYTAPTAIRALMaaGDD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 326 RINEVDFSELRITSAGGMALQ-TSVADRWQKLTGNK-PAEGY-GLSETSPVLCSNTVTEEGNRVGTIGIPWPSTYMKCVT 402
Cdd:cd17634 347 AIEGTDRSSLRILGSVGEPINpEAYEWYWKKIGKEKcPVVDTwWQTETGGFMITPLPGAIELKAGSATRPVFGVQPAVVD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 403 EDGTEAALGEPGEI-----WAKGPQVFGGYYNRPDESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPN 477
Cdd:cd17634 427 NEGHPQPGGTEGNLvitdpWPGQTRTLFGDHERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTA 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 478 EIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKK----DEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKI 553
Cdd:cd17634 507 EIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNhgvePSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
.
gi 518832993 554 L 554
Cdd:cd17634 587 M 587
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
53-561 |
9.51e-30 |
|
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: 122.08 E-value: 9.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 53 GKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTV--VNTNplYTPREMQHQFNDSGAK 130
Cdd:cd05940 1 DEALTYAELDAMANRYARWLK-SLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAalINYN--LRGESLAHCLNVSSAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 131 AIVIlanfagnlekilsqtaiehvivtqigdllgfpkklivnavvkyvkkmvpayhlpgaisfgdalsrgsrqplkpvai 210
Cdd:cd05940 78 HLVV---------------------------------------------------------------------------- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 211 kntDLAFVQYTGGTTGVSKGAALTHRNIISNVicqdEWMKPAGVPDGQGIIVAALPLYHVYALTTNALASLKSGsMNLLI 290
Cdd:cd05940 82 ---DAALYIYTSGTTGLPKAAIISHRRAWRGG----AFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASG-ATLVI 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 291 TNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPR-INEVDFselRITSAGGMALQTSVADRWQKLTG-NKPAEGYGLS 368
Cdd:cd05940 154 RKKFSASNFWDDIRKYQATIFQYIGELCRYLLNQPPkPTERKH---KVRMIFGNGLRPDIWEEFKERFGvPRIAEFYAAT 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 369 EtspvlCSNTVTEEGNRVGTIG-IPWPSTY------MKCVTEDGT----------EAALGEPGE----IWAKGPqvFGGY 427
Cdd:cd05940 231 E-----GNSGFINFFGKPGAIGrNPSLLRKvaplalVKYDLESGEpirdaegrciKVPRGEPGLlisrINPLEP--FDGY 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 428 YNRPDESAKVLE------DGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGV--PN 499
Cdd:cd05940 304 TDPAATEKKILRdvfkkgDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVqvPG 383
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518832993 500 EKSGETVKIFVVKKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREE 561
Cdd:cd05940 384 TDGRAGMAAIVLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNE 445
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
53-561 |
2.49e-29 |
|
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: 122.01 E-value: 2.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 53 GKQITFSELDTLSQQFASFLQNDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAI 132
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 133 VILANFAGNLEKILSqtaiehvivtqigdllgfpkKLIVNAVVKYVkkMVPAYHLPGAISFGDALSRGSRQPLK---PVA 209
Cdd:cd05938 83 VVAPELQEAVEEVLP--------------------ALRADGVSVWY--LSHTSNTEGVISLLDKVDAASDEPVPaslRAH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 210 IKNTDLAFVQYTGGTTGVSKGAALTHRNII--SNV-----ICQDEwmkpagvpdgqgIIVAALPLYHVYALTTNALASLK 282
Cdd:cd05938 141 VTIKSPALYIYTSGTTGLPKAARISHLRVLqcSGFlslcgVTADD------------VIYITLPLYHSSGFLLGIGGCIE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 283 SGSMNLLitnPRDLNA--FIDDLKKYKITAFTGLNTLYNGLLNHP-RINEVDFSeLRItsAGGMALQTSVADRWQKLTGN 359
Cdd:cd05938 209 LGATCVL---KPKFSAsqFWDDCRKHNVTVIQYIGELLRYLCNQPqSPNDRDHK-VRL--AIGNGLRADVWREFLRRFGP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 360 -KPAEGYGLSETSPVLCSNTvteegNRVGTIG-------IPWPSTYMKCVTEDG----------TEAALGEPGEIWAKGP 421
Cdd:cd05938 283 iRIREFYGSTEGNIGFFNYT-----GKIGAVGrvsylykLLFPFELIKFDVEKEepvrdaqgfcIPVAKGEPGLLVAKIT 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 422 QV--FGGYYNRPDESAK-----VLEDG--WFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEV 492
Cdd:cd05938 358 QQspFLGYAGDKEQTEKkllrdVFKKGdvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEV 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518832993 493 ACVGVPneKSGETVKI----FVVKKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREE 561
Cdd:cd05938 438 NVYGVT--VPGHEGRIgmaaVKLKPGHEFDGKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRLVEE 508
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
36-559 |
5.89e-29 |
|
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: 120.14 E-value: 5.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 36 IEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLY 115
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRA-RGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 116 TPREMQHQFNDSGAKaivilanfagnlekilsqtaiehVIVTQIGDLLGFPKKLIVnavvkyvkkmVPAYHLPGAISFGD 195
Cdd:cd17651 80 PAERLAFMLADAGPV-----------------------LVLTHPALAGELAVELVA----------VTLLDQPGAAAGAD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 196 ALSRGSRQPlkpvaiknTDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMkpagvPDGQGIIVAALPLYHVYALTT 275
Cdd:cd17651 127 AEPDPALDA--------DDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARAS-----SLGPGARTLQFAGLGFDVSVQ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 276 NALASLKSGSMNLLITNP--RDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQtsVADRW 353
Cdd:cd17651 194 EIFSTLCAGATLVLPPEEvrTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLV--LTEDL 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 354 QKLTGNKPAE----GYGLSETSpVLCSNTVTEEGN---RVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGG 426
Cdd:cd17651 272 REFCAGLPGLrlhnHYGPTETH-VVTALSLPGDPAawpAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 427 YYNRPDESA-KVLEDGW------FKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPN 499
Cdd:cd17651 351 YLNRPELTAeRFVPDPFvpgarmYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLARED 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518832993 500 EKSGETVKIFVVKKDEA-LTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLR 559
Cdd:cd17651 431 RPGEKRLVAYVVGDPEApVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
217-552 |
7.40e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 117.87 E-value: 7.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 217 FVQYTGGTTGVSKG----------AALTHRNIISNVICQDEWMKPAGVPDGQGIIVAALPLYHVYALTTnALASLKSGSM 286
Cdd:cd05924 7 YILYTGGTTGMPKGvmwrqedifrMLMGGADFGTGEFTPSEDAHKAAAAAAGTVMFPAPPLMHGTGSWT-AFGGLLGGQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 287 NLLITNPRDLNAFIDDLKKYKITaftgLNTLYNGLLNHPRINE------VDFSELRITSAGGMALQTSVADRWQKLTGNK 360
Cdd:cd05924 86 VVLPDDRFDPEEVWRTIEKHKVT----SMTIVGDAMARPLIDAlrdagpYDLSSLFAISSGGALLSPEVKQGLLELVPNI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 361 P-AEGYGLSETSpVLCSNTVTEEGNRVGTIGIPWPSTYMkcVTEDGTEAALGEPGEIW-AKGPQVFGGYYNRPDESAKVL 438
Cdd:cd05924 162 TlVDAFGSSETG-FTGSGHSAGSGPETGPFTRANPDTVV--LDDDGRVVPPGSGGVGWiARRGHIPLGYYGDEAKTAETF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 439 E--DG--WFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVkIFVVKKD 514
Cdd:cd05924 239 PevDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEV-VAVVQLR 317
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 518832993 515 EA--LTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGK 552
Cdd:cd05924 318 EGagVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
187-553 |
1.09e-28 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 121.61 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 187 LPGAISFGDALsRGSRQPLKP-VAIKN---TDLAFVQYTGGTTGVSKGAALTHRNIISNvICQDEWMKPAGVPDgqgIIV 262
Cdd:PRK06814 764 VRAQIGLADKI-KGLLAGRFPlVYFCNrdpDDPAVILFTSGSEGTPKGVVLSHRNLLAN-RAQVAARIDFSPED---KVF 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 263 AALPLYHVYALTTNALASLKSGSMNLLITNPR----------DLNAfiddlkkykiTAFTGLNTLYNGLLN--HPrineV 330
Cdd:PRK06814 839 NALPVFHSFGLTGGLVLPLLSGVKVFLYPSPLhyriipeliyDTNA----------TILFGTDTFLNGYARyaHP----Y 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 331 DFSELRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETSPVLCSNTVTEegNRVGTIGIPWPSTYMKCVTEDGTEaal 410
Cdd:PRK06814 905 DFRSLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMH--NKAGTVGRLLPGIEYRLEPVPGID--- 979
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 411 gEPGEIWAKGPQVFGGYYnRPDESA--KVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQC-P 487
Cdd:PRK06814 980 -EGGRLFVRGPNVMLGYL-RAENPGvlEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELwP 1057
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518832993 488 GVLEVAcVGVPNEKSGETVKIFVVKKDeaLTEDSITRYCREN-LTAYKVPKHIEFRTELPKSNVGKI 553
Cdd:PRK06814 1058 DALHAA-VSIPDARKGERIILLTTASD--ATRAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKI 1121
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
53-490 |
2.19e-28 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 121.04 E-value: 2.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 53 GKQITFSELDTLSQQFASFLQNdlKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVntnPLYTPREM--QHQfndsgAK 130
Cdd:PRK05691 38 GVVLSYRDLDLRARTIAAALQA--RASFGDRAVLLFPSGPDYVAAFFGCLYAGVIAV---PAYPPESArrHHQ-----ER 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 131 AIVILANFAGNLekiLSQTAIEHVIVTQIGDLLG--FPKKLIVnavvkyvkkmvpayhlpgaisfgDALSRGSRQPLKPV 208
Cdd:PRK05691 108 LLSIIADAEPRL---LLTVADLRDSLLQMEELAAanAPELLCV-----------------------DTLDPALAEAWQEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 209 AIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNvicqdEWMKPAGV-----PDGqgIIVAALPLYHVYALTTNALASLKS 283
Cdd:PRK05691 162 ALQPDDIAFLQYTSGSTALPKGVQVSHGNLVAN-----EQLIRHGFgidlnPDD--VIVSWLPLYHDMGLIGGLLQPIFS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 284 G------SMNLLITNP-RDLNAfiddLKKYKITAFTGLNTLYNglLNHPRINE-----VDFSELRITSAGGMALQTSVAD 351
Cdd:PRK05691 235 GvpcvlmSPAYFLERPlRWLEA----ISEYGGTISGGPDFAYR--LCSERVSEsalerLDLSRWRVAYSGSEPIRQDSLE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 352 RWQK------LTGNKPAEGYGLSETspvlcsnTVTEEGNRVGTiGIPW-----------------PSTYMKC-------- 400
Cdd:PRK05691 309 RFAEkfaacgFDPDSFFASYGLAEA-------TLFVSGGRRGQ-GIPAleldaealarnraepgtGSVLMSCgrsqpgha 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 401 --VTEDGTEAALGEP--GEIWAKGPQVFGGYYNRPDESAK--VLEDG--WFKTGDIGVMTaDGYFKIVDRKKDMILVSGF 472
Cdd:PRK05691 381 vlIVDPQSLEVLGDNrvGEIWASGPSIAHGYWRNPEASAKtfVEHDGrtWLRTGDLGFLR-DGELFVTGRLKDMLIVRGH 459
|
490
....*....|....*...
gi 518832993 473 NVYPNEIEEVVSQCPGVL 490
Cdd:PRK05691 460 NLYPQDIEKTVEREVEVV 477
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
46-558 |
3.09e-28 |
|
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: 117.57 E-value: 3.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 46 APAYACMGKQITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFN 125
Cdd:cd17650 3 AIAVSDATRQLTYRELNERANQLARTLRG-LGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 126 DSGAKAIVIlanfagnlekilsqtaiehvivtqigdllgfpkklivnavvkyvkkmvpayhlpgaisfgdalsrgsrQPl 205
Cdd:cd17650 82 DSGAKLLLT--------------------------------------------------------------------QP- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 206 kpvaiknTDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMKPAGVPdgqgiiVAALPL----YHVYAlTTNALASL 281
Cdd:cd17650 93 -------EDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFP------VRLLQMasfsFDVFA-GDFARSLL 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 282 KSGSMnllITNPRDL----NAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGgmalQTSVADRWQK-- 355
Cdd:cd17650 159 NGGTL---VICPDEVkldpAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVG----SDGCKAQDFKtl 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 356 ----LTGNKPAEGYGLSET---SPVLCSNTVTEEGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYY 428
Cdd:cd17650 232 aarfGQGMRIINSYGVTEAtidSTYYEEGRDPLGDSANVPIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYL 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 429 NRPDESA-KVLEDGW------FKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEvACVGVPNEK 501
Cdd:cd17650 312 NRPELTAeRFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDE-AVVAVREDK 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 518832993 502 SGETVKIFVVKKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPL 558
Cdd:cd17650 391 GGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
56-562 |
4.05e-28 |
|
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: 116.90 E-value: 4.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 56 ITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIVIL 135
Cdd:cd05974 1 VSFAEMSARSSRVANFLR-SIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAVYAAVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 136 ANFAGNLEKILSQTAiehvivtqigDLLGFPKklivnaVVKYVKKMVPAYHLPGAISFGdalsrgsrqpLKPVAIkntdl 215
Cdd:cd05974 80 ENTHADDPMLLYFTS----------GTTSKPK------LVEHTHRSYPVGHLSTMYWIG----------LKPGDV----- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 216 afvqytggttgvskgaaltHRNIISnvicqDEWMKpagvpdgqgiivaalplyHVYaltTNALASLKSGSMNLLITNPR- 294
Cdd:cd05974 129 -------------------HWNISS-----PGWAK------------------HAW---SCFFAPWNAGATVFLFNYARf 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 295 DLNAFIDDLKKYKITAFTGLNTLYNGLLNHPrINEVDFSeLRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETSpVL 374
Cdd:cd05974 164 DAKRVLAALVRYGVTTLCAPPTVWRMLIQQD-LASFDVK-LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETT-AL 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 375 CSNTvTEEGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPG-EIWAKGPQ-VFGGYYNRPDESAKVLEDGWFKTGDIGVMT 452
Cdd:cd05974 241 VGNS-PGQPVKAGSMGRPLPGYRVALLDPDGAPATEGEVAlDLGDTRPVgLMKGYAGDPDKTAHAMRGGYYRTGDIAMRD 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 453 ADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVV-------KKDEALtedSITRY 525
Cdd:cd05974 320 EDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVlragyepSPETAL---EIFRF 396
|
490 500 510
....*....|....*....|....*....|....*..
gi 518832993 526 CRENLTAYKVPKHIEFRtELPKSNVGKILRRPLREEE 562
Cdd:cd05974 397 SRERLAPYKRIRRLEFA-ELPKTISGKIRRVELRRRE 432
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
35-560 |
5.37e-28 |
|
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: 117.26 E-value: 5.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 35 LIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPL 114
Cdd:cd05918 4 LIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLR-SLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 115 YtPREmqhqfndsgakaivilanfagNLEKILSQTAIEHVIVTQIgdllgfpkklivnavvkyvkkmvpayhlpgaisfg 194
Cdd:cd05918 83 H-PLQ---------------------RLQEILQDTGAKVVLTSSP----------------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 195 dalsrgsrqplkpvaiknTDLAFVQYTGGTTGVSKGAALTHRNIISNVICQdewmkpagvpdgqgiiVAALPL------Y 268
Cdd:cd05918 106 ------------------SDAAYVIFTSGSTGKPKGVVIEHRALSTSALAH----------------GRALGLtsesrvL 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 269 HVYALT-----TNALASLKSGSMnLLITNPRD-LNAFIDDLKKYKIT-AF---TGLNTLyngllnHPRinevDFSELRIT 338
Cdd:cd05918 152 QFASYTfdvsiLEIFTTLAAGGC-LCIPSEEDrLNDLAGFINRLRVTwAFltpSVARLL------DPE----DVPSLRTL 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 339 SAGGMALQTSVADRWQ---KLTGnkpaeGYGLSETSpVLCSNTVTEEGNRVGTIGIPWPSTYmkCVTEDGTE---AALGE 412
Cdd:cd05918 221 VLGGEALTQSDVDTWAdrvRLIN-----AYGPAECT-IAATVSPVVPSTDPRNIGRPLGATC--WVVDPDNHdrlVPIGA 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 413 PGEIWAKGPQVFGGYYNRPDESAKV-LED-GW------------FKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNE 478
Cdd:cd05918 293 VGELLIEGPILARGYLNDPEKTAAAfIEDpAWlkqegsgrgrrlYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGE 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 479 IEEVVSQCPGVLEVACVGVPNEKSGETVKI---FVVKKDEALTED------------------SITRYCRENLTAYKVPK 537
Cdd:cd05918 373 IEHHLRQSLPGAKEVVVEVVKPKDGSSSPQlvaFVVLDGSSSGSGdgdslflepsdefralvaELRSKLRQRLPSYMVPS 452
|
570 580
....*....|....*....|...
gi 518832993 538 HIEFRTELPKSNVGKILRRPLRE 560
Cdd:cd05918 453 VFLPLSHLPLTASGKIDRRALRE 475
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
207-565 |
8.54e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 115.90 E-value: 8.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 207 PVAIKNTDLAF----VQYTGGTTGVSKGAALTHRNIISNVICQDEWMKpagVPDGQGIIVAAlPLYHVYALTTNALASLK 282
Cdd:PRK08308 91 TKLEAVNYLAEepslLQYSSGTTGEPKLIRRSWTEIDREIEAYNEALN---CEQDETPIVAC-PVTHSYGLICGVLAALT 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 283 SGSMNLLIT--NPRDLnafIDDLKKYKITAFTGLNTLYNGLLNHPRINEvdfselRITSAggMALQTSVADRW-QKLTGN 359
Cdd:PRK08308 167 RGSKPVIITnkNPKFA---LNILRNTPQHILYAVPLMLHILGRLLPGTF------QFHAV--MTSGTPLPEAWfYKLRER 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 360 KP--AEGYGLSETSPVLCSNTVTEEGNrvgtIGIPWPSTYMKcvtedgTEAALGEPGEI--WAKGPQVFggyynrpdesa 435
Cdd:PRK08308 236 TTymMQQYGCSEAGCVSICPDMKSHLD----LGNPLPHVSVS------AGSDENAPEEIvvKMGDKEIF----------- 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 436 kvledgwfkTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVkKDE 515
Cdd:PRK08308 295 ---------TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVI-SHE 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 518832993 516 ALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREEELAK 565
Cdd:PRK08308 365 EIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELGEVTA 414
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
54-565 |
1.33e-27 |
|
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: 117.21 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 54 KQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIV 133
Cdd:cd05968 90 RTLTYGELLYEVKRLANGLR-ALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALI 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 134 I---------LANFAGNLEKILSQTA-IEHVIVTQIGDLLGFPkklivnAVVKYVkkmvpAYHLPGAISFGDALSRGSRQ 203
Cdd:cd05968 169 TadgftrrgrEVNLKEEADKACAQCPtVEKVVVVRHLGNDFTP------AKGRDL-----SYDEEKETAGDGAERTESED 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 204 PLkpvaikntdlaFVQYTGGTTGVSKGAALTHrniisnvicqdewmkpAGVPdgqgiIVAALPLYHVYalttnalaSLKS 283
Cdd:cd05968 238 PL-----------MIIYTSGTTGKPKGTVHVH----------------AGFP-----LKAAQDMYFQF--------DLKP 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 284 GSMNLLITN-------------------------------PRDLNAFIDDlkkYKITAFtGLN-TLYNGLLNHPR--INE 329
Cdd:cd05968 278 GDLLTWFTDlgwmmgpwlifgglilgatmvlydgapdhpkADRLWRMVED---HEITHL-GLSpTLIRALKPRGDapVNA 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 330 VDFSELRITSAGGMALQtsvADRWQ-----KLTGNKPAEGY-GLSETSPVLCSNTVTEEGNRVGTIGiPWPSTYMKCVTE 403
Cdd:cd05968 354 HDLSSLRVLGSTGEPWN---PEPWNwlfetVGKGRNPIINYsGGTEISGGILGNVLIKPIKPSSFNG-PVPGMKADVLDE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 404 DGTEAAlGEPGE--IWAKGPQVFGGYYNRPDESAKV----LEDGWFKtGDIGVMTADGYFKIVDRKKDMILVSGFNVYPN 477
Cdd:cd05968 430 SGKPAR-PEVGElvLLAPWPGMTRGFWRDEDRYLETywsrFDNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPA 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 478 EIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKD-----EALTEDSITRYCRENLTAYKvPKHIEFRTELPKSNVGK 552
Cdd:cd05968 508 EIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPgvtptEALAEELMERVADELGKPLS-PERILFVKDLPKTRNAK 586
|
570
....*....|...
gi 518832993 553 ILRRPLREEELAK 565
Cdd:cd05968 587 VMRRVIRAAYLGK 599
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
213-520 |
1.44e-27 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 117.25 E-value: 1.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 213 TDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMKPAG-VPDGQGIIVAALPLYHVYALTTNALASLKSGSMNLLIT 291
Cdd:PLN02861 220 TDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKVTDrVATEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQG 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 292 NPRDLnafIDDLKKYKITAFTGLNTLYN----------------------------------GLLNH---PRINEVDFSE 334
Cdd:PLN02861 300 DIRYL---MEDVQALKPTIFCGVPRVYDriytgimqkissggmlrkklfdfaynyklgnlrkGLKQEeasPRLDRLVFDK 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 335 L--------RITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETspvlCSNTVTEEGN---RVGTIGIPWPS--TYMKCV 401
Cdd:PLN02861 377 IkeglggrvRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTES----CGGCFTSIANvfsMVGTVGVPMTTieARLESV 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 402 TEDGTEAALGEP-GEIWAKGPQVFGGYYNRPDESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVS-GFNVYPNEI 479
Cdd:PLN02861 453 PEMGYDALSDVPrGEICLRGNTLFSGYHKRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSqGEYVAVENL 532
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 518832993 480 EEVVSQCPGVLEVACVGvpneKSGETVKIFVVKKDEALTED 520
Cdd:PLN02861 533 ENTYSRCPLIASIWVYG----NSFESFLVAVVVPDRQALED 569
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
204-556 |
3.13e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 115.86 E-value: 3.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 204 PLKPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVicqdEWMKPAGVPD-GQGIIVAALPLYHVYALTTNALASLK 282
Cdd:PRK07768 143 PIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANA----EAMFVAAEFDvETDVMVSWLPLFHDMGMVGFLTVPMY 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 283 SGSMNLLITnPRDlnaFIDD-------LKKYKITAFTGLNTLYN----GLLNHPRINEVDFSELRITSAGGMALQTSVAD 351
Cdd:PRK07768 219 FGAELVKVT-PMD---FLRDpllwaelISKYRGTMTAAPNFAYAllarRLRRQAKPGAFDLSSLRFALNGAEPIDPADVE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 352 RWqkLTGNKP--------AEGYGLSET------SPVLCSNTVTE----------------EGN--RVGTIGIPWPSTYMK 399
Cdd:PRK07768 295 DL--LDAGARfglrpeaiLPAYGMAEAtlavsfSPCGAGLVVDEvdadllaalrravpatKGNtrRLATLGPPLPGLEVR 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 400 CVTEDGTEAALGEPGEIWAKGPQVFGGYYNRPDESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEI 479
Cdd:PRK07768 373 VVDEDGQVLPPRGVGVIELRGESVTPGYLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDI 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 480 EEVVSQCPGVLE--VACVGVPNEKSGETVKIfVVKKDEALTEDSITRYCREnlTAYKVPKHIEFRTE---------LPKS 548
Cdd:PRK07768 453 ERAAARVEGVRPgnAVAVRLDAGHSREGFAV-AVESNAFEDPAEVRRIRHQ--VAHEVVAEVGVRPRnvvvlgpgsIPKT 529
|
....*...
gi 518832993 549 NVGKiLRR 556
Cdd:PRK07768 530 PSGK-LRR 536
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
34-558 |
1.26e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 115.64 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 34 ALIEEGVKRFSSAPAyACMGKQ-ITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTN 112
Cdd:PRK12467 516 QLIEAQARQHPERPA-LVFGEQvLSYAELNRQANRLAHVLI-AAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLD 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 113 PLYtPRE-MQHQFNDSGAKAIvilanfagnlekiLSQtaiEHVIvtqigdllgfpKKLIVNAVVKYVKKMVPAyhlpgai 191
Cdd:PRK12467 594 PEY-PQDrLAYMLDDSGVRLL-------------LTQ---SHLL-----------AQLPVPAGLRSLCLDEPA------- 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 192 sfgdALSRGSRQPLKPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWmkPAGVPDGQGIIVA--ALPLYH 269
Cdd:PRK12467 639 ----DLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAER--LQLAADDSMLMVStfAFDLGV 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 270 VYALTtnALASLKSgsmnLLITNP---RDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVdfSELRITSAGGMALQ 346
Cdd:PRK12467 713 TELFG--ALASGAT----LHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALP--RPQRALVCGGEALQ 784
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 347 TSVADRW-QKLTGNKPAEGYGLSETSPVLCSNTVTEEGNRVGT--IGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQV 423
Cdd:PRK12467 785 VDLLARVrALGPGARLINHYGPTETTVGVSTYELSDEERDFGNvpIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGL 864
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 424 FGGYYNRPDESA-KVLEDGW-------FKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACV 495
Cdd:PRK12467 865 ARGYHRRPALTAeRFVPDPFgadggrlYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVL 944
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518832993 496 GVPNEKSGETVKIFVVKK-----DEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPL 558
Cdd:PRK12467 945 AQPGDAGLQLVAYLVPAAvadgaEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
36-564 |
1.46e-26 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 113.07 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 36 IEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAI---QMPNLLqypIAMFGALRAGLTVVntn 112
Cdd:PRK04813 8 IEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFID-SLKLPDKSPIIVfghMSPEML---ATFLGAVKAGHAYI--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 113 P--LYTPREMQHQFNDSGAKAIVILANfagnlEKILSQTAIEHVIVTQIGDLLGFPKKLIVNAVVKyvkkmvpayhlpga 190
Cdd:PRK04813 81 PvdVSSPAERIEMIIEVAKPSLIIATE-----ELPLEILGIPVITLDELKDIFATGNPYDFDHAVK-------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 191 isfGDalsrgsrqplkpvaikntDLAFVQYTGGTTGVSKGAALTHRNIISNVicqdEWMKPA-GVPDGQGIIvaALPLYH 269
Cdd:PRK04813 142 ---GD------------------DNYYIIFTSGTTGKPKGVQISHDNLVSFT----NWMLEDfALPEGPQFL--NQAPYS 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 270 vYALTTNALA-SLKSGS-MNLL----ITNPRDLNAfidDLKKYKITAFTG---------LNTLYNGLlNHPRINEVDFSe 334
Cdd:PRK04813 195 -FDLSVMDLYpTLASGGtLVALpkdmTANFKQLFE---TLPQLPINVWVStpsfadmclLDPSFNEE-HLPNLTHFLFC- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 335 lritsagGMALQTSVAdrwQKLTGNKPA----EGYGLSETSPVLCSNTVTEE----GNRVgTIGIPWPSTYMKCVTEDGT 406
Cdd:PRK04813 269 -------GEELPHKTA---KKLLERFPSatiyNTYGPTEATVAVTSIEITDEmldqYKRL-PIGYAKPDSPLLIIDEEGT 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 407 EAALGEPGEIWAKGPQVFGGYYNRPDESAKVL--EDGW--FKTGDIGVMtadgyfkivdrKKDMILVSG-------FNVY 475
Cdd:PRK04813 338 KLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFftFDGQpaYHTGDAGYL-----------EDGLLFYQGridfqikLNGY 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 476 PNEIEEV---VSQCPGVLEvaCVGVPNEKSGETVKI--FVVKKDEALTED-SITRYCRENLT----AYKVPKHIEFRTEL 545
Cdd:PRK04813 407 RIELEEIeqnLRQSSYVES--AVVVPYNKDHKVQYLiaYVVPKEEDFEREfELTKAIKKELKerlmEYMIPRKFIYRDSL 484
|
570
....*....|....*....
gi 518832993 546 PKSNVGKILRRPLREEELA 564
Cdd:PRK04813 485 PLTPNGKIDRKALIEEVNK 503
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
35-558 |
2.34e-26 |
|
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: 112.03 E-value: 2.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 35 LIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPL 114
Cdd:cd12115 4 LVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRA-AGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 115 YtPREmqhqfndsgakaivilanfagNLEKILSQTAIEHVIVTQigdllgfpkklivnavvkyvkkmvpayhlpgaisfg 194
Cdd:cd12115 83 Y-PPE---------------------RLRFILEDAQARLVLTDP------------------------------------ 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 195 dalsrgsrqplkpvaiknTDLAFVQYTGGTTGVSKGAALTHRNIISNVicqdEWMKPAGVPDGQGIIVAA------LPLY 268
Cdd:cd12115 105 ------------------DDLAYVIYTSGSTGRPKGVAIEHRNAAAFL----QWAAAAFSAEELAGVLAStsicfdLSVF 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 269 HVYA-LTTNALASLKSGSMNLLiTNPRDLNAfiddlkkykitafTGLNT---LYNGLLNHPRINEvdfsELRITSAGGMA 344
Cdd:cd12115 163 ELFGpLATGGKVVLADNVLALP-DLPAAAEV-------------TLINTvpsAAAELLRHDALPA----SVRVVNLAGEP 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 345 L-QTSVADRWQKLTGNKPAEGYGLSETSPVLCSNTVTEEGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQV 423
Cdd:cd12115 225 LpRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGASGEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGV 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 424 FGGYYNRPDESA-KVLEDGW------FKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEvACVG 496
Cdd:cd12115 305 ARGYLGRPGLTAeRFLPDPFgpgarlYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVRE-AVVV 383
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518832993 497 VPNEKSGET--VKIFVVKKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPL 558
Cdd:cd12115 384 AIGDAAGERrlVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
192-507 |
4.08e-26 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 112.99 E-value: 4.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 192 SFGDALSRGSRQPLKPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNV----ICQDEWMKPAGVPDgqgIIVAALPL 267
Cdd:PLN02430 199 SWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVrgvdLFMEQFEDKMTHDD---VYLSFLPL 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 268 YHVYALTTNALASLKSGSMNLLitnPRDLNAFIDDLKKYKITAFTG------------------LNTL----YNGLLNH- 324
Cdd:PLN02430 276 AHILDRMIEEYFFRKGASVGYY---HGDLNALRDDLMELKPTLLAGvprvferihegiqkalqeLNPRrrliFNALYKYk 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 325 --------------PRINEVDFSE--------LRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETspvlCSNTVT-- 380
Cdd:PLN02430 353 lawmnrgyshkkasPMADFLAFRKvkaklggrLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTET----LGPTTLgf 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 381 -EEGNRVGTIGIPwpSTYMKCVTEDGTEAA---LGEP--GEIWAKGPQVFGGYYNRPDESAKVLEDGWFKTGDIGVMTAD 454
Cdd:PLN02430 429 pDEMCMLGTVGAP--AVYNELRLEEVPEMGydpLGEPprGEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILPN 506
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518832993 455 GYFKIVDRKKDMILVS-GFNVYPNEIEEVVSQCPGVLEVACVG-----------VPNEksgETVK 507
Cdd:PLN02430 507 GVLKIIDRKKNLIKLSqGEYVALEYLENVYGQNPIVEDIWVYGdsfksmlvavvVPNE---ENTN 568
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
31-558 |
4.92e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 113.90 E-value: 4.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 31 SLAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLqndLKLQKGD--RIAIQMPNLLQYPIAMFGALRAGLTV 108
Cdd:PRK12316 4552 CVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHAL---IARGVGPevLVGIAMERSAEMMVGLLAVLKAGGAY 4628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 109 VNTNPLYtPRE-MQHQFNDSGAKaivILANFAGNLEKILSQTAIEHVIVTQIGDLLGFPkklivnavvkyvkkmvpayhl 187
Cdd:PRK12316 4629 VPLDPEY-PRErLAYMMEDSGAA---LLLTQSHLLQRLPIPDGLASLALDRDEDWEGFP--------------------- 4683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 188 pgaisfgdalsrgSRQPLKPVAIKNtdLAFVQYTGGTTGVSKGAALTHRNIISNVIcqdeWM--KPAGVPDGQGII---- 261
Cdd:PRK12316 4684 -------------AHDPAVRLHPDN--LAYVIYTSGSTGRPKGVAVSHGSLVNHLH----ATgeRYELTPDDRVLQfmsf 4744
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 262 ---VAALPLYHVyaLTTNAlaslksgsmNLLITNPR--DLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRiNEVDFSELR 336
Cdd:PRK12316 4745 sfdGSHEGLYHP--LINGA---------SVVIRDDSlwDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAE-RDGEPPSLR 4812
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 337 ITSAGGMALQTSVADR-WQKLTGNKPAEGYGLSETS-PVLCSNT--VTEEGNRVGTIGIPWPSTYMKCVTEDGTEAALGE 412
Cdd:PRK12316 4813 VYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTvTVLLWKArdGDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGV 4892
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 413 PGEIWAKGPQVFGGYYNRPDESA-KVLEDGW-------FKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVS 484
Cdd:PRK12316 4893 AGELYLGGEGVARGYLERPALTAeRFVPDPFgapggrlYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLR 4972
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 485 QCPGVLEVACVGVPNeKSGETVKIFVVKKDEALTE---------DSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILR 555
Cdd:PRK12316 4973 EHPAVREAVVIAQEG-AVGKQLVGYVVPQDPALADadeaqaelrDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDR 5051
|
...
gi 518832993 556 RPL 558
Cdd:PRK12316 5052 KAL 5054
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
56-496 |
7.28e-26 |
|
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: 112.07 E-value: 7.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 56 ITFSELDTLSQQFA-SFLQndLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSgaKAIVI 134
Cdd:cd05933 9 LTYKEYYEACRQAAkAFLK--LGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETS--EANIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 135 LANFAGNLEKILsqtaiehvivtQIGDLLgfPKkliVNAVVKYVKKMVPayHLPGAISFGDALSRGSRQPLKPV-----A 209
Cdd:cd05933 85 VVENQKQLQKIL-----------QIQDKL--PH---LKAIIQYKEPLKE--KEPNLYSWDEFMELGRSIPDEQLdaiisS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 210 IKNTDLAFVQYTGGTTGVSKGAALTHRNI--ISNVICQDEWMKPAgvPDGQGIIVAALPLYHVYALTTNALASLKSGSmn 287
Cdd:cd05933 147 QKPNQCCTLIYTSGTTGMPKGVMLSHDNItwTAKAASQHMDLRPA--TVGQESVVSYLPLSHIAAQILDIWLPIKVGG-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 288 lLITNPrDLNA----FIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELR---ITSAGGMALQTSVA---------- 350
Cdd:cd05933 223 -QVYFA-QPDAlkgtLVKTLREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKrkiASWAKGVGLETNLKlmggespspl 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 351 -------------------DRWQKL-TGNKP----------------AEGYGLSETSPvlcSNTVTEEGN-RVGTIGIPW 393
Cdd:cd05933 301 fyrlakklvfkkvrkalglDRCQKFfTGAAPisretlefflslnipiMELYGMSETSG---PHTISNPQAyRLLSCGKAL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 394 PSTYMKCVTEDgteaALGEpGEIWAKGPQVFGGYYNRPDESAKVL-EDGWFKTGDIGVMTADGYFKIVDRKKDMILVS-G 471
Cdd:cd05933 378 PGCKTKIHNPD----ADGI-GEICFWGRHVFMGYLNMEDKTEEAIdEDGWLHSGDLGKLDEDGFLYITGRIKELIITAgG 452
|
490 500
....*....|....*....|....*.
gi 518832993 472 FNVYPNEIEEVV-SQCPGVLEVACVG 496
Cdd:cd05933 453 ENVPPVPIEDAVkKELPIISNAMLIG 478
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
21-558 |
8.32e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 113.33 E-value: 8.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 21 PHDINPDSYTSLAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFG 100
Cdd:PRK12467 1565 ATHTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLI-ALGVGPEVLVGIAVERSLEMVVGLLA 1643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 101 ALRAGLTVVNTNPLYTPREMQHQFNDSGakaIVILANFAGNLEKILSQTAIEHVIVTQIGDLLGfpkklivnavvkyvkk 180
Cdd:PRK12467 1644 ILKAGGAYVPLDPEYPRERLAYMIEDSG---IELLLTQSHLQARLPLPDGLRSLVLDQEDDWLE---------------- 1704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 181 mvpayhlpgaisfgdalsrgSRQPLKP-VAIKNTDLAFVQYTGGTTGVSKGAALTHRNIIsNVICqdeWMKPAGVPDGQG 259
Cdd:PRK12467 1705 --------------------GYSDSNPaVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALV-NRLC---ATQEAYQLSAAD 1760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 260 IIVaalpLYHVYALTTNA---LASLKSGSmNLLITNP---RDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFS 333
Cdd:PRK12467 1761 VVL----QFTSFAFDVSVwelFWPLINGA-RLVIAPPgahRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLS 1835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 334 eLRITSAGGMALQTSVADRW-QKLTGNKPAEGYGLSETSPVLCSNTVT---EEGNRVGTIGIPWP--STYMkcVTEDGTE 407
Cdd:PRK12467 1836 -LRRVVCGGEALEVEALRPWlERLPDTGLFNLYGPTETAVDVTHWTCRrkdLEGRDSVPIGQPIAnlSTYI--LDASLNP 1912
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 408 AALGEPGEIWAKGPQVFGGYYNRPDESA-KVLEDGW-------FKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEI 479
Cdd:PRK12467 1913 VPIGVAGELYLGGVGLARGYLNRPALTAeRFVADPFgtvgsrlYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEI 1992
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 480 EEVVSQCPGVLEVACVGVpNEKSGETVKIFVVKKDEALTEDSITR-YCRENLTA--------YKVPKHIEFRTELPKSNV 550
Cdd:PRK12467 1993 EARLREQGGVREAVVIAQ-DGANGKQLVAYVVPTDPGLVDDDEAQvALRAILKNhlkaslpeYMVPAHLVFLARMPLTPN 2071
|
....*...
gi 518832993 551 GKILRRPL 558
Cdd:PRK12467 2072 GKLDRKAL 2079
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
15-498 |
1.13e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 111.36 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 15 HYPPGvphdinpdsyTSLAALIEEGVKRFSSAPAYACM---------GKQITFSELDTLSQQFASFLQNdlKLQKGDRIA 85
Cdd:PRK07769 16 RFPPN----------TNLVRHVERWAKVRGDKLAYRFLdfsterdgvARDLTWSQFGARNRAVGARLQQ--VTKPGDRVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 86 IQMPNLLQYPIAMFGALRAGLTVVntnPLYTPREMQHqfndsgakaivilanfAGNLEKILSQtAIEHVIVTQIGDLLGf 165
Cdd:PRK07769 84 ILAPQNLDYLIAFFGALYAGRIAV---PLFDPAEPGH----------------VGRLHAVLDD-CTPSAILTTTDSAEG- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 166 pkklivnaVVKYVKKmVPAYHLPGAISFgDALSRGSRQPLKPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVIcq 245
Cdd:PRK07769 143 --------VRKFFRA-RPAKERPRVIAV-DAVPDEVGATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVL-- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 246 deWMKPAGVPDGQGIIVAALPLYHVYALTTNALASLKSGSMNLL-----ITNP----RDLNAFIDDLKK---------YK 307
Cdd:PRK07769 211 --QVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMspaafVRRPgrwiRELARKPGGTGGtfsaapnfaFE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 308 ITAFTGLntlyngllnhPRINE--VDFSELRITSAGGMALQTSVADRWQ--------KLTGNKPAegYGLSETSpVLCSN 377
Cdd:PRK07769 289 HAAARGL----------PKDGEppLDLSNVKGLLNGSEPVSPASMRKFNeafapyglPPTAIKPS--YGMAEAT-LFVST 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 378 TVTEEGNRV-----------------------------GTIGIpwpSTYMKCV-TEDGTEAALGEPGEIWAKGPQVFGGY 427
Cdd:PRK07769 356 TPMDEEPTViyvdrdelnagrfvevpadapnavaqvsaGKVGV---SEWAVIVdPETASELPDGQIGEIWLHGNNIGTGY 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 428 YNRPDESAKVL-----------------EDG-WFKTGDIGVMTaDGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGV 489
Cdd:PRK07769 433 WGKPEETAATFqnilksrlseshaegapDDAlWVRTGDYGVYF-DGELYITGRVKDLVIIDGRNHYPQDLEYTAQEATKA 511
|
570
....*....|..
gi 518832993 490 LE---VACVGVP 498
Cdd:PRK07769 512 LRtgyVAAFSVP 523
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
46-559 |
2.84e-25 |
|
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: 108.61 E-value: 2.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 46 APAYACMGKQITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFN 125
Cdd:cd17649 3 AVALVFGDQSLSYAELDARANRLAHRLRA-LGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 126 DSGAkaivilanfagnlekilsqtaieHVIVTQIGDllgfpkklivnavvkyvkkmvpayhlpgaisfgdalsrgsrqpl 205
Cdd:cd17649 82 DSGA-----------------------GLLLTHHPR-------------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 206 kpvaikntDLAFVQYTGGTTGVSKGAALTHRNII--------------SNVICQ----------DEWMKPAGVpdGQGII 261
Cdd:cd17649 95 --------QLAYVIYTSGSTGTPKGVAVSHGPLAahcqataerygltpGDRELQfasfnfdgahEQLLPPLIC--GACVV 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 262 VAALPLYhvyaLTTNALASL-KSGSMNLLITNPRDLNAFIDDLKkykitaftglntlyngllnhpRINEVDFSELRITSA 340
Cdd:cd17649 165 LRPDELW----ASADELAEMvRELGVTVLDLPPAYLQQLAEEAD---------------------RTGDGRPPSLRLYIF 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 341 GGMALQTSVADRWQKlTGNKPAEGYGLSET--SPVL--CSNTVTEEGNRVgTIGIPWPSTYMKCVTEDGTEAALGEPGEI 416
Cdd:cd17649 220 GGEALSPELLRRWLK-APVRLFNAYGPTEAtvTPLVwkCEAGAARAGASM-PIGRPLGGRSAYILDADLNPVPVGVTGEL 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 417 WAKGPQVFGGYYNRPDESA-KVLEDG-------WFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPG 488
Cdd:cd17649 298 YIGGEGLARGYLGRPELTAeRFVPDPfgapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPG 377
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518832993 489 VLEVACVGVPNEKSGETVKIFVVKKDEALTED--SITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLR 559
Cdd:cd17649 378 VREAAVVALDGAGGKQLVAYVVLRAAAAQPELraQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
200-561 |
3.26e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 109.35 E-value: 3.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 200 GSRQPLKPV-AIKNTDLAFVQYTGGTTGVSK------------GAALTHRniiSNVICQDewmkpagvpdgqgIIVAALP 266
Cdd:PRK13388 136 AAAGALTPHrEVDAMDPFMLIFTSGTTGAPKavrcshgrlafaGRALTER---FGLTRDD-------------VCYVSMP 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 267 LYH---VYALTTNALASlkSGSMNLlitnPRDLNA--FIDDLKKYKITAFTglntlYNG-----LLNHPRINEVDFSELR 336
Cdd:PRK13388 200 LFHsnaVMAGWAPAVAS--GAAVAL----PAKFSAsgFLDDVRRYGATYFN-----YVGkplayILATPERPDDADNPLR 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 337 ItsaggmALQTSVADR----WQKLTGNKPAEGYGLSETSPVLcsntVTEEGNRVGTIGIPW-------PSTYMKCVT--- 402
Cdd:PRK13388 269 V------AFGNEASPRdiaeFSRRFGCQVEDGYGSSEGAVIV----VREPGTPPGSIGRGApgvaiynPETLTECAVarf 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 403 -EDGT----EAALGEPgeIWAKGPQVFGGYYNRPDESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPN 477
Cdd:PRK13388 339 dAHGAllnaDEAIGEL--VNTAGAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAA 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 478 EIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKDEA-LTEDSITRY--CRENLTAYKVPKHIEFRTELPKSNVGKIL 554
Cdd:PRK13388 417 PIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGAtFDPDAFAAFlaAQPDLGTKAWPRYVRIAADLPSTATNKVL 496
|
....*..
gi 518832993 555 RRPLREE 561
Cdd:PRK13388 497 KRELIAQ 503
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
45-558 |
2.75e-24 |
|
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: 105.80 E-value: 2.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 45 SAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQF 124
Cdd:cd17652 2 DAPAVVFGDETLTYAELNARANRLARLLA-ARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 125 NDSGAkaivilanfagnlekilsqtaieHVIVTQIGDLlgfpkklivnavvkyvkkmvpayhlpgaisfgdalsrgsrqp 204
Cdd:cd17652 81 ADARP-----------------------ALLLTTPDNL------------------------------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 205 lkpvaikntdlAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMkpaGVPDGQGIIVAALPLYHVYALttNALASLKSG 284
Cdd:cd17652 96 -----------AYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAF---DVGPGSRVLQFASPSFDASVW--ELLMALLAG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 285 SmNLLITNPRDLNA---FIDDLKKYKITAFT----GLNTLyngllnhpriNEVDFSELRITSAGGMALQTSVADRWQKlt 357
Cdd:cd17652 160 A-TLVLAPAEELLPgepLADLLREHRITHVTlppaALAAL----------PPDDLPDLRTLVVAGEACPAELVDRWAP-- 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 358 GNKPAEGYGLSETSpVLCSNTVTEEGNRVGTIGIPWPST--YmkcVTEDGTE-AALGEPGEIWAKGPQVFGGYYNRPDES 434
Cdd:cd17652 227 GRRMINAYGPTETT-VCATMAGPLPGGGVPPIGRPVPGTrvY---VLDARLRpVPPGVPGELYIAGAGLARGYLNRPGLT 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 435 A-KVLEDGW-------FKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEvACVGVPNEKSGET- 505
Cdd:cd17652 303 AeRFVADPFgapgsrmYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAE-AVVVVRDDRPGDKr 381
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 518832993 506 -VKIFVVKKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPL 558
Cdd:cd17652 382 lVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
54-496 |
2.85e-24 |
|
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: 106.74 E-value: 2.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 54 KQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVntnPLYT---PREMQHQFNDSGAK 130
Cdd:cd17641 10 QEFTWADYADRVRAFALGLL-ALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSL---GIYQdsmAEEVAYLLNYTGAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 131 aiVILANFAGNLEKILS-QTAIEHVivtqigdllgfpkklivNAVVKYVKKMVPAYHLPGAISFGDALSRG----SRQP- 204
Cdd:cd17641 86 --VVIAEDEEQVDKLLEiADRIPSV-----------------RYVIYCDPRGMRKYDDPRLISFEDVVALGraldRRDPg 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 205 --LKPVA-IKNTDLAFVQYTGGTTGVSKGAALTHRNIISnvicqdewMKPAGVP-DGQGI---IVAALPL----YHVYAL 273
Cdd:cd17641 147 lyEREVAaGKGEDVAVLCTTSGTTGKPKLAMLSHGNFLG--------HCAAYLAaDPLGPgdeYVSVLPLpwigEQMYSV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 274 ---------------TTNALASLKSGSMNLLITNPR-------DLNAFIDDLKKYKITAF-------------------- 311
Cdd:cd17641 219 gqalvcgfivnfpeePETMMEDLREIGPTFVLLPPRvwegiaaDVRARMMDATPFKRFMFelgmklglraldrgkrgrpv 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 312 -TGLNTLY---NGLLNHPRINEVDFSELRITSAGGMALQTSVADRWQKLtGNKPAEGYGLSETSPVLcsnTVTEEGN-RV 386
Cdd:cd17641 299 sLWLRLASwlaDALLFRPLRDRLGFSRLRSAATGGAALGPDTFRFFHAI-GVPLKQLYGQTELAGAY---TVHRDGDvDP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 387 GTIGIPWPstymkcvtedGTEAALGEPGEIWAKGPQVFGGYYNRPDESAK-VLEDGWFKTGDIGVMTADGYFKIVDRKKD 465
Cdd:cd17641 375 DTVGVPFP----------GTEVRIDEVGEILVRSPGVFVGYYKNPEATAEdFDEDGWLHTGDAGYFKENGHLVVIDRAKD 444
|
490 500 510
....*....|....*....|....*....|..
gi 518832993 466 -MILVSGFNVYPNEIEEVVSQCPGVLEVACVG 496
Cdd:cd17641 445 vGTTSDGTRFSPQFIENKLKFSPYIAEAVVLG 476
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
56-566 |
2.90e-24 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 107.51 E-value: 2.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 56 ITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIVIL 135
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVA-LGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICD 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 136 ANFAGNLEKILSQ-TAIEHVI-VTQIGDLLGFPKKLIVNAVVkyvkkmvpayhlpgaISFGDALSRGSRQPLKPVAIKNT 213
Cdd:PLN02387 186 SKQLKKLIDISSQlETVKRVIyMDDEGVDSDSSLSGSSNWTV---------------SSFSEVEKLGKENPVDPDLPSPN 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 214 DLAFVQYTGGTTGVSKGAALTHRNIISNVicqdewmkpAGV----PD--GQGIIVAALPLYHVYALT------------- 274
Cdd:PLN02387 251 DIAVIMYTSGSTGLPKGVMMTHGNIVATV---------AGVmtvvPKlgKNDVYLAYLPLAHILELAaesvmaavgaaig 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 275 -------TNALASLKSGSM--------NLLITNPRDLNAFIDDLKKyKITAFTGL-NTLYN------------------G 320
Cdd:PLN02387 322 ygspltlTDTSNKIKKGTKgdasalkpTLMTAVPAILDRVRDGVRK-KVDAKGGLaKKLFDiaykrrlaaiegswfgawG 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 321 L-------LNHPRINEVDFSELRITSAGGMALqTSVADRWQKLTGNKP-AEGYGLSETspvlCSN-TVTE-EGNRVGTIG 390
Cdd:PLN02387 401 LekllwdaLVFKKIRAVLGGRIRFMLSGGAPL-SGDTQRFINICLGAPiGQGYGLTET----CAGaTFSEwDDTSVGRVG 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 391 IPWPSTYMKCVT-EDGTEAALGEP---GEIWAKGPQVFGGYYN---RPDESAKVLEDG--WFKTGDIGVMTADGYFKIVD 461
Cdd:PLN02387 476 PPLPCCYVKLVSwEEGGYLISDKPmprGEIVIGGPSVTLGYFKnqeKTDEVYKVDERGmrWFYTGDIGQFHPDGCLEIID 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 462 RKKDMI-LVSGFNVYPNEIEEVVSQCPGVLEVA---------CVG--VPN--------EKSGETVKIF--VVKKDEALTE 519
Cdd:PLN02387 556 RKKDIVkLQHGEYVSLGKVEAALSVSPYVDNIMvhadpfhsyCVAlvVPSqqalekwaKKAGIDYSNFaeLCEKEEAVKE 635
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 518832993 520 --DSITRYCREN-LTAYKVPKHIEFRTEL--PKSNVG----KILRRPLR---EEELAKL 566
Cdd:PLN02387 636 vqQSLSKAAKAArLEKFEIPAKIKLLPEPwtPESGLVtaalKLKREQIRkkfKDDLKKL 694
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
55-555 |
6.59e-24 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 105.86 E-value: 6.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 55 QITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVntnPLYTPremqhqfndsgakaivi 134
Cdd:PRK09192 49 ALPYQTLRARAEAGARRLLA-LGLKPGDRVALIAETDGDFVEAFFACQYAGLVPV---PLPLP----------------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 135 lANFAGnlekilsqtaiEHVIVTQIGDLLGF--PKKLIVNAVVK-YVKKMVPAYHLPGAISFGDALSR-GSRQPLKPvaI 210
Cdd:PRK09192 108 -MGFGG-----------RESYIAQLRGMLASaqPAAIITPDELLpWVNEATHGNPLLHVLSHAWFKALpEADVALPR--P 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 211 KNTDLAFVQYTGGTTGVSKGAALTHRNIISNV--ICQDewmkpagvpdgqGIIVAA-------LPLYHVYALTTNALASL 281
Cdd:PRK09192 174 TPDDIAYLQYSSGSTRFPRGVIITHRALMANLraISHD------------GLKVRPgdrcvswLPFYHDMGLVGFLLTPV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 282 KSG-SMNLLITNP---RDLnAFIDDLKK------------YKITAFTGlntlyngllNHPRINEVDFSELRITSAGG--- 342
Cdd:PRK09192 242 ATQlSVDYLPTRDfarRPL-QWLDLISRnrgtisysppfgYELCARRV---------NSKDLAELDLSCWRVAGIGAdmi 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 343 -MALQTSVADRWQKLTGNKPA--EGYGLSET------SPV---LCSNTVTEE--------------GNRVGTI---GIPW 393
Cdd:PRK09192 312 rPDVLHQFAEAFAPAGFDDKAfmPSYGLAEAtlavsfSPLgsgIVVEEVDRDrleyqgkavapgaeTRRVRTFvncGKAL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 394 PSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRpDESAKVLE-DGWFKTGDIGVMtADGYFKIVDRKKDMILVSGF 472
Cdd:PRK09192 392 PGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRD-EESQDVLAaDGWLDTGDLGYL-LDGYLYITGRAKDLIIINGR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 473 NVYPNEIEEVVSQCPGVL--EVACVGVPNEkSGETVKIFV------VKKDEALTeDSITRYCRenlTAYKVPKHIEF--- 541
Cdd:PRK09192 470 NIWPQDIEWIAEQEPELRsgDAAAFSIAQE-NGEKIVLLVqcrisdEERRGQLI-HALAALVR---SEFGVEAAVELvpp 544
|
570
....*....|....
gi 518832993 542 RTeLPKSNVGKILR 555
Cdd:PRK09192 545 HS-LPRTSSGKLSR 557
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
55-560 |
7.10e-24 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 105.21 E-value: 7.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 55 QITFSELDTLSQQFASFLqNDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIVI 134
Cdd:cd05915 24 RTTYAEVYQRARRLMGGL-RALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 135 LANFAGNLEKILSqtaiehvivtqigdllgfpkkLIVNAVVKYVKKmvPAYHlpgaiSFGDALSRGSR--QPLKPVaiKN 212
Cdd:cd05915 103 DPNLLPLVEAIRG---------------------ELKTVQHFVVMD--EKAP-----EGYLAYEEALGeeADPVRV--PE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 213 TDLAFVQYTGGTTGVSKGAALTHRNIISNV----ICQDEWMKPAGVpdgqgiIVAALPLYHV----YALTTNALaslksG 284
Cdd:cd05915 153 RAACGMAYTTGTTGLPKGVVYSHRALVLHSlaasLVDGTALSEKDV------VLPVVPMFHVnawcLPYAATLV-----G 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 285 SMNLLITNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMAlQTSVADRWQKLTGNKPAEG 364
Cdd:cd05915 222 AKQVLPGPRLDPASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGSA-APRSLIARFERMGVEVRQG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 365 YGLSETSPVLCS-------NTVTEEGN-----RVG------TIGIPWPSTYmkCVTEDGTEAALgepgeIWAKGPQVFGG 426
Cdd:cd05915 301 YGLTETSPVVVQnfvkshlESLSEEEKltlkaKTGlpiplvRLRVADEEGR--PVPKDGKALGE-----VQLKGPWITGG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 427 YY-NRPDESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGET 505
Cdd:cd05915 374 YYgNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQER 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 518832993 506 VKIFVVKKDEALTEDSITRYCRENLTAYK-VPKHIEFRTELPKSNVGKILRRPLRE 560
Cdd:cd05915 454 PLAVVVPRGEKPTPEELNEHLLKAGFAKWqLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
53-561 |
7.98e-24 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 104.81 E-value: 7.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 53 GKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGL--TVVNTNpLYTPrEMQHQFNDSGAK 130
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQ-AQGYRSGDVVALFMENRLEFVALWLGLAKIGVetALINSN-LRLE-SLLHCITVSKAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 131 AIVIlanfagNLEKILSQTAIEHVIVTQIGDLlgfpkklivnavvkyvkkmvpayhlpgaisfgdalsrgsrqplkpvai 210
Cdd:cd05939 78 ALIF------NLLDPLLTQSSTEPPSQDDVNF------------------------------------------------ 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 211 knTDLAFVQYTGGTTGVSKGAALTHRNIIsnvicqdeWMKpAGVPDGQG-----IIVAALPLYHVYALTTNALASLKSGs 285
Cdd:cd05939 104 --RDKLFYIYTSGTTGLPKAAVIVHSRYY--------RIA-AGAYYAFGmrpedVVYDCLPLYHSAGGIMGVGQALLHG- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 286 MNLLITNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTsvadrWQKLTGN----KP 361
Cdd:cd05939 172 STVVIRKKFSASNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKHNVRLAVGNGLRPQI-----WEQFVRRfgipQI 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 362 AEGYGLSEtspvlCSNTVTEEGNRVGTIG----IP---WPSTYMKCvTEDGTEA-----------ALGEPGE----IWAK 419
Cdd:cd05939 247 GEFYGATE-----GNSSLVNIDNHVGACGfnsrILpsvYPIRLIKV-DEDTGELirdsdglcipcQPGEPGLlvgkIIQN 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 420 GP-QVFGGYYNRPDESAKVLE------DGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEV 492
Cdd:cd05939 321 DPlRRFDGYVNEGATNKKIARdvfkkgDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDV 400
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 493 ACVGVPNEKS-GETVKIFVVKKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREE 561
Cdd:cd05939 401 VVYGVEVPGVeGRAGMAAIVDPERKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKE 470
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
55-558 |
1.53e-23 |
|
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: 104.09 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 55 QITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIVI 134
Cdd:cd17656 13 KLTYRELNERSNQLARFLRE-KGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 135 LANFAGNLEKILSQTAIEHVIVTQIgdlLGFPKKLIVNavvkyvkkmvpayhlpgaisfgdalsrgsrqplkpvaikNTD 214
Cdd:cd17656 92 QRHLKSKLSFNKSTILLEDPSISQE---DTSNIDYINN---------------------------------------SDD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 215 LAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMkpaGVPDGQGIIVAALPLYHVyaLTTNALASLKSGSMNLLITNP- 293
Cdd:cd17656 130 LLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKT---NINFSDKVLQFATCSFDV--CYQEIFSTLLSGGTLYIIREEt 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 294 -RDLNAFIDDLKKYKI-TAFtgLNTLYNGLLNHPRINEVDFSEL--RITSAGGMALQTSVADRWQKLTGNKPAEGYGLSE 369
Cdd:cd17656 205 kRDVEQLFDLVKRHNIeVVF--LPVAFLKFIFSEREFINRFPTCvkHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 370 TSPV-LCSNTVTEEGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRPDESA-KVLEDGW----- 442
Cdd:cd17656 283 THVVtTYTINPEAEIPELPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAeKFFPDPFdpner 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 443 -FKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVkKDEALTEDS 521
Cdd:cd17656 363 mYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV-MEQELNISQ 441
|
490 500 510
....*....|....*....|....*....|....*..
gi 518832993 522 ITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPL 558
Cdd:cd17656 442 LREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
52-559 |
2.15e-23 |
|
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: 104.18 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 52 MGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGL--TVVNTNplYTPREMQHQFNDSGA 129
Cdd:cd05966 81 QSRTITYRELLREVCRFANVLK-SLGVKKGDRVAIYMPMIPELVIAMLACARIGAvhSVVFAG--FSAESLADRINDAQC 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 130 KaIVILAN--FAG----NLEKILSQ-----TAIEHVIVtqigdllgfpkklivnavVKYVKKMVPayHLPGAISFGDALS 198
Cdd:cd05966 158 K-LVITADggYRGgkviPLKEIVDEalekcPSVEKVLV------------------VKRTGGEVP--MTEGRDLWWHDLM 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 199 RGSRQPLKPVAIKNTDLAFVQYTGGTTGVSKG-----------AALTHRNIISNvicQDE----------WMKpagvpdG 257
Cdd:cd05966 217 AKQSPECEPEWMDSEDPLFILYTSGSTGKPKGvvhttggyllyAATTFKYVFDY---HPDdiywctadigWIT------G 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 258 QGiivaalplYHVYALTTNALASLksgsMNLLITNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPR--INEVDFSEL 335
Cdd:cd05966 288 HS--------YIVYGPLANGATTV----MFEGTPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDewVKKHDLSSL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 336 RI-TSAG---------------GMAlQTSVADR-WQKLTG-----NKPaegyGLSETSPvlcsntvteegnrvGTIGIPW 393
Cdd:cd05966 356 RVlGSVGepinpeawmwyyeviGKE-RCPIVDTwWQTETGgimitPLP----GATPLKP--------------GSATRPF 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 394 PSTYMKCVTEDGTEAALGEPGEIWAKGP------QVFGGYYNRPDESAKVLEdGWFKTGDIGVMTADGYFKIVDRKKDMI 467
Cdd:cd05966 417 FGIEPAILDEEGNEVEGEVEGYLVIKRPwpgmarTIYGDHERYEDTYFSKFP-GYYFTGDGARRDEDGYYWITGRVDDVI 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 468 LVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKDEALTEDSITR----YCRENLTAYKVPKHIEFRT 543
Cdd:cd05966 496 NVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKelrkHVRKEIGPIATPDKIQFVP 575
|
570
....*....|....*.
gi 518832993 544 ELPKSNVGKILRRPLR 559
Cdd:cd05966 576 GLPKTRSGKIMRRILR 591
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
182-560 |
1.00e-22 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 99.73 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 182 VPAYHLPGAISFGDALSRGsrQPLKPvaikntDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMkpagvpDGQGII 261
Cdd:PRK07824 12 VPAQDERRAALLRDALRVG--EPIDD------DVALVVATSGTTGTPKGAMLTAAALTASADATHDRL------GGPGQW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 262 VAALPLYHVYALTTnALASLKSGSMNLLITNPRDLNafIDDLKKykITAFTGLNTLYNGL--------LNHPRINEVdFS 333
Cdd:PRK07824 78 LLALPAHHIAGLQV-LVRSVIAGSEPVELDVSAGFD--PTALPR--AVAELGGGRRYTSLvpmqlakaLDDPAATAA-LA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 334 ELRITSAGGMALQTSVADRWQKLtGNKPAEGYGLSETspvlCSNTVTEegnrvgtiGIPWpstymkcvteDGTEAALGEp 413
Cdd:PRK07824 152 ELDAVLVGGGPAPAPVLDAAAAA-GINVVRTYGMSET----SGGCVYD--------GVPL----------DGVRVRVED- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 414 GEIWAKGPQVFGGYYNRPDESAKVlEDGWFKTGDIGVMTaDGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVA 493
Cdd:PRK07824 208 GRIALGGPTLAKGYRNPVDPDPFA-EPGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCA 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518832993 494 CVGVPNEKSGETVKIFVVKK-DEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLRE 560
Cdd:PRK07824 286 VFGLPDDRLGQRVVAAVVGDgGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
208-562 |
1.17e-22 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 102.48 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 208 VAIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVicqdEWMKPAGVPDGQGIIVAALPLYHVYALTTNALASLKSGSMN 287
Cdd:PRK08043 360 VKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANV----EQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEV 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 288 LLITNPRDLNAFIDDLKKYKITAFTGLNTLyngLLNHPRI-NEVDFSELRITSAGGMALQTSVADRWQKLTGNKPAEGYG 366
Cdd:PRK08043 436 FLYPSPLHYRIVPELVYDRNCTVLFGTSTF---LGNYARFaNPYDFARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYG 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 367 LSETSPVLCSNTVTeeGNRVGTIGIPWPSTYMKCVTEDGTEaalgEPGEIWAKGPQVFGGYY--NRPDE----SAK---- 436
Cdd:PRK08043 513 VTECAPVVSINVPM--AAKPGTVGRILPGMDARLLSVPGIE----QGGRLQLKGPNIMNGYLrvEKPGVlevpTAEnarg 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 437 VLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVkkDEA 516
Cdd:PRK08043 587 EMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEALVLFTT--DSE 664
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 518832993 517 LTEDSITRYCREN-LTAYKVPKHIEFRTELPKSNVGK----ILRRPLREEE 562
Cdd:PRK08043 665 LTREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGKpdfvTLKSMVDEPE 715
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
35-558 |
4.32e-22 |
|
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: 99.17 E-value: 4.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 35 LIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPL 114
Cdd:cd17645 3 LFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLR-GKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 115 YTPREMQHQFNDSGAKaivilanfagnlekilsqtaiehVIVTQIGDLlgfpkklivnavvkyvkkmvpayhlpgaisfg 194
Cdd:cd17645 82 YPGERIAYMLADSSAK-----------------------ILLTNPDDL-------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 195 dalsrgsrqplkpvaikntdlAFVQYTGGTTGVSKGAALTHRNIISnvICqdEWMKPA-GV-PDGQGIIVAALPLYhvyA 272
Cdd:cd17645 107 ---------------------AYVIYTSGSTGLPKGVMIEHHNLVN--LC--EWHRPYfGVtPADKSLVYASFSFD---A 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 273 LTTNALASLKSGSMNLLITNPRDLNafIDDLKKYKITAFTGLNTLYNGLLNhpRINEVDFSELRITSAGGMALQTSVADR 352
Cdd:cd17645 159 SAWEIFPHLTAGAALHVVPSERRLD--LDALNDYFNQEGITISFLPTGAAE--QFMQLDNQSLRVLLTGGDKLKKIERKG 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 353 WQKLTGnkpaegYGLSETSPVLCSNTV-TEEGNRvgTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRP 431
Cdd:cd17645 235 YKLVNN------YGPTENTVVATSFEIdKPYANI--PIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRP 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 432 DESAK-------VLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGE 504
Cdd:cd17645 307 ELTAEkfivhpfVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRK 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 518832993 505 TVKIFVVKKDEALTEdSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPL 558
Cdd:cd17645 387 YLVAYVTAPEEIPHE-ELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
218-558 |
6.38e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 99.30 E-value: 6.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 218 VQYTGGTTGVSKGAALTHRnIISNVICQDEWMKPAGVPDGQGIIVAaLPLYHVYALTTNALASLKSGSmnLLITNPRDLN 297
Cdd:PRK13383 179 VLLTSGTTGKPKGVPRAPQ-LRSAVGVWVTILDRTRLRTGSRISVA-MPMFHGLGLGMLMLTIALGGT--VLTHRHFDAE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 298 AFIDDLKKYKITAFTGLNTLYNGLLNHP-RINEVD-FSELRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETSpVLC 375
Cdd:PRK13383 255 AALAQASLHRADAFTAVPVVLARILELPpRVRARNpLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVG-IGA 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 376 SNTVTEEGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYynrPDESAKVLEDGWFKTGDIGVMTADG 455
Cdd:PRK13383 334 LATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRY---TDGGGKAVVDGMTSTGDMGYLDNAG 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 456 YFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVV-KKDEALTEDSITRYCRENLTAYK 534
Cdd:PRK13383 411 RLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVlHPGSGVDAAQLRDYLKDRVSRFE 490
|
330 340
....*....|....*....|....
gi 518832993 535 VPKHIEFRTELPKSNVGKILRRPL 558
Cdd:PRK13383 491 QPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
213-561 |
1.78e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 97.83 E-value: 1.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 213 TDLAFVQYTGGTTGVSKGAALTHRNIIS--NVICQDEWMKPAGVpdgqgiIVAALPLYH---VYALTTNALASlkSGSMN 287
Cdd:PRK07867 152 DDLFMLIFTSGTSGDPKAVRCTHRKVASagVMLAQRFGLGPDDV------CYVSMPLFHsnaVMAGWAVALAA--GASIA 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 288 LlitnPRDLNA--FIDDLKKYKITAFTglntlYNG------LLNHPRINEVDfSELRI---TSAGGMALqtsvaDRWQKL 356
Cdd:PRK07867 224 L----RRKFSAsgFLPDVRRYGATYAN-----YVGkplsyvLATPERPDDAD-NPLRIvygNEGAPGDI-----ARFARR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 357 TGNKPAEGYGLSETSPVLCSNTVTEEGN---RVGTIGIPWPSTYMKC----VTEDGTEAALGEPGEIW-AKGPQVFGGYY 428
Cdd:PRK07867 289 FGCVVVDGFGSTEGGVAITRTPDTPPGAlgpLPPGVAIVDPDTGTECppaeDADGRLLNADEAIGELVnTAGPGGFEGYY 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 429 NRPDESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKI 508
Cdd:PRK07867 369 NDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMA 448
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 518832993 509 FVVKKDEA-LTEDSITRY--CRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREE 561
Cdd:PRK07867 449 ALVLAPGAkFDPDAFAEFlaAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAE 504
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
76-455 |
3.90e-21 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 96.81 E-value: 3.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 76 LKLQK--GDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIvilanfagnlekILSQTAIEH 153
Cdd:PRK06334 60 TKVSKypDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHV------------LTSKQLMQH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 154 VIVTQiGDLLGFPKKLIvnavvkYVKKMVPAYHLPGAISFGDALSRGSRQPLKPVAIKNT---DLAFVQYTGGTTGVSKG 230
Cdd:PRK06334 128 LAQTH-GEDAEYPFSLI------YMEEVRKELSFWEKCRIGIYMSIPFEWLMRWFGVSDKdpeDVAVILFTSGTEKLPKG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 231 AALTHRNIISNvicQDEWMKPAGvPDGQGIIVAALPLYHVYALTTNALASLKSG-----SMNLLitNPRDLNAFIDDLkk 305
Cdd:PRK06334 201 VPLTHANLLAN---QRACLKFFS-PKEDDVMMSFLPPFHAYGFNSCTLFPLLSGvpvvfAYNPL--YPKKIVEMIDEA-- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 306 yKITAFTGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSVADRWQKLTGN-KPAEGYGLSETSPVLCSNTVTEEGN 384
Cdd:PRK06334 273 -KVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHiQLRQGYGTTECSPVITINTVNSPKH 351
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518832993 385 RvGTIGIPWPSTYMKCVTEDgTEAAL--GEPGEIWAKGPQVFGGYYNRpDESAKVLE---DGWFKTGDIGVMTADG 455
Cdd:PRK06334 352 E-SCVGMPIRGMDVLIVSEE-TKVPVssGETGLVLTRGTSLFSGYLGE-DFGQGFVElggETWYVTGDLGYVDRHG 424
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
478-552 |
4.47e-21 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 87.21 E-value: 4.47e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518832993 478 EIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVV-KKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGK 552
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVlKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
56-464 |
5.74e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 96.97 E-value: 5.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 56 ITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKAIVIL 135
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLA-ELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCN 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 136 ANFAGNLEKILSQTAIEHVIVTQIGDLlgfpkklivnavvkyvkkmvPA------YHLpgaISFGDALSRG----SRQPL 205
Cdd:PTZ00216 201 GKNVPNLLRLMKSGGMPNTTIIYLDSL--------------------PAsvdtegCRL---VAWTDVVAKGhsagSHHPL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 206 kPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMKPA-GVPDGQGIIVAALPLYHVYALT-TNALasLKS 283
Cdd:PTZ00216 258 -NIPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLNDLiGPPEEDETYCSYLPLAHIMEFGvTNIF--LAR 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 284 GSmnlLIT--NPRDL-NAFI---DDLKKYKITAFTGL------------------NTLYNGLLNH--------------- 324
Cdd:PTZ00216 335 GA---LIGfgSPRTLtDTFArphGDLTEFRPVFLIGVprifdtikkaveaklppvGSLKRRVFDHayqsrlralkegkdt 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 325 PRINEVDFS--------ELRITSAGGMALQTSVADrWQKLTGNKPAEGYGLSETspvLCSNTVTEEGN-RVGTIGIPWPS 395
Cdd:PTZ00216 412 PYWNEKVFSapravlggRVRAMLSGGGPLSAATQE-FVNVVFGMVIQGWGLTET---VCCGGIQRTGDlEPNAVGQLLKG 487
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518832993 396 TYMKCV-TEDGTEAALGEP-GEIWAKGPQVFGGYYNRPDESAKVL-EDGWFKTGDIGVMTADGYFKIVDRKK 464
Cdd:PTZ00216 488 VEMKLLdTEEYKHTDTPEPrGEILLRGPFLFKGYYKQEELTREVLdEDGWFHTGDVGSIAANGTLRIIGRVK 559
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
26-508 |
6.56e-21 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 96.73 E-value: 6.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 26 PDSYTsLAALIEEGVKRFSSAPAY---------ACMGKQITFSELDTLSQQFASFLQNdlKLQKGDRIAIQMPNLLQYPI 96
Cdd:PRK12476 31 PPGTT-LISLIERNIANVGDTVAYryldhshsaAGCAVELTWTQLGVRLRAVGARLQQ--VAGPGDRVAILAPQGIDYVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 97 AMFGALRAGLTVVntnPLYTPRemqhqfndsgakaiviLANFAGNLEKILSQTAIEHVIVTQIGDllgfpkklivNAVVK 176
Cdd:PRK12476 108 GFFAAIKAGTIAV---PLFAPE----------------LPGHAERLDTALRDAEPTVVLTTTAAA----------EAVEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 177 YVKKMvPAYHLPGAISFgDALSRGSRQPLKPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVIcqdEWMKPAGVPD 256
Cdd:PRK12476 159 FLRNL-PRLRRPRVIAI-DAIPDSAGESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLV---QMILSIDLLD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 257 GQGIIVAALPLYHVYALTTNALASLKSGSMNLL-----ITNP----RDLNAFIDDLK--------KYKITAFTGLNtlyn 319
Cdd:PRK12476 234 RNTHGVSWLPLYHDMGLSMIGFPAVYGGHSTLMsptafVRRPqrwiKALSEGSRTGRvvtaapnfAYEWAAQRGLP---- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 320 gllnhPRINEVDFSELR-------ITSAGGMALQTSVADRWQKLTGNKPAegYGLSETSpVLCSNT----------VTEE 382
Cdd:PRK12476 310 -----AEGDDIDLSNVVliigsepVSIDAVTTFNKAFAPYGLPRTAFKPS--YGIAEAT-LFVATIapdaepsvvyLDRE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 383 GNRVG----------------TIGIPWPSTYMKCVTED-GTEAALGEPGEIWAKGPQVFGGYYNRPDESAKV-------- 437
Cdd:PRK12476 382 QLGAGravrvaadapnavahvSCGQVARSQWAVIVDPDtGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTfgaklqsr 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 438 LEDG-----------WFKTGDIGVMTaDGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQC-PGVLE--VACVGVPNEKSG 503
Cdd:PRK12476 462 LAEGshadgaaddgtWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIEATVAEAsPMVRRgyVTAFTVPAEDNE 540
|
....*
gi 518832993 504 ETVKI 508
Cdd:PRK12476 541 RLVIV 545
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
35-558 |
6.62e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 97.72 E-value: 6.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 35 LIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPL 114
Cdd:PRK12316 3062 LFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLI-ERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPE 3140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 115 YTPREMQHQFNDSGAkaivilanfagnlEKILSQTAIEHVIVTQIGDLLGFPkklivnavvkyvkkmvpayhlpgaisfg 194
Cdd:PRK12316 3141 YPEERLAYMLEDSGA-------------QLLLSQSHLRLPLAQGVQVLDLDR---------------------------- 3179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 195 DALSRGSRQPlkPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNIiSNVICQDEWMKPAGVPDGqgiiVAALPLYHVYALT 274
Cdd:PRK12316 3180 GDENYAEANP--AIRTMPENLAYVIYTSGSTGKPKGVGIRHSAL-SNHLCWMQQAYGLGVGDR----VLQFTTFSFDVFV 3252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 275 TNALASLKSGSMNLL--ITNPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINevDFSELRITSAGGMALQTSVADR 352
Cdd:PRK12316 3253 EELFWPLMSGARVVLagPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAH--RCTSLKRIVCGGEALPADLQQQ 3330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 353 WqkLTGNKPAEGYGLSETSPVLCSNTVTEEGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRPD 432
Cdd:PRK12316 3331 V--FAGLPLYNLYGPTEATITVTHWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPG 3408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 433 ESAKVLEDGWF-------KTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVpnekSGET 505
Cdd:PRK12316 3409 LTAERFVPDPFvpgerlyRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAV----DGRQ 3484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 518832993 506 VKIFVVKKDEALT-EDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPL 558
Cdd:PRK12316 3485 LVAYVVPEDEAGDlREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
32-568 |
6.74e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 97.72 E-value: 6.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 32 LAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNT 111
Cdd:PRK12316 2005 VHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLR-ARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPL 2083
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 112 NPLYtPRE-MQHQFNDSGAKaivILANFAGNLEKILSQTAIEHVIVTQIGDLLGFPKKlivnavvkyvkkmVPAYHLPGA 190
Cdd:PRK12316 2084 DPNY-PAErLAYMLEDSGAA---LLLTQRHLLERLPLPAGVARLPLDRDAEWADYPDT-------------APAVQLAGE 2146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 191 isfgdalsrgsrqplkpvaikntDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEW--MKPAGVP--------DGqgi 260
Cdd:PRK12316 2147 -----------------------NLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERyeLSPADCElqfmsfsfDG--- 2200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 261 ivAALPLYHvyALTTNALASLKSGSMnllitnpRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRInEVDFSELRITSA 340
Cdd:PRK12316 2201 --AHEQWFH--PLLNGARVLIRDDEL-------WDPEQLYDEMERHGVTILDFPPVYLQQLAEHAER-DGRPPAVRVYCF 2268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 341 GGMALQTSVADR-WQKLTGNKPAEGYGLSE---TSPVLCSNTVTEEGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEI 416
Cdd:PRK12316 2269 GGEAVPAASLRLaWEALRPVYLFNGYGPTEavvTPLLWKCRPQDPCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGEL 2348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 417 WAKGPQVFGGYYNRPDESA-KVLEDGW-------FKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPG 488
Cdd:PRK12316 2349 YLGGEGLARGYLNRPGLTAeRFVPDPFsasgerlYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPA 2428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 489 VLEVACVGVpNEKSGETVKIFVVKKDEA-LTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREEELAKLK 567
Cdd:PRK12316 2429 VREAVVVAQ-DGASGKQLVAYVVPDDAAeDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLR 2507
|
.
gi 518832993 568 K 568
Cdd:PRK12316 2508 Q 2508
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
204-496 |
2.50e-20 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 95.09 E-value: 2.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 204 PLKpvaiKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMKPAGVP-DGQGIIVAALPLYHVYALTTNALASLK 282
Cdd:PLN02614 218 PIK----KKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANAAlTVKDVYLSYLPLAHIFDRVIEECFIQH 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 283 SGSMNLLitnPRDLNAFIDDLKKYKITAFTG----LNTLYNGLLNH---------------------------------P 325
Cdd:PLN02614 294 GAAIGFW---RGDVKLLIEDLGELKPTIFCAvprvLDRVYSGLQKKlsdggflkkfvfdsafsykfgnmkkgqshveasP 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 326 RINEVDFSEL--------RITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETspvlCSNTVT---EEGNRVGTIGIPWP 394
Cdd:PLN02614 371 LCDKLVFNKVkqglggnvRIILSGAAPLASHVESFLRVVACCHVLQGYGLTES----CAGTFVslpDELDMLGTVGPPVP 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 395 ST--YMKCVTEDGTEAALGEP-GEIWAKGPQVFGGYYNRPDESAKVLEDGWFKTGDIGVMTADGYFKIVDRKKDMI-LVS 470
Cdd:PLN02614 447 NVdiRLESVPEMEYDALASTPrGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFkLSQ 526
|
330 340
....*....|....*....|....*.
gi 518832993 471 GFNVYPNEIEEVVSQCPGVLEVACVG 496
Cdd:PLN02614 527 GEYVAVENIENIYGEVQAVDSVWVYG 552
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
35-558 |
4.76e-20 |
|
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: 93.27 E-value: 4.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 35 LIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPL 114
Cdd:cd17644 5 LFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQS-LGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 115 YtPREmqhqfndsgakaivilanfagNLEKILSQTAIEhVIVTQigdllgfpkklivnavvkyvkkmvpayhlpgaisfg 194
Cdd:cd17644 84 Y-PQE---------------------RLTYILEDAQIS-VLLTQ------------------------------------ 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 195 dalsrgsrqplkpvaikNTDLAFVQYTGGTTGVSKGAALTHRNIISNVI-CQDEWMKPAGVPDGQ----GIIVAALPLYh 269
Cdd:cd17644 105 -----------------PENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHgLIKEYGITSSDRVLQfasiAFDVAAEEIY- 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 270 vyalttnalASLKSGSMNLLITNP--RDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVDF-SELRITSAGGMALQ 346
Cdd:cd17644 167 ---------VTLLSGATLVLRPEEmrSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLpSSLRLVIVGGEAVQ 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 347 TSVADRWQKLTGNKPA--EGYGLSE---TSPVLCSNTVTEEGNRVGTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGP 421
Cdd:cd17644 238 PELVRQWQKNVGNFIQliNVYGPTEatiAATVCRLTQLTERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGV 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 422 QVFGGYYNRPDESA-KVLEDGW--------FKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVlEV 492
Cdd:cd17644 318 GLARGYLNRPELTAeKFISHPFnsseserlYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDV-KT 396
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518832993 493 ACVGVPNEKSGET--VKIFVVKKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPL 558
Cdd:cd17644 397 AVVIVREDQPGNKrlVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
75-450 |
8.52e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 93.19 E-value: 8.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 75 DLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTprEMQHQFN------DSGAKAIVI---LANFAGNLEkI 145
Cdd:PRK12582 99 DLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYS--LMSHDHAklkhlfDLVKPRVVFaqsGAPFARALA-A 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 146 LSQTAIEHVIVTQIGDLLGfpkklivnavvkyvkkmvpayhlpgAISFGDALS-------RGSRQPLKPVAIkntdlAFV 218
Cdd:PRK12582 176 LDLLDVTVVHVTGPGEGIA-------------------------SIAFADLAAtpptaavAAAIAAITPDTV-----AKY 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 219 QYTGGTTGVSKGAALTHRNIISNvICQDEWMKPAGVPDGQGIIVAALPLYHVYALTTNALASLKSGSmNLLITNPRDLNA 298
Cdd:PRK12582 226 LFTSGSTGMPKAVINTQRMMCAN-IAMQEQLRPREPDPPPPVSLDWMPWNHTMGGNANFNGLLWGGG-TLYIDDGKPLPG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 299 FID----DLKKYKITAF----TGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSVADRWQKL----TGNK-P-AEG 364
Cdd:PRK12582 304 MFEetirNLREISPTVYgnvpAGYAMLAEAMEKDDALRRSFFKNLRLMAYGGATLSDDLYERMQALavrtTGHRiPfYTG 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 365 YGLSETSPVLCSNT-VTEegnRVGTIGIPWPSTYMKCvtedgteAALGEPGEIWAKGPQVFGGYYNRPDESAKVL-EDGW 442
Cdd:PRK12582 384 YGATETAPTTTGTHwDTE---RVGLIGLPLPGVELKL-------APVGDKYEVRVKGPNVTPGYHKDPELTAAAFdEEGF 453
|
....*...
gi 518832993 443 FKTGDIGV 450
Cdd:PRK12582 454 YRLGDAAR 461
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
202-497 |
2.68e-19 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 91.37 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 202 RQPLKPVAikNTDLAFVQYTGGTTGVSKGAALTHRNIISNVicqdewmkpAGVPDGQGIIVAA------LPLYHVYALTT 275
Cdd:PRK05851 143 SASLTPPD--SGGPAVLQGTAGSTGTPRTAILSPGAVLSNL---------RGLNARVGLDAATdvgcswLPLYHDMGLAF 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 276 NALASLKSGSMNLLITNPRDLNAF--IDDLKKYKITAFTGLNTLYNGLLNHP-RINEVDFSELRITSAGGMALQTSVADR 352
Cdd:PRK05851 212 LLTAALAGAPLWLAPTTAFSASPFrwLSWLSDSRATLTAAPNFAYNLIGKYArRVSDVDLGALRVALNGGEPVDCDGFER 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 353 WqkLTGNKP--------AEGYGLSETSpvlCSNTVTEEG----------------NRVGTIGIPWPSTYMKCVTEDGTEA 408
Cdd:PRK05851 292 F--ATAMAPfgfdagaaAPSYGLAEST---CAVTVPVPGiglrvdevttddgsgaRRHAVLGNPIPGMEVRISPGDGAAG 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 409 ALG-EPGEIWAKGPQVFGGYYNRPDESAkvleDGWFKTGDIGVMTADGyFKIVDRKKDMILVSGFNVYPNEIEEVVSQCP 487
Cdd:PRK05851 367 VAGrEIGEIEIRGASMMSGYLGQAPIDP----DDWFPTGDLGYLVDGG-LVVCGRAKELITVAGRNIFPTEIERVAAQVR 441
|
330
....*....|
gi 518832993 488 GVLEVACVGV 497
Cdd:PRK05851 442 GVREGAVVAV 451
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
414-560 |
3.67e-19 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 90.44 E-value: 3.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 414 GEIWAKGPQVFGGYYNRPDESAKVledgwFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVA 493
Cdd:PRK07445 302 GNITIQAQSLALGYYPQILDSQGI-----FETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVC 376
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518832993 494 CVGVPNEKSGETVKIFVVKKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLRE 560
Cdd:PRK07445 377 VLGLPDPHWGEVVTAIYVPKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
30-564 |
6.57e-19 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 91.26 E-value: 6.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 30 TSLAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVV 109
Cdd:PRK10252 458 TTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLR-ERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWL 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 110 NTNPLYTPREMQHQFNDSGAKAIVILANFAGNlekilsqtaiehvivtqigdllgFPkklivnavvkyvkkmvpayHLPG 189
Cdd:PRK10252 537 PLDTGYPDDRLKMMLEDARPSLLITTADQLPR-----------------------FA-------------------DVPD 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 190 AI--SFGDALSRGSRQPLKPVaiKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVicqdEWMKpagvpdgqgiivaalpl 267
Cdd:PRK10252 575 LTslCYNAPLAPQGAAPLQLS--QPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRL----LWMQ----------------- 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 268 yHVYALTTNALASLK-----------------SGSmNLLITNP---RD---LNAFIDDlkkYKIT----------AFTGL 314
Cdd:PRK10252 632 -NHYPLTADDVVLQKtpcsfdvsvweffwpfiAGA-KLVMAEPeahRDplaMQQFFAE---YGVTtthfvpsmlaAFVAS 706
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 315 NTlyngllnhPRINEVDFSELRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETS------PVLCSNTVTEEGNRVgT 388
Cdd:PRK10252 707 LT--------PEGARQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAvdvswyPAFGEELAAVRGSSV-P 777
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 389 IGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRPDESA-KVLEDGW------FKTGDIGVMTADGYFKIVD 461
Cdd:PRK10252 778 IGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTAsRFIADPFapgermYRTGDVARWLDDGAVEYLG 857
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 462 RKKDMILVSGFNVYPNEIEEVVSQCPGVLEV---ACVGVPNEKSG----ETVKIFVVKKDEALTEDSITRYCRENLTAYK 534
Cdd:PRK10252 858 RSDDQLKIRGQRIELGEIDRAMQALPDVEQAvthACVINQAAATGgdarQLVGYLVSQSGLPLDTSALQAQLRERLPPHM 937
|
570 580 590
....*....|....*....|....*....|
gi 518832993 535 VPKHIEFRTELPKSNVGKILRRPLREEELA 564
Cdd:PRK10252 938 VPVVLLQLDQLPLSANGKLDRKALPLPELK 967
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
48-556 |
1.36e-18 |
|
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: 88.61 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 48 AYACMGKQITFSELDTLSQQFASFLQNDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDS 127
Cdd:cd17648 5 AVVYGDKRLTYRELNERANRLAHYLLSVAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 128 GAKaivilanfagnlekilsqtaiehVIVTQIgdllgfpkklivnavvkyvkkmvpayhlpgaisfgdalsrgsrqplkp 207
Cdd:cd17648 85 GAR-----------------------VVITNS------------------------------------------------ 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 208 vaiknTDLAFVQYTGGTTGVSKGAALTHRNIISnviCQDEWMKPAGVPDGQGIIVAALPLY----HVYALTTnalaSLKS 283
Cdd:cd17648 94 -----TDLAYAIYTSGTTGKPKGVLVEHGSVVN---LRTSLSERYFGRDNGDEAVLFFSNYvfdfFVEQMTL----ALLN 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 284 GSmNLLITNPRDL---NAFIDDLKKYKITAFTGLNTLyngllnhprINEVDFSE---LRITSAGGMALQTSVADRWQKLT 357
Cdd:cd17648 162 GQ-KLVVPPDEMRfdpDRFYAYINREKVTYLSGTPSV---------LQQYDLARlphLKRVDAAGEEFTAPVFEKLRSRF 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 358 GNKPAEGYGLSETSpVLCSNTVTEEGNRV-GTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNRPD---- 432
Cdd:cd17648 232 AGLIINAYGPTETT-VTNHKRFFPGDQRFdKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPEltae 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 433 -------ESAKVLEDG----WFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVG--VPN 499
Cdd:cd17648 311 rflpnpfQTEQERARGrnarLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAkeDAS 390
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518832993 500 EKSGETVKIFV---VKKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKI-LRR 556
Cdd:cd17648 391 QAQSRIQKYLVgyyLPEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLdVRA 451
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
34-511 |
1.64e-18 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 88.80 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 34 ALIEEGVKRFSSAPAYacmgKQITFSELDTLSQQFASFLqNDLKLQKGDRiAIQM--PNLLQYPIaMFGALRAGLTVVNT 111
Cdd:PRK09274 24 AVAVPGGRGADGKLAY----DELSFAELDARSDAIAHGL-NAAGIGRGMR-AVLMvtPSLEFFAL-TFALFKAGAVPVLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 112 NPlytprEMqhqfndsGAKaivilanfagNLEKILSQTAIEHVI---VTQIGD-LLGFPKKLIVNAVVkyvkkmVPAYHL 187
Cdd:PRK09274 97 DP-----GM-------GIK----------NLKQCLAEAQPDAFIgipKAHLARrLFGWGKPSVRRLVT------VGGRLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 188 PGAISFGDALSRGSRQPLKPVAIKNTDLAFVQYTGGTTGVSKGAALTHRNI---ISNVicQDEW-MKPAGVpDgqgiiva 263
Cdd:PRK09274 149 WGGTTLATLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFeaqIEAL--REDYgIEPGEI-D------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 264 aLPLYHVYALTTNAL--ASL-------KSGSMNllitnPRDLNAFIDdlkKYKITAFTGLNTLYNGLLNHPRINEVDFSE 334
Cdd:PRK09274 219 -LPTFPLFALFGPALgmTSVipdmdptRPATVD-----PAKLFAAIE---RYGVTNLFGSPALLERLGRYGEANGIKLPS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 335 L-RITSAGGMAlQTSVADRWQKLTgNKPAE---GYGLSETSPVlCSNTVTE---------------------EGNRVGTI 389
Cdd:PRK09274 290 LrRVISAGAPV-PIAVIERFRAML-PPDAEiltPYGATEALPI-SSIESREilfatraatdngagicvgrpvDGVEVRII 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 390 GI---PWPSTymkcvtEDGTEAALGEPGEIWAKGPQVFGGYYNRP--DESAKVLEDG---WFKTGDIGVMTADGYFKIVD 461
Cdd:PRK09274 367 AIsdaPIPEW------DDALRLATGEIGEIVVAGPMVTRSYYNRPeaTRLAKIPDGQgdvWHRMGDLGYLDAQGRLWFCG 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 518832993 462 RKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPneKSGETVKIFVV 511
Cdd:PRK09274 441 RKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVG--VPGAQRPVLCV 488
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
214-561 |
2.55e-18 |
|
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: 87.87 E-value: 2.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 214 DLAFVQYTGGTTGVSKGAALTHRN--IISNVICQDEWMKPagvPDGqgiIVAALPLYHVYALTTNALASLKSGSmNLLIT 291
Cdd:cd05937 88 DPAILIYTSGTTGLPKAAAISWRRtlVTSNLLSHDLNLKN---GDR---TYTCMPLYHGTAAFLGACNCLMSGG-TLALS 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 292 NPRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRinEVDFSELRITSAGGMALQTSVADRWQKlTGNKPAEGYGLSETS 371
Cdd:cd05937 161 RKFSASQFWKDVRDSGATIIQYVGELCRYLLSTPP--SPYDRDHKVRVAWGNGLRPDIWERFRE-RFNVPEIGEFYAATE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 372 PVLCSNTVTEEGNRVGTIG-----IPW------------PST---YMKCVTEDGTEAALGEPGEIWAKGP----QVFGGY 427
Cdd:cd05937 238 GVFALTNHNVGDFGAGAIGhhgliRRWkfenqvvlvkmdPETddpIRDPKTGFCVRAPVGEPGEMLGRVPfknrEAFQGY 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 428 YNRPDESAK-----VLEDG--WFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGV--P 498
Cdd:cd05937 318 LHNEDATESklvrdVFRKGdiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVkvP 397
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518832993 499 NEKsGETVKIFVVKKDEALTEDSIT-----RYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLREE 561
Cdd:cd05937 398 GHD-GRAGCAAITLEESSAVPTEFTksllaSLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDE 464
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
53-555 |
4.96e-18 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 87.40 E-value: 4.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 53 GKQITFSELDTLSQQFASFLQNDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPRemqhqfndsgakai 132
Cdd:cd05905 12 ATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQ-------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 133 vilanfagNLEKILSQTAIeHVIVTQIGDLLGFPKKLI--VNAVVKyVKKMvpayHLPGAISFGDaLSRGSRQPLKPVAI 210
Cdd:cd05905 78 --------QLGFLLGTCKV-RVALTVEACLKGLPKKLLksKTAAEI-AKKK----GWPKILDFVK-IPKSKRSKLKKWGP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 211 K----NTDLAFVQYTGGTTGVSKGAALTHRNIISnvICQDEWMKPAGVPDGQgiIVAALPLYHVYALTTNALASLKSG-- 284
Cdd:cd05905 143 HpptrDGDTAYIEYSFSSDGSLSGVAVSHSSLLA--HCRALKEACELYESRP--LVTVLDFKSGLGLWHGCLLSVYSGhh 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 285 ----SMNLLITNPRdlnAFIDDLKKYKI-TAFTGLNTLYNGLLNHPRINE------VDFSELR-ITSAGGMALQTSVADR 352
Cdd:cd05905 219 tiliPPELMKTNPL---LWLQTLSQYKVrDAYVKLRTLHWCLKDLSSTLAslknrdVNLSSLRmCMVPCENRPRISSCDS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 353 WQKLTGNKP-------------------AEGYGLSETSPVLCS---------NTVTEEGNRVGTI---GIPWPSTYMKCV 401
Cdd:cd05905 296 FLKLFQTLGlspravstefgtrvnpficWQGTSGPEPSRVYLDmralrhgvvRLDERDKPNSLPLqdsGKVLPGAQVAIV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 402 TEDGTEAAL-GEPGEIWAKGPQVFGGYYNRPDE-------------SAKVLEDGWFKTGDIGVM------TADGYFKI-- 459
Cdd:cd05905 376 NPETKGLCKdGEIGEIWVNSPANASGYFLLDGEtndtfkvfpstrlSTGITNNSYARTGLLGFLrptkctDLNVEEHDll 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 460 --VDRKKDMILVSGFNVYPNEIEEVVSQC-PGVLEVA-------------CVGVPNEKSGETVKIFVVkkdEALTEDSIT 523
Cdd:cd05905 456 fvVGSIDETLEVRGLRHHPSDIEATVMRVhPYRGRCAvfsitglvvvvaeQPPGSEEEALDLVPLVLN---AILEEHQVI 532
|
570 580 590
....*....|....*....|....*....|..
gi 518832993 524 RYCrenlTAYKVPKHiefrteLPKSNVGKILR 555
Cdd:cd05905 533 VDC----VALVPPGS------LPKNPLGEKQR 554
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
29-555 |
1.28e-17 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 86.33 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 29 YTSLAALIEEGVKRFSSAPAYAC--MGKQI--TFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRA 104
Cdd:PTZ00237 62 YNVLDIHVKNPLKRDQDALIYECpyLKKTIklTYYQLYEKVCEFSRVLLN-LNISKNDNVLIYMANTLEPLIAMLSCARI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 105 GLTVVNTNPLYTPREMQHQFNDSGAKAIvILANFAGNLEKILSQT-----AIE-------HVIVTqigdllgFPKKLIVN 172
Cdd:PTZ00237 141 GATHCVLFDGYSVKSLIDRIETITPKLI-ITTNYGILNDEIITFTpnlkeAIElstfkpsNVITL-------FRNDITSE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 173 AVVKYVKKMVPayhLPGAISFGDALSRGSRQPLKP----VAIKNTDLAFVQYTGGTTGVSKGAAlthRNIISNVIC---Q 245
Cdd:PTZ00237 213 SDLKKIETIPT---IPNTLSWYDEIKKIKENNQSPfyeyVPVESSHPLYILYTSGTTGNSKAVV---RSNGPHLVGlkyY 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 246 DEWMKPAGVP------DGQGIIVAALPLYhvyalttnalASLKSGSMNLL----ITNPRDLNAFI-DDLKKYKIT-AFTG 313
Cdd:PTZ00237 287 WRSIIEKDIPtvvfshSSIGWVSFHGFLY----------GSLSLGNTFVMfeggIIKNKHIEDDLwNTIEKHKVThTLTL 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 314 LNTLYNGLLNHPRINEV----DFSELRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSET--SPVLCSNTVTEEGNrvg 387
Cdd:PTZ00237 357 PKTIRYLIKTDPEATIIrskyDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGYGQTEIgiTYLYCYGHINIPYN--- 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 388 TIGIPWPSTYMKCVTEDGTEAALGEPGEIWAK--GPQVFGGYYNRPDESAKVLED---GWFKTGDIGVMTADGYFKIVDR 462
Cdd:PTZ00237 434 ATGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpMPPSFATTFYKNDEKFKQLFSkfpGYYNSGDLGFKDENGYYTIVSR 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 463 KKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKS-GETVKIFVVKKDEALT-------EDSITRYCRENLTAYK 534
Cdd:PTZ00237 514 SDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCyNVPIGLLVLKQDQSNQsidlnklKNEINNIITQDIESLA 593
|
570 580
....*....|....*....|.
gi 518832993 535 VPKHIEFRTELPKSNVGKILR 555
Cdd:PTZ00237 594 VLRKIIIVNQLPKTKTGKIPR 614
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
54-447 |
3.33e-17 |
|
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: 84.79 E-value: 3.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 54 KQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTprEMQHQFndsgAKaiv 133
Cdd:cd05921 24 RRVTYAEALRQVRAIAQGLL-DLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYS--LMSQDL----AK--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 134 iLANFAGNLEK--ILSQTAiehvivTQIGDLLGFPKKLIVNAVVKYvkkmvpaYHLPG--AISFGDALSRGSRQPLKPV- 208
Cdd:cd05921 94 -LKHLFELLKPglVFAQDA------APFARALAAIFPLGTPLVVSR-------NAVAGrgAISFAELAATPPTAAVDAAf 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 209 -AIKNTDLAFVQYTGGTTGVSKGAALTHRNIISNVICQDE-WMKPAGVPDgqgIIVAALPLYHVYALTTNALASLKSGSm 286
Cdd:cd05921 160 aAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQtYPFFGEEPP---VLVDWLPWNHTFGGNHNFNLVLYNGG- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 287 NLLITN----PRDLNAFIDDLKKYKITAF----TGLNTLYNGLLNHPRINEVDFSELRITSAGGMALQTSVADRWQKL-- 356
Cdd:cd05921 236 TLYIDDgkpmPGGFEETLRNLREISPTVYfnvpAGWEMLVAALEKDEALRRRFFKRLKLMFYAGAGLSQDVWDRLQALav 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 357 --TGNKP--AEGYGLSETSPvLCSNTvTEEGNRVGTIGIPWPSTYMKCVTEDGTEaalgepgEIWAKGPQVFGGYYNRPD 432
Cdd:cd05921 316 atVGERIpmMAGLGATETAP-TATFT-HWPTERSGLIGLPAPGTELKLVPSGGKY-------EVRVKGPNVTPGYWRQPE 386
|
410
....*....|....*.
gi 518832993 433 ESAKVL-EDGWFKTGD 447
Cdd:cd05921 387 LTAQAFdEEGFYCLGD 402
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
14-558 |
7.77e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 84.83 E-value: 7.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 14 AHYPPGVPHDINP--DSYTS---LAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLqndlkLQKG---DR-I 84
Cdd:PRK12467 3074 AHERRQVLHAWNAtaAAYPSerlVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRL-----IAIGvgpDVlV 3148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 85 AIQMPNLLQYPIAMFGALRAGLTVVNTNPLYtPRE-MQHQFNDSGAKAIVILANFagnLEKiLSQTAIEHVIVTQIGDLL 163
Cdd:PRK12467 3149 GVAVERSVEMIVALLAVLKAGGAYVPLDPEY-PRErLAYMIEDSGVKLLLTQAHL---LEQ-LPAPAGDTALTLDRLDLN 3223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 164 GFPKklivnavvkyvkkmvpayHLPGAISFGDalsrgsrqplkpvaikntDLAFVQYTGGTTGVSKGAALTHrNIISNVI 243
Cdd:PRK12467 3224 GYSE------------------NNPSTRVMGE------------------NLAYVIYTSGSTGKPKGVGVRH-GALANHL 3266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 244 CqdeWMKPAGVPDGQGIIVAALPlYHVYALTTNALASLKSGSMNLLITNP-RDLNAFIDDLKKYKITAFTGLNTLYNGLL 322
Cdd:PRK12467 3267 C---WIAEAYELDANDRVLLFMS-FSFDGAQERFLWTLICGGCLVVRDNDlWDPEELWQAIHAHRISIACFPPAYLQQFA 3342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 323 NHPRINevDFSELRITSAGGMALQT-SVADRWQKLTGNKPAEGYGLSETSPVLCSNTVTEEGNRVGT---IGIPWPStyM 398
Cdd:PRK12467 3343 EDAGGA--DCASLDIYVFGGEAVPPaAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPyapIGRPVAG--R 3418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 399 KCVTEDGT--EAALGEPGEIWAKGPQVFGGYYNRPDESA-KVLEDGW-------FKTGDIGVMTADGYFKIVDRKKDMIL 468
Cdd:PRK12467 3419 SIYVLDGQlnPVPVGVAGELYIGGVGLARGYHQRPSLTAeRFVADPFsgsggrlYRTGDLARYRADGVIEYLGRIDHQVK 3498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 469 VSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKS 548
Cdd:PRK12467 3499 IRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLG 3578
|
570
....*....|
gi 518832993 549 NVGKILRRPL 558
Cdd:PRK12467 3579 PNGKVDRKAL 3588
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
443-559 |
9.66e-17 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 83.46 E-value: 9.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 443 FKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKDEALTEDSI 522
Cdd:PRK10524 475 YSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADRE 554
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 518832993 523 TRYCRE---------NLTAYKVPKHIEFRTELPKSNVGKILRRPLR 559
Cdd:PRK10524 555 ARLALEkeimalvdsQLGAVARPARVWFVSALPKTRSGKLLRRAIQ 600
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
221-447 |
1.14e-16 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 83.39 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 221 TGGTTGVSKGAALTHRNIISNVIcqdewMKPAGVP---DGQGIIVAALPLYHVYALTTN---ALASlkSGSMnllitnpr 294
Cdd:PRK08180 217 TSGSTGLPKAVINTHRMLCANQQ-----MLAQTFPflaEEPPVLVDWLPWNHTFGGNHNlgiVLYN--GGTL-------- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 295 dlnaFIDD--------------LKKYKITAFTGLNTLYNGLLNH----PRINEVDFSELRITSAGGMALQTSVADRWQKL 356
Cdd:PRK08180 282 ----YIDDgkptpggfdetlrnLREISPTVYFNVPKGWEMLVPAlerdAALRRRFFSRLKLLFYAGAALSQDVWDRLDRV 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 357 ----TGNKP--AEGYGLSETSPVLCSntVTEEGNRVGTIGIPWPSTYMKCVTEDGTEaalgepgEIWAKGPQVFGGYYNR 430
Cdd:PRK08180 358 aeatCGERIrmMTGLGMTETAPSATF--TTGPLSRAGNIGLPAPGCEVKLVPVGGKL-------EVRVKGPNVTPGYWRA 428
|
250
....*....|....*...
gi 518832993 431 PDESAKVL-EDGWFKTGD 447
Cdd:PRK08180 429 PELTAEAFdEEGYYRSGD 446
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
32-560 |
1.73e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 80.60 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 32 LAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNT 111
Cdd:PRK05691 1133 LPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLR-DKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPL 1211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 112 NPLYTPREMQHQFNDSGAKaivILANFAGNLEKiLSQTAIEHVIVTQIGDLLGFPKKlivnavvkyvkkmVPAYHLPGai 191
Cdd:PRK05691 1212 DPDYPAERLAYMLADSGVE---LLLTQSHLLER-LPQAEGVSAIALDSLHLDSWPSQ-------------APGLHLHG-- 1272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 192 sfgdalsrgsrqplkpvaiknTDLAFVQYTGGTTGVSKGAALTHRNIISNVicqdEWMKPAGVPDGQGIIVAALPL-YHV 270
Cdd:PRK05691 1273 ---------------------DNLAYVIYTSGSTGQPKGVGNTHAALAERL----QWMQATYALDDSDVLMQKAPIsFDV 1327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 271 ------YALTTNAlaslksgsmNLLITNP---RDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINEVdfSELRITSAG 341
Cdd:PRK05691 1328 svwecfWPLITGC---------RLVLAGPgehRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAAC--TSLRRLFSG 1396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 342 GMALQTSVADR-WQKLTGNKPAEGYGLSETS-PVLCSNTVTEEGNRVgTIGIPWPSTYMKCVTEDGTEAALGEPGEIWAK 419
Cdd:PRK05691 1397 GEALPAELRNRvLQRLPQVQLHNRYGPTETAiNVTHWQCQAEDGERS-PIGRPLGNVLCRVLDAELNLLPPGVAGELCIG 1475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 420 GPQVFGGYYNRPDESAKVL------EDG--WFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVlE 491
Cdd:PRK05691 1476 GAGLARGYLGRPALTAERFvpdplgEDGarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGV-A 1554
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 492 VACVGVPNEKSG-ETVKIFVVKKDEALTEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLRE 560
Cdd:PRK05691 1555 QAAVLVREGAAGaQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPE 1624
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
201-470 |
5.90e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 78.22 E-value: 5.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 201 SRQPLKPVAIKNTDLAFVQ---YTGGTTGVSKGAALTHRNIISNVICQDEW-MKPAGVPDGQgiiVAALPLYHVYALTTN 276
Cdd:PTZ00342 289 TKNKTTNYKIQNEDPDFITsivYTSGTSGKPKGVMLSNKNLYNTVVPLCKHsIFKKYNPKTH---LSYLPISHIYERVIA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 277 ALASLKSGSMNLLitnPRDLNAFIDDLKKYKITAFTGL----NTLYNGLL----NHPRI---------------NEVDFS 333
Cdd:PTZ00342 366 YLSFMLGGTINIW---SKDINYFSKDIYNSKGNILAGVpkvfNRIYTNIMteinNLPPLkrflvkkilslrksnNNGGFS 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 334 E-------------------LRITSAGGMALQTSVADRWQKLTGNKPAEGYGLSETS-PVLCSNTvteEGNRVGTIGIPW 393
Cdd:PTZ00342 443 KflegithisskikdkvnpnLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTgPIFVQHA---DDNNTESIGGPI 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 394 -PSTYMKCVTEDGTEAALGEP-GEIWAKGPQVFGGYYNRPDESAKVL-EDGWFKTGDIGVMTADGYFKIVDRKKDMILVS 470
Cdd:PTZ00342 520 sPNTKYKVRTWETYKATDTLPkGELLIKSDSIFSGYFLEKEQTKNAFtEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLS 599
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
214-512 |
8.61e-14 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 73.65 E-value: 8.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 214 DLAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMKPAGvpdgQGIIVAALPLYHVYA----LTT--NALASLKSGSmn 287
Cdd:cd05910 86 EPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRP----GEVDLATFPLFALFGpalgLTSviPDMDPTRPAR-- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 288 lliTNPRDLNAFIddlKKYKITAFTGLNTLYNGLLNHPRINEVDFSELR-ITSAGGmALQTSVADRWQKLT--GNKPAEG 364
Cdd:cd05910 160 ---ADPQKLVGAI---RQYGVSIVFGSPALLERVARYCAQHGITLPSLRrVLSAGA-PVPIALAARLRKMLsdEAEILTP 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 365 YGLSETSPV--------LCSNTVTEEGNRVGTIGIPWPSTYMKCVT---------EDGTEAALGEPGEIWAKGPQVFGGY 427
Cdd:cd05910 233 YGATEALPVssigsrelLATTTAATSGGAGTCVGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTVTPTY 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 428 YNRPDESA--KVLEDG---WFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVpnEKS 502
Cdd:cd05910 313 VNRPVATAlaKIDDNSegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV--GKP 390
|
330
....*....|
gi 518832993 503 GETVKIFVVK 512
Cdd:cd05910 391 GCQLPVLCVE 400
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
439-559 |
4.47e-13 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 72.10 E-value: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 439 EDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKDEALT 518
Cdd:PRK00174 481 FKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEP 560
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 518832993 519 EDSITR----YCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLR 559
Cdd:PRK00174 561 SDELRKelrnWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILR 605
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
195-544 |
1.23e-12 |
|
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: 70.56 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 195 DALSRGSRQ--PLKPVAIKNTD--LAFVQYTGGTTGVSKGAALTHRNIisnvicQDEWMKPAGVPDG---QGIIVAALPL 267
Cdd:cd17632 201 TLIAVRGRDlpPAPLFRPEPDDdpLALLIYTSGSTGTPKGAMYTERLV------ATFWLKVSSIQDIrppASITLNFMPM 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 268 YHVYAltTNAL-ASLKSGSMNLLITNPrDLNAFIDDLKKYKITAFtglntlynGLLnhPRINEVDF----SELRITSAGG 342
Cdd:cd17632 275 SHIAG--RISLyGTLARGGTAYFAAAS-DMSTLFDDLALVRPTEL--------FLV--PRVCDMLFqryqAELDRRSVAG 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 343 M---ALQTSV-ADRWQKLTGNKPA--------------------------EGYGLSETSPVLcsntvteegnRVGTIGIP 392
Cdd:cd17632 342 AdaeTLAERVkAELRERVLGGRLLaavcgsaplsaemkafmeslldldlhDGYGSTEAGAVI----------LDGVIVRP 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 393 wPSTYMKCVteDGTEaaLG-----EP---GEIWAKGPQVFGGYYNRPDESAKVL-EDGWFKTGDIGVMTADGYFKIVDRK 463
Cdd:cd17632 412 -PVLDYKLV--DVPE--LGyfrtdRPhprGELLVKTDTLFPGYYKRPEVTAEVFdEDGFYRTGDVMAELGPDRLVYVDRR 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 464 KDMI-LVSGFNVYPNEIEEVVSQCPGVLEVACVGvpnekSGETVKIF--VVKKDEALTE-----------DSITRYCREN 529
Cdd:cd17632 487 NNVLkLSQGEFVTVARLEAVFAASPLVRQIFVYG-----NSERAYLLavVVPTQDALAGedtarlraalaESLQRIAREA 561
|
410
....*....|....*.
gi 518832993 530 -LTAYKVPKHIEFRTE 544
Cdd:cd17632 562 gLQSYEIPRDFLIETE 577
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
214-567 |
4.98e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 65.96 E-value: 4.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 214 DLAFVQYTGGTTGVSKGAALTHRNIISNVICQdewmkpagVP----DGQGIIVA--------------ALPLYHV-YALT 274
Cdd:PRK05691 3870 NLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSK--------VPylalSEADVIAQtasqsfdisvwqflAAPLFGArVEIV 3941
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 275 TNALAslksgsmnllitnpRDLNAFIDDLKKYKITAFTGLNTLYNGLLNHPRINevdFSELRITSAGGMALQTSVADRW- 353
Cdd:PRK05691 3942 PNAIA--------------HDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQA---LDGLRWMLPTGEAMPPELARQWl 4004
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 354 QKLTGNKPAEGYGLSETSPVLCSNTVTEEGNRvGT---IGIPWPSTYMKCVTEDGTEAALGEPGEIWAKGPQVFGGYYNR 430
Cdd:PRK05691 4005 QRYPQIGLVNAYGPAECSDDVAFFRVDLASTR-GSylpIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGD 4083
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 431 PDESAKVL--------EDGWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVAcVGVPNEKS 502
Cdd:PRK05691 4084 PLRTALAFvphpfgapGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAA-VAVQEGVN 4162
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518832993 503 GETVKIFVVKKDEALTEDSITRYCRENLTA----YKVPKHIEFRTELPKSNVGKILRRPLREEELAKLK 567
Cdd:PRK05691 4163 GKHLVGYLVPHQTVLAQGALLERIKQRLRAelpdYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQ 4231
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
19-565 |
6.96e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 65.57 E-value: 6.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 19 GVPHDINPDSytSLAALIEEGVKRFSSAPAYACMGKQITFSELDTLSQQFASFLQnDLKLQKGDRIAIQMPNLLQYPIAM 98
Cdd:PRK05691 2179 GEAGEARLDQ--TLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALR-ERGVGPQVRVGLALERSLEMVVGL 2255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 99 FGALRAGLTVVNTNPLYTPREMQHQFNDSGakaIVILanfagnlekiLSQTAIEhvivtqigDLLGfpkklivnavvkyv 178
Cdd:PRK05691 2256 LAILKAGGAYVPLDPEYPLERLHYMIEDSG---IGLL----------LSDRALF--------EALG-------------- 2300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 179 kkmvpayHLPGAISF------GDALSRGSRQPLKPVAIKNtDLAFVQYTGGTTGVSKGAALTHRNIIsnvicqdewMKPA 252
Cdd:PRK05691 2301 -------ELPAGVARwcleddAAALAAYSDAPLPFLSLPQ-HQAYLIYTSGSTGKPKGVVVSHGEIA---------MHCQ 2363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 253 GVPDGQGIIVAALPLyHVYALTTNA-----LASLKSGSMNLLITNPR-DLNAFIDDLKKYKITAFtGLNTLYNGLLNHPR 326
Cdd:PRK05691 2364 AVIERFGMRADDCEL-HFYSINFDAaserlLVPLLCGARVVLRAQGQwGAEEICQLIREQQVSIL-GFTPSYGSQLAQWL 2441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 327 INEVDFSELRITSAGGMALqtsVADRWQKLTGN-KPA---EGYGLSET--SPVLC-SNTVTEEGNRVGTIGIPWPSTYMK 399
Cdd:PRK05691 2442 AGQGEQLPVRMCITGGEAL---TGEHLQRIRQAfAPQlffNAYGPTETvvMPLAClAPEQLEEGAASVPIGRVVGARVAY 2518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 400 CVTEDGTEAALGEPGEIWAKGPQVFGGYYNRPDESAKVL------EDG--WFKTGDIGVMTADGYFKIVDRKKDMILVSG 471
Cdd:PRK05691 2519 ILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFvadpfaADGgrLYRTGDLVRLRADGLVEYVGRIDHQVKIRG 2598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 472 FNVYPNEIEEVVSQCPGVLEVACVGVPNEkSGETVKIFVVKKDEALTEDSITR-------YCRENLTAYKVPKHIEFRTE 544
Cdd:PRK05691 2599 FRIELGEIESRLLEHPAVREAVVLALDTP-SGKQLAGYLVSAVAGQDDEAQAAlrealkaHLKQQLPDYMVPAHLILLDS 2677
|
570 580
....*....|....*....|...
gi 518832993 545 LPKSNVGKILRR--PLREEELAK 565
Cdd:PRK05691 2678 LPLTANGKLDRRalPAPDPELNR 2700
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
441-560 |
1.41e-10 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 64.15 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 441 GWFKTGDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKKD-EALTE 519
Cdd:PLN02654 513 GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEgVPYSE 592
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 518832993 520 D---SITRYCRENLTAYKVPKHIEFRTELPKSNVGKILRRPLRE 560
Cdd:PLN02654 593 ElrkSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 636
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
215-493 |
1.17e-08 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 57.48 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 215 LAFVQYTGGTTGVSKGAALTHRNIISNVICQDEWMKPAgvpdgQGIIVAALPLYHVYALTTNALASLKSGSMnLLI--TN 292
Cdd:cd17654 120 LAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNIT-----SEDILFLTSPLTFDPSVVEIFLSLSSGAT-LLIvpTS 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 293 PRDLNAFIDDL--KKYKITAFTGLNTLYNGLLNHPRINEV--DFSELRITSAGGMALQTSVADR-W-QKLTGNKPAEGYG 366
Cdd:cd17654 194 VKVLPSKLADIlfKRHRITVLQATPTLFRRFGSQSIKSTVlsATSSLRVLALGGEPFPSLVILSsWrGKGNRTRIFNIYG 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 367 LSETSPVLCSNTVTEEGNRVgTIGIPWPSTYMKCVTEDGTEaalgepgeiwAKGpQVFGGYYNR----PDESAKVLEDgW 442
Cdd:cd17654 274 ITEVSCWALAYKVPEEDSPV-QLGSPLLGTVIEVRDQNGSE----------GTG-QVFLGGLNRvcilDDEVTVPKGT-M 340
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 518832993 443 FKTGDIgVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVA 493
Cdd:cd17654 341 RATGDF-VTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCA 390
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
414-568 |
3.14e-07 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 52.95 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 414 GEIWAKGPQVFGGYYnrpdESAKVL----EDGWFKTGDIGVMtADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQCPGV 489
Cdd:PRK09029 305 GEIWLRGASLALGYW----RQGQLVplvnDEGWFATRDRGEW-QNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLV 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 490 LEVACVGVPNEKSGETvKIFVVKKDEALTEDSITRYCRENLTAYKVPkhIEF---RTELPKSNVgKILRRPLREEELAKL 566
Cdd:PRK09029 380 QQVFVVPVADAEFGQR-PVAVVESDSEAAVVNLAEWLQDKLARFQQP--VAYyllPPELKNGGI-KISRQALKEWVAQQL 455
|
..
gi 518832993 567 KK 568
Cdd:PRK09029 456 GN 457
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
390-561 |
2.64e-06 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 50.46 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 390 GIPWPStYMKCVtedgteaalgepGEIwAKGPQVFGG------------YYN-RPDESAKVLEdgwfKTGDIGVMTADGY 456
Cdd:PLN03052 543 GNPYPD-DAPCT------------GEL-ALFPLMFGAsstllnadhykvYFKgMPVFNGKILR----RHGDIFERTSGGY 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 457 FKIVDRKKDMILVSGFNVYPNEIEEV---VSQCpgVLEVACVGVPNEKSG-ETVKIFVVKKDEALTEDSITRYCRENLTA 532
Cdd:PLN03052 605 YRAHGRADDTMNLGGIKVSSVEIERVcnaADES--VLETAAIGVPPPGGGpEQLVIAAVLKDPPGSNPDLNELKKIFNSA 682
|
170 180 190
....*....|....*....|....*....|....*..
gi 518832993 533 --------YKVpKHIEFRTELPKSNVGKILRRPLREE 561
Cdd:PLN03052 683 iqkklnplFKV-SAVVIVPSFPRTASNKVMRRVLRQQ 718
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
446-561 |
6.27e-06 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 49.04 E-value: 6.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 446 GDIGVMTADGYFKIVDRKKDMILVSGFNVYPNEIEEVVSQC-PGVLEVACVGVPNEKSG-ETVKIFVVKKDEALTEDS-- 521
Cdd:PLN03051 362 GDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACDRAvAGIAETAAVGVAPPDGGpELLVIFLVLGEEKKGFDQar 441
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 518832993 522 -------ITRYCRENLTA-YKVpKHIEFRTELPKSNVGKILRRPLREE 561
Cdd:PLN03051 442 pealqkkFQEAIQTNLNPlFKV-SRVKIVPELPRNASNKLLRRVLRDQ 488
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
56-230 |
6.62e-06 |
|
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: 48.81 E-value: 6.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 56 ITFSELDTLSQQFASFLQNdLKLQKGDRIAIQMPNLLQYPIAMFGALRAGLTVVNTNPLYTPREMQHQFNDSGAKaIVIL 135
Cdd:cd05943 99 VTWAELRRRVARLAAALRA-LGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPK-VLFA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 136 AN---FAGnleKILSQTAIEHVIVTQIGDLLgfpKKLIVNAVVKYVKKMVPayHLPGAISFGDALSRGSRQPLKPVAIKN 212
Cdd:cd05943 177 VDaytYNG---KRHDVREKVAELVKGLPSLL---AVVVVPYTVAAGQPDLS--KIAKALTLEDFLATGAAGELEFEPLPF 248
|
170
....*....|....*...
gi 518832993 213 TDLAFVQYTGGTTGVSKG 230
Cdd:cd05943 249 DHPLYILYSSGTTGLPKC 266
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
443-520 |
3.75e-05 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 46.30 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 443 FKTGDIGVMTAD----GYF-----KIVDRKKDMILVSGFNVYPNEIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKK 513
Cdd:COG1541 297 YRTGDLTRLLPEpcpcGRThprigRILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVELA 376
|
....*..
gi 518832993 514 DEALTED 520
Cdd:COG1541 377 PGASLEA 383
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
478-560 |
2.86e-04 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 43.63 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518832993 478 EIEEVVSQCPGVLEVACVGVPNEKSGETVKIFVVKK-----DEALtEDSITRYCRENLTAYKVPKHIEFRTELPKSNVGK 552
Cdd:PRK03584 535 EIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAegvtlDDAL-RARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGK 613
|
....*...
gi 518832993 553 ILRRPLRE 560
Cdd:PRK03584 614 KVELPVKK 621
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
458-489 |
9.71e-03 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 38.76 E-value: 9.71e-03
10 20 30
....*....|....*....|....*....|..
gi 518832993 458 KIVDRKKDMILVSGFNVYPNEIEEVVSQCPGV 489
Cdd:cd05913 317 RITGRSDDMLIIRGVNVFPSQIEDVLLKIPGL 348
|
|
| |
