|
Name |
Accession |
Description |
Interval |
E-value |
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
1-361 |
0e+00 |
|
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: 685.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 1 MLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVGTPDAGAYFRVLAEHGVAALFTAPTAIR 80
Cdd:cd05967 258 ALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPVGTPDPGAFWRVIEKYQVNALFTAPTAIR 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 81 AIRQQDPGAALGKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPITASCVGLGNsKTPPPGQAGKS 160
Cdd:cd05967 338 AIRKEDPDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETGWPITANPVGLEP-LPIKAGSPGKP 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 161 VPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDV 240
Cdd:cd05967 417 VPGYQVQVLDEDGEPVGPNELGNIVIKLPLPPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDV 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 241 INVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEEIVKHVRQNIGPVAAFRNAVF 320
Cdd:cd05967 497 INVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEELEKELVALVREQIGPVAAFRLVIF 576
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1057503158 321 VKQLPKTRSGKIPRSALSAIVNGKPYKITSTIEDPSIFGHV 361
Cdd:cd05967 577 VKRLPKTRSGKILRRTLRKIADGEDYTIPSTIEDPSVLDEI 617
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
2-363 |
7.04e-152 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 439.55 E-value: 7.04e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 2 LHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVgTPDAGAYFRVLAEHGVAALFTAPTAIRA 81
Cdd:COG0365 213 AATTAKYVLDLKPGDVFWCTADIGWATGHSYIVYGPLLNGATVVLYEGRPD-FPDPGRLWELIEKYGVTVFFTAPTAIRA 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 82 IRQQDPgaALGKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPITASCVGlgnskTPP-PGQAGKS 160
Cdd:COG0365 292 LMKAGD--EPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPG-----LPVkPGSMGKP 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 161 VPGYNVMILDDNMQKLKARCLGNIVVKLPLPpGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDV 240
Cdd:COG0365 365 VPGYDVAVVDEDGNPVPPGEEGELVIKGPWP-GMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDV 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 241 INVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVlEEIVKHVRQNIGPVAAFRNAVF 320
Cdd:COG0365 444 INVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDELA-KELQAHVREELGPYAYPREIEF 522
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1057503158 321 VKQLPKTRSGKIPRSALSAIVNGKPYKITSTIEDPSIFGHVEE 363
Cdd:COG0365 523 VDELPKTRSGKIMRRLLRKIAEGRPLGDTSTLEDPEALDEIKE 565
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
5-367 |
7.21e-121 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 362.73 E-value: 7.21e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 5 SMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVgTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQ 84
Cdd:PRK10524 265 SMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPT-RPDAGIWWRIVEKYKVNRMFSAPTAIRVLKK 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 85 QDPgaALGKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPITASCVGLGnSKTPPPGQAGKSVPGY 164
Cdd:PRK10524 344 QDP--ALLRKHDLSSLRALFLAGEPLDEPTASWISEALGVPVIDNYWQTETGWPILAIARGVE-DRPTRLGSPGVPMYGY 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 165 NVMILDDNM-QKLKARCLGNIVVKLPLPPGAFSGLWKNQEAFKHLYFEKF-PGYYDTMDAGYMDEEGYLYVMSRVDDVIN 242
Cdd:PRK10524 421 NVKLLNEVTgEPCGPNEKGVLVIEGPLPPGCMQTVWGDDDRFVKTYWSLFgRQVYSTFDWGIRDADGYYFILGRTDDVIN 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 243 VAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRK-DINATEEQVLE---EIVKHVRQNIGPVAAFRNA 318
Cdd:PRK10524 501 VAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDsDSLADREARLAlekEIMALVDSQLGAVARPARV 580
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1057503158 319 VFVKQLPKTRSGKIPRSALSAIVNGKPYKITSTIEDPSIFGHVEEMLKQ 367
Cdd:PRK10524 581 WFVSALPKTRSGKLLRRAIQAIAEGRDPGDLTTIEDPAALQQIRQALEE 629
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
12-354 |
4.16e-107 |
|
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: 326.44 E-value: 4.16e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 12 LQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVgTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAAL 91
Cdd:cd05966 270 YHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMFEGTPT-YPDPGRYWDIVEKHKVTIFYTAPTAIRALMKF--GDEW 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 92 GKQYSLTRFKTLFVAGERCDVETLEWSKNV---FRVPVLDHWWQTETGSPITASCVGLGNSKtppPGQAGKSVPGYNVMI 168
Cdd:cd05966 347 VKKHDLSSLRVLGSVGEPINPEAWMWYYEVigkERCPIVDTWWQTETGGIMITPLPGATPLK---PGSATRPFFGIEPAI 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 169 LDDNMQKLKARCLGNIVVKLPLPpGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRI 248
Cdd:cd05966 424 LDEEGNEVEGEVEGYLVIKRPWP-GMARTIYGDHERYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 249 SAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEqVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTR 328
Cdd:cd05966 503 GTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDE-LRKELRKHVRKEIGPIATPDKIQFVPGLPKTR 581
|
330 340
....*....|....*....|....*..
gi 1057503158 329 SGKIPRSALSAIVNG-KPYKITSTIED 354
Cdd:cd05966 582 SGKIMRRILRKIAAGeEELGDTSTLAD 608
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
4-332 |
1.29e-105 |
|
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: 322.22 E-value: 1.29e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 4 WSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVGtPDAGAYFRVLAEHGVAALFTAPTAIRAIR 83
Cdd:cd17634 263 TTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNW-PTPARMWQVVDKHGVNILYTAPTAIRALM 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 84 QQDPGAALGkqYSLTRFKTLFVAGERCDVETLEWSKNVF---RVPVLDHWWQTETGSPITASCVGLGNSKTpppGQAGKS 160
Cdd:cd17634 342 AAGDDAIEG--TDRSSLRILGSVGEPINPEAYEWYWKKIgkeKCPVVDTWWQTETGGFMITPLPGAIELKA---GSATRP 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 161 VPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWKNQEaFKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDV 240
Cdd:cd17634 417 VFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGQTRTLFGDHER-FEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDV 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 241 INVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEqVLEEIVKHVRQNIGPVAAFRNAVF 320
Cdd:cd17634 496 INVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPE-LYAELRNWVRKEIGPLATPDVVHW 574
|
330
....*....|..
gi 1057503158 321 VKQLPKTRSGKI 332
Cdd:cd17634 575 VDSLPKTRSGKI 586
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
2-363 |
4.32e-101 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 311.49 E-value: 4.32e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 2 LHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVgTPDAGAYFRVLAEHGVAALFTAPTAIRA 81
Cdd:TIGR02188 266 AAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPT-YPDPGRFWEIIEKHKVTIFYTAPTAIRA 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 82 IRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEWSKNVF---RVPVLDHWWQTETGSPITASCVGLGNSKtppPGQAG 158
Cdd:TIGR02188 345 LMRL--GDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVgkeRCPIVDTWWQTETGGIMITPLPGATPTK---PGSAT 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 159 KSVPGYNVMILDDNMQKLKARCLGNI-VVKLPLpPGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRV 237
Cdd:TIGR02188 420 LPFFGIEPAVVDEEGNPVEGPGEGGYlVIKQPW-PGMLRTIYGDHERFVDTYFSPFPGYYFTGDGARRDKDGYIWITGRV 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 238 DDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEqVLEEIVKHVRQNIGPVAAFRN 317
Cdd:TIGR02188 499 DDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDE-LRKELRKHVRKEIGPIAKPDK 577
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1057503158 318 AVFVKQLPKTRSGKIPRSALSAIVNGKP--YKITSTIEDPSIFGHVEE 363
Cdd:TIGR02188 578 IRFVPGLPKTRSGKIMRRLLRKIAAGEAeiLGDTSTLEDPSVVEELIE 625
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
3-368 |
3.49e-100 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 309.38 E-value: 3.49e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 3 HWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVgTPDAGAYFRVLAEHGVAALFTAPTAIRA- 81
Cdd:PRK00174 275 AMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLMFEGVPN-YPDPGRFWEVIDKHKVTIFYTAPTAIRAl 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 82 IRQqdpGAALGKQYSLTRFKTLFVAGERCDVETLEWSKNVF---RVPVLDHWWQTETGSPITASCVGLGNSKtppPGQAG 158
Cdd:PRK00174 354 MKE---GDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVggeRCPIVDTWWQTETGGIMITPLPGATPLK---PGSAT 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 159 KSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPpGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVD 238
Cdd:PRK00174 428 RPLPGIQPAVVDEEGNPLEGGEGGNLVIKDPWP-GMMRTIYGDHERFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVD 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 239 DVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEqVLEEIVKHVRQNIGPVAAFRNA 318
Cdd:PRK00174 507 DVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDE-LRKELRNWVRKEIGPIAKPDVI 585
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1057503158 319 VFVKQLPKTRSGKIPRSALSAIVNGKPykI---TSTIEDPSIfghVEEMLKQA 368
Cdd:PRK00174 586 QFAPGLPKTRSGKIMRRILRKIAEGEE--IlgdTSTLADPSV---VEKLIEAR 633
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
9-340 |
2.19e-85 |
|
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: 265.52 E-value: 2.19e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 9 IYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPvgtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpG 88
Cdd:cd05969 124 VLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRF----DAESWYGIIERVKVTVWYTAPTAIRMLMKE--G 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 89 AALGKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPITASCVGLgnskTPPPGQAGKSVPGYNVMI 168
Cdd:cd05969 198 DELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYPCM----PIKPGSMGKPLPGVKAAV 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 169 LDDNMQKLKARCLGNIVVKlPLPPGAFSGLWKNQEAFKhLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRI 248
Cdd:cd05969 274 VDENGNELPPGTKGILALK-PGWPSMFRGIWNDEERYK-NSFID--GWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRV 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 249 SAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEqVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTR 328
Cdd:cd05969 350 GPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDE-LKEEIINFVRQKLGAHVAPREIEFVDNLPKTR 428
|
330
....*....|..
gi 1057503158 329 SGKIPRSALSAI 340
Cdd:cd05969 429 SGKIMRRVLKAK 440
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
3-339 |
3.68e-84 |
|
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: 261.89 E-value: 3.68e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 3 HWS-MSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVgtpDAGAYFRVLAEHGVAALFTAPTAIRA 81
Cdd:cd05972 109 HIPtAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRF---DAERILELLERYGVTSFCGPPTAYRM 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 82 IRQQDPgaalgKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGspitascVGLGNSKTPP--PGQAGK 159
Cdd:cd05972 186 LIKQDL-----SSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETG-------LTVGNFPDMPvkPGSMGR 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 160 SVPGYNVMILDDNMQKLKARCLGNIVVKLPlPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDD 239
Cdd:cd05972 254 PTPGYDVAIIDDDGRELPPGEEGDIAIKLP-PPGLFLGYVGDPEKTEASIRG---DYYLTGDRAYRDEDGYFWFVGRADD 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 240 VINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVlEEIVKHVRQNIGPVAAFRNAV 319
Cdd:cd05972 330 IIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELA-EELQGHVKKVLAPYKYPREIE 408
|
330 340
....*....|....*....|
gi 1057503158 320 FVKQLPKTRSGKIPRSALSA 339
Cdd:cd05972 409 FVEELPKTISGKIRRVELRD 428
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
12-354 |
5.64e-75 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 242.11 E-value: 5.64e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 12 LQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPvgtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAAL 91
Cdd:PRK04319 243 LHEDDVYWCTADPGWVTGTSYGIFAPWLNGATNVIDGGRF----SPERWYRILEDYKVTVWYTAPTAIRMLMGA--GDDL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 92 GKQYSLTRFKtlFVA--GERCDVETLEWSKNVFRVPVLDHWWQTETGSPITAscvglgNSKTPP--PGQAGKSVPGYNVM 167
Cdd:PRK04319 317 VKKYDLSSLR--HILsvGEPLNPEVVRWGMKVFGLPIHDNWWMTETGGIMIA------NYPAMDikPGSMGKPLPGIEAA 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 168 ILDDNMQKLKARCLGNIVVKLPLPpGAFSGLWKNQEAFKHlYFEkfPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHR 247
Cdd:PRK04319 389 IVDDQGNELPPNRMGNLAIKKGWP-SMMRGIWNNPEKYES-YFA--GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGER 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 248 ISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEqVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKT 327
Cdd:PRK04319 465 VGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEE-LKEEIRGFVKKGLGAHAAPREIEFKDKLPKT 543
|
330 340
....*....|....*....|....*..
gi 1057503158 328 RSGKIPRSALSAIVNGKPYKITSTIED 354
Cdd:PRK04319 544 RSGKIMRRVLKAWELGLPEGDLSTMED 570
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
5-332 |
3.41e-70 |
|
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: 222.93 E-value: 3.41e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 5 SMSSIYGLQPGEVWWAASDLGWVvGHSYICYGPLLHGNTTVLYEGkpvgtPDAGAYFRVLAEHGVAALFTAPTAIRAIRQ 84
Cdd:cd04433 31 ALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK-----FDPEAALELIEREKVTILLGVPTLLARLLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 85 QDPGAAlgkqYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPITASCVGLGNSKtppPGQAGKSVPGY 164
Cdd:cd04433 105 APESAG----YDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDARK---PGSVGRPVPGV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 165 NVMILDDNMQKLKARCLGNIVVKLPLPpgaFSGLWKNQEAFkhlYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVA 244
Cdd:cd04433 178 EVRIVDPDGGELPPGEIGELVVRGPSV---MKGYWNNPEAT---AAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 245 GHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQL 324
Cdd:cd04433 252 GENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDA----EELRAHVRERLAPYKVPRRVVFVDAL 327
|
....*...
gi 1057503158 325 PKTRSGKI 332
Cdd:cd04433 328 PRTASGKI 335
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
13-368 |
1.63e-66 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 222.08 E-value: 1.63e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 13 QPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPvGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAALG 92
Cdd:PLN02654 315 KPTDVYWCTADCGWITGHSYVTYGPMLNGATVLVFEGAP-NYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRD--GDEYV 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 93 KQYSLTRFKTLFVAGERCDVETLEWSKNVF---RVPVLDHWWQTETGSPITASCVGLGNSKtppPGQAGKSVPGYNVMIL 169
Cdd:PLN02654 392 TRHSRKSLRVLGSVGEPINPSAWRWFFNVVgdsRCPISDTWWQTETGGFMITPLPGAWPQK---PGSATFPFFGVQPVIV 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 170 DDNMQKLKARCLGNIVVKLPLPpGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRIS 249
Cdd:PLN02654 469 DEKGKEIEGECSGYLCVKKSWP-GAFRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIG 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 250 AGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEqVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRS 329
Cdd:PLN02654 548 TAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEE-LRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRS 626
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1057503158 330 GKIPRSALSAIVNGKPYKI--TSTIEDPSIfghVEEMLKQA 368
Cdd:PLN02654 627 GKIMRRILRKIASRQLDELgdTSTLADPGV---VDQLIALA 664
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
5-337 |
1.12e-61 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 204.27 E-value: 1.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 5 SMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGkpvgtPDAGAYFRVLAEHGVAALFTAPTAIRAIRQ 84
Cdd:COG0318 131 AIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPR-----FDPERVLELIERERVTVLFGVPTMLARLLR 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 85 QdPGAAlgkQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPITascVGLGNSKTPPPGQAGKSVPGY 164
Cdd:COG0318 206 H-PEFA---RYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVT---VNPEDPGERRPGSVGRPLPGV 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 165 NVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKhlyfEKFP-GYYDTMDAGYMDEEGYLYVMSRVDDVINV 243
Cdd:COG0318 279 EVRIVDEDGRELPPGEVGEIVVR---GPNVMKGYWNDPEATA----EAFRdGWLRTGDLGRLDEDGYLYIVGRKKDMIIS 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 244 AGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEeivkHVRQNIGPVAAFRNAVFVKQ 323
Cdd:COG0318 352 GGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRA----FLRERLARYKVPRRVEFVDE 427
|
330
....*....|....
gi 1057503158 324 LPKTRSGKIPRSAL 337
Cdd:COG0318 428 LPRTASGKIDRRAL 441
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
3-367 |
3.67e-61 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 207.67 E-value: 3.67e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 3 HWSMSSIYGLQpgEVWWAASDLGWVVGHSYIcYGPLLHGNTTVLYEGKPVGTPDAGAYF-RVLAEHGVAALFTAPTAIRA 81
Cdd:PTZ00237 286 YWRSIIEKDIP--TVVFSHSSIGWVSFHGFL-YGSLSLGNTFVMFEGGIIKNKHIEDDLwNTIEKHKVTHTLTLPKTIRY 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 82 IRQQDPGAA-LGKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGspiTASCVGLGNSKTPPpGQAGKS 160
Cdd:PTZ00237 363 LIKTDPEATiIRSKYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGYGQTEIG---ITYLYCYGHINIPY-NATGVP 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 161 VPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWKNQEAFKHLyFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDV 240
Cdd:PTZ00237 439 SIFIKPSILSEDGKELNVNEIGEVAFKLPMPPSFATTFYKNDEKFKQL-FSKFPGYYNSGDLGFKDENGYYTIVSRSDDQ 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 241 INVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATE---EQVLEEIVKHVRQNIGPVAAFRN 317
Cdd:PTZ00237 518 IKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQSidlNKLKNEINNIITQDIESLAVLRK 597
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1057503158 318 AVFVKQLPKTRSGKIPRSALSAIVNGKPYKITSTIEDPSIFGHVEEMLKQ 367
Cdd:PTZ00237 598 IIIVNQLPKTKTGKIPRQIISKFLNDSNYQLPDNVNDSEIFYKIKELYMK 647
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
13-339 |
3.41e-59 |
|
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: 197.65 E-value: 3.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 13 QPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVgtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpgaalG 92
Cdd:cd05971 129 RDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKF---DPKAALDLMSRYGVTTAFLPPTALKMMRQQ------G 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 93 KQYSLT--RFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSpITASCVGLGNSKtppPGQAGKSVPGYNVMILD 170
Cdd:cd05971 200 EQLKHAqvKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNL-VIGNCSALFPIK---PGSMGKPIPGHRVAIVD 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 171 DNMQKLKARCLGNIVVKLPlPPGAFSGLWKNQEAFKhlyfEKFPG-YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRIS 249
Cdd:cd05971 276 DNGTPLPPGEVGEIAVELP-DPVAFLGYWNNPSATE----KKMAGdWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIG 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 250 AGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDInATEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRS 329
Cdd:cd05971 351 PAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGE-TPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTAT 429
|
330
....*....|
gi 1057503158 330 GKIPRSALSA 339
Cdd:cd05971 430 GKIRRRELRA 439
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
11-337 |
1.71e-55 |
|
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: 187.73 E-value: 1.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 11 GLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKpvGTPDAgaYFRVLAEHGVAALFTAPTAIRAIRQQDPGAA 90
Cdd:cd05973 125 DLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGG--FSVES--TWRVIERLGVTNLAGSPTAYRLLMAAGAEVP 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 91 LGKQYSLTRFKTlfvAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPItasCVGLGNSKTPPPGQAGKSVPGYNVMILD 170
Cdd:cd05973 201 ARPKGRLRRVSS---AGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVL---ANHHALEHPVHAGSAGRAMPGWRVAVLD 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 171 DNMQKLKARCLGNIVVKLPLPPGA-FSGLWK-NQEAFKHlyfekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRI 248
Cdd:cd05973 275 DDGDELGPGEPGRLAIDIANSPLMwFRGYQLpDTPAIDG-------GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRI 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 249 SAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEqVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTR 328
Cdd:cd05973 348 GPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPA-LADELQLHVKKRLSAHAYPRTIHFVDELPKTP 426
|
....*....
gi 1057503158 329 SGKIPRSAL 337
Cdd:cd05973 427 SGKIQRFLL 435
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
12-355 |
1.96e-50 |
|
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: 178.07 E-value: 1.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 12 LQPGEVWWAASDLGWVVGhSYICYGPLLHGNTTVLYEGKPvGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAAL 91
Cdd:cd05968 275 LKPGDLLTWFTDLGWMMG-PWLIFGGLILGATMVLYDGAP-DHPKADRLWRMVEDHEITHLGLSPTLIRALKPR--GDAP 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 92 GKQYSLTRFKTLFVAGERCDVETLEWSKNVF---RVPVLDHWWQTETGSPItascvgLGNSKTPP--PGQAGKSVPGYNV 166
Cdd:cd05968 351 VNAHDLSSLRVLGSTGEPWNPEPWNWLFETVgkgRNPIINYSGGTEISGGI------LGNVLIKPikPSSFNGPVPGMKA 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 167 MILDDNMQKLKARcLGNIVVKLPLPpGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGH 246
Cdd:cd05968 425 DVLDESGKPARPE-VGELVLLAPWP-GMTRGFWRDEDRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGK 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 247 RISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEqVLEEIVKHVRQNIGPVAAFRNAVFVKQLPK 326
Cdd:cd05968 503 RVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEA-LAEELMERVADELGKPLSPERILFVKDLPK 581
|
330 340
....*....|....*....|....*....
gi 1057503158 327 TRSGKIPRSALSAIVNGKPYKITSTIEDP 355
Cdd:cd05968 582 TRNAKVMRRVIRAAYLGKELGDLSSLENP 610
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
12-337 |
3.32e-45 |
|
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: 162.66 E-value: 3.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 12 LQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVgtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPgaal 91
Cdd:cd05970 223 VREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVYDYDKF---DPKALLEKLSKYGVTTFCAPPTIYRFLIREDL---- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 92 gKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPI-TASCVglgnskTPPPGQAGKSVPGYNVMILD 170
Cdd:cd05970 296 -SRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIaTFPWM------EPKPGSMGKPAPGYEIDLID 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 171 DNMQKLKARCLGNIVVKLP--LPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRI 248
Cdd:cd05970 369 REGRSCEAGEEGEIVIRTSkgKPVGLFGGYYKDAEKTAEVWHD---GYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRI 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 249 SAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEqVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTR 328
Cdd:cd05970 446 GPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEE-LKKELQDHVKKVTAPYKYPRIVEFVDELPKTI 524
|
....*....
gi 1057503158 329 SGKIPRSAL 337
Cdd:cd05970 525 SGKIRRVEI 533
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
11-337 |
2.93e-44 |
|
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: 159.94 E-value: 2.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 11 GLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVgtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPgaa 90
Cdd:cd05928 212 DLTASDIMWNTSDTGWIKSAWSSLFEPWIQGACVFVHHLPRF---DPLVILKTLSSYPITTFCGAPTVYRMLVQQDL--- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 91 lgKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGspitascVGLGNSKTP--PPGQAGKSVPGYNVMI 168
Cdd:cd05928 286 --SSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETG-------LICANFKGMkiKPGSMGKASPPYDVQI 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 169 LDDNMQKLKARCLGNIVVKL-PLPP-GAFSGLWKNQEAFKHLYFEKFpgyYDTMDAGYMDEEGYLYVMSRVDDVINVAGH 246
Cdd:cd05928 357 IDDNGNVLPPGTEGDIGIRVkPIRPfGLFSGYVDNPEKTAATIRGDF---YLTGDRGIMDEDGYFWFMGRADDVINSSGY 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 247 RISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATE-EQVLEEIVKHVRQNIGPVAAFRNAVFVKQLP 325
Cdd:cd05928 434 RIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSHDpEQLTKELQQHVKSVTAPYKYPRKVEFVQELP 513
|
330
....*....|..
gi 1057503158 326 KTRSGKIPRSAL 337
Cdd:cd05928 514 KTVTGKIQRNEL 525
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1-334 |
4.16e-44 |
|
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: 157.77 E-value: 4.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 1 MLHWSMSSIY--GLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGkpvgtPDAGAYFRVLAEHGVAALFTAPTA 78
Cdd:cd17631 123 LLWNAVNALAalDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRK-----FDPETVLDLIERHRVTSFFLVPTM 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 79 IRAIRQQdPGAAlgkQYSLTRFKTLFVAGERCDVETLE-WSknVFRVPVLDHWWQTETGSPITASCVGLGNSKtppPGQA 157
Cdd:cd17631 198 IQALLQH-PRFA---TTDLSSLRAVIYGGAPMPERLLRaLQ--ARGVKFVQGYGMTETSPGVTFLSPEDHRRK---LGSA 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 158 GKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEA----FKHlyfekfpGYYDTMDAGYMDEEGYLYV 233
Cdd:cd17631 269 GRPVFFVEVRIVDPDGREVPPGEVGEIVVR---GPHVMAGYWNRPEAtaaaFRD-------GWFHTGDLGRLDEDGYLYI 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 234 MSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVA 313
Cdd:cd17631 339 VDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDE----DELIAHCRERLARYK 414
|
330 340
....*....|....*....|.
gi 1057503158 314 AFRNAVFVKQLPKTRSGKIPR 334
Cdd:cd17631 415 IPKSVEFVDALPRNATGKILK 435
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
9-337 |
1.55e-41 |
|
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: 150.71 E-value: 1.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 9 IYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKpvgTPDAgaYFRVLAEHGVAALFTAPTAIRAIRQQDPG 88
Cdd:cd05958 133 VLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEA---TPDL--LLSAIARYKPTVLFTAPTAYRAMLAHPDA 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 89 AalgkQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETgspitascVGLGNSKTPP---PGQAGKSVPGYN 165
Cdd:cd05958 208 A----GPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEM--------FHIFISARPGdarPGATGKPVPGYE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 166 VMILDDNMQKLKARCLGNIVVKLPlppgafSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAG 245
Cdd:cd05958 276 AKVVDDEGNPVPDGTIGRLAVRGP------TGCRYLADKRQRTYVQG--GWNITGDTYSRDPDGYFRHQGRSDDMIVSGG 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 246 HRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDInATEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLP 325
Cdd:cd05958 348 YNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGV-IPGPVLARELQDHAKAHIAPYKYPRAIEFVTELP 426
|
330
....*....|..
gi 1057503158 326 KTRSGKIPRSAL 337
Cdd:cd05958 427 RTATGKLQRFAL 438
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
11-244 |
2.47e-41 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 149.77 E-value: 2.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 11 GLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPvgTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGaa 90
Cdd:pfam00501 196 GLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFP--ALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAP-- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 91 lgKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPITasCVGLGNSKTPPPGQAGKSVPGYNVMILD 170
Cdd:pfam00501 272 --KRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVT--TPLPLDEDLRSLGSVGRPLPGTEVKIVD 347
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057503158 171 DN-MQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVA 244
Cdd:pfam00501 348 DEtGEPVPPGEPGELCVR---GPGVMKGYLNDPELTAEAFDED--GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
33-337 |
1.09e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 141.86 E-value: 1.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 33 ICYGPLLHGNTTVLyegkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQqdpgAALGKQYSLTRFKTLFVAGERCDV 112
Cdd:PRK06187 225 LPYLALMAGAKQVI-----PRRFDPENLLDLIETERVTFFFAVPTIWQMLLK----APRAYFVDFSSLRLVIYGGAALPP 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 113 ETLEWSKNVFRVPVLDHWWQTETGSPITAScvglgnsktPPPGQ----------AGKSVPGYNVMILDDNMQKLKARC-- 180
Cdd:PRK06187 296 ALLREFKEKFGIDLVQGYGMTETSPVVSVL---------PPEDQlpgqwtkrrsAGRPLPGVEARIVDDDGDELPPDGge 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 181 LGNIVVKlplPPGAFSGLWKNQEAFKhlyfEKFP-GYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILS 259
Cdd:PRK06187 367 VGEIIVR---GPWLMQGYWNRPEATA----ETIDgGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYG 439
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1057503158 260 HGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 337
Cdd:PRK06187 440 HPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDA----KELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
37-332 |
6.08e-37 |
|
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: 139.27 E-value: 6.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 37 PLLHG---NTTV--LYEGKPVGT---PDAGAYFRVLAEHGVAALFTAPtAIRAIRQQDPgaaLGKQYSLTRFKTLFVAGE 108
Cdd:cd05911 197 PLYHIyglFTTLasLLNGATVIImpkFDSELFLDLIEKYKITFLYLVP-PIAAALAKSP---LLDKYDLSSLRVILSGGA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 109 RCDVETLEWSKNVFRVPVLDHWW-QTETGSPITascvglgnsKTPP----PGQAGKSVPGYNVMILDDN-MQKLKARCLG 182
Cdd:cd05911 273 PLSKELQELLAKRFPNATIKQGYgMTETGGILT---------VNPDgddkPGSVGRLLPNVEAKIVDDDgKDSLGPNEPG 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 183 NIVVKLPLppgAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGT 262
Cdd:cd05911 344 EICVRGPQ---VMKGYYNNPEATKETFDED--GWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPG 418
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1057503158 263 VADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAV-FVKQLPKTRSGKI 332
Cdd:cd05911 419 VADAAVIGIPDEVSGELPRAYVVRKPGEKLTE----KEVKDYVAKKVASYKQLRGGVvFVDEIPKSASGKI 485
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
37-337 |
1.69e-36 |
|
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: 137.69 E-value: 1.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 37 PLLHGNTTVLyegkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGaalgKQYSLTRFKTLFVAGERCDVETLE 116
Cdd:cd05936 190 PLALGATIVL-----IPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEF----KKRDFSSLRLCISGGAPLPVEVAE 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 117 WSKNVFRVPVLDHWWQTETgSPITASCVGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFS 196
Cdd:cd05936 261 RFEELTGVPIVEGYGLTET-SPVVAVNPLDGPRK---PGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVR---GPQVMK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 197 GLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLK 276
Cdd:cd05936 334 GYWNRPEETAEAFVD---GWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYS 410
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1057503158 277 GHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 337
Cdd:cd05936 411 GEAVKAFVVLKEGASLTE----EEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
6-339 |
6.33e-35 |
|
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: 132.69 E-value: 6.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 6 MSSIY--GLQPGEVWWAASDLGWVvGHSYIC-YGPLLHGNTTVLYEGKPVgtpDAGAYFRVLAEHGVAALFTAPTAIRAI 82
Cdd:cd05974 115 LSTMYwiGLKPGDVHWNISSPGWA-KHAWSCfFAPWNAGATVFLFNYARF---DAKRVLAALVRYGVTTLCAPPTVWRML 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 83 RQQDpgaalgkqysLTRFKT----LFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPItascvglGNSKTPP--PGQ 156
Cdd:cd05974 191 IQQD----------LASFDVklreVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALV-------GNSPGQPvkAGS 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 157 AGKSVPGYNVMILDDNMQKLKArclGNIVVKL--PLPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVM 234
Cdd:cd05974 254 MGRPLPGYRVALLDPDGAPATE---GEVALDLgdTRPVGLMKGYAGDPDKTAHAMRG---GYYRTGDIAMRDEDGYLTYV 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 235 SRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLeEIVKHVRQNIGPVAA 314
Cdd:cd05974 328 GRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETAL-EIFRFSRERLAPYKR 406
|
330 340
....*....|....*....|....*
gi 1057503158 315 FRNAVFVkQLPKTRSGKIPRSALSA 339
Cdd:cd05974 407 IRRLEFA-ELPKTISGKIRRVELRR 430
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
9-337 |
1.22e-34 |
|
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: 132.20 E-value: 1.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 9 IYGLQPGEVWWAASDL--GWVVGHSYIcyGPLLHGNTTVLYEGKPvgtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQd 86
Cdd:cd05919 127 ALGLTPGDRVFSSAKMffGYGLGNSLW--FPLAVGASAVLNPGWP----TAERVLATLARFRPTVLYGVPTFYANLLDS- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 87 pgaALGKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPITASCVGLGNsktppPGQAGKSVPGYNV 166
Cdd:cd05919 200 ---CAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWR-----LGSTGRPVPGYEI 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 167 MILDDNMQKLKARCLGNIVVKLPlppGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGH 246
Cdd:cd05919 272 RLVDEEGHTIPPGEEGDLLVRGP---SAAVGYWNNPEKSRATFNG---GWYRTGDKFCRDADGWYTHAGRADDMLKVGGQ 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 247 RISAGAIEESILSHGTVADCAVVGKEDpLKGHVPLALCVLRKDINATEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPK 326
Cdd:cd05919 346 WVSPVEVESLIIQHPAVAEAAVVAVPE-STGLSRLTAFVVLKSPAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPR 424
|
330
....*....|.
gi 1057503158 327 TRSGKIPRSAL 337
Cdd:cd05919 425 TATGKLQRFKL 435
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
35-337 |
1.71e-32 |
|
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: 125.87 E-value: 1.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 35 YGPLLHGNTTVLYEgkpvgTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAalgkQYSLTRFKTLFVAGERCDVET 114
Cdd:cd05934 142 LAALSVGATLVLLP-----RFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSP----DDRAHRLRAAYGAPNPPELHE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 115 lEWSKNvFRVPVLDHWWQTETGSPITASCVGlgnskTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGA 194
Cdd:cd05934 213 -EFEER-FGVRLLEGYGMTETIVGVIGPRDE-----PRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRGLRGWGF 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 195 FSGLWKNQEA----FKHlyfekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVG 270
Cdd:cd05934 286 FKGYYNMPEAtaeaMRN-------GWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVA 358
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1057503158 271 KEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 337
Cdd:cd05934 359 VPDEVGEDEVKAVVVLRPGETLDP----EELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQL 421
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
9-337 |
5.56e-32 |
|
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: 125.94 E-value: 5.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 9 IYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPvgTPDAgaYFRVLAEHGVAALFTAPTaIRAIRQQDPG 88
Cdd:cd05959 199 VLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERP--TPAA--VFKRIRRYRPTVFFGVPT-LYAAMLAAPN 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 89 AalgKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSpitascVGLGNskTP---PPGQAGKSVPGYN 165
Cdd:cd05959 274 L---PSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLH------IFLSN--RPgrvRYGTTGKPVPGYE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 166 VMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKhlyfEKFPGY-YDTMDAGYMDEEGYLYVMSRVDDVINVA 244
Cdd:cd05959 343 VELRDEDGGDVADGEPGELYVR---GPSSATMYWNNRDKTR----DTFQGEwTRTGDKYVRDDDGFYTYAGRADDMLKVS 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 245 GHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEqVLEEIVKHVRQNIGPVAAFRNAVFVKQL 324
Cdd:cd05959 416 GIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEA-LEEELKEFVKDRLAPYKYPRWIVFVDEL 494
|
330
....*....|...
gi 1057503158 325 PKTRSGKIPRSAL 337
Cdd:cd05959 495 PKTATGKIQRFKL 507
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
73-338 |
1.80e-31 |
|
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: 123.96 E-value: 1.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 73 FTA-PTaIRAIRQQDPGAALGKQYSLTRFktLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPITASCVglgNSKT 151
Cdd:cd05926 242 YTAvPT-IHQILLNRPEPNPESPPPKLRF--IRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNPL---PPGP 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 152 PPPGQAGKSVpGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHlYFEKFpGYYDTMDAGYMDEEGYL 231
Cdd:cd05926 316 RKPGSVGKPV-GVEVRILDEDGEILPPGVVGEICLR---GPNVTRGYLNNPEANAE-AAFKD-GWFRTGDLGYLDADGYL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 232 YVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIgp 311
Cdd:cd05926 390 FLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTE----EELRAFCRKHL-- 463
|
250 260 270
....*....|....*....|....*....|
gi 1057503158 312 vAAF---RNAVFVKQLPKTRSGKIPRSALS 338
Cdd:cd05926 464 -AAFkvpKKVYFVDELPKTATGKIQRRKVA 492
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1-337 |
7.78e-29 |
|
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: 116.09 E-value: 7.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 1 MLHWsMSSIYGLQPGEVWWAASDLGWVVGHSYIcYGPLLHGNTTVLYEGKPVGTPDAgaYFRVLAEHGVAALFTAPTAIR 80
Cdd:cd05930 121 LLLW-MQEAYPLTPGDRVLQFTSFSFDVSVWEI-FGALLAGATLVVLPEEVRKDPEA--LADLLAEEGITVLHLTPSLLR 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 81 AIRQQDPGAALgkqyslTRFKTLFVAGERCDVETLE-WSKNVFRVPVLDHWWQTETGSPITASCVGLGN-SKTPPPgqAG 158
Cdd:cd05930 197 LLLQELELAAL------PSLRLVLVGGEALPPDLVRrWRELLPGARLVNLYGPTEATVDATYYRVPPDDeEDGRVP--IG 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 159 KSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGLW---------------KNQEAFKHLYFekFPG--YYDTMD 221
Cdd:cd05930 269 RPIPNTRVYVLDENLR--------------PVPPGVPGELYiggaglargylnrpeLTAERFVPNPF--GPGerMYRTGD 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 222 AGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDinatEEQVLEEI 301
Cdd:cd05930 333 LVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEG----GELDEEEL 408
|
330 340 350
....*....|....*....|....*....|....*....
gi 1057503158 302 VKHVRQNIGPV---AAFrnaVFVKQLPKTRSGKIPRSAL 337
Cdd:cd05930 409 RAHLAERLPDYmvpSAF---VVLDALPLTPNGKVDRKAL 444
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
10-332 |
4.37e-27 |
|
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: 110.93 E-value: 4.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 10 YGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEgkpVGTPDAGAyfRVLAEHGVAALFTAPT----AIRAIRQQ 85
Cdd:cd05903 129 LGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQD---IWDPDKAL--ALMREHGVTFMMGATPfltdLLNAVEEA 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 86 DPgaalgkqySLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSpitascvGLGNSKTPPPGQA----GKSV 161
Cdd:cd05903 204 GE--------PLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPG-------AVTSITPAPEDRRlytdGRPL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 162 PGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQeafkHLYFEKFP-GYYDTMDAGYMDEEGYLYVMSRVDDV 240
Cdd:cd05903 269 PGVEIKVVDDTGATLAPGVEGELLSR---GPSVFLGYLDRP----DLTADAAPeGWFRTGDLARLDEDGYLRITGRSKDI 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 241 INVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATeeqvLEEIVKHV-RQNIGPVAAFRNAV 319
Cdd:cd05903 342 IIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLT----FDELVAYLdRQGVAKQYWPERLV 417
|
330
....*....|...
gi 1057503158 320 FVKQLPKTRSGKI 332
Cdd:cd05903 418 HVDDLPRTPSGKV 430
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
19-339 |
3.20e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 109.31 E-value: 3.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 19 WAASDLGWVVGHSYICYGPLLH------------GNTTVLYEGKpvgtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQD 86
Cdd:PRK06188 199 IQLAEWEWPADPRFLMCTPLSHaggafflptllrGGTVIVLAKF-----DPAEVLRAIEEQRITATFLVPTMIYALLDHP 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 87 PGAAlgkqYSLTRFKTLFVAGERCD----VETLEWSKNVFrvpvLDHWWQTETGSPIT---------------ASCvglg 147
Cdd:PRK06188 274 DLRT----RDLSSLETVYYGASPMSpvrlAEAIERFGPIF----AQYYGQTEAPMVITylrkrdhdpddpkrlTSC---- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 148 nsktpppgqaGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGafsGLWK----NQEAFKHlyfekfpGYYDTMDAG 223
Cdd:PRK06188 342 ----------GRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMD---GYWNrpeeTAEAFRD-------GWLHTGDVA 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 224 YMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVK 303
Cdd:PRK06188 402 REDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDA----AELQA 477
|
330 340 350
....*....|....*....|....*....|....*.
gi 1057503158 304 HVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSA 339
Cdd:PRK06188 478 HVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRA 513
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
27-337 |
8.00e-26 |
|
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: 108.09 E-value: 8.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 27 VVGHSYICYGPLLHGNTTVLyegkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpgaALGKQYSLTRFKTLFVA 106
Cdd:cd05904 213 IYGLSSFALGLLRLGATVVV-----MPRFDLEELLAAIERYKVTHLPVVPPIVLALVKS----PIVDKYDLSSLRQIMSG 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 107 GERCDVETLEWSKNVF-RVPVLDHWWQTETgSPITASCVGLGNSKTPPpGQAGKSVPGYNVMILDdnmqklkarclgnIV 185
Cdd:cd05904 284 AAPLGKELIEAFRAKFpNVDLGQGYGMTES-TGVVAMCFAPEKDRAKY-GSVGRLVPNVEAKIVD-------------PE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 186 VKLPLPPGaFSG-LW-----------KNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAI 253
Cdd:cd05904 349 TGESLPPN-QTGeLWirgpsimkgylNNPEATAATIDKE--GWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAEL 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 254 EESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEEIVKHVrqniGPVAAFRNAVFVKQLPKTRSGKIP 333
Cdd:cd05904 426 EALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQV----APYKKVRKVAFVDAIPKSPSGKIL 501
|
....
gi 1057503158 334 RSAL 337
Cdd:cd05904 502 RKEL 505
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
100-344 |
9.55e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 107.74 E-value: 9.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 100 FKTLFVAGERCDVETLEWSKNvFRVPVLDHWWQTETGSPITascvglgnskTPPP-------GQAGKSVPGYNVMILDDN 172
Cdd:PRK03640 256 FRCMLLGGGPAPKPLLEQCKE-KGIPVYQSYGMTETASQIV----------TLSPedaltklGSAGKPLFPCELKIEKDG 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 173 mQKLKARCLGNIVVKLP-LPPGAFSGLWKNQEAFKHlyfekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAG 251
Cdd:PRK03640 325 -VVVPPFEEGEIVVKGPnVTKGYLNREDATRETFQD-------GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 252 AIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINateeqvLEEIVKHVRQNIG----PVAAFrnavFVKQLPKT 327
Cdd:PRK03640 397 EIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVT------EEELRHFCEEKLAkykvPKRFY----FVEELPRN 466
|
250
....*....|....*..
gi 1057503158 328 RSGKIPRSALSAIVNGK 344
Cdd:PRK03640 467 ASGKLLRHELKQLVEEM 483
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
253-331 |
9.63e-26 |
|
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: 98.39 E-value: 9.63e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1057503158 253 IEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGK 331
Cdd:pfam13193 2 VESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLE----EELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
36-332 |
1.10e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 108.10 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 36 GPLLH-GNTTVLYEGkpvgtPDAGAYFRVLAEHGVAALFTAPTA-IRAIRQQDPGaalgkQYSLTRFKTLFVAGERCDVE 113
Cdd:PRK08316 232 GPYLYvGATNVILDA-----PDPELILRTIEAERITSFFAPPTVwISLLRHPDFD-----TRDLSSLRKGYYGASIMPVE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 114 TLEWSKNvfRVPVLDHW---WQTETGSPITAscvgLGnsktpP------PGQAGKsvPGYNV--MILDDNMQKLKARCLG 182
Cdd:PRK08316 302 VLKELRE--RLPGLRFYncyGQTEIAPLATV----LG-----PeehlrrPGSAGR--PVLNVetRVVDDDGNDVAPGEVG 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 183 NIVVKlplPPGAFSGLWKN----QEAFKHlyfekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESIL 258
Cdd:PRK08316 369 EIVHR---SPQLMLGYWDDpektAEAFRG-------GWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALY 438
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1057503158 259 SHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKI 332
Cdd:PRK08316 439 THPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTE----DELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
124-337 |
1.14e-25 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 106.66 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 124 VPVLDHWWQTETGSPITASCVGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKarcLGNIVVKLP-LPPGAFSGLWKNQ 202
Cdd:cd05912 214 IPVYQSYGMTETCSQIVTLSPEDALNK---IGSAGKPLFPVELKIEDDGQPPYE---VGEILLKGPnVTKGYLNRPDATE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 203 EAFKHlyfekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLA 282
Cdd:cd05912 288 ESFEN-------GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVA 360
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1057503158 283 LCVLRKDINAteeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 337
Cdd:cd05912 361 FVVSERPISE------EELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
36-334 |
1.51e-25 |
|
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: 104.79 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 36 GPLLH-----GNTTVLYEGKPV---GTPDAGAYFRVLAEHGVAALFTAPTAIRA-IRQQDPgaalgkqysLTRFKTLFVA 106
Cdd:cd17633 48 GPLSHslflyGAISALYLGGTFigqRKFNPKSWIRKINQYNATVIYLVPTMLQAlARTLEP---------ESKIKSIFSS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 107 GERCDVETLEWSKNVFRVPVLDHWWQTETGSPITASCvglgNSKTPPPGQAGKSVPGYNVMILDDNmqklkARCLGNIVV 186
Cdd:cd17633 119 GQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNF----NQESRPPNSVGRPFPNVEIEIRNAD-----GGEIGKIFV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 187 KLPLppgAFSGLWKNQEAFKHlyfekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADC 266
Cdd:cd17633 190 KSEM---VFSGYVRGGFSNPD-------GWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEA 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1057503158 267 AVVGKEDPLKGHVPLALCVLRKdinATEEQVLEEIVKHVRQNIGPvaafRNAVFVKQLPKTRSGKIPR 334
Cdd:cd17633 260 IVVGIPDARFGEIAVALYSGDK---LTYKQLKRFLKQKLSRYEIP----KKIIFVDSLPYTSSGKIAR 320
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
40-334 |
3.98e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 106.28 E-value: 3.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 40 HGNTTVLYEGKPVgtpDAGAYFRVLAEHGVAALFTAPTaIRAIRQQDPGAALGKQYSLtrfKTLFVAGE---RCDvetle 116
Cdd:PRK07470 229 RGAATVLLPSERF---DPAEVWALVERHRVTNLFTVPT-ILKMLVEHPAVDRYDHSSL---RYVIYAGApmyRAD----- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 117 wSKNVFRV--PVLDHWWqtetgspitascvGL----GNSKTPPP-------------GQAGKSVPGYNVMILDDNMQKLK 177
Cdd:PRK07470 297 -QKRALAKlgKVLVQYF-------------GLgevtGNITVLPPalhdaedgpdariGTCGFERTGMEVQIQDDEGRELP 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 178 ARCLGNIVVklpLPPGAFSGLWKNQEA----FKHlyfekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAI 253
Cdd:PRK07470 363 PGETGEICV---IGPAVFAGYYNNPEAnakaFRD-------GWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREI 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 254 EESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEeivkHVRQNIGPVAAFRNAVFVKQLPKTRSGKIP 333
Cdd:PRK07470 433 EEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAELLA----WLDGKVARYKLPKRFFFWDALPKSGYGKIT 508
|
.
gi 1057503158 334 R 334
Cdd:PRK07470 509 K 509
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
3-337 |
6.45e-25 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 106.19 E-value: 6.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 3 HWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLyeGKPVGTPDAGAY---FRVLAEHGVAALFTAPTAI 79
Cdd:PRK07529 242 AWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVL--ATPQGYRGPGVIanfWKIVERYRINFLSGVPTVY 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 80 RAIRQQDPGAAlgkqySLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTEtgspitASCVglgNSKTPP-----P 154
Cdd:PRK07529 320 AALLQVPVDGH-----DISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTE------ATCV---SSVNPPdgerrI 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 155 GQAGKSVPGYNV--MILDDN---MQKLKARCLGNIVVKlplPPGAFSGlWKNQEAFKHLYFEkfPGYYDTMDAGYMDEEG 229
Cdd:PRK07529 386 GSVGLRLPYQRVrvVILDDAgryLRDCAVDEVGVLCIA---GPNVFSG-YLEAAHNKGLWLE--DGWLNTGDLGRIDADG 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 230 YLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEeivkHVRQNI 309
Cdd:PRK07529 460 YFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLA----FARDHI 535
|
330 340
....*....|....*....|....*....
gi 1057503158 310 GPVAAFRNAV-FVKQLPKTRSGKIPRSAL 337
Cdd:PRK07529 536 AERAAVPKHVrILDALPKTAVGKIFKPAL 564
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
182-337 |
1.61e-24 |
|
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: 103.71 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 182 GNIVVKlplPPGAFSGLWK----NQEAFKHLYFEKFpgyYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESI 257
Cdd:cd05935 279 GEIVVR---GPQIFKGYWNrpeeTEESFIEIKGRRF---FRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 258 LSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 337
Cdd:cd05935 353 YKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTE--EDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
1-355 |
2.59e-24 |
|
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: 104.28 E-value: 2.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 1 MLHWSMssiyglQPGEVWWAASDLGWVVGHSYIcyGPLLHGNTTVLYEGKPvGTPDAGAYFRVLAEHGVAALFTAPTAIR 80
Cdd:cd05943 283 ILHCDL------RPGDRLFYYTTCGWMMWNWLV--SGLAVGATIVLYDGSP-FYPDTNALWDLADEEGITVFGTSAKYLD 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 81 AIRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEW-SKNVFRvpvlDHWWQTETGSPITASCVGLGNSKTPP-PGQAG 158
Cdd:cd05943 354 ALEKA--GLKPAETHDLSSLRTILSTGSPLKPESFDYvYDHIKP----DVLLASISGGTDIISCFVGGNPLLPVyRGEIQ 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 159 KSVPGYNVMILDDNMQKLKARcLGNIVVKLPLP--PGAFsglWKNQEA--FKHLYFEKFPGYYDTMDAGYMDEEGYLYVM 234
Cdd:cd05943 428 CRGLGMAVEAFDEEGKPVWGE-KGELVCTKPFPsmPVGF---WNDPDGsrYRAAYFAKYPGVWAHGDWIEITPRGGVVIL 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 235 SRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDP-LKGHVPLALcVLRKDINATEEqVLEEIVKHVRQNIGPva 313
Cdd:cd05943 504 GRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKdGDERVILFV-KLREGVELDDE-LRKRIRSTIRSALSP-- 579
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1057503158 314 afR---NAVF-VKQLPKTRSGKIPRSALSAIVNGKPYKITSTIEDP 355
Cdd:cd05943 580 --RhvpAKIIaVPDIPRTLSGKKVEVAVKKIIAGRPVKNAGALANP 623
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
60-340 |
2.85e-24 |
|
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: 103.76 E-value: 2.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 60 YFRVLAEHGVAALFTAPTAIRAIrqqdPGAALGKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVP-VLDHWWQTETGSP 138
Cdd:cd17642 267 FLRSLQDYKVQSALLVPTLFAFF----AKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSA 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 139 ITAScvglgNSKTPPPGQAGKSVPGYNVMILD-DNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYY 217
Cdd:cd17642 343 ILIT-----PEGDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVK---GPMIMKGYVNNPEATKALIDKD--GWL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 218 DTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEqv 297
Cdd:cd17642 413 HSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEK-- 490
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1057503158 298 leEIVKHVRQNIGPVAAFRNAV-FVKQLPKTRSGKIPRSALSAI 340
Cdd:cd17642 491 --EVMDYVASQVSTAKRLRGGVkFVDEVPKGLTGKIDRRKIREI 532
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
4-337 |
3.64e-24 |
|
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: 101.79 E-value: 3.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 4 WSMSSIYGLQPGEVWWAASDLgWVVGHSYICYGPLLHGNTTVLYEGkPVGTPDAGAY---FRVLAEHGVAALFTAPTAIR 80
Cdd:cd05944 32 WMLALNSLFDPDDVLLCGLPL-FHVNGSVVTLLTPLASGAHVVLAG-PAGYRNPGLFdnfWKLVERYRITSLSTVPTVYA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 81 AIRQQDPGAALGkqySLtrfKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTEtgspitASCVglgNSKTPP-----PG 155
Cdd:cd05944 110 ALLQVPVNADIS---SL---RFAMSGAAPLPVELRARFEDATGLPVVEGYGLTE------ATCL---VAVNPPdgpkrPG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 156 QAGKSVPGYNVMIL-DDNMQKLKARC----LGNIVVKlplPPGAFsGLWKNQEAFKHLYFEkfPGYYDTMDAGYMDEEGY 230
Cdd:cd05944 175 SVGLRLPYARVRIKvLDGVGRLLRDCapdeVGEICVA---GPGVF-GGYLYTEGNKNAFVA--DGWLNTGDLGRLDADGY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 231 LYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEeivkHVRQNIG 310
Cdd:cd05944 249 LFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEELLA----WARDHVP 324
|
330 340
....*....|....*....|....*...
gi 1057503158 311 PVAAFRNAVFV-KQLPKTRSGKIPRSAL 337
Cdd:cd05944 325 ERAAVPKHIEVlEELPVTAVGKVFKPAL 352
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
38-337 |
2.36e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 101.39 E-value: 2.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 38 LLHGNTTVLYegkPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIrQQDPGAAlGKQYSLtRFKTlFVAGERCDVETLEW 117
Cdd:PRK07786 238 LLLGAPTVIY---PLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAV-CAEQQAR-PRDLAL-RVLS-WGAAPASDTLLRQM 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 118 SKNVFRVPVLDHWWQTETgSPITasCVGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSG 197
Cdd:PRK07786 311 AATFPEAQILAAFGQTEM-SPVT--CMLLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYR---APTLMSG 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 198 LWKNQEAFKhlyfEKFPG-YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLK 276
Cdd:PRK07786 385 YWNNPEATA----EAFAGgWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKW 460
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1057503158 277 GHVPLALCVLRkdiNATEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 337
Cdd:PRK07786 461 GEVPVAVAAVR---NDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTEL 518
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
11-341 |
3.22e-23 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 98.56 E-value: 3.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 11 GLQPGEVWWAASDLGWVVGhsyicYGPLLHGnttvLYEGKP--VGTPDAGAYFRvLAEHGVAALFTAPTAIRAIRQQDPG 88
Cdd:cd17630 37 GFGGGDSWLLSLPLYHVGG-----LAILVRS----LLAGAElvLLERNQALAED-LAPPGVTHVSLVPTQLQRLLDSGQG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 89 AAlgkqySLTRFKTLFVAGERCDVETLEWSKNVfRVPVLDHWWQTETGSPITASCVGLgnsktPPPGQAGKSVPGYNVMI 168
Cdd:cd17630 107 PA-----ALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTETASQVATKRPDG-----FGRGGVGVLLPGRELRI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 169 LDDNMQKLKARCLGNIVVKLPLPPGAFSGLWknqeafkhlyfekfpgyYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRI 248
Cdd:cd17630 176 VEDGEIWVGGASLAMGYLRGQLVPEFNEDGW-----------------FTTKDLGELHADGRLTVLGRADNMIISGGENI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 249 SAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRkdinatEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTR 328
Cdd:cd17630 239 QPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGR------GPADPAELRAWLKDKLARFKLPKRIYPVPELPRTG 312
|
330
....*....|...
gi 1057503158 329 SGKIPRSALSAIV 341
Cdd:cd17630 313 GGKVDRRALRAWL 325
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
36-337 |
2.40e-22 |
|
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: 97.75 E-value: 2.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 36 GPLLHGNTTVLyegkpVGTPDAGAYFRVLAEHGVAALFTAPTA----IRAIRQQDPGAALGKQYSLTRFKtLFVAGERC- 110
Cdd:cd05941 151 CPLFAGASVEF-----LPKFDPKEVAISRLMPSITVFMGVPTIytrlLQYYEAHFTDPQFARAAAAERLR-LMVSGSAAl 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 111 DVETLEWSKNVFRVPVLDHWWQTETGspITASCVGLGNSKtppPGQAGKSVPGYNVMILDDNMQK-LKARCLGNIVVKlp 189
Cdd:cd05941 225 PVPTLEEWEAITGHTLLERYGMTEIG--MALSNPLDGERR---PGTVGMPLPGVQARIVDEETGEpLPRGEVGEIQVR-- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 190 lPPGAFSGLWKNQEAFKhlyfEKFP--GYYDTMDAGYMDEEGYLYVMSRV-DDVINVAGHRISAGAIEESILSHGTVADC 266
Cdd:cd05941 298 -GPSVFKEYWNKPEATK----EEFTddGWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSEC 372
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1057503158 267 AVVGKEDPLKGHVPLALCVLRKDINATEeqvLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 337
Cdd:cd05941 373 AVIGVPDPDWGERVVAVVVLRAGAAALS---LEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
15-343 |
3.99e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 97.26 E-value: 3.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 15 GEVWWAASD----LGWVVGHSYICYGPLLH------GNTTVLYEGKPVGTP---DAGAYFRVLAEHGVAALFTAP---TA 78
Cdd:PRK06145 172 GNLHWKSIDhviaLGLTASERLLVVGPLYHvgafdlPGIAVLWVGGTLRIHrefDPEAVLAAIERHRLTCAWMAPvmlSR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 79 IRAIRQQDpgaalgkQYSLTRFKTLFVAGERC-DVETLEWSKNVFRVPVLDHWWQTETGSPITASCVGLGNSKTpppGQA 157
Cdd:PRK06145 252 VLTVPDRD-------RFDLDSLAWCIGGGEKTpESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREIEKI---GST 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 158 GKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRV 237
Cdd:PRK06145 322 GRALAHVEIRIADGAGRWLPPNMKGEICMR---GPKVTKGYWKDPEKTAEAFYG---DWFRSGDVGYLDEEGFLYLTDRK 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 238 DDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATeeqvLEEIVKHVRQNIGPVAAFRN 317
Cdd:PRK06145 396 KDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLT----LEALDRHCRQRLASFKVPRQ 471
|
330 340
....*....|....*....|....*.
gi 1057503158 318 AVFVKQLPKTRSGKIPRSALSAIVNG 343
Cdd:PRK06145 472 LKVRDELPRNPSGKVLKRVLRDELNG 497
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
124-337 |
1.20e-21 |
|
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: 96.16 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 124 VPVLDHWWQTETgSPI-TASCVGLGNSKTPPPGQA------GKSVPGYNVMILDDNMQKLKA--RCLGNIVVKLP-LPPG 193
Cdd:cd12119 305 VRVIHAWGMTET-SPLgTVARPPSEHSNLSEDEQLalrakqGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPwVTKS 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 194 AFsglwKNQEAfKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKED 273
Cdd:cd12119 384 YY----KNDEE-SEALTED--GWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPH 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1057503158 274 PLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 337
Cdd:cd12119 457 PKWGERPLAVVVLKEGATVTA----EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
154-337 |
2.20e-21 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 94.81 E-value: 2.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 154 PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLppgAFSGLWkNQEAFKhLYFEKFPGYYDTMDAGYMDEEGYLYV 233
Cdd:cd05922 285 PGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPN---VMKGYW-NDPPYR-RKEGRGGGVLHTGDLARRDEDGFLFI 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 234 MSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVplALCVLRKDinateEQVLEEIVKHVRQNIGPVA 313
Cdd:cd05922 360 VGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKL--ALFVTAPD-----KIDPKDVLRSLAERLPPYK 432
|
170 180
....*....|....*....|....
gi 1057503158 314 AFRNAVFVKQLPKTRSGKIPRSAL 337
Cdd:cd05922 433 VPATVRVVDELPLTASGKVDYAAL 456
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
24-319 |
6.04e-21 |
|
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: 93.43 E-value: 6.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 24 LGWVVGHSYICYGPLLHGNTTVLYEGKPVGTPDagayfrvLAEHGVAALFTAPTAIR----AIRQQDPGAALGKQY---S 96
Cdd:cd05907 137 LAHVFERRAGLYVPLLAGARIYFASSAETLLDD-------LSEVRPTVFLAVPRVWEkvyaAIKVKAVPGLKRKLFdlaV 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 97 LTRFKTLFVAGERCDVETLEWsknvFR---VPVLDHWWQTETGSPITASCVGlgnskTPPPGQAGKSVPGYNVMILDDnm 173
Cdd:cd05907 210 GGRLRFAASGGAPLPAELLHF----FRalgIPVYEGYGLTETSAVVTLNPPG-----DNRIGTVGKPLPGVEVRIADD-- 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 174 qklkarclGNIVVKlplPPGAFSGLWKNQEAFKHLYFEkfPGYYDTMDAGYMDEEGYLYVMSRVDDVI-NVAGHRISAGA 252
Cdd:cd05907 279 --------GEILVR---GPNVMLGYYKNPEATAEALDA--DGWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEP 345
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 253 IEESILSHGTVADCAVVGKEDPlkghVPLALCVLRKDIN---ATEEQVLEEIVKHVRQNIGPVAAFRNAV 319
Cdd:cd05907 346 IENALKASPLISQAVVIGDGRP----FLVALIVPDPEALeawAEEHGIAYTDVAELAANPAVRAEIEAAV 411
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
130-334 |
1.64e-20 |
|
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: 91.18 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 130 WW----QTETGSPITASCVglgnskTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLppgAFSGLWKNQEAF 205
Cdd:cd17637 139 FWslygQTETSGLVTLSPY------RERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPL---VFQGYWNLPELT 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 206 KHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRV--DDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLAL 283
Cdd:cd17637 210 AYTFRN---GWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAV 286
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1057503158 284 CVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPR 334
Cdd:cd17637 287 CVLKPGATLTA----DELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
62-340 |
1.74e-20 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 92.62 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 62 RVLAEHGVAALFTAPTAIRAIRQqdpgAALGKQYSLTRFKTLFVAGERCDVetlewsknvfrvPVLDHWwqTETGSPITA 141
Cdd:PRK06839 232 SMIEKHKVTVVMGVPTIHQALIN----CSKFETTNLQSVRWFYNGGAPCPE------------ELMREF--IDRGFLFGQ 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 142 scvGLGNSKTPP-------------PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHL 208
Cdd:PRK06839 294 ---GFGMTETSPtvfmlseedarrkVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIR---GPNVMKEYWNRPDATEET 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 209 YFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRK 288
Cdd:PRK06839 368 IQD---GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKS 444
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1057503158 289 DINATEEQVLEeivkHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAI 340
Cdd:PRK06839 445 SSVLIEKDVIE----HCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
122-340 |
1.76e-20 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 92.51 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 122 FRVPVLDHWWQTETGSPITAScvglgnSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPlPPGAF-SGLW- 199
Cdd:PRK06155 316 FGVDLLDGYGSTETNFVIAVT------HGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRAD-EPFAFaTGYFg 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 200 ---KNQEAFKHLYFEkfpgyydTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLK 276
Cdd:PRK06155 389 mpeKTVEAWRNLWFH-------TGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELG 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1057503158 277 GHVPLALCVLRkdinatEEQVLE--EIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAI 340
Cdd:PRK06155 462 EDEVMAAVVLR------DGTALEpvALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
35-337 |
2.64e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 92.40 E-value: 2.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 35 YGPLLHGNTTVLYEGKPVGTP--DAGAYFRVLAEHGVAALFTAPTAIRAIRQqdpgAALGKQYSLTRFKTLFVAGERCDV 112
Cdd:PRK06710 262 YGMTAVMNLSIMQGYKMVLIPkfDMKMVFEAIKKHKVTLFPGAPTIYIALLN----SPLLKEYDISSIRACISGSAPLPV 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 113 ETLEWSKNVFRVPVLDHWWQTETgSPITASCVgLGNSKTPppGQAGKSVPGYNVMILD-DNMQKLKARCLGNIVVKlplP 191
Cdd:PRK06710 338 EVQEKFETVTGGKLVEGYGLTES-SPVTHSNF-LWEKRVP--GSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVK---G 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 192 PGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGK 271
Cdd:PRK06710 411 PQIMKGYWNKPEETAAVLQD---GWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGV 487
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1057503158 272 EDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 337
Cdd:PRK06710 488 PDPYRGETVKAFVVLKEGTECSE----EELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
20-337 |
5.60e-20 |
|
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: 90.90 E-value: 5.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 20 AASDLGWVVGHSYICYGPLLHG------NTTVLYEGKPVGTP--DAGAYFRVLAEHGVAALFTAPTAIRAIRQQdPGAAL 91
Cdd:cd05929 160 AALGFGPGADSVYLSPAPLYHAapfrwsMTALFMGGTLVLMEkfDPEEFLRLIERYRVTFAQFVPTMFVRLLKL-PEAVR 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 92 GKqYSLTRFKTLFVAGERCDVET----LEWSKnvfrvPVLdhwWQTETGSPITASCVGLGNSKTPPPGQAGKSVPGyNVM 167
Cdd:cd05929 239 NA-YDLSSLKRVIHAAAPCPPWVkeqwIDWGG-----PII---WEYYGGTEGQGLTIINGEEWLTHPGSVGRAVLG-KVH 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 168 ILDDNMQklkarclgnivvklPLPPGAFSGLW-KNQEAFK-HLYFEKFP-----GYYDTM-DAGYMDEEGYLYVMSRVDD 239
Cdd:cd05929 309 ILDEDGN--------------EVPPGEIGEVYfANGPGFEyTNDPEKTAaarneGGWSTLgDVGYLDEDGYLYLTDRRSD 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 240 VINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALcVLRKDINATEEQVLEEIVKHVRQNIGPVAAFRNAV 319
Cdd:cd05929 375 MIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAV-VQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIE 453
|
330
....*....|....*...
gi 1057503158 320 FVKQLPKTRSGKIPRSAL 337
Cdd:cd05929 454 FVAELPRDDTGKLYRRLL 471
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
39-337 |
6.13e-20 |
|
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: 91.03 E-value: 6.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 39 LHGNTTVLyegkPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIrqqdPGAALGKQYSLTRFKTLFVAGERCDVETLEWS 118
Cdd:cd05923 216 LALDGTYV----VVEEFDPADALKLIEQERVTSLFATPTHLDAL----AAAAEFAGLKLSSLRHVTFAGATMPDAVLERV 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 119 KNVFRVPVLDHWWQTETGSPITAscvglgnsKTPPPGQAGKsvPGYN-----VMILDDNMQKLKARCLGNIVVKLPlPPG 193
Cdd:cd05923 288 NQHLPGEKVNIYGTTEAMNSLYM--------RDARTGTEMR--PGFFsevriVRIGGSPDEALANGEEGELIVAAA-ADA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 194 AFSGLWKNQEA-FKHLYFekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKE 272
Cdd:cd05923 357 AFTGYLNQPEAtAKKLQD----GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVA 432
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1057503158 273 DPLKGHVPLAlCVLRKDINATEEQvLEEIVKHvrqniGPVAAF---RNAVFVKQLPKTRSGKIPRSAL 337
Cdd:cd05923 433 DERWGQSVTA-CVVPREGTLSADE-LDQFCRA-----SELADFkrpRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
131-337 |
1.32e-19 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 90.08 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 131 WQTETGSPITAscvGLGNSKTPP------------PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGL 198
Cdd:PRK07059 347 WLEMTGCPITE---GYGLSETSPvatcnpvdatefSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIR---GPQVMAGY 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 199 WKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGH 278
Cdd:PRK07059 421 WNRPDETAKVMTAD--GFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGE 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1057503158 279 VpLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 337
Cdd:PRK07059 499 A-VKLFVVKKDPALTE----EDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
2-268 |
1.40e-19 |
|
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: 89.25 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 2 LHWSMSSIYGLQPGEVWWAASDLGWVVGHSYIcYGPLLHGNTTVLYEGKPVGtPDAGAYFRVLAEHGVAALFTAPTAIRA 81
Cdd:TIGR01733 148 LLAWLARRYGLDPDDRVLQFASLSFDASVEEI-FGALLAGATLVVPPEDEER-DDAALLAALIAEHPVTVLNLTPSLLAL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 82 IRQQDPGAalgkqysLTRFKTLFVAGERCDVETLE-WSKNVFRVPVLDHWWQTET--GSPITASCVGLGNSKTPPPgqAG 158
Cdd:TIGR01733 226 LAAALPPA-------LASLRLVILGGEALTPALVDrWRARGPGARLINLYGPTETtvWSTATLVDPDDAPRESPVP--IG 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 159 KSVPGYNVMILDDNMQKLKARCLGNIVVklpLPPGAFSGLW----KNQEAFKHLYFEKFPGY--YDTMDAGYMDEEGYLY 232
Cdd:TIGR01733 297 RPLANTRLYVLDDDLRPVPVGVVGELYI---GGPGVARGYLnrpeLTAERFVPDPFAGGDGArlYRTGDLVRYLPDGNLE 373
|
250 260 270
....*....|....*....|....*....|....*.
gi 1057503158 233 VMSRVDDVINVAGHRISAGAIEESILSHGTVADCAV 268
Cdd:TIGR01733 374 FLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
40-337 |
3.10e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 88.83 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 40 HGNTTVLYEgkpvgTPDAGAYFRVLAEHGVAALFTAPTAIRaiRQQDPGAALGKQYSLTRFKTLFVAGERCDVETLEWSK 119
Cdd:PRK07788 272 LGSTVVLRR-----RFDPEATLEDIAKHKATALVVVPVMLS--RILDLGPEVLAKYDTSSLKIIFVSGSALSPELATRAL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 120 NVFRvPVLDHWW-QTETGSPITAscvglgnskTPP-----PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPpg 193
Cdd:PRK07788 345 EAFG-PVLYNLYgSTEVAFATIA---------TPEdlaeaPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFP-- 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 194 aFSGlwknqeafkhlYF-----EKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAV 268
Cdd:PRK07788 413 -FEG-----------YTdgrdkQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAV 480
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1057503158 269 VGKEDPLKGHVPLALCVLRKDINATEEQVLEeivkHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 337
Cdd:PRK07788 481 IGVDDEEFGQRLRAFVVKAPGAALDEDAIKD----YVRDNLARYKVPRDVVFLDELPRNPTGKVLKREL 545
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
154-339 |
4.08e-18 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 85.58 E-value: 4.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 154 PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVK-LPLPPGAFSGLWKNQEAfkhlyfekfpGYYDTMDAGYMDEEGYLY 232
Cdd:PRK13382 364 PDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRnDTQFDGYTSGSTKDFHD----------GFMASGDVGYLDENGRLF 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 233 VMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPV 312
Cdd:PRK13382 434 VVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATP----ETLKQHVRDNLANY 509
|
170 180
....*....|....*....|....*..
gi 1057503158 313 AAFRNAVFVKQLPKTRSGKIPRSALSA 339
Cdd:PRK13382 510 KVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
2-337 |
5.44e-18 |
|
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: 84.67 E-value: 5.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 2 LHWSMSSIYGLQPGEVWWAAsdlgwvvgHSYI-------CYGPLLHGNTTVLYEGKPVGTPDAgaYFRVLAEHGVAALFT 74
Cdd:cd17643 121 LFAATQRWFGFNEDDVWTLF--------HSYAfdfsvweIWGALLHGGRLVVVPYEVARSPED--FARLLRDEGVTVLNQ 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 75 APTAIRAIRQ---QDPGAALGKQYsltrfktLFVAGERCDVETLE-WSKNVF--RVPVLDHWWQTETG-----SPITASC 143
Cdd:cd17643 191 TPSAFYQLVEaadRDGRDPLALRY-------VIFGGEALEAAMLRpWAGRFGldRPQLVNMYGITETTvhvtfRPLDAAD 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 144 VGLGNSKTpppgqAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGLW----------KNQEAfkhLYFEKF 213
Cdd:cd17643 264 LPAAAASP-----IGRPLPGLRVYVLDADGR--------------PVPPGVVGELYvsgagvargyLGRPE---LTAERF 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 214 -------PG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVpLALC 284
Cdd:cd17643 322 vanpfggPGsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTR-LVAY 400
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1057503158 285 VlrkDINATEEQVLEEIVKHVRQNIGPV---AAFrnaVFVKQLPKTRSGKIPRSAL 337
Cdd:cd17643 401 V---VADDGAAADIAELRALLKELLPDYmvpARY---VPLDALPLTVNGKLDRAAL 450
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1-339 |
6.33e-18 |
|
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: 85.68 E-value: 6.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 1 MLHWsMSSIYGLQPGEVWWAASDLGWVVGHSYIcYGPLLHGNTTVLYEgkPVGTPDAGAYFRVLAEHGVAALFTAPTAIR 80
Cdd:COG1020 645 LLAW-MQRRYGLGPGDRVLQFASLSFDASVWEI-FGALLSGATLVLAP--PEARRDPAALAELLARHRVTVLNLTPSLLR 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 81 AIRQQDPGAalgkqysLTRFKTLFVAGERCDVETLE-WSKNVFRVPVLDHWWQTETGspITASCvglgnSKTPPPGQAGK 159
Cdd:COG1020 721 ALLDAAPEA-------LPSLRLVLVGGEALPPELVRrWRARLPGARLVNLYGPTETT--VDSTY-----YEVTPPDADGG 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 160 SVP------GYNVMILDDNMQklkarclgnivvklPLPPGAfSG-LW---------------KNQEAFKHLYFEkFPG-- 215
Cdd:COG1020 787 SVPigrpiaNTRVYVLDAHLQ--------------PVPVGV-PGeLYiggaglargylnrpeLTAERFVADPFG-FPGar 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 216 YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLkGHVPLALCVLRKDINATEE 295
Cdd:COG1020 851 LYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAP-GDKRLVAYVVPEAGAAAAA 929
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1057503158 296 QVLEEIVKHVRQNIGPVAAFrnaVFVKQLPKTRSGKIPRSALSA 339
Cdd:COG1020 930 ALLRLALALLLPPYMVPAAV---VLLLPLPLTGNGKLDRLALPA 970
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
155-337 |
7.92e-18 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 84.72 E-value: 7.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 155 GQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVM 234
Cdd:PRK08974 378 GSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVK---GPQVMLGYWQRPEATDEVIKD---GWLATGDIAVMDEEGFLRIV 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 235 SRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVpLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAA 314
Cdd:PRK08974 452 DRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEA-VKIFVVKKDPSLTE----EELITHCRRHLTGYKV 526
|
170 180
....*....|....*....|...
gi 1057503158 315 FRNAVFVKQLPKTRSGKIPRSAL 337
Cdd:PRK08974 527 PKLVEFRDELPKSNVGKILRREL 549
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
131-337 |
1.07e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 84.43 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 131 WQTETGSPItasCVGLGNSKTPP-----------PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLW 199
Cdd:PRK05677 346 WKEVTGCAI---CEGYGMTETSPvvsvnpsqaiqVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVK---GPQVMKGYW 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 200 KNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHV 279
Cdd:PRK05677 420 QRPEATDEILDSD--GWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEA 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1057503158 280 PLALCVLRKDINATEEQVLEeivkHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 337
Cdd:PRK05677 498 IKVFVVVKPGETLTKEQVME----HMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
154-332 |
1.70e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 83.41 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 154 PGQAGKSVPGyNVMILDDNMQKLKARCLGNIVVKLPLPPgaFSGLwKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYV 233
Cdd:PRK08276 314 PGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYP--FEYH-NDPEKTAAARNPH--GWVTVGDVGYLDEDGYLYL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 234 MSRVDDVInvaghrISAGA------IEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVlEEIVKHVRQ 307
Cdd:PRK08276 388 TDRKSDMI------ISGGVniypqeIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDALA-AELIAWLRG 460
|
170 180
....*....|....*....|....*
gi 1057503158 308 NIGPVAAFRNAVFVKQLPKTRSGKI 332
Cdd:PRK08276 461 RLAHYKCPRSIDFEDELPRTPTGKL 485
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
119-337 |
1.91e-17 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 83.77 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 119 KNVFRVPVLDHWWQTETgSPitASCVglgNSKTPPP--GQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFS 196
Cdd:PRK08751 350 KQVTGLTLVEAYGLTET-SP--AACI---NPLTLKEynGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIK---GPQVMK 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 197 GLWKNQEAFKHLYfeKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLK 276
Cdd:PRK08751 421 GYWKRPEETAKVM--DADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKS 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1057503158 277 GHVpLALCVLRKDINATEEQVLEeivkHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 337
Cdd:PRK08751 499 GEI-VKVVIVKKDPALTAEDVKA----HARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
111-334 |
2.17e-17 |
|
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: 82.31 E-value: 2.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 111 DVETLEWSKNVfrvPVLDHWWQTETGspiTASCVGLGNSkTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlpl 190
Cdd:cd17635 133 DVRFIEATGLT---NTAQVYGLSETG---TALCLPTDDD-SIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIK--- 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 191 PPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVG 270
Cdd:cd17635 203 SPANMLGYWNNPERTAEVLID---GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYE 279
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1057503158 271 KEDPLKGHVpLALCVLRKDINatEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPR 334
Cdd:cd17635 280 ISDEEFGEL-VGLAVVASAEL--DENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
182-332 |
2.60e-17 |
|
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: 83.12 E-value: 2.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 182 GNIVVKlplppgafsGLWKN----QEAFKHlyfekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESI 257
Cdd:cd12118 346 GNIVMK---------GYLKNpeatAEAFRG-------GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVL 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1057503158 258 LSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIgpvAAF---RNAVFVkQLPKTRSGKI 332
Cdd:cd12118 410 YKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTE----EEIIAFCREHL---AGFmvpKTVVFG-ELPKTSTGKI 479
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
190-337 |
2.67e-17 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 83.35 E-value: 2.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 190 LPPGAFSGLW-----------KNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESIL 258
Cdd:PLN02574 396 LPPGNCGELWiqgpgvmkgylNNPKATQSTIDKD--GWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLI 473
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1057503158 259 SHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEEIVKHVrqniGPVAAFRNAVFVKQLPKTRSGKIPRSAL 337
Cdd:PLN02574 474 SHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVAKQV----APYKKVRKVVFVQSIPKSPAGKILRREL 548
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
35-337 |
2.91e-17 |
|
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: 82.68 E-value: 2.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 35 YGPLLHGNTTVlyegkPVG---TPDAGAYFRVLAEHGVAALFTAPTAIRAIRQqDPGAALGKQYSLTRFktLFvAGERCD 111
Cdd:cd05945 157 YPALASGATLV-----PVPrdaTADPKQLFRFLAEHGITVWVSTPSFAAMCLL-SPTFTPESLPSLRHF--LF-CGEVLP 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 112 VETLEWSKNVF-RVPVLDHWWQTETgspiTASCVG-------LGNSKTPPPGQAgksVPGYNVMILDDNMQKLKARCLGN 183
Cdd:cd05945 228 HKTARALQQRFpDARIYNTYGPTEA----TVAVTYievtpevLDGYDRLPIGYA---KPGAKLVILDEDGRPVPPGEKGE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 184 IVVKlplPPGAFSGLWKNQEafKHLY-FEKFPGY--YDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSH 260
Cdd:cd05945 301 LVIS---GPSVSKGYLNNPE--KTAAaFFPDEGQraYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQV 375
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1057503158 261 GTVADCAVVGKEDPLKGHVPLALCVLRkdiNATEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 337
Cdd:cd05945 376 PGVKEAVVVPKYKGEKVTELIAFVVPK---PGAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
11-345 |
3.55e-17 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 82.79 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 11 GLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEgkpVGTPDAGAyfRVLAEHGVAalFT---APTAIRAIRQQDP 87
Cdd:PRK13295 234 GLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQD---IWDPARAA--ELIRTEGVT--FTmasTPFLTDLTRAVKE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 88 GAalgkqYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSpitASCVGLGNSKTPPPGQAGKSVPGYNVM 167
Cdd:PRK13295 307 SG-----RPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA---VTLTKLDDPDERASTTDGCPLPGVEVR 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 168 ILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQeafkHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHR 247
Cdd:PRK13295 379 VVDADGAPLPAGQIGRLQVR---GCSNFGGYLKRP----QLNGTDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGEN 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 248 ISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRkdinATEEQVLEEIV-----KHVRQNIGPvaafRNAVFVK 322
Cdd:PRK13295 452 IPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPR----PGQSLDFEEMVeflkaQKVAKQYIP----ERLVVRD 523
|
330 340
....*....|....*....|...
gi 1057503158 323 QLPKTRSGKIPRSALSAIVNGKP 345
Cdd:PRK13295 524 ALPRTPSGKIQKFRLREMLRGED 546
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
35-337 |
3.57e-17 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 82.37 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 35 YGPLLHGNTTVLYEgkpvgtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQD--PGAAlgkqysltrfKTLFVAGE---R 109
Cdd:cd12115 165 FGPLATGGKVVLAD-------NVLALPDLPAAAEVTLINTVPSAAAELLRHDalPASV----------RVVNLAGEplpR 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 110 CDVETLEWSKNVFRVPVLdhWWQTETGSPITASCVGLGNSKTPPpgqAGKSVPGYNVMILDDNMQklkarclgnivvklP 189
Cdd:cd12115 228 DLVQRLYARLQVERVVNL--YGPSEDTTYSTVAPVPPGASGEVS---IGRPLANTQAYVLDRALQ--------------P 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 190 LPPGAFSGLWKNQEAFKHLYF-------EKF------PG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIE 254
Cdd:cd12115 289 VPLGVPGELYIGGAGVARGYLgrpgltaERFlpdpfgPGarLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIE 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 255 ESILSHGTVADCAVVGKEDPLKGHVPLALCVLRkdinATEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPR 334
Cdd:cd12115 369 AALRSIPGVREAVVVAIGDAAGERRLVAYIVAE----PGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDR 444
|
...
gi 1057503158 335 SAL 337
Cdd:cd12115 445 SAL 447
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
56-337 |
3.89e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 82.36 E-value: 3.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 56 DAGAYFRVLAEHGVAALFTAPTAIraIRQQDPGAALGKQYSLTRFKTLFVAGERCDVET----LEWSKNVfrvpVLDHWW 131
Cdd:PRK13390 230 DAQATLGHVERYRITVTQMVPTMF--VRLLKLDADVRTRYDVSSLRAVIHAAAPCPVDVkhamIDWLGPI----VYEYYS 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 132 QTET-GSPITASCVGLGNsktppPGQAGKSVPGyNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWKNQEAFKHlyf 210
Cdd:PRK13390 304 STEAhGMTFIDSPDWLAH-----PGSVGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQH--- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 211 EKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDI 290
Cdd:PRK13390 375 PAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGI 454
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1057503158 291 NATEEqVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 337
Cdd:PRK13390 455 RGSDE-LARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
182-332 |
4.61e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 82.30 E-value: 4.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 182 GNIVVKlplppgafsGLWKNQEAFKhlyfEKFP-GYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSH 260
Cdd:PRK08162 395 GNIVMK---------GYLKNPKATE----EAFAgGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRH 461
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1057503158 261 GTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIgpvAAFR--NAVFVKQLPKTRSGKI 332
Cdd:PRK08162 462 PAVLVAAVVAKPDPKWGEVPCAFVELKDGASATE----EEIIAHCREHL---AGFKvpKAVVFGELPKTSTGKI 528
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
179-343 |
4.78e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 82.37 E-value: 4.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 179 RCLGNIVVKlplPPGAFSGLWKN----QEAFKHlyfekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIE 254
Cdd:PLN03102 390 KTMGEIVIK---GSSIMKGYLKNpkatSEAFKH-------GWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVE 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 255 ESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLE------EIVKHVRQNIGPVAAFRNAVFVKQLPKTR 328
Cdd:PLN03102 460 NVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKlvtrerDLIEYCRENLPHFMCPRKVVFLQELPKNG 539
|
170
....*....|....*
gi 1057503158 329 SGKIPRSALSAIVNG 343
Cdd:PLN03102 540 NGKILKPKLRDIAKG 554
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
215-337 |
9.65e-17 |
|
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: 81.35 E-value: 9.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 215 GYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRkdinaTE 294
Cdd:COG1021 409 GFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPR-----GE 483
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1057503158 295 EQVLEEIVKHVRQnIGpVAAFR---NAVFVKQLPKTRSGKIPRSAL 337
Cdd:COG1021 484 PLTLAELRRFLRE-RG-LAAFKlpdRLEFVDALPLTAVGKIDKKAL 527
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
12-337 |
1.35e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 81.02 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 12 LQPGEVWWAASDLGWVVGhSYICYGPLLHGNTTVLYEGKPVGtpdaGAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAAL 91
Cdd:PLN03051 157 IQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGAPLG----RGFGKFVQDAGVTVLGLVPSIVKAWRHT--GAFA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 92 GKQYSLTRFKTLFVAGERCDVETLEW--SKNVFRVPVLDHWWQTETGSPITASCVGLGNSktppPGQAGKSVPGYNVMIL 169
Cdd:PLN03051 230 MEGLDWSKLRVFASTGEASAVDDVLWlsSVRGYYKPVIEYCGGTELASGYISSTLLQPQA----PGAFSTASLGTRFVLL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 170 DDNMQKL--KARCLGNIVVKLPLPPGAFSGLWKNQEAfkhLYFEKFPGYY----------DTMDAgymDEEGYLYVMSRV 237
Cdd:PLN03051 306 NDNGVPYpdDQPCVGEVALAPPMLGASDRLLNADHDK---VYYKGMPMYGskgmplrrhgDIMKR---TPGGYFCVQGRA 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 238 DDVINVAGHRISAGAIEESIL-SHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEEIVKH-----VRQNIGP 311
Cdd:PLN03051 380 DDTMNLGGIKTSSVEIERACDrAVAGIAETAAVGVAPPDGGPELLVIFLVLGEEKKGFDQARPEALQKkfqeaIQTNLNP 459
|
330 340
....*....|....*....|....*.
gi 1057503158 312 VAAFRNAVFVKQLPKTRSGKIPRSAL 337
Cdd:PLN03051 460 LFKVSRVKIVPELPRNASNKLLRRVL 485
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
182-332 |
2.48e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 80.00 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 182 GNIVVKlplPPGAFSGLWKNQEAFKHLYFEkFPG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILS 259
Cdd:PRK08314 385 GEIVVH---GPQVFKGYWNRPEATAEAFIE-IDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYK 460
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1057503158 260 HGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKI 332
Cdd:PRK08314 461 HPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTTE--EEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
142-337 |
3.82e-16 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 79.64 E-value: 3.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 142 SCVGLGNSKtPPPGQA-------GKSVPGYNVMILD-DNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKf 213
Cdd:PLN02330 342 SCITLTHGD-PEKGHGiakknsvGFILPNLEVKFIDpDTGRSLPKNTPGELCVR---SQCVMQGYYNNKEETDRTIDED- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 214 pGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINAT 293
Cdd:PLN02330 417 -GWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKES 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1057503158 294 EEQVLEeivkHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 337
Cdd:PLN02330 496 EEDILN----FVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
144-339 |
6.89e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 78.88 E-value: 6.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 144 VGLGNSKTPP-----PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGlwKNQEAFkhlyfekFPGYYD 218
Cdd:PRK13383 329 VGIGALATPAdlrdaPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTD--GGGKAV-------VDGMTS 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 219 TMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVL 298
Cdd:PRK13383 400 TGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLR 479
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1057503158 299 EEIVKHVRQNIGPvaafRNAVFVKQLPKTRSGKIPRSALSA 339
Cdd:PRK13383 480 DYLKDRVSRFEQP----RDINIVSSIPRNPTGKVLRKELPG 516
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
215-337 |
7.23e-16 |
|
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: 78.52 E-value: 7.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 215 GYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRkdinatE 294
Cdd:cd05920 364 GFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLR------D 437
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1057503158 295 EQVLEEIVKHVRQNIGpVAAFR---NAVFVKQLPKTRSGKIPRSAL 337
Cdd:cd05920 438 PPPSAAQLRRFLRERG-LAAYKlpdRIEFVDSLPLTAVGKIDKKAL 482
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
38-334 |
7.68e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 77.70 E-value: 7.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 38 LLHGNTTVLyegkPVGTPDAGAYFRVLAEHGVAALFTAPTA-IRAIRQQDPgaalgKQYSLTRFKTLFVAGERCDVETLE 116
Cdd:cd05917 66 LTHGATMVF----PSPSFDPLAVLEAIEKEKCTALHGVPTMfIAELEHPDF-----DKFDLSSLRTGIMAGAPCPPELMK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 117 WSKNVFRVP-VLDHWWQTETgSPIT------------------------ASCVGLGNSKTPPPGQAGK-SVPGYNVMIld 170
Cdd:cd05917 137 RVIEVMNMKdVTIAYGMTET-SPVStqtrtddsiekrvntvgrimphteAKIVDPEGGIVPPVGVPGElCIRGYSVMK-- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 171 dnmqklkarclgnivvklplppgafsGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISA 250
Cdd:cd05917 214 --------------------------GYWNDPEKTAEAIDGD--GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYP 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 251 GAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSG 330
Cdd:cd05917 266 REIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTE----EDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSG 341
|
....
gi 1057503158 331 KIPR 334
Cdd:cd05917 342 KIQK 345
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
38-345 |
1.34e-15 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 78.30 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 38 LLHGNTTVLYEGKPvGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEW 117
Cdd:PRK03584 326 LLVGATLVLYDGSP-FYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKA--GLVPGETHDLSALRTIGSTGSPLPPEGFDW 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 118 -SKNVFRvpvlDHWWQTETGSPITASCVGLGNSKTPP-PGQAGKSVPGYNVMILDDNMQKLKARcLGNIVVKLPLP--Pg 193
Cdd:PRK03584 403 vYEHVKA----DVWLASISGGTDICSCFVGGNPLLPVyRGEIQCRGLGMAVEAWDEDGRPVVGE-VGELVCTKPFPsmP- 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 194 afSGLW--KNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAG-------AIEEsilshgtVA 264
Cdd:PRK03584 477 --LGFWndPDGSRYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAeiyrqveALPE-------VL 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 265 DCAVVGKEDPLKG-HVPLaLCVLRKDINATEEqVLEEIVKHVRQNIGP--VAAfrNAVFVKQLPKTRSGKIPRSALSAIV 341
Cdd:PRK03584 548 DSLVIGQEWPDGDvRMPL-FVVLAEGVTLDDA-LRARIRTTIRTNLSPrhVPD--KIIAVPDIPRTLSGKKVELPVKKLL 623
|
....
gi 1057503158 342 NGKP 345
Cdd:PRK03584 624 HGRP 627
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
122-338 |
1.57e-15 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 77.80 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 122 FRVPVLDHWWQTETgspitasCVGLgnsKTPPPGQA------GKSVPGYNVMILDDNMQKLKARCLGNIVVKLPlpPGA- 194
Cdd:PRK08008 311 FGVRLLTSYGMTET-------IVGI---IGDRPGDKrrwpsiGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGV--PGKt 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 195 -FSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKED 273
Cdd:PRK08008 379 iFKEYYLDPKATAKVLEAD--GWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKD 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1057503158 274 PLKGHVPLALCVLrkdiNATEEQVLEEIVKHVRQNIgpvAAFRNAVFV---KQLPKTRSGKIPRSALS 338
Cdd:PRK08008 457 SIRDEAIKAFVVL----NEGETLSEEEFFAFCEQNM---AKFKVPSYLeirKDLPRNCSGKIIKKNLK 517
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
137-337 |
2.65e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 76.87 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 137 SPITASCvGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYfeKFPGY 216
Cdd:PRK07656 320 SGVTTFN-RLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVR---GPNVMKGYYDDPEATAAAI--DADGW 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 217 YDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQ 296
Cdd:PRK07656 394 LHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEE 473
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1057503158 297 VLEeivkHVRQNIgpvAAF---RNAVFVKQLPKTRSGKIPRSAL 337
Cdd:PRK07656 474 LIA----YCREHL---AKYkvpRSIEFLDELPKNATGKVLKRAL 510
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
215-339 |
8.76e-15 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 75.40 E-value: 8.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 215 GYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATE 294
Cdd:PLN02246 412 GWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITE 491
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1057503158 295 EQVLEEIVKHV--RQNIGPVaafrnaVFVKQLPKTRSGKIPRSALSA 339
Cdd:PLN02246 492 DEIKQFVAKQVvfYKRIHKV------FFVDSIPKAPSGKILRKDLRA 532
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
214-339 |
1.16e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 74.31 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 214 PGYYDTMDAGYMDEeGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVlrKDINAT 293
Cdd:PRK07824 233 PGWFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVV--GDGGPA 309
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1057503158 294 EeqVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSA 339
Cdd:PRK07824 310 P--TLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
30-337 |
1.55e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 74.43 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 30 HSYICYGPL--LHGNTTVLYEGK--PVGTPDAgayfrvLAEHGVAALFTAPTAIRAIrqqdpgaalgkqYSLTRFK---- 101
Cdd:PRK07638 195 HSLFLYGAIstLYVGQTVHLMRKfiPNQVLDK------LETENISVMYTVPTMLESL------------YKENRVIenkm 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 102 TLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPITAScvgLGNSKTPPPGQAGKsvPGYNVMILDDNM--QKLKAR 179
Cdd:PRK07638 257 KIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSFVTAL---VDEESERRPNSVGR--PFHNVQVRICNEagEEVQKG 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 180 CLGNIVVKLPLppgAFSGlWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILS 259
Cdd:PRK07638 332 EIGTVYVKSPQ---FFMG-YIIGGVLARELNAD--GWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHE 405
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1057503158 260 HGTVADCAVVGKEDPLKGHVPLALCvlrkDINATEEQvleeIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 337
Cdd:PRK07638 406 HPAVDEIVVIGVPDSYWGEKPVAII----KGSATKQQ----LKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
24-337 |
1.93e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 74.46 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 24 LGWVVGHS-YICYGPLLH--GNTT----VLYEGKPVGTPD---AGAYFRVLAEH--GVAALFTAPTAIRAIRQQdPGAAL 91
Cdd:PRK09088 170 LGRVDAHSsFLCDAPMFHiiGLITsvrpVLAVGGSILVSNgfePKRTLGRLGDPalGITHYFCVPQMAQAFRAQ-PGFDA 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 92 GkqySLTRFKTLFVAGERCDVETLEWSKNVfRVPVLDHWWQTETGS--PITASCvGLGNSKTpppGQAGKSVPGYNVMIL 169
Cdd:PRK09088 249 A---ALRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMSEAGTvfGMSVDC-DVIRAKA---GAAGIPTPTVQTRVV 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 170 DDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRIS 249
Cdd:PRK09088 321 DDQGNDCPAGVPGELLLR---GPNLSPGYWRRPQATARAFTGD--GWFRTGDIARRDADGFFWVVDRKKDMFISGGENVY 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 250 AGAIEESILSHGTVADCAVVGKEDPLKGHVPLaLCVLRKDINATEeqvLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRS 329
Cdd:PRK09088 396 PAEIEAVLADHPGIRECAVVGMADAQWGEVGY-LAIVPADGAPLD---LERIRSHLSTRLAKYKVPKHLRLVDALPRTAS 471
|
....*...
gi 1057503158 330 GKIPRSAL 337
Cdd:PRK09088 472 GKLQKARL 479
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
158-339 |
2.35e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 74.31 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 158 GKSVPGYNVMILD-DNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSR 236
Cdd:PRK06178 390 GLPVPGTEFKICDfETGELLPLGAEGEIVVR---TPSLLKGYWNKPEATAEALRD---GWLHTGDIGKIDEQGFLHYLGR 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 237 VDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGP--VAA 314
Cdd:PRK06178 464 RKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTA----AALQAWCRENMAVykVPE 539
|
170 180
....*....|....*....|....*
gi 1057503158 315 FRnavFVKQLPKTRSGKIPRSALSA 339
Cdd:PRK06178 540 IR---IVDALPMTATGKVRKQDLQA 561
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
122-339 |
4.65e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 73.18 E-value: 4.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 122 FRVPVLDHWWQTETGSPITascvglgnsKTP--PPGQAGKSVPGYNVM-----------ILDDNMQKLKARCLGNIVVkl 188
Cdd:PRK07867 289 FGCVVVDGFGSTEGGVAIT---------RTPdtPPGALGPLPPGVAIVdpdtgtecppaEDADGRLLNADEAIGELVN-- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 189 PLPPGAFSGLWKNQEAFKhlyfEKF-PGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCA 267
Cdd:PRK07867 358 TAGPGGFEGYYNDPEADA----ERMrGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVA 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1057503158 268 VVGKEDPLKGHVPLALCVLRKDINATEEQVLEEIvkHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSA 339
Cdd:PRK07867 434 VYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFL--AAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
219-334 |
5.76e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 72.38 E-value: 5.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 219 TMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINateeqvL 298
Cdd:PRK08308 295 TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEID------P 368
|
90 100 110
....*....|....*....|....*....|....*.
gi 1057503158 299 EEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPR 334
Cdd:PRK08308 369 VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSR 404
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
34-332 |
7.90e-14 |
|
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: 72.36 E-value: 7.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 34 CYG-------PLLHGNTTVLY----EGKPVGtpdagayfRVLAEHGVAALFTAPTAIRAIrqqdpgAALGKQYSLTRFKT 102
Cdd:cd05909 200 SFGltgclwlPLLSGIKVVFHpnplDYKKIP--------ELIYDKKATILLGTPTFLRGY------ARAAHPEDFSSLRL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 103 LFVAGERCDVETLEWSKNVFRVPVLDHWWQTETgSPITAScvglgNSKTPP--PGQAGKSVPGYNVMILD-DNMQKLKAR 179
Cdd:cd05909 266 VVAGAEKLKDTLRQEFQEKFGIRILEGYGTTEC-SPVISV-----NTPQSPnkEGTVGRPLPGMEVKIVSvETHEEVPIG 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 180 CLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILS 259
Cdd:cd05909 340 EGGLLLVR---GPNVMLGYLNEPELTSFAFGD---GWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSE 413
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1057503158 260 H-GTVADCAVVGKEDPLKGHVpLALCVLRKDINATEeqvLEEIVKHVrqNIGPVAAFRNAVFVKQLPKTRSGKI 332
Cdd:cd05909 414 IlPEDNEVAVVSVPDGRKGEK-IVLLTTTTDTDPSS---LNDILKNA--GISNLAKPSYIHQVEEIPLLGTGKP 481
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
62-337 |
7.93e-14 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 72.29 E-value: 7.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 62 RVLAEHGVAALFTAPTAIRAIrqqDPGAALGkqysltrFKTLFVAGERCDVETLE-WSKNvfRVpVLDHWWQTETgsPIT 140
Cdd:cd17652 178 DLLREHRITHVTLPPAALAAL---PPDDLPD-------LRTLVVAGEACPAELVDrWAPG--RR-MINAYGPTET--TVC 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 141 ASCVGLGNSKTPPPgqAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPG-------AFSGLWK---NQEAfkhLYF 210
Cdd:cd17652 243 ATMAGPLPGGGVPP--IGRPVPGTRVYVLDARLR--------------PVPPGvpgelyiAGAGLARgylNRPG---LTA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 211 EKF-------PG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPL 281
Cdd:cd17652 304 ERFvadpfgaPGsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLV 383
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1057503158 282 ALCVLRKDINATEEQVLEEIVKHVRQNIGPvAAFrnaVFVKQLPKTRSGKIPRSAL 337
Cdd:cd17652 384 AYVVPAPGAAPTAAELRAHLAERLPGYMVP-AAF---VVLDALPLTPNGKLDRRAL 435
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
35-337 |
8.37e-14 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 72.23 E-value: 8.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 35 YGPLLHGNTTVLYEGKPVGTPDAGAyfRVLAEHGVAALFTAPTAIRAIRQQDPGAalgkqysLTRFKTLFVAGERCDVet 114
Cdd:cd12117 195 WGALLNGARLVLAPKGTLLDPDALG--ALIAEEGVTVLWLTAALFNQLADEDPEC-------FAGLRELLTGGEVVSP-- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 115 lewsKNVFRVpvLDHW-----WQ----TETGSPITASCVglgnskTPPPGQA-----GKSVPGYNVMILDDNMQklkarc 180
Cdd:cd12117 264 ----PHVRRV--LAACpglrlVNgygpTENTTFTTSHVV------TELDEVAgsipiGRPIANTRVYVLDEDGR------ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 181 lgnivvklPLPPGAF-------SGLWK---NQEAfkhLYFEKF------PG--YYDTMDAGYMDEEGYLYVMSRVDDVIN 242
Cdd:cd12117 326 --------PVPPGVPgelyvggDGLALgylNRPA---LTAERFvadpfgPGerLYRTGDLARWLPDGRLEFLGRIDDQVK 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 243 VAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINAteeqvlEEIVKHVRQNIGPV---AAFrnaV 319
Cdd:cd12117 395 IRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDA------AELRAFLRERLPAYmvpAAF---V 465
|
330
....*....|....*...
gi 1057503158 320 FVKQLPKTRSGKIPRSAL 337
Cdd:cd12117 466 VLDELPLTANGKVDRRAL 483
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
133-334 |
1.19e-13 |
|
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: 71.70 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 133 TETGsPITAScvglgnskTPPP----GQAGKSVPGYNVMILDDNMQKLKarclGNIVVKlplPPGAFSGLWKNQEAFKHL 208
Cdd:cd05914 268 TETA-PIISY--------SPPNrirlGSAGKVIDGVEVRIDSPDPATGE----GEIIVR---GPNVMKGYYKNPEATAEA 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 209 YFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVI-NVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHV---PLALC 284
Cdd:cd05914 332 FDKD--GWFHTGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVALAyidPDFLD 409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1057503158 285 VLRKDINATEEQVLEEIVKHVRQNigpVAAFRNAVFVK----QLPKTRSGKIPR 334
Cdd:cd05914 410 VKALKQRNIIDAIKWEVRDKVNQK---VPNYKKISKVKivkeEFEKTPKGKIKR 460
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
131-340 |
1.62e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 71.78 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 131 WQTETGSPITAscvGLGNSKTPP-----P-------GQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGL 198
Cdd:PRK12492 353 WEQLTGCTIVE---GYGLTETSPvastnPygelarlGTVGIPVPGTALKVIDDDGNELPLGERGELCIK---GPQVMKGY 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 199 WKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGH 278
Cdd:PRK12492 427 WQQPEATAEALDAE--GWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGE 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1057503158 279 VpLALCVLRKDINATeeqvLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAI 340
Cdd:PRK12492 505 A-VKLFVVARDPGLS----VEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
215-337 |
2.56e-13 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 70.94 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 215 GYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATE 294
Cdd:PRK06018 410 GFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATR 489
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1057503158 295 eqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 337
Cdd:PRK06018 490 ----EEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
36-330 |
5.10e-13 |
|
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: 69.25 E-value: 5.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 36 GPLLH------GNTTVLYEGKPVGTP--DAGAYFRVLAEHGVAALFTAPTAIRAIRQqdpgaalgkqysltrfktlFVAG 107
Cdd:cd17636 48 GPLFHigtlmfTLATFHAGGTNVFVRrvDAEEVLELIEAERCTHAFLLPPTIDQIVE-------------------LNAD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 108 ERCDVETL-------EWSKNVfrvPVLDHWW--------QTETGSPITAScvGLGNSKTpppGQAGKSVPGYNVMILDDN 172
Cdd:cd17636 109 GLYDLSSLrsspaapEWNDMA---TVDTSPWgrkpggygQTEVMGLATFA--ALGGGAI---GGAGRPSPLVQVRILDED 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 173 MQKLKARCLGNIVVKLPLppgAFSGLWK----NQEAFKHlyfekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRI 248
Cdd:cd17636 181 GREVPDGEVGEIVARGPT---VMAGYWNrpevNARRTRG-------GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 249 SAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTR 328
Cdd:cd17636 251 YPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTE----AELIEHCRARIASYKKPKSVEFADALPRTA 326
|
..
gi 1057503158 329 SG 330
Cdd:cd17636 327 GG 328
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
32-337 |
6.16e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 69.72 E-value: 6.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 32 YICYGPLLH-------------GNTTVLYEgkpvgTPDAGAYFRVLAEHGVAALFTAPTA-IRAIRQQDpgaALGKQYSL 97
Cdd:PRK13391 203 YLSPAPLYHsapqravmlvirlGGTVIVME-----HFDAEQYLALIEEYGVTHTQLVPTMfSRMLKLPE---EVRDKYDL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 98 TRFKTLFVAGERCDVETLEwsknvfrvPVLDhWWqtetgSPIT----ASCVGLGNSKTPP------PGQAGKSVPGyNVM 167
Cdd:PRK13391 275 SSLEVAIHAAAPCPPQVKE--------QMID-WW-----GPIIheyyAATEGLGFTACDSeewlahPGTVGRAMFG-DLH 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 168 ILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWKNQEAfKHlyfeKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHR 247
Cdd:PRK13391 340 ILDDDGAELPPGEPGTIWFEGGRPFEYLNDPAKTAEA-RH----PDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVN 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 248 ISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEqVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKT 327
Cdd:PRK13391 415 IYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPA-LAAELIAFCRQRLSRQKCPRSIDFEDELPRL 493
|
330
....*....|
gi 1057503158 328 RSGKIPRSAL 337
Cdd:PRK13391 494 PTGKLYKRLL 503
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
157-337 |
6.24e-13 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 69.78 E-value: 6.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 157 AGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSR 236
Cdd:PRK06087 357 DGYAAAGVEIKVVDEARKTLPPGCEGEEASR---GPNVFMGYLDEPELTARALDEE--GWYYSGDLCRMDEAGYIKITGR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 237 VDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvLEEIV-----KHVRQNIGP 311
Cdd:PRK06087 432 KKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLT---LEEVVaffsrKRVAKYKYP 508
|
170 180
....*....|....*....|....*.
gi 1057503158 312 vaafRNAVFVKQLPKTRSGKIPRSAL 337
Cdd:PRK06087 509 ----EHIVVIDKLPRTASGKIQKFLL 530
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
35-339 |
8.31e-13 |
|
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: 69.28 E-value: 8.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 35 YGPLLHGNTTVLYEGKPVGtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALgkqysltRFKTLFVAGERCDVET 114
Cdd:cd17655 197 FASLLSGNTLYIVRKETVL--DGQALTQYIRQNRITIIDLTPAHLKLLDAADDSEGL-------SLKHLIVGGEALSTEL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 115 LEWSKNVFR--VPVLDHWWQTETgsPITAS---CVGLGNSKTPPPgqAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlp 189
Cdd:cd17655 268 AKKIIELFGtnPTITNAYGPTET--TVDASiyqYEPETDQQVSVP--IGKPLGNTRIYILDQYGRPQPVGVAGELYIG-- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 190 lPPGAFSGLWKNQEafkhLYFEKF------PG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHG 261
Cdd:cd17655 342 -GEGVARGYLNRPE----LTAEKFvddpfvPGerMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHP 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 262 TVADCAVVGKEDPLKGHVPLALCVLRKDInaTEEQVLEEIVKHVRQNIGPvaafrnAVFVK--QLPKTRSGKIPRSALSA 339
Cdd:cd17655 417 DIKEAVVIARKDEQGQNYLCAYIVSEKEL--PVAQLREFLARELPDYMIP------SYFIKldEIPLTPNGKVDRKALPE 488
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
9-332 |
8.52e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 69.34 E-value: 8.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 9 IYGLQPGEVwwaasdlgwvvghsYICYGPLLHG--NTTVLYEGKPVGT----P--DAGAYFRVLAEHGVAALFTAPTAIr 80
Cdd:PRK12406 190 IYGLKPGIR--------------ALLTGPLYHSapNAYGLRAGRLGGVlvlqPrfDPEELLQLIERHRITHMHMVPTMF- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 81 aIRQQDPGAALGKQYSLTRFKTLFVAGERCDVET----LEWSKNVfrvpVLDHWWQTETGSPITAScvglGNSKTPPPGQ 156
Cdd:PRK12406 255 -IRLLKLPEEVRAKYDVSSLRHVIHAAAPCPADVkramIEWWGPV----IYEYYGSTESGAVTFAT----SEDALSHPGT 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 157 AGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGaFSglWKNQEAfKHLYFEKfPGYYDTMDAGYMDEEGYLYVMSR 236
Cdd:PRK12406 326 VGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPD-FT--YHNKPE-KRAEIDR-GGFITSGDVGYLDADGYLFLCDR 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 237 VDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHvplALC-VLRKDINATEEqvLEEIVKHVRQNIGPVAAF 315
Cdd:PRK12406 401 KRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGE---ALMaVVEPQPGATLD--EADIRAQLKARLAGYKVP 475
|
330
....*....|....*..
gi 1057503158 316 RNAVFVKQLPKTRSGKI 332
Cdd:PRK12406 476 KHIEIMAELPREDSGKI 492
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
70-270 |
8.75e-13 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 69.36 E-value: 8.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 70 AALFTAPTAIRAIRQ-QDPGAALGKQYSL--------------TRFKTLFVAGERCDVETLEWsknvFR---VPVLDHWW 131
Cdd:COG1022 304 WALAVGRRYARARLAgKSPSLLLRLKHALadklvfsklrealgGRLRFAVSGGAALGPELARF----FRalgIPVLEGYG 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 132 QTETGSPITASCvgLGNSKtppPGQAGKSVPGYNVMILDDnmqklkarclGNIVVKlplPPGAFSGLWKNQEAFKHLYFE 211
Cdd:COG1022 380 LTETSPVITVNR--PGDNR---IGTVGPPLPGVEVKIAED----------GEILVR---GPNVMKGYYKNPEATAEAFDA 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 212 KfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVA-GHRISAGAIEESILSHGTVADCAVVG 270
Cdd:COG1022 442 D--GWLHTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
22-351 |
1.04e-12 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 69.29 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 22 SDLGWVVGHSYICYG-------PLLHGNTTVLyEGKPVGTPDAG---AYFRVLAEHGVAALFT------APTAIRAIRqq 85
Cdd:PRK06060 187 EDTGLCSARMYFAYGlgnsvwfPLATGGSAVI-NSAPVTPEAAAilsARFGPSVLYGVPNFFArvidscSPDSFRSLR-- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 86 dpgaalgkqysltrfkTLFVAGERCDVETLEWSKNVFR-VPVLDHWWQTETGSPITASCVGLGNsktppPGQAGKSVPGY 164
Cdd:PRK06060 264 ----------------CVVSAGEALELGLAERLMEFFGgIPILDGIGSTEVGQTFVSNRVDEWR-----LGTLGRVLPPY 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 165 NVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFkhLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVA 244
Cdd:PRK06060 323 EIRVVAPDGTTAGPGVEGDLWVR---GPAIAKGYWNRPDSP--VANE---GWLDTRDRVCIDSDGWVTYRCRADDTEVIG 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 245 GHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVlrkdiNATEEQVLEEIVKHV-RQNIGPVAAF----RNAV 319
Cdd:PRK06060 395 GVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLV-----ATSGATIDGSVMRDLhRGLLNRLSAFkvphRFAV 469
|
330 340 350
....*....|....*....|....*....|...
gi 1057503158 320 fVKQLPKTRSGKIPRSALSAIVNGKP-YKITST 351
Cdd:PRK06060 470 -VDRLPRTPNGKLVRGALRKQSPTKPiWELSLT 501
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
35-337 |
1.14e-12 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 68.93 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 35 YGPLLHGNTTVLYEGKPVGTPDAgaYFRVLAEHGVAALFTAPT-------AIRAIRQQDPGAalgkqysltrFKTLFVAG 107
Cdd:cd17649 154 LPPLICGACVVLRPDELWASADE--LAEMVRELGVTVLDLPPAylqqlaeEADRTGDGRPPS----------LRLYIFGG 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 108 ERCDVETLeWSKNVFRVPVLDHWWQTETGSPITASCVGLGNSKTPPPGQAGKSVPGYNVMILDDNMQklkarclgnivvk 187
Cdd:cd17649 222 EALSPELL-RRWLKAPVRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPLGGRSAYILDADLN------------- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 188 lPLPPGAFSGLWKNQEAFKHLYF-------EKF-------PG--YYDTMD-AGYMDEeGYLYVMSRVDDVINVAGHRISA 250
Cdd:cd17649 288 -PVPVGVTGELYIGGEGLARGYLgrpeltaERFvpdpfgaPGsrLYRTGDlARWRDD-GVIEYLGRVDHQVKIRGFRIEL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 251 GAIEESILSHGTVADCAVVGKEDPLkGHVPLALCVLRKDinATEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSG 330
Cdd:cd17649 366 GEIEAALLEHPGVREAAVVALDGAG-GKQLVAYVVLRAA--AAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNG 442
|
....*..
gi 1057503158 331 KIPRSAL 337
Cdd:cd17649 443 KLDRKAL 449
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
196-337 |
1.34e-12 |
|
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: 68.61 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 196 SGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPL 275
Cdd:cd05915 372 GGYYGNEEATRSALTPD--GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPK 449
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1057503158 276 KGHVPLALCVLrKDINATEeqvlEEIVKHVRQNIGPVAAF-RNAVFVKQLPKTRSGKIPRSAL 337
Cdd:cd05915 450 WQERPLAVVVP-RGEKPTP----EELNEHLLKAGFAKWQLpDAYVFAEEIPRTSAGKFLKRAL 507
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
12-337 |
1.50e-12 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 68.95 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 12 LQPGEVWWAASDLGWVVGHsYICYGPLLHGNTTVLYEGKPVGTpdagAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAAL 91
Cdd:PLN03052 394 IRKGDIVCWPTNLGWMMGP-WLVYASLLNGATLALYNGSPLGR----GFAKFVQDAKVTMLGTVPSIVKTWKNTNCMAGL 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 92 gkqySLTRFKTLFVAGERCDVETLEW--SKNVFRvPVLDHWWQTETGSP-ITASCVglgnsktPPPGQAGKSVP--GYNV 166
Cdd:PLN03052 469 ----DWSSIRCFGSTGEASSVDDYLWlmSRAGYK-PIIEYCGGTELGGGfVTGSLL-------QPQAFAAFSTPamGCKL 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 167 MILDDNMQKL--KARCLGNIVVkLPLPPGAFSGLWkNQEAFKhLYFEKFPGYYDTMDAGYMDE-----EGYLYVMSRVDD 239
Cdd:PLN03052 537 FILDDSGNPYpdDAPCTGELAL-FPLMFGASSTLL-NADHYK-VYFKGMPVFNGKILRRHGDIfertsGGYYRAHGRADD 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 240 VINVAGHRISAGAIEESI-LSHGTVADCAVVGKEDPLKGhvPLALC---VLRKDINATEEqvLEEIVK----HVRQNIGP 311
Cdd:PLN03052 614 TMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPPGGG--PEQLViaaVLKDPPGSNPD--LNELKKifnsAIQKKLNP 689
|
330 340
....*....|....*....|....*.
gi 1057503158 312 VAAFRNAVFVKQLPKTRSGKIPRSAL 337
Cdd:PLN03052 690 LFKVSAVVIVPSFPRTASNKVMRRVL 715
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
35-337 |
2.02e-12 |
|
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: 68.09 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 35 YGPLLHGNTTVLYEGKpvGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALGKqysltrfkTLFVAGERCDVET 114
Cdd:cd12116 186 LLPLLAGARVVIAPRE--TQRDPEALARLIEAHSITVMQATPATWRMLLDAGWQGRAGL--------TALCGGEALPPDL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 115 LEwsKNVFRVPVLdhwWQ----TETgsPITASCVGLGNSKTPPPgqAGKSVPGYNVMILDDNMQklkarclgnivvklPL 190
Cdd:cd12116 256 AA--RLLSRVGSL---WNlygpTET--TIWSTAARVTAAAGPIP--IGRPLANTQVYVLDAALR--------------PV 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 191 PPGAFSGLWKNQEAFKHLYF-------EKF-------PG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIE 254
Cdd:cd12116 313 PPGVPGELYIGGDGVAQGYLgrpaltaERFvpdpfagPGsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 255 ESILSHGTVADCAVVGKEDPLKGHVpLALCVLRKDINATEEQVLEEIVKHVRQNIGPVAAFRnavfVKQLPKTRSGKIPR 334
Cdd:cd12116 393 AALAAHPGVAQAAVVVREDGGDRRL-VAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVR----LDALPLTANGKLDR 467
|
...
gi 1057503158 335 SAL 337
Cdd:cd12116 468 KAL 470
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
25-332 |
2.09e-12 |
|
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: 67.14 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 25 GWVVGhsyicygpLLHGNTTVlyegkPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdPGAalgKQYSLTRFKTLF 104
Cdd:cd17638 59 GIVAC--------LLTGATVV-----PVAVFDVDAILEAIERERITVLPGPPTLFQSLLDH-PGR---KKFDLSSLRAAV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 105 VAGERCDVETLEWSKNVFRV-PVLDHWWQTETGspiTASCVGLGNSKTPPPGQAGKSVPGYNVMILDDnmqklkarclGN 183
Cdd:cd17638 122 TGAATVPVELVRRMRSELGFeTVLTAYGLTEAG---VATMCRPGDDAETVATTCGRACPGFEVRIADD----------GE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 184 IVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTV 263
Cdd:cd17638 189 VLVR---GYNVMQGYLDDPEATAEAIDAD--GWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGV 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1057503158 264 ADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVleeiVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKI 332
Cdd:cd17638 264 AQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDV----IAWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
32-332 |
2.53e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 67.88 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 32 YICYGPLL-------HGNTTVLyegkPVGTPDAGAYFRVLAEHGVAALFTAPTA-IRAIRQQDPGAalgkqYSLTRFKTL 103
Cdd:PRK12583 252 YHCFGMVLanlgcmtVGACLVY----PNEAFDPLATLQAVEEERCTALYGVPTMfIAELDHPQRGN-----FDLSSLRTG 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 104 FVAGERCDVETLEWSKNVFRVP-VLDHWWQTETgSPIT------------ASCVG-------------LGNskTPPPGQA 157
Cdd:PRK12583 323 IMAGAPCPIEVMRRVMDEMHMAeVQIAYGMTET-SPVSlqttaaddlerrVETVGrtqphlevkvvdpDGA--TVPRGEI 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 158 GK-SVPGYNVMIlddnmqklkarclgnivvklplppgafsGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSR 236
Cdd:PRK12583 400 GElCTRGYSVMK----------------------------GYWNNPEATAESIDED--GWMHTGDLATMDEQGYVRIVGR 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 237 VDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFR 316
Cdd:PRK12583 450 SKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASE----EELREFCKARIAHFKVPR 525
|
330
....*....|....*.
gi 1057503158 317 NAVFVKQLPKTRSGKI 332
Cdd:PRK12583 526 YFRFVDEFPMTVTGKV 541
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
122-339 |
2.73e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 67.74 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 122 FRVPVLDHWWQTETGSPITAScvglgnsKTPPPGQAGKSVPGynVMILDDNMQKLKARC--------------LGNIVVK 187
Cdd:PRK13388 287 FGCQVEDGYGSSEGAVIVVRE-------PGTPPGSIGRGAPG--VAIYNPETLTECAVArfdahgallnadeaIGELVNT 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 188 LPlpPGAFSGLWKNQEA----FKHlyfekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTV 263
Cdd:PRK13388 358 AG--AGFFEGYYNNPEAtaerMRH-------GMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAI 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1057503158 264 ADCAVVGKEDPLKGHVPLALCVLRKDINATEEQvLEEIVkHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSA 339
Cdd:PRK13388 429 NRVAVYAVPDERVGDQVMAALVLRDGATFDPDA-FAAFL-AAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
158-336 |
4.17e-12 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 67.34 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 158 GKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLyfeKFPGYYDTMDAGYMdEEGYLYVMSRV 237
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICVR---GPSLMSGYFRDEESQDVL---AADGWLDTGDLGYL-LDGYLYITGRA 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 238 DDVINVAGHRISAGAIEESILSHGTV--ADCAVVGKEDPlKGHVPLALCVLRKDINATEEQVLEEIVKHVRQNIGpVAAF 315
Cdd:PRK09192 461 KDLIIINGRNIWPQDIEWIAEQEPELrsGDAAAFSIAQE-NGEKIVLLVQCRISDEERRGQLIHALAALVRSEFG-VEAA 538
|
170 180
....*....|....*....|.
gi 1057503158 316 RNAVFVKQLPKTRSGKIPRSA 336
Cdd:PRK09192 539 VELVPPHSLPRTSSGKLSRAK 559
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
95-343 |
1.12e-11 |
|
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: 65.77 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 95 YSLTRFKTLFVAGERCDVET-------LEWSK---NVFRvPVldhWWQTETGSPITASCVglgnSKTPPPGQA------G 158
Cdd:cd05906 286 WDLSSLRYLVNAGEAVVAKTirrllrlLEPYGlppDAIR-PA---FGMTETCSGVIYSRS----FPTYDHSQAlefvslG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 159 KSVPGYNVMILDDNMQKLKARCLGNIVVKLPLppgAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEeGYLYVMSRVD 238
Cdd:cd05906 358 RPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPV---VTKGYYNNPEANAEAFTED--GWFRTGDLGFLDN-GNLTITGRTK 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 239 DVINVAG-----HRISAgAIEE-SILSHGTVADCAVvgkEDPLKGHVPLALC-VLRKDINATEEQVLEEIVKHVRQNIGP 311
Cdd:cd05906 432 DTIIVNGvnyysHEIEA-AVEEvPGVEPSFTAAFAV---RDPGAETEELAIFfVPEYDLQDALSETLRAIRSVVSREVGV 507
|
250 260 270
....*....|....*....|....*....|...
gi 1057503158 312 VAAFRNAVFVKQLPKTRSGKIPRSAL-SAIVNG 343
Cdd:cd05906 508 SPAYLIPLPKEEIPKTSLGKIQRSKLkAAFEAG 540
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
215-339 |
1.27e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 65.78 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 215 GYYDTMDAGYMDEEGYLYVMSRVD-DVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINAt 293
Cdd:PRK07787 350 GWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAA- 428
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1057503158 294 eeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSA 339
Cdd:PRK07787 429 -----DELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2-339 |
1.54e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 66.13 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 2 LHWsMSSIYGLQPGEVWWAASDLGWVVGHsYICYGPLLHGNTTVLyeGKPVGTPDAGAYFRVLAEHGVAALFTAPTAIRA 81
Cdd:PRK12316 684 LCW-MQQAYGLGVGDTVLQKTPFSFDVSV-WEFFWPLMSGARLVV--AAPGDHRDPAKLVELINREGVDTLHFVPSMLQA 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 82 IrQQDPGAAlgkqySLTRFKTLFVAGERCDVETLEwskNVF-RVP---VLDHWWQTETGSPIT-ASCVGLGNSKTPppgq 156
Cdd:PRK12316 760 F-LQDEDVA-----SCTSLRRIVCSGEALPADAQE---QVFaKLPqagLYNLYGPTEAAIDVThWTCVEEGGDSVP---- 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 157 AGKSVPGYNVMILDDNMQKLKARCLGNIVVklplppgAFSGLWKNQEAFKHLYFEKF-PG-------YYDTMDAGYMDEE 228
Cdd:PRK12316 827 IGRPIANLACYILDANLEPVPVGVLGELYL-------AGRGLARGYHGRPGLTAERFvPSpfvagerMYRTGDLARYRAD 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 229 GYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEdplkGHVPLALCVLRKDINATEEQVLEEIVKHVRQN 308
Cdd:PRK12316 900 GVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVLESEGGDWREALKAHLAASLPEY 975
|
330 340 350
....*....|....*....|....*....|.
gi 1057503158 309 IGPVaafrNAVFVKQLPKTRSGKIPRSALSA 339
Cdd:PRK12316 976 MVPA----QWLALERLPLTPNGKLDRKALPA 1002
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
182-339 |
2.02e-11 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 65.25 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 182 GNIVVKlplppgafsGLWKNQEAFKhlyfEKFP-GYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSH 260
Cdd:PLN02479 409 GNMVMK---------GYLKNPKANE----EAFAnGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTH 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 261 GTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVL-EEIVKHVRQNIGPVAAFRNAVFvKQLPKTRSGKIPRSALSA 339
Cdd:PLN02479 476 PAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEAALaEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRA 554
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
35-332 |
2.46e-11 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 65.33 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 35 YGPLLHGNTTVlYEGKPVgtpDAGAYFRVLAEHGVAALFTAPTAIRA-IRQQ--DPgaalgkqyslTRFKTL--FVAG-E 108
Cdd:PRK08633 843 WLPLLEGIKVV-YHPDPT---DALGIAKLVAKHRATILLGTPTFLRLyLRNKklHP----------LMFASLrlVVAGaE 908
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 109 RCDVETLEWSKNVFRVPVLDHWWQTETGSPITASC-----VGLGNSKTPPPGQAGKSVPGYNVMILD-DNMQKLKARCLG 182
Cdd:PRK08633 909 KLKPEVADAFEEKFGIRILEGYGATETSPVASVNLpdvlaADFKRQTGSKEGSVGMPLPGVAVRIVDpETFEELPPGEDG 988
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 183 NIVVKlplPPGAFSGLWKNQ----EAFKHLyfeKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESI- 257
Cdd:PRK08633 989 LILIG---GPQVMKGYLGDPektaEVIKDI---DGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELa 1062
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1057503158 258 -LSHGTVADCAVVGKEDPLKGHvplALCVLRKDINATEEQVLEEIVKHVRQNIGPVAAFrnaVFVKQLPKTRSGKI 332
Cdd:PRK08633 1063 kALGGEEVVFAVTAVPDEKKGE---KLVVLHTCGAEDVEELKRAIKESGLPNLWKPSRY---FKVEALPLLGSGKL 1132
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
189-342 |
4.08e-11 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 64.24 E-value: 4.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 189 PLPPG-----------AFSGLWK----NQEAFKHlyfekfPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAI 253
Cdd:PRK10946 374 PLPQGevgrlmtrgpyTFRGYYKspqhNASAFDA------NGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEI 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 254 EESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATeeqvleEIVKHVRQNigPVAAFR---NAVFVKQLPKTRSG 330
Cdd:PRK10946 448 ENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKAV------QLRRFLREQ--GIAEFKlpdRVECVDSLPLTAVG 519
|
170
....*....|..
gi 1057503158 331 KIPRSALSAIVN 342
Cdd:PRK10946 520 KVDKKQLRQWLA 531
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
214-342 |
4.36e-11 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 63.86 E-value: 4.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 214 PGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINAt 293
Cdd:PRK07445 323 QGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSIS- 401
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1057503158 294 eeqvLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVN 342
Cdd:PRK07445 402 ----LEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAV 446
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
29-363 |
6.46e-11 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 63.65 E-value: 6.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 29 GHSYICYGPLLHgnttVLYEGKPVGTPDAGAYFrVLAEHGVaalfTAPTAIRAIRQQDPGAALG---------------- 92
Cdd:PRK05620 224 GESFLCCVPIYH----VLSWGVPLAAFMSGTPL-VFPGPDL----SAPTLAKIIATAMPRVAHGvptlwiqlmvhylknp 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 93 -KQYSLTrfkTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETgSPItascvglGNSKTPPPGQAGKSVPGYNV----- 166
Cdd:PRK05620 295 pERMSLQ---EIYVGGSAVPPILIKAWEERYGVDVVHVWGMTET-SPV-------GTVARPPSGVSGEARWAYRVsqgrf 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 167 -------MILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWKNQEAFKHLYF---------EKFP--GYYDTMDAGYMDEE 228
Cdd:PRK05620 364 pasleyrIVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPTEEGGGAASTFrgedvedanDRFTadGWLRTGDVGSVTRD 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 229 GYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVlEEIVKHVRQN 308
Cdd:PRK05620 444 GFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETA-ERLRDQLRDR 522
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1057503158 309 IGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNGKPYKITsTIEDPSIFGHVEE 363
Cdd:PRK05620 523 LPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHLADGDFEII-KLKGPGESGESDS 576
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
157-336 |
1.02e-10 |
|
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: 63.03 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 157 AGKSVPGYNVMILDDN-MQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKFP----GYYDTMDAGYMDEeGYL 231
Cdd:cd05931 357 CGRPLPDQEVRIVDPEtGRELPDGEVGEIWVR---GPSVASGYWGRPEATAETFGALAAtdegGWLRTGDLGFLHD-GEL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 232 YVMSRVDDVINVAGHRISAGAIEESILSH------GTVADCAVVGKEDplkGHVPLALCVLRKDINATEEQVLEEIVKHV 305
Cdd:cd05931 433 YITGRLKDLIIVRGRNHYPQDIEATAEEAhpalrpGCVAAFSVPDDGE---ERLVVVAEVERGADPADLAAIAAAIRAAV 509
|
170 180 190
....*....|....*....|....*....|...
gi 1057503158 306 RQNIGpVAAfRNAVFVKQ--LPKTRSGKIPRSA 336
Cdd:cd05931 510 AREHG-VAP-ADVVLVRPgsIPRTSSGKIQRRA 540
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
99-337 |
1.05e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 62.80 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 99 RFKTL---FVAGERCDVETLEWSKNVFRVPVLDHWWQTETgSPITASCVgLGNSKTPPPGQA--------GKSVPGYNVM 167
Cdd:PRK07008 291 RFSTLrrtVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEM-SPLGTLCK-LKWKHSQLPLDEqrkllekqGRVIYGVDMK 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 168 ILDDNMQKL--KARCLGNIVVKLPlppgafsglWKNQEAFKHlyfEKFP---GYYDTMDAGYMDEEGYLYVMSRVDDVIN 242
Cdd:PRK07008 369 IVGDDGRELpwDGKAFGDLQVRGP---------WVIDRYFRG---DASPlvdGWFPTGDVATIDADGFMQITDRSKDVIK 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 243 VAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRqniGPVAAFR---NAV 319
Cdd:PRK07008 437 SGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTR----EELLAFYE---GKVAKWWipdDVV 509
|
250
....*....|....*...
gi 1057503158 320 FVKQLPKTRSGKIPRSAL 337
Cdd:PRK07008 510 FVDAIPHTATGKLQKLKL 527
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
158-341 |
3.70e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 61.17 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 158 GKSVPGYNVMILDDNMQKLKARCLGNIVVKLP-LPPG--AFSGLWKNQEAfkhlyfekfPGYYDTMDAGYMDEEGYLYVM 234
Cdd:PRK07768 363 GPPLPGLEVRVVDEDGQVLPPRGVGVIELRGEsVTPGylTMDGFIPAQDA---------DGWLDTGDLGYLTEEGEVVVC 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 235 SRVDDVINVAGHRISAGAIEESILS-HGTVADCAV-VGKEDPLK--GHVPLALCVLRKDInATEEQVLEEIVKHVRQNIG 310
Cdd:PRK07768 434 GRVKDVIIMAGRNIYPTDIERAAARvEGVRPGNAVaVRLDAGHSreGFAVAVESNAFEDP-AEVRRIRHQVAHEVVAEVG 512
|
170 180 190
....*....|....*....|....*....|...
gi 1057503158 311 pvAAFRNAVFVK--QLPKTRSGKIPRSALSAIV 341
Cdd:PRK07768 513 --VRPRNVVVLGpgSIPKTPSGKLRRANAAELV 543
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
37-337 |
6.19e-10 |
|
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: 60.37 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 37 PLLHGNTTVLYEgkPVGTPDAGAYFRVLAEHGVAALFTAPTAIRA-IRQQDPGAALgkqySLTRfktLFVAGERCDVETL 115
Cdd:cd17646 200 PLVAGARLVVAR--PGGHRDPAYLAALIREHGVTTCHFVPSMLRVfLAEPAAGSCA----SLRR---VFCSGEALPPELA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 116 EWSKNVFRVPVLDHWWQTETGSPITA-SCVGlgnSKTPPPGQAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPGA 194
Cdd:cd17646 271 ARFLALPGAELHNLYGPTEAAIDVTHwPVRG---PAETPSVPIGRPVPNTRLYVLDDALR--------------PVPVGV 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 195 FSGL----------WKNQEAfkhLYFEKF------PG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEES 256
Cdd:cd17646 334 PGELylggvqlargYLGRPA---LTAERFvpdpfgPGsrMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 257 ILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEEivkHVRQNIGPV---AAFrnaVFVKQLPKTRSGKIP 333
Cdd:cd17646 411 LAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPDTAALRA---HLAERLPEYmvpAAF---VVLDALPLTANGKLD 484
|
....
gi 1057503158 334 RSAL 337
Cdd:cd17646 485 RAAL 488
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
111-338 |
6.61e-10 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 60.29 E-value: 6.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 111 DVETLEWSKNVFRVPVLDHWWQTETGSPITASCV-GLGNSKTP--PPGQAGKSVpGYNVMILDDNMQKLKARCLGNIVVK 187
Cdd:PRK05852 308 TAETAQALQTEFAAPVVCAFGMTEATHQVTTTQIeGIGQTENPvvSTGLVGRST-GAQIRIVGSDGLPLPAGAVGEVWLR 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 188 LPLPPGAFSGLWKNQEA-FKHlyfekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADC 266
Cdd:PRK05852 387 GTTVVRGYLGDPTITAAnFTD-------GWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEA 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057503158 267 AVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPV---AAFRNAvfvKQLPKTRSGKIPRSALS 338
Cdd:PRK05852 460 AVFGVPDQLYGEAVAAVIVPRESAPPTA----EELVQFCRERLAAFeipASFQEA---SGLPHTAKGSLDRRAVA 527
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
35-337 |
1.88e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 59.59 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 35 YGPLLHGNTTVLyegKPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAAlgkqySLTRFKTLFVAGERCDVET 114
Cdd:PRK12316 4754 YHPLINGASVVI---RDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDG-----EPPSLRVYCFGGEAVAQAS 4825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 115 L-EWSKNVFRVPVLDHWWQTETG-SPITASCvglgnSKTPPPGQA----GKSVPGYNVMILDDNMQklkarclgnivvkl 188
Cdd:PRK12316 4826 YdLAWRALKPVYLFNGYGPTETTvTVLLWKA-----RDGDACGAAympiGTPLGNRSGYVLDGQLN-------------- 4886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 189 PLPPGAFSGLWKNQEAFKHLYF-------EKF-------PG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGA 252
Cdd:PRK12316 4887 PLPVGVAGELYLGGEGVARGYLerpaltaERFvpdpfgaPGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGE 4966
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 253 IEESILSHGTVADCAVVGKEDPLKGH-----VPLALCVLrkDINATEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKT 327
Cdd:PRK12316 4967 IEARLREHPAVREAVVIAQEGAVGKQlvgyvVPQDPALA--DADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLT 5044
|
330
....*....|
gi 1057503158 328 RSGKIPRSAL 337
Cdd:PRK12316 5045 PNGKLDRKAL 5054
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
56-337 |
2.19e-09 |
|
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: 58.63 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 56 DAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpgaALGKQYSLTRFKTLFVAGERCDVETLEWSKNVF--RVPVLDHWWQT 133
Cdd:cd17650 173 DPAALYDLILKSRITLMESTPALIRPVMAY----VYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFgqGMRIINSYGVT 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 134 ET---GSPITASCVGLGNSKTPPpgqAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGLW----------- 199
Cdd:cd17650 249 EAtidSTYYEEGRDPLGDSANVP---IGRPLPNTAMYVLDERLQ--------------PQPVGVAGELYiggagvargyl 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 200 ----KNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPl 275
Cdd:cd17650 312 nrpeLTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDK- 390
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1057503158 276 KGHVPL-ALCVLRKDINATEeqVLEEIVKHVRQNIGPvAAFrnaVFVKQLPKTRSGKIPRSAL 337
Cdd:cd17650 391 GGEARLcAYVVAAATLNTAE--LRAFLAKELPSYMIP-SYY---VQLDALPLTPNGKVDRRAL 447
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
59-337 |
3.27e-09 |
|
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: 58.22 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 59 AYFRVLAEHGVAALFTAPTAIRAIrqqdpgaalgkqysltrfktlFVAGERCDVETLE-WSKNVF-RVPVLDHWWQTEtg 136
Cdd:cd17644 206 AYWHLLVLELLLSTIDLPSSLRLV---------------------IVGGEAVQPELVRqWQKNVGnFIQLINVYGPTE-- 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 137 SPITASCVGL-----GNSKTPPpgqAGKSVPGYNVMILDDNMQKLKARCLGNIVV-KLPLPPGAFSGLWKNQEAFKHLYF 210
Cdd:cd17644 263 ATIAATVCRLtqlteRNITSVP---IGRPIANTQVYILDENLQPVPVGVPGELHIgGVGLARGYLNRPELTAEKFISHPF 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 211 EKFPG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRK 288
Cdd:cd17644 340 NSSESerLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHY 419
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1057503158 289 D-INATEEqvLEEIVKHVRQNIGPVAAFrnaVFVKQLPKTRSGKIPRSAL 337
Cdd:cd17644 420 EeSPSTVE--LRQFLKAKLPDYMIPSAF---VVLEELPLTPNGKIDRRAL 464
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
38-338 |
4.21e-09 |
|
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: 57.70 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 38 LLHGNTTVLyegkpvgtPDAGAYFRVLAEHgVAALFTAPTAIRAIRQQDpgaalgkqysLTRFKTLFVAGERCdvetlew 117
Cdd:cd17653 168 LCNGGTLVL--------ADPSDPFAHVART-VDALMSTPSILSTLSPQD----------FPNLKTIFLGGEAV------- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 118 SKnvfrvPVLDHWWQ----------TETgspitaSCVGLGNSKTPppGQA---GKSVPGYNVMILDDNMQKLKARCLGNI 184
Cdd:cd17653 222 PP-----SLLDRWSPgrrlynaygpTEC------TISSTMTELLP--GQPvtiGKPIPNSTCYILDADLQPVPEGVVGEI 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 185 VVklpLPPGAFSGLWKNQEA----FKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESIL-S 259
Cdd:cd17653 289 CI---SGVQVARGYLGNPALtaskFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLqS 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 260 HGTVADCAVVGKEDPLKGHV-PLalcvlrkdiNATEEQVLEEIVKHVRQNIGP---VAafrnavfVKQLPKTRSGKIPRS 335
Cdd:cd17653 366 QPEVTQAAAIVVNGRLVAFVtPE---------TVDVDGLRSELAKHLPSYAVPdriIA-------LDSFPLTANGKVDRK 429
|
...
gi 1057503158 336 ALS 338
Cdd:cd17653 430 ALR 432
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
35-339 |
7.17e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 57.66 E-value: 7.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 35 YGPLLHGNTTVLyeGKPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIrQQDPGAAlgkqySLTRFKTLFVAGERCDVET 114
Cdd:PRK12316 3256 FWPLMSGARVVL--AGPEDWRDPALLVELINSEGVDVLHAYPSMLQAF-LEEEDAH-----RCTSLKRIVCGGEALPADL 3327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 115 LEwsKNVFRVPVLDHWWQTETGSPITASCVGLGNSKTPPpgqAGKSVPGYNVMILDDNMQKLKARCLGNIVVK-LPLPPG 193
Cdd:PRK12316 3328 QQ--QVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAVP---IGRPIANRACYILDGSLEPVPVGALGELYLGgEGLARG 3402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 194 AFSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKE- 272
Cdd:PRK12316 3403 YHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDg 3482
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1057503158 273 DPLKGHVPLalcvlrkdiNATEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSA 339
Cdd:PRK12316 3483 RQLVAYVVP---------EDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPR 3540
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
38-338 |
8.99e-09 |
|
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: 56.64 E-value: 8.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 38 LLHGNTTVLYEGKPVGTPDAgaYFRVLAEHGVAALFTAPTAIRAIRqqdpgaaLGKQYSLTRfktLFVAGERCDVETLEW 117
Cdd:cd17648 159 LLNGQKLVVPPDEMRFDPDR--FYAYINREKVTYLSGTPSVLQQYD-------LARLPHLKR---VDAAGEEFTAPVFEK 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 118 SKNVFRVPVLDHWWQTETGspITascvglgNSKTPPPGQA------GKSVPGYNVMILDDNMQklkarclgnivvklPLP 191
Cdd:cd17648 227 LRSRFAGLIINAYGPTETT--VT-------NHKRFFPGDQrfdkslGRPVRNTKCYVLNDAMK--------------RVP 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 192 PGAFSGL----------WKNQEAfkhLYFEKF----------------PGYYDTMDAGYMDEEGYLYVMSRVDDVINVAG 245
Cdd:cd17648 284 VGAVGELylggdgvargYLNRPE---LTAERFlpnpfqteqerargrnARLYKTGDLVRWLPSGELEYLGRNDFQVKIRG 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 246 HRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPlalcvLRKDINA---TEEQVLEE--IVKHVRQNIGPVAAFRNAVF 320
Cdd:cd17648 361 QRIEPGEVEAALASYPGVRECAVVAKEDASQAQSR-----IQKYLVGyylPEPGHVPEsdLLSFLRAKLPRYMVPARLVR 435
|
330
....*....|....*...
gi 1057503158 321 VKQLPKTRSGKIPRSALS 338
Cdd:cd17648 436 LEGIPVTINGKLDVRALP 453
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
49-274 |
3.51e-08 |
|
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: 55.12 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 49 GKPVGTPDAGAY-------FRVLAEH-GVAALFTAPTAirairqqdpGAALGKQysltrfktlfvagercdvetlewskn 120
Cdd:cd17641 295 GRPVSLWLRLASwladallFRPLRDRlGFSRLRSAATG---------GAALGPD-------------------------- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 121 VFR------VPVLDHWWQTETGSPITASCVGlgnskTPPPGQAGKSVPGYNVMIldDNMqklkarclGNIVVKlplPPGA 194
Cdd:cd17641 340 TFRffhaigVPLKQLYGQTELAGAYTVHRDG-----DVDPDTVGVPFPGTEVRI--DEV--------GEILVR---SPGV 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 195 FSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVA-GHRISAGAIEESILSHGTVADCAVVGKED 273
Cdd:cd17641 402 FVGYYKNPEATAEDFDED--GWLHTGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQFIENKLKFSPYIAEAVVLGAGR 479
|
.
gi 1057503158 274 P 274
Cdd:cd17641 480 P 480
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
133-348 |
6.71e-08 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 54.24 E-value: 6.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 133 TETGSpiTASCVGLGNSKTP--PPGQAGKSVPGYNVMILDDN------MQKLKARCLGNIVVKlplPPGAFSGLWKNQEA 204
Cdd:PRK05857 320 SETGC--TALCLPTDDGSIVkiEAGAVGRPYPGVDVYLAATDgigptaPGAGPSASFGTLWIK---SPANMLGYWNNPER 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 205 FKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGH-VPLAL 283
Cdd:PRK05857 395 TAEVLID---GWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGAlVGLAV 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1057503158 284 cVLRKDINATEEQVLEE-IVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNGKPYKI 348
Cdd:PRK05857 472 -VASAELDESAARALKHtIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATADKARV 536
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
213-331 |
8.55e-08 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 53.54 E-value: 8.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 213 FPGYYDTMDAGymdeeGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINA 292
Cdd:cd05924 248 VPGDRATVEAD-----GTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREGAGV 322
|
90 100 110
....*....|....*....|....*....|....*....
gi 1057503158 293 TEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGK 331
Cdd:cd05924 323 DL----EELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
56-351 |
9.71e-08 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 53.65 E-value: 9.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 56 DAGAYFRVLAEHGVAALFTAPTAIRAIRQqdPGAALGKQYSLTRFKTLFVAGERCDVETLEWSKNVF-RVPVLDHWWQTE 134
Cdd:PLN02860 248 DAKAALQAIKQHNVTSMITVPAMMADLIS--LTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFpNAKLFSAYGMTE 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 135 TGSPIT----------------ASCVGLGNSKTPPPGQA--GKSVPGYNVMILDDNMQKLkarclGNIVVKlplPPGAFS 196
Cdd:PLN02860 326 ACSSLTfmtlhdptlespkqtlQTVNQTKSSSVHQPQGVcvGKPAPHVELKIGLDESSRV-----GRILTR---GPHVML 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 197 GLW-KNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPL 275
Cdd:PLN02860 398 GYWgQNSETASVLSND---GWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSR 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 276 KGHVPLALCVLR---------KDINATEEQVLEEIVK-HVRQnigpvaafrnavfvkqlpKTRSG-KIPRsalSAIVNGK 344
Cdd:PLN02860 475 LTEMVVACVRLRdgwiwsdneKENAKKNLTLSSETLRhHCRE------------------KNLSRfKIPK---LFVQWRK 533
|
....*..
gi 1057503158 345 PYKITST 351
Cdd:PLN02860 534 PFPLTTT 540
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
182-330 |
1.01e-07 |
|
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: 53.59 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 182 GNIVVKLPLPP-GAFSGLWKNQEAFKHLY----FEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEES 256
Cdd:cd05937 300 GEMLGRVPFKNrEAFQGYLHNEDATESKLvrdvFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADV 379
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057503158 257 ILSHGTVADCAVVGKEDP-LKGHVPLALCVLRKDINATEEQVLEEIVKHVRQNigpVAAFRNAVFVKQLPKTRSG 330
Cdd:cd05937 380 LGAHPDIAEANVYGVKVPgHDGRAGCAAITLEESSAVPTEFTKSLLASLARKN---LPSYAVPLFLRLTEEVATT 451
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
215-332 |
1.07e-07 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 53.66 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 215 GYYD----------------TMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGH 278
Cdd:PRK08315 411 GYWNdpektaeaidadgwmhTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGE 490
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1057503158 279 VPLALCVLRKDINATEEQVLE---------EIVKHVRqnigpvaafrnavFVKQLPKTRSGKI 332
Cdd:PRK08315 491 EVCAWIILRPGATLTEEDVRDfcrgkiahyKIPRYIR-------------FVDEFPMTVTGKI 540
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
217-337 |
3.17e-07 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 51.89 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 217 YDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQ 296
Cdd:cd12114 361 YRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIAPDA 440
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1057503158 297 VLEEIVKHVRQNIGPvaafRNAVFVKQLPKTRSGKIPRSAL 337
Cdd:cd12114 441 LRAFLAQTLPAYMIP----SRVIALEALPLTANGKVDRAAL 477
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
214-331 |
4.93e-07 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 51.63 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 214 PGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHvplALCVLRKDINAT 293
Cdd:PRK08043 590 RGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGE---ALVLFTTDSELT 666
|
90 100 110
....*....|....*....|....*....|....*....
gi 1057503158 294 EEQVLeeivKHVRQNIGP-VAAFRNAVFVKQLPKTRSGK 331
Cdd:PRK08043 667 REKLQ----QYAREHGVPeLAVPRDIRYLKQLPLLGSGK 701
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
158-336 |
1.78e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 50.17 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 158 GKSVPGYNVMILDDN-MQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfPG--YYDTMDAGYMdEEGYLYVM 234
Cdd:PRK05691 373 GRSQPGHAVLIVDPQsLEVLGDNRVGEIWAS---GPSIAHGYWRNPEASAKTFVEH-DGrtWLRTGDLGFL-RDGELFVT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 235 SRVDDVINVAGHRISAGAIEESI------LSHGTVADCAVvgKEDPLKGhVPLALCVLRKDINATEEQVLeeiVKHVRQN 308
Cdd:PRK05691 448 GRLKDMLIVRGHNLYPQDIEKTVerevevVRKGRVAAFAV--NHQGEEG-IGIAAEISRSVQKILPPQAL---IKSIRQA 521
|
170 180 190
....*....|....*....|....*....|....
gi 1057503158 309 IGpvAAFRNAVFV------KQLPKTRSGKIPRSA 336
Cdd:PRK05691 522 VA--EACQEAPSVvlllnpGALPKTSSGKLQRSA 553
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
158-337 |
2.25e-06 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 49.09 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 158 GKSVPGYNVMILDDNMQKLKARCLGNIVVklplppgAFSGLWKNQEAFKHLYFEKF------PG--YYDTMDAGYMDEEG 229
Cdd:cd17645 265 GKPIDNTRVYILDEALQLQPIGVAGELCI-------AGEGLARGYLNRPELTAEKFivhpfvPGerMYRTGDLAKFLPDG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 230 YLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDplKGHVPlALCVLrkdINATEEQVLEEIVKHVRQNI 309
Cdd:cd17645 338 NIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKED--ADGRK-YLVAY---VTAPEEIPHEELREWLKNDL 411
|
170 180
....*....|....*....|....*...
gi 1057503158 310 GPVAAFRNAVFVKQLPKTRSGKIPRSAL 337
Cdd:cd17645 412 PDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
158-343 |
3.10e-06 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 48.74 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 158 GKSVPGYNVMILDDNMQKLKARCLGNIVVKLP-LPPGAFSGLWKNQEAFKHlyFEKFPGYYdTMDAGYMDEeGYLYVMSR 236
Cdd:PRK04813 321 GYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPsVSKGYLNNPEKTAEAFFT--FDGQPAYH-TGDAGYLED-GLLFYQGR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 237 VDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEEIVKHVRQNIGPVAAFR 316
Cdd:PRK04813 397 IDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFEREFELTKAIKKELKERLMEYMIPR 476
|
170 180
....*....|....*....|....*..
gi 1057503158 317 NAVFVKQLPKTRSGKIPRSALSAIVNG 343
Cdd:PRK04813 477 KFIYRDSLPLTPNGKIDRKALIEEVNK 503
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
215-347 |
3.61e-06 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 49.19 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 215 GYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHvPLALCVLRKDINAte 294
Cdd:PRK06814 1010 GWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGE-RIILLTTASDATR-- 1086
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1057503158 295 eqvlEEIVKHVRQN-IGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNGKPYK 347
Cdd:PRK06814 1087 ----AAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKIDYVAVTKLAEEAAAK 1136
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
35-331 |
4.03e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 48.73 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 35 YGPLLHGNTTVLYegkPVGTPDAGAYFRVLAEHGVAALFTAPTA-----IRAIRQqdpgaalGKQYSLTRFKTLFVAG-- 107
Cdd:PRK07798 238 FAALFSGQTVVLL---PDVRFDADEVWRTIEREKVNVITIVGDAmarplLDALEA-------RGPYDLSSLFAIASGGal 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 108 --ERCDVETLEWSKNVFrvpVLDHWWQTETGSpitascVGLGNSKTPPPGQAGKSV-PGYNVMILDDNMQKLK------- 177
Cdd:PRK07798 308 fsPSVKEALLELLPNVV---LTDSIGSSETGF------GGSGTVAKGAVHTGGPRFtIGPRTVVLDEDGNPVEpgsgeig 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 178 --ARClGNIvvklPLppgafsGLWKNQEAFKHLYFEK------FPGYYDTMDAgymdeEGYLYVMSRVDDVINVAGHRIS 249
Cdd:PRK07798 379 wiARR-GHI----PL------GYYKDPEKTAETFPTIdgvryaIPGDRARVEA-----DGTITLLGRGSVCINTGGEKVF 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 250 AGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRS 329
Cdd:PRK07798 443 PEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDL----AELRAHCRSSLAGYKVPRAIWFVDEVQRSPA 518
|
..
gi 1057503158 330 GK 331
Cdd:PRK07798 519 GK 520
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
217-337 |
6.09e-06 |
|
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: 47.85 E-value: 6.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 217 YDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINatEEQ 296
Cdd:cd17656 364 YRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELN--ISQ 441
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1057503158 297 VLEEIVKHVRQNIGPvAAFrnaVFVKQLPKTRSGKIPRSAL 337
Cdd:cd17656 442 LREYLAKQLPEYMIP-SFF---VPLDQLPLTPNGKVDRKAL 478
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
35-337 |
8.70e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 47.85 E-value: 8.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 35 YGPLLHGNTTVLYEGKpVGTPDAgaYFRVLAEHGVAALFTAPTAIRAIRQQDPGAalgkqySLTRFKTLFVAGERCDVET 114
Cdd:PRK12467 3297 LWTLICGGCLVVRDND-LWDPEE--LWQAIHAHRISIACFPPAYLQQFAEDAGGA------DCASLDIYVFGGEAVPPAA 3367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 115 LEWSKNVF-RVPVLDHWWQTETGSPITASCVGLGNSKTPPPGQAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPG 193
Cdd:PRK12467 3368 FEQVKRKLkPRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLN--------------PVPVG 3433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 194 AFSGLWKNQEAFKHLYFEK------------FPG----YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESI 257
Cdd:PRK12467 3434 VAGELYIGGVGLARGYHQRpsltaerfvadpFSGsggrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARL 3513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 258 LSHGTVADCAVVGKeDPLKGHVPLALCVLrkdiNATEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 337
Cdd:PRK12467 3514 LQHPSVREAVVLAR-DGAGGKQLVAYVVP----ADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
34-339 |
2.03e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 46.87 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 34 CYGPLLHGNTTVLyegKPVGTPDAGAYFRVLAEHGVAALFTAPT-----AIRAIRQQDPGAAlgkqysltrfKTLFVAGE 108
Cdd:PRK12316 2205 WFHPLLNGARVLI---RDDELWDPEQLYDEMERHGVTILDFPPVylqqlAEHAERDGRPPAV----------RVYCFGGE 2271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 109 RCDVETLE-WSKNVFRVPVLDHWWQTETG-SPITASC--VGLGNSKTPPPGQAGKSVPGYnvmILDDNMQklkarclgni 184
Cdd:PRK12316 2272 AVPAASLRlAWEALRPVYLFNGYGPTEAVvTPLLWKCrpQDPCGAAYVPIGRALGNRRAY---ILDADLN---------- 2338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 185 vvklPLPPGAFSGLWKNQEAFKHLYFEKfPG-----------------YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHR 247
Cdd:PRK12316 2339 ----LLAPGMAGELYLGGEGLARGYLNR-PGltaerfvpdpfsasgerLYRTGDLARYRADGVVEYLGRIDHQVKIRGFR 2413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 248 ISAGAIEESILSHGTVADCAVVGKEDPlkGHVPLALCVLRKDInatEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKT 327
Cdd:PRK12316 2414 IELGEIEARLQAHPAVREAVVVAQDGA--SGKQLVAYVVPDDA---AEDLLAELRAWLAARLPAYMVPAHWVVLERLPLN 2488
|
330
....*....|..
gi 1057503158 328 RSGKIPRSALSA 339
Cdd:PRK12316 2489 PNGKLDRKALPK 2500
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
217-340 |
4.40e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 45.54 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 217 YDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHvpLALCVLRKDINATEEQ 296
Cdd:PRK05691 4104 YRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNGKH--LVGYLVPHQTVLAQGA 4181
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1057503158 297 VLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAI 340
Cdd:PRK05691 4182 LLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPAL 4225
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
158-338 |
9.84e-05 |
|
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: 44.02 E-value: 9.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 158 GKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMdEEGYLYVMSRV 237
Cdd:cd05908 317 GKPIDETDIRICDEDNKILPDGYIGHIQIR---GKNVTPGYYNNPEATAKVFTDD--GWLKTGDLGFI-RNGRLVITGRE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 238 DDVI-----NVAGHRISAGAIEESILSHGTVADCAVVGKEDplKGHVPLALCVLRKDINATEEQVlEEIVKHVRQNIGpv 312
Cdd:cd05908 391 KDIIfvngqNVYPHDIERIAEELEGVELGRVVACGVNNSNT--RNEEIFCFIEHRKSEDDFYPLG-KKIKKHLNKRGG-- 465
|
170 180
....*....|....*....|....*.
gi 1057503158 313 AAFRNAVFVKQLPKTRSGKIPRSALS 338
Cdd:cd05908 466 WQINEVLPIRRIPKTTSGKVKRYELA 491
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
192-337 |
1.48e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 43.58 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 192 PGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGK 271
Cdd:PRK06164 385 PSLMRGYLDNPDATARALTDD--GYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA 462
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 272 EdpLKGH-VPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSG---KIPRSAL 337
Cdd:PRK06164 463 T--RDGKtVPVAFVIPTDGASPDE----AGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRL 526
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
8-300 |
1.29e-03 |
|
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: 40.52 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 8 SIYGLQPGEVWWAASDLgwvvghsYICYGPLLhGNTTVLYEGKPV--GTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQ 85
Cdd:cd05910 119 QLYGIRPGEVDLATFPL-------FALFGPAL-GLTSVIPDMDPTrpARADPQKLVGAIRQYGVSIVFGSPALLERVARY 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 86 dpGAALGKQysLTRFKTLFVAGERCDVETLEWSKNVF--RVPVLDHWWQTETgSPITA-SCVGLGNSKTPPPGQA----- 157
Cdd:cd05910 191 --CAQHGIT--LPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEA-LPVSSiGSRELLATTTAATSGGagtcv 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 158 GKSVPGYNVMILD---------DNMQKLKARCLGNIVVKLPL---------PPGAFSGLWKNQEAFKHlyfekfpgyyDT 219
Cdd:cd05910 266 GRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTvtptyvnrpVATALAKIDDNSEGFWH----------RM 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 220 MDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHvPLaLCVLRKDINATEEQVLE 299
Cdd:cd05910 336 GDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQL-PV-LCVEPLPGTITPRARLE 413
|
.
gi 1057503158 300 E 300
Cdd:cd05910 414 Q 414
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
195-327 |
1.83e-03 |
|
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: 40.03 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 195 FSGLWKNQEAFKHLY---FEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGK 271
Cdd:cd05940 300 FDGYTDPAATEKKILrdvFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGV 379
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1057503158 272 EDP-LKGHVPLALCVLRkdinATEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKT 327
Cdd:cd05940 380 QVPgTDGRAGMAAIVLQ----PNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEIT 432
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
89-257 |
1.96e-03 |
|
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: 40.03 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 89 AALGkqysLTRFKTLFVAGERCDVETLEW--SKNVfrvPVLDHWWQTETGSPITAScvGLGNSKTpppGQAGKSVPGYNV 166
Cdd:cd05933 315 KALG----LDRCQKFFTGAAPISRETLEFflSLNI---PIMELYGMSETSGPHTIS--NPQAYRL---LSCGKALPGCKT 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 167 MILDDNMQKLKARCL-GNIVvklplppgaFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVA- 244
Cdd:cd05933 383 KIHNPDADGIGEICFwGRHV---------FMGYLNMEDKTEEAIDED--GWLHSGDLGKLDEDGFLYITGRIKELIITAg 451
|
170
....*....|...
gi 1057503158 245 GHRISAGAIEESI 257
Cdd:cd05933 452 GENVPPVPIEDAV 464
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
217-341 |
2.00e-03 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 39.83 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 217 YDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVAD--CAVVGKEDPLKGHVPLALCVLRKDINATE 294
Cdd:cd05918 337 YRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKevVVEVVKPKDGSSSPQLVAFVVLDGSSSGS 416
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1057503158 295 EQVLEEIVKHVRQNIGPVAAFRNA--------------VFVKQLPKTRSGKIPRSALSAIV 341
Cdd:cd05918 417 GDGDSLFLEPSDEFRALVAELRSKlrqrlpsymvpsvfLPLSHLPLTASGKIDRRALRELA 477
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
10-309 |
4.24e-03 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 39.11 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 10 YGLQPGEVwwaasDLgwvvgHSY---ICYGPLLhGNTTVLYE---GKPvGTPDAGAYFRVLAEHGVAALFTAPTAIRAIR 83
Cdd:PRK09274 210 YGIEPGEI-----DL-----PTFplfALFGPAL-GMTSVIPDmdpTRP-ATVDPAKLFAAIERYGVTNLFGSPALLERLG 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 84 QqdpgAALGKQYSLTRFKTLFVAG--------ERC------DVETLewskNVF----RVPV---------LDHWWQTETG 136
Cdd:PRK09274 278 R----YGEANGIKLPSLRRVISAGapvpiaviERFramlppDAEIL----TPYgateALPIssiesreilFATRAATDNG 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 137 SPItasCVGlgnsktpppgqagKSVPGYNVMILD---------DNMQKLKARCLGNIVVKLPL-------PPGA--FSGL 198
Cdd:PRK09274 350 AGI---CVG-------------RPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVAGPMvtrsyynRPEAtrLAKI 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057503158 199 WKNQEAFKHlyfekfpgyyDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKedPLKGH 278
Cdd:PRK09274 414 PDGQGDVWH----------RMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGV--GVPGA 481
|
330 340 350
....*....|....*....|....*....|..
gi 1057503158 279 VPLALCV-LRKDINATEEQVLEEIVKHVRQNI 309
Cdd:PRK09274 482 QRPVLCVeLEPGVACSKSALYQELRALAAAHP 513
|
|
| |
