|
Name |
Accession |
Description |
Interval |
E-value |
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
47-497 |
0e+00 |
|
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: 834.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 47 VPEYFNFASDVLDRWAKVEKEGKKTKNPALWWVDGDGEEVKWSFEELGVLSRKAANVLSGACSLQCGDRVLLLLPRIPEW 126
Cdd:cd05928 1 VPEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 127 WLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVITNDSVASTVESVEADCQSLKFKLLVSEGHREGWLSFKDLLK 206
Cdd:cd05928 81 WLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 207 TAPSDHRCVTTKSQHPVAIYFTSGTTGAPKMTEHSHCSYGIGLTVS---------------------------------- 252
Cdd:cd05928 161 EASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNgrywldltasdimwntsdtgwiksawsslfepwi 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 253 -GSCTF--------------------------------------------NSLRHCVSAGEPINPEVMAKWKAWTGLDIH 287
Cdd:cd05928 241 qGACVFvhhlprfdplvilktlssypittfcgaptvyrmlvqqdlssykfPSLQHCVTGGEPLNPEVLEKWKAQTGLDIY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 288 ECYGQTETVLVCGNFKGMEIKPGSMGKPSPGYDVKIIDENGNILPPGKEGEIAIKVKPTRPLFLFTCYTDDPEKTKATVR 367
Cdd:cd05928 321 EGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYVDNPEKTAATIR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 368 GDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYVSH 447
Cdd:cd05928 401 GDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSH 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2024458455 448 DPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELRQKEW 497
Cdd:cd05928 481 DPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDKEW 530
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
47-499 |
9.86e-180 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 515.82 E-value: 9.86e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 47 VPEYFNFASDVLDRWAkvekEGKKTKnPALWWVDGDGEEVKWSFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEW 126
Cdd:COG0365 4 VGGRLNIAYNCLDRHA----EGRGDK-VALIWEGEDGEERTLTYAELRREVNRFANALR-ALGVKKGDRVAIYLPNIPEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 127 WLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVITNDSVA---------STVESVEADCQSLKFKLLV----SEG 193
Cdd:COG0365 78 VIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLrggkvidlkEKVDEALEELPSLEHVIVVgrtgADV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 194 HREGWLSFKDLLKTAPSDHRCVTTKSQHPVAIYFTSGTTGAPKMTEHSH------------------------C------ 243
Cdd:COG0365 158 PMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHggylvhaattakyvldlkpgdvfwCtadigw 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 244 ----SYGI------GLTV---SGSCTFN-----------------------------------------SLRHCVSAGEP 269
Cdd:COG0365 238 atghSYIVygpllnGATVvlyEGRPDFPdpgrlweliekygvtvfftaptairalmkagdeplkkydlsSLRLLGSAGEP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 270 INPEVMAKWKAWTGLDIHECYGQTETV-LVCGNFKGMEIKPGSMGKPSPGYDVKIIDENGNILPPGKEGEIAIKvkptRP 348
Cdd:COG0365 318 LNPEVWEWWYEAVGVPIVDGWGQTETGgIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIK----GP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 349 L-FLFTCYTDDPEKTKATVRGDF---YVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVS 424
Cdd:COG0365 394 WpGMFRGYWNDPERYRETYFGRFpgwYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVG 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024458455 425 SPDPIRGEVVKAFVVLTPNYVshDPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELRQKEWRR 499
Cdd:COG0365 474 VPDEIRGQVVKAFVVLKPGVE--PSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGR 546
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
88-493 |
2.98e-171 |
|
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: 489.16 E-value: 2.98e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 88 WSFEELGVLSRKAANVLSGACsLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVITN 167
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLG-LRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 168 dsvastvesveadcqslkfkllvseghregwlsfkdllktapsdhrcvttkSQHPVAIYFTSGTTGAPKMTEHSHcSYGI 247
Cdd:cd05972 80 ---------------------------------------------------AEDPALIYFTSGTTGLPKGVLHTH-SYPL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 248 G-----------------LTVS------------------GSCTF----------------------------------- 257
Cdd:cd05972 108 GhiptaaywlglrpddihWNIAdpgwakgawssffgpwllGATVFvyegprfdaerilellerygvtsfcgpptayrmli 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 258 ---------NSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTETVLVCGNFKGMEIKPGSMGKPSPGYDVKIIDENG 328
Cdd:cd05972 188 kqdlssykfSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 329 NILPPGKEGEIAIKVKPtrpLFLFTCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVE 408
Cdd:cd05972 268 RELPPGEEGDIAIKLPP---PGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 409 SALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYvsHDPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIR 488
Cdd:cd05972 345 SALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGY--EPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIR 422
|
....*
gi 2024458455 489 RNELR 493
Cdd:cd05972 423 RVELR 427
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
36-496 |
7.16e-167 |
|
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: 482.38 E-value: 7.16e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 36 YELIKQQYRPEVPEYFNFASDVLDRWAKVEKEgkktKNpALWWVDGDGEEVKWSFEELGVLSRKAANVLSgACSLQCGDR 115
Cdd:cd05970 1 YEDFHNNFSINVPENFNFAYDVVDAMAKEYPD----KL-ALVWCDDAGEERIFTFAELADYSDKTANFFK-AMGIGKGDT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 116 VLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVIT--NDSVASTVESVEADCQSLKFKLLVSEG 193
Cdd:cd05970 75 VMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAiaEDNIPEEIEKAAPECPSKPKLVWVGDP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 194 HREGWLSFKDLLKTAPSD----HRCVTTKSQHPVAIYFTSGTTGAPKMTEHSHcSYGIG-----------------LTVS 252
Cdd:cd05970 155 VPEGWIDFRKLIKNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDF-TYPLGhivtakywqnvregglhLTVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 253 ------------------GSCTF--------------------------------------------NSLRHCVSAGEPI 270
Cdd:cd05970 234 dtgwgkavwgkiygqwiaGAAVFvydydkfdpkalleklskygvttfcapptiyrfliredlsrydlSSLRYCTTAGEAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 271 NPEVMAKWKAWTGLDIHECYGQTETVLVCGNFKGMEIKPGSMGKPSPGYDVKIIDENGNILPPGKEGEIAIKVKPTRPLF 350
Cdd:cd05970 314 NPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGKPVG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 351 LFTCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIR 430
Cdd:cd05970 394 LFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIR 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024458455 431 GEVVKAFVVLTPNYVShdPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELRQKE 496
Cdd:cd05970 474 GQVVKATIVLAKGYEP--SEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRERD 537
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
30-496 |
3.25e-121 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 366.53 E-value: 3.25e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 30 AQTSFSYELIKQQYRPEVPEYFNFASDVLDRWAKVEKEGKktknPALWWVDGDGEEvKWSFEELGVLSRKAANVLSGAcS 109
Cdd:PRK04319 21 TYATFSWEEVEKEFSWLETGKVNIAYEAIDRHADGGRKDK----VALRYLDASRKE-KYTYKELKELSNKFANVLKEL-G 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 110 LQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVITNDSVASTVesVEADCQSLKFKLL 189
Cdd:PRK04319 95 VEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERK--PADDLPSLKHVLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 190 VSE--GHREGWLSFKDLLKTAPSDHRCVTTKSQHPVAIYFTSGTTGAPKMTEHSH-----------------------C- 243
Cdd:PRK04319 173 VGEdvEEGPGTLDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHnamlqhyqtgkyvldlheddvywCt 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 244 ---------SYGI------GLT-----------------------------------------VSGSCTFNSLRHCVSAG 267
Cdd:PRK04319 253 adpgwvtgtSYGIfapwlnGATnvidggrfsperwyriledykvtvwytaptairmlmgagddLVKKYDLSSLRHILSVG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 268 EPINPEVMaKW--KAWtGLDIHECYGQTET--VLVCgNFKGMEIKPGSMGKPSPGYDVKIIDENGNILPPGKEGEIAIKv 343
Cdd:PRK04319 333 EPLNPEVV-RWgmKVF-GLPIHDNWWMTETggIMIA-NYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIK- 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 344 kPTRPLfLFTCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVV 423
Cdd:PRK04319 409 -KGWPS-MMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVI 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024458455 424 SSPDPIRGEVVKAFVVLTPNYvshDP-EKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELRQKE 496
Cdd:PRK04319 487 GKPDPVRGEIIKAFVALRPGY---EPsEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAWE 557
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
88-496 |
3.82e-104 |
|
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: 318.68 E-value: 3.82e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 88 WSFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVITN 167
Cdd:cd05969 1 YTFAQLKVLSARFANVLK-SLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 168 DSVAStvesveadcqslkfkllvseghregwlsfkdllKTAPSDhrcvttksqhPVAIYFTSGTTGAPKMTEHSH----- 242
Cdd:cd05969 80 EELYE---------------------------------RTDPED----------PTLLHYTSGTTGTPKGVLHVHdamif 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 243 ------------------C----------SYGI----------------------------------------------- 247
Cdd:cd05969 117 yyftgkyvldlhpddiywCtadpgwvtgtVYGIwapwlngvtnvvyegrfdaeswygiiervkvtvwytaptairmlmke 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 248 GLTVSGSCTFNSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTET-VLVCGNFKGMEIKPGSMGKPSPGYDVKIIDE 326
Cdd:cd05969 197 GDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETgSIMIANYPCMPIKPGSMGKPLPGVKAAVVDE 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 327 NGNILPPGKEGEIAIKvkPTRPLfLFTCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFE 406
Cdd:cd05969 277 NGNELPPGTKGILALK--PGWPS-MFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 407 VESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYvshDP-EKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISG 485
Cdd:cd05969 354 VESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGF---EPsDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSG 430
|
490
....*....|.
gi 2024458455 486 KIRRNELRQKE 496
Cdd:cd05969 431 KIMRRVLKAKE 441
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
56-499 |
3.48e-102 |
|
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: 313.67 E-value: 3.48e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 56 DVLDRWAKVEKEgkktkNPALwwVDGDGEevkWSFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLNVACMR 135
Cdd:COG0318 3 DLLRRAAARHPD-----RPAL--VFGGRR---LTYAELDARARRLAAALR-ALGVGPGDRVALLLPNSPEFVVAFLAALR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 136 TGTVPIPGTQQLTAKDILYRLQKSKAKGVITndsvastvesveadcqslkfkllvseghregwlsfkdllktapsdhrcv 215
Cdd:COG0318 72 AGAVVVPLNPRLTAEELAYILEDSGARALVT------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 216 ttksqhpVAIYFTSGTTGAPKMTEHSH---------CSYGIGLT-------------------------VSGSCT----- 256
Cdd:COG0318 103 -------ALILYTSGTTGRPKGVMLTHrnllanaaaIAAALGLTpgdvvlvalplfhvfgltvgllaplLAGATLvllpr 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 257 --------------------------------------FNSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTET-VL 297
Cdd:COG0318 176 fdpervlelierervtvlfgvptmlarllrhpefarydLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETsPV 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 298 VCGNFKGM-EIKPGSMGKPSPGYDVKIIDENGNILPPGKEGEIAIkvkptRPLFLFTCYTDDPEKTKATVRGDFYVTGDR 376
Cdd:COG0318 256 VTVNPEDPgERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVV-----RGPNVMKGYWNDPEATAEAFRDGWLRTGDL 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 377 GLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNyVSHDPEkmmkDL 456
Cdd:COG0318 331 GRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPG-AELDAE----EL 405
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2024458455 457 QDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELRQKEWRR 499
Cdd:COG0318 406 RAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAG 448
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
89-496 |
9.55e-102 |
|
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: 312.19 E-value: 9.55e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 89 SFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAkgvitnd 168
Cdd:cd05974 2 SFAEMSARSSRVANFLR-SIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 169 SVASTVESVEADcqslkfkllvseghregwlsfkdllktapsdhrcvttksqHPVAIYFTSGTTGAPKMTEHSHCSYGIG 248
Cdd:cd05974 74 VYAAVDENTHAD----------------------------------------DPMLLYFTSGTTSKPKLVEHTHRSYPVG 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 249 ----------------LTVSG--------SCTFN---------------------------------------------- 258
Cdd:cd05974 114 hlstmywiglkpgdvhWNISSpgwakhawSCFFApwnagatvflfnyarfdakrvlaalvrygvttlcapptvwrmliqq 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 259 -------SLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTETVLVCGNFKGMEIKPGSMGKPSPGYDVKIIDENGNil 331
Cdd:cd05974 194 dlasfdvKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGA-- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 332 pPGKEGEIAIKVKPTRPLFLFTCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESAL 411
Cdd:cd05974 272 -PATEGEVALDLGDTRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVL 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 412 IEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYvSHDPEkMMKDLQDHVKKATAPYKYPRKMEFvRELPKTISGKIRRNE 491
Cdd:cd05974 351 IEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGY-EPSPE-TALEIFRFSRERLAPYKRIRRLEF-AELPKTISGKIRRVE 427
|
....*
gi 2024458455 492 LRQKE 496
Cdd:cd05974 428 LRRRE 432
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
82-494 |
4.65e-99 |
|
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: 305.51 E-value: 4.65e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 82 DGEEVKWSFEELGVLSRKAANVLSGAcSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKA 161
Cdd:cd05971 1 KGTPEKVTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 162 KGVITNdsvastvesveadcqslkfkllvseghregwlsfkdllktAPSDhrcvttksqhPVAIYFTSGTTGAPKMTEHS 241
Cdd:cd05971 80 SALVTD----------------------------------------GSDD----------PALIIYTSGTTGPPKGALHA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 242 H----------------------CSYG-------------------IGLTV--------SGSCTF--------------- 257
Cdd:cd05971 110 HrvllghlpgvqfpfnlfprdgdLYWTpadwawigglldvllpslyFGVPVlahrmtkfDPKAALdlmsrygvttaflpp 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 258 -----------------NSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTETVLVCGNFKG-MEIKPGSMGKPSPGY 319
Cdd:cd05971 190 talkmmrqqgeqlkhaqVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNCSAlFPIKPGSMGKPIPGH 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 320 DVKIIDENGNILPPGKEGEIAIKvKPTRPLFLftCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAG 399
Cdd:cd05971 270 RVAIVDDNGTPLPPGEVGEIAVE-LPDPVAFL--GYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 400 YRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYVshDPEKMMKDLQDHVKKATAPYKYPRKMEFVREL 479
Cdd:cd05971 347 YRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGET--PSDALAREIQELVKTRLAAHEYPREIEFVNEL 424
|
490
....*....|....*
gi 2024458455 480 PKTISGKIRRNELRQ 494
Cdd:cd05971 425 PRTATGKIRRRELRA 439
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
49-493 |
2.69e-92 |
|
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: 290.04 E-value: 2.69e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 49 EYFNFASDVLDRWAKVEkeGKKTknpALwwVDGDGEevkWSFEELGVLSRKAANVLSGAcSLQCGDRVLLLLPRIPEWWL 128
Cdd:cd05959 1 EKYNAATLVDLNLNEGR--GDKT---AF--IDDAGS---LTYAELEAEARRVAGALRAL-GVKREERVLLIMLDTVDFPT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 129 LNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVITNDSVASTVESVEADCQSLKFKLLVSEGHRE--GWLSFKDLLK 206
Cdd:cd05959 70 AFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPeaGALLLAELVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 207 TAPSDHRCVTTKSQHPVAIYFTSGTTGAPKMTEHSHCS------------------------------YGIG------LT 250
Cdd:cd05959 150 AEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADiywtaelyarnvlgireddvcfsaaklffaYGLGnsltfpLS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 251 VSGSCT-------------------------------------------FNSLRHCVSAGEPINPEVMAKWKAWTGLDIH 287
Cdd:cd05959 230 VGATTVlmperptpaavfkrirryrptvffgvptlyaamlaapnlpsrdLSSLRLCVSAGEALPAEVGERWKARFGLDIL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 288 ECYGQTETV-LVCGNFKGmEIKPGSMGKPSPGYDVKIIDENGNILPPGKEGEIAIKVKPTRPLflftcYTDDPEKTKATV 366
Cdd:cd05959 310 DGIGSTEMLhIFLSNRPG-RVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATM-----YWNNRDKTRDTF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 367 RGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYvs 446
Cdd:cd05959 384 QGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGY-- 461
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2024458455 447 HDPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELR 493
Cdd:cd05959 462 EDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
55-493 |
5.85e-91 |
|
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: 285.23 E-value: 5.85e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 55 SDVLDRWAKvekegKKTKNPALWWVDgdgeeVKWSFEELGVLSRKAANVLSGAcSLQCGDRVLLLLPRIPEWWLLNVACM 134
Cdd:cd05936 2 ADLLEEAAR-----RFPDKTALIFMG-----RKLTYRELDALAEAFAAGLQNL-GVQPGDRVALMLPNCPQFPIAYFGAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 135 RTGTVPIPGTQQLTAKDILYRLQKSKAKGVITNdsvastvesveadcqslkfkllvseghregwLSFKDLLKTAPSDHRC 214
Cdd:cd05936 71 KAGAVVVPLNPLYTPRELEHILNDSGAKALIVA-------------------------------VSFTDLLAAGAPLGER 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 215 VTTKSQHPVAIYFTSGTTGAPKMTEHSH-------------------------C------SYGigLTVSGSCT------- 256
Cdd:cd05936 120 VALTPEDVAVLQYTSGTTGVPKGAMLTHrnlvanalqikawledllegddvvlAalplfhVFG--LTVALLLPlalgati 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 257 -------------------------------------------FNSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQT 293
Cdd:cd05936 198 vliprfrpigvlkeirkhrvtifpgvptmyiallnapefkkrdFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLT 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 294 ETV-LVCGNFKGMEIKPGSMGKPSPGYDVKIIDENGNILPPGKEGEIAIK---VkptrplflFTCYTDDPEKTKATVRGD 369
Cdd:cd05936 278 ETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRgpqV--------MKGYWNRPEETAEAFVDG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 370 FYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNyvsHDP 449
Cdd:cd05936 350 WLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEG---ASL 426
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2024458455 450 EKmmKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELR 493
Cdd:cd05936 427 TE--EEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
89-494 |
7.89e-89 |
|
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: 279.02 E-value: 7.89e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 89 SFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVITNd 168
Cdd:cd05973 2 TFGELRALSARFANALQ-ELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 169 svASTVESVEADcqslkfkllvseghregwlsfkdllktapsdhrcvttksqhPVAIYFTSGTTGAPK---------MTE 239
Cdd:cd05973 80 --AANRHKLDSD-----------------------------------------PFVMMFTSGTTGLPKgvpvplralAAF 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 240 HSHCSYGIGLT------------------------------------------------------VSGSCTF-------- 257
Cdd:cd05973 117 GAYLRDAVDLRpedsfwnaadpgwayglyyaitgplalghptilleggfsvestwrvierlgvtnLAGSPTAyrllmaag 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 258 --------NSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTETVLVCGNFKGME--IKPGSMGKPSPGYDVKIIDEN 327
Cdd:cd05973 197 aevparpkGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEhpVHAGSAGRAMPGWRVAVLDDD 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 328 GNILPPGKEGEIAIKVKPTrPLFLFTCYTDDPEKTKAtvrGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEV 407
Cdd:cd05973 277 GDELGPGEPGRLAIDIANS-PLMWFRGYQLPDTPAID---GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 408 ESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNyvsHDP-EKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGK 486
Cdd:cd05973 353 ESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGG---HEGtPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGK 429
|
....*...
gi 2024458455 487 IRRNELRQ 494
Cdd:cd05973 430 IQRFLLRR 437
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
221-488 |
2.91e-84 |
|
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: 263.76 E-value: 2.91e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 221 HPVAIYFTSGTTGAPKMTEHSHCSY---------------------------------GIGLTVSGS------------- 254
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLlaaaaalaasggltegdvflstlplfhigglfgLLGALLAGGtvvllpkfdpeaa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 255 --------CTFN----------------------SLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTET-VLVCGNFK 303
Cdd:cd04433 81 lelierekVTILlgvptllarllkapesagydlsSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETgGTVATGPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 304 GMEI-KPGSMGKPSPGYDVKIIDENGNILPPGKEGEIAIKVkPTRPLFlftcYTDDPEKTKATVRGDFYVTGDRGLMDED 382
Cdd:cd04433 161 DDDArKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRG-PSVMKG----YWNNPEATAAVDEDGWYRTGDLGRLDED 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 383 GYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPnyvSHDPEKmmKDLQDHVKK 462
Cdd:cd04433 236 GYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRP---GADLDA--EELRAHVRE 310
|
330 340
....*....|....*....|....*.
gi 2024458455 463 ATAPYKYPRKMEFVRELPKTISGKIR 488
Cdd:cd04433 311 RLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
85-493 |
1.55e-82 |
|
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: 262.80 E-value: 1.55e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 85 EVKWSFEELGVLSRKAANVLSGACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGV 164
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 165 ITNDSVaSTVEsveaDCQSLKFKLLVSEG-------HREGWLSFK----DLLKTAPSDHRCVTTKsqhpvaIYFTSGTTG 233
Cdd:cd05958 88 LCAHAL-TASD----DICILAFTSGTTGApkatmhfHRDPLASADryavNVLRLREDDRFVGSPP------LAFTFGLGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 234 -------------------APKM-------------TEHSHCSYGIGLTVSGSCTFNSLRHCVSAGEPINPEVMAKWKAW 281
Cdd:cd05958 157 vllfpfgvgasgvlleeatPDLLlsaiarykptvlfTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 282 TGLDIHECYGQTETVLVCGNFKGMEIKPGSMGKPSPGYDVKIIDENGNILPPGKEGEIAIKvKPTrplflfTCYTDDPEK 361
Cdd:cd05958 237 TGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVR-GPT------GCRYLADKR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 362 TKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLT 441
Cdd:cd05958 310 QRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLR 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2024458455 442 PnyvSHDP-EKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELR 493
Cdd:cd05958 390 P---GVIPgPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
84-497 |
5.86e-77 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 250.49 E-value: 5.86e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 84 EEVKWSFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKG 163
Cdd:PRK06187 28 DGRRTTYAELDERVNRLANALR-ALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 164 VITNDSVASTVESVEADCQSLKFKLLVSEGHREG----WLSFKDLLKTAPSDHRCVTTKSQHPVAIYFTSGTTGAPK--- 236
Cdd:PRK06187 107 VLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAAPlapeVGEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKgvv 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 237 -----MTEHS----------------------HCsYGIGL-------------------------------TVSGsCT-- 256
Cdd:PRK06187 187 lshrnLFLHSlavcawlklsrddvylvivpmfHV-HAWGLpylalmagakqviprrfdpenlldlietervTFFF-AVpt 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 257 ---------------FNSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTET--VLVCG----NFKGMEIKPGSMGKP 315
Cdd:PRK06187 265 iwqmllkaprayfvdFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETspVVSVLppedQLPGQWTKRRSAGRP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 316 SPGYDVKIIDENGNILPP-GKE-GEIAIKvKPTrplfLFTCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADD 393
Cdd:PRK06187 345 LPGVEARIVDDDGDELPPdGGEvGEIIVR-GPW----LMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKD 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 394 VINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNyVSHDPekmmKDLQDHVKKATAPYKYPRKM 473
Cdd:PRK06187 420 VIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPG-ATLDA----KELRAFLRGRLAKFKLPKRI 494
|
490 500
....*....|....*....|....
gi 2024458455 474 EFVRELPKTISGKIRRNELRQKEW 497
Cdd:PRK06187 495 AFVDELPRTSVGKILKRVLREQYA 518
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
49-494 |
1.74e-72 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 238.58 E-value: 1.74e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 49 EYFNFASDVLDRwAKVEKEGKKTKnpalwWVDGDGeevKWSFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWL 128
Cdd:TIGR02262 1 EKYNAAEDLLDR-NVVEGRGGKTA-----FIDDIS---SLSYGELEAQVRRLAAALR-RLGVKREERVLLLMLDGVDFPI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 129 LNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVITNDSVASTVESVEADCQSLKfKLLVSEGHREGWLSFKDLLKTA 208
Cdd:TIGR02262 71 AFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALGKSPHLE-HRVVVGRPEAGEVQLAELLATE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 209 PSDHRCVTTKSQHPVAIYFTSGTTGAPKMTEHSHCS------------------------------YGIG------LTVS 252
Cdd:TIGR02262 150 SEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNpywtaelyarntlgireddvcfsaaklffaYGLGnaltfpMSVG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 253 GSCTFNS-------------------------------------------LRHCVSAGEPINPEVMAKWKAWTGLDIHEC 289
Cdd:TIGR02262 230 ATTVLMGerptpdavfdrlrrhqptifygvptlyaamladpnlpsedqvrLRLCTSAGEALPAEVGQRWQARFGVDIVDG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 290 YGQTETV-LVCGNFKGmEIKPGSMGKPSPGYDVKIIDENGNILPPGKEGEIAIKvKPTRPlflfTCYTDDPEKTKATVRG 368
Cdd:TIGR02262 310 IGSTEMLhIFLSNLPG-DVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLIS-GPSSA----TMYWNNRAKSRDTFQG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 369 DFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYvshd 448
Cdd:TIGR02262 384 EWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQ---- 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2024458455 449 pEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELRQ 494
Cdd:TIGR02262 460 -TALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
89-493 |
8.38e-70 |
|
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: 229.27 E-value: 8.38e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 89 SFEELGVLSRKAANVLSGAcSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVITND 168
Cdd:cd05919 12 TYGQLHDGANRLGSALRNL-GVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 169 --------SVAST-----VESVEAD----CQSLKFKLL-VSEGHRE--------GW-----LSFK-------DLLKTAPS 210
Cdd:cd05919 91 ddiayllySSGTTgppkgVMHAHRDpllfADAMAREALgLTPGDRVfssakmffGYglgnsLWFPlavgasaVLNPGWPT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 211 DHRCVTTKSQHPVAIYFtsgttGAPKMTEHShcsygIGLTVSGSCTFNSLRHCVSAGEPINPEVMAKWKAWTGLDIHECY 290
Cdd:cd05919 171 AERVLATLARFRPTVLY-----GVPTFYANL-----LDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 291 GQTETVLVCGNFKGMEIKPGSMGKPSPGYDVKIIDENGNILPPGKEGEIAIKvKPTrplfLFTCYTDDPEKTKATVRGDF 370
Cdd:cd05919 241 GATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVR-GPS----AAVGYWNNPEKSRATFNGGW 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 371 YVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYVSHdpE 450
Cdd:cd05919 316 YRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQ--E 393
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2024458455 451 KMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELR 493
Cdd:cd05919 394 SLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
52-493 |
4.55e-69 |
|
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: 232.52 E-value: 4.55e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 52 NFASDVLDRWakVEKEGKKTknpALWW-VDGDGEEVKWSFEELGVLSRKAANVLSGAcSLQCGDRVLLLLPRIPEWWLLN 130
Cdd:TIGR02188 57 NVSYNCVDRH--LEARPDKV---AIIWeGDEPGEVRKITYRELHREVCRFANVLKSL-GVKKGDRVAIYMPMIPEAAIAM 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 131 VACMRTG---TVPIPGtqqLTAKDILYRLQKSKAKGVITNDSV----------ASTVESVEADCQSLKfKLLV------- 190
Cdd:TIGR02188 131 LACARIGaihSVVFGG---FSAEALADRINDAGAKLVITADEGlrggkviplkAIVDEALEKCPVSVE-HVLVvrrtgnp 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 191 ----SEGhREGWlsFKDLLKTAPSDHRCVTTKSQHPVAIYFTSGTTGAPK------------------------------ 236
Cdd:TIGR02188 207 vvpwVEG-RDVW--WHDLMAKASAYCEPEPMDSEDPLFILYTSGSTGKPKgvlhttggyllyaamtmkyvfdikdgdifw 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 237 -------MTEHSHCSYG---IGLTV---SGSCTF-----------------------------------------NSLRH 262
Cdd:TIGR02188 284 ctadvgwITGHSYIVYGplaNGATTvmfEGVPTYpdpgrfweiiekhkvtifytaptairalmrlgdewvkkhdlSSLRL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 263 CVSAGEPINPEVmakWK-AWTGLDIHEC-----YGQTET--VLVCGNFKGMEIKPGSMGKPSPGYDVKIIDENGNILP-P 333
Cdd:TIGR02188 364 LGSVGEPINPEA---WMwYYKVVGKERCpivdtWWQTETggIMITPLPGATPTKPGSATLPFFGIEPAVVDEEGNPVEgP 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 334 GKEGEIAIKvKPtRPLFLFTCYtDDPEKTKATVRGDF---YVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESA 410
Cdd:TIGR02188 441 GEGGYLVIK-QP-WPGMLRTIY-GDHERFVDTYFSPFpgyYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESA 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 411 LIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYvSHDPEkMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRN 490
Cdd:TIGR02188 518 LVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGY-EPDDE-LRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRR 595
|
...
gi 2024458455 491 ELR 493
Cdd:TIGR02188 596 LLR 598
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
84-489 |
6.39e-69 |
|
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: 227.11 E-value: 6.39e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 84 EEVKWSFEELGVLSRKAANVLSGAcSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYrlqkskakg 163
Cdd:cd17631 17 GGRSLTYAELDERVNRLAHALRAL-GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAY--------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 164 vITNDSVASTVesveadcqslkfkllvseghregwlsFKDllktapsdhrcvttksqhPVAIYFTSGTTGAPKMTEHSH- 242
Cdd:cd17631 87 -ILADSGAKVL--------------------------FDD------------------LALLMYTSGTTGRPKGAMLTHr 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 243 --------CSYGIGLTVSGSC----------------------------------------------------------- 255
Cdd:cd17631 122 nllwnavnALAALDLGPDDVLlvvaplfhigglgvftlptllrggtvvilrkfdpetvldlierhrvtsfflvptmiqal 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 256 ---------TFNSLRHCVSAGEPINPEVMAKWKAwTGLDIHECYGQTETV-LVCGNFKGMEI-KPGSMGKPSPGYDVKII 324
Cdd:cd17631 202 lqhprfattDLSSLRAVIYGGAPMPERLLRALQA-RGVKFVQGYGMTETSpGVTFLSPEDHRrKLGSAGRPVFFVEVRIV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 325 DENGNILPPGKEGEIAIKvKPTrplfLFTCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGP 404
Cdd:cd17631 281 DPDGREVPPGEVGEIVVR-GPH----VMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYP 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 405 FEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNyVSHDPEkmmkDLQDHVKKATAPYKYPRKMEFVRELPKTIS 484
Cdd:cd17631 356 AEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPG-AELDED----ELIAHCRERLARYKIPKSVEFVDALPRNAT 430
|
....*
gi 2024458455 485 GKIRR 489
Cdd:cd17631 431 GKILK 435
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
52-494 |
1.18e-68 |
|
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: 230.91 E-value: 1.18e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 52 NFASDVLDRWakVEKEGKKTknpALWWvDGD--GEEVKWSFEELGVLSRKAANVLSGAcSLQCGDRVLLLLPRIPEWWLL 129
Cdd:cd05966 53 NISYNCLDRH--LKERGDKV---AIIW-EGDepDQSRTITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPELVIA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 130 NVACMRTG---TVPIPGtqqLTAKDILYRLQKSKAKGVITNDSV---------ASTVESVEADCQSLKfKLLV------- 190
Cdd:cd05966 126 MLACARIGavhSVVFAG---FSAESLADRINDAQCKLVITADGGyrggkviplKEIVDEALEKCPSVE-KVLVvkrtgge 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 191 ---SEGhREGWLSfkDLLKTAPSDHRCVTTKSQHPVAIYFTSGTTGAPKMTEHSHCSYGIGLTVSGSCTFN--------- 258
Cdd:cd05966 202 vpmTEG-RDLWWH--DLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDyhpddiywc 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 259 ---------------------------------------------------------------------------SLRHC 263
Cdd:cd05966 279 tadigwitghsyivygplangattvmfegtptypdpgrywdivekhkvtifytaptairalmkfgdewvkkhdlsSLRVL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 264 VSAGEPINPEvmakwkAWTGLDIH----EC-----YGQTETvlvcGNF------KGMEIKPGSMGKPSPGYDVKIIDENG 328
Cdd:cd05966 359 GSVGEPINPE------AWMWYYEVigkeRCpivdtWWQTET----GGImitplpGATPLKPGSATRPFFGIEPAILDEEG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 329 NILPPGKEGEIAIKvKPTrPLFLFTCYTDDP--EKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFE 406
Cdd:cd05966 429 NEVEGEVEGYLVIK-RPW-PGMARTIYGDHEryEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAE 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 407 VESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYvsHDPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGK 486
Cdd:cd05966 507 VESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGE--EPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGK 584
|
....*...
gi 2024458455 487 IRRNELRQ 494
Cdd:cd05966 585 IMRRILRK 592
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
50-494 |
3.65e-66 |
|
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: 224.50 E-value: 3.65e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 50 YFNFASDVLDRWAkvekEGKKTKNPALWWVDG-DGEEVKWSFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWL 128
Cdd:cd05967 48 RLNTCYNALDRHV----EAGRGDQIALIYDSPvTGTERTYTYAELLDEVSRLAGVLR-KLGVVKGDRVIIYMPMIPEAAI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 129 LNVACMRTG---TVPIPGtqqLTAKDILYRLQKSKAKGVITndsvastvesveADC-----QSLKFKLLVSE-----GHR 195
Cdd:cd05967 123 AMLACARIGaihSVVFGG---FAAKELASRIDDAKPKLIVT------------ASCgiepgKVVPYKPLLDKalelsGHK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 196 -------------------EGWLSFKDLLKTAPSdHRCVTTKSQHPVAIYFTSGTTGAPK-------------------- 236
Cdd:cd05967 188 phhvlvlnrpqvpadltkpGRDLDWSELLAKAEP-VDCVPVAATDPLYILYTSGTTGKPKgvvrdngghavalnwsmrni 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 237 -----------------MTEHSHCSYG---IGLT-------------------------VSG------------------ 253
Cdd:cd05967 267 ygikpgdvwwaasdvgwVVGHSYIVYGpllHGATtvlyegkpvgtpdpgafwrviekyqVNAlftaptairairkedpdg 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 254 ----SCTFNSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTET-VLVCGNFKGME---IKPGSMGKPSPGYDVKIID 325
Cdd:cd05967 347 kyikKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETgWPITANPVGLEplpIKAGSPGKPVPGYQVQVLD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 326 ENGNILPPGKEGEIAIKVkPTRPLFLFTCYTDDpEKTKATVRGDF---YVTGDRGLMDEDGYFWFVGRADDVINSAGYRI 402
Cdd:cd05967 427 EDGEPVGPNELGNIVIKL-PLPPGCLLTLWKND-ERFKKLYLSKFpgyYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRL 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 403 GPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNyVSHDPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKT 482
Cdd:cd05967 505 STGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEG-VKITAEELEKELVALVREQIGPVAAFRLVIFVKRLPKT 583
|
570
....*....|..
gi 2024458455 483 ISGKIRRNELRQ 494
Cdd:cd05967 584 RSGKILRRTLRK 595
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
84-494 |
3.87e-65 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 219.42 E-value: 3.87e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 84 EEVKWSFEELGVLSRKAANVLSGAcSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKG 163
Cdd:PRK08316 33 GDRSWTYAELDAAVNRVAAALLDL-GLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 164 VITNDSVASTVESVEADCQSLKFKLLVSEG---HREGWLSFKDLLKTAPSDHRCVTTKSQHPVAIYFTSGTTGAPKMTEH 240
Cdd:PRK08316 112 FLVDPALAPTAEAALALLPVDTLILSLVLGgreAPGGWLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAML 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 241 SH---------CSYGIGLTvSGSCTFNS--LRHC-----------------VSAGEPINPEVMAK--------------- 277
Cdd:PRK08316 192 THraliaeyvsCIVAGDMS-ADDIPLHAlpLYHCaqldvflgpylyvgatnVILDAPDPELILRTieaeritsffapptv 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 278 W------------------KAWTG------------------LDIHECYGQTE-----TVLvcgNFKGMEIKPGSMGKPS 316
Cdd:PRK08316 271 WisllrhpdfdtrdlsslrKGYYGasimpvevlkelrerlpgLRFYNCYGQTEiaplaTVL---GPEEHLRRPGSAGRPV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 317 PGYDVKIIDENGNILPPGKEGEIAikvkpTRPLFLFTCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVIN 396
Cdd:PRK08316 348 LNVETRVVDDDGNDVAPGEVGEIV-----HRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIK 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 397 SAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNyVSHDPEkmmkDLQDHVKKATAPYKYPRKMEFV 476
Cdd:PRK08316 423 TGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAG-ATVTED----ELIAHCRARLAGFKVPKRVIFV 497
|
490
....*....|....*...
gi 2024458455 477 RELPKTISGKIRRNELRQ 494
Cdd:PRK08316 498 DELPRNPSGKILKRELRE 515
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
52-494 |
4.88e-65 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 221.94 E-value: 4.88e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 52 NFASDVLDRwaKVEKEGKKTknpALWWVDGDGEEV-KWSFEELGVLSRKAANVLSGAcSLQCGDRVLLLLPRIPEWWLLN 130
Cdd:PRK00174 67 NVSYNCLDR--HLKTRGDKV---AIIWEGDDPGDSrKITYRELHREVCRFANALKSL-GVKKGDRVAIYMPMIPEAAVAM 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 131 VACMRTG---TVPIPGtqqLTAKDILYRLQKSKAKGVITND-------SVA--STVESVEADCQSLKfKLLV-------- 190
Cdd:PRK00174 141 LACARIGavhSVVFGG---FSAEALADRIIDAGAKLVITADegvrggkPIPlkANVDEALANCPSVE-KVIVvrrtggdv 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 191 -SEGHREGWlsFKDLLKTAPSDHRCVTTKSQHPVAIYFTSGTTGAPK--------------------------------- 236
Cdd:PRK00174 217 dWVEGRDLW--WHELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKgvlhttggylvyaamtmkyvfdykdgdvywcta 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 237 ----MTEHSHCSYG---IGLTV---SGSCTF-----------------------------------------NSLRHCVS 265
Cdd:PRK00174 295 dvgwVTGHSYIVYGplaNGATTlmfEGVPNYpdpgrfwevidkhkvtifytaptairalmkegdehpkkydlSSLRLLGS 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 266 AGEPINPEvmakwkAWT------GLD---IHECYGQTETvlvcGnfkGMEI---------KPGSMGKPSPGYDVKIIDEN 327
Cdd:PRK00174 375 VGEPINPE------AWEwyykvvGGErcpIVDTWWQTET----G---GIMItplpgatplKPGSATRPLPGIQPAVVDEE 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 328 GNILPPGKEGEIAIKvKPTrPLFLFTCYtDDPEKTKATVRGDF---YVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGP 404
Cdd:PRK00174 442 GNPLEGGEGGNLVIK-DPW-PGMMRTIY-GDHERFVKTYFSTFkgmYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGT 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 405 FEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYVSHDpeKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTIS 484
Cdd:PRK00174 519 AEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSD--ELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRS 596
|
570
....*....|
gi 2024458455 485 GKIRRNELRQ 494
Cdd:PRK00174 597 GKIMRRILRK 606
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
87-494 |
9.20e-64 |
|
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: 213.69 E-value: 9.20e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 87 KWSFEELGVLSRKAANVLSGACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKS------- 159
Cdd:cd05941 11 SITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSepslvld 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 160 ------------KAKGV-ITNDSVASTVESV-------EAD----------CQSLKFKLLVS--EGHREGWLSFKDLLKT 207
Cdd:cd05941 91 palilytsgttgRPKGVvLTHANLAANVRALvdawrwtEDDvllhvlplhhVHGLVNALLCPlfAGASVEFLPKFDPKEV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 208 APSDHrcvttksqHPVAIYFTSGTTGAPKMTEHSHCSYGIGLTVSGSCtFNSLRHCVSAGEPINPEVMAKWKAWTGLDIH 287
Cdd:cd05941 171 AISRL--------MPSITVFMGVPTIYTRLLQYYEAHFTDPQFARAAA-AERLRLMVSGSAALPVPTLEEWEAITGHTLL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 288 ECYGQTETVLVCGN-FKGmEIKPGSMGKPSPGYDVKIIDENGN-ILPPGKEGEIAIKvKPTrplfLFTCYTDDPEKTKAT 365
Cdd:cd05941 242 ERYGMTEIGMALSNpLDG-ERRPGTVGMPLPGVQARIVDEETGePLPRGEVGEIQVR-GPS----VFKEYWNKPEATKEE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 366 VRGD-FYVTGDRGLMDEDGYFWFVGR-ADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPN 443
Cdd:cd05941 316 FTDDgWFKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAG 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2024458455 444 YVSHDPEkmmkDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELRQ 494
Cdd:cd05941 396 AAALSLE----ELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
52-487 |
1.06e-62 |
|
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: 214.75 E-value: 1.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 52 NFASDVLDRwaKVEKEGKKTknpALWWVDGDGEEVK-WSFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLN 130
Cdd:cd17634 53 NLAANALDR--HLRENGDRT---AIIYEGDDTSQSRtISYRELHREVCRFAGTLL-DLGVKKGDRVAIYMPMIPEAAVAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 131 VACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVITNDS----------VASTVESVEADCQSLKFKLLVSeghREG--- 197
Cdd:cd17634 127 LACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGgvragrsvplKKNVDDALNPNVTSVEHVIVLK---RTGsdi 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 198 ------WLSFKDLLKTAPSDHRCVTTKSQHPVAIYFTSGTTGAPK----------------------------------- 236
Cdd:cd17634 204 dwqegrDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKgvlhttggylvyaattmkyvfdygpgdiywctadv 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 237 --MTEHSHCSYGiGLtVSGSCTF-------------------------------------------------NSLRHCVS 265
Cdd:cd17634 284 gwVTGHSYLLYG-PL-ACGATTLlyegvpnwptparmwqvvdkhgvnilytaptairalmaagddaiegtdrSSLRILGS 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 266 AGEPINPEVMAkWkAWTGLDIHEC-----YGQTETV-LVCGNFKGME-IKPGSMGKPSPGYDVKIIDENGNILPPGKEGE 338
Cdd:cd17634 362 VGEPINPEAYE-W-YWKKIGKEKCpvvdtWWQTETGgFMITPLPGAIeLKAGSATRPVFGVQPAVVDNEGHPQPGGTEGN 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 339 IAIKVkPTRPLFLfTCYTDDPEKTK---ATVRGdFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHP 415
Cdd:cd17634 440 LVITD-PWPGQTR-TLFGDHERFEQtyfSTFKG-MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHP 516
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024458455 416 AVLESAVVSSPDPIRGEVVKAFVVLTPNYVshDPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKI 487
Cdd:cd17634 517 KVAEAAVVGIPHAIKGQAPYAYVVLNHGVE--PSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
87-493 |
4.06e-60 |
|
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: 203.29 E-value: 4.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 87 KWSFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVIT 166
Cdd:cd05934 3 RWTYAELLRESARIAAALA-ALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 167 NdsvastvesveadcqslkfkllvseghregwlsfkdllktapsdhrcvttksqhPVAIYFTSGTTGAPK---------- 236
Cdd:cd05934 82 D------------------------------------------------------PASILYTSGTTGPPKgvvithanlt 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 237 -----------MTE-----------HSHC-SYGIGLTVSGSCT-----------------------FNSL---------- 260
Cdd:cd05934 108 fagyysarrfgLGEddvyltvlplfHINAqAVSVLAALSVGATlvllprfsasrfwsdvrrygatvTNYLgamlsyllaq 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 261 -------RHCVSA--GEPINPEVMAKWKAWTGLDIHECYGQTETVLVCGNFKGMEIKPGSMGKPSPGYDVKIIDENGNIL 331
Cdd:cd05934 188 ppspddrAHRLRAayGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQEL 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 332 PPGKEGEIAIKvkPTRPLFLFTCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESAL 411
Cdd:cd05934 268 PAGEPGELVIR--GLRGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAI 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 412 IEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNyVSHDPEKMMKDLQDHVkkatAPYKYPRKMEFVRELPKTISGKIRRNE 491
Cdd:cd05934 346 LRHPAVREAAVVAVPDEVGEDEVKAVVVLRPG-ETLDPEELFAFCEGQL----AYFKVPRYIRFVDDLPKTPTEKVAKAQ 420
|
..
gi 2024458455 492 LR 493
Cdd:cd05934 421 LR 422
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
84-495 |
1.46e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 201.67 E-value: 1.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 84 EEVKWSFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKG 163
Cdd:PRK07656 27 GDQRLTYAELNARVRRAAAALA-ALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 164 VITNDSVASTVESVEADCQSLKFKLLVSEG----HREGWLSFKDLLKTAPSDHRCVTTKSQHPVAIYFTSGTTGAPK--M 237
Cdd:PRK07656 106 LFVLGLFLGVDYSATTRLPALEHVVICETEeddpHTEKMKTFTDFLAAGDPAERAPEVDPDDVADILFTSGTTGRPKgaM 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 238 TEH--------SHCSYG-----------------IGLTV-------SGSC-----TFN---------------------- 258
Cdd:PRK07656 186 LTHrqllsnaaDWAEYLgltegdrylaanpffhvFGYKAgvnaplmRGATilplpVFDpdevfrlieteritvlpgpptm 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 259 ----------------SLRHCVSAGEPINPEVMAKWKAWTGLD-IHECYGQTE---TVLVCGNFKGMEIKPGSMGKPSPG 318
Cdd:PRK07656 266 ynsllqhpdrsaedlsSLRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEasgVTTFNRLDDDRKTVAGTIGTAIAG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 319 YDVKIIDENGNILPPGKEGEIAIKvKPTrplfLFTCYTDDPEKTKATVRGDFYV-TGDRGLMDEDGYFWFVGRADDVINS 397
Cdd:PRK07656 346 VENKIVNELGEEVPVGEVGELLVR-GPN----VMKGYYDDPEATAAAIDADGWLhTGDLGRLDEEGYLYIVDRKKDMFIV 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 398 AGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNyvshdPEKMMKDLQDHVKKATAPYKYPRKMEFVR 477
Cdd:PRK07656 421 GGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPG-----AELTEEELIAYCREHLAKYKVPRSIEFLD 495
|
490
....*....|....*...
gi 2024458455 478 ELPKTISGKIRRNELRQK 495
Cdd:PRK07656 496 ELPKNATGKVLKRALREK 513
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
81-398 |
9.65e-58 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 197.15 E-value: 9.65e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 81 GDGEEVKWSFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLNVACMRTG--TVPI-PGtqqLTAKDILYRLQ 157
Cdd:pfam00501 15 EVGEGRRLTYRELDERANRLAAGLR-ALGVGKGDRVAILLPNSPEWVVAFLACLKAGavYVPLnPR---LPAEELAYILE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 158 KSKAKGVITNDS-VASTVESVEADCQSLKFKLLVS-EGHREGWLSFKDLLKTAPSDHRCVTTKSQHPVAIYFTSGTTGAP 235
Cdd:pfam00501 91 DSGAKVLITDDAlKLEELLEALGKLEVVKLVLVLDrDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 236 KMTEHSH-------------------------------------CSYGIGLTVSGSCT---------------------- 256
Cdd:pfam00501 171 KGVMLTHrnlvanvlsikrvrprgfglgpddrvlstlplfhdfgLSLGLLGPLLAGATvvlppgfpaldpaalleliery 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 257 -------------------------FNSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTET-VLVCGNFKGME--IK 308
Cdd:pfam00501 251 kvtvlygvptllnmlleagapkralLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETtGVVTTPLPLDEdlRS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 309 PGSMGKPSPGYDVKIIDEN-GNILPPGKEGEIAIKvkptRPlFLFTCYTDDPEKTKAT-VRGDFYVTGDRGLMDEDGYFW 386
Cdd:pfam00501 331 LGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVR----GP-GVMKGYLNDPELTAEAfDEDGWYRTGDLGRRDEDGYLE 405
|
410
....*....|..
gi 2024458455 387 FVGRADDVINSA 398
Cdd:pfam00501 406 IVGRKKDQIKLG 417
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
82-494 |
3.39e-57 |
|
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: 197.53 E-value: 3.39e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 82 DGEEVKWSFEELGVLSRKAANVLSGAcSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKA 161
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAAL-GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 162 KGVITNDsvastVESVEADCQSLKFKLLVSE-GHREGWLSF---KDLLKTAPSDHRCVTT----KSQHPVAIYFTSGTTG 233
Cdd:cd05926 88 KLVLTPK-----GELGPASRAASKLGLAILElALDVGVLIRapsAESLSNLLADKKNAKSegvpLPDDLALILHTSGTTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 234 APKMTEHSH--------------------CSY-------GIGLTV-------SGSC----------TF------------ 257
Cdd:cd05926 163 RPKGVPLTHrnlaasatnitntykltpddRTLvvmplfhVHGLVAsllstlaAGGSvvlpprfsasTFwpdvrdynatwy 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 258 ----------------------NSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTETV--LVCGNFKGMEIKPGSMG 313
Cdd:cd05926 243 tavptihqillnrpepnpesppPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqMTSNPLPPGPRKPGSVG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 314 KPSpGYDVKIIDENGNILPPGKEGEIAIKVKP-TRPlflftcYTDDPEKTKA-TVRGDFYVTGDRGLMDEDGYFWFVGRA 391
Cdd:cd05926 323 KPV-GVEVRILDEDGEILPPGVVGEICLRGPNvTRG------YLNNPEANAEaAFKDGWFRTGDLGYLDADGYLFLTGRI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 392 DDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYvshdpEKMMKDLQDHVKKATAPYKYPR 471
Cdd:cd05926 396 KELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGA-----SVTEEELRAFCRKHLAAFKVPK 470
|
490 500
....*....|....*....|...
gi 2024458455 472 KMEFVRELPKTISGKIRRNELRQ 494
Cdd:cd05926 471 KVYFVDELPKTATGKIQRRKVAE 493
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
73-492 |
2.31e-56 |
|
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: 195.53 E-value: 2.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 73 NPALwwVDG-DGEEVkwSFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKD 151
Cdd:cd05904 21 RPAL--IDAaTGRAL--TYAELERRVRRLAAGLA-KRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 152 ILYRLQKSKAKGVITndsVASTVESVeadcQSLKFKLLVSEGHREGWLSFKDLLKTAPSDHRCVTTKSQH-PVAIYFTSG 230
Cdd:cd05904 96 IAKQVKDSGAKLAFT---TAELAEKL----ASLALPVVLLDSAEFDSLSFSDLLFEADEAEPPVVVIKQDdVAALLYSSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 231 TTGAPK--MTEH------------------------------SHcSYGIGL----------TV----------------- 251
Cdd:cd05904 169 TTGRSKgvMLTHrnliamvaqfvagegsnsdsedvflcvlpmFH-IYGLSSfalgllrlgaTVvvmprfdleellaaier 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 252 ---------------------SGSCTFNSLRHCVSAGEPINPEVMAKWKA-WTGLDIHECYGQTET---VLVCGNFKGME 306
Cdd:cd05904 248 ykvthlpvvppivlalvkspiVDKYDLSSLRQIMSGAAPLGKELIEAFRAkFPNVDLGQGYGMTEStgvVAMCFAPEKDR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 307 IKPGSMGKPSPGYDVKIID-ENGNILPPGKEGEIAIKvKPTrplfLFTCYTDDPEKTKATVRGDFYV-TGDRGLMDEDGY 384
Cdd:cd05904 328 AKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIR-GPS----IMKGYLNNPEATAATIDKEGWLhTGDLCYIDEDGY 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 385 FWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNyvSHDPEkmmKDLQDHVKKAT 464
Cdd:cd05904 403 LFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPG--SSLTE---DEIMDFVAKQV 477
|
490 500
....*....|....*....|....*...
gi 2024458455 465 APYKYPRKMEFVRELPKTISGKIRRNEL 492
Cdd:cd05904 478 APYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
52-493 |
2.91e-56 |
|
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: 197.71 E-value: 2.91e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 52 NFASDVLDRWakvekEGKKTKNPALWWVDGDGEEVKWSFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLNV 131
Cdd:cd05968 61 NIVEQLLDKW-----LADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGLR-ALGVGKGDRVGIYLPMIPEIVPAFL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 132 ACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVITND---------SVASTVESVEADCQSLKfKLLVSEG-------HR 195
Cdd:cd05968 135 AVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADgftrrgrevNLKEEADKACAQCPTVE-KVVVVRHlgndftpAK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 196 EGWLSFKDLLKTAPSdhRCVTTKSQHPVAIYFTSGTTGAPKMTEHSHCSYGI---------------------------- 247
Cdd:cd05968 214 GRDLSYDEEKETAGD--GAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLkaaqdmyfqfdlkpgdlltwftdlgwmm 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 248 -------GLTVSG-------------------------------SCTF-----------------NSLRHCVSAGEPINP 272
Cdd:cd05968 292 gpwlifgGLILGAtmvlydgapdhpkadrlwrmvedheithlglSPTLiralkprgdapvnahdlSSLRVLGSTGEPWNP 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 273 EVMaKWKAWTGLD----IHECYGQTETVL-VCGNFKGMEIKPGSMGKPSPGYDVKIIDENGNILPPgKEGEIAIKvKP-- 345
Cdd:cd05968 372 EPW-NWLFETVGKgrnpIINYSGGTEISGgILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARP-EVGELVLL-APwp 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 346 --TRPLFlftcytDDPEKTKATVRG---DFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLES 420
Cdd:cd05968 449 gmTRGFW------RDEDRYLETYWSrfdNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLES 522
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024458455 421 AVVSSPDPIRGEVVKAFVVLTPNYVSHD--PEKMMKDLQDHVKKATApykyPRKMEFVRELPKTISGKIRRNELR 493
Cdd:cd05968 523 AAIGVPHPVKGEAIVCFVVLKPGVTPTEalAEELMERVADELGKPLS----PERILFVKDLPKTRNAKVMRRVIR 593
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
89-492 |
1.31e-54 |
|
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: 189.23 E-value: 1.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 89 SFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVITN- 167
Cdd:cd05935 3 TYLELLEVVKKLASFLS-NKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGs 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 168 --DSVA-----STVESVEADCQSLKFKLLVSEGHREGW--LSFKDL-LKTAPSDHrcvTTKSQHPVAIYFTSGTT----- 232
Cdd:cd05935 82 elDDLAlipytSGTTGLPKGCMHTHFSAAANALQSAVWtgLTPSDViLACLPLFH---VTGFVGSLNTAVYVGGTyvlma 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 233 -----GAPKMTEHSHCSYGIGLT-----------VSGSCtFNSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTETV 296
Cdd:cd05935 159 rwdreTALELIEKYKVTFWTNIPtmlvdllatpeFKTRD-LSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 297 LVCGNFKGMEIKPGSMGKPSPGYDVKIID-ENGNILPPGKEGEIAIKvKPTrplfLFTCYTDDPEKTKA---TVRG-DFY 371
Cdd:cd05935 238 SQTHTNPPLRPKLQCLGIP*FGVDARVIDiETGRELPPNEVGEIVVR-GPQ----IFKGYWNRPEETEEsfiEIKGrRFF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 372 VTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYVSHDPEk 451
Cdd:cd05935 313 RTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTE- 391
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2024458455 452 mmKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNEL 492
Cdd:cd05935 392 --EDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
88-495 |
2.46e-54 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 190.09 E-value: 2.46e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 88 WSFEELGVLSRKAANVLsGACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVITN 167
Cdd:PRK07514 29 YTYGDLDAASARLANLL-VALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 168 DSVASTVESVEADCQSLKFKLLVSEGHreGwlSFKDLLKTAPSDHRCVTTKSQHPVAIYFTSGTTGAPK--M-------- 237
Cdd:PRK07514 108 PANFAWLSKIAAAAGAPHVETLDADGT--G--SLLEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKgaMlshgnlls 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 238 -----------TE-----------HSHcsygiGLTVSGSC---------------------------------TF----- 257
Cdd:PRK07514 184 naltlvdywrfTPddvlihalpifHTH-----GLFVATNVallagasmiflpkfdpdavlalmpratvmmgvpTFytrll 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 258 ----------NSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTETVLVCGN-FKGmEIKPGSMGKPSPGYDVKIID- 325
Cdd:PRK07514 259 qeprltreaaAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTETNMNTSNpYDG-ERRAGTVGFPLPGVSLRVTDp 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 326 ENGNILPPGKEGEIAIKvKPTrplfLFTCYTDDPEKTKATVRGD-FYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGP 404
Cdd:PRK07514 338 ETGAELPPGEIGMIEVK-GPN----VFKGYWRMPEKTAEEFRADgFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYP 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 405 FEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNyVSHDPEKMMKDLQDHVkkatAPYKYPRKMEFVRELPKTIS 484
Cdd:PRK07514 413 KEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPG-AALDEAAILAALKGRL----ARFKQPKRVFFVDELPRNTM 487
|
490
....*....|.
gi 2024458455 485 GKIRRNELRQK 495
Cdd:PRK07514 488 GKVQKNLLREQ 498
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
79-487 |
6.40e-54 |
|
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: 188.58 E-value: 6.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 79 VDGDgEEVKWSFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQK 158
Cdd:cd05911 3 IDAD-TGKELTYAQLRTLSRRLAAGLR-KLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 159 SKAKGVITNdsvASTVESVEADCQSLKF--KLLVSEGHREGWLSFKDLLKT-----APSDHRCVTTKSQHPVAIYFTSGT 231
Cdd:cd05911 81 SKPKVIFTD---PDGLEKVKEAAKELGPkdKIIVLDDKPDGVLSIEDLLSPtlgeeDEDLPPPLKDGKDDTAAILYSSGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 232 TGAPK--MTEHSHC-----------------------------SYGI---------GLTV-------------------- 251
Cdd:cd05911 158 TGLPKgvCLSHRNLianlsqvqtflygndgsndvilgflplyhIYGLfttlasllnGATViimpkfdselfldliekyki 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 252 ---------------SGSCT---FNSLRHCVSAGEPINPEVMAKWKA-WTGLDIHECYGQTETVLVCGNFKGMEIKPGSM 312
Cdd:cd05911 238 tflylvppiaaalakSPLLDkydLSSLRVILSGGAPLSKELQELLAKrFPNATIKQGYGMTETGGILTVNPDGDDKPGSV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 313 GKPSPGYDVKIIDENGN-ILPPGKEGEIAIkvkptRPLFLFTCYTDDPEKTKAT-VRGDFYVTGDRGLMDEDGYFWFVGR 390
Cdd:cd05911 318 GRLLPNVEAKIVDDDGKdSLGPNEPGEICV-----RGPQVMKGYYNNPEATKETfDEDGWLHTGDIGYFDEDGYLYIVDR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 391 ADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNyvshdpEKMM-KDLQDHVKKATAPYKY 469
Cdd:cd05911 393 KKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPG------EKLTeKEVKDYVAKKVASYKQ 466
|
490
....*....|....*....
gi 2024458455 470 PRK-MEFVRELPKTISGKI 487
Cdd:cd05911 467 LRGgVVFVDEIPKSASGKI 485
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
89-499 |
6.78e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 189.79 E-value: 6.78e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 89 SFEELGVLSRKAANVLSGACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVITND 168
Cdd:PRK08314 37 SYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 169 SVASTVESVEADCQ-----------------SLKF-KLLVSEGHRE-----GWLSFKDLLK--------TAPSDHRCVtt 217
Cdd:PRK08314 117 ELAPKVAPAVGNLRlrhvivaqysdylpaepEIAVpAWLRAEPPLQalapgGVVAWKEALAaglappphTAGPDDLAV-- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 218 ksqhpvaIYFTSGTTGAPKMTEHSHCSY----------------GIGLTV------------------SGS--------- 254
Cdd:PRK08314 195 -------LPYTSGTTGVPKGCMHTHRTVmanavgsvlwsnstpeSVVLAVlplfhvtgmvhsmnapiyAGAtvvlmprwd 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 255 ------------CTF----------------------NSLRHCVSAGEPInPEVMA-KWKAWTGLDIHECYGQTETV--- 296
Cdd:PRK08314 268 reaaarlieryrVTHwtniptmvvdflaspglaerdlSSLRYIGGGGAAM-PEAVAeRLKELTGLDYVEGYGLTETMaqt 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 297 ---------LVCgnfkgmeikpgsMGKPSPGYDVKIID-ENGNILPPGKEGEIAIKvKPTrplfLFTCYTDDPEKTKA-- 364
Cdd:PRK08314 347 hsnppdrpkLQC------------LGIPTFGVDARVIDpETLEELPPGEVGEIVVH-GPQ----VFKGYWNRPEATAEaf 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 365 -TVRGD-FYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTP 442
Cdd:PRK08314 410 iEIDGKrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRP 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024458455 443 NYVSHDPEkmmKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELRQKEWRR 499
Cdd:PRK08314 490 EARGKTTE---EEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKAR 543
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
79-497 |
7.03e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 186.26 E-value: 7.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 79 VDGDGEEvkWSFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQK 158
Cdd:PRK08276 5 MAPSGEV--VTYGELEARSNRLAHGLR-ALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 159 SKAKGVITNDSVASTVESVEADCQSLKFKLLVSEGHREGWLSFKDLL----KTAPSDHRCVTTksqhpvaIYFTSGTTGA 234
Cdd:PRK08276 82 SGAKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALaaqpDTPIADETAGAD-------MLYSSGTTGR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 235 PK------------------MTEHSHCSYGIGLTVSGSCT---------FN----------------------------- 258
Cdd:PRK08276 155 PKgikrplpgldpdeapgmmLALLGFGMYGGPDSVYLSPAplyhtaplrFGmsalalggtvvvmekfdaeealalieryr 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 259 ----------------------------SLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTE----TVLVCGNFKGme 306
Cdd:PRK08276 235 vthsqlvptmfvrmlklpeevrarydvsSLRVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSEgggvTVITSEDWLA-- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 307 iKPGSMGKPSPGyDVKIIDENGNILPPGKEGEIAIKvkptRPLFLFTcYTDDPEKTKATVRGDFYVT-GDRGLMDEDGYF 385
Cdd:PRK08276 313 -HPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFE----MDGYPFE-YHNDPEKTAAARNPHGWVTvGDVGYLDEDGYL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 386 WFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAfVVLTPNYVSHDPEkMMKDLQDHVKKATA 465
Cdd:PRK08276 386 YLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA-VVQPADGADAGDA-LAAELIAWLRGRLA 463
|
490 500 510
....*....|....*....|....*....|..
gi 2024458455 466 PYKYPRKMEFVRELPKTISGKIRRNELRQKEW 497
Cdd:PRK08276 464 HYKCPRSIDFEDELPRTPTGKLYKRRLRDRYW 495
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
64-493 |
8.90e-51 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 181.03 E-value: 8.90e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 64 VEKEGKKTknpALWWVDGDGEEVKWSFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPE----WWLLnvACMrtGTV 139
Cdd:PRK08008 17 ADVYGHKT---ALIFESSGGVVRRYSYLELNEEINRTANLFY-SLGIRKGDKVALHLDNCPEfifcWFGL--AKI--GAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 140 PIPGTQQLTAKDILYRLQKSKAKGVITNDSVASTVESVEADC-QSLKFKLL--VSEGHREGWLSFKDLLKTAPSDHRCVT 216
Cdd:PRK08008 89 MVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDaTPLRHICLtrVALPADDGVSSFTQLKAQQPATLCYAP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 217 TKSQHPVA-IYFTSGTTGAPKMTEHSHCS------YG----------IGLTVSGS----CTFNSLRHCVSAG-------- 267
Cdd:PRK08008 169 PLSTDDTAeILFTSGTTSRPKGVVITHYNlrfagyYSawqcalrdddVYLTVMPAfhidCQCTAAMAAFSAGatfvllek 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 268 ------------------------------EPINP--------EVM-------AKWKAWT---GLDIHECYGQTETVL-V 298
Cdd:PRK08008 249 ysarafwgqvckyratitecipmmirtlmvQPPSAndrqhclrEVMfylnlsdQEKDAFEerfGVRLLTSYGMTETIVgI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 299 CGNFKGMEIKPGSMGKPSPGYDVKIIDENGNILPPGKEGEIAIKVKPTRPLFlfTCYTDDPEKTKATVRGDFYV-TGDRG 377
Cdd:PRK08008 329 IGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVPGKTIF--KEYYLDPKATAKVLEADGWLhTGDTG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 378 LMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNyVSHDPEKMMKDLQ 457
Cdd:PRK08008 407 YVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEG-ETLSEEEFFAFCE 485
|
490 500 510
....*....|....*....|....*....|....*.
gi 2024458455 458 DHVKKatapYKYPRKMEFVRELPKTISGKIRRNELR 493
Cdd:PRK08008 486 QNMAK----FKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
44-492 |
1.73e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 181.01 E-value: 1.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 44 RPEVPEY-FNFA--SDVLDRWAKVEKEgkktkNPALWWVdgdGEEVkwSFEELGVLSRKAANVLSGAcSLQCGDRVLLLL 120
Cdd:PRK06178 22 IPREPEYpHGERplTEYLRAWARERPQ-----RPAIIFY---GHVI--TYAELDELSDRFAALLRQR-GVGAGDRVAVFL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 121 PRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVITNDSVASTVESVEADCqSLKFKLLVS--------- 191
Cdd:PRK06178 91 PNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAET-SLRHVIVTSladvlpaep 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 192 -----EGHR------EGWLSFKDLLKTAPSDHRCVTTKSQHPVAIYFTSGTTGAPKMTEHSH--------CSYGIGLT-- 250
Cdd:PRK06178 170 tlplpDSLRaprlaaAGAIDLLPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQrdmvytaaAAYAVAVVgg 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 251 -------------------------VSGSCT-------------------------------------------FNSLRH 262
Cdd:PRK06178 250 edsvflsflpefwiagenfgllfplFSGATLvllarwdavafmaaveryrvtrtvmlvdnavelmdhprfaeydLSSLRQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 263 --CVSAGEPINPEVMAKWKAWTGLDIHE-CYGQTETvLVCGNF-KGMEI-------KPGSMGKPSPGYDVKIID-ENGNI 330
Cdd:PRK06178 330 vrVVSFVKKLNPDYRQRWRALTGSVLAEaAWGMTET-HTCDTFtAGFQDddfdllsQPVFVGLPVPGTEFKICDfETGEL 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 331 LPPGKEGEIAIKvKPTrplfLFTCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESA 410
Cdd:PRK06178 409 LPLGAEGEIVVR-TPS----LLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEAL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 411 LIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYvSHDPEkmmkDLQDHVKKATAPYKYPrKMEFVRELPKTISGKIRRN 490
Cdd:PRK06178 484 LGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGA-DLTAA----ALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQ 557
|
..
gi 2024458455 491 EL 492
Cdd:PRK06178 558 DL 559
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
55-494 |
3.68e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 180.20 E-value: 3.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 55 SDVLDRwaKVEKEGKKtknPALWWVdgdGEEVkwSFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLNVACM 134
Cdd:PRK05605 35 VDLYDN--AVARFGDR---PALDFF---GATT--TYAELGKQVRRAAAGLR-ALGVRPGDRVAIVLPNCPQHIVAFYAVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 135 RTGTVPIPGTQQLTAKDILYRLQKSKAKGVITNDSVASTVESVEADC-----------------QSLKFKLLVSE----- 192
Cdd:PRK05605 104 RLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTpletivsvnmiaampllQRLALRLPIPAlrkar 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 193 ----GHREGWLSFKDLLKTAP------SDHRCVTTKSqhPVAIYFTSGTTGAPKMTEHSH---CS--------------- 244
Cdd:PRK05605 184 aaltGPAPGTVPWETLVDAAIggdgsdVSHPRPTPDD--VALILYTSGTTGKPKGAQLTHrnlFAnaaqgkawvpglgdg 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 245 -------------YG--IGLTVSGSC------------------------TF----------------------NSLRHC 263
Cdd:PRK05605 262 pervlaalpmfhaYGltLCLTLAVSIggelvllpapdidlildamkkhppTWlpgvpplyekiaeaaeergvdlSGVRNA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 264 VSAGEPINPEVMAKWKAWTGLDIHECYGQTETV-LVCGNFKGMEIKPGSMGKPSPGYDVKIID-EN-GNILPPGKEGEIA 340
Cdd:PRK05605 342 FSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSDDRRPGYVGVPFPDTEVRIVDpEDpDETMPDGEEGELL 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 341 IKvKPTRplflFTCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLES 420
Cdd:PRK05605 422 VR-GPQV----FKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDA 496
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024458455 421 AVVSSPDPIRGEVVKAFVVLTPNyVSHDPEkmmkDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELRQ 494
Cdd:PRK05605 497 AVVGLPREDGSEEVVAAVVLEPG-AALDPE----GLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
85-494 |
1.07e-49 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 178.41 E-value: 1.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 85 EVKWSFEELGVLSRKAANVLSGAcSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGV 164
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 165 ITNDSVASTVESVEADCQSLKFKLLVSEGHREGWLSFKDLLKTAPSDHR--CVTTKSQHPVAIYFTSGTTGAPK------ 236
Cdd:PRK06155 123 VVEAALLAALEAADPGDLPLPAVWLLDAPASVSVPAGWSTAPLPPLDAPapAAAVQPGDTAAILYTSGTTGPSKgvccph 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 237 ---------MTEHSH-----------------------------CSYGIGLTVSGS----------CTF----------- 257
Cdd:PRK06155 203 aqfywwgrnSAEDLEigaddvlyttlplfhtnalnaffqallagATYVLEPRFSASgfwpavrrhgATVtyllgamvsil 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 258 -----------NSLRHCVSAGEPinPEVMAKWKAWTGLDIHECYGQTETVLVCGNFKGmEIKPGSMGKPSPGYDVKIIDE 326
Cdd:PRK06155 283 lsqparesdraHRVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTHG-SQRPGSMGRLAPGFEARVVDE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 327 NGNILPPGKEGEIAIKVKPtrPLFLFTCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFE 406
Cdd:PRK06155 360 HDQELPDGEPGELLLRADE--PFAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFE 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 407 VESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNyVSHDPEkmmkDLQDHVKKATAPYKYPRKMEFVRELPKTISGK 486
Cdd:PRK06155 438 VEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDG-TALEPV----ALVRHCEPRLAYFAVPRYVEFVAALPKTENGK 512
|
....*...
gi 2024458455 487 IRRNELRQ 494
Cdd:PRK06155 513 VQKFVLRE 520
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
257-493 |
2.49e-49 |
|
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: 176.03 E-value: 2.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 257 FNSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTETV-LVCGNFKGMEIKPGSMGKPSPGyDVKIIDENGNILPPGK 335
Cdd:cd05929 243 LSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQgLTIINGEEWLTHPGSVGRAVLG-KVHILDEDGNEVPPGE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 336 EGEIAIKVKPTrplflFTcYTDDPEKTKATVRGDFYVT-GDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEH 414
Cdd:cd05929 322 IGEVYFANGPG-----FE-YTNDPEKTAAARNEGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAH 395
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024458455 415 PAVLESAVVSSPDPIRGEVVKAfvVLTPNYVSHDPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELR 493
Cdd:cd05929 396 PKVLDAAVVGVPDEELGQRVHA--VVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
80-499 |
3.53e-49 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 178.61 E-value: 3.53e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 80 DGDGEEVKWSFEELgvLSR--KAANVLSgACSLQCGDRVLLLLPRIPE--WWLLnvACMRTGTV-PIPGTqqLTAKDILY 154
Cdd:PRK07529 51 DPLDRPETWTYAEL--LADvtRTANLLH-SLGVGPGDVVAFLLPNLPEthFALW--GGEAAGIAnPINPL--LEPEQIAE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 155 RLQKSKAKGVIT-----NDSVASTVESVEADCQSLKFKLLV-----------------SEGHREGWLSFKDLLKTAPSDH 212
Cdd:PRK07529 124 LLRAAGAKVLVTlgpfpGTDIWQKVAEVLAALPELRTVVEVdlarylpgpkrlavpliRRKAHARILDFDAELARQPGDR 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 213 R-CVTTKSQHPVAIYF-TSGTTGAPKMTEHSH-----------------------C---------SYGIGLT--VSGS-- 254
Cdd:PRK07529 204 LfSGRPIGPDDVAAYFhTGGTTGMPKLAQHTHgnevanawlgalllglgpgdtvfCglplfhvnaLLVTGLAplARGAhv 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 255 -------------------------CTF---------------------NSLRHCVSAGEPINPEVMAKWKAWTGLDIHE 288
Cdd:PRK07529 284 vlatpqgyrgpgvianfwkiveryrINFlsgvptvyaallqvpvdghdiSSLRYALCGAAPLPVEVFRRFEAATGVRIVE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 289 CYGQTE-TVLVCGNFKGMEIKPGSMGKPSPGYDVKII--DENGNIL---PPGKEGEIAIKvKPTrplfLFTCYTDDPEKT 362
Cdd:PRK07529 364 GYGLTEaTCVSSVNPPDGERRIGSVGLRLPYQRVRVVilDDAGRYLrdcAVDEVGVLCIA-GPN----VFSGYLEAAHNK 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 363 KATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTP 442
Cdd:PRK07529 439 GLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKP 518
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024458455 443 NyVSHDPEKMMKDLQDHVKKATApykYPRKMEFVRELPKTISGKIRRNELRQKEWRR 499
Cdd:PRK07529 519 G-ASATEAELLAFARDHIAERAA---VPKHVRILDALPKTAVGKIFKPALRRDAIRR 571
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
259-489 |
1.99e-48 |
|
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: 169.76 E-value: 1.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 259 SLRHcVSAGEpiNPEVMAKWKAWTGLDIHECYGQTETV-LVCgnFKGMEIKPGSMGKPSPGYDVKIIDENGNILPPGKEG 337
Cdd:cd17637 115 SLRH-VLGLD--APETIQRFEETTGATFWSLYGQTETSgLVT--LSPYRERPGSAGRPGPLVRVRIVDDNDRPVPAGETG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 338 EIAIKvkptRPLfLFTCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGR--ADDVINSAGYRIGPFEVESALIEHP 415
Cdd:cd17637 190 EIVVR----GPL-VFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWYAGRkpEKELIKPGGENVYPAEVEKVILEHP 264
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024458455 416 AVLESAVVSSPDPIRGEVVKAFVVLTPnyvSHDPEKmmKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRR 489
Cdd:cd17637 265 AIAEVCVIGVPDPKWGEGIKAVCVLKP---GATLTA--DELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
84-496 |
3.26e-48 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 173.22 E-value: 3.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 84 EEVKWSFEELGVLSRKAANVLSGACsLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKG 163
Cdd:PRK03640 24 EEKKVTFMELHEAVVSVAGKLAALG-VKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKC 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 164 VITNDSVASTVESVeadcQSLKFKLLVSEGHREgwlsfKDLLKTAPSDHrcVTTksqhpvaIYFTSGTTGAPK------- 236
Cdd:PRK03640 103 LITDDDFEAKLIPG----ISVKFAELMNGPKEE-----AEIQEEFDLDE--VAT-------IMYTSGTTGKPKgviqtyg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 237 --------------MTEHS---------HCS----------YGI--------------GLTVSGSCTF------------ 257
Cdd:PRK03640 165 nhwwsavgsalnlgLTEDDcwlaavpifHISglsilmrsviYGMrvvlvekfdaekinKLLQTGGVTIisvvstmlqrll 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 258 ---------NSLRHCVSAGEPINPEVMAKWKAWtGLDIHECYGQTETV--LVCGNFKGMEIKPGSMGKPSPGYDVKIIDe 326
Cdd:PRK03640 245 erlgegtypSSFRCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETAsqIVTLSPEDALTKLGSAGKPLFPCELKIEK- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 327 NGNILPPGKEGEIAIKvKPTrplfLFTCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFE 406
Cdd:PRK03640 323 DGVVVPPFEEGEIVVK-GPN----VTKGYLNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 407 VESALIEHPAVLESAVVSSPDPIRGEVVKAFVVltpnyvsHDPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGK 486
Cdd:PRK03640 398 IEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVV-------KSGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGK 470
|
490
....*....|
gi 2024458455 487 IRRNELRQKE 496
Cdd:PRK03640 471 LLRHELKQLV 480
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
259-497 |
3.26e-47 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 171.03 E-value: 3.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 259 SLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTETVLVcgNFKGME---IKPGSMGKPSPGYDVKIIDENGNILPPGK 335
Cdd:PRK12406 272 SLRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGAV--TFATSEdalSHPGTVGKAAPGAELRFVDEDGRPLPQGE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 336 EGEIAIKVkPTRPLFlftCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHP 415
Cdd:PRK12406 350 IGEIYSRI-AGNPDF---TYHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVP 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 416 AVLESAVVSSPDPIRGEVVKAFVVLTPNyVSHDPEkmmkDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELRQK 495
Cdd:PRK12406 426 GVHDCAVFGIPDAEFGEALMAVVEPQPG-ATLDEA----DIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
|
..
gi 2024458455 496 EW 497
Cdd:PRK12406 501 YW 502
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
83-495 |
3.94e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 171.50 E-value: 3.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 83 GEEVKWSfeELGVLSRKAANVLSGAcSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAK 162
Cdd:PRK07786 40 GNTTTWR--ELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 163 GVITNDSVASTVESVEADCQSLKFKLLVSEGHREGWLSFKDLLKTAPSDHRCVTTKSQHPVAIYFTSGTTGAPKMTEHSH 242
Cdd:PRK07786 117 VVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 243 ---------CSYGIGLTVSGSCTFNS--LRHCVSAGE--------------PI---NPE----------------VMAKW 278
Cdd:PRK07786 197 anltgqamtCLRTNGADINSDVGFVGvpLFHIAGIGSmlpglllgaptviyPLgafDPGqlldvleaekvtgiflVPAQW 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 279 KA------------------W-------TGLD----------IHECYGQTETVLVCGNFKGMEI--KPGSMGKPSPGYDV 321
Cdd:PRK07786 277 QAvcaeqqarprdlalrvlsWgaapasdTLLRqmaatfpeaqILAAFGQTEMSPVTCMLLGEDAirKLGSVGKVIPTVAA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 322 KIIDENGNILPPGKEGEIAIKvKPTrplfLFTCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYR 401
Cdd:PRK07786 357 RVVDENMNDVPVGEVGEIVYR-APT----LMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGEN 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 402 IGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNyvshDPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPK 481
Cdd:PRK07786 432 IYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRND----DAALTLEDLAEFLTDRLARYKHPKALEIVDALPR 507
|
490
....*....|....
gi 2024458455 482 TISGKIRRNELRQK 495
Cdd:PRK07786 508 NPAGKVLKTELRER 521
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
84-494 |
5.78e-47 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 171.49 E-value: 5.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 84 EEVKWSFEEL-GVLSRKAANVLsgACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAK 162
Cdd:PRK12583 42 QALRYTWRQLaDAVDRLARGLL--ALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 163 GVITNDSVAST----------VESVEADCQSL------KFKLLVSEGHRE--GWLSFKDLLKTAPS------DHRCVTTK 218
Cdd:PRK12583 120 WVICADAFKTSdyhamlqellPGLAEGQPGALacerlpELRGVVSLAPAPppGFLAWHELQARGETvsrealAERQASLD 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 219 SQHPVAIYFTSGTTGAPK---------------------MTEHS---------HCsYGIGLTV-----SGSCT------- 256
Cdd:PRK12583 200 RDDPINIQYTSGTTGFPKgatlshhnilnngyfvaeslgLTEHDrlcvpvplyHC-FGMVLANlgcmtVGACLvypneaf 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 257 -------------------------------------FNSLRHCVSAGEPINPEVMAKWKAWTGL-DIHECYGQTET--- 295
Cdd:PRK12583 279 dplatlqaveeerctalygvptmfiaeldhpqrgnfdLSSLRTGIMAGAPCPIEVMRRVMDEMHMaEVQIAYGMTETspv 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 296 VLVCGNFKGMEIKPGSMGKPSPGYDVKIIDENGNILPPGKEGEIAikvkpTRPLFLFTCYTDDPEKTKATVRGDFYV-TG 374
Cdd:PRK12583 359 SLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELC-----TRGYSVMKGYWNNPEATAESIDEDGWMhTG 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 375 DRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYVSHDPEkmmk 454
Cdd:PRK12583 434 DLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEE---- 509
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2024458455 455 dLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELRQ 494
Cdd:PRK12583 510 -LREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMRE 548
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
257-493 |
6.28e-47 |
|
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: 166.30 E-value: 6.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 257 FNSLRHCVSAGEPINPEVMAKWKAWTGL-DIHECYGQTETVLVCGNFK---GMEIKPGSMGKPSPGYDVKIIDENGNILP 332
Cdd:cd05917 117 LSSLRTGIMAGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRtddSIEKRVNTVGRIMPHTEAKIVDPEGGIVP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 333 P-GKEGEIAIkvkptRPLFLFTCYTDDPEKTKATVRGD-FYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESA 410
Cdd:cd05917 197 PvGVPGELCI-----RGYSVMKGYWNDPEKTAEAIDGDgWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEF 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 411 LIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNyvshdPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRN 490
Cdd:cd05917 272 LHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEG-----AELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKF 346
|
...
gi 2024458455 491 ELR 493
Cdd:cd05917 347 KLR 349
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
55-494 |
1.40e-46 |
|
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: 169.56 E-value: 1.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 55 SDVLDRWAkvEKEGKKTknpALwwVDGDGEevkWSFEELGVLSRKAANVLSGAcSLQCGDRVLLLLPRIPEWWLLNVACM 134
Cdd:COG1021 28 GDLLRRRA--ERHPDRI---AV--VDGERR---LSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 135 RTGTVPI---PGTQQLtakDILYRLQKSKAKGVITNDSVA-----STVESVEADCQSLKFKLLVseGHREGWLSFKDLLk 206
Cdd:COG1021 97 RAGAIPVfalPAHRRA---EISHFAEQSEAVAYIIPDRHRgfdyrALARELQAEVPSLRHVLVV--GDAGEFTSLDALL- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 207 TAPSDHRCVTTKSQHpVAIYFTS-GTTGAPKM---------------------TEHS---------H----CSYGI---- 247
Cdd:COG1021 171 AAPADLSEPRPDPDD-VAFFQLSgGTTGLPKLiprthddylysvrasaeicglDADTvylaalpaaHnfplSSPGVlgvl 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 248 --GLTV----SGSCT--F--------------------------------NSLRHCVSAGEPINPEVMAkwkawtgldih 287
Cdd:COG1021 250 yaGGTVvlapDPSPDtaFplierervtvtalvpplallwldaaersrydlSSLRVLQVGGAKLSPELAR----------- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 288 ecygQTETVLVCG---NFkGM--------------EIKPGSMGKP-SPGYDVKIIDENGNILPPGKEGEIAikvkpTRPL 349
Cdd:COG1021 319 ----RVRPALGCTlqqVF-GMaeglvnytrlddpeEVILTTQGRPiSPDDEVRIVDEDGNPVPPGEVGELL-----TRGP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 350 FLFTCYTDDPEKTKA--TVRGdFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPD 427
Cdd:COG1021 389 YTIRGYYRAPEHNARafTPDG-FYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPD 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024458455 428 PIRGEVVKAFVVLTpnyvshDPEKMMKDLQDHVK-KATAPYKYPRKMEFVRELPKTISGKIRRNELRQ 494
Cdd:COG1021 468 EYLGERSCAFVVPR------GEPLTLAELRRFLReRGLAAFKLPDRLEFVDALPLTAVGKIDKKALRA 529
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
258-494 |
7.87e-46 |
|
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: 165.21 E-value: 7.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 258 NSLRHCVSAGEPINPEVMAKWKAwTGLDIHECYGQTETV--LVCGNFKGMEIKPGSMGKPSPGYDVKIIDENGnilPPGK 335
Cdd:cd05912 189 NNLRCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTETCsqIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQ---PPYE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 336 EGEIAIK---VKPTrplflftcYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALI 412
Cdd:cd05912 265 VGEILLKgpnVTKG--------YLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLL 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 413 EHPAVLESAVVSSPDPIRGEVVKAFVVLtpnyvshDPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNEL 492
Cdd:cd05912 337 SHPAIKEAGVVGIPDDKWGQVPVAFVVS-------ERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
..
gi 2024458455 493 RQ 494
Cdd:cd05912 410 KQ 411
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
88-499 |
1.39e-45 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 167.23 E-value: 1.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 88 WSFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVITN 167
Cdd:PRK06087 50 YTYSALDHAASRLANWLL-AKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 168 DSVAST-----VESVEADCQSLKFKLLV-SEGHREGWLSFKDLLKTAPSDHRCVTTKSQHPVAIYFTSGTTGAPK----- 236
Cdd:PRK06087 129 TLFKQTrpvdlILPLQNQLPQLQQIVGVdKLAPATSSLSLSQIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKgvmlt 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 237 -----MTEHSHCSyGIGLT-------------------------VSGS---------------------CT--------- 256
Cdd:PRK06087 209 hnnilASERAYCA-RLNLTwqdvfmmpaplghatgflhgvtapfLIGArsvlldiftpdaclalleqqrCTcmlgatpfi 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 257 -------------FNSLRHCVSAGEPInPEVMAKWKAWTGLDIHECYGQTETV--LVCGNFKGMEIKPGSMGKPSPGYDV 321
Cdd:PRK06087 288 ydllnllekqpadLSALRFFLCGGTTI-PKKVARECQQRGIKLLSVYGSTESSphAVVNLDDPLSRFMHTDGYAAAGVEI 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 322 KIIDENGNILPPGKEGEIAikvkpTRPLFLFTCYTDDPEKTKATVRGD-FYVTGDRGLMDEDGYFWFVGRADDVINSAGY 400
Cdd:PRK06087 367 KVVDEARKTLPPGCEGEEA-----SRGPNVFMGYLDEPELTARALDEEgWYYSGDLCRMDEAGYIKITGRKKDIIVRGGE 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 401 RIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYvsHDPEkmMKDLQDHV-KKATAPYKYPRKMEFVREL 479
Cdd:PRK06087 442 NISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPH--HSLT--LEEVVAFFsRKRVAKYKYPEHIVVIDKL 517
|
490 500
....*....|....*....|
gi 2024458455 480 PKTISGKIRRNELRQKEWRR 499
Cdd:PRK06087 518 PRTASGKIQKFLLRKDIMRR 537
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
257-493 |
2.11e-45 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 167.12 E-value: 2.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 257 FNSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTET--VLVCGNFKGMEIKpGSMGKPSPGYDVKIIDENGNILPPG 334
Cdd:PRK07059 326 FSKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETspVATCNPVDATEFS-GTIGLPLPSTEVSIRDDDGNDLPLG 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 335 KEGEIAIKvKPTrplfLFTCYTDDPEKTKATVRGD-FYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIE 413
Cdd:PRK07059 405 EPGEICIR-GPQ----VMAGYWNRPDETAKVMTADgFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVAS 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 414 HPAVLESAVVSSPDPIRGEVVKAFVvltpnyVSHDPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELR 493
Cdd:PRK07059 480 HPGVLEVAAVGVPDEHSGEAVKLFV------VKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
258-499 |
3.06e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 166.75 E-value: 3.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 258 NSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTETVLVC-GNFKGMEIKPGSMGKPSPGYDVKIID-ENGNILPPGK 335
Cdd:PRK06710 323 SSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVThSNFLWEKRVPGSIGVPWPDTEAMIMSlETGEALPPGE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 336 EGEIAIKvKPTrplfLFTCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHP 415
Cdd:PRK06710 403 IGEIVVK-GPQ----IMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHE 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 416 AVLESAVVSSPDPIRGEVVKAFVVLTPNYVSHDPEkmmkdLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELRQK 495
Cdd:PRK06710 478 KVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEE-----LNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEE 552
|
....
gi 2024458455 496 EWRR 499
Cdd:PRK06710 553 EKRK 556
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
58-489 |
6.54e-45 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 166.66 E-value: 6.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 58 LDRWAKvekegKKTKNPALWWVDGD-GEEVKWSFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLNVACMRT 136
Cdd:PRK10524 59 VDRHLA-----KRPEQLALIAVSTEtDEERTYTFRQLHDEVNRMAAMLR-SLGVQRGDRVLIYMPMIAEAAFAMLACARI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 137 G---TVPIPGtqqLTAKDILYRLQKSKAKGVITNDS------VASTVESVEADCQSLKFK----LLVSEG-HREGWLSFK 202
Cdd:PRK10524 133 GaihSVVFGG---FASHSLAARIDDAKPVLIVSADAgsrggkVVPYKPLLDEAIALAQHKprhvLLVDRGlAPMARVAGR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 203 DL----LKTAPSDHR--CVTTKSQHPVAIYFTSGTTGAPKMTE------------------------------------- 239
Cdd:PRK10524 210 DVdyatLRAQHLGARvpVEWLESNEPSYILYTSGTTGKPKGVQrdtggyavalatsmdtifggkagetffcasdigwvvg 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 240 HSHCSYG---IGLTV---SG-------------------SCTF----------------------NSLRHCVSAGEPINp 272
Cdd:PRK10524 290 HSYIVYApllAGMATimyEGlptrpdagiwwrivekykvNRMFsaptairvlkkqdpallrkhdlSSLRALFLAGEPLD- 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 273 EVMAKWKAWT-GLDIHECYGQTET---VLvcGNFKGMEIKP---GSMGKPSPGYDVKIIDEN-GNILPPGKEGEIAIkVK 344
Cdd:PRK10524 369 EPTASWISEAlGVPVIDNYWQTETgwpIL--AIARGVEDRPtrlGSPGVPMYGYNVKLLNEVtGEPCGPNEKGVLVI-EG 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 345 PTRPLFLFTCYTDDPEKTK---ATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESA 421
Cdd:PRK10524 446 PLPPGCMQTVWGDDDRFVKtywSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVA 525
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024458455 422 VVSSPDPIRGEVVKAFVVLTPNYVSHDPEKMMK---DLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRR 489
Cdd:PRK10524 526 VVGVKDALKGQVAVAFVVPKDSDSLADREARLAlekEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLR 596
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
83-492 |
6.93e-45 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 164.26 E-value: 6.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 83 GEEVKWSFEELGVLSRKAANVLSGACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAK 162
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 163 GVITNDSVASTVESVEAdcqslkfkllVSEGHREGWL-SFKDLLKTAPSDhrCVTTKSQHPVAIYFTSGTTGAPK----- 236
Cdd:PRK06839 103 VLFVEKTFQNMALSMQK----------VSYVQRVISItSLKEIEDRKIDN--FVEKNESASFIICYTSGTTGKPKgavlt 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 237 ----------------MTEHSHCSY--------GIGL---------------------------------TVSGSCT--- 256
Cdd:PRK06839 171 qenmfwnalnntfaidLTMHDRSIVllplfhigGIGLfafptlfaggviivprkfeptkalsmiekhkvtVVMGVPTihq 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 257 ------------FNSLRHCVSAGEPINPEVMAKWKAwTGLDIHECYGQTET-----VLVCGNFKGmeiKPGSMGKPSPGY 319
Cdd:PRK06839 251 alincskfettnLQSVRWFYNGGAPCPEELMREFID-RGFLFGQGFGMTETsptvfMLSEEDARR---KVGSIGKPVLFC 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 320 DVKIIDENGNILPPGKEGEIAIKvKPTrplfLFTCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAG 399
Cdd:PRK06839 327 DYELIDENKNKVEVGEVGELLIR-GPN----VMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 400 YRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYVSHDpekmmKDLQDHVKKATAPYKYPRKMEFVREL 479
Cdd:PRK06839 402 ENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIE-----KDVIEHCRLFLAKYKIPKEIVFLKEL 476
|
490
....*....|...
gi 2024458455 480 PKTISGKIRRNEL 492
Cdd:PRK06839 477 PKNATGKIQKAQL 489
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
257-496 |
1.28e-44 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 164.84 E-value: 1.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 257 FNSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTE-TVLVCGNFKGMEIKPGSMGKPSPGYDVKIIDENGNILPPGK 335
Cdd:PRK08974 324 FSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTEcSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGE 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 336 EGEIAIKvKPTrplfLFTCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHP 415
Cdd:PRK08974 404 PGELWVK-GPQ----VMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHP 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 416 AVLESAVVSSPDPIRGEVVKAFVvltpnyVSHDPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELRQK 495
Cdd:PRK08974 479 KVLEVAAVGVPSEVSGEAVKIFV------VKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
|
.
gi 2024458455 496 E 496
Cdd:PRK08974 553 A 553
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
261-494 |
1.07e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 160.54 E-value: 1.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 261 RHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTETVLVCGNFKGMEIKPGSMGKPSPGYDVKIIDENGNILPPGKE--GE 338
Cdd:PRK07787 244 RLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGEtvGE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 339 IAIKvKPTrplfLFTCYTDDPEKTKATVRGD-FYVTGDRGLMDEDGYFWFVGR-ADDVINSAGYRIGPFEVESALIEHPA 416
Cdd:PRK07787 324 LQVR-GPT----LFDGYLNRPDATAAAFTADgWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPG 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024458455 417 VLESAVVSSPDPIRGEVVKAFVvltpnyVSHDPEKmMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELRQ 494
Cdd:PRK07787 399 VREAAVVGVPDDDLGQRIVAYV------VGADDVA-ADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
89-493 |
1.83e-42 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 158.89 E-value: 1.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 89 SFEELGVLSRKAANVLSGACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVITND 168
Cdd:PRK08751 52 TYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVID 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 169 SVASTVESVEADCQ-----------------------SLKF-KLLVSEGHREGWLSFKDLLKTApSDHRCVTTKSQHP-- 222
Cdd:PRK08751 132 NFGTTVQQVIADTPvkqvittglgdmlgfpkaalvnfVVKYvKKLVPEYRINGAIRFREALALG-RKHSMPTLQIEPDdi 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 223 VAIYFTSGTTGAPK------------MTEHSHCSYGIG--------------------LTVS-------GSCT------- 256
Cdd:PRK08751 211 AFLQYTGGTTGVAKgamlthrnlvanMQQAHQWLAGTGkleegcevvitalplyhifaLTANglvfmkiGGCNhlisnpr 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 257 -------------------------------------FNSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTETV-LV 298
Cdd:PRK08751 291 dmpgfvkelkktrftaftgvntlfngllntpgfdqidFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSpAA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 299 CGNFKGMEIKPGSMGKPSPGYDVKIIDENGNILPPGKEGEIAIKvKPTrplfLFTCYTDDPEKTKATVRGDFYV-TGDRG 377
Cdd:PRK08751 371 CINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIK-GPQ----VMKGYWKRPEETAKVMDADGWLhTGDIA 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 378 LMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVvltpnyVSHDPEKMMKDLQ 457
Cdd:PRK08751 446 RMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVI------VKKDPALTAEDVK 519
|
490 500 510
....*....|....*....|....*....|....*.
gi 2024458455 458 DHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELR 493
Cdd:PRK08751 520 AHARANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
89-494 |
5.40e-42 |
|
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: 155.23 E-value: 5.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 89 SFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLNVACMRTG--TVPIP---GTQQLTakdilYRLQKSKAKG 163
Cdd:cd05903 3 TYSELDTRADRLAAGLA-ALGVGPGDVVAFQLPNWWEFAVLYLACLRIGavTNPILpffREHELA-----FILRRAKAKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 164 VITNDSVASTveSVEADcqslkfkllvseghregwlsfkdllktaPSDhrcvttksqhPVAIYFTSGTTGAPKMTEHSHC 243
Cdd:cd05903 77 FVVPERFRQF--DPAAM----------------------------PDA----------VALLLFTSGTTGEPKGVMHSHN 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 244 S---------------------------------YG------IGLTV----------------SGSCTF----------- 257
Cdd:cd05903 117 TlsasirqyaerlglgpgdvflvaspmahqtgfvYGftlpllLGAPVvlqdiwdpdkalalmrEHGVTFmmgatpfltdl 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 258 -----------NSLRHCVSAGEPINPEVMAKwkAWTGLDIHEC--YGQTETVLVCGNfkgmeIKPG-------SMGKPSP 317
Cdd:cd05903 197 lnaveeageplSRLRTFVCGGATVPRSLARR--AAELLGAKVCsaYGSTECPGAVTS-----ITPApedrrlyTDGRPLP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 318 GYDVKIIDENGNILPPGKEGEIAIKvKPTrplfLFTCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINS 397
Cdd:cd05903 270 GVEIKVVDDTGATLAPGVEGELLSR-GPS----VFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 398 AGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPnyvSHDPEkmMKDLQDHVKKA-TAPYKYPRKMEFV 476
Cdd:cd05903 345 GGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKS---GALLT--FDELVAYLDRQgVAKQYWPERLVHV 419
|
490
....*....|....*...
gi 2024458455 477 RELPKTISGKIRRNELRQ 494
Cdd:cd05903 420 DDLPRTPSGKVQKFRLRE 437
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
81-497 |
8.37e-42 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 156.39 E-value: 8.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 81 GDGEEVkwSFEELGVLSRKAANVLSGAcSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSK 160
Cdd:PRK13391 20 STGEVV--TYRELDERSNRLAHLFRSL-GLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 161 AKGVITNDSVASTVESVEADCQSLKFKLLV-SEGHREGWLSFKDLLKTAPSDHRCVTTKSQhpvAIYFTSGTTGAPK--- 236
Cdd:PRK13391 97 ARALITSAAKLDVARALLKQCPGVRHRLVLdGDGELEGFVGYAEAVAGLPATPIADESLGT---DMLYSSGTTGRPKgik 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 237 -----------------------MTE-----------HSHCSYGIGLTVSGSCT-------------------------- 256
Cdd:PRK13391 174 rplpeqppdtplpltaflqrlwgFRSdmvylspaplyHSAPQRAVMLVIRLGGTvivmehfdaeqylalieeygvthtql 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 257 --------------------FNSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTETVLVCG-NFKGMEIKPGSMGKP 315
Cdd:PRK13391 254 vptmfsrmlklpeevrdkydLSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGLGFTAcDSEEWLAHPGTVGRA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 316 SPGyDVKIIDENGNILPPGKEGEIAIKVKptRPlflFTcYTDDPEKTKAT--VRGDFYVTGDRGLMDEDGYFWFVGRADD 393
Cdd:PRK13391 334 MFG-DLHILDDDGAELPPGEPGTIWFEGG--RP---FE-YLNDPAKTAEArhPDGTWSTVGDIGYVDEDGYLYLTDRAAF 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 394 VINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNyVSHDPEkMMKDLQDHVKKATAPYKYPRKM 473
Cdd:PRK13391 407 MIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDG-VDPGPA-LAAELIAFCRQRLSRQKCPRSI 484
|
490 500
....*....|....*....|....
gi 2024458455 474 EFVRELPKTISGKIRRNELRQKEW 497
Cdd:PRK13391 485 DFEDELPRLPTGKLYKRLLRDRYW 508
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
290-497 |
1.06e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 156.30 E-value: 1.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 290 YGQTE---TVLVCGNFKGMEIKP---GSMGKPSPGYDVKIIDENGNILPPGKEGEIAIKvkptRPLfLFTCYTDDPEKTK 363
Cdd:PRK06188 313 YGQTEapmVITYLRKRDHDPDDPkrlTSCGRPTPGLRVALLDEDGREVAQGEVGEICVR----GPL-VMDGYWNRPEETA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 364 ATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPN 443
Cdd:PRK06188 388 EAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPG 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2024458455 444 yVSHDPEkmmkDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELRQKEW 497
Cdd:PRK06188 468 -AAVDAA----ELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARYW 516
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
257-496 |
1.29e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 153.77 E-value: 1.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 257 FNSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTETV-LVCGNFKGmEIKPGSMGKPSPGYDVKIIDENGNILPPGK 335
Cdd:PRK05677 325 FSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSpVVSVNPSQ-AIQVGTIGIPVPSTLCKVIDDDGNELPLGE 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 336 EGEIAIKvKPTrplfLFTCYTDDPEKTKATVRGDFYV-TGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEH 414
Cdd:PRK05677 404 VGELCVK-GPQ----VMKGYWQRPEATDEILDSDGWLkTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAAL 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 415 PAVLESAVVSSPDPIRGEVVKAFVVLTPNyVSHDPEKMMKdlqdHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELRQ 494
Cdd:PRK05677 479 PGVLQCAAIGVPDEKSGEAIKVFVVVKPG-ETLTKEQVME----HMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRD 553
|
..
gi 2024458455 495 KE 496
Cdd:PRK05677 554 EE 555
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
89-495 |
2.64e-40 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 152.44 E-value: 2.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 89 SFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVITNd 168
Cdd:PLN02246 52 TYADVELLSRRVAAGLH-KLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQ- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 169 svASTVESVEADCQSLKFKLLVSEGHREGWLSFKDLLKTAPSDHRCVTTKSQHPVAIYFTSGTTGAPK--MTEHSHCSYG 246
Cdd:PLN02246 130 --SCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFSELTQADENELPEVEISPDDVVALPYSSGTTGLPKgvMLTHKGLVTS 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 247 IGLTVSG--------------------------SCTFNSLR----------------------HCVSAGEPINPEVMAKW 278
Cdd:PLN02246 208 VAQQVDGenpnlyfhsddvilcvlpmfhiyslnSVLLCGLRvgaailimpkfeigalleliqrHKVTIAPFVPPIVLAIA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 279 K-------------------AWTGLDIHEC-------------YGQTE--TVL-VCGNF--KGMEIKPGSMGKPSPGYDV 321
Cdd:PLN02246 288 KspvvekydlssirmvlsgaAPLGKELEDAfraklpnavlgqgYGMTEagPVLaMCLAFakEPFPVKSGSCGTVVRNAEL 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 322 KIID-ENGNILPPGKEGEIAIkvkptRPLFLFTCYTDDPEKTKATVRGDFYV-TGDRGLMDEDGYFWFVGRADDVINSAG 399
Cdd:PLN02246 368 KIVDpETGASLPRNQPGEICI-----RGPQIMKGYLNDPEATANTIDKDGWLhTGDIGYIDDDDELFIVDRLKELIKYKG 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 400 YRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNY-VSHDpekmmkDLQDHVKKATAPYKYPRKMEFVRE 478
Cdd:PLN02246 443 FQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSeITED------EIKQFVAKQVVFYKRIHKVFFVDS 516
|
490
....*....|....*..
gi 2024458455 479 LPKTISGKIRRNELRQK 495
Cdd:PLN02246 517 IPKAPSGKILRKDLRAK 533
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
79-492 |
5.01e-40 |
|
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: 150.56 E-value: 5.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 79 VDGDGeevKWSFEELGVLSRKAANVLSGAcSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPI---PGTQQLtakDILYR 155
Cdd:cd05920 35 VDGDR---RLTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVlalPSHRRS---ELSAF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 156 LQKSKAKGVITNDSVAstvesvEADCQSLkfkllvseghregwlsFKDLLKTAPSdhrcvttksqhpVAIYFTS-GTTGA 234
Cdd:cd05920 108 CAHAEAVAYIVPDRHA------GFDHRAL----------------ARELAESIPE------------VALFLLSgGTTGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 235 PKMTEHSHCSYGIGLTVSGS-CTFNS----------------------------------------------LRHCVSA- 266
Cdd:cd05920 154 PKLIPRTHNDYAYNVRASAEvCGLDQdtvylavlpaahnfplacpgvlgtllaggrvvlapdpspdaafpliEREGVTVt 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 267 ------------------------------GEPINPEVMAKWKAWTGLDIHECYGQTETVLvcgNFKGM----EIKPGSM 312
Cdd:cd05920 234 alvpalvslwldaaasrradlsslrllqvgGARLSPALARRVPPVLGCTLQQVFGMAEGLL---NYTRLddpdEVIIHTQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 313 GKP-SPGYDVKIIDENGNILPPGKEGEIAikvkpTRPLFLFTCYTDDPEKTKATVRGD-FYVTGDRGLMDEDGYFWFVGR 390
Cdd:cd05920 311 GRPmSPDDEIRVVDEEGNPVPPGEEGELL-----TRGPYTIRGYYRAPEHNARAFTPDgFYRTGDLVRRTPDGYLVVEGR 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 391 ADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTpnyvshDPEKMMKDLQDHVKKA-TAPYKY 469
Cdd:cd05920 386 IKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLR------DPPPSAAQLRRFLRERgLAAYKL 459
|
490 500
....*....|....*....|...
gi 2024458455 470 PRKMEFVRELPKTISGKIRRNEL 492
Cdd:cd05920 460 PDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
259-493 |
5.63e-40 |
|
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: 150.28 E-value: 5.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 259 SLRHCVSAGEPINPEVMAKWK-AWTGLDIHECYGQTETvlvcgnFKGMEI--------KPGSMGKPSPGYDVKIIDENGN 329
Cdd:cd05922 232 SLRYLTQAGGRLPQETIARLReLLPGAQVYVMYGQTEA------TRRMTYlpperileKPGSIGLAIPGGEFEILDDDGT 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 330 ILPPGKEGEIAikvkPTRPLFLFTCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVES 409
Cdd:cd05922 306 PTPPGEPGEIV----HRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 410 ALIEHPAVLESAVVSSPDPIrGEVVKAFVVLtpnyvshDPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRR 489
Cdd:cd05922 382 AARSIGLIIEAAAVGLPDPL-GEKLALFVTA-------PDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDY 453
|
....
gi 2024458455 490 NELR 493
Cdd:cd05922 454 AALR 457
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
73-495 |
1.19e-39 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 151.12 E-value: 1.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 73 NPALWWVDGDgeeVKWSFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPI---PGTQQlta 149
Cdd:PRK08315 32 REALVYRDQG---LRWTYREFNEEVDALAKGLL-ALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVtinPAYRL--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 150 KDILYRLQKSKAKGVITNDSVAST--VESVE------ADCQ----------SLKFKLLVSEGHREGWLSFKDLLK--TAP 209
Cdd:PRK08315 105 SELEYALNQSGCKALIAADGFKDSdyVAMLYelapelATCEpgqlqsarlpELRRVIFLGDEKHPGMLNFDELLAlgRAV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 210 SDHRCVTTKSQ----HPVAIYFTSGTTGAPK---MTEHS---------------------------HCsYGIGLTVSGS- 254
Cdd:PRK08315 185 DDAELAARQATldpdDPINIQYTSGTTGFPKgatLTHRNilnngyfigeamklteedrlcipvplyHC-FGMVLGNLACv 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 255 --------------------------CT----------------------FNSLRHCVSAGEPINPEVMAKWKAWTGL-D 285
Cdd:PRK08315 264 thgatmvypgegfdplatlaaveeerCTalygvptmfiaeldhpdfarfdLSSLRTGIMAGSPCPIEVMKRVIDKMHMsE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 286 IHECYGQTETVLVcgNFK-----GMEIKPGSMGKPSPGYDVKIID-ENGNILPPGKEGEIAikvkpTRPLFLFTCYTDDP 359
Cdd:PRK08315 344 VTIAYGMTETSPV--STQtrtddPLEKRVTTVGRALPHLEVKIVDpETGETVPRGEQGELC-----TRGYSVMKGYWNDP 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 360 EKTKATVRGDFYV-TGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFV 438
Cdd:PRK08315 417 EKTAEAIDADGWMhTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWI 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024458455 439 VLTPNyVSHDPEkmmkDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELRQK 495
Cdd:PRK08315 497 ILRPG-ATLTEE----DVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREM 548
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
98-493 |
1.39e-39 |
|
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: 149.76 E-value: 1.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 98 RKAANVLSGAcSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVITNdsvastvesv 177
Cdd:cd12118 40 RRLASALAAL-GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVD---------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 178 eadcQSLKFKLLVSEGHRE-GWLSfkdllktaPSDHRcvttksqHPVAIYFTSGTTGAPKMTEHSH-------------- 242
Cdd:cd12118 109 ----REFEYEDLLAEGDPDfEWIP--------PADEW-------DPIALNYTSGTTGRPKGVVYHHrgaylnalanilew 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 243 -----CSY-------------------GIGLT------VSGSCTFNSLR------------------------------- 261
Cdd:cd12118 170 emkqhPVYlwtlpmfhcngwcfpwtvaAVGGTnvclrkVDAKAIYDLIEkhkvthfcgaptvlnmlanappsdarplphr 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 262 -HCVSAGEPINPEVMAKWKAwTGLDIHECYGQTET---VLVCgnfkgmEIKPGSMGKPSP-----------GY----DVK 322
Cdd:cd12118 250 vHVMTAGAPPPAAVLAKMEE-LGFDVTHVYGLTETygpATVC------AWKPEWDELPTEerarlkarqgvRYvgleEVD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 323 IIDENGNILPP--GKE-GEIAIkvkptRPLFLFTCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAG 399
Cdd:cd12118 323 VLDPETMKPVPrdGKTiGEIVF-----RGNIVMKGYLKNPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 400 YRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYvshdpEKMMKDLQDHVKKATAPYKYPRKMEFvREL 479
Cdd:cd12118 398 ENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGA-----KVTEEEIIAFCREHLAGFMVPKTVVF-GEL 471
|
490
....*....|....
gi 2024458455 480 PKTISGKIRRNELR 493
Cdd:cd12118 472 PKTSTGKIQKFVLR 485
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
259-495 |
2.12e-39 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 149.91 E-value: 2.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 259 SLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTETVLVC-GNFKGMEIKPGSMGKPSPGYDVKIIDENGNILPPGKEG 337
Cdd:PRK13382 313 SLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIAtATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVG 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 338 EIAIkvkptRPLFLFTCYTddPEKTKATVRGdFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAV 417
Cdd:PRK13382 393 TIFV-----RNDTQFDGYT--SGSTKDFHDG-FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDV 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024458455 418 LESAVVSSPDPIRGEVVKAFVVLTPnyvshDPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELRQK 495
Cdd:PRK13382 465 AEAAVIGVDDEQYGQRLAAFVVLKP-----GASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
259-493 |
3.47e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 149.69 E-value: 3.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 259 SLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTE-TVLVCGNFKGMEIKPGSMGKPSPGYDVKIIDENGNILPPGKEG 337
Cdd:PRK07788 324 SLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEvAFATIATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVG 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 338 EIAIkvkptRPLFLFTCYTDDpeKTKATVRGdFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAV 417
Cdd:PRK07788 404 RIFV-----GNGFPFEGYTDG--RDKQIIDG-LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDV 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024458455 418 LESAVVSSPDPIRGEVVKAFVVLTPNyvsHDPEKmmKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELR 493
Cdd:PRK07788 476 VEAAVIGVDDEEFGQRLRAFVVKAPG---AALDE--DAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELR 546
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
236-499 |
1.01e-38 |
|
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: 144.55 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 236 KMTEHSHCSYGIG--------LTVSGSCTFNSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTE-TVLVCGNFKGME 306
Cdd:cd05944 91 KLVERYRITSLSTvptvyaalLQVPVNADISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEaTCLVAVNPPDGP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 307 IKPGSMGKPSPGYDVKI--IDENGNIL---PPGKEGEIAIKvKPTrplfLFTCYTDDPEKTKATVRGDFYVTGDRGLMDE 381
Cdd:cd05944 171 KRPGSVGLRLPYARVRIkvLDGVGRLLrdcAPDEVGEICVA-GPG----VFGGYLYTEGNKNAFVADGWLNTGDLGRLDA 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 382 DGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYVShDPEKMMKDLQDHVK 461
Cdd:cd05944 246 DGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVV-EEEELLAWARDHVP 324
|
250 260 270
....*....|....*....|....*....|....*...
gi 2024458455 462 KATApykYPRKMEFVRELPKTISGKIRRNELRQKEWRR 499
Cdd:cd05944 325 ERAA---VPKHIEVLEELPVTAVGKVFKPALRADAIHR 359
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
74-499 |
4.32e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 143.26 E-value: 4.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 74 PALWWvdgdGEEVkWSFEEL--GVLSRKAANVLSGacsLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKD 151
Cdd:PRK07470 24 IALVW----GDRS-WTWREIdaRVDALAAALAARG---VRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 152 ILYRLQKSKAKGVITNDSVASTVESVEAdcQSLKFKLLVSEGHREGWLSFKDLLKTAP-SDHRCVTTKSQHPVAIYFTSG 230
Cdd:PRK07470 96 VAYLAEASGARAMICHADFPEHAAAVRA--ASPDLTHVVAIGGARAGLDYEALVARHLgARVANAAVDHDDPCWFFFTSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 231 TTGAPK--------M--------------TEHSHCS-------YGIGL-----TVSGSCTF------------------- 257
Cdd:PRK07470 174 TTGRPKaavlthgqMafvitnhladlmpgTTEQDASlvvaplsHGAGIhqlcqVARGAATVllpserfdpaevwalverh 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 258 --------------------------NSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTEtvlVCGNFK-------- 303
Cdd:PRK07470 254 rvtnlftvptilkmlvehpavdrydhSSLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGE---VTGNITvlppalhd 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 304 ---GMEIKPGSMGKPSPGYDVKIIDENGNILPPGKEGEIAIkvkptRPLFLFTCYTDDPEKTKATVRGDFYVTGDRGLMD 380
Cdd:PRK07470 331 aedGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICV-----IGPAVFAGYYNNPEANAKAFRDGWFRTGDLGHLD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 381 EDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNyVSHDPEkmmkDLQDHV 460
Cdd:PRK07470 406 ARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDG-APVDEA----ELLAWL 480
|
490 500 510
....*....|....*....|....*....|....*....
gi 2024458455 461 KKATAPYKYPRKMEFVRELPKTISGKIRRNELRQKEWRR 499
Cdd:PRK07470 481 DGKVARYKLPKRFFFWDALPKSGYGKITKKMVREELEER 519
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
87-493 |
1.09e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 141.48 E-value: 1.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 87 KWSFEELGVLSRKAANVLSGACSLQcGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVIT 166
Cdd:PRK09088 22 RWTYAELDALVGRLAAVLRRRGCVD-GERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 167 NDSVAStvesveADCQSLKFKLLVSEGHREGwlsfKDLLKTAPSDHrcvttksqhPVAIYFTSGTTGAPK---MTE---- 239
Cdd:PRK09088 101 DDAVAA------GRTDVEDLAAFIASADALE----PADTPSIPPER---------VSLILFTSGTSGQPKgvmLSErnlq 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 240 HSHCSYG--------------------IGLTVS--------GSC------------------------------------ 255
Cdd:PRK09088 162 QTAHNFGvlgrvdahssflcdapmfhiIGLITSvrpvlavgGSIlvsngfepkrtlgrlgdpalgithyfcvpqmaqafr 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 256 ---TFN--SLRH---CVSAGEPINPEVMAKWKAwTGLDIHECYGQTE--TVLvcgnfkGMEI-------KPGSMGKPSPG 318
Cdd:PRK09088 242 aqpGFDaaALRHltaLFTGGAPHAAEDILGWLD-DGIPMVDGFGMSEagTVF------GMSVdcdviraKAGAAGIPTPT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 319 YDVKIIDENGNILPPGKEGEIAIKvKPTrplfLFTCYTDDPEKTKATVRGD-FYVTGDRGLMDEDGYFWFVGRADDVINS 397
Cdd:PRK09088 315 VQTRVVDDQGNDCPAGVPGELLLR-GPN----LSPGYWRRPQATARAFTGDgWFRTGDIARRDADGFFWVVDRKKDMFIS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 398 AGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYVShDPEkmmkDLQDHVKKATAPYKYPRKMEFVR 477
Cdd:PRK09088 390 GGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPL-DLE----RIRSHLSTRLAKYKVPKHLRLVD 464
|
490
....*....|....*.
gi 2024458455 478 ELPKTISGKIRRNELR 493
Cdd:PRK09088 465 ALPRTASGKLQKARLR 480
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
83-493 |
1.77e-36 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 141.30 E-value: 1.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 83 GEEVkwSFEELGVLSRKAANVLSGAcSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAK 162
Cdd:PRK13390 22 GEQV--SYRQLDDDSAALARVLYDA-GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGAR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 163 GVITNDSVASTVESVEADcqslkFKLLVSEGHR-EGWLSFKDLLKTA-PSdhrcVTTKSQHPVAIYfTSGTTGAPK---- 236
Cdd:PRK13390 99 VLVASAALDGLAAKVGAD-----LPLRLSFGGEiDGFGSFEAALAGAgPR----LTEQPCGAVMLY-SSGTTGFPKgiqp 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 237 -----------------------MTE-----------HSH----CS--YGIGLTVSGSCTFN------------------ 258
Cdd:PRK13390 169 dlpgrdvdapgdpivaiarafydISEsdiyyssapiyHAAplrwCSmvHALGGTVVLAKRFDaqatlghveryritvtqm 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 259 ----------------------SLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTE----TVLVCGNFKGmeiKPGSM 312
Cdd:PRK13390 249 vptmfvrllkldadvrtrydvsSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEahgmTFIDSPDWLA---HPGSV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 313 GKPSPGyDVKIIDENGNILPPGKEGEIAIKvkptRPLFLFTcYTDDPEKTKATVR--GDFYVT-GDRGLMDEDGYFWFVG 389
Cdd:PRK13390 326 GRSVLG-DLHICDDDGNELPAGRIGTVYFE----RDRLPFR-YLNDPEKTAAAQHpaHPFWTTvGDLGSVDEDGYLYLAD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 390 RADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYvshDP-EKMMKDLQDHVKKATAPYK 468
Cdd:PRK13390 400 RKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGI---RGsDELARELIDYTRSRIAHYK 476
|
490 500
....*....|....*....|....*
gi 2024458455 469 YPRKMEFVRELPKTISGKIRRNELR 493
Cdd:PRK13390 477 APRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
290-485 |
2.08e-36 |
|
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: 137.43 E-value: 2.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 290 YGQTETV-LVCgnFKGMEIK-PGSMGKPSPGYDVKIIDENGNILPPGKEGEIAIkvkptRPLFLFTCYTDDPEKTKATVR 367
Cdd:cd17636 143 YGQTEVMgLAT--FAALGGGaIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVA-----RGPTVMAGYWNRPEVNARRTR 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 368 GDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNyVSH 447
Cdd:cd17636 216 GGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPG-ASV 294
|
170 180 190
....*....|....*....|....*....|....*...
gi 2024458455 448 DPEkmmkDLQDHVKKATAPYKYPRKMEFVRELPKTISG 485
Cdd:cd17636 295 TEA----ELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
210-492 |
2.29e-36 |
|
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: 139.97 E-value: 2.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 210 SDHRCVTTKSQHPVAIYFTSGTTGAPK--MTEH-------------------------SHCSYGIGLT------VSGSC- 255
Cdd:cd05930 83 SGAKLVLTDPDDLAYVIYTSGSTGKPKgvMVEHrglvnlllwmqeaypltpgdrvlqfTSFSFDVSVWeifgalLAGATl 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 256 -------------------------------------------TFNSLRHCVSAGEPINPEVMAKW-KAWTGLDIHECYG 291
Cdd:cd05930 163 vvlpeevrkdpealadllaeegitvlhltpsllrlllqelelaALPSLRLVLVGGEALPPDLVRRWrELLPGARLVNLYG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 292 QTETVLVCGNF--KGMEIKPGSM--GKPSPGYDVKIIDENGNILPPGKEGEIAIkvkptrplflftC-------YTDDPE 360
Cdd:cd05930 243 PTEATVDATYYrvPPDDEEDGRVpiGRPIPNTRVYVLDENLRPVPPGVPGELYI------------GgaglargYLNRPE 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 361 KTKATVRGD-------FYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEV 433
Cdd:cd05930 311 LTAERFVPNpfgpgerMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKR 390
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024458455 434 VKAFVVLtpnyvSHDPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNEL 492
Cdd:cd05930 391 LVAYVVP-----DEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
80-494 |
6.53e-36 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 140.19 E-value: 6.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 80 DGDGEEVKWSFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKS 159
Cdd:PRK13295 48 LGTGAPRRFTYRELAALVDRVAVGLA-RLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 160 KAKGVIT-----NDSVASTVESVEADCQSLKfKLLVSEGhrEGWLSFKDLLKT-----APSDHRCVTTKSQHP--VA-IY 226
Cdd:PRK13295 127 ESKVLVVpktfrGFDHAAMARRLRPELPALR-HVVVVGG--DGADSFEALLITpaweqEPDAPAILARLRPGPddVTqLI 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 227 FTSGTTGAPKMTEHSHCS---------------------------------YGIGLTVS--------------------- 252
Cdd:PRK13295 204 YTSGTTGEPKGVMHTANTlmanivpyaerlglgaddvilmaspmahqtgfmYGLMMPVMlgatavlqdiwdparaaelir 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 253 --------GSCTF---------------NSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTETVLVCGNFKG--MEI 307
Cdd:PRK13295 284 tegvtftmASTPFltdltravkesgrpvSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVTLTKLDdpDER 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 308 KPGSMGKPSPGYDVKIIDENGNILPPGKEGEIAIkvkptRPLFLFTCYTDDPEKTKATVRGdFYVTGDRGLMDEDGYFWF 387
Cdd:PRK13295 364 ASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQV-----RGCSNFGGYLKRPQLNGTDADG-WFDTGDLARIDADGYIRI 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 388 VGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYvSHDPEKMMKDLQDHvkKATAPY 467
Cdd:PRK13295 438 SGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQ-SLDFEEMVEFLKAQ--KVAKQY 514
|
490 500
....*....|....*....|....*..
gi 2024458455 468 kYPRKMEFVRELPKTISGKIRRNELRQ 494
Cdd:PRK13295 515 -IPERLVVRDALPRTPSGKIQKFRLRE 540
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
73-495 |
2.41e-35 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 139.08 E-value: 2.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 73 NPALWWVDgDGEEVKWSFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLNVACMRTG--TVPIPGTqqLTAK 150
Cdd:COG1022 27 RVALREKE-DGIWQSLTWAEFAERVRALAAGLL-ALGVKPGDRVAILSDNRPEWVIADLAILAAGavTVPIYPT--SSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 151 DILYRLQKSKAKGVIT-NDSVASTVESVEADCQSLKFKLLVSEG---HREGWLSFKDLLKTAPS-------DHRCVTTKS 219
Cdd:COG1022 103 EVAYILNDSGAKVLFVeDQEQLDKLLEVRDELPSLRHIVVLDPRglrDDPRLLSLDELLALGREvadpaelEARRAAVKP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 220 QHPVAIYFTSGTTGAPKMTEHSH----------------------CSY-----------GIGLTVSGSCT---------- 256
Cdd:COG1022 183 DDLATIIYTSGTTGRPKGVMLTHrnllsnarallerlplgpgdrtLSFlplahvfertvSYYALAAGATVafaespdtla 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 257 ---------------------------------------FNS-------------------------------------- 259
Cdd:COG1022 263 edlrevkptfmlavprvwekvyagiqakaeeagglkrklFRWalavgrryararlagkspslllrlkhaladklvfsklr 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 260 ------LRHCVSAGEPINPEVmAKWKAWTGLDIHECYGQTET-VLVCGNFKGmEIKPGSMGKPSPGYDVKIidengnilp 332
Cdd:COG1022 343 ealggrLRFAVSGGAALGPEL-ARFFRALGIPVLEGYGLTETsPVITVNRPG-DNRIGTVGPPLPGVEVKI--------- 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 333 pGKEGEIAIK---VkptrplflFTCYTDDPEKTKATVRGD--FYvTGDRGLMDEDGYFWFVGRADDVI-NSAGYRIGPFE 406
Cdd:COG1022 412 -AEDGEILVRgpnV--------MKGYYKNPEATAEAFDADgwLH-TGDIGELDEDGFLRITGRKKDLIvTSGGKNVAPQP 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 407 VESALIEHPAVLESAVVsspdpirGE----VVkAFVVLTPNYVSH----------DPEKMMKD------LQDHVKKAT-- 464
Cdd:COG1022 482 IENALKASPLIEQAVVV-------GDgrpfLA-ALIVPDFEALGEwaeenglpytSYAELAQDpevralIQEEVDRANag 553
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 2024458455 465 -APYKYPRKMEFvreLPK---------TISGKIRRNELRQK 495
Cdd:COG1022 554 lSRAEQIKRFRL---LPKeftiengelTPTLKLKRKVILEK 591
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
257-493 |
4.85e-34 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 134.95 E-value: 4.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 257 FNSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTETV-LVCGNFKGMEIKPGSMGKPSPGYDVKIIDENGNILPPGK 335
Cdd:PRK12492 332 FSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGE 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 336 EGEIAIKvKPTrplfLFTCYTDDPEKTKATVRGD-FYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEH 414
Cdd:PRK12492 412 RGELCIK-GPQ----VMKGYWQQPEATAEALDAEgWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAH 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024458455 415 PAVLESAVVSSPDPIRGEVVKAFVvltpnyVSHDPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELR 493
Cdd:PRK12492 487 PKVANCAAIGVPDERSGEAVKLFV------VARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
80-494 |
5.05e-34 |
|
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: 134.30 E-value: 5.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 80 DGDGEEVKWSFEELGVLSRKAANVLSGAcSLQCGDRVLLLLpripewW--------LLNVACMrtGTVPIPGTQQLTAKD 151
Cdd:cd12119 18 THEGEVHRYTYAEVAERARRLANALRRL-GVKPGDRVATLA------WnthrhlelYYAVPGM--GAVLHTINPRLFPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 152 ILYRLQKSKAKGVITNDSVASTVESVEADCQSLK-FKLLVSEGHR-----EGWLSFKDLLKTAPSDHRCVTTKSQHPVAI 225
Cdd:cd12119 89 IAYIINHAEDRVVFVDRDFLPLLEAIAPRLPTVEhVVVMTDDAAMpepagVGVLAYEELLAAESPEYDWPDFDENTAAAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 226 YFTSGTTGAPKMTEHSHCSY-----------GIGLTVS------------------------GS---------------- 254
Cdd:cd12119 169 CYTSGTTGNPKGVVYSHRSLvlhamaalltdGLGLSESdvvlpvvpmfhvnawglpyaaamvGAklvlpgpyldpaslae 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 255 ------CTFN----------------------SLRHCVSAGEPINPEVMAKWKAwTGLDIHECYGQTET--VLVCGNFKG 304
Cdd:cd12119 249 lieregVTFAagvptvwqglldhleangrdlsSLRRVVIGGSAVPRSLIEAFEE-RGVRVIHAWGMTETspLGTVARPPS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 305 MEIKPG---------SMGKPSPGYDVKIIDENGNILP-PGKE-GEIAIkvkptRPLFLFTCYTDDPEKTKATVRGDFYVT 373
Cdd:cd12119 328 EHSNLSedeqlalraKQGRPVPGVELRIVDDDGRELPwDGKAvGELQV-----RGPWVTKSYYKNDEESEALTEDGWLRT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 374 GDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNyvsHDPEKmm 453
Cdd:cd12119 403 GDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEG---ATVTA-- 477
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2024458455 454 KDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELRQ 494
Cdd:cd12119 478 EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
97-495 |
2.88e-33 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 132.80 E-value: 2.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 97 SRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVITNDSVASTVES 176
Cdd:PLN02330 65 TRRFAKALR-SLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 177 VEADCqslkfkLLVSEGHREGWLSFKDLLKTApsdHRCVTTKSQHPV------AIYFTSGTTGAPK--MTEHSH-----C 243
Cdd:PLN02330 144 LGLPV------IVLGEEKIEGAVNWKELLEAA---DRAGDTSDNEEIlqtdlcALPFSSGTTGISKgvMLTHRNlvanlC 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 244 S--YGIG------------------LTVSGSC------------------------------TFN--------------- 258
Cdd:PLN02330 215 SslFSVGpemigqvvtlglipffhiYGITGICcatlrnkgkvvvmsrfelrtflnalitqevSFApivppiilnlvknpi 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 259 ---------SLRHCVSAGEPINPEVMAKWKA-WTGLDIHECYGQTE---TVLVCGN-FKGMEI-KPGSMGKPSPGYDVKI 323
Cdd:PLN02330 295 veefdlsklKLQAIMTAAAPLAPELLTAFEAkFPGVQVQEAYGLTEhscITLTHGDpEKGHGIaKKNSVGFILPNLEVKF 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 324 ID-ENGNILPPGKEGEIAIkvkptRPLFLFTCYTDDPEKTKATVRGDFYV-TGDRGLMDEDGYFWFVGRADDVINSAGYR 401
Cdd:PLN02330 375 IDpDTGRSLPKNTPGELCV-----RSQCVMQGYYNNKEETDRTIDEDGWLhTGDIGYIDDDGDIFIVDRIKELIKYKGFQ 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 402 IGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYVSHDpekmmKDLQDHVKKATAPYKYPRKMEFVRELPK 481
Cdd:PLN02330 450 VAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESE-----EDILNFVAANVAHYKKVRVVQFVDSIPK 524
|
490
....*....|....
gi 2024458455 482 TISGKIRRNELRQK 495
Cdd:PLN02330 525 SLSGKIMRRLLKEK 538
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
110-492 |
3.25e-33 |
|
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: 131.86 E-value: 3.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 110 LQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVITNDSVASTVESVEADCQSLKFKLL 189
Cdd:cd05923 50 LRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAVDAQVMDAIFQSGVRVLALSDL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 190 VSEGHREgwlSFKDLLKTAPSdhrcvttKSQHPVAIYFTSGTTGAPK---------------MTEHSHCSYG-----IGL 249
Cdd:cd05923 130 VGLGEPE---SAGPLIEDPPR-------EPEQPAFVFYTSGTTGLPKgavipqraaesrvlfMSTQAGLRHGrhnvvLGL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 250 -----------TVSGSCTFN------------------------------------------------SLRHCVSAGEPI 270
Cdd:cd05923 200 mplyhvigffaVLVAALALDgtyvvveefdpadalklieqervtslfatpthldalaaaaefaglklsSLRHVTFAGATM 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 271 NPEVMAKWKAWTGLDIHECYGQTETVlvcgNFKGME-IKPGSMGKPSPGYDVKIIDENGN---ILPPGKEGEIAIKVKPT 346
Cdd:cd05923 280 PDAVLERVNQHLPGEKVNIYGTTEAM----NSLYMRdARTGTEMRPGFFSEVRIVRIGGSpdeALANGEEGELIVAAAAD 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 347 RPlflFTCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSP 426
Cdd:cd05923 356 AA---FTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVA 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024458455 427 DPIRGEVVKAFVVLTPNYVShdpekmmKDLQDHVKKAT--APYKYPRKMEFVRELPKTISGKIRRNEL 492
Cdd:cd05923 433 DERWGQSVTACVVPREGTLS-------ADELDQFCRASelADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
258-493 |
4.64e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 131.55 E-value: 4.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 258 NSLRHCVSAGEPiNPE--VMAKWKAWTGLDIHECYGQTETvlvCGNFKGMEI-----KPGSMGKPSPGYDVKIIDENGNI 330
Cdd:PRK06145 264 DSLAWCIGGGEK-TPEsrIRDFTRVFTRARYIDAYGLTET---CSGDTLMEAgreieKIGSTGRALAHVEIRIADGAGRW 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 331 LPPGKEGEIAIK-VKPTRPlflftcYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVES 409
Cdd:PRK06145 340 LPPNMKGEICMRgPKVTKG------YWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVER 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 410 ALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYVSHDPEkmmkdLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRR 489
Cdd:PRK06145 414 VIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEA-----LDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLK 488
|
....
gi 2024458455 490 NELR 493
Cdd:PRK06145 489 RVLR 492
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
74-492 |
5.77e-33 |
|
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: 130.44 E-value: 5.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 74 PALWWvdgdgEEVKWSFEELGVLSRKAANVLSGACsLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPgtqqltakdil 153
Cdd:cd05945 8 PAVVE-----GGRTLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVP----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 154 yrlqkskakgvITNDSVASTVESVEADCQSlkfkllvseghregwlsfkDLLKTAPSDhrcvttksqhPVAIYFTSGTTG 233
Cdd:cd05945 71 -----------LDASSPAERIREILDAAKP-------------------ALLIADGDD----------NAYIIFTSGSTG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 234 APKMTEHSH----------CSYGI-----------------------------------------------------GLT 250
Cdd:cd05945 111 RPKGVQISHdnlvsftnwmLSDFPlgpgdvflnqapfsfdlsvmdlypalasgatlvpvprdatadpkqlfrflaehGIT 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 251 V-----------SGSCTFN-----SLRHCVSAGEPINPEVMAKWKAWT-GLDIHECYGQTETVLVCgnfKGMEIKPGSM- 312
Cdd:cd05945 191 VwvstpsfaamcLLSPTFTpeslpSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATVAV---TYIEVTPEVLd 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 313 -------GKPSPGYDVKIIDENGNILPPGKEGEIAIkVKPTrplfLFTCYTDDPEKTKATVRGDF----YVTGDRGLMDE 381
Cdd:cd05945 268 gydrlpiGYAKPGAKLVILDEDGRPVPPGEKGELVI-SGPS----VSKGYLNNPEKTAAAFFPDEgqraYRTGDLVRLEA 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 382 DGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPnyvsHDPEKMMKDLQDHVK 461
Cdd:cd05945 343 DGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKP----GAEAGLTKAIKAELA 418
|
490 500 510
....*....|....*....|....*....|.
gi 2024458455 462 KATAPYKYPRKMEFVRELPKTISGKIRRNEL 492
Cdd:cd05945 419 ERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
258-494 |
1.17e-32 |
|
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: 130.72 E-value: 1.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 258 NSLRHCVSAGEPINPEVMAKWKAWTGLD-IHECYGQTETVLVCGNFKGMEIKPGSMGKPSPGYDVKIID-ENGNILPPGK 335
Cdd:cd17642 301 SNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 336 EGEIAIKVKptrplFLFTCYTDDPEKTKATVRGDFYV-TGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEH 414
Cdd:cd17642 381 RGELCVKGP-----MIMKGYVNNPEATKALIDKDGWLhSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQH 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 415 PAVLESAVVSSPDPIRGEVVKAFVVLTPNyvshdpeKMM--KDLQDHVKKATAPYKYPR-KMEFVRELPKTISGKIRRNE 491
Cdd:cd17642 456 PKIFDAGVAGIPDEDAGELPAAVVVLEAG-------KTMteKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRK 528
|
...
gi 2024458455 492 LRQ 494
Cdd:cd17642 529 IRE 531
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
52-494 |
1.38e-32 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 131.56 E-value: 1.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 52 NFASDVLDRwaKVEKeGKKTKNPALWWVDGDGEEVKWSFEELgvLSR--KAANVLSgACSLQCGDRVLLLLPRIPEWWLL 129
Cdd:PLN02654 88 NICYNCLDR--NVEA-GNGDKIAIYWEGNEPGFDASLTYSEL--LDRvcQLANYLK-DVGVKKGDAVVIYLPMLMELPIA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 130 NVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVITNDSV--------------ASTVESVEAD-----CQSLKFKLLV 190
Cdd:PLN02654 162 MLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITCNAVkrgpktinlkdivdAALDESAKNGvsvgiCLTYENQLAM 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 191 S------EGHREGWlsFKDLLKTAPSDHRCVTTKSQHPVAIYFTSGTTGAPK---------------------------- 236
Cdd:PLN02654 242 KredtkwQEGRDVW--WQDVVPNYPTKCEVEWVDAEDPLFLLYTSGSTGKPKgvlhttggymvytattfkyafdykptdv 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 237 ---------MTEHSHCSYGI---GLTV-----------SGSC---------------------------------TFNSL 260
Cdd:PLN02654 320 ywctadcgwITGHSYVTYGPmlnGATVlvfegapnypdSGRCwdivdkykvtifytaptlvrslmrdgdeyvtrhSRKSL 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 261 RHCVSAGEPINPevmAKWKaW-------TGLDIHECYGQTETvlvcGNFKGMEI------KPGSMGKPSPGYDVKIIDEN 327
Cdd:PLN02654 400 RVLGSVGEPINP---SAWR-WffnvvgdSRCPISDTWWQTET----GGFMITPLpgawpqKPGSATFPFFGVQPVIVDEK 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 328 GNILppgkEGEIA--IKVKPTRPLFLFTCYTDDP--EKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIG 403
Cdd:PLN02654 472 GKEI----EGECSgyLCVKKSWPGAFRTLYGDHEryETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIG 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 404 PFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNyVSHDpEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTI 483
Cdd:PLN02654 548 TAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEG-VPYS-EELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTR 625
|
570
....*....|.
gi 2024458455 484 SGKIRRNELRQ 494
Cdd:PLN02654 626 SGKIMRRILRK 636
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
110-493 |
1.59e-32 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 131.69 E-value: 1.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 110 LQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVITNDSV------ASTVESVEadcqs 183
Cdd:PRK06060 52 LSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALrdrfqpSRVAEAAE----- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 184 lkfklLVSEGHREGwlsfkdllktaPSDHRCVTTKSqHPVAIYfTSGTTGAPKMTEHSHC-------------------- 243
Cdd:PRK06060 127 -----LMSEAARVA-----------PGGYEPMGGDA-LAYATY-TSGTTGPPKAAIHRHAdpltfvdamcrkalrltped 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 244 ----------SYGIGLTV--------------------------------------------SGSCT---FNSLRHCVSA 266
Cdd:PRK06060 189 tglcsarmyfAYGLGNSVwfplatggsavinsapvtpeaaailsarfgpsvlygvpnffarvIDSCSpdsFRSLRCVVSA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 267 GEPINPEVMAKW-KAWTGLDIHECYGQTETVLVCGNFKGMEIKPGSMGKPSPGYDVKIIDENGNILPPGKEGEIAIKvKP 345
Cdd:PRK06060 269 GEALELGLAERLmEFFGGIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVR-GP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 346 TrplfLFTCYTDDPEKTkaTVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSS 425
Cdd:PRK06060 348 A----IAKGYWNRPDSP--VANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAV 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024458455 426 PDPIRGEVVKAFVVltPNYVSHDPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELR 493
Cdd:PRK06060 422 RESTGASTLQAFLV--ATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
221-489 |
9.82e-32 |
|
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: 124.05 E-value: 9.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 221 HPVAIYFTSGTTGAPK------------MTE--------------------HSHCSYGI------GLTVSGSCTFNSLRH 262
Cdd:cd17633 1 NPFYIGFTSGTTGLPKayyrserswiesFVCnedlfnisgedailapgplsHSLFLYGAisalylGGTFIGQRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 263 C---------------------VSAGEPINPEVM-----AKW---------KAWTGLDIHECYGQTETVLVCGNFKGMEI 307
Cdd:cd17633 81 IrkinqynatviylvptmlqalARTLEPESKIKSifssgQKLfestkkklkNIFPKANLIEFYGTSELSFITYNFNQESR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 308 KPGSMGKPSPGYDVKIIDENGnilppGKEGEIAIKVKptrplFLFTCYTDDPEKTKatvrGDFYVTGDRGLMDEDGYFWF 387
Cdd:cd17633 161 PPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSE-----MVFSGYVRGGFSNP----DGWMSVGDIGYVDEEGYLYL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 388 VGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAfvVLTPNYVSHdpekmmKDLQDHVKKATAPY 467
Cdd:cd17633 227 VGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVA--LYSGDKLTY------KQLKRFLKQKLSRY 298
|
330 340
....*....|....*....|..
gi 2024458455 468 KYPRKMEFVRELPKTISGKIRR 489
Cdd:cd17633 299 EIPKKIIFVDSLPYTSSGKIAR 320
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
244-489 |
5.80e-31 |
|
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: 122.75 E-value: 5.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 244 SYGIGLTVSGSCTFNSLRHCVSAGE-PINPEVmaKWKAWTGL-DIHECYGQTETVLV-CGNFKGMEIKPGSMGKPSPGYD 320
Cdd:cd17635 103 SKLVSELKSANATVPSLRLIGYGGSrAIAADV--RFIEATGLtNTAQVYGLSETGTAlCLPTDDDSIEINAVGRPYPGVD 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 321 VKIIDENGNILPPGKEGEIAIKVkptrPLFLfTCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGY 400
Cdd:cd17635 181 VYLAATDGIAGPSASFGTIWIKS----PANM-LGYWNNPERTAEVLIDGWVNTGDLGERREDGFLFITGRSSESINCGGV 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 401 RIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTpnyvSHDPEKMMKDLQDHVKKATAPYKYPRKMEFVRELP 480
Cdd:cd17635 256 KIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAS----AELDENAIRALKHTIRRELEPYARPSTIVIVTDIP 331
|
....*....
gi 2024458455 481 KTISGKIRR 489
Cdd:cd17635 332 RTQSGKVKR 340
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
259-495 |
5.71e-30 |
|
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: 119.36 E-value: 5.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 259 SLRHCVSAGEPINPEVMAKWKAwTGLDIHECYGQTETV-LVCGNFKGmEIKPGSMGKPSPGYDVKIIDEngnilppgkeG 337
Cdd:cd17630 112 SLRAVLLGGAPIPPELLERAAD-RGIPLYTTYGMTETAsQVATKRPD-GFGRGGVGVLLPGRELRIVED----------G 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 338 EIAIKvkptrPLFLFTCYTDDPEKTKATVRGDFYvTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAV 417
Cdd:cd17630 180 EIWVG-----GASLAMGYLRGQLVPEFNEDGWFT-TKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAV 253
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024458455 418 LESAVVSSPDPIRGEVVKAFVVLTPnyvSHDPEkmmkDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELRQK 495
Cdd:cd17630 254 RDAFVVGVPDEELGQRPVAVIVGRG---PADPA----ELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAW 324
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
51-486 |
8.40e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 122.30 E-value: 8.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 51 FNFAsDVLDRWAKVEKEgkktkNPALwwVDGDgeeVKWSFEELGVLSRKAANVLSGAcSLQCGDRVLLLLPRIPEWWLLN 130
Cdd:PRK07798 3 WNIA-DLFEAVADAVPD-----RVAL--VCGD---RRLTYAELEERANRLAHYLIAQ-GLGPGDHVGIYARNRIEYVEAM 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 131 VACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVITNDSVASTVESVEADCQSLKFKLLVSEG----HREGWLSFKDLLK 206
Cdd:PRK07798 71 LGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLPKLRTLVVVEDGsgndLLPGAVDYEDALA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 207 TAPSDhRCVTTKSQHPVAIYFTSGTTGAPK-------------------------MTEHSH---CSYGIGLTV------- 251
Cdd:PRK07798 151 AGSPE-RDFGERSPDDLYLLYTGGTTGMPKgvmwrqedifrvllggrdfatgepiEDEEELakrAAAGPGMRRfpapplm 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 252 -------------SGSCT-------FN----------------------------------------SLRHCVSAGEPIN 271
Cdd:PRK07798 230 hgagqwaafaalfSGQTVvllpdvrFDadevwrtierekvnvitivgdamarplldaleargpydlsSLFAIASGGALFS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 272 PEVMAKWKAW-TGLDIHECYGQTETvlvcgNFKGMEIK---PGSMGKPS--PGYDVKIIDENGNILPPG--KEGEIAIKv 343
Cdd:PRK07798 310 PSVKEALLELlPNVVLTDSIGSSET-----GFGGSGTVakgAVHTGGPRftIGPRTVVLDEDGNPVEPGsgEIGWIARR- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 344 kPTRPLflftCYTDDPEKTKAT---VRGDFY-VTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLE 419
Cdd:PRK07798 384 -GHIPL----GYYKDPEKTAETfptIDGVRYaIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVAD 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024458455 420 SAVVSSPDPIRGEVVKAFVVLTPNyVSHDPEkmmkDLQDHVKKATAPYKYPRKMEFVRELPKTISGK 486
Cdd:PRK07798 459 ALVVGVPDERWGQEVVAVVQLREG-ARPDLA----ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
251-493 |
9.66e-30 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 122.64 E-value: 9.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 251 VSGSCtFNSLRHCVSAGEPINPEVMAKW-KAWTGLDIHECYGQTETVLVcgNFKGMEIKP----GSMGKPSPGYDVKIID 325
Cdd:PLN02574 313 VCGEV-LKSLKQVSCGAAPLSGKFIQDFvQTLPHVDFIQGYGMTESTAV--GTRGFNTEKlskySSVGLLAPNMQAKVVD 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 326 -ENGNILPPGKEGEIAIKvKPTrplfLFTCYTDDPEKTKATVRGDFYV-TGDRGLMDEDGYFWFVGRADDVINSAGYRIG 403
Cdd:PLN02574 390 wSTGCLLPPGNCGELWIQ-GPG----VMKGYLNNPKATQSTIDKDGWLrTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIA 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 404 PFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVltpnyvsHDPEKMM--KDLQDHVKKATAPYKYPRKMEFVRELPK 481
Cdd:PLN02574 465 PADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVV-------RRQGSTLsqEAVINYVAKQVAPYKKVRKVVFVQSIPK 537
|
250
....*....|..
gi 2024458455 482 TISGKIRRNELR 493
Cdd:PLN02574 538 SPAGKILRRELK 549
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
74-492 |
1.44e-29 |
|
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: 121.23 E-value: 1.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 74 PALWWvdgdgEEVKWSFEELGVLSRKAANVLSGAcSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDIL 153
Cdd:cd17646 15 PAVVD-----EGRTLTYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 154 YRLQKSKAKGVITN-DSVASTVESVEADcqslkfkLLVSEGhregwlsfkdlLKTAPSDHRCVTTKSQHPVAIYFTSGTT 232
Cdd:cd17646 89 YMLADAGPAVVLTTaDLAARLPAGGDVA-------LLGDEA-----------LAAPPATPPLVPPRPDNLAYVIYTSGST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 233 GAPK--MTEHS---------HCSYGIGLT----------------------VSGSC------------------------ 255
Cdd:cd17646 151 GRPKgvMVTHAgivnrllwmQDEYPLGPGdrvlqktplsfdvsvwelfwplVAGARlvvarpgghrdpaylaalirehgv 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 256 TF--------------------NSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTET---VLVCGNFKGMEIKPGSM 312
Cdd:cd17646 231 TTchfvpsmlrvflaepaagscASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAaidVTHWPVRGPAETPSVPI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 313 GKPSPGYDVKIIDENGNILPPGKEGEIAIK-VKPTRPlflftcYTDDPEKTKATVRGD-------FYVTGDRGLMDEDGY 384
Cdd:cd17646 311 GRPVPNTRLYVLDDALRPVPVGVPGELYLGgVQLARG------YLGRPALTAERFVPDpfgpgsrMYRTGDLARWRPDGA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 385 FWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYVSHDPEKmmkdLQDHVKKAT 464
Cdd:cd17646 385 LEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPDTAA----LRAHLAERL 460
|
490 500
....*....|....*....|....*...
gi 2024458455 465 APYKYPRKMEFVRELPKTISGKIRRNEL 492
Cdd:cd17646 461 PEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
83-492 |
2.41e-29 |
|
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: 120.01 E-value: 2.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 83 GEEVKWSFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKA- 161
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLI-ALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 162 -----------------------KGV-ITNDSVASTVESV------EADCQSLKFKLLvseGH---REGWLSFkdllkta 208
Cdd:cd05907 80 alfvedpddlatiiytsgttgrpKGVmLSHRNILSNALALaerlpaTEGDRHLSFLPL---AHvfeRRAGLYV------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 209 psdhrCVTtksqHPVAIYFTSGTT---------------GAPKMTEhSHCSYGIGLTVSG-------SCTFNSLRHCVSA 266
Cdd:cd05907 150 -----PLL----AGARIYFASSAEtllddlsevrptvflAVPRVWE-KVYAAIKVKAVPGlkrklfdLAVGGRLRFAASG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 267 GEPINPEVMAKWKAwTGLDIHECYGQTETV-LVCGNFKGmEIKPGSMGKPSPGYDVKIidengnilppGKEGEIAIkvkp 345
Cdd:cd05907 220 GAPLPAELLHFFRA-LGIPVYEGYGLTETSaVVTLNPPG-DNRIGTVGKPLPGVEVRI----------ADDGEILV---- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 346 tRPLFLFTCYTDDPEKTKATVRGD-FYVTGDRGLMDEDGYFWFVGRADDVI-NSAGYRIGPFEVESALIEHPAVLESAVV 423
Cdd:cd05907 284 -RGPNVMLGYYKNPEATAEALDADgWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 424 SSPDPirgeVVKAFVVLTPNYVSH----------------DPEKMMKDLQDHVKKATA---PYKYPRKMEFVrELPKTI- 483
Cdd:cd05907 363 GDGRP----FLVALIVPDPEALEAwaeehgiaytdvaelaANPAVRAEIEAAVEAANArlsRYEQIKKFLLL-PEPFTIe 437
|
490
....*....|....*
gi 2024458455 484 ------SGKIRRNEL 492
Cdd:cd05907 438 ngeltpTLKLKRPVI 452
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
257-492 |
3.81e-29 |
|
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: 120.00 E-value: 3.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 257 FNSLRHCVSAGEPINPEVMAKW-KAWTGLDIHECYGQTE--TVLVCGNFKGMEIKPGS--MGKPSPGYDVKIIDENGNIL 331
Cdd:cd12117 248 FAGLRELLTGGEVVSPPHVRRVlAACPGLRLVNGYGPTEntTFTTSHVVTELDEVAGSipIGRPIANTRVYVLDEDGRPV 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 332 PPGKEGEIaikvkptrplflftC---------YTDDPEKTKA-------TVRGDFYVTGDRGLMDEDGYFWFVGRADDVI 395
Cdd:cd12117 328 PPGVPGEL--------------YvggdglalgYLNRPALTAErfvadpfGPGERLYRTGDLARWLPDGRLEFLGRIDDQV 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 396 NSAGYRIGPFEVESALIEHPAVLESAV-VSSPDPIRGEVVkAFVVLTPNyVSHDpekmmkDLQDHVKKATAPYKYPRKME 474
Cdd:cd12117 394 KIRGFRIELGEIEAALRAHPGVREAVVvVREDAGGDKRLV-AYVVAEGA-LDAA------ELRAFLRERLPAYMVPAAFV 465
|
250
....*....|....*...
gi 2024458455 475 FVRELPKTISGKIRRNEL 492
Cdd:cd12117 466 VLDELPLTANGKVDRRAL 483
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
259-489 |
3.76e-28 |
|
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: 114.52 E-value: 3.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 259 SLRHCVSAGEPINPEVMAKWKAWTGLD-IHECYGQTETVLV--CGNFKGMEIKPGSMGKPSPGYDVKIIDEngnilppgk 335
Cdd:cd17638 116 SLRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVAtmCRPGDDAETVATTCGRACPGFEVRIADD--------- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 336 eGEIAIkvkptRPLFLFTCYTDDPEKTKATVRGDFYV-TGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEH 414
Cdd:cd17638 187 -GEVLV-----RGYNVMQGYLDDPEATAEAIDADGWLhTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEH 260
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024458455 415 PAVLESAVVSSPDPIRGEVVKAFVVLTPNyVSHDPEKMMKDLQDHVkkatAPYKYPRKMEFVRELPKTISGKIRR 489
Cdd:cd17638 261 PGVAQVAVIGVPDERMGEVGKAFVVARPG-VTLTEEDVIAWCRERL----ANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
313-494 |
4.24e-28 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 117.40 E-value: 4.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 313 GKP-SPGYDVKIIDENGNILPPGKEGEIAikvkpTRPLFLFTCYTDDPEKTKATVRGD-FYVTGDRGLMDEDGYFWFVGR 390
Cdd:PRK10946 356 GRPmSPDDEVWVADADGNPLPQGEVGRLM-----TRGPYTFRGYYKSPQHNASAFDANgFYCSGDLVSIDPDGYITVVGR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 391 ADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTpnyvshDPEKMMkDLQDHVK-KATAPYKY 469
Cdd:PRK10946 431 EKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVK------EPLKAV-QLRRFLReQGIAEFKL 503
|
170 180
....*....|....*....|....*
gi 2024458455 470 PRKMEFVRELPKTISGKIRRNELRQ 494
Cdd:PRK10946 504 PDRVECVDSLPLTAVGKVDKKQLRQ 528
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
83-493 |
7.98e-28 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 116.29 E-value: 7.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 83 GEEVKWSFEELGVLSRKAANVLSGAcSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAK 162
Cdd:cd17651 16 AEGRRLTYAELDRRANRLAHRLRAR-GVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 163 GVITNDSVASTVESVEADcqslkfkllvseghreGWLSFKDLLKTAPSDHRCVTTKSQHPVAIYFTSGTTGAPK--MTEH 240
Cdd:cd17651 95 LVLTHPALAGELAVELVA----------------VTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKgvVMPH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 241 S--------HCSY-------------GIGLTVS----------------------------------------------- 252
Cdd:cd17651 159 RslanlvawQARAsslgpgartlqfaGLGFDVSvqeifstlcagatlvlppeevrtdppalaawldeqrisrvflptval 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 253 ---------GSCTFNSLRHCVSAGEP-INPEVMAKWKAW-TGLDIHECYGQTE----TVLVCGNFKGMEIKPGSMGKPSP 317
Cdd:cd17651 239 ralaehgrpLGVRLAALRYLLTGGEQlVLTEDLREFCAGlPGLRLHNHYGPTEthvvTALSLPGDPAAWPAPPPIGRPID 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 318 GYDVKIIDENGNILPPGKEGEIAIKVKPtrplfLFTCYTDDPEKTKAT-VRGDF------YVTGDRGLMDEDGYFWFVGR 390
Cdd:cd17651 319 NTRVYVLDAALRPVPPGVPGELYIGGAG-----LARGYLNRPELTAERfVPDPFvpgarmYRTGDLARWLPDGELEFLGR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 391 ADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNyVSHDPEkmmkDLQDHVKKATAPYKYP 470
Cdd:cd17651 394 ADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPE-APVDAA----ELRAALATHLPEYMVP 468
|
490 500
....*....|....*....|...
gi 2024458455 471 RKMEFVRELPKTISGKIRRNELR 493
Cdd:cd17651 469 SAFVLLDALPLTPNGKLDRRALP 491
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
89-423 |
9.53e-28 |
|
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: 114.67 E-value: 9.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 89 SFEELGVLSRKAANVLSGACSLQCGDRVLLLLPRIPEW--WLLnvACMRTGT--VPIpgtqqltakDILY---RLQ---- 157
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELvvAIL--AVLKAGAayVPL---------DPAYpaeRLAfile 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 158 KSKAKGVITNDSVASTVESVeadcqslkfkllVSEGHREGWLSFKDLLKTAPSDHRCVTTKSQHPVAIYFTSGTTGAPK- 236
Cdd:TIGR01733 70 DAGARLLLTDSALASRLAGL------------VLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKg 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 237 -MTEH-----------------------SHCSY---------------GIGLTV------------------SGSCTF-- 257
Cdd:TIGR01733 138 vVVTHrslvnllawlarrygldpddrvlQFASLsfdasveeifgallaGATLVVppedeerddaallaaliaEHPVTVln 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 258 -----------------NSLRHCVSAGEPINPEVMAKWKA-WTGLDIHECYGQTETVLVCGNF---KGMEIKPGSM--GK 314
Cdd:TIGR01733 218 ltpsllallaaalppalASLRLVILGGEALTPALVDRWRArGPGARLINLYGPTETTVWSTATlvdPDDAPRESPVpiGR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 315 PSPGYDVKIIDENGNILPPGKEGEIAIkvkpTRPLfLFTCYTDDPEKTKA---------TVRGDFYVTGDRGLMDEDGYF 385
Cdd:TIGR01733 298 PLANTRLYVLDDDLRPVPVGVVGELYI----GGPG-VARGYLNRPELTAErfvpdpfagGDGARLYRTGDLVRYLPDGNL 372
|
410 420 430
....*....|....*....|....*....|....*...
gi 2024458455 386 WFVGRADDVINSAGYRIGPFEVESALIEHPAVlESAVV 423
Cdd:TIGR01733 373 EFLGRIDDQVKIRGYRIELGEIEAALLRHPGV-REAVV 409
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
84-495 |
1.28e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 116.20 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 84 EEVKWSFEELGVLSRKAANVLSGAcSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKG 163
Cdd:PRK08162 40 GDRRRTWAETYARCRRLASALARR-GIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 164 VITNDSVASTVESVEADCQSLKfkLLV--------SEGHREGWLSFKDLLK--------TAPSDHrcvttksQHPVAIYF 227
Cdd:PRK08162 119 LIVDTEFAEVAREALALLPGPK--PLVidvddpeyPGGRFIGALDYEAFLAsgdpdfawTLPADE-------WDAIALNY 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 228 TSGTTGAPK---------------------MTEHS---------HCS-YGIGLTVSGS-----CT--------FNSLR-H 262
Cdd:PRK08162 190 TSGTTGNPKgvvyhhrgaylnalsnilawgMPKHPvylwtlpmfHCNgWCFPWTVAARagtnvCLrkvdpkliFDLIReH 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 263 CVS-------------------------------AGEPINPEVMAKWKAwTGLDIHECYGQTET---VLVC--------- 299
Cdd:PRK08162 270 GVThycgapivlsalinapaewragidhpvhamvAGAAPPAAVIAKMEE-IGFDLTHVYGLTETygpATVCawqpewdal 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 300 -----GNFKGME------------IKPGSMgKPSPgYDVKIIDE---NGNILPPGkegeiaikvkptrplflftcYTDDP 359
Cdd:PRK08162 349 plderAQLKARQgvryplqegvtvLDPDTM-QPVP-ADGETIGEimfRGNIVMKG--------------------YLKNP 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 360 EKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVV 439
Cdd:PRK08162 407 KATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVE 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024458455 440 LTPNyVSHDPEkmmkDLQDHVKKATAPYKYPRKMEFVrELPKTISGKIRRNELRQK 495
Cdd:PRK08162 487 LKDG-ASATEE----EIIAHCREHLAGFKVPKAVVFG-ELPKTSTGKIQKFVLREQ 536
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
99-494 |
1.53e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 115.26 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 99 KAANVLSGACSLQcgDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVITNDSVASTVESVE 178
Cdd:PRK07638 38 KVANWLNEKESKN--KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTERYKLNDLPDEE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 179 ADCqslkfkLLVSEghregWLSFKDLLKTAPSDhrcvTTKSQH-PVAIYFTSGTTGAPK--------------------- 236
Cdd:PRK07638 116 GRV------IEIDE-----WKRMIEKYLPTYAP----IENVQNaPFYMGFTSGSTGKPKaflraqqswlhsfdcnvhdfh 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 237 MTE-----------HSHCSYG------IGLTVSGSCTFNS---------------------LRHCVSAGEPINPEVM--- 275
Cdd:PRK07638 181 MKRedsvliagtlvHSLFLYGaistlyVGQTVHLMRKFIPnqvldkletenisvmytvptmLESLYKENRVIENKMKiis 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 276 --AKWKA---------WTGLDIHECYGQTE----TVLVCGNFkgmEIKPGSMGKPSPGYDVKIIDENGNILPPGKEGEIA 340
Cdd:PRK07638 261 sgAKWEAeakekikniFPYAKLYEFYGASElsfvTALVDEES---ERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVY 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 341 IKvkptRPLFlFTCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLES 420
Cdd:PRK07638 338 VK----SPQF-FMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEI 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024458455 421 AVVSSPDPIRGEVVKAFVvltpnyvshDPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELRQ 494
Cdd:PRK07638 413 VVIGVPDSYWGEKPVAII---------KGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKS 477
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
113-494 |
4.27e-27 |
|
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: 113.97 E-value: 4.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 113 GDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVITNDSVASTVESVEADCQSLKFKLLVSE 192
Cdd:cd05909 31 GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQFIEKLKLHHLFDVEYDARIVYLE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 193 GHREGwLSFKDLLKTA------PSDHR----CVTTKSQHPVAIYFTSGTTGAPKMTEHSHCS------------------ 244
Cdd:cd05909 111 DLRAK-ISKADKCKAFlagkfpPKWLLrifgVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNllanveqitaifdpnped 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 245 ---------YGIGLTVSG-----------------------------SCT--------------------FNSLRHCVSA 266
Cdd:cd05909 190 vvfgalpffHSFGLTGCLwlpllsgikvvfhpnpldykkipeliydkKATillgtptflrgyaraahpedFSSLRLVVAG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 267 GEPINPEVMAKWKAWTGLDIHECYGQTET--VLVCgNFKGMEIKPGSMGKPSPGYDVKIIDENGNI-LPPGKEGEIAIKv 343
Cdd:cd05909 270 AEKLKDTLRQEFQEKFGIRILEGYGTTECspVISV-NTPQSPNKEGTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVR- 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 344 KPTrplfLFTCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEH-PAVLESAV 422
Cdd:cd05909 348 GPN----VMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAV 423
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024458455 423 VSSPDPIRGEVVKAFvvltpnYVSHDPEKmmKDLQDHVKKATAPYKY-PRKMEFVRELPKTISGKIRRNELRQ 494
Cdd:cd05909 424 VSVPDGRKGEKIVLL------TTTTDTDP--SSLNDILKNAGISNLAkPSYIHQVEEIPLLGTGKPDYVTLKA 488
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
259-493 |
5.70e-27 |
|
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: 113.23 E-value: 5.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 259 SLRHCVSAGEPINPEVMAKWKAWTGLDIHEcYGQTETV---LVCGNFKGMEIKPGSM--GKPSPGYDVKIIDENGNILPP 333
Cdd:cd17649 213 SLRLYIFGGEALSPELLRRWLKAPVRLFNA-YGPTEATvtpLVWKCEAGAARAGASMpiGRPLGGRSAYILDADLNPVPV 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 334 GKEGEIAIKVKPtrplfLFTCYTDDPEKTKATVRGD--------FYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPF 405
Cdd:cd17649 292 GVTGELYIGGEG-----LARGYLGRPELTAERFVPDpfgapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELG 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 406 EVESALIEHPAVLESAVVSSPDPIRGEVVkAFVVL-TPNYVSHDPEKmmkdLQDHVKKATAPYKYPRKMEFVRELPKTIS 484
Cdd:cd17649 367 EIEAALLEHPGVREAAVVALDGAGGKQLV-AYVVLrAAAAQPELRAQ----LRTALRASLPDYMVPAHLVFLARLPLTPN 441
|
....*....
gi 2024458455 485 GKIRRNELR 493
Cdd:cd17649 442 GKLDRKALP 450
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
83-494 |
5.82e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 114.07 E-value: 5.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 83 GEEVKWSFEELGVLSRKAANVLsGACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAK 162
Cdd:PRK06164 31 DEDRPLSRAELRALVDRLAAWL-AAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRAR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 163 GVITNDS-----VASTVESVEADC-QSLKFKLLVSEGH-------REGWLSFKDLLKTAPSDHRCVTTKSQHPVAIYFT- 228
Cdd:PRK06164 110 WLVVWPGfkgidFAAILAAVPPDAlPPLRAIAVVDDAAdatpapaPGARVQLFALPDPAPPAAAGERAADPDAGALLFTt 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 229 SGTTGAPKMTEHS------HC-----SYGIG--------LTVSGSCTFNSLRHCVSAGEPI------------------- 270
Cdd:PRK06164 190 SGTTSGPKLVLHRqatllrHAraiarAYGYDpgavllaaLPFCGVFGFSTLLGALAGGAPLvcepvfdaartaralrrhr 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 271 ------NPEVM-------------------------------AKWKAWTGLDIHECYGQTETvlvcgnFKGMEIKPGSM- 312
Cdd:PRK06164 270 vthtfgNDEMLrrildtageradfpsarlfgfasfapalgelAALARARGVPLTGLYGSSEV------QALVALQPATDp 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 313 --------GKP-SPGYDVKIID-ENGNILPPGKEGEIAIKVkPTrplfLFTCYTDDPEKTKATVRGD-FYVTGDRGLMDE 381
Cdd:PRK06164 344 vsvrieggGRPaSPEARVRARDpQDGALLPDGESGEIEIRA-PS----LMRGYLDNPDATARALTDDgYFRTGDLGYTRG 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 382 DGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSpdPIRGE-VVKAFVVLTPNyVSHDPEKMMKdlqdHV 460
Cdd:PRK06164 419 DGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKtVPVAFVIPTDG-ASPDEAGLMA----AC 491
|
490 500 510
....*....|....*....|....*....|....*..
gi 2024458455 461 KKATAPYKYPRKMEFVRELPKTISG---KIRRNELRQ 494
Cdd:PRK06164 492 REALAGFKVPARVQVVEAFPVTESAngaKIQKHRLRE 528
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
260-492 |
1.84e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 112.40 E-value: 1.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 260 LRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTET-VLVCGNFKGMEIKPGSMGKPSPGYDVKIIDENGNILPPGKEGE 338
Cdd:PRK13383 294 LRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVgIGALATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGR 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 339 IAI--KVKPTRplflftcYTDDpeKTKATVRGdFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPA 416
Cdd:PRK13383 374 IFVggELAGTR-------YTDG--GGKAVVDG-MTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPA 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024458455 417 VLESAVVSSPDPIRGEVVKAFVVLTPNyVSHDPEKmmkdLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNEL 492
Cdd:PRK13383 444 VADNAVIGVPDERFGHRLAAFVVLHPG-SGVDAAQ----LRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
406-486 |
3.03e-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: 101.47 E-value: 3.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 406 EVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYvshdpEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISG 485
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGV-----ELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSG 75
|
.
gi 2024458455 486 K 486
Cdd:pfam13193 76 K 76
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
259-486 |
4.71e-26 |
|
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: 109.01 E-value: 4.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 259 SLRHCVSAGEPINPEVMAKW-KAWTGLDIHECYGQTET-VLVCGNFKGMEIKPGSMGKPSPgyDVKIIDENGNILPPGKE 336
Cdd:cd05924 135 SLFAISSGGALLSPEVKQGLlELVPNITLVDAFGSSETgFTGSGHSAGSGPETGPFTRANP--DTVVLDDDGRVVPPGSG 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 337 GEIAIKVKPTRPLflftCYTDDPEKTKAT---VRGDFY-VTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALI 412
Cdd:cd05924 213 GVGWIARRGHIPL----GYYGDEAKTAETfpeVDGVRYaVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALK 288
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024458455 413 EHPAVLESAVVSSPDPIRGEVVKAFVVLTPNyvsHDPEkmMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGK 486
Cdd:cd05924 289 SHPAVYDVLVVGRPDERWGQEVVAVVQLREG---AGVD--LEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
82-489 |
8.89e-26 |
|
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: 109.84 E-value: 8.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 82 DGEEVKWSFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKA 161
Cdd:cd05914 2 YYGGEPLTYKDLADNIAKFALLLK-INGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 162 KGVIT--NDSVAS----------------TVESVEADCQSLKFKLLVSEG---------HREGWLSFKDLLKTAPSDHRC 214
Cdd:cd05914 81 KAIFVsdEDDVALinytsgttgnskgvmlTYRNIVSNVDGVKEVVLLGKGdkilsilplHHIYPLTFTLLLPLLNGAHVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 215 VTTKSQHPVAI----YFTSGTTGAP---------KMTEHSHCSYGIGLTVSGSCTFN-----------------SLRHCV 264
Cdd:cd05914 161 FLDKIPSAKIIalafAQVTPTLGVPvplviekifKMDIIPKLTLKKFKFKLAKKINNrkirklafkkvheafggNIKEFV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 265 SAGEPINPEVMAKWKAwTGLDIHECYGQTETV-LVCGNFKGmEIKPGSMGKPSPGYDVKIIDENgnilPPGKEGEIAIKV 343
Cdd:cd05914 241 IGGAKINPDVEEFLRT-IGFPYTIGYGMTETApIISYSPPN-RIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIVRG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 344 KPtrplfLFTCYTDDPEKTKA--TVRGDFYvTGDRGLMDEDGYFWFVGRADDVI-NSAGYRIGPFEVESALIEHPAVLES 420
Cdd:cd05914 315 PN-----VMKGYYKNPEATAEafDKDGWFH-TGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPFVLES 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024458455 421 AVVsspdpIRGEVVKAFVVLTPNY-------VSHDPEKMMKDLQDHVKKATAPYKYPRKMEFVRE-LPKTISGKIRR 489
Cdd:cd05914 389 LVV-----VQEKKLVALAYIDPDFldvkalkQRNIIDAIKWEVRDKVNQKVPNYKKISKVKIVKEeFEKTPKGKIKR 460
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
84-492 |
3.26e-25 |
|
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: 108.15 E-value: 3.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 84 EEVKWSFEELGVLSRKAANVLS--GACSlqcGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKA 161
Cdd:cd12116 9 DDRSLSYAELDERANRLAARLRarGVGP---GDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 162 KGVITNDSVASTvesveADCQSLKFKLLVSEGHREGwlsfkDLLKTAPSDHrcvttksqHPVAIYFTSGTTGAPKMTEHS 241
Cdd:cd12116 86 ALVLTDDALPDR-----LPAGLPVLLLALAAAAAAP-----AAPRTPVSPD--------DLAYVIYTSGSTGRPKGVVVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 242 HCS-----------YGIG-----------------------LTVSGSCTFNSLRHCVSAG------EPINPEVM----AK 277
Cdd:cd12116 148 HRNlvnflhsmrerLGLGpgdrllavttyafdisllelllpLLAGARVVIAPRETQRDPEalarliEAHSITVMqatpAT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 278 WK-----AWTGLD-------------------------IHECYGQTETVL------VCGNFKGMEIkpgsmGKPSPGYDV 321
Cdd:cd12116 228 WRmlldaGWQGRAgltalcggealppdlaarllsrvgsLWNLYGPTETTIwstaarVTAAAGPIPI-----GRPLANTQV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 322 KIIDENGNILPPGKEGEIAIK---VKP---TRPLFLFTCYTDDPEktkATVRGDFYVTGDRGLMDEDGYFWFVGRADDVI 395
Cdd:cd12116 303 YVLDAALRPVPPGVPGELYIGgdgVAQgylGRPALTAERFVPDPF---AGPGSRLYRTGDLVRRRADGRLEYLGRADGQV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 396 NSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVkAFVVLtPNYVSHDPEKMMKDLQDHVkkatapykyPRKM-- 473
Cdd:cd12116 380 KIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVL-KAGAAPDAAALRAHLRATL---------PAYMvp 448
|
490 500
....*....|....*....|..
gi 2024458455 474 -EFVR--ELPKTISGKIRRNEL 492
Cdd:cd12116 449 sAFVRldALPLTANGKLDRKAL 470
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
259-492 |
3.75e-25 |
|
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: 107.78 E-value: 3.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 259 SLRHCVSAGEPINPEVMAKWKAWTGLDIHEC---YGQTET-VLVcgNFKGM---EIKPGSM---GKPSPGYDVKIIDENG 328
Cdd:cd17643 211 ALRYVIFGGEALEAAMLRPWAGRFGLDRPQLvnmYGITETtVHV--TFRPLdaaDLPAAAAspiGRPLPGLRVYVLDADG 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 329 NILPPGKEGEIAI---KVKP---TRPLFLFTCYTDDPeKTKATVRGdfYVTGDRGLMDEDGYFWFVGRADDVINSAGYRI 402
Cdd:cd17643 289 RPVPPGVVGELYVsgaGVARgylGRPELTAERFVANP-FGGPGSRM--YRTGDLARRLPDGELEYLGRADEQVKIRGFRI 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 403 GPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNyvshdPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKT 482
Cdd:cd17643 366 ELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDG-----AAADIAELRALLKELLPDYMVPARYVPLDALPLT 440
|
250
....*....|
gi 2024458455 483 ISGKIRRNEL 492
Cdd:cd17643 441 VNGKLDRAAL 450
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
94-493 |
3.83e-24 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 105.65 E-value: 3.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 94 GVLSRkAANVLSGAcsLQCGDRVLLLLPRiPEW---WLLNVACMrtGTVPIPGTQQLTAKDILYRLQKSKAKGVITNDSV 170
Cdd:PLN02860 41 GVLSL-AAGLLRLG--LRNGDVVAIAALN-SDLyleWLLAVACA--GGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETC 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 171 ASTVESVEAD-CQSLKFKLLVSEGHREGWLSFKDLLKTAPSDHRCVTTKSQHP-------VAIYFTSGTTGAPKMTEHSH 242
Cdd:PLN02860 115 SSWYEELQNDrLPSLMWQVFLESPSSSVFIFLNSFLTTEMLKQRALGTTELDYawapddaVLICFTSGTTGRPKGVTISH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 243 CS-------------YG-------------IG-------LTVSGSC-----------TFNSLR-HCVSAGEPInPEVMAK 277
Cdd:PLN02860 195 SAlivqslakiaivgYGeddvylhtaplchIGglssalaMLMVGAChvllpkfdakaALQAIKqHNVTSMITV-PAMMAD 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 278 ----------WKAWTGL-------------------------DIHECYGQTET----------VLVCGNFK-----GMEI 307
Cdd:PLN02860 274 lisltrksmtWKVFPSVrkilngggslssrllpdakklfpnaKLFSAYGMTEAcssltfmtlhDPTLESPKqtlqtVNQT 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 308 KPGS--------MGKPSPGYDVKI-IDEngnilpPGKEGEIAikvkpTRPLFLFTCYTDDPEKTKATVRGDFYV-TGDRG 377
Cdd:PLN02860 354 KSSSvhqpqgvcVGKPAPHVELKIgLDE------SSRVGRIL-----TRGPHVMLGYWGQNSETASVLSNDGWLdTGDIG 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 378 LMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYVSHDPEKMMK--- 454
Cdd:PLN02860 423 WIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGWIWSDNEKENAkkn 502
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2024458455 455 ------DLQDHV-KKATAPYKYPRKMEFVRE-LPKTISGKIRRNELR 493
Cdd:PLN02860 503 ltlsseTLRHHCrEKNLSRFKIPKLFVQWRKpFPLTTTGKIRRDEVR 549
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
55-493 |
4.84e-24 |
|
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: 105.44 E-value: 4.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 55 SDVLDRWAKVEKEGKKTknpalwWVDGDGEEVKWSFEELGVLSRKAANVLsGACSLQCGDRVLLLLPR----IPEWWlln 130
Cdd:cd05906 13 LELLLRAAERGPTKGIT------YIDADGSEEFQSYQDLLEDARRLAAGL-RQLGLRPGDSVILQFDDnedfIPAFW--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 131 vACMRTGTVPIPgtqqlTAKDILYRLQKSKAKG------------VITNDSVASTVESVEADCQSLKFKLLVSEghregw 198
Cdd:cd05906 83 -ACVLAGFVPAP-----LTVPPTYDEPNARLRKlrhiwqllgspvVLTDAELVAEFAGLETLSGLPGIRVLSIE------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 199 lsfkdLLKTAPSDHRCVTTKSQHPVAIYFTSGTTGAPKMTEHSH------------------------------------ 242
Cdd:cd05906 151 -----ELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHrnilarsagkiqhngltpqdvflnwvpldhvgglve 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 243 ---------CS----------------------YGIGLT-----------------VSGSCTFNSLRHCVSAGEPINPEV 274
Cdd:cd05906 226 lhlravylgCQqvhvpteeiladplrwldlidrYRVTITwapnfafallndlleeiEDGTWDLSSLRYLVNAGEAVVAKT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 275 MAKWK---AWTGLD---IHECYGQTET---VLVCGNFKGMEIKPG----SMGKPSPGYDVKIIDENGNILPPGKEGEIAI 341
Cdd:cd05906 306 IRRLLrllEPYGLPpdaIRPAFGMTETcsgVIYSRSFPTYDHSQAlefvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 342 kvkptRPLFLFTCYTDDPEKTKATVRGD-FYVTGDRGLMDeDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLES 420
Cdd:cd05906 386 -----RGPVVTKGYYNNPEANAEAFTEDgWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPS 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024458455 421 --AVVSSPDPIRGEVVKAfVVLTPNYVSHDP-EKMMKDLQDHVKKA---TAPYKYPRKMEfvrELPKTISGKIRRNELR 493
Cdd:cd05906 460 ftAAFAVRDPGAETEELA-IFFVPEYDLQDAlSETLRAIRSVVSREvgvSPAYLIPLPKE---EIPKTSLGKIQRSKLK 534
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
266-492 |
7.19e-24 |
|
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: 103.94 E-value: 7.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 266 AGEPINPEVMAK-WKAWTGLDIHECYGQTETVLVCgnfKGMEIKPG-----SMGKPSPGYDVKIIDENGNILPPGKEGEI 339
Cdd:cd12115 221 AGEPLPRDLVQRlYARLQVERVVNLYGPSEDTTYS---TVAPVPPGasgevSIGRPLANTQAYVLDRALQPVPLGVPGEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 340 AIKVKPtrplfLFTCYTDDPEKTKATVRGD-------FYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALI 412
Cdd:cd12115 298 YIGGAG-----VARGYLGRPGLTAERFLPDpfgpgarLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALR 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 413 EHPAVLESAVVSSPDPIRGEVVKAFVVLTPnyvshDPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNEL 492
Cdd:cd12115 373 SIPGVREAVVVAIGDAAGERRLVAYIVAEP-----GAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
113-459 |
8.06e-24 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 104.60 E-value: 8.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 113 GDRVLLLLPRIPEWWLLNVACMRTGTVPI---PGtqqLTAKDILYRLQKSKAKGVITND--SVASTV-----ESVeadcq 182
Cdd:PRK09274 66 GMRAVLMVTPSLEFFALTFALFKAGAVPVlvdPG---MGIKNLKQCLAEAQPDAFIGIPkaHLARRLfgwgkPSV----- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 183 slkfKLLVSEGHREGW----LSfKDLLKTAPSDHRCVTTKSQHPVAIYFTSGTTGAPKMTEHSH-----------CSYGI 247
Cdd:PRK09274 138 ----RRLVTVGGRLLWggttLA-TLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHgmfeaqiealrEDYGI 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 248 --------------------GLT----------------------------------------VSGSC-----TFNSLRH 262
Cdd:PRK09274 213 epgeidlptfplfalfgpalGMTsvipdmdptrpatvdpaklfaaierygvtnlfgspallerLGRYGeangiKLPSLRR 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 263 CVSAGEPINPEVMAKWKAW--TGLDIHECYGQTETVLVCgNFKGMEIKPGS-----------MGKPSPGYDVKIID---- 325
Cdd:PRK09274 293 VISAGAPVPIAVIERFRAMlpPDAEILTPYGATEALPIS-SIESREILFATraatdngagicVGRPVDGVEVRIIAisda 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 326 -----ENGNILPPGKEGEIAIK---VkpTRplflftCYTDDPEKTKAT----VRGDFY-VTGDRGLMDEDGYFWFVGR-A 391
Cdd:PRK09274 372 pipewDDALRLATGEIGEIVVAgpmV--TR------SYYNRPEATRLAkipdGQGDVWhRMGDLGYLDAQGRLWFCGRkA 443
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024458455 392 DDVINSAGyRIGPFEVESALIEHPAVLESAVVSSPDPirGEVVKAFVVLTPNYVSHDPEKMMKDLQDH 459
Cdd:PRK09274 444 HRVETAGG-TLYTIPCERIFNTHPGVKRSALVGVGVP--GAQRPVLCVELEPGVACSKSALYQELRAL 508
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
259-492 |
1.11e-23 |
|
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: 103.10 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 259 SLRHCVSAGEPINPEVMAKWKawTGLDIHECYGQTETVlVC----GNFKGMEIKPgsMGKPSPGYDVKIIDENGNILPPG 334
Cdd:cd17652 205 DLRTLVVAGEACPAELVDRWA--PGRRMINAYGPTETT-VCatmaGPLPGGGVPP--IGRPVPGTRVYVLDARLRPVPPG 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 335 KEGEIAIK-VKPTRPlflftcYTDDPEKTK--------ATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPF 405
Cdd:cd17652 280 VPGELYIAgAGLARG------YLNRPGLTAerfvadpfGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELG 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 406 EVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPnyvshDPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISG 485
Cdd:cd17652 354 EVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAP-----GAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNG 428
|
....*..
gi 2024458455 486 KIRRNEL 492
Cdd:cd17652 429 KLDRRAL 435
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
309-498 |
2.41e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 103.22 E-value: 2.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 309 PGSMGKPSPGydVKIID-ENGNILPPGK-------EGEIAIK--VKPTRPlFLFTCYTDDPEKTKATVRGDFYVTGDRGL 378
Cdd:PRK07867 314 PGALGPLPPG--VAIVDpDTGTECPPAEdadgrllNADEAIGelVNTAGP-GGFEGYYNDPEADAERMRGGVYWSGDLAY 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 379 MDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNyVSHDPEKMMKDLqd 458
Cdd:PRK07867 391 RDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPG-AKFDPDAFAEFL-- 467
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2024458455 459 HVKKATAPYKYPRKMEFVRELPKTISGKIRRNELRQKEWR 498
Cdd:PRK07867 468 AAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEGVD 507
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
214-494 |
5.07e-23 |
|
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: 101.23 E-value: 5.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 214 CVTTKSQHPVA-IYFTSGTTGAPK--MTEHSH-----------------------------CSYGIGL------------ 249
Cdd:cd17653 98 LLTTDSPDDLAyIIFTSGSTGIPKgvMVPHRGvlnyvsqpparldvgpgsrvaqvlsiafdACIGEIFstlcnggtlvla 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 250 -------TVSGSCT----------------FNSLRHCVSAGEPINPEVMAKWkaWTGLDIHECYGQTETVLVCgNFKGME 306
Cdd:cd17653 178 dpsdpfaHVARTVDalmstpsilstlspqdFPNLKTIFLGGEAVPPSLLDRW--SPGRRLYNAYGPTECTISS-TMTELL 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 307 -IKPGSMGKPSPGYDVKIIDENGNILPPGKEGEIAIK-VKPTRPlflftcYTDDPEKTKATVRGD-------FYVTGDRG 377
Cdd:cd17653 255 pGQPVTIGKPIPNSTCYILDADLQPVPEGVVGEICISgVQVARG------YLGNPALTASKFVPDpfwpgsrMYRTGDYG 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 378 LMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSpdpIRGEVVkAFVvlTPNYVSHDpekmmkDLQ 457
Cdd:cd17653 329 RWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIV---VNGRLV-AFV--TPETVDVD------GLR 396
|
330 340 350
....*....|....*....|....*....|....*..
gi 2024458455 458 DHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELRQ 494
Cdd:cd17653 397 SELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
89-495 |
9.47e-23 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 101.50 E-value: 9.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 89 SFEELGVLSRKAANVLSGAcSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVITND 168
Cdd:PRK05852 45 SYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 169 SVASTVESVEADCQSLKFKLLVSEGHREGWLSFkDLLKTAPSDHRCVTTKSQHP--VAIYFTSGTTGAPKMTEHSHCS-- 244
Cdd:PRK05852 124 DGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSV-HLDAATEPTPATSTPEGLRPddAMIMFTGGTTGLPKMVPWTHANia 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 245 -------------------------YGIGLT-------VSGSC------------TF----------------------- 257
Cdd:PRK05852 203 ssvraiitgyrlsprdatvavmplyHGHGLIaallatlASGGAvllpargrfsahTFwddikavgatwytavptihqill 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 258 ------------NSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTET--------VLVCGNFKGMEIKPGSMGKpSP 317
Cdd:PRK05852 283 eraatepsgrkpAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEAthqvtttqIEGIGQTENPVVSTGLVGR-ST 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 318 GYDVKIIDENGNILPPGKEGEIAIKvKPTrplfLFTCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINS 397
Cdd:PRK05852 362 GAQIRIVGSDGLPLPAGAVGEVWLR-GTT----VVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINR 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 398 AGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVltPNYVSHdPEKmmKDLQDHVKKATAPYKYPRKMEFVR 477
Cdd:PRK05852 437 GGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIV--PRESAP-PTA--EELVQFCRERLAAFEIPASFQEAS 511
|
490
....*....|....*...
gi 2024458455 478 ELPKTISGKIRRNELRQK 495
Cdd:PRK05852 512 GLPHTAKGSLDRRAVAEQ 529
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
215-494 |
9.80e-23 |
|
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: 101.08 E-value: 9.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 215 VTTKSQHPVAIYFTSGTTGAPK--MTEH-SHCS------YGIGLT------------------------VSGSC------ 255
Cdd:cd05918 101 LTSSPSDAAYVIFTSGSTGKPKgvVIEHrALSTsalahgRALGLTsesrvlqfasytfdvsileifttlAAGGClcipse 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 256 --------------------------------TFNSLRHCVSAGEPINPEVMAKWkaWTGLDIHECYGQTE-TVLVCGNF 302
Cdd:cd05918 181 edrlndlagfinrlrvtwafltpsvarlldpeDVPSLRTLVLGGEALTQSDVDTW--ADRVRLINAYGPAEcTIAATVSP 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 303 KGMEIKPGSMGKPSPG--YdvkIID-ENGNIL-PPGKEGEIAIkvkpTRPLfLFTCYTDDPEKTKATV------------ 366
Cdd:cd05918 259 VVPSTDPRNIGRPLGAtcW---VVDpDNHDRLvPIGAVGELLI----EGPI-LARGYLNDPEKTAAAFiedpawlkqegs 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 367 --RGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVK---AFVVLT 441
Cdd:cd05918 331 grGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPqlvAFVVLD 410
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024458455 442 P------------NYVSHDPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELRQ 494
Cdd:cd05918 411 GsssgsgdgdslfLEPSDEFRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRE 475
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
355-495 |
1.28e-22 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 101.07 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 355 YTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVV 434
Cdd:PLN02479 416 YLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESP 495
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024458455 435 KAFVVLTPNYVSHDPEKMMKDLQDHVKKATAPYKYPRKMEFvRELPKTISGKIRRNELRQK 495
Cdd:PLN02479 496 CAFVTLKPGVDKSDEAALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRAK 555
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
290-489 |
2.63e-22 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 100.59 E-value: 2.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 290 YGQTET-VLVCGNFKGMEIKPGSMGKPSPGYDVKIIDENGNILPPGKEGEIAIKVkPTRPLFLFTCYTDDpEKTKA--TV 366
Cdd:PTZ00237 412 YGQTEIgITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKL-PMPPSFATTFYKND-EKFKQlfSK 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 367 RGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLtpNYVS 446
Cdd:PTZ00237 490 FPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVL--KQDQ 567
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2024458455 447 HDPEKMMKDLQDH----VKKATAPYKYPRKMEFVRELPKTISGKIRR 489
Cdd:PTZ00237 568 SNQSIDLNKLKNEinniITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
256-492 |
2.69e-22 |
|
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: 99.71 E-value: 2.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 256 TFNSLRHCVSAGEPINPEVMAKWKAWTGL--DIHECYGQTETVLVC--GNFKGMEIKPGS--MGKPSPGYDVKIIDENGN 329
Cdd:cd17655 249 EGLSLKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPTETTVDAsiYQYEPETDQQVSvpIGKPLGNTRIYILDQYGR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 330 ILPPGKEGEIAIKVKPtrplfLFTCYTDDPEKTKAT------VRGD-FYVTGDRGLMDEDGYFWFVGRADDVINSAGYRI 402
Cdd:cd17655 329 PQPVGVAGELYIGGEG-----VARGYLNRPELTAEKfvddpfVPGErMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRI 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 403 GPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVltpnyvsHDPEKMMKDLQDHVKKATAPYKYPRKmeFVR--ELP 480
Cdd:cd17655 404 ELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIV-------SEKELPVAQLREFLARELPDYMIPSY--FIKldEIP 474
|
250
....*....|..
gi 2024458455 481 KTISGKIRRNEL 492
Cdd:cd17655 475 LTPNGKVDRKAL 486
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
80-494 |
3.11e-22 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 100.01 E-value: 3.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 80 DGDGEEVKWSFEELGVLSRKAANVLSGACslQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPG---TQQLTAKDILYRL 156
Cdd:cd05931 17 DEGGREETLTYAELDRRARAIAARLQAVG--KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLpppTPGRHAERLAAIL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 157 QKSKAKGVITNDSVASTVESVEADcqslkfkllvSEGHREGWLSFKDLLKTAPSDHRCVTTKSQHPVA-IYFTSGTTGAP 235
Cdd:cd05931 95 ADAGPRVVLTTAAALAAVRAFAAS----------RPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAyLQYTSGSTGTP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 236 K---------------------MTEHSHC------------SYGIGLTV--SGSCTF----------------------- 257
Cdd:cd05931 165 KgvvvthrnllanvrqirraygLDPGDVVvswlplyhdmglIGGLLTPLysGGPSVLmspaaflrrplrwlrlisryrat 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 258 -----N---------------------SLRHCVSAGEPINPEVMAKWK---AWTGLD---IHECYGQTE-TVLVCGNFKG 304
Cdd:cd05931 245 isaapNfaydlcvrrvrdedlegldlsSWRVALNGAEPVRPATLRRFAeafAPFGFRpeaFRPSYGLAEaTLFVSGGPPG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 305 ---------MEIKPG----------------SMGKPSPGYDVKIIDENGNI-LPPGKEGEIAIK---VKPTrplflftcY 355
Cdd:cd05931 325 tgpvvlrvdRDALAGravavaaddpaarelvSCGRPLPDQEVRIVDPETGReLPDGEVGEIWVRgpsVASG--------Y 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 356 TDDPEKTKATVR-------GDFYVTGDRGLMDeDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLES---AVVSS 425
Cdd:cd05931 397 WGRPEATAETFGalaatdeGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRPgcvAAFSV 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024458455 426 PDPIRGEVVkAFVVLTPNYVSHDPEKMMKDLQDHVKKAT--APykypRKMEFVR--ELPKTISGKIRRNELRQ 494
Cdd:cd05931 476 PDDGEERLV-VVAEVERGADPADLAAIAAAIRAAVAREHgvAP----ADVVLVRpgSIPRTSSGKIQRRACRA 543
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
258-498 |
3.04e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 96.63 E-value: 3.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 258 NSLRhcVSAGEPINPEVMAKWKAWTGLDIHECYGQTETVLVCGNFKGMeiKPGSMGKPSPG---YD--------VKIIDE 326
Cdd:PRK13388 265 NPLR--VAFGNEASPRDIAEFSRRFGCQVEDGYGSSEGAVIVVREPGT--PPGSIGRGAPGvaiYNpetltecaVARFDA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 327 NGNILPPGKE-GEIAIKVKPTRplflFTCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPF 405
Cdd:PRK13388 341 HGALLNADEAiGELVNTAGAGF----FEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAA 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 406 EVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNyVSHDPEKMMKDL---QDHVKKAtapykYPRKMEFVRELPKT 482
Cdd:PRK13388 417 PIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDG-ATFDPDAFAAFLaaqPDLGTKA-----WPRYVRIAADLPST 490
|
250
....*....|....*.
gi 2024458455 483 ISGKIRRNELRQKEWR 498
Cdd:PRK13388 491 ATNKVLKRELIAQGWA 506
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
356-496 |
3.93e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 95.49 E-value: 3.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 356 TDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVK 435
Cdd:PRK08308 278 ENAPEEIVVKMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVK 357
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024458455 436 AfvvltpNYVSH---DPEKMMKDLQDHVkkatAPYKYPRKMEFVRELPKTISGKIRRNELRQKE 496
Cdd:PRK08308 358 A------KVISHeeiDPVQLREWCIQHL----APYQVPHEIESVTEIPKNANGKVSRKLLELGE 411
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
262-493 |
4.39e-21 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 96.63 E-value: 4.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 262 HCVSAGEPiNPEVMAKWKAWTGLDIHECYGQTET---VLVCG---------NFKGMEIKP--GSMGKPSPGYDVKIIDEN 327
Cdd:PLN03102 304 HVLTGGSP-PPAALVKKVQRLGFQVMHAYGLTEAtgpVLFCEwqdewnrlpENQQMELKArqGVSILGLADVDVKNKETQ 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 328 GNILPPGKE-GEIAIKVKPtrplfLFTCYTDDPEKTKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFE 406
Cdd:PLN03102 383 ESVPRDGKTmGEIVIKGSS-----IMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 407 VESALIEHPAVLESAVVSSPDPIRGEVVKAFVVL--TPNYVSHDPEKMM---KDLQDHVKKATAPYKYPRKMEFVRELPK 481
Cdd:PLN03102 458 VENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLekGETTKEDRVDKLVtreRDLIEYCRENLPHFMCPRKVVFLQELPK 537
|
250
....*....|..
gi 2024458455 482 TISGKIRRNELR 493
Cdd:PLN03102 538 NGNGKILKPKLR 549
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
289-494 |
2.47e-20 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 93.52 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 289 CYGQTETV-LVCgnfkgmEIKPG-------SMGKPSPGYDVKIidengnilPPGKEGEIAIKvkpTRPLFL--FTCYTDD 358
Cdd:PRK07445 260 TYGMTETAsQIA------TLKPDdflagnnSSGQVLPHAQITI--------PANQTGNITIQ---AQSLALgyYPQILDS 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 359 PEktkatvrgdFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFV 438
Cdd:PRK07445 323 QG---------IFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIY 393
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024458455 439 VltPNYVSHDPEKmmkdLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELRQ 494
Cdd:PRK07445 394 V--PKDPSISLEE----LKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
73-499 |
2.50e-20 |
|
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: 94.92 E-value: 2.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 73 NPALwwVDGDGEevkWSFEELGVLSRKAANVLsGACSLQCGDRVLLLLPRIPEW--WLLnvACMRTGT--VPIpgtqqlt 148
Cdd:COG1020 492 AVAV--VFGDQS---LTYAELNARANRLAHHL-RALGVGPGDLVGVCLERSLEMvvALL--AVLKAGAayVPL------- 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 149 akD-------ILYRLQKSKAKGVITNDSVASTVESVEADCqslkfkLLVSEghregwlsfkDLLKTAPSDHRCVTTKSQH 221
Cdd:COG1020 557 --DpaypaerLAYMLEDAGARLVLTQSALAARLPELGVPV------LALDA----------LALAAEPATNPPVPVTPDD 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 222 PVAIYFTSGTTGAPK--MTEH----SHCS-----YGIG-----------------------LTVSGSC------------ 255
Cdd:COG1020 619 LAYVIYTSGSTGRPKgvMVEHralvNLLAwmqrrYGLGpgdrvlqfaslsfdasvweifgaLLSGATLvlappearrdpa 698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 256 ------------------------------TFNSLRHCVSAGEPINPEVMAKWKA-WTGLDIHECYGQTETVLV--CGNF 302
Cdd:COG1020 699 alaellarhrvtvlnltpsllralldaapeALPSLRLVLVGGEALPPELVRRWRArLPGARLVNLYGPTETTVDstYYEV 778
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 303 KGMEIKPGSM--GKPSPGYDVKIIDENGNILPPGKEGEIAIkvkptrplflftC-------YTDDPEKTKA-------TV 366
Cdd:COG1020 779 TPPDADGGSVpiGRPIANTRVYVLDAHLQPVPVGVPGELYI------------GgaglargYLNRPELTAErfvadpfGF 846
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 367 RGD-FYVTGDRGLMDEDGYFWFVGRADD-V-INsaGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPN 443
Cdd:COG1020 847 PGArLYRTGDLARWLPDGNLEFLGRADDqVkIR--GFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAG 924
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024458455 444 YVSHDPEkmmkdLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELRQKEWRR 499
Cdd:COG1020 925 AAAAAAL-----LRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAA 975
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
307-494 |
6.36e-20 |
|
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: 92.49 E-value: 6.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 307 IKPGSMGKPSPGYDVKIIDENGNILPPGkegeiaikvkptrplflftcYTDDPEKTKATV-RGDFYVTGDRGLMDEDGYF 385
Cdd:cd05915 346 ADEEGRPVPKDGKALGEVQLKGPWITGG--------------------YYGNEEATRSALtPDGFFRTGDIAVWDEEGYV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 386 WFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTpnyvshDPEKMMKDLQDHVKKATA 465
Cdd:cd05915 406 EIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPR------GEKPTPEELNEHLLKAGF 479
|
170 180 190
....*....|....*....|....*....|
gi 2024458455 466 PYKY-PRKMEFVRELPKTISGKIRRNELRQ 494
Cdd:cd05915 480 AKWQlPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
80-494 |
9.90e-20 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 92.15 E-value: 9.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 80 DGDGEEVKwSFEELGVLSRKAANVLSGACSLQCGDRVLLLLPRIPEWW--LLNVACMrtGTVPIPGTQQLTAKDILYRLQ 157
Cdd:PRK05620 32 GGAEQEQT-TFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLevLFAVACM--GAVFNPLNKQLMNDQIVHIIN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 158 KSKAKGVITNDSVASTVESVEADCQSLKFKLLVSEGH--------REGW--LSFKDLLKTAPSDHRCVTTKSQHPVAIYF 227
Cdd:PRK05620 109 HAEDEVIVADPRLAEQLGEILKECPCVRAVVFIGPSDadsaaahmPEGIkvYSYEALLDGRSTVYDWPELDETTAAAICY 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 228 TSGTTGAPKMTEHSH--------------------------C-------SYGI--------------GLTVS-------- 252
Cdd:PRK05620 189 STGTTGAPKGVVYSHrslylqslslrttdslavthgesflcCvpiyhvlSWGVplaafmsgtplvfpGPDLSaptlakii 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 253 ---------GSCTF---------------NSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTETVLVcgnfkGMEIK 308
Cdd:PRK05620 269 atamprvahGVPTLwiqlmvhylknpperMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPV-----GTVAR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 309 PG-------------SMGKPSPGYDVKIIDEnGNILPPG--KEGEIAIK-------------VKPTRPLFLFTCYTDDPE 360
Cdd:PRK05620 344 PPsgvsgearwayrvSQGRFPASLEYRIVND-GQVMESTdrNEGEIQVRgnwvtasyyhsptEEGGGAASTFRGEDVEDA 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 361 KTKATVRGdFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVL 440
Cdd:PRK05620 423 NDRFTADG-WLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVL 501
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024458455 441 TPNY--VSHDPEKMMKDLQDHVKKATAPYKYprkmEFVRELPKTISGKIRRNELRQ 494
Cdd:PRK05620 502 APGIepTRETAERLRDQLRDRLPNWMLPEYW----TFVDEIDKTSVGKFDKKDLRQ 553
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
257-487 |
1.39e-19 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 92.68 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 257 FNSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTET----------VLVCGNFKGMEIKPGSMGKPSPGYDVKIID- 325
Cdd:PRK08633 897 FASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETspvasvnlpdVLAADFKRQTGSKEGSVGMPLPGVAVRIVDp 976
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 326 ENGNILPPGKEGEIAIK---VkptrplflFTCYTDDPEKTKATVR----GDFYVTGDRGLMDEDGYFWFVGRADDVINSA 398
Cdd:PRK08633 977 ETFEELPPGEDGLILIGgpqV--------MKGYLGDPEKTAEVIKdidgIGWYVTGDKGHLDEDGFLTITDRYSRFAKIG 1048
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 399 GYRIGPFEVESALIE--HPAVLESAVVSSPDPIRGEvvKAFVVLTPNyvSHDPEKmmkdLQDHVKKATAP--YKyPRKME 474
Cdd:PRK08633 1049 GEMVPLGAVEEELAKalGGEEVVFAVTAVPDEKKGE--KLVVLHTCG--AEDVEE----LKRAIKESGLPnlWK-PSRYF 1119
|
250
....*....|...
gi 2024458455 475 FVRELPKTISGKI 487
Cdd:PRK08633 1120 KVEALPLLGSGKL 1132
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
290-489 |
8.79e-19 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 89.18 E-value: 8.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 290 YGQTE-TVLVcgnfKGMEI--------KPGSMGKPSPGYDVKIIDENGNILPPGKEGEIAIK---VKPTrplflftcYTD 357
Cdd:PRK04813 293 YGPTEaTVAV----TSIEItdemldqyKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISgpsVSKG--------YLN 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 358 DPEKTKA---TVRGD-FYVTGDRGLMDeDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVlESAVVSspdPI-RGE 432
Cdd:PRK04813 361 NPEKTAEaffTFDGQpAYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYV-ESAVVV---PYnKDH 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 433 VVK---AFVVLTPNYVSHDPEkMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRR 489
Cdd:PRK04813 436 KVQyliAYVVPKEEDFEREFE-LTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDR 494
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
82-429 |
1.34e-18 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 88.68 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 82 DGEEVKWSFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKA 161
Cdd:cd05932 1 GGQVVEFTWGEVADKARRLAAALR-ALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 162 KGVITN--DSVASTVESVEADCQSLKFKLLVSEGHREGWlsfKDLLKTAPSDHRCVTTKSQHPVAIYFTSGTTGAPKMTE 239
Cdd:cd05932 80 KALFVGklDDWKAMAPGVPEGLISISLPPPSAANCQYQW---DDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGVM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 240 HSHCSYG---------IGLT-------------------------VSGSCTF---------------------------- 257
Cdd:cd05932 157 LTFGSFAwaaqagiehIGTEendrmlsylplahvtervfveggslYGGVLVAfaesldtfvedvqrarptlffsvprlwt 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 258 ------------------------NSL-RHCVSAG-------------EPINPEVMaKWKAWTGLDIHECYGQTETVLVC 299
Cdd:cd05932 237 kfqqgvqdkipqqklnlllkipvvNSLvKRKVLKGlgldqcrlagcgsAPVPPALL-EWYRSLGLNILEAYGMTENFAYS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 300 GNFKGMEIKPGSMGKPSPGYDVKIidengnilppGKEGEIAIKVKPtrplfLFTCYTDDPEKTKATVRGD-FYVTGDRGL 378
Cdd:cd05932 316 HLNYPGRDKIGTVGNAGPGVEVRI----------SEDGEILVRSPA-----LMMGYYKDPEATAEAFTADgFLRTGDKGE 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2024458455 379 MDEDGYFWFVGRADDVINSA-GYRIGPFEVESALIEHPAVLESAVVSS--PDPI 429
Cdd:cd05932 381 LDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSglPAPL 434
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
258-492 |
1.90e-18 |
|
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: 87.88 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 258 NSLRHCVSAGEPINPEVMAKWKAWTGLDIH--ECYGQTE---TVLVC--GNFKGMEIKPGSMGKPSPGYDVKIIDENGNI 330
Cdd:cd17644 224 SSLRLVIVGGEAVQPELVRQWQKNVGNFIQliNVYGPTEatiAATVCrlTQLTERNITSVPIGRPIANTQVYILDENLQP 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 331 LPPGKEGEIAI------KVKPTRPLFLFTCYTDDPEKTKATVRgdFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGP 404
Cdd:cd17644 304 VPVGVPGELHIggvglaRGYLNRPELTAEKFISHPFNSSESER--LYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 405 FEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVltPNYvshDPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTIS 484
Cdd:cd17644 382 GEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIV--PHY---EESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPN 456
|
....*...
gi 2024458455 485 GKIRRNEL 492
Cdd:cd17644 457 GKIDRRAL 464
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
57-492 |
6.25e-18 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 86.60 E-value: 6.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 57 VLDRWakVEKEGKKTKNPALWWVDGDGEevkWSFEEL-GVLSRKAANVLSGACSLqcGDRVLLLLPRIPEWWLLNVACMR 135
Cdd:PRK05857 16 VLDRV--FEQARQQPEAIALRRCDGTSA---LRYRELvAEVGGLAADLRAQSVSR--GSRVLVISDNGPETYLSVLACAK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 136 TGTVPIPGTQQLTAKDILYRLQKSKAKGVITNDSVASTVESVEADCQSLKfKLLVSEGHREGWLSF---KDLLKTAPSdh 212
Cdd:PRK05857 89 LGAIAVMADGNLPIAAIERFCQITDPAAALVAPGSKMASSAVPEALHSIP-VIAVDIAAVTRESEHsldAASLAGNAD-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 213 rcvtTKSQHPVAIYFTSGTTGAPKMTEHSHCSY--------GIGLT----VSGSCTF---------------NSLRH--- 262
Cdd:PRK05857 166 ----QGSEDPLAMIFTSGTTGEPKAVLLANRTFfavpdilqKEGLNwvtwVVGETTYsplpathigglwwilTCLMHggl 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 263 CVSAGEP-----------------INPEVMAK-------------------------------WKAWTGLDIHECYGQTE 294
Cdd:PRK05857 242 CVTGGENttslleilttnavattcLVPTLLSKlvselksanatvpslrlvgyggsraiaadvrFIEATGVRTAQVYGLSE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 295 T-----VLVCGNFKGMEIKPGSMGKPSPGYDVKIIDENG------NILPPGKEGEIAIKvKPTRPLflftCYTDDPEKTK 363
Cdd:PRK05857 322 TgctalCLPTDDGSIVKIEAGAVGRPYPGVDVYLAATDGigptapGAGPSASFGTLWIK-SPANML----GYWNNPERTA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 364 ATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPN 443
Cdd:PRK05857 397 EVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAE 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2024458455 444 YVSHDPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNEL 492
Cdd:PRK05857 477 LDESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
313-492 |
1.14e-17 |
|
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: 85.40 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 313 GKPSPGYDVKIIDENGNILPPGKEGEIAIKvkpTRPLFLftCYTDDPEKTKA-----TVRGDFYVTGDRGLMDEDGYFWF 387
Cdd:cd12114 303 GRPLANQRYRVLDPRGRDCPDWVPGELWIG---GRGVAL--GYLGDPELTAArfvthPDGERLYRTGDLGRYRPDGTLEF 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 388 VGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPiRGEVVKAFVVLTPNYVSHDPEkmmkDLQDHVKKATAPY 467
Cdd:cd12114 378 LGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDGTPIAPD----ALRAFLAQTLPAY 452
|
170 180
....*....|....*....|....*
gi 2024458455 468 KYPRKMEFVRELPKTISGKIRRNEL 492
Cdd:cd12114 453 MIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
259-492 |
3.97e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 85.01 E-value: 3.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 259 SLRHCVSAGEPINPEVMAKWKAwtGLDIHECYGQTETVLVCGNFKGMEIKPGS--MGKPSPGYDVKIIDENGNILPPGKE 336
Cdd:PRK12316 3312 SLKRIVCGGEALPADLQQQVFA--GLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILDGSLEPVPVGAL 3389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 337 GEIAI------KVKPTRPLFLFTCYTDDPEKTKatvrGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESA 410
Cdd:PRK12316 3390 GELYLggeglaRGYHNRPGLTAERFVPDPFVPG----ERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEAR 3465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 411 LIEHPAVLESAVVSspdpIRGEVVKAFVVLTpnyvshDPEKMMKD-LQDHVKKATAPYKYPRKMEFVRELPKTISGKIRR 489
Cdd:PRK12316 3466 LLEHPWVREAVVLA----VDGRQLVAYVVPE------DEAGDLREaLKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDR 3535
|
...
gi 2024458455 490 NEL 492
Cdd:PRK12316 3536 KAL 3538
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
257-446 |
4.74e-17 |
|
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: 84.01 E-value: 4.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 257 FNSLRHCVSAGEPINPEVMAKWKAwTGLDIHECYGQTETVLVCGNFKGMEIKPGSMGKPSPGYDVKIiDENGNIL--PPG 334
Cdd:cd17641 323 FSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRI-DEVGEILvrSPG 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 335 kegeiaikvkptrplfLFTCYTDDPEKTKATVRGD-FYVTGDRGLMDEDGYFWFVGRADDVINSA-GYRIGPFEVESALI 412
Cdd:cd17641 401 ----------------VFVGYYKNPEATAEDFDEDgWLHTGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQFIENKLK 464
|
170 180 190
....*....|....*....|....*....|....
gi 2024458455 413 EHPAVLESAVVSSPDPIrgevVKAFVVLTPNYVS 446
Cdd:cd17641 465 FSPYIAEAVVLGAGRPY----LTAFICIDYAIVG 494
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
46-487 |
6.42e-17 |
|
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: 83.47 E-value: 6.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 46 EVPEYF-----NFASDVLdrwakvekEGKKTKNPALWWVDGDGEEVKWSFEELGVLSRKAANVLSgACSLQCGDRVLLLL 120
Cdd:cd05943 60 PGARWFpgarlNYAENLL--------RHADADDPAAIYAAEDGERTEVTWAELRRRVARLAAALR-ALGVKPGDRVAGYL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 121 PRIPEwwlLNVACMRT---GTVPIPGTQQLTAKDILYRLQKSKAKGVITNDSV---------ASTVESVEADCQSLKFKL 188
Cdd:cd05943 131 PNIPE---AVVAMLATasiGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDAYtyngkrhdvREKVAELVKGLPSLLAVV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 189 LVSEGHREG---------WLSFKDLLKTAPSDHRC-VTTKSQHPVAIYFTSGTTGAPKMTEHSH---------------- 242
Cdd:cd05943 208 VVPYTVAAGqpdlskiakALTLEDFLATGAAGELEfEPLPFDHPLYILYSSGTTGLPKCIVHGAggtllqhlkehilhcd 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 243 ------------CSY----------GIGLTV---SGS-----------------CTF----------------------- 257
Cdd:cd05943 288 lrpgdrlfyyttCGWmmwnwlvsglAVGATIvlyDGSpfypdtnalwdladeegITVfgtsakyldalekaglkpaethd 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 258 -NSLRHCVSAGEPINPE----VMAKWKAwtglDIHECY--GQTEtvlVCGNFKGM----EIKPGSMGKPSPGYDVKIIDE 326
Cdd:cd05943 368 lSSLRTILSTGSPLKPEsfdyVYDHIKP----DVLLASisGGTD---IISCFVGGnpllPVYRGEIQCRGLGMAVEAFDE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 327 NGNILPpGKEGEIAI-KVKPTRPLFLFtcytDDPEKTK------ATVRGdFYVTGDRGLMDEDGYFWFVGRADDVINSAG 399
Cdd:cd05943 441 EGKPVW-GEKGELVCtKPFPSMPVGFW----NDPDGSRyraayfAKYPG-VWAHGDWIEITPRGGVVILGRSDGTLNPGG 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 400 YRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNyVSHDPEkMMKDLQDHVKKATAPYKYPRKMEFVREL 479
Cdd:cd05943 515 VRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREG-VELDDE-LRKRIRSTIRSALSPRHVPAKIIAVPDI 592
|
....*...
gi 2024458455 480 PKTISGKI 487
Cdd:cd05943 593 PRTLSGKK 600
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
87-492 |
8.78e-17 |
|
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: 82.60 E-value: 8.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 87 KWSFEELGVLSRKAANVLSGaCSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVIT 166
Cdd:cd17645 23 SLTYKQLNEKANQLARHLRG-KGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 167 N-DSVASTVESVEADCQSlkfKLLVSEGHREGWLSF--KDLLKTAPSDHRCVTTKSQHPVAIY--FTSGTTGAPKMTEHS 241
Cdd:cd17645 102 NpDDLAYVIYTSGSTGLP---KGVMIEHHNLVNLCEwhRPYFGVTPADKSLVYASFSFDASAWeiFPHLTAGAALHVVPS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 242 HCSYGI----------GLTVS----GSC-TF-----NSLRHCVSAGEPINPEVMAKWKAWTGldihecYGQTETVLVCGN 301
Cdd:cd17645 179 ERRLDLdalndyfnqeGITISflptGAAeQFmqldnQSLRVLLTGGDKLKKIERKGYKLVNN------YGPTENTVVATS 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 302 FkgmEIKPG----SMGKPSPGYDVKIIDENGNILPPGKEGEIAIKVKPtrplfLFTCYTDDPEKTKATVRGD-------F 370
Cdd:cd17645 253 F---EIDKPyaniPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEG-----LARGYLNRPELTAEKFIVHpfvpgerM 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 371 YVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVlTPNYVshDPE 450
Cdd:cd17645 325 YRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT-APEEI--PHE 401
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2024458455 451 KmmkdLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNEL 492
Cdd:cd17645 402 E----LREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
107-423 |
1.01e-16 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 82.41 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 107 ACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYrlqkskakgvITNDSVASTVesveadcqslkf 186
Cdd:cd17640 24 SLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLY----------ILNHSESVAL------------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 187 kllvseghregwlsfkdLLKTAPSDhrcVTTksqhpvaIYFTSGTTGAPK--MTEHS----------------------- 241
Cdd:cd17640 82 -----------------VVENDSDD---LAT-------IIYTSGTTGNPKgvMLTHAnllhqirslsdivppqpgdrfls 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 242 -----H-----CSYGIgLTVSGSCTFNSLRHCVSAGEPINPEVMAK----WKAW-------------------------- 281
Cdd:cd17640 135 ilpiwHsyersAEYFI-FACGCSQAYTSIRTLKDDLKRVKPHYIVSvprlWESLysgiqkqvsksspikqflflfflsgg 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 282 ----------------------TGLDIHECYGQTET--VLVCGNFKgmEIKPGSMGKPSPGYDVKIIDENGN-ILPPGKE 336
Cdd:cd17640 214 ifkfgisgggalpphvdtffeaIGIEVLNGYGLTETspVVSARRLK--CNVRGSVGRPLPGTEIKIVDPEGNvVLPPGEK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 337 GEIAIKVKPtrplfLFTCYTDDPEKTKATVRGD-FYVTGDRGLMDEDGYFWFVGRADDVIN-SAGYRIGPFEVESALIEH 414
Cdd:cd17640 292 GIVWVRGPQ-----VMKGYYKNPEATSKVLDSDgWFNTGDLGWLTCGGELVLTGRAKDTIVlSNGENVEPQPIEEALMRS 366
|
....*....
gi 2024458455 415 PaVLESAVV 423
Cdd:cd17640 367 P-FIEQIMV 374
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
259-494 |
1.25e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 83.47 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 259 SLRHCVSAGEPINPEVMAK-WKAWTGLDIHECYGQTETVLVC-------GNFKGMEIKPgsMGKPSPGYDVKIIDENGNI 330
Cdd:PRK12316 4810 SLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTVTVllwkardGDACGAAYMP--IGTPLGNRSGYVLDGQLNP 4887
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 331 LPPGKEGEIAIKVKPT------RPLFLFTCYTDDPEKTKAtvrGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGP 404
Cdd:PRK12316 4888 LPVGVAGELYLGGEGVargyleRPALTAERFVPDPFGAPG---GRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIEL 4964
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 405 FEVESALIEHPAVLESAVVSSPDPIRGEVVkAFVVLTPNYVSHDPEK---MMKDLQDHVKKATAPYKYPRKMEFVRELPK 481
Cdd:PRK12316 4965 GEIEARLREHPAVREAVVIAQEGAVGKQLV-GYVVPQDPALADADEAqaeLRDELKAALRERLPEYMVPAHLVFLARMPL 5043
|
250
....*....|...
gi 2024458455 482 TISGKIRRNELRQ 494
Cdd:PRK12316 5044 TPNGKLDRKALPQ 5056
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
259-496 |
1.44e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 83.29 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 259 SLRHCVSAGEPINPEVMAKWKAWT-GLDIHECYGQTETVLVCGNFK----GMEIKPGSMGKPSPGYDVKIIDENGNILPP 333
Cdd:PRK12467 772 PQRALVCGGEALQVDLLARVRALGpGARLINHYGPTETTVGVSTYElsdeERDFGNVPIGQPLANLGLYILDHYLNPVPV 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 334 GKEGEIAI------KVKPTRPLFLFTCYTDDPEKTKAtvrGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEV 407
Cdd:PRK12467 852 GVVGELYIggaglaRGYHRRPALTAERFVPDPFGADG---GRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEI 928
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 408 ESALIEHPAVLESAVVSSPDPIRGEVVkAFVVLTPNYVSHDPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKI 487
Cdd:PRK12467 929 EARLLAQPGVREAVVLAQPGDAGLQLV-AYLVPAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKL 1007
|
....*....
gi 2024458455 488 RRNELRQKE 496
Cdd:PRK12467 1008 DRKALPKPD 1016
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
257-492 |
4.87e-16 |
|
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: 80.60 E-value: 4.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 257 FNSLRHCVSAGEPI---NP--EVMAKwkawTGLDIHECYGQTETVLVcgnfKGMEIKPGS-------MGKPSPGYDVKII 324
Cdd:cd17656 244 PTCVKHIITAGEQLvitNEfkEMLHE----HNVHLHNHYGPSETHVV----TTYTINPEAeipelppIGKPISNTWIYIL 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 325 DENGNILPPGKEGEIAIK-VKPTRPLFLFTCYTDD---PEKTKATVRgdFYVTGDRGLMDEDGYFWFVGRADDVINSAGY 400
Cdd:cd17656 316 DQEQQLQPQGIVGELYISgASVARGYLNRQELTAEkffPDPFDPNER--MYRTGDLARYLPDGNIEFLGRADHQVKIRGY 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 401 RIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVltpnyvshdPEKMM--KDLQDHVKKATAPYKYPRKMEFVRE 478
Cdd:cd17656 394 RIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV---------MEQELniSQLREYLAKQLPEYMIPSFFVPLDQ 464
|
250
....*....|....
gi 2024458455 479 LPKTISGKIRRNEL 492
Cdd:cd17656 465 LPLTPNGKVDRKAL 478
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
259-492 |
8.34e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 80.98 E-value: 8.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 259 SLRHCVSAGEPINPEVMAKWKA-WTGLDIHECYGQTETVLV-----CGNFKGMEIKPGSMGKPSPGYDVKIIDENGNILP 332
Cdd:PRK12467 3352 SLDIYVFGGEAVPPAAFEQVKRkLKPRGLTNGYGPTEAVVTvtlwkCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVP 3431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 333 PGKEGEIAIKVKPT------RPLFLFTCYTDDPEKTKAtvrGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFE 406
Cdd:PRK12467 3432 VGVAGELYIGGVGLargyhqRPSLTAERFVADPFSGSG---GRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGE 3508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 407 VESALIEHPAVLESAVVSSpDPIRGEVVKAFVVLtpnyvsHDPEKMMKD-LQDHVKKATAPYKYPRKMEFVRELPKTISG 485
Cdd:PRK12467 3509 IEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVP------ADPQGDWREtLRDHLAASLPDYMVPAQLLVLAAMPLGPNG 3581
|
....*..
gi 2024458455 486 KIRRNEL 492
Cdd:PRK12467 3582 KVDRKAL 3588
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
258-492 |
8.66e-16 |
|
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: 79.37 E-value: 8.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 258 NSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTETVLVCGN--FKGMEIKPGSMGKPSPGYDVKIIDENGNILPPGK 335
Cdd:cd17648 207 PHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNHKrfFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 336 EGEIAIK---VKP--------TRPLFLFTCYTDDPEKTKATvRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGP 404
Cdd:cd17648 287 VGELYLGgdgVARgylnrpelTAERFLPNPFQTEQERARGR-NARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEP 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 405 FEVESALIEHPAVLESAVVSSPDP-IRGEVVKAFVVltpNYVSHDPEKMMK-DLQDHVKKATAPYKYPRKMEFVRELPKT 482
Cdd:cd17648 366 GEVEAALASYPGVRECAVVAKEDAsQAQSRIQKYLV---GYYLPEPGHVPEsDLLSFLRAKLPRYMVPARLVRLEGIPVT 442
|
250
....*....|
gi 2024458455 483 ISGKIRRNEL 492
Cdd:cd17648 443 INGKLDVRAL 452
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
373-493 |
1.52e-15 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 78.16 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 373 TGDRGLMDeDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVltpnyVSHDPEKM 452
Cdd:PRK07824 238 TDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVV-----GDGGPAPT 311
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2024458455 453 MKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELR 493
Cdd:PRK07824 312 LEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALV 352
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
55-493 |
3.05e-15 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 78.38 E-value: 3.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 55 SDVLDRWAKvekegKKTKNPALwwVDGDGEevkWSFEELGVLSRKAANVLSGAcSLQCGDRVLLLLPRIPEWWLLNVACM 134
Cdd:PRK08279 40 GDVFEEAAA-----RHPDRPAL--LFEDQS---ISYAELNARANRYAHWAAAR-GVGKGDVVALLMENRPEYLAAWLGLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 135 RTG-TVPIPGTQQlTAKDILYRLQKSKAKGVITNDSVASTVESVEADCQSLKFKLLVSEGH---REGWLSFKDLLKTAPS 210
Cdd:PRK08279 109 KLGaVVALLNTQQ-RGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTlddPEGYEDLAAAAAGAPT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 211 DHRCVTTKSQ--HPvAIY-FTSGTTGAPKMTEHSH----CSYGI-----------------------GLTV-------SG 253
Cdd:PRK08279 188 TNPASRSGVTakDT-AFYiYTSGTTGLPKAAVMSHmrwlKAMGGfggllrltpddvlycclplyhntGGTVawssvlaAG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 254 S---------------------CTF----------------------NSLRHCVSAGepINPEVMAKWKAWTGLD-IHEC 289
Cdd:PRK08279 267 AtlalrrkfsasrfwddvrryrATAfqyigelcryllnqppkptdrdHRLRLMIGNG--LRPDIWDEFQQRFGIPrILEF 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 290 YGQTETVLVCGNFKGmeiKPGSMGKpSPGYD------VK--------IIDENGNILP--PGKEGEIAIKVKPTRPlflFT 353
Cdd:PRK08279 345 YAASEGNVGFINVFN---FDGTVGR-VPLWLahpyaiVKydvdtgepVRDADGRCIKvkPGEVGLLIGRITDRGP---FD 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 354 CYTDdPEKTKATV------RGDFYV-TGDrgLM--DEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAV-- 422
Cdd:PRK08279 418 GYTD-PEASEKKIlrdvfkKGDAWFnTGD--LMrdDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVyg 494
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024458455 423 VSSPDpIRGEVVKAFVVLTPnyvshDPEKMMKDLQDHVKKATAPYKYPRkmeFVR---ELPKTISGKIRRNELR 493
Cdd:PRK08279 495 VEVPG-TDGRAGMAAIVLAD-----GAEFDLAALAAHLYERLPAYAVPL---FVRlvpELETTGTFKYRKVDLR 559
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
254-492 |
6.02e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 78.08 E-value: 6.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 254 SCTfnSLRHCVSAGEPINPEVMAK--WKAWTGlDIHECYGQTETVLVCGNFKGMEIKPGS--MGKPSPGYDVKIIDENGN 329
Cdd:PRK12316 768 SCT--SLRRIVCSGEALPADAQEQvfAKLPQA-GLYNLYGPTEAAIDVTHWTCVEEGGDSvpIGRPIANLACYILDANLE 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 330 ILPPGKEGEIAI------KVKPTRPLFLFTCYTDDPektkaTVRGD-FYVTGDRGLMDEDGYFWFVGRADDVINSAGYRI 402
Cdd:PRK12316 845 PVPVGVLGELYLagrglaRGYHGRPGLTAERFVPSP-----FVAGErMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRI 919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 403 GPFEVESALIEHPAVLESAVVSspdpIRGEVVKAFVVLTpNYVSHDPEkmmkDLQDHVKKATAPYKYPRKMEFVRELPKT 482
Cdd:PRK12316 920 ELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLE-SEGGDWRE----ALKAHLAASLPEYMVPAQWLALERLPLT 990
|
250
....*....|
gi 2024458455 483 ISGKIRRNEL 492
Cdd:PRK12316 991 PNGKLDRKAL 1000
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
259-489 |
1.25e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 76.19 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 259 SLRHCVSAGEPINPEVMAKW---KAWTGLD---IHECYGQTETVLV-----CGNfkGMEI------------------KP 309
Cdd:PRK07768 277 SLRFALNGAEPIDPADVEDLldaGARFGLRpeaILPAYGMAEATLAvsfspCGA--GLVVdevdadllaalrravpatKG 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 310 G-----SMGKPSPGYDVKIIDENGNILPPGKEGEIAIKVKPTRPLFLftcytdDPEKTKATVRGD-FYVTGDRGLMDEDG 383
Cdd:PRK07768 355 NtrrlaTLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGYL------TMDGFIPAQDADgWLDTGDLGYLTEEG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 384 YFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPiRGEVVKAFVVLTPNYVSHDPE---KMMKDLQDHV 460
Cdd:PRK07768 429 EVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRLD-AGHSREGFAVAVESNAFEDPAevrRIRHQVAHEV 507
|
250 260 270
....*....|....*....|....*....|.
gi 2024458455 461 KKATApyKYPRKMEFVR--ELPKTISGKIRR 489
Cdd:PRK07768 508 VAEVG--VRPRNVVVLGpgSIPKTPSGKLRR 536
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
87-496 |
1.41e-14 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 75.92 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 87 KWSFEELGVLSRKAANVLSGAcSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVIT 166
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQAQ-GYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 167 NdsvastvesveadcqslkfkllvseghregwlsFKDLLKTAPSDHRCVT-TKSQHPVAIY-FTSGTTGAPK-------- 236
Cdd:cd05939 82 N---------------------------------LLDPLLTQSSTEPPSQdDVNFRDKLFYiYTSGTTGLPKaavivhsr 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 237 ---MTEHSHCSYGI----------------------------GLTV------SGS----------CTFNSL--------- 260
Cdd:cd05939 129 yyrIAAGAYYAFGMrpedvvydclplyhsaggimgvgqallhGSTVvirkkfSASnfwddcvkynCTIVQYigeicryll 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 261 ---------RHCV--SAGEPINPEVmakWKAWTG----LDIHECYGQTETVLVCGNFKGmeiKPGSMG----KPSPGYDV 321
Cdd:cd05939 209 aqppseeeqKHNVrlAVGNGLRPQI---WEQFVRrfgiPQIGEFYGATEGNSSLVNIDN---HVGACGfnsrILPSVYPI 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 322 KII-----------DENGNILP--PGKEGEIAIKVKPTRPLFLFTCYTDDPEKTKATVR-----GD-FYVTGDRGLMDED 382
Cdd:cd05939 283 RLIkvdedtgelirDSDGLCIPcqPGEPGLLVGKIIQNDPLRRFDGYVNEGATNKKIARdvfkkGDsAFLSGDVLVMDEL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 383 GYFWFVGRADDVINSAGYRIGPFEVEsALIEHPAVLESAV---VSSPDpIRGEVVKAFVVLTPNYVshDPEKMMKDLQdh 459
Cdd:cd05939 363 GYLYFKDRTGDTFRWKGENVSTTEVE-GILSNVLGLEDVVvygVEVPG-VEGRAGMAAIVDPERKV--DLDRFSAVLA-- 436
|
490 500 510
....*....|....*....|....*....|....*..
gi 2024458455 460 vkKATAPYKYPRKMEFVRELPKTISGKIRRNELrQKE 496
Cdd:cd05939 437 --KSLPPYARPQFIRLLPEVDKTGTFKLQKTDL-QKE 470
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
259-492 |
2.39e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 76.35 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 259 SLRHCVSAGEPINPEVMAKWKA---WTGLdiHECYGQTETVL-----VC--GNFKGMEIKPgsMGKPSPGYDVKIIDENG 328
Cdd:PRK12467 1835 SLRRVVCGGEALEVEALRPWLErlpDTGL--FNLYGPTETAVdvthwTCrrKDLEGRDSVP--IGQPIANLSTYILDASL 1910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 329 NILPPGKEGEIAI------KVKPTRPLFLFTCYTDDPEktkATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRI 402
Cdd:PRK12467 1911 NPVPIGVAGELYLggvglaRGYLNRPALTAERFVADPF---GTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRI 1987
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 403 GPFEVESALIEHPAVLESAVVSSpDPIRGEVVKAFVV-LTPNYVSHD--PEKMMKDLQDHVKKATAPYKYPRKMEFVREL 479
Cdd:PRK12467 1988 ELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVpTDPGLVDDDeaQVALRAILKNHLKASLPEYMVPAHLVFLARM 2066
|
250
....*....|...
gi 2024458455 480 PKTISGKIRRNEL 492
Cdd:PRK12467 2067 PLTPNGKLDRKAL 2079
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
89-477 |
2.45e-14 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 75.41 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 89 SFEELGVLSRKAANVLSGACSLQCGDRVLLLLPRIPEW---WL------LNVACMRTgtvpipgtqQLTAKDILYRLQKS 159
Cdd:cd05938 7 TYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFlwiWLglaklgCPVAFLNT---------NIRSKSLLHCFRCC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 160 KAKGVITNdsvASTVESVEADCQSLKFK-----LLVSEGHREGWLSFKDLLKTAPSD------HRCVTTKSQhpvAIY-F 227
Cdd:cd05938 78 GAKVLVVA---PELQEAVEEVLPALRADgvsvwYLSHTSNTEGVISLLDKVDAASDEpvpaslRAHVTIKSP---ALYiY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 228 TSGTTGAPKMTEHSH-----CSY---------------------------------GIGLTV------SGSCTFNSLR-- 261
Cdd:cd05938 152 TSGTTGLPKAARISHlrvlqCSGflslcgvtaddviyitlplyhssgfllgiggciELGATCvlkpkfSASQFWDDCRkh 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 262 --------------------------HCV--SAGEPINPEVmakWKAWT----GLDIHECYGQTETVLVCGNFKGmeiKP 309
Cdd:cd05938 232 nvtviqyigellrylcnqpqspndrdHKVrlAIGNGLRADV---WREFLrrfgPIRIREFYGSTEGNIGFFNYTG---KI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 310 GSMGKPS-------P----GYDVK----IIDENGNILP--PGKEGEIAIKVKPTRPlflFTCYTDDPEKTK----ATV-- 366
Cdd:cd05938 306 GAVGRVSylykllfPfeliKFDVEkeepVRDAQGFCIPvaKGEPGLLVAKITQQSP---FLGYAGDKEQTEkkllRDVfk 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 367 RGDFYV-TGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAV--VSSPDpIRGEVVKAFVVLTPN 443
Cdd:cd05938 383 KGDVYFnTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVygVTVPG-HEGRIGMAAVKLKPG 461
|
490 500 510
....*....|....*....|....*....|....
gi 2024458455 444 YvshdpEKMMKDLQDHVKKATAPYKYPRkmeFVR 477
Cdd:cd05938 462 H-----EFDGKKLYQHVREYLPAYARPR---FLR 487
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
313-494 |
3.92e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 74.74 E-value: 3.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 313 GKPSPGYDVKIIDENGNILP-PGKE-GEIAIKvkptRPLFLFTCYTDDpekTKATVRGDFYvTGDRGLMDEDGYFWFVGR 390
Cdd:PRK07008 359 GRVIYGVDMKIVGDDGRELPwDGKAfGDLQVR----GPWVIDRYFRGD---ASPLVDGWFP-TGDVATIDADGFMQITDR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 391 ADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNY-VSHDpekmmkDLQDHVKKATAPYKY 469
Cdd:PRK07008 431 SKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAeVTRE------ELLAFYEGKVAKWWI 504
|
170 180
....*....|....*....|....*
gi 2024458455 470 PRKMEFVRELPKTISGKIRRNELRQ 494
Cdd:PRK07008 505 PDDVVFVDAIPHTATGKLQKLKLRE 529
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
313-495 |
8.68e-14 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 73.63 E-value: 8.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 313 GKPSPGYDVKIIDENGNILP-PGKE-GEIAIKvkptrplflftcytdDPEKTKATVRGD--------FYVTGDRGLMDED 382
Cdd:PRK06018 359 GYPPFGVEMKITDDAGKELPwDGKTfGRLKVR---------------GPAVAAAYYRVDgeildddgFFDTGDVATIDAY 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 383 GYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNyVSHDPEKMMKDLQDHVKK 462
Cdd:PRK06018 424 GYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPG-ETATREEILKYMDGKIAK 502
|
170 180 190
....*....|....*....|....*....|...
gi 2024458455 463 atapYKYPRKMEFVRELPKTISGKIRRNELRQK 495
Cdd:PRK06018 503 ----WWMPDDVAFVDAIPHTATGKILKTALREQ 531
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
259-492 |
1.13e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 74.22 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 259 SLRHCVSAGEPINPEVMAKWkaWTGLD---IHECYGQTETVLVCGNFKGMEIKPGS-----MGKPSPGYDVKIIDENGNI 330
Cdd:PRK12316 2262 AVRVYCFGGEAVPAASLRLA--WEALRpvyLFNGYGPTEAVVTPLLWKCRPQDPCGaayvpIGRALGNRRAYILDADLNL 2339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 331 LPPGKEGEIAI------KVKPTRPLFLFTCYTDDPektKATVRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGP 404
Cdd:PRK12316 2340 LAPGMAGELYLggeglaRGYLNRPGLTAERFVPDP---FSASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIEL 2416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 405 FEVESALIEHPAVLESAVVSSpDPIRGEVVKAFVVltPNYVSHDpekMMKDLQDHVKKATAPYKYPRKMEFVRELPKTIS 484
Cdd:PRK12316 2417 GEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVV--PDDAAED---LLAELRAWLAARLPAYMVPAHWVVLERLPLNPN 2490
|
....*...
gi 2024458455 485 GKIRRNEL 492
Cdd:PRK12316 2491 GKLDRKAL 2498
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
274-492 |
1.24e-13 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 72.89 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 274 VMAKWKAW------TGLDIHECYGQTETVLVCGNFK-GMEIKPGS----MGKPSPGYDVKIIDENGNILPPGKEGEIAIK 342
Cdd:cd17650 223 CKAQDFKTlaarfgQGMRIINSYGVTEATIDSTYYEeGRDPLGDSanvpIGRPLPNTAMYVLDERLQPQPVGVAGELYIG 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 343 VKPtrplfLFTCYTDDPEKTK---------ATVRgdFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIE 413
Cdd:cd17650 303 GAG-----VARGYLNRPELTAerfvenpfaPGER--MYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLAR 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 414 HPAVLESAVVSSPDPiRGEV-VKAFVVltpnyVSHDPEkmMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNEL 492
Cdd:cd17650 376 HPAIDEAVVAVREDK-GGEArLCAYVV-----AAATLN--TAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
285-493 |
2.99e-13 |
|
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: 71.62 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 285 DIHECYGQTETVLVCGNFKGmeiKPGSMGKPSPG-----------YDVK----IIDENGNI--LPPGKEGEIAIKVKPTR 347
Cdd:cd05940 222 RIAEFYAATEGNSGFINFFG---KPGAIGRNPSLlrkvaplalvkYDLEsgepIRDAEGRCikVPRGEPGLLISRINPLE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 348 PlflFTCYTDDPEKTKATVR-----GD-FYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESA 421
Cdd:cd05940 299 P---FDGYTDPAATEKKILRdvfkkGDaWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEAN 375
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024458455 422 V--VSSPDpIRGEVVKAFVVLTPNYvshdpEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELR 493
Cdd:cd05940 376 VygVQVPG-TDGRAGMAAIVLQPNE-----EFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLR 443
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
259-492 |
1.04e-12 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 69.81 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 259 SLRHCVSAGEPINPEVMAKWKAWTGLDIHEC--YGQTETVLVCGNFK-GMEIKPGSMGKPSPGYDVKIIDENGNilppGK 335
Cdd:cd17654 239 SLRVLALGGEPFPSLVILSSWRGKGNRTRIFniYGITEVSCWALAYKvPEEDSPVQLGSPLLGTVIEVRDQNGS----EG 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 336 EGEIAIKVKPTRplflftCYTDDPEktkATVRGDFYVTGDRgLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHP 415
Cdd:cd17654 315 TGQVFLGGLNRV------CILDDEV---TVPKGTMRATGDF-VTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCL 384
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024458455 416 AVLESAVVSSPDpirgEVVKAFVVLTPnyvSHDPEKmmKDLQDHVKkatAPYKYPRKMEFVRELPKTISGKIRRNEL 492
Cdd:cd17654 385 GVESCAVTLSDQ----QRLIAFIVGES---SSSRIH--KELQLTLL---SSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
252-499 |
1.63e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 70.58 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 252 SGSCTfnSLRHCVSAGEPINPEVMAK-WKAWTGLDIHECYGQTETVL-----VCGNFKGmEIKPgsMGKPSPGYDVKIID 325
Cdd:PRK05691 1384 AAACT--SLRRLFSGGEALPAELRNRvLQRLPQVQLHNRYGPTETAInvthwQCQAEDG-ERSP--IGRPLGNVLCRVLD 1458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 326 ENGNILPPGKEGEIAI-----------KVKPTRPLFLFTCYTDDPEKtkatvrgdFYVTGDRGLMDEDGYFWFVGRADDV 394
Cdd:PRK05691 1459 AELNLLPPGVAGELCIggaglargylgRPALTAERFVPDPLGEDGAR--------LYRTGDRARWNADGALEYLGRLDQQ 1530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 395 INSAGYRIGPFEVESALIEHPAVLESAVVsspdpIRGEVVKAFVVltpNYVShdPEKMMKDLQDHVKKATA----PYKYP 470
Cdd:PRK05691 1531 VKLRGFRVEPEEIQARLLAQPGVAQAAVL-----VREGAAGAQLV---GYYT--GEAGQEAEAERLKAALAaelpEYMVP 1600
|
250 260
....*....|....*....|....*....
gi 2024458455 471 RKMEFVRELPKTISGKIRRNELRQKEWRR 499
Cdd:PRK05691 1601 AQLIRLDQMPLGPSGKLDRRALPEPVWQQ 1629
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
120-493 |
1.78e-12 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 69.46 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 120 LPRIPEWWLLNVACMRTGTVPIPGTQQLTAKDILYRLQKSKAKGVITNDSV----------ASTVESVEADCQSLKfkll 189
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVlrggralplySKVVEAAPAKAIVLP---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 190 VSEGH-----REGWLSFKDLLKTA-------PSDHRCVTTKSQHPVAIYFTSGTTGAPKMTEHSHCS------------- 244
Cdd:PLN03051 77 AAGEPvavplREQDLSWCDFLGVAaaqgsvgGNEYSPVYAPVESVTNILFSSGTTGEPKAIPWTHLSplrcasdgwahmd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 245 --------------YGIGLTVSGSCTFNSLRHCVSAGEPIN------------------PEVMAKWKA----------WT 282
Cdd:PLN03051 157 iqpgdvvcwptnlgWMMGPWLLYSAFLNGATLALYGGAPLGrgfgkfvqdagvtvlglvPSIVKAWRHtgafamegldWS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 283 GL-------------DIH-------------ECYGQTEtvLVCGNFKGMEIKP---GSMGKPSPGYDVKIIDENGNILPP 333
Cdd:PLN03051 237 KLrvfastgeasavdDVLwlssvrgyykpviEYCGGTE--LASGYISSTLLQPqapGAFSTASLGTRFVLLNDNGVPYPD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 334 GKE--GEIAIkvkptRPLFLFTcytddpekTKATVRGDFYVT------------------GDRGLMDEDGYFWFVGRADD 393
Cdd:PLN03051 315 DQPcvGEVAL-----APPMLGA--------SDRLLNADHDKVyykgmpmygskgmplrrhGDIMKRTPGGYFCVQGRADD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 394 VINSAGYRIGPFEVESALIE-HPAVLESAVVSSPDPIRGE----VVKAFVVLTPNYVSHDPEKMMKDLQDHVKKATAPYK 468
Cdd:PLN03051 382 TMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGPellvIFLVLGEEKKGFDQARPEALQKKFQEAIQTNLNPLF 461
|
490 500
....*....|....*....|....*
gi 2024458455 469 YPRKMEFVRELPKTISGKIRRNELR 493
Cdd:PLN03051 462 KVSRVKIVPELPRNASNKLLRRVLR 486
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
89-423 |
2.31e-12 |
|
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: 69.03 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 89 SFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPI---PGTQQLTAKDILYRLQKSKAKGVI 165
Cdd:cd05910 4 SFRELDERSDRIAQGLT-AYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVlidPGMGRKNLKQCLQEAEPDAFIGIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 166 TNDSVASTVES----------------VEADCQSLKFKLLVSEGHRE--GWLSFKdLLKTA--------PSDHRC----- 214
Cdd:cd05910 83 KADEPAAILFTsgstgtpkgvvyrhgtFAAQIDALRQLYGIRPGEVDlaTFPLFA-LFGPAlgltsvipDMDPTRparad 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 215 ----VTTKSQHPVAIYFtsgttGAPKMTEhshcsygiglTVSGSC-----TFNSLRHCVSAGEPINPEVMAKWKAWT--G 283
Cdd:cd05910 162 pqklVGAIRQYGVSIVF-----GSPALLE----------RVARYCaqhgiTLPSLRRVLSAGAPVPIALAARLRKMLsdE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 284 LDIHECYGQTETVLVCgNFKGMEI--------KPGS---MGKPSPGYDVKIID---------ENGNILPPGKEGEIAIK- 342
Cdd:cd05910 227 AEILTPYGATEALPVS-SIGSRELlatttaatSGGAgtcVGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVTg 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 343 --VKPTrplflftcYTDDPEKTKATVRGD-----FYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHP 415
Cdd:cd05910 306 ptVTPT--------YVNRPVATALAKIDDnsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHP 377
|
....*...
gi 2024458455 416 AVLESAVV 423
Cdd:cd05910 378 GVRRSALV 385
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
244-492 |
3.26e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 69.43 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 244 SYGIGLT--VSGSCTFNSLRHCVSAGEPINPEVMAKWK-AWTGLDIHECYGQTETV---LVCGNFKGMEIKPGS--MGKP 315
Cdd:PRK05691 2432 SYGSQLAqwLAGQGEQLPVRMCITGGEALTGEHLQRIRqAFAPQLFFNAYGPTETVvmpLACLAPEQLEEGAASvpIGRV 2511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 316 SPGYDVKIIDENGNILPPGKEGEIAIKVKPT------RPLFLFTCYTDDPEKTKAtvrGDFYVTGDRGLMDEDGYFWFVG 389
Cdd:PRK05691 2512 VGARVAYILDADLALVPQGATGELYVGGAGLaqgyhdRPGLTAERFVADPFAADG---GRLYRTGDLVRLRADGLVEYVG 2588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 390 RADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYVSHDPEKMMKDLQDHVKKATAPYKY 469
Cdd:PRK05691 2589 RIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVSAVAGQDDEAQAALREALKAHLKQQLPDYMV 2668
|
250 260
....*....|....*....|...
gi 2024458455 470 PRKMEFVRELPKTISGKIRRNEL 492
Cdd:PRK05691 2669 PAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
65-495 |
4.25e-12 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 68.57 E-value: 4.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 65 EKEGKKTKNPALWWVD--GDGEEV-KWSFEELGVLSRKAANVLSGAcSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPI 141
Cdd:PLN03052 183 PKPSKTDDSIAIIWRDegSDDLPVnRMTLSELRSQVSRVANALDAL-GFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVV 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 142 PGTQQLTAKDILYRLQKSKAKGVITNDSV-----------------ASTVESVEADCQSLKFKLlvseghREGWLSFKDL 204
Cdd:PLN03052 262 SIADSFAPSEIATRLKISKAKAIFTQDVIvrggksiplysrvveakAPKAIVLPADGKSVRVKL------REGDMSWDDF 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 205 LKTA-----PSDHRCVTTKSQHPVAIYFTSGTTGAPKMTEHSHCS---------------------------YGIGLTVS 252
Cdd:PLN03052 336 LARAnglrrPDEYKAVEQPVEAFTNILFSSGTTGEPKAIPWTQLTplraaadawahldirkgdivcwptnlgWMMGPWLV 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 253 GSCTFNSLRHCVSAGEPIN------------------PEVMAKWKA---WTGLD-------------------------- 285
Cdd:PLN03052 416 YASLLNGATLALYNGSPLGrgfakfvqdakvtmlgtvPSIVKTWKNtncMAGLDwssircfgstgeassvddylwlmsra 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 286 ----IHECYGQTEtvLVCGNFKGMEIKPGSMGK---PSPGYDVKIIDENGNILP---PGKeGEIAIKvkptrPLFL---- 351
Cdd:PLN03052 496 gykpIIEYCGGTE--LGGGFVTGSLLQPQAFAAfstPAMGCKLFILDDSGNPYPddaPCT-GELALF-----PLMFgass 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 352 -------FTCYTDD-PEKTKATVR--GD-FYVTgdrglmdEDGYFWFVGRADDVINSAGYRIGPFEVE----SAlieHPA 416
Cdd:PLN03052 568 tllnadhYKVYFKGmPVFNGKILRrhGDiFERT-------SGGYYRAHGRADDTMNLGGIKVSSVEIErvcnAA---DES 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 417 VLESAVVSSPDPIRG--EVVKAFVVLTPNYVSHDPEKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNELRQ 494
Cdd:PLN03052 638 VLETAAIGVPPPGGGpeQLVIAAVLKDPPGSNPDLNELKKIFNSAIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQ 717
|
.
gi 2024458455 495 K 495
Cdd:PLN03052 718 Q 718
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
311-495 |
5.39e-12 |
|
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: 67.90 E-value: 5.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 311 SMGKPSPGYDVKIIDENGNILPPGKEGEIAIKVKPTRPlflftCYTDDPEKTKATVRGDFYV-TGDRGLMdEDGYFWFVG 389
Cdd:cd05908 315 EVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTP-----GYYNNPEATAKVFTDDGWLkTGDLGFI-RNGRLVITG 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 390 RADDVINSAGYRIGPFEVESALIEHPAVLESAVVS---SPDPIRGEVVKAFVVLTPNyvSHDPEKMMKDLQDHVKKATA- 465
Cdd:cd05908 389 REKDIIFVNGQNVYPHDIERIAEELEGVELGRVVAcgvNNSNTRNEEIFCFIEHRKS--EDDFYPLGKKIKKHLNKRGGw 466
|
170 180 190
....*....|....*....|....*....|..
gi 2024458455 466 --PYKYPrkmefVRELPKTISGKIRRNELRQK 495
Cdd:cd05908 467 qiNEVLP-----IRRIPKTTSGKVKRYELAQR 493
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
64-492 |
8.44e-12 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 67.76 E-value: 8.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 64 VEKEGKKTKN-PALwwVDGDgeeVKWSFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLNVACMRTGTVPIP 142
Cdd:PRK10252 464 VAQQAAKTPDaPAL--ADAR---YQFSYREMREQVVALANLLR-ERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 143 -GTQQLTAKdILYRLQKSKAKGVITNDSVASTVesveADCQSLKFkllvseghregwLSFKDLLkTAPSDHRCVTTKSQH 221
Cdd:PRK10252 538 lDTGYPDDR-LKMMLEDARPSLLITTADQLPRF----ADVPDLTS------------LCYNAPL-APQGAAPLQLSQPHH 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 222 PVAIYFTSGTTGAPK--MTEHS---------HCSYGIGLT------------VS----------GSC------------- 255
Cdd:PRK10252 600 TAYIIFTSGSTGRPKgvMVGQTaivnrllwmQNHYPLTADdvvlqktpcsfdVSvweffwpfiaGAKlvmaepeahrdpl 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 256 -----------------------------------TFNSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTE-TVLVC 299
Cdd:PRK10252 680 amqqffaeygvttthfvpsmlaafvasltpegarqSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEaAVDVS 759
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 300 GNFKGMEIKPGSMGKPSP-GYDV-----KIIDENGNILPPGKEGEIAIK-VKptrplfLFTCYTDDPEKTKATVRGD--- 369
Cdd:PRK10252 760 WYPAFGEELAAVRGSSVPiGYPVwntglRILDARMRPVPPGVAGDLYLTgIQ------LAQGYLGRPDLTASRFIADpfa 833
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 370 ----FYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLES---AVVSSPDPIRGEVVKAFV--VL 440
Cdd:PRK10252 834 pgerMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAvthACVINQAAATGGDARQLVgyLV 913
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2024458455 441 TPNYVSHDpekmMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNEL 492
Cdd:PRK10252 914 SQSGLPLD----TSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
236-411 |
1.05e-11 |
|
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: 67.00 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 236 KMTEHSHCSYGIGLT-------VSGSCTFNSLRHCVSAGEPINPEVMakwKAWTGLDI--HECYGQTE-----TVLVCGN 301
Cdd:cd05933 291 LMGGESPSPLFYRLAkklvfkkVRKALGLDRCQKFFTGAAPISRETL---EFFLSLNIpiMELYGMSEtsgphTISNPQA 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 302 FKgmeikPGSMGKPSPGYDVKIIDENGNilppgKEGEIAIkvkptRPLFLFTCYTDDPEKTKATVRGDFYV-TGDRGLMD 380
Cdd:cd05933 368 YR-----LLSCGKALPGCKTKIHNPDAD-----GIGEICF-----WGRHVFMGYLNMEDKTEEAIDEDGWLhSGDLGKLD 432
|
170 180 190
....*....|....*....|....*....|..
gi 2024458455 381 EDGYFWFVGRADDVINSA-GYRIGPFEVESAL 411
Cdd:cd05933 433 EDGFLYITGRIKELIITAgGENVPPVPIEDAV 464
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
52-487 |
3.46e-11 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 65.59 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 52 NFASDVLdRWAKVEKegkktknPALWWVDGDGEEVKWSFEELGVLSRKAANVLSgACSLQCGDRVLLLLPRIPEWWLLNV 131
Cdd:PRK03584 87 NYAENLL-RHRRDDR-------PAIIFRGEDGPRRELSWAELRRQVAALAAALR-ALGVGPGDRVAAYLPNIPETVVAML 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 132 ACMRTGTV-----PIPGTQQltakdILYRLQKSKAKGVITNDS----------------VASTVESVEADCQSLKFKLLV 190
Cdd:PRK03584 158 ATASLGAIwsscsPDFGVQG-----VLDRFGQIEPKVLIAVDGyryggkafdrrakvaeLRAALPSLEHVVVVPYLGPAA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 191 SEGHREGWLSFKDLLKTAPSDH-RCVTTKSQHPVAIYFTSGTTGAPKMTEHSH--------------------------- 242
Cdd:PRK03584 233 AAAALPGALLWEDFLAPAEAAElEFEPVPFDHPLWILYSSGTTGLPKCIVHGHggillehlkelglhcdlgpgdrffwyt 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 243 -CSY--------------------------------------GI----------------GLTVSGSCTFNSLRHCVSAG 267
Cdd:PRK03584 313 tCGWmmwnwlvsgllvgatlvlydgspfypdpnvlwdlaaeeGVtvfgtsakyldacekaGLVPGETHDLSALRTIGSTG 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 268 EPINPE----VMAKWKAwtglDIH--ECYGQTEtvlVCGNFKG----MEIKPGSMGKPSPGYDVKIIDENGNilpP--GK 335
Cdd:PRK03584 393 SPLPPEgfdwVYEHVKA----DVWlaSISGGTD---ICSCFVGgnplLPVYRGEIQCRGLGMAVEAWDEDGR---PvvGE 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 336 EGEIAI-KVKPTRPLFLFtcytDDPEKTKatVR-------------GDFYVTGDRGlmdedGYFwFVGRADDVINSAGYR 401
Cdd:PRK03584 463 VGELVCtKPFPSMPLGFW----NDPDGSR--YRdayfdtfpgvwrhGDWIEITEHG-----GVV-IYGRSDATLNRGGVR 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 402 IGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYVSHDPekMMKDLQDHVKKATAPYKYPRKMEFVRELPK 481
Cdd:PRK03584 531 IGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDDA--LRARIRTTIRTNLSPRHVPDKIIAVPDIPR 608
|
....*.
gi 2024458455 482 TISGKI 487
Cdd:PRK03584 609 TLSGKK 614
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
257-487 |
5.09e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 65.37 E-value: 5.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 257 FNSLRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTET--VLVCGNfkGMEIKPGSMGKPSPGYDVKI-----IDENGN 329
Cdd:PRK06814 906 FRSLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETapVIALNT--PMHNKAGTVGRLLPGIEYRLepvpgIDEGGR 983
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 330 ILPPGkegeiaikvkPTrpLFLFTCYTDDPEKTKATVRGdFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVES 409
Cdd:PRK06814 984 LFVRG----------PN--VMLGYLRAENPGVLEPPADG-WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEE 1050
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024458455 410 ALIEHPAVLESAVVSSPDPIRGEVVkafVVLTpnyVSHDPEKmmKDLQDHVKKATAPYKY-PRKMEFVRELPKTISGKI 487
Cdd:PRK06814 1051 LAAELWPDALHAAVSIPDARKGERI---ILLT---TASDATR--AAFLAHAKAAGASELMvPAEIITIDEIPLLGTGKI 1121
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
248-492 |
6.13e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 65.57 E-value: 6.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 248 GLTVSGSCTFNSLRHCVSAGEPINPEVMAKW-KAWTGLDIHECYGQTETVLVCGNFK-GMEIKPGS---MGKPSPGYDVK 322
Cdd:PRK05691 3973 GMLAEDRQALDGLRWMLPTGEAMPPELARQWlQRYPQIGLVNAYGPAECSDDVAFFRvDLASTRGSylpIGSPTDNNRLY 4052
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 323 IIDENGNILPPGKEGEIAIK-VKPTRPlflftcYTDDPEKT-KATVRGDF-------YVTGDRGLMDEDGYFWFVGRADD 393
Cdd:PRK05691 4053 LLDEALELVPLGAVGELCVAgTGVGRG------YVGDPLRTaLAFVPHPFgapgerlYRTGDLARRRSDGVLEYVGRIDH 4126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 394 VINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPiRGEVVKAFvvLTPNYVSHDPEKMMKDLQDHVKKATAPYKYPRKM 473
Cdd:PRK05691 4127 QVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGV-NGKHLVGY--LVPHQTVLAQGALLERIKQRLRAELPDYMVPLHW 4203
|
250
....*....|....*....
gi 2024458455 474 EFVRELPKTISGKIRRNEL 492
Cdd:PRK05691 4204 LWLDRLPLNANGKLDRKAL 4222
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
313-494 |
1.29e-10 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 63.49 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 313 GKPSPGYDVKIIDENGNILPPGKEGEIAIKvKPTrplfLFTCYTDDPEKTKATVRGDFYVTGDRGLMdEDGYFWFVGRAD 392
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICVR-GPS----LMSGYFRDEESQDVLAADGWLDTGDLGYL-LDGYLYITGRAK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 393 DVINSAGYRIGPFEVESALIEHPAVL--ESAVVSSPDPiRGEVVkafVVLTPNYVShDPE---KMMKDLQDHVKKATApy 467
Cdd:PRK09192 462 DLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQE-NGEKI---VLLVQCRIS-DEErrgQLIHALAALVRSEFG-- 534
|
170 180
....*....|....*....|....*....
gi 2024458455 468 kYPRKMEFV--RELPKTISGKIRRNELRQ 494
Cdd:PRK09192 535 -VEAAVELVppHSLPRTSSGKLSRAKAKK 562
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
267-497 |
8.26e-09 |
|
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: 57.83 E-value: 8.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 267 GEPINPEVMAKWKAWTGL-DIHECYGQTETVLVCGNFKGMEIKPGSMGKPSP------GYD---VKIIDENGNIL----- 331
Cdd:cd05937 209 GNGLRPDIWERFRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLirrwkfENQvvlVKMDPETDDPIrdpkt 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 332 ------PPGKEGEIAIKVkPTRPLFLFTCYTDDPEKTKATV------RGD-FYVTGDRGLMDEDGYFWFVGRADDVINSA 398
Cdd:cd05937 289 gfcvraPVGEPGEMLGRV-PFKNREAFQGYLHNEDATESKLvrdvfrKGDiYFRTGDLLRQDADGRWYFLDRLGDTFRWK 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 399 GYRIGPFEVESALIEHPAVLESAVVSSPDP-IRGEVVKAFVVLTPNYVSHDPEKMMKdLQDHVKKATAPYKYPRKMEFVR 477
Cdd:cd05937 368 SENVSTTEVADVLGAHPDIAEANVYGVKVPgHDGRAGCAAITLEESSAVPTEFTKSL-LASLARKNLPSYAVPLFLRLTE 446
|
250 260
....*....|....*....|
gi 2024458455 478 ELPKTISGKIRRNELRQKEW 497
Cdd:cd05937 447 EVATTDNHKQQKGVLRDEGV 466
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
264-428 |
6.79e-08 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 54.91 E-value: 6.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 264 VSAGEPINPEVMAKWKAWTGLDIHECYGQTETvlVCGNFKGM--EIKPGSMGKPSPGYDVKIID--E-NGNILPPGKEGE 338
Cdd:cd05927 280 LTGSAPLSPEVLEFLRVALGCPVLEGYGQTEC--TAGATLTLpgDTSVGHVGGPLPCAEVKLVDvpEmNYDAKDPNPRGE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 339 IAIKvKPTrplfLFTCYTDDPEKTKATVRGD-FYVTGDRGLMDEDGYFWFVGRADDVIN-SAGYRIGPFEVESALIEHPA 416
Cdd:cd05927 358 VCIR-GPN----VFSGYYKDPEKTAEALDEDgWLHTGDIGEWLPNGTLKIIDRKKNIFKlSQGEYVAPEKIENIYARSPF 432
|
170 180
....*....|....*....|....
gi 2024458455 417 V---------LES---AVVsSPDP 428
Cdd:cd05927 433 VaqifvygdsLKSflvAIV-VPDP 455
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
366-492 |
1.19e-07 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 54.06 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 366 VRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLES------------AVVS--SPDPIRG 431
Cdd:cd17647 369 PRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENitlvrrdkdeepTLVSyiVPRFDKP 448
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024458455 432 EVVKAFVVLTPNYVSHDP--------EKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKIRRNEL 492
Cdd:cd17647 449 DDESFAQEDVPKEVSTDPivkgligyRKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
259-494 |
1.59e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 53.62 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 259 SLRHCVSAGEPINPEVMAKWKAWT---GLD---IHECYGQTE-----TVLVCGNfkGMEIKPGSM------------GKP 315
Cdd:PRK05851 273 ALRVALNGGEPVDCDGFERFATAMapfGFDagaAAPSYGLAEstcavTVPVPGI--GLRVDEVTTddgsgarrhavlGNP 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 316 SPGYDVKIIDENGNILPPGKE-GEIAIkvkptRPLFLFTCYT-DDPEKtkatvRGDFYVTGDRGLMDEDGYFwFVGRADD 393
Cdd:PRK05851 351 IPGMEVRISPGDGAAGVAGREiGEIEI-----RGASMMSGYLgQAPID-----PDDWFPTGDLGYLVDGGLV-VCGRAKE 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 394 VINSAGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGevVKAFVVLTPNYVSHDPEKMMKDLQDHVkkATAPYKYPRKM 473
Cdd:PRK05851 420 LITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGS--ARPGLVIAAEFRGPDEAGARSEVVQRV--ASECGVVPSDV 495
|
250 260
....*....|....*....|...
gi 2024458455 474 EFVR--ELPKTISGKIRRNELRQ 494
Cdd:PRK05851 496 VFVApgSLPRTSSGKLRRLAVKR 518
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
260-436 |
1.84e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 50.48 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 260 LRHCVSAGEPINPEVMAKWKAWTGLDIHECYGQTETVLVCGNFKGMEIKPGSMGKPSPGYDVKIIDengniLP------- 332
Cdd:PLN02736 378 VRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVD-----VPemnytse 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 333 --PGKEGEIAIKvKPTrplfLFTCYTDDPEKTKATVRGDFYV-TGDRGLMDEDGYFWFVGRADDVINSA-GYRIGPFEVE 408
Cdd:PLN02736 453 dqPYPRGEICVR-GPI----IFKGYYKDEVQTREVIDEDGWLhTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPEKIE 527
|
170 180 190
....*....|....*....|....*....|....*....
gi 2024458455 409 SALIEHPAVLESAV-----------VSSPDPirgEVVKA 436
Cdd:PLN02736 528 NVYAKCKFVAQCFVygdslnsslvaVVVVDP---EVLKA 563
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
358-487 |
3.45e-05 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 46.60 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 358 DPEKTKAT------VRGDFYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLE------------ 419
Cdd:TIGR03443 661 DKENNKPErefwlgPRDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVREnvtlvrrdkdee 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 420 ----SAVVSSPDPirgEVVKAFVVLTPNYVSHDP--------EKMMKDLQDHVKKATAPYKYPRKMEFVRELPKTISGKI 487
Cdd:TIGR03443 741 ptlvSYIVPQDKS---DELEEFKSEVDDEESSDPvvkglikyRKLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKV 817
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
290-390 |
1.93e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 44.20 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 290 YGQTETVLVCGNFKGMEIKPGSMGKPSPGYDVKI--IDENGNILPPGKEGEIAIkvkptRPLFLFTCYTDDPEKTKATVR 367
Cdd:PTZ00216 459 WGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLldTEEYKHTDTPEPRGEILL-----RGPFLFKGYYKQEELTREVLD 533
|
90 100
....*....|....*....|....
gi 2024458455 368 GD-FYVTGDRGLMDEDGYFWFVGR 390
Cdd:PTZ00216 534 EDgWFHTGDVGSIAANGTLRIIGR 557
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
264-432 |
2.77e-04 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 43.60 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 264 VSAGEPINPEvMAKWKAWT-GLDIHECYGQTETvlvcgnfkGMEIKPGSMGKPsPGYDVKIID--ENGNILP--PGKEGE 338
Cdd:cd17632 368 VCGSAPLSAE-MKAFMESLlDLDLHDGYGSTEA--------GAVILDGVIVRP-PVLDYKLVDvpELGYFRTdrPHPRGE 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 339 IAIKVKPtrplfLFTCYTDDPEKTkATVRGD--FYVTGDrgLMDEDG--YFWFVGRADDVIN-SAGYRIGPFEVESALIE 413
Cdd:cd17632 438 LLVKTDT-----LFPGYYKRPEVT-AEVFDEdgFYRTGD--VMAELGpdRLVYVDRRNNVLKlSQGEFVTVARLEAVFAA 509
|
170 180 190
....*....|....*....|....*....|..
gi 2024458455 414 HPAV-------------LESAVVSSPDPIRGE 432
Cdd:cd17632 510 SPLVrqifvygnserayLLAVVVPTQDALAGE 541
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
252-414 |
4.94e-04 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 42.50 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 252 SGSCtFNSLRHCVSAGEPINPEVMAK-WKAWTGLDIHECYGQTETVLVCG-NFKGMEIKPGSMGKPSPGYDVKIIDENGN 329
Cdd:PRK06334 294 QESC-LPSLRFVVIGGDAFKDSLYQEaLKTFPHIQLRQGYGTTECSPVITiNTVNSPKHESCVGMPIRGMDVLIVSEETK 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 330 IlpPGKEGEIAIKVkpTRPLFLFTCYT-DDPEKTKATVRGD-FYVTGDRGLMDEDGYFWFVGRADDVINSAGYRIGPFEV 407
Cdd:PRK06334 373 V--PVSSGETGLVL--TRGTSLFSGYLgEDFGQGFVELGGEtWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEAL 448
|
....*..
gi 2024458455 408 ESALIEH 414
Cdd:PRK06334 449 ESILMEG 455
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
259-489 |
5.32e-04 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 42.44 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 259 SLRHCVSAGEPInPEVMAKW--KAWtGLDIHECYGQTET-VLV---CGNFKGMEIKPGSMgkpspgYdVKIID-ENGNIL 331
Cdd:COG1541 204 SLKKGIFGGEPW-SEEMRKEieERW-GIKAYDIYGLTEVgPGVayeCEAQDGLHIWEDHF------L-VEIIDpETGEPV 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 332 PPGKEGEIaikvkptrplfLFTCYTDD--PektkaTVRgdfYVTGDRG-LMDE-----------DGyfwFVGRADDVINS 397
Cdd:COG1541 275 PEGEEGEL-----------VVTTLTKEamP-----LIR---YRTGDLTrLLPEpcpcgrthpriGR---ILGRADDMLII 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 398 AGYRIGPFEVESALIEHPAVLESAVVSSPDPIRGEVVKAFVVLTPNYvshDPEKMMKDLQDHVKKATapyKYPRKMEFVR 477
Cdd:COG1541 333 RGVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVELAPGA---SLEALAEAIAAALKAVL---GLRAEVELVE 406
|
250
....*....|....
gi 2024458455 478 --ELPKTiSGKIRR 489
Cdd:COG1541 407 pgSLPRS-EGKAKR 419
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
288-398 |
9.20e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 42.01 E-value: 9.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 288 ECYGQTETVLVCGNFKGmeIKPGSMGKPSPG--------YDVK----IIDENGnILPPGKEGEIAIKVKPTRPlflftcy 355
Cdd:PRK07868 749 EFFATTDGQAVLANVSG--AKIGSKGRPLPGagrvelaaYDPEhdliLEDDRG-FVRRAEVNEVGVLLARARG------- 818
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2024458455 356 tddPEKTKATVRGDFYVTGDRGL-------MDEDGYFWFVGRADDVINSA 398
Cdd:PRK07868 819 ---PIDPTASVKRGVFAPADTWIsteylfrRDDDGDYWLVDRRGSVIRTA 865
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
281-428 |
2.81e-03 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 40.24 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 281 WTGldihecYGQTE---TVlvCGnfKGMEIKPGsMGKPSPGYDVKIIDEN----GNILPPG--KEGEIaikvkptRPLfl 351
Cdd:PRK09029 268 WCG------YGLTEmasTV--CA--KRADGLAG-VGSPLPGREVKLVDGEiwlrGASLALGywRQGQL-------VPL-- 327
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024458455 352 ftcyTDDpektkatvRGDFYvTGDRGLMDeDGYFWFVGRADDVINSAGYRIGPFEVESALIEHPAVLESAVVSSPDP 428
Cdd:PRK09029 328 ----VND--------EGWFA-TRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADA 390
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
150-244 |
9.26e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 38.80 E-value: 9.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024458455 150 KDILYRLQKSKAKG--VITNDSVASTVESveADCQSLKFKLLVSEGHREGwlsfkdllktapSDHRCVTTKSQHPVA-IY 226
Cdd:PTZ00216 205 PNLLRLMKSGGMPNttIIYLDSLPASVDT--EGCRLVAWTDVVAKGHSAG------------SHHPLNIPENNDDLAlIM 270
|
90
....*....|....*...
gi 2024458455 227 FTSGTTGAPKMTEHSHCS 244
Cdd:PTZ00216 271 YTSGTTGDPKGVMHTHGS 288
|
|
| |
