|
Name |
Accession |
Description |
Interval |
E-value |
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
25-561 |
0e+00 |
|
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: 706.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 25 FHTLSPTSFLPRAAAIEPEAVAIHHVTannqvLRRTYAETADRARGLAYYL---KKHGFKRVGVLCPNTPAFLESIFGIA 101
Cdd:cd12118 1 YVPLTPLSFLERAAAVYPDRTSIVYGD-----RRYTWRQTYDRCRRLASALaalGISRGDTVAVLAPNTPAMYELHFGVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 102 AAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQEFLsllqsyrasrpsipiivdmdtdategelsgpfdevvleglTYD 181
Cdd:cd12118 76 MAGAVLNALNTRLDAEEIAFILRHSEAKVLFVDREFE----------------------------------------YED 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 182 LDTGAKGWPGLEaQAASEDDVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLnshRGRCRYLWTLPMFHACGWTF 261
Cdd:cd12118 116 LLAEGDPDFEWI-PPADEWDPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEM---KQHPVYLWTLPMFHCNGWCF 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 262 PWAVTAVRGTHYCLRKIDYPQIWKLLKQEHITHFNAAPTVNTLLCNSKE--AEPLPEPVHVTVAASPPTPHLFEQMTNLN 339
Cdd:cd12118 192 PWTVAAVGGTNVCLRKVDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPsdARPLPHRVHVMTAGAPPPAAVLAKMEELG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 340 LHPVHVYGMTETYGPITKGYYLPAWDNLPSSERYKKMARQGHGFVTSLPVRVIKTDvaegTVIDVARDGKEIGEIVFVGN 419
Cdd:cd12118 272 FDVTHVYGLTETYGPATVCAWKPEWDELPTEERARLKARQGVRYVGLEEVDVLDPE----TMKPVPRDGKTIGEIVFRGN 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 420 ICARGYYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSH 499
Cdd:cd12118 348 IVMKGYLKNPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEK 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169764941 500 WGERPKAFVTVKPGKFLTGSEVIEWARNAsdISKFMIPREVeVVAELPKTSTGKVRKNILRD 561
Cdd:cd12118 428 WGEVPCAFVELKEGAKVTEEEIIAFCREH--LAGFMVPKTV-VFGELPKTSTGKIQKFVLRD 486
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
23-564 |
0e+00 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 534.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 23 VNFHTLSPTSFLPRAAAIEPEAVAIHHVTannqvLRRTYAETADRARGLAYYLKKHGFKR---VGVLCPNTPAFLESIFG 99
Cdd:PRK08162 13 ANYVPLTPLSFLERAAEVYPDRPAVIHGD-----RRRTWAETYARCRRLASALARRGIGRgdtVAVLLPNIPAMVEAHFG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 100 IAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQEFLSLLQSYRA--SRPSIPIIVDMDTDATEGELSGPFD-EVVLe 176
Cdd:PRK08162 88 VPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAEVAREALAllPGPKPLVIDVDDPEYPGGRFIGALDyEAFL- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 177 gltydldtgAKGWPGLEAQA-ASEDDVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLNSHrgrCRYLWTLPMFH 255
Cdd:PRK08162 167 ---------ASGDPDFAWTLpADEWDAIALNYTSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKH---PVYLWTLPMFH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 256 ACGWTFPWAVTAVRGTHYCLRKIDYPQIWKLLKQEHITHFNAAPTVNTLLCNSKEA--EPLPEPVHVTVAASPPTPHLFE 333
Cdd:PRK08162 235 CNGWCFPWTVAARAGTNVCLRKVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEwrAGIDHPVHAMVAGAAPPAAVIA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 334 QMTNLNLHPVHVYGMTETYGPITKGYYLPAWDNLPSSERYKKMARQGHGFVTSLPVRVIKTDvaegTVIDVARDGKEIGE 413
Cdd:PRK08162 315 KMEEIGFDLTHVYGLTETYGPATVCAWQPEWDALPLDERAQLKARQGVRYPLQEGVTVLDPD----TMQPVPADGETIGE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 414 IVFVGNICARGYYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVV 493
Cdd:PRK08162 391 IMFRGNIVMKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVV 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169764941 494 AVPDSHWGERPKAFVTVKPGKFLTGSEVIEWARnaSDISKFMIPREVeVVAELPKTSTGKVRKNILRDWAK 564
Cdd:PRK08162 471 AKPDPKWGEVPCAFVELKDGASATEEEIIAHCR--EHLAGFKVPKAV-VFGELPKTSTGKIQKFVLREQAK 538
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
24-564 |
2.57e-139 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 415.78 E-value: 2.57e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 24 NFHTLSPTSFLPRAAAIEPEAVAIHHVTannqvLRRTYAETADRARGLAYYLKKHGFKR---VGVLCPNTPAFLESIFGI 100
Cdd:PLN02479 16 NYTALTPLWFLERAAVVHPTRKSVVHGS-----VRYTWAQTYQRCRRLASALAKRSIGPgstVAVIAPNIPAMYEAHFGV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 101 AAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQEFLSLLQSyrasrpSIPIIvdmdTDATEGELSGPFDEVVLE---- 176
Cdd:PLN02479 91 PMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQEFFTLAEE------ALKIL----AEKKKSSFKPPLLIVIGDptcd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 177 --GLTYDLDTGA--------KGWPGLE-AQAASEDDVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLNSHrgrC 245
Cdd:PLN02479 161 pkSLQYALGKGAieyekfleTGDPEFAwKPPADEWQSIALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEG---A 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 246 RYLWTLPMFHACGWTFPWAVTAVRGTHYCLRKIDYPQIWKLLKQEHITHFNAAPTVNTLLCNSKEAE---PLPEPVHVTV 322
Cdd:PLN02479 238 VYLWTLPMFHCNGWCFTWTLAALCGTNICLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSEtilPLPRVVHVMT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 323 AASPPTPHLFEQMTNLNLHPVHVYGMTETYGPITKGYYLPAWDNLPSSERYKKMARQGHGFVTSLPVRVIKTDvaegTVI 402
Cdd:PLN02479 318 AGAAPPPSVLFAMSEKGFRVTHTYGLSETYGPSTVCAWKPEWDSLPPEEQARLNARQGVRYIGLEGLDVVDTK----TMK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 403 DVARDGKEIGEIVFVGNICARGYYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLV 482
Cdd:PLN02479 394 PVPADGKTMGEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 483 THPDILEAGVVAVPDSHWGERPKAFVTVKPgkfltGSEVIEWARNASDISKF--------MIPREVeVVAELPKTSTGKV 554
Cdd:PLN02479 474 THPAVLEASVVARPDERWGESPCAFVTLKP-----GVDKSDEAALAEDIMKFcrerlpayWVPKSV-VFGPLPKTATGKI 547
|
570
....*....|
gi 169764941 555 RKNILRDWAK 564
Cdd:PLN02479 548 QKHVLRAKAK 557
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
28-565 |
2.59e-121 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 369.73 E-value: 2.59e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 28 LSPTSFLPRAAAIEPEAVAIHHVTAnnqvlRRTYAETADRARGLAYYLKKHGFKR---VGVLCPNTPAFLESIFGIAAAG 104
Cdd:PLN03102 14 LTPITFLKRASECYPNRTSIIYGKT-----RFTWPQTYDRCCRLAASLISLNITKndvVSVLAPNTPAMYEMHFAVPMAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 105 AVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQEF-------LSLLQSYRaSRPSIPIIVDMDTDATEGELSGPFDevvLEG 177
Cdd:PLN03102 89 AVLNPINTRLDATSIAAILRHAKPKILFVDRSFeplarevLHLLSSED-SNLNLPVIFIHEIDFPKRPSSEELD---YEC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 178 LTydldtgAKGWPGLEAQAA-----SEDDVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIesglNSHRGRCR-YLWTL 251
Cdd:PLN03102 165 LI------QRGEPTPSLVARmfriqDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAII----GWEMGTCPvYLWTL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 252 PMFHACGWTFPWAVTAVRGTHYCLRKIDYPQIWKLLKQEHITHFNAAPTVNTLLC--NSKEAEPLPEPVHVTVAASPPTP 329
Cdd:PLN03102 235 PMFHCNGWTFTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLkgNSLDLSPRSGPVHVLTGGSPPPA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 330 HLFEQMTNLNLHPVHVYGMTETYGPITKGYYLPAWDNLPSSERYKKMARQGHGFVTSLPVRVIKTDVAEgtviDVARDGK 409
Cdd:PLN03102 315 ALVKKVQRLGFQVMHAYGLTEATGPVLFCEWQDEWNRLPENQQMELKARQGVSILGLADVDVKNKETQE----SVPRDGK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 410 EIGEIVFVGNICARGYYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILE 489
Cdd:PLN03102 391 TMGEIVIKGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 490 AGVVAVPDSHWGERPKAFVTVKPG---------KFLTGS-EVIEWARnaSDISKFMIPREVEVVAELPKTSTGKVRKNIL 559
Cdd:PLN03102 471 TAVVAMPHPTWGETPCAFVVLEKGettkedrvdKLVTRErDLIEYCR--ENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
....*.
gi 169764941 560 RDWAKG 565
Cdd:PLN03102 549 RDIAKG 554
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
33-561 |
2.00e-116 |
|
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: 355.01 E-value: 2.00e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 33 FLPRAAAIEPEAVaIHHVTANNQVLRRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVA 109
Cdd:cd12119 1 LLEHAARLHGDRE-IVSRTHEGEVHRYTYAEVAERARRLANALRRLGVKpgdRVATLAWNTHRHLELYYAVPGMGAVLHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 110 VNYRLKEDDIAYIFTHSDVEAIIVDQEFLSLLQSYRASRPSIPIIVDMDTDATEGELSGP----FDEVVLEGltydldTG 185
Cdd:cd12119 80 INPRLFPEQIAYIINHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAMPEPAGVgvlaYEELLAAE------SP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 186 AKGWPGLEaqaasEDDVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLNSHRGRCrYLWTLPMFHACGWTFPWAV 265
Cdd:cd12119 154 EYDWPDFD-----ENTAAAICYTSGTTGNPKGVVYSHRSLVLHAMAALLTDGLGLSESDV-VLPVVPMFHVNAWGLPYAA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 266 TAVrGTHYCL--RKIDYPQIWKLLKQEHITHFNAAPTVNTLLCNSKEAEP--LPEPVHVTVAASPPTPHLFEQMTNLNLH 341
Cdd:cd12119 228 AMV-GAKLVLpgPYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGrdLSSLRRVVIGGSAVPRSLIEAFEERGVR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 342 PVHVYGMTETYGPITKGYYLPAWDNLPSSERYKKMARQGHgFVTSLPVRVIKTDvaeGTVIDvaRDGKEIGEIVFVGNIC 421
Cdd:cd12119 307 VIHAWGMTETSPLGTVARPPSEHSNLSEDEQLALRAKQGR-PVPGVELRIVDDD---GRELP--WDGKAVGELQVRGPWV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 422 ARGYYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWG 501
Cdd:cd12119 381 TKSYYKNDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWG 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 502 ERPKAFVTVKPGKFLTGSEVIEWARnaSDISKFMIPREVEVVAELPKTSTGKVRKNILRD 561
Cdd:cd12119 461 ERPLAVVVLKEGATVTAEELLEFLA--DKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
31-566 |
1.81e-114 |
|
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: 347.57 E-value: 1.81e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 31 TSFLPRAAAIEPEAVAIHHvtannQVLRRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVN 107
Cdd:COG0318 2 ADLLRRAAARHPDRPALVF-----GGRRLTYAELDARARRLAAALRALGVGpgdRVALLLPNSPEFVVAFLAALRAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 108 VAVNYRLKEDDIAYIFTHSDVEAIIVdqeflsllqsyrasrpsipiivdmdtdategelsgpfdevvlegltydldtgak 187
Cdd:COG0318 77 VPLNPRLTAEELAYILEDSGARALVT------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 188 gwpgleaqaaseddvIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLnshRGRCRYLWTLPMFHACGWTF-PWAVT 266
Cdd:COG0318 103 ---------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGL---TPGDVVLVALPLFHVFGLTVgLLAPL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 267 AVRGTHYCLRKIDYPQIWKLLKQEHITHFNAAPTVNTLLCNSKEAEP--LPEPVHVTVAASPPTPHLFEQMTN-LNLHPV 343
Cdd:COG0318 165 LAGATLVLLPRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARydLSSLRLVVSGGAPLPPELLERFEErFGVRIV 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 344 HVYGMTETYGPITkgyylpawdNLPSSERYKKMARQGHgFVTSLPVRVI---KTDVAEGtvidvardgkEIGEIVFVGNI 420
Cdd:COG0318 245 EGYGLTETSPVVT---------VNPEDPGERRPGSVGR-PLPGVEVRIVdedGRELPPG----------EVGEIVVRGPN 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 421 CARGYYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHW 500
Cdd:COG0318 305 VMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKW 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169764941 501 GERPKAFVTVKPGKFLTGSEVIEWARNAsdISKFMIPREVEVVAELPKTSTGKVRKNILRDWAKGA 566
Cdd:COG0318 385 GERVVAFVVLRPGAELDAEELRAFLRER--LARYKVPRRVEFVDELPRTASGKIDRRALRERYAAG 448
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
57-561 |
4.46e-112 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 344.09 E-value: 4.46e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 57 LRRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIV 133
Cdd:PRK06187 30 RRTTYAELDERVNRLANALRALGVKkgdRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 134 DQEFLSLLQSYRASRPSIP--IIVDMDTDATEGELSGPFDEVvLEGLTYDLDtgakgWPGLEaqaasEDDVIALAYTSGT 211
Cdd:PRK06187 110 DSEFVPLLAAILPQLPTVRtvIVEGDGPAAPLAPEVGEYEEL-LAAASDTFD-----FPDID-----ENDAAAMLYTSGT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 212 TARPKGVEYTHRGCYLAAMGnvIESGLNSHRGRcRYLWTLPMFHACGWTFPWAVTAVRGTHYCLRKIDYPQIWKLLKQEH 291
Cdd:PRK06187 179 TGHPKGVVLSHRNLFLHSLA--VCAWLKLSRDD-VYLVIVPMFHVHAWGLPYLALMAGAKQVIPRRFDPENLLDLIETER 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 292 ITHFNAAPTV-NTLLcnskeAEPLPEPV------HVTVAASPPTPHL---FEQMTNLNLhpVHVYGMTETYGPITkgyYL 361
Cdd:PRK06187 256 VTFFFAVPTIwQMLL-----KAPRAYFVdfsslrLVIYGGAALPPALlreFKEKFGIDL--VQGYGMTETSPVVS---VL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 362 PAWDNLPssERYKKMARQGhgfvTSLP---VRVIKTDVAEgtvidVARDGKEIGEIVFVGNICARGYYKDPDATRKLFAG 438
Cdd:PRK06187 326 PPEDQLP--GQWTKRRSAG----RPLPgveARIVDDDGDE-----LPPDGGEVGEIIVRGPWLMQGYWNRPEATAETIDG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 439 GVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTG 518
Cdd:PRK06187 395 GWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDA 474
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 169764941 519 SEVIEWARNasDISKFMIPREVEVVAELPKTSTGKVRKNILRD 561
Cdd:PRK06187 475 KELRAFLRG--RLAKFKLPKRIAFVDELPRTSVGKILKRVLRE 515
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
36-556 |
1.30e-92 |
|
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: 290.67 E-value: 1.30e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 36 RAAAIEPEAVAIhhVTANNqvlRRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNY 112
Cdd:cd17631 3 RRARRHPDRTAL--VFGGR---SLTYAELDERVNRLAHALRALGVAkgdRVAVLSKNSPEFLELLFAAARLGAVFVPLNF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 113 RLKEDDIAYIFTHSDVEAIIvdqeflsllqsyrasrpsipiivdmdtdategelsgpfdevvlegltydldtgakgwpgl 192
Cdd:cd17631 78 RLTPPEVAYILADSGAKVLF------------------------------------------------------------ 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 193 eaqaaseDDVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLnshRGRCRYLWTLPMFHACGWTFPWAVTAVRG-T 271
Cdd:cd17631 98 -------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDL---GPDDVLLVVAPLFHIGGLGVFTLPTLLRGgT 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 272 HYCLRKIDYPQIWKLLKQEHITHFNAAPTVNTLLCNSKEAEP--LPEPVHVTVAASPPTPHLFEQMTNLNLHPVHVYGMT 349
Cdd:cd17631 168 VVILRKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATtdLSSLRAVIYGGAPMPERLLRALQARGVKFVQGYGMT 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 350 ETYGPITKgyylpawdnLPSSERYKKMARQGHGfVTSLPVRVIKTDVAEgtvidvARDGkEIGEIVFVGNICARGYYKDP 429
Cdd:cd17631 248 ETSPGVTF---------LSPEDHRRKLGSAGRP-VFFVEVRIVDPDGRE------VPPG-EVGEIVVRGPHVMAGYWNRP 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 430 DATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVT 509
Cdd:cd17631 311 EATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVV 390
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 169764941 510 VKPGKFLTGSEVIEWARnaSDISKFMIPREVEVVAELPKTSTGKVRK 556
Cdd:cd17631 391 PRPGAELDEDELIAHCR--ERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
201-555 |
2.65e-79 |
|
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: 252.98 E-value: 2.65e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 201 DVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLNSHRgrcRYLWTLPMFHACGWTFPWAVTAVRGTHYCLRKIDY 280
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGD---VFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 281 PQIWKLLKQEHITHFNAAPTVNTLLC--NSKEAEPLPEPVHVTVAASPPTPHLFEQMTNL-NLHPVHVYGMTETYGPITk 357
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLkaPESAGYDLSSLRALVSGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVA- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 358 GYYLPAWDNLPSSerykkmarqghgfvTSLPVRVIKTDV--AEGTVIDVardgKEIGEIVFVGNICARGYYKDPDATRKL 435
Cdd:cd04433 157 TGPPDDDARKPGS--------------VGRPVPGVEVRIvdPDGGELPP----GEIGELVVRGPSVMKGYWNNPEATAAV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 436 FAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKF 515
Cdd:cd04433 219 DEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGAD 298
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 169764941 516 LTGSEVIEWARnaSDISKFMIPREVEVVAELPKTSTGKVR 555
Cdd:cd04433 299 LDAEELRAHVR--ERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
34-560 |
6.26e-77 |
|
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: 250.94 E-value: 6.26e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 34 LPRAAAIEPEAVAIhhvtaNNQVLRRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAV 110
Cdd:cd05936 5 LEEAARRFPDKTAL-----IFMGRKLTYRELDALAEAFAAGLQNLGVQpgdRVALMLPNCPQFPIAYFGALKAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 111 NYRLKEDDIAYIFTHSDVEAIIVDQEFLSLLQSyrasrpsipiivdmdtdategelsgpfdevvlegltydlDTGAKGWP 190
Cdd:cd05936 80 NPLYTPRELEHILNDSGAKALIVAVSFTDLLAA---------------------------------------GAPLGERV 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 191 GLEAqaaseDDVIALAYTSGTTARPKGVEYTHRGcYLAAMGNVIESGLNSHRGRCRYLWTLPMFHACGWTFPWAVTAVRG 270
Cdd:cd05936 121 ALTP-----EDVAVLQYTSGTTGVPKGAMLTHRN-LVANALQIKAWLEDLLEGDDVVLAALPLFHVFGLTVALLLPLALG 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 271 -THYCLRKIDYPQIWKLLKQEHITHFNAAPTV-NTLLCNSKEAEPLPEPVHVTV--AASPPTPHL--FEQMTNLNLhpVH 344
Cdd:cd05936 195 aTIVLIPRFRPIGVLKEIRKHRVTIFPGVPTMyIALLNAPEFKKRDFSSLRLCIsgGAPLPVEVAerFEELTGVPI--VE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 345 VYGMTETyGPITKGyylpawdNLPSSERykkmaRQGH-GF-VTSLPVRVIKTDVAEgtvidvARDGkEIGEIVFVGNICA 422
Cdd:cd05936 273 GYGLTET-SPVVAV-------NPLDGPR-----KPGSiGIpLPGTEVKIVDDDGEE------LPPG-EVGELWVRGPQVM 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 423 RGYYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGE 502
Cdd:cd05936 333 KGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGE 412
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 169764941 503 RPKAFVTVKPGKFLTGSEVIEWARnaSDISKFMIPREVEVVAELPKTSTGKVRKNILR 560
Cdd:cd05936 413 AVKAFVVLKEGASLTEEEIIAFCR--EQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
28-560 |
3.39e-75 |
|
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: 247.73 E-value: 3.39e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 28 LSPTSFLPRAAaiepeaVAIHHVTANNqvLRRTYAETADRARGLAYYLKKHGFKR---VGVLCPNTPAFLESIFGIAAAG 104
Cdd:cd05915 2 ERAAALFGRKE------VVSRLHTGEV--HRTTYAEVYQRARRLMGGLRALGVGVgdrVATLGFNHFRHLEAYFAVPGMG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 105 AVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQEFLSLLQSyrasrpSIPIIVDMDTDATEGELSGPFDEVvlegltydLDT 184
Cdd:cd05915 74 AVLHTANPRLSPKEIAYILNHAEDKVLLFDPNLLPLVEA------IRGELKTVQHFVVMDEKAPEGYLA--------YEE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 185 GAKGWPGLeaQAASEDDVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLNShRGRCRYLWTLPMFHACGWTFPWA 264
Cdd:cd05915 140 ALGEEADP--VRVPERAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTAL-SEKDVVLPVVPMFHVNAWCLPYA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 265 VTAVRGTHYCLRKIDYPQ-IWKLLKQEHITHFNAAPTVNTLLCNSKEA--EPLPEPVHVTVAASPPtPHLFEQMTNLNLH 341
Cdd:cd05915 217 ATLVGAKQVLPGPRLDPAsLVELFDGEGVTFTAGVPTVWLALADYLEStgHRLKTLRRLVVGGSAA-PRSLIARFERMGV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 342 PVHV-YGMTETYGPITKGYYLPAWDNLPSSERYKKMARQGHGFVTSlpvrviKTDVAEGTVIDVARDGKEIGEIVFVGNI 420
Cdd:cd05915 296 EVRQgYGLTETSPVVVQNFVKSHLESLSEEEKLTLKAKTGLPIPLV------RLRVADEEGRPVPKDGKALGEVQLKGPW 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 421 CARGYYKDPDATRKL-FAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSH 499
Cdd:cd05915 370 ITGGYYGNEEATRSAlTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPK 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169764941 500 WGERPKAFVTVKPGKfLTGSEVIEWARNASDISKfMIPREVEVVAELPKTSTGKVRKNILR 560
Cdd:cd05915 450 WQERPLAVVVPRGEK-PTPEELNEHLLKAGFAKW-QLPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
34-561 |
1.82e-72 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 240.58 E-value: 1.82e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 34 LPRAAAIEPEAVAIHhvtanNQVLRRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAV 110
Cdd:PRK07656 11 LARAARRFGDKEAYV-----FGDQRLTYAELNARVRRAAAALAALGIGkgdRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 111 NYRLKEDDIAYIFTHSDVEAIIVDQEFLSLLQSYRASRPSIP--IIVDMDTDATEGELSGPFDEVVlegltydldtgAKG 188
Cdd:PRK07656 86 NTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEhvVICETEEDDPHTEKMKTFTDFL-----------AAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 189 WPGLEAQAASEDDVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLNSHRgrcRYLWTLPMFHACGWTFPWAVTAV 268
Cdd:PRK07656 155 DPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGD---RYLAANPFFHVFGYKAGVNAPLM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 269 RG-THYCLRKIDYPQIWKLLKQEHITHFNAAPTV-NTLLCN-SKEAEPLPE-PVHVTVAASPPtPHLFEQM-TNLNLHPV 343
Cdd:PRK07656 232 RGaTILPLPVFDPDEVFRLIETERITVLPGPPTMyNSLLQHpDRSAEDLSSlRLAVTGAASMP-VALLERFeSELGVDIV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 344 -HVYGMTETYGPITkgyylpawdnlpsserykkMARQGHGFVTslpvrvIKTDVaeGTVID------VARDGKEIGEIVf 416
Cdd:PRK07656 311 lTGYGLSEASGVTT-------------------FNRLDDDRKT------VAGTI--GTAIAgvenkiVNELGEEVPVGE- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 417 VGNICAR------GYYKDPDATRK-LFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILE 489
Cdd:PRK07656 363 VGELLVRgpnvmkGYYDDPEATAAaIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAE 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169764941 490 AGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIEWARnaSDISKFMIPREVEVVAELPKTSTGKVRKNILRD 561
Cdd:PRK07656 443 AAVIGVPDERLGEVGKAYVVLKPGAELTEEELIAYCR--EHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
34-468 |
5.68e-70 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 231.05 E-value: 5.68e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 34 LPRAAAIEPEAVAIHHVTANnqvlRRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAV 110
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGR----RLTYRELDERANRLAAGLRALGVGkgdRVAILLPNSPEWVVAFLACLKAGAVYVPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 111 NYRLKEDDIAYIFTHSDVEAIIVDQEF-LSLLQSYRASRPSIPIIVDMDTDAtegelsgpfdevVLEGLTYDLDTGAKGW 189
Cdd:pfam00501 77 NPRLPAEELAYILEDSGAKVLITDDALkLEELLEALGKLEVVKLVLVLDRDP------------VLKEEPLPEEAKPADV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 190 PGLEAQAASEDDVIALAYTSGTTARPKGVEYTHRG-CYLAAMGNVIESGLNSHRGRCRYLWTLPMFHACGWT-FPWAVTA 267
Cdd:pfam00501 145 PPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNlVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSlGLLGPLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 268 VRGTHYCLRKI---DYPQIWKLLKQEHITHFNAAPTVNTLLCNSKEAEPLPEP--VHVTVAASPPTPHLFEQMTNLNLHP 342
Cdd:pfam00501 225 AGATVVLPPGFpalDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSslRLVLSGGAPLPPELARRFRELFGGA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 343 V-HVYGMTETYGPITKGyylpawdnLPSSERYKKMARQGhgfvTSLP-VRVIKTDVAEGtviDVARDGkEIGEIVFVGNI 420
Cdd:pfam00501 305 LvNGYGLTETTGVVTTP--------LPLDEDLRSLGSVG----RPLPgTEVKIVDDETG---EPVPPG-EPGELCVRGPG 368
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 169764941 421 CARGYYKDPDATRKLF-AGGVLHSGDLAVWHADGSIQIQDRAKDIIISG 468
Cdd:pfam00501 369 VMKGYLNDPELTAEAFdEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
56-561 |
2.00e-66 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 225.40 E-value: 2.00e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 56 VLRRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAII 132
Cdd:PRK06018 37 IVRTTYAQIHDRALKVSQALDRDGIKlgdRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 133 VDQEFLSLLQSYRASRPSIPIIVDMDTDATEGELSGP----FDEVVLEGltyDLDTGAKGWPgleaqaasEDDVIALAYT 208
Cdd:PRK06018 117 TDLTFVPILEKIADKLPSVERYVVLTDAAHMPQTTLKnavaYEEWIAEA---DGDFAWKTFD--------ENTAAGMCYT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 209 SGTTARPKGVEYTHRGCYLAAMgnvIESGLNSHRGRCR--YLWTLPMFHACGWTFPWAVTAVrGTHYCL--RKIDYPQIW 284
Cdd:PRK06018 186 SGTTGDPKGVLYSHRSNVLHAL---MANNGDALGTSAAdtMLPVVPLFHANSWGIAFSAPSM-GTKLVMpgAKLDGASVY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 285 KLLKQEHITHFNAAPTVNTLLCNSKEAE--PLPEPVHVTVAASPPTPHLFEQMTNLNLHPVHVYGMTETyGPI-TKGYYL 361
Cdd:PRK06018 262 ELLDTEKVTFTAGVPTVWLMLLQYMEKEglKLPHLKMVVCGGSAMPRSMIKAFEDMGVEVRHAWGMTEM-SPLgTLAALK 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 362 PAWDNLPSSERYKKMARQGHgfvtslPVRVIKTDVAEGTVIDVARDGKEIGEIVFVGNICARGYYKDPDATrkLFAGGVL 441
Cdd:PRK06018 341 PPFSKLPGDARLDVLQKQGY------PPFGVEMKITDDAGKELPWDGKTFGRLKVRGPAVAAAYYRVDGEI--LDDDGFF 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 442 HSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEV 521
Cdd:PRK06018 413 DTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEI 492
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 169764941 522 IEWARnaSDISKFMIPREVEVVAELPKTSTGKVRKNILRD 561
Cdd:PRK06018 493 LKYMD--GKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
33-566 |
2.07e-65 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 223.06 E-value: 2.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 33 FLPRAAAIEPEAVAIHHVTANNQVLRRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIaaagavnva 109
Cdd:COG0365 14 CLDRHAEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRALGVKkgdRVAIYLPNIPEAVIAMLAC--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 110 vnYRL-----------KEDDIAYIFTHSDVEAIIVDQEFlsllqsYRASR--PSIPIIvdmdtDATEGELSGPFDEVVLE 176
Cdd:COG0365 85 --ARIgavhspvfpgfGAEALADRIEDAEAKVLITADGG------LRGGKviDLKEKV-----DEALEELPSLEHVIVVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 177 GLTYDLDT-GAKGWPGLEAQAASE--------DDVIALAYTSGTTARPKGVEYTHRGcYLAAMGNVIESGLNSHRGRcRY 247
Cdd:COG0365 152 RTGADVPMeGDLDWDELLAAASAEfepeptdaDDPLFILYTSGTTGKPKGVVHTHGG-YLVHAATTAKYVLDLKPGD-VF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 248 LWTLPmfhaCGWT--------FPWAV--TAV--RGthyclrKIDYPQ---IWKLLKQEHITHFNAAPTV-NTLLcnsKEA 311
Cdd:COG0365 230 WCTAD----IGWAtghsyivyGPLLNgaTVVlyEG------RPDFPDpgrLWELIEKYGVTVFFTAPTAiRALM---KAG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 312 EPLPEPV------HVTVAASPPTPHLFEQ-MTNLNLHPVHVYGMTETYGPITKGyyLPAWDNLPSSerykkMARQGHGFV 384
Cdd:COG0365 297 DEPLKKYdlsslrLLGSAGEPLNPEVWEWwYEAVGVPIVDGWGQTETGGIFISN--LPGLPVKPGS-----MGKPVPGYD 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 385 tslpVRVIktDvAEGTVIDVArdgkEIGEIV----FVGniCARGYYKDPDATRKLFAG---GVLHSGDLAVWHADGSIQI 457
Cdd:COG0365 370 ----VAVV--D-EDGNPVPPG----EEGELVikgpWPG--MFRGYWNDPERYRETYFGrfpGWYRTGDGARRDEDGYFWI 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 458 QDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTG---SEVIEWARNasDISKF 534
Cdd:COG0365 437 LGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDelaKELQAHVRE--ELGPY 514
|
570 580 590
....*....|....*....|....*....|..
gi 169764941 535 MIPREVEVVAELPKTSTGKVRKNILRDWAKGA 566
Cdd:COG0365 515 AYPREIEFVDELPKTRSGKIMRRLLRKIAEGR 546
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
60-560 |
3.64e-63 |
|
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: 213.31 E-value: 3.64e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 60 TYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDqe 136
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRpgdRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 137 flsllqsyrasrpsipiivdmdtdategelsgPFdevvlegltydldtgakgwpgleaqaaseddviALAYTSGTTARPK 216
Cdd:cd05934 83 --------------------------------PA---------------------------------SILYTSGTTGPPK 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 217 GVEYTHRGCYLAAMGNVIESGLNSHRgrcRYLWTLPMFHACGWTFPWAVTAVRGTHYCL-RKIDYPQIWKLLKQEHITHF 295
Cdd:cd05934 98 GVVITHANLTFAGYYSARRFGLGEDD---VYLTVLPLFHINAQAVSVLAALSVGATLVLlPRFSASRFWSDVRRYGATVT 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 296 NAAPTVNTLLCnskEAEPLPEPVH--VTVAASPPTPHL----FEQMTNLNLhpVHVYGMTETYGPItkgyylpaWDNLPS 369
Cdd:cd05934 175 NYLGAMLSYLL---AQPPSPDDRAhrLRAAYGAPNPPElheeFEERFGVRL--LEGYGMTETIVGV--------IGPRDE 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 370 SERYKKMARQGHGFvtslPVRVIKTDVAEgtvidvARDGkEIGEIV---FVGNICARGYYKDPDATRKLFAGGVLHSGDL 446
Cdd:cd05934 242 PRRPGSIGRPAPGY----EVRIVDDDGQE------LPAG-EPGELVirgLRGWGFFKGYYNMPEATAEAMRNGWFHTGDL 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 447 AVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIEWAR 526
Cdd:cd05934 311 GYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCE 390
|
490 500 510
....*....|....*....|....*....|....
gi 169764941 527 naSDISKFMIPREVEVVAELPKTSTGKVRKNILR 560
Cdd:cd05934 391 --GQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
21-566 |
4.57e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 215.95 E-value: 4.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 21 QRVNFHTLSptSFLPRAAAIEPEAVAIHHVTannqvLRRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESI 97
Cdd:PRK08316 6 TRARRQTIG--DILRRSARRYPDKTALVFGD-----RSWTYAELDAAVNRVAAALLDLGLKkgdRVAALGHNSDAYALLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 98 FGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQEFLSLLQSYRASRPSIPIIVDMDTDATEGELSgpfdevvLEG 177
Cdd:PRK08316 79 LACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPGG-------WLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 178 LTYDLDTGAKGWPGLEAqaaSEDDVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLNSHRgrcRYLWTLPMFHAC 257
Cdd:PRK08316 152 FADWAEAGSVAEPDVEL---ADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADD---IPLHALPLYHCA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 258 GW-TFPWAVTAVRGTHYCLRKIDYPQIWKLLKQEHITHFNAAPTVNTLLCNSkeaePLPEPVHVT------VAASP-PTP 329
Cdd:PRK08316 226 QLdVFLGPYLYVGATNVILDAPDPELILRTIEAERITSFFAPPTVWISLLRH----PDFDTRDLSslrkgyYGASImPVE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 330 HLFEQMTNL-NLHPVHVYGMTETyGPITKGyylpawdnLPSSERYKKMARQGhgfvtsLPVRVIKTDVAEGTVIDVARDg 408
Cdd:PRK08316 302 VLKELRERLpGLRFYNCYGQTEI-APLATV--------LGPEEHLRRPGSAG------RPVLNVETRVVDDDGNDVAPG- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 409 kEIGEIVFVGNICARGYYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDIL 488
Cdd:PRK08316 366 -EVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVA 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169764941 489 EAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIEWARnaSDISKFMIPREVEVVAELPKTSTGKVRKNILRDWAKGA 566
Cdd:PRK08316 445 EVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCR--ARLAGFKVPKRVIFVDELPRNPSGKILKRELRERYAGA 520
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
58-565 |
1.44e-62 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 214.96 E-value: 1.44e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 58 RRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVD 134
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALAALGVEpgdRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 135 QEFLSLLQSYRASRPSIPIIVDMdTDATegelSGPFDEVVLegLTY-DLDTGAKG---WPGLEAQAASeddviALAYTSG 210
Cdd:PRK07008 119 LTFLPLVDALAPQCPNVKGWVAM-TDAA----HLPAGSTPL--LCYeTLVGAQDGdydWPRFDENQAS-----SLCYTSG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 211 TTARPKGVEYTHRGCYLAAMGNVIESGLNShRGRCRYLWTLPMFHACGWTFPWAVtAVRGTHYCL--RKIDYPQIWKLLK 288
Cdd:PRK07008 187 TTGNPKGALYSHRSTVLHAYGAALPDAMGL-SARDAVLPVVPMFHVNAWGLPYSA-PLTGAKLVLpgPDLDGKSLYELIE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 289 QEHITHFNAAPTVNTLLCNSKEAEPLP-EPVHVTV---AASPPTP-HLFEQmtNLNLHPVHVYGMTETYGPITKGYYLPA 363
Cdd:PRK07008 265 AERVTFSAGVPTVWLGLLNHMREAGLRfSTLRRTViggSACPPAMiRTFED--EYGVEVIHAWGMTEMSPLGTLCKLKWK 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 364 WDNLPSSERYKKMARQGHGfVTSLPVRVIKTDVAEgtvidVARDGKEIGEIVFVGNICARGYYKDPDATrklFAGGVLHS 443
Cdd:PRK07008 343 HSQLPLDEQRKLLEKQGRV-IYGVDMKIVGDDGRE-----LPWDGKAFGDLQVRGPWVIDRYFRGDASP---LVDGWFPT 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 444 GDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIE 523
Cdd:PRK07008 414 GDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLA 493
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 169764941 524 WARnaSDISKFMIPREVEVVAELPKTSTGKVRKNILRDWAKG 565
Cdd:PRK07008 494 FYE--GKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQFRD 533
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
60-554 |
3.07e-62 |
|
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: 212.46 E-value: 3.07e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 60 TYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQE 136
Cdd:cd05911 12 TYAQLRTLSRRLAAGLRKLGLKkgdVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDPD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 137 FLSLLQSYRASRPSIPIIVDMDTdatEGELSGPFDEVVLEGLtydldtGAKGWPGLEAQAASEDDVIALAYTSGTTARPK 216
Cdd:cd05911 92 GLEKVKEAAKELGPKDKIIVLDD---KPDGVLSIEDLLSPTL------GEEDEDLPPPLKDGKDDTAAILYSSGTTGLPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 217 GVEYTHRGCyLAAMGNVIESGLNSHRGRCRYLWTLPMFHACGwtFPWAVTA-VRG-THYCLRKIDYPQIWKLLKQEHITH 294
Cdd:cd05911 163 GVCLSHRNL-IANLSQVQTFLYGNDGSNDVILGFLPLYHIYG--LFTTLASlLNGaTVIIMPKFDSELFLDLIEKYKITF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 295 FNAAPTVNTLLCNSKEAEP--LPEPVHVTVAASPPTPHLFEQMTNL--NLHPVHVYGMTETYGPITkgyYLPAWDNLPSS 370
Cdd:cd05911 240 LYLVPPIAAALAKSPLLDKydLSSLRVILSGGAPLSKELQELLAKRfpNATIKQGYGMTETGGILT---VNPDGDDKPGS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 371 ErykkmarqGHgFVTSLPVRVIKTDVAEGTVIDvardgkEIGEIVFVGNICARGYYKDPDATRKLF-AGGVLHSGDLAVW 449
Cdd:cd05911 317 V--------GR-LLPNVEAKIVDDDGKDSLGPN------EPGEICVRGPQVMKGYYNNPEATKETFdEDGWLHTGDIGYF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 450 HADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIEWARNAS 529
Cdd:cd05911 382 DEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKV 461
|
490 500
....*....|....*....|....*
gi 169764941 530 DISKFMIPReVEVVAELPKTSTGKV 554
Cdd:cd05911 462 ASYKQLRGG-VVFVDEIPKSASGKI 485
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
60-561 |
1.52e-58 |
|
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: 202.93 E-value: 1.52e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 60 TYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQ- 135
Cdd:cd05926 16 TYADLAELVDDLARQLAALGIKkgdRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPKg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 136 EFLSLLQSyrASRPSIPIiVDMDTDATEGELSGPFDEvvlegLTYDLDTGAKGWPGLEAQaasEDDVIALAYTSGTTARP 215
Cdd:cd05926 96 ELGPASRA--ASKLGLAI-LELALDVGVLIRAPSAES-----LSNLLADKKNAKSEGVPL---PDDLALILHTSGTTGRP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 216 KGVEYTHRGcYLAAMGNVIesglNSHR--GRCRYLWTLPMFHACGwtfpwAVTAVRGTHYCLRKIDYP------QIWKLL 287
Cdd:cd05926 165 KGVPLTHRN-LAASATNIT----NTYKltPDDRTLVVMPLFHVHG-----LVASLLSTLAAGGSVVLPprfsasTFWPDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 288 KQEHITHFNAAPTVNTLLCNSKEAEPLPEPVHVTV---AASPPTPHLFEQMTNLNLHPV-HVYGMTETYGPITKgyylpa 363
Cdd:cd05926 235 RDYNATWYTAVPTIHQILLNRPEPNPESPPPKLRFirsCSASLPPAVLEALEATFGAPVlEAYGMTEAAHQMTS------ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 364 wDNLPSSERYKKMARQGHGfvtslpvrvikTDVAegtviDVARDGKE-----IGEIVFVGNICARGYYKDPDATRKL-FA 437
Cdd:cd05926 309 -NPLPPGPRKPGSVGKPVG-----------VEVR-----ILDEDGEIlppgvVGEICLRGPNVTRGYLNNPEANAEAaFK 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 438 GGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLT 517
Cdd:cd05926 372 DGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVT 451
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 169764941 518 GSEVIEWARnaSDISKFMIPREVEVVAELPKTSTGKVRKNILRD 561
Cdd:cd05926 452 EEELRAFCR--KHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
34-560 |
1.19e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 193.46 E-value: 1.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 34 LPRAAAIEPEAVAIHHVTANNqvlrrTYAETADRARGLAYYLKKHGF---KRVGVLCPNTPAFLESIFGIAAAGAVNVAV 110
Cdd:PRK07786 23 LARHALMQPDAPALRFLGNTT-----TWRELDDRVAALAGALSRRGVgfgDRVLILMLNRTEFVESVLAANMLGAIAVPV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 111 NYRLKEDDIAYIFTHSDVEAIIVDQEFLSLLQSYRASRPSIPIIVDMDTDATEGELSgpFDEVVLEgltydldTGakgwP 190
Cdd:PRK07786 98 NFRLTPPEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLG--YEDLLAE-------AG----P 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 191 GLEAQAASEDDVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGL--NSHRGRCrylwTLPMFH--ACGWTFPWAVT 266
Cdd:PRK07786 165 AHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGAdiNSDVGFV----GVPLFHiaGIGSMLPGLLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 267 AVRGTHYCLRKIDYPQIWKLLKQEHITHFNAAPTVNTLLCNSKEAEPLPEPVHV-TVAASPPTPHLFEQMTNL--NLHPV 343
Cdd:PRK07786 241 GAPTVIYPLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVlSWGAAPASDTLLRQMAATfpEAQIL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 344 HVYGMTETyGPITKgyylpawdNLPSSERYKKMARQGHgfvtslPVRVIKTDVAEGTVIDVARDgkEIGEIVFVGNICAR 423
Cdd:PRK07786 321 AAFGQTEM-SPVTC--------MLLGEDAIRKLGSVGK------VIPTVAARVVDENMNDVPVG--EVGEIVYRAPTLMS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 424 GYYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGER 503
Cdd:PRK07786 384 GYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEV 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 169764941 504 PKAFVTVKPG-KFLTGSEVIEWARNasDISKFMIPREVEVVAELPKTSTGKVRKNILR 560
Cdd:PRK07786 464 PVAVAAVRNDdAALTLEDLAEFLTD--RLARYKHPKALEIVDALPRNPAGKVLKTELR 519
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
38-566 |
1.04e-53 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 189.79 E-value: 1.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 38 AAIEPEAVAIhhVTANNQVlrrTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRL 114
Cdd:PRK03640 12 AFLTPDRTAI--EFEEKKV---TFMELHEAVVSVAGKLAALGVKkgdRVALLMKNGMEMILVIHALQQLGAVAVLLNTRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 115 KEDDIAYIFTHSDVEAIIVDQEFLSLLQsyrasrPSIPIIVD--MDTDATEGELSGPFDEvvlegltydldtgakgwpgl 192
Cdd:PRK03640 87 SREELLWQLDDAEVKCLITDDDFEAKLI------PGISVKFAelMNGPKEEAEIQEEFDL-------------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 193 eaqaaseDDVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLNSHRgrcRYLWTLPMFHACGWTfpwavTAVRGTH 272
Cdd:PRK03640 141 -------DEVATIMYTSGTTGKPKGVIQTYGNHWWSAVGSALNLGLTEDD---CWLAAVPIFHISGLS-----ILMRSVI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 273 YCLR-----KIDYPQIWKLLKQEHITHFNAAPTVNTLLCNSKEAEPLPEPVHVTVAASPPTPH-LFEQMTNLNLHPVHVY 346
Cdd:PRK03640 206 YGMRvvlveKFDAEKINKLLQTGGVTIISVVSTMLQRLLERLGEGTYPSSFRCMLLGGGPAPKpLLEQCKEKGIPVYQSY 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 347 GMTETYGPITKgyyLPAWDNLpsseryKKMARQGHgfvTSLPVRviktdvaegtvIDVARDGK-----EIGEIVFVGNIC 421
Cdd:PRK03640 286 GMTETASQIVT---LSPEDAL------TKLGSAGK---PLFPCE-----------LKIEKDGVvvppfEEGEIVVKGPNV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 422 ARGYYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWG 501
Cdd:PRK03640 343 TKGYLNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWG 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169764941 502 ERPKAFVTVkpGKFLTGSEVIEWARNasDISKFMIPREVEVVAELPKTSTGKVRKNILRDWAKGA 566
Cdd:PRK03640 423 QVPVAFVVK--SGEVTEEELRHFCEE--KLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVEEM 483
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
196-560 |
1.69e-52 |
|
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: 185.28 E-value: 1.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 196 AASEDDVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLnshRGRCRYLWTLPMFHACGWTFPWAVTAVRGTHYCL 275
Cdd:cd05903 89 AAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGL---GPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 276 RkidypQIW------KLLKQEHITHFNAAPTVNTLLCNSKE--AEPLPEPVHVTVAASPPTPHLFEQM-TNLNLHPVHVY 346
Cdd:cd05903 166 Q-----DIWdpdkalALMREHGVTFMMGATPFLTDLLNAVEeaGEPLSRLRTFVCGGATVPRSLARRAaELLGAKVCSAY 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 347 GMTETYGPITkgyylpawdNLPSSERYKKMARQGHGFvtsLPVRVIKTDVAEGTVidvarDGKEIGEIVFVGNICARGYY 426
Cdd:cd05903 241 GSTECPGAVT---------SITPAPEDRRLYTDGRPL---PGVEIKVVDDTGATL-----APGVEGELLSRGPSVFLGYL 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 427 KDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKA 506
Cdd:cd05903 304 DRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACA 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 169764941 507 FVTVKPGKFLTGSEVIEWARNASdISKFMIPREVEVVAELPKTSTGKVRKNILR 560
Cdd:cd05903 384 VVVTKSGALLTFDELVAYLDRQG-VAKQYWPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
60-561 |
1.13e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 184.70 E-value: 1.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 60 TYAETADRARGLAYYLKKHGFKR---VGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQE 136
Cdd:PRK06145 29 SYAEFHQRILQAAGMLHARGIGQgdvVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 137 FlsllqsyrASRPSI--PIIVdMDTDATEgelsgpfDEVVLegltydldtGAKGWPGLEAQAASEDDVIALAYTSGTTAR 214
Cdd:PRK06145 109 F--------DAIVALetPKIV-IDAAAQA-------DSRRL---------AQGGLEIPPQAAVAPTDLVRLMYTSGTTDR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 215 PKGVEYTHRGCYLAAMGNVIESGLNSHRgrcRYLWTLPMFHACGWTFP-WAVTAVRGTHYCLRKIDYPQIWKLLKQEHIT 293
Cdd:PRK06145 164 PKGVMHSYGNLHWKSIDHVIALGLTASE---RLLVVGPLYHVGAFDLPgIAVLWVGGTLRIHREFDPEAVLAAIERHRLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 294 HFNAAPTVNTLLCNskeaepLPEPVHV-------TVAASPPTPHL-FEQMTNL--NLHPVHVYGMTETYGPitkgyylpa 363
Cdd:PRK06145 241 CAWMAPVMLSRVLT------VPDRDRFdldslawCIGGGEKTPESrIRDFTRVftRARYIDAYGLTETCSG--------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 364 wDNLPSSER-YKKMARQGHgfvtSLPVRVIKTDVAEGTVIDVARDGkeigEIVFVGNICARGYYKDPDATRKLFAGGVLH 442
Cdd:PRK06145 306 -DTLMEAGReIEKIGSTGR----ALAHVEIRIADGAGRWLPPNMKG----EICMRGPKVTKGYWKDPEKTAEAFYGDWFR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 443 SGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVI 522
Cdd:PRK06145 377 SGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALD 456
|
490 500 510
....*....|....*....|....*....|....*....
gi 169764941 523 EWARnaSDISKFMIPREVEVVAELPKTSTGKVRKNILRD 561
Cdd:PRK06145 457 RHCR--QRLASFKVPRQLKVRDELPRNPSGKVLKRVLRD 493
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
41-561 |
2.19e-51 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 184.98 E-value: 2.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 41 EPEAVAIHHvtannQVLRRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAA--AGAVNVAVNYRLK 115
Cdd:PRK12583 33 DREALVVRH-----QALRYTWRQLADAVDRLARGLLALGVQpgdRVGIWAPNCAEWLLTQFATARigAILVNINPAYRAS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 116 EddIAYIFTHSDVEAIIVDQEF---------LSLLQSYRASRPSIPI---------IVDMDTDATEGELSgpFDEVVLEG 177
Cdd:PRK12583 108 E--LEYALGQSGVRWVICADAFktsdyhamlQELLPGLAEGQPGALAcerlpelrgVVSLAPAPPPGFLA--WHELQARG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 178 LTY---DLDtgakgwpglEAQAA-SEDDVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLNSHRgrcRYLWTLPM 253
Cdd:PRK12583 184 ETVsreALA---------ERQASlDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHD---RLCVPVPL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 254 FHACGwtfpwAVTAVRGTHYCLRKIDYPQIW-------KLLKQEHITHFNAAPT--VNTLLCNSKEAEPLPEPVHVTVAA 324
Cdd:PRK12583 252 YHCFG-----MVLANLGCMTVGACLVYPNEAfdplatlQAVEEERCTALYGVPTmfIAELDHPQRGNFDLSSLRTGIMAG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 325 SPPTPHLFEQ-MTNLNLHPVHV-YGMTETyGPITkgYYLPAWDNLPssERYKKMAR-QGHgfvtsLPVRVIKTDVAEgtv 401
Cdd:PRK12583 327 APCPIEVMRRvMDEMHMAEVQIaYGMTET-SPVS--LQTTAADDLE--RRVETVGRtQPH-----LEVKVVDPDGAT--- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 402 idVARDgkEIGEIVFVGNICARGYYKDPDATRK-LFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESM 480
Cdd:PRK12583 394 --VPRG--EIGELCTRGYSVMKGYWNNPEATAEsIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 481 LVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIEWARnaSDISKFMIPREVEVVAELPKTSTGKVRKNILR 560
Cdd:PRK12583 470 LFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCK--ARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMR 547
|
.
gi 169764941 561 D 561
Cdd:PRK12583 548 E 548
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
192-561 |
1.11e-50 |
|
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: 179.46 E-value: 1.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 192 LEAQAASEDDVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLNSHRgrcRYLWTLPMFHACGWTfpwavTAVRG- 270
Cdd:cd05912 69 LKDSDVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDD---NWLCALPLFHISGLS-----ILMRSv 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 271 ----THYCLRKIDYPQIWKLLKQEHITHFNAAPTVNTLLcnskeAEPLPEPVHVTV-----AASPPTPHLFEQMTNLNLH 341
Cdd:cd05912 141 iygmTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRL-----LEILGEGYPNNLrcillGGGPAPKPLLEQCKEKGIP 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 342 PVHVYGMTETYGPITkgyylpawdNLPSSERYKKMARQGHgfvTSLPVRV-IKTDVAEGtvidvardgKEIGEIVFVGNI 420
Cdd:cd05912 216 VYQSYGMTETCSQIV---------TLSPEDALNKIGSAGK---PLFPVELkIEDDGQPP---------YEVGEILLKGPN 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 421 CARGYYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHW 500
Cdd:cd05912 275 VTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKW 354
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169764941 501 GERPKAFVTVKpgKFLTGSEVIEWARnaSDISKFMIPREVEVVAELPKTSTGKVRKNILRD 561
Cdd:cd05912 355 GQVPVAFVVSE--RPISEEELIAYCS--EKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
58-560 |
8.46e-50 |
|
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: 179.49 E-value: 8.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 58 RRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVD 134
Cdd:cd05959 29 SLTYAELEAEARRVAGALRALGVKreeRVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 135 QEFLSLLQSyrASRPSIPIIVDMDtdATEGElsGPFDEVVLegLTYDLDTGAkgwPGLEAQAASEDDVIALAYTSGTTAR 214
Cdd:cd05959 109 GELAPVLAA--ALTKSEHTLVVLI--VSGGA--GPEAGALL--LAELVAAEA---EQLKPAATHADDPAFWLYSSGSTGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 215 PKGVEYTHRGCYLAA---MGNVIesGLNSHRgrcRYLWTLPMFHACGW----TFPWAVTAVrgthyCLRKIDYPQ---IW 284
Cdd:cd05959 178 PKGVVHLHADIYWTAelyARNVL--GIREDD---VCFSAAKLFFAYGLgnslTFPLSVGAT-----TVLMPERPTpaaVF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 285 KLLKQEHITHFNAAPTVNTLLCNSKEA-EPLPEPVHVTVAASPPTP-HLFEQMTNL-NLHPVHVYGMTETyGPItkgyYL 361
Cdd:cd05959 248 KRIRRYRPTVFFGVPTLYAAMLAAPNLpSRDLSSLRLCVSAGEALPaEVGERWKARfGLDILDGIGSTEM-LHI----FL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 362 pawDNLPSSERYKKMARQGHGFVTSLpvrviktdVAEGTViDVArDGkEIGEIVFVGNICARGYYKDPDATRKLFAGGVL 441
Cdd:cd05959 323 ---SNRPGRVRYGTTGKPVPGYEVEL--------RDEDGG-DVA-DG-EPGELYVRGPSSATMYWNNRDKTRDTFQGEWT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 442 HSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTG--- 518
Cdd:cd05959 389 RTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEale 468
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 169764941 519 SEVIEWARNAsdISKFMIPREVEVVAELPKTSTGKVRKNILR 560
Cdd:cd05959 469 EELKEFVKDR--LAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
33-564 |
4.90e-49 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 178.47 E-value: 4.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 33 FLPRAAAIEP--EAVAIHHvtannQVLRRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTP-------------AFL 94
Cdd:PRK08315 21 LLDRTAARYPdrEALVYRD-----QGLRWTYREFNEEVDALAKGLLALGIEkgdRVGIWAPNVPewvltqfatakigAIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 95 ESIfgiaaagavnvAVNYRLKEddIAYIFTHSDVEAIIV-----DQEFLSLLQS------------YRASR-PSIPIIVD 156
Cdd:PRK08315 96 VTI-----------NPAYRLSE--LEYALNQSGCKALIAadgfkDSDYVAMLYElapelatcepgqLQSARlPELRRVIF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 157 MDTDATEGELSgpFDEVVLEGLTYDLDTgakgwpgLEAQAA--SEDDVIALAYTSGTTARPKGVEYTHRgcylaamgNVI 234
Cdd:PRK08315 163 LGDEKHPGMLN--FDELLALGRAVDDAE-------LAARQAtlDPDDPINIQYTSGTTGFPKGATLTHR--------NIL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 235 ESGLNShrGRC-------RYLWTLPMFHACGwtfpwAVTAVRG--TH-----YCLRKIDYPQIWKLLKQEHITHFNAAPT 300
Cdd:PRK08315 226 NNGYFI--GEAmklteedRLCIPVPLYHCFG-----MVLGNLAcvTHgatmvYPGEGFDPLATLAAVEEERCTALYGVPT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 301 VNTllcnskeAEpLPEPVHVT----------VAASP-PTPHLFEQMTNLNLHPVH-VYGMTETyGPITkgyylpawdnlp 368
Cdd:PRK08315 299 MFI-------AE-LDHPDFARfdlsslrtgiMAGSPcPIEVMKRVIDKMHMSEVTiAYGMTET-SPVS------------ 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 369 sserykkmarqghgFVT----SLPVRVikTDV------AEGTVIDVardgkEIGEIVFVGN---ICARG------YYKDP 429
Cdd:PRK08315 358 --------------TQTrtddPLEKRV--TTVgralphLEVKIVDP-----ETGETVPRGEqgeLCTRGysvmkgYWNDP 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 430 DATRK-LFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFV 508
Cdd:PRK08315 417 EKTAEaIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWI 496
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 169764941 509 TVKPGKFLTGSEVIEWARNasDISKFMIPREVEVVAELPKTSTGKVRKNILRDWAK 564
Cdd:PRK08315 497 ILRPGATLTEEDVRDFCRG--KIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMI 550
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
52-560 |
1.99e-48 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 176.03 E-value: 1.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 52 ANNQVLRRTYA---ETADRARGLAYYLKKHGFKRVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDV 128
Cdd:PRK08008 31 SGGVVRRYSYLelnEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 129 EAIIVDQEFLSLlqsYRASRPSIPIivdmdtdategelsgPFDEVVLEGLTYDLDTGAKGWPGLEAQAA---------SE 199
Cdd:PRK08008 111 SLLVTSAQFYPM---YRQIQQEDAT---------------PLRHICLTRVALPADDGVSSFTQLKAQQPatlcyapplST 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 200 DDVIALAYTSGTTARPKGVEYTH-----RGCYLAAMGNVIESGlnshrgrcRYLWTLPMFHA-CGWTFPWAVTAVRGTHY 273
Cdd:PRK08008 173 DDTAEILFTSGTTSRPKGVVITHynlrfAGYYSAWQCALRDDD--------VYLTVMPAFHIdCQCTAAMAAFSAGATFV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 274 CLRKIDYPQIWKllkqeHITHFNAAPTvntllcnskEAEPLpepVHVTVAASPPTP-----HLFEQMTNLNLHP------ 342
Cdd:PRK08008 245 LLEKYSARAFWG-----QVCKYRATIT---------ECIPM---MIRTLMVQPPSAndrqhCLREVMFYLNLSDqekdaf 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 343 --------VHVYGMTETY-GPITkgyylpawdNLPSSER-YKKMARQGHGFvtslpvrviktdvaEGTVIDVarDGKEI- 411
Cdd:PRK08008 308 eerfgvrlLTSYGMTETIvGIIG---------DRPGDKRrWPSIGRPGFCY--------------EAEIRDD--HNRPLp 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 412 -GEIvfvGNICARG---------YYKDPDATRKLF-AGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESM 480
Cdd:PRK08008 363 aGEI---GEICIKGvpgktifkeYYLDPKATAKVLeADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENI 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 481 LVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIEWARNasDISKFMIPREVEVVAELPKTSTGKVRKNILR 560
Cdd:PRK08008 440 IATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQ--NMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
60-560 |
3.12e-48 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 176.51 E-value: 3.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 60 TYAETADRARGLAYYLKKH----GFKRVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQ 135
Cdd:PRK05620 40 TFAAIGARAAALAHALHDElgitGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 136 EFLSLLQSYRASRPSIPIIV---DMDTDATEGELSGPFD----EVVLEGLTYDLDtgakgWPGLEaqaasEDDVIALAYT 208
Cdd:PRK05620 120 RLAEQLGEILKECPCVRAVVfigPSDADSAAAHMPEGIKvysyEALLDGRSTVYD-----WPELD-----ETTAAAICYS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 209 SGTTARPKGVEYTHRGCYLAAMGNVIESGLNSHRGRcRYLWTLPMFHACGWTFPWAvTAVRGTHYCL--RKIDYPQIWKL 286
Cdd:PRK05620 190 TGTTGAPKGVVYSHRSLYLQSLSLRTTDSLAVTHGE-SFLCCVPIYHVLSWGVPLA-AFMSGTPLVFpgPDLSAPTLAKI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 287 LKQEHITHFNAAPTVNTLLC-----NSKEAEPLPEpVHVTVAASPPTP-HLFEQMTNLNLhpVHVYGMTETyGPITKGYY 360
Cdd:PRK05620 268 IATAMPRVAHGVPTLWIQLMvhylkNPPERMSLQE-IYVGGSAVPPILiKAWEERYGVDV--VHVWGMTET-SPVGTVAR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 361 LPAwdNLPSSERYKKMARQGHgFVTSLPVRViktdVAEGTVIDvARDGKEiGEIVFVGNICARGYYKDP----------- 429
Cdd:PRK05620 344 PPS--GVSGEARWAYRVSQGR-FPASLEYRI----VNDGQVME-STDRNE-GEIQVRGNWVTASYYHSPteegggaastf 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 430 ------DATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGER 503
Cdd:PRK05620 415 rgedveDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGER 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 169764941 504 PKAFVTVKPGKFLTgSEVIEWARNA--SDISKFMIPREVEVVAELPKTSTGKVRKNILR 560
Cdd:PRK05620 495 PLAVTVLAPGIEPT-RETAERLRDQlrDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLR 552
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
38-561 |
8.52e-48 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 173.89 E-value: 8.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 38 AAIEPEAVAIhhvTANNQVLrrTYAETADRARGLAYYLK-----KHGfKRVGVLCPNTPAFLESIFGIAAAGAVNVAVNY 112
Cdd:PRK06839 12 AYLHPDRIAI---ITEEEEM--TYKQLHEYVSKVAAYLIyelnvKKG-ERIAILSQNSLEYIVLLFAIAKVECIAVPLNI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 113 RLKEDDIAYIFTHSDVEAIIVDQEFLSLLQSYRASRPSIPIIVdmdtdategelsgpfdevvLEGLTYDLDTGAKGwpgl 192
Cdd:PRK06839 86 RLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVIS-------------------ITSLKEIEDRKIDN---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 193 eAQAASEDDVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLNSHrGRCRYLwtLPMFHACG---WTFPWAVTAvr 269
Cdd:PRK06839 143 -FVEKNESASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMH-DRSIVL--LPLFHIGGiglFAFPTLFAG-- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 270 GTHYCLRKIDYPQIWKLLKQEHITHFNAAPTVNTLLCNS-KEAEPLPEPVHVTVAASPPTP-HLFEQMTNLNLHPVHVYG 347
Cdd:PRK06839 217 GVIIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCsKFETTNLQSVRWFYNGGAPCPeELMREFIDRGFLFGQGFG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 348 MTETYgpitkgyylPAWDNLPSSERYKKMARQGHGfVTSLPVRVI---KTDVAEGtvidvardgkEIGEIVFVGNICARG 424
Cdd:PRK06839 297 MTETS---------PTVFMLSEEDARRKVGSIGKP-VLFCDYELIdenKNKVEVG----------EVGELLIRGPNVMKE 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 425 YYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERP 504
Cdd:PRK06839 357 YWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIP 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169764941 505 KAFVTVKPGKFLTGSEVIEWARnaSDISKFMIPREVEVVAELPKTSTGKVRK----NILRD 561
Cdd:PRK06839 437 IAFIVKKSSSVLIEKDVIEHCR--LFLAKYKIPKEIVFLKELPKNATGKIQKaqlvNQLKS 495
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
60-561 |
1.43e-47 |
|
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: 171.75 E-value: 1.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 60 TYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDqe 136
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRkgdRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 137 flsllqsyrasrpsipiivdmdtdategelsgpfdevvlegltydldtgakgwpgleaqaasEDDVIALAYTSGTTARPK 216
Cdd:cd05972 80 --------------------------------------------------------------AEDPALIYFTSGTTGLPK 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 217 GVEYTHRgcYLAAMGNVIESGLNSHRGRCryLWTLPmfhACGW--------TFPWAVTAVRGTHYcLRKIDYPQIWKLLK 288
Cdd:cd05972 98 GVLHTHS--YPLGHIPTAAYWLGLRPDDI--HWNIA---DPGWakgawssfFGPWLLGATVFVYE-GPRFDAERILELLE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 289 QEHITHFNAAPTVNTLLCNSKEAEPLPEPVHVTVAASPP-TPH---LFEQMTNLNLHpvHVYGMTETygPITKGYYlPAW 364
Cdd:cd05972 170 RYGVTSFCGPPTAYRMLIKQDLSSYKFSHLRLVVSAGEPlNPEvieWWRAATGLPIR--DGYGQTET--GLTVGNF-PDM 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 365 DNLPSSerykkMARQGHGFvtslpvrviktDVAegtVIDvaRDGKEI--GEivfVGNICAR--------GYYKDPDATRK 434
Cdd:cd05972 245 PVKPGS-----MGRPTPGY-----------DVA---IID--DDGRELppGE---EGDIAIKlpppglflGYVGDPEKTEA 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 435 LFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGk 514
Cdd:cd05972 301 SIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSG- 379
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 169764941 515 fLTGSEVIewarnASDISKFM--------IPREVEVVAELPKTSTGKVRKNILRD 561
Cdd:cd05972 380 -YEPSEEL-----AEELQGHVkkvlapykYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
31-564 |
5.45e-47 |
|
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: 172.25 E-value: 5.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 31 TSFLPRAAAIEPEAVAihhVTANNQvlRRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAaagavn 107
Cdd:COG1021 28 GDLLRRRAERHPDRIA---VVDGER--RLSYAELDRRADRLAAGLLALGLRpgdRVVVQLPNVAEFVIVFFALF------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 108 vavnyRL-----------KEDDIAYIFTHSDVEAIIVDQE-----FLSLLQSYRASRPSIPIIVdMDTDATEGElsgPFD 171
Cdd:COG1021 97 -----RAgaipvfalpahRRAEISHFAEQSEAVAYIIPDRhrgfdYRALARELQAEVPSLRHVL-VVGDAGEFT---SLD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 172 EVVLEGLtydldtgakgwpGLEAQAASEDDVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLNSHRgrcRYLWTL 251
Cdd:COG1021 168 ALLAAPA------------DLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADT---VYLAAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 252 PMFHacgwTFPWAVTAVRGTHY---CLRKIDYP---QIWKLLKQEHITHFNAAPTVNTLLCNSKEAEP--LPEPVHVTVA 323
Cdd:COG1021 233 PAAH----NFPLSSPGVLGVLYaggTVVLAPDPspdTAFPLIERERVTVTALVPPLALLWLDAAERSRydLSSLRVLQVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 324 ASPPTPHLFEQMTN-LNLHPVHVYGMTEtyGPI--------------TKGYYLPAWDnlpssErykkmarqghgfvtslp 388
Cdd:COG1021 309 GAKLSPELARRVRPaLGCTLQQVFGMAE--GLVnytrlddpeeviltTQGRPISPDD-----E----------------- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 389 VRVIK---TDVAEGtvidvardgkEIGEIVFVGNICARGYYKDPDATRKLF-AGGVLHSGDLAVWHADGSIQIQDRAKDI 464
Cdd:COG1021 365 VRIVDedgNPVPPG----------EVGELLTRGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRAKDQ 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 465 IISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKpGKFLTGSEVIEWARnASDISKFMIPREVEVVA 544
Cdd:COG1021 435 INRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPR-GEPLTLAELRRFLR-ERGLAAFKLPDRLEFVD 512
|
570 580
....*....|....*....|
gi 169764941 545 ELPKTSTGKVRKNILRDWAK 564
Cdd:COG1021 513 ALPLTAVGKIDKKALRAALA 532
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
115-567 |
6.96e-47 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 172.55 E-value: 6.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 115 KEDDIAYIFTHSDVEAIIVDQEF--LSLLQSYRASRPSIP-----IIVDMDT-DATEGELSGPFDEvvlegltYDLDTGA 186
Cdd:PRK13295 115 RERELSFMLKHAESKVLVVPKTFrgFDHAAMARRLRPELPalrhvVVVGGDGaDSFEALLITPAWE-------QEPDAPA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 187 kgwpGLEAQAASEDDVIALAYTSGTTARPKGVEYTHrgcylaamgNVIESGLNSHRGRCRY------LWTLPMFHACGWT 260
Cdd:PRK13295 188 ----ILARLRPGPDDVTQLIYTSGTTGEPKGVMHTA---------NTLMANIVPYAERLGLgaddviLMASPMAHQTGFM 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 261 FPWAVTAVRGTHYCLRKI-DYPQIWKLLKQEHITHFNAAPTVNTLLCNSKEAEPLPEPVHVT--VAASPPTPHLFEQMTN 337
Cdd:PRK13295 255 YGLMMPVMLGATAVLQDIwDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTflCAGAPIPGALVERARA 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 338 -LNLHPVHVYGMTETyGPITKGyylpawdnLPSSERYKKMARQGHgfvtSLP---VRVIKTDVAEGTVidvardgKEIGE 413
Cdd:PRK13295 335 aLGAKIVSAWGMTEN-GAVTLT--------KLDDPDERASTTDGC----PLPgveVRVVDADGAPLPA-------GQIGR 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 414 IVFVGNICARGYYKDPDATRKLfAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVV 493
Cdd:PRK13295 395 LQVRGCSNFGGYLKRPQLNGTD-ADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIV 473
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169764941 494 AVPDSHWGERPKAFVTVKPGKFLTGSEVIEWARnASDISKFMIPREVEVVAELPKTSTGKVRKNILRDWAKGAN 567
Cdd:PRK13295 474 AYPDERLGERACAFVVPRPGQSLDFEEMVEFLK-AQKVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRGED 546
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
60-559 |
1.37e-46 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 169.17 E-value: 1.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 60 TYAETADRARGLAYYLKKHGF---KRVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQe 136
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIrsgSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 137 flsllqsyrasrpsipiivdmdtdategelsgPFDEVVLEGLTYDlDTGAKGWPGLEAQAASEDDVIA-LAYTSGTTARP 215
Cdd:TIGR01923 80 --------------------------------LLEEKDFQADSLD-RIEAAGRYETSLSASFNMDQIAtLMFTSGTTGKP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 216 KGVEYTHRGCYLAAMGnvieSGLNSHRGRC-RYLWTLPMFHACGWTFPWAVTAVRGTHYCLRKidYPQIWKLLKQEHITH 294
Cdd:TIGR01923 127 KAVPHTFRNHYASAVG----SKENLGFTEDdNWLLSLPLYHISGLSILFRWLIEGATLRIVDK--FNQLLEMIANERVTH 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 295 FNAAPTVNTLLCNSKEAEPLPEPVHVTVAASPPTphLFEQMTNLNLHPVHVYGMTETYGPITkgyylpawdnlpSSERYK 374
Cdd:TIGR01923 201 ISLVPTQLNRLLDEGGHNENLRKILLGGSAIPAP--LIEEAQQYGLPIYLSYGMTETCSQVT------------TATPEM 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 375 KMARQGHGFVtsLPVRVIKTDVAegtvidvarDGKEIGEIVFVGNICARGYYKDPDATRKLFAGGVLHSGDLAVWHADGS 454
Cdd:TIGR01923 267 LHARPDVGRP--LAGREIKIKVD---------NKEGHGEIMVKGANLMKGYLYQGELTPAFEQQGWFNTGDIGELDGEGF 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 455 IQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFvtVKPGKFLTGSEVIEWARnaSDISKF 534
Cdd:TIGR01923 336 LYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAY--IVSESDISQAKLIAYLT--EKLAKY 411
|
490 500
....*....|....*....|....*
gi 169764941 535 MIPREVEVVAELPKTSTGKVRKNIL 559
Cdd:TIGR01923 412 KVPIAFEKLDELPYNASGKILRNQL 436
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
116-569 |
2.25e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 170.55 E-value: 2.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 116 EDDIAYIFTHSDVEAIIVD-QEFLSLLQSYRASRPSIPIIVDMdtdategelsGPFDEVVlegltyDLDTGAKGWPGLEA 194
Cdd:PRK06188 98 LDDHAYVLEDAGISTLIVDpAPFVERALALLARVPSLKHVLTL----------GPVPDGV------DLLAAAAKFGPAPL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 195 QAASE-DDVIALAYTSGTTARPKGVEYTHRGcyLAAMgNVIESGLNSHRGRCRYLWTLPMFHACGWTFpwAVTAVRG-TH 272
Cdd:PRK06188 162 VAAALpPDIAGLAYTGGTTGKPKGVMGTHRS--IATM-AQIQLAEWEWPADPRFLMCTPLSHAGGAFF--LPTLLRGgTV 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 273 YCLRKIDYPQIWKLLKQEHITHFNAAPT-VNTLL-CNSKEAEPLPEPVHVTVAASPPTP-HLFEQMTNLNlhPV--HVYG 347
Cdd:PRK06188 237 IVLAKFDPAEVLRAIEEQRITATFLVPTmIYALLdHPDLRTRDLSSLETVYYGASPMSPvRLAEAIERFG--PIfaQYYG 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 348 MTETYGPITkgyYLPAWDNLPSSERykkmaRQGH-GFVTSLpvrvikTDVAegtVIDvaRDGKEI--GEivfVGNICAR- 423
Cdd:PRK06188 315 QTEAPMVIT---YLRKRDHDPDDPK-----RLTScGRPTPG------LRVA---LLD--EDGREVaqGE---VGEICVRg 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 424 -----GYYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDS 498
Cdd:PRK06188 373 plvmdGYWNRPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDE 452
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169764941 499 HWGERPKAFVTVKPGKFLTGSEVIEWARNAsdisKFMI--PREVEVVAELPKTSTGKVRKNILRD--WAkGANRS 569
Cdd:PRK06188 453 KWGEAVTAVVVLRPGAAVDAAELQAHVKER----KGSVhaPKQVDFVDSLPLTALGKPDKKALRAryWE-GRGRA 522
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
200-560 |
9.43e-46 |
|
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: 164.76 E-value: 9.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 200 DDVIALAYTSGTTARPKGVEYTHRgcylaamgNVIESGlnSHRGRcRYLWT--------LPMFHACGwtfpwavtAVRGT 271
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHH--------NIVNNG--YFIGE-RLGLTeqdrlcipVPLFHCFG--------SVLGV 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 272 HYCLRK----------IDYPQIWKLLKQEHITHFNAAPTVNTLLCNSKEaEPLPEPVHV---TVAASPPTPHLFEQMTN- 337
Cdd:cd05917 63 LACLTHgatmvfpspsFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPD-FDKFDLSSLrtgIMAGAPCPPELMKRVIEv 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 338 LNLHPVHV-YGMTETyGPITkgyyLPAWDNLPSSERYKKMAR-QGHgfvtsLPVRVIktDVAEGTVIDVArdgkEIGEIV 415
Cdd:cd05917 142 MNMKDVTIaYGMTET-SPVS----TQTRTDDSIEKRVNTVGRiMPH-----TEAKIV--DPEGGIVPPVG----VPGELC 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 416 FVGNICARGYYKDPDATRKLFAG-GVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVA 494
Cdd:cd05917 206 IRGYSVMKGYWNDPEKTAEAIDGdGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVG 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169764941 495 VPDSHWGERPKAFVTVKPGKFLTGSEVIEWARNasDISKFMIPREVEVVAELPKTSTGKVRKNILR 560
Cdd:cd05917 286 VPDERYGEEVCAWIRLKEGAELTEEDIKAYCKG--KIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
58-553 |
3.35e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 167.37 E-value: 3.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 58 RRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVD 134
Cdd:PRK07798 28 RLTYAELEERANRLAHYLIAQGLGpgdHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVYE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 135 QEFLSLLQSYRASRPSIPIIVDMDTDATEGELSGpfdevvleGLTYDlDTGAKGWPGLEAQAASEDDVIALaYTSGTTAR 214
Cdd:PRK07798 108 REFAPRVAEVLPRLPKLRTLVVVEDGSGNDLLPG--------AVDYE-DALAAGSPERDFGERSPDDLYLL-YTGGTTGM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 215 PKGVEYTHRGCYLAAM-------GNVIESgLNSHRGRC------RYLWTLPMFHACG-WTfpwAVTAVRGTH----YCLR 276
Cdd:PRK07798 178 PKGVMWRQEDIFRVLLggrdfatGEPIED-EEELAKRAaagpgmRRFPAPPLMHGAGqWA---AFAALFSGQtvvlLPDV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 277 KIDYPQIWKLLKQEHITHFN------AAPTVNTLLcnSKEAEPLPEPVHVTVAASPPTPH----LFEQMTNLNLhpvhvy 346
Cdd:PRK07798 254 RFDADEVWRTIEREKVNVITivgdamARPLLDALE--ARGPYDLSSLFAIASGGALFSPSvkeaLLELLPNVVL------ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 347 gmTETYGpitkgyylpawdnlpSSErykkMARQGHGFVTSLPVRV--IKTDVAEGTVIdVARDGK-------EIGEIVFV 417
Cdd:PRK07798 326 --TDSIG---------------SSE----TGFGGSGTVAKGAVHTggPRFTIGPRTVV-LDEDGNpvepgsgEIGWIARR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 418 GNIcARGYYKDPDATRKLF--AGGVLHS--GDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVV 493
Cdd:PRK07798 384 GHI-PLGYYKDPEKTAETFptIDGVRYAipGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVV 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 494 AVPDSHWGERPKAFVTVKPGKFLTGSEVIEWARnaSDISKFMIPREVEVVAELPKTSTGK 553
Cdd:PRK07798 463 GVPDERWGQEVVAVVQLREGARPDLAELRAHCR--SSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
60-560 |
5.58e-45 |
|
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: 166.26 E-value: 5.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 60 TYAETADRARGLAYYLKKHGFKR---VGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQE 136
Cdd:cd05904 34 TYAELERRVRRLAAGLAKRGGRKgdvVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 137 FLSLLQSYrasrpSIPIIVdmdtdategelsgpFDEVVLEGLTYDLDTGAKGWPGLEAQAASEDDVIALAYTSGTTARPK 216
Cdd:cd05904 114 LAEKLASL-----ALPVVL--------------LDSAEFDSLSFSDLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 217 GVEYTHRGcyLAAMGNVIESGLNSHRGR-CRYLWTLPMFHACGWT-FPWAVTAVRGTHYCLRKIDYPQIWKLLKQEHITH 294
Cdd:cd05904 175 GVMLTHRN--LIAMVAQFVAGEGSNSDSeDVFLCVLPMFHIYGLSsFALGLLRLGATVVVMPRFDLEELLAAIERYKVTH 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 295 FNAAPTVNTLLCNSKEAEP--LPEPVHVTVAASPPTPHL---FEQmtnlNLHPVHV---YGMTETYGPITKGyylpawdn 366
Cdd:cd05904 253 LPVVPPIVLALVKSPIVDKydLSSLRQIMSGAAPLGKELieaFRA----KFPNVDLgqgYGMTESTGVVAMC-------- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 367 lPSSEryKKMARQGH-GFVTSlpvrviktdVAEGTVIDVArDGK-----EIGEIVFVGNICARGYYKDPDATRKLFAG-G 439
Cdd:cd05904 321 -FAPE--KDRAKYGSvGRLVP---------NVEAKIVDPE-TGEslppnQTGELWIRGPSIMKGYLNNPEATAATIDKeG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 440 VLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGS 519
Cdd:cd05904 388 WLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTED 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 169764941 520 EVIEWarnasdISKFMIP----REVEVVAELPKTSTGKvrknILR 560
Cdd:cd05904 468 EIMDF------VAKQVAPykkvRKVAFVDAIPKSPSGK----ILR 502
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
59-568 |
8.14e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 163.15 E-value: 8.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 59 RTYAETADRARGLAYYLKKHGFKR---VGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQ 135
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREgdvVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 136 EFLSLLQSYRASRPSIPIIVDMDTDATEGELsgPFDEVVLEGLTYDLDTGAKGWPgleaqaaseddviaLAYTSGTTARP 215
Cdd:PRK08276 92 ALADTAAELAAELPAGVPLLLVVAGPVPGFR--SYEEALAAQPDTPIADETAGAD--------------MLYSSGTTGRP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 216 KGVEYTHRGCYLAAMGNVIESGLN---SHRGRCRYLWTLPMFHACGWTFPWAVTAVRGTHYCLRKIDYPQIWKLLKQEHI 292
Cdd:PRK08276 156 KGIKRPLPGLDPDEAPGMMLALLGfgmYGGPDSVYLSPAPLYHTAPLRFGMSALALGGTVVVMEKFDAEEALALIERYRV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 293 THFNAAPTVNTLLCNskeaepLPEPV----------HVTVAASPPTPHLFEQmtnlnlhpvhvygMTETYGPITKGYYlp 362
Cdd:PRK08276 236 THSQLVPTMFVRMLK------LPEEVrarydvsslrVAIHAAAPCPVEVKRA-------------MIDWWGPIIHEYY-- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 363 awdnlPSSErykkmarqGHG--FVTSL-----PVRVIKTDVAEGTVIDvaRDGKE-----IGEIVFVGNICARGYYKDPD 430
Cdd:PRK08276 295 -----ASSE--------GGGvtVITSEdwlahPGSVGKAVLGEVRILD--EDGNElppgeIGTVYFEMDGYPFEYHNDPE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 431 ATRKLFAG-GVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVT 509
Cdd:PRK08276 360 KTAAARNPhGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQ 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169764941 510 VKPGKFLT---GSEVIEWARNAsdISKFMIPREVEVVAELPKTSTGKVRKNILRD--WAKGANR 568
Cdd:PRK08276 440 PADGADAGdalAAELIAWLRGR--LAHYKCPRSIDFEDELPRTPTGKLYKRRLRDryWEGRQRA 501
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
34-567 |
1.01e-43 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 163.59 E-value: 1.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 34 LPRAAAIEPEAVAIHHVTAnnqvlRRTYAETADRARGLAYYLK-KHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVA 109
Cdd:PRK08314 16 LEVSARRYPDKTAIVFYGR-----AISYRELLEEAERLAGYLQqECGVRkgdRVLLYMQNSPQFVIAYYAILRANAVVVP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 110 VNYRLKEDDIAYIFTHSDVEAIIVDQEFLSLLQSYRASRPSIPIIVDM--DTDATEGELS--------GPFDEVVLEGLT 179
Cdd:PRK08314 91 VNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHVIVAQysDYLPAEPEIAvpawlraePPLQALAPGGVV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 180 YDLDTGAKGWPGLEAQAASeDDVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLNSHRgrcRYLWTLPMFHACGw 259
Cdd:PRK08314 171 AWKEALAAGLAPPPHTAGP-DDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPES---VVLAVLPLFHVTG- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 260 tFPWAVTA---VRGTHYCLRKIDYPQIWKLLKQEHITHFNAAPT-VNTLLCNSKEAE--------------PLPEPVhvt 321
Cdd:PRK08314 246 -MVHSMNApiyAGATVVLMPRWDREAAARLIERYRVTHWTNIPTmVVDFLASPGLAErdlsslryiggggaAMPEAV--- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 322 vaasppTPHLFEQmTNLNLhpVHVYGMTETYGPITKgyylpawdNLPssERYKkmaRQGHGFVT-SLPVRVIktDVAEGT 400
Cdd:PRK08314 322 ------AERLKEL-TGLDY--VEGYGLTETMAQTHS--------NPP--DRPK---LQCLGIPTfGVDARVI--DPETLE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 401 VIDVArdgkEIGEIVFVGNICARGYYKDPDATRKLFA--GG--VLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVA 476
Cdd:PRK08314 378 ELPPG----EVGEIVVHGPQVFKGYWNRPEATAEAFIeiDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAE 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 477 LESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGS--EVIEWARnaSDISKFMIPREVEVVAELPKTSTGKV 554
Cdd:PRK08314 454 VENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTTeeEIIAWAR--EHMAAYKYPRIVEFVDSLPKSGSGKI 531
|
570
....*....|...
gi 169764941 555 RKNILRDWAKGAN 567
Cdd:PRK08314 532 LWRQLQEQEKARA 544
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
34-559 |
1.04e-43 |
|
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: 162.68 E-value: 1.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 34 LPRAAAIEPEAVAIHHVTANnqvLRRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAV 110
Cdd:cd05923 7 LRRAASRAPDACAIADPARG---LRLTYSELRARIEAVAARLHARGLRpgqRVAVVLPNSVEAVIALLALHRLGAVPALI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 111 NYRLKEDDIAYIFTHSDVEAIIVDqeflsllqsyrasrpsiPIIVDMDTDATEGelsgpfdeVVLEGLTYDLDTGA--KG 188
Cdd:cd05923 84 NPRLKAAELAELIERGEMTAAVIA-----------------VDAQVMDAIFQSG--------VRVLALSDLVGLGEpeSA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 189 WPGLEAQAASEDDVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLNSHRGRcRYLWTLPMFHACGWTFPWAVTAV 268
Cdd:cd05923 139 GPLIEDPPREPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRHN-VVLGLMPLYHVIGFFAVLVAALA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 269 RGTHYCL-RKIDYPQIWKLLKQEHITHFNAAPTVNTLLCNSKEAEP--LPEPVHVTVAASPPTPHLFEQMTN-LNLHPVH 344
Cdd:cd05923 218 LDGTYVVvEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGlkLSSLRHVTFAGATMPDAVLERVNQhLPGEKVN 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 345 VYGMTETYGPItkgyylpawdnlpsserYKKMARQGHGFVTSLPVRVIKTDVAEGTVIDVArDGKEiGEIVF--VGNICA 422
Cdd:cd05923 298 IYGTTEAMNSL-----------------YMRDARTGTEMRPGFFSEVRIVRIGGSPDEALA-NGEE-GELIVaaAADAAF 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 423 RGYYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGE 502
Cdd:cd05923 359 TGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQ 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 169764941 503 RPKAFVTVKPGKfLTGSEVIEWARnASDISKFMIPREVEVVAELPKTSTGKVRKNIL 559
Cdd:cd05923 439 SVTACVVPREGT-LSADELDQFCR-ASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
204-561 |
1.52e-43 |
|
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: 160.92 E-value: 1.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 204 ALAYTSGTTARPKGVEYTHRGcyLAAMGNVIESGLNsHRGRCRYLWTLPMFHACGWTFPWAVT-AVRGTHYCLRKIDYPQ 282
Cdd:cd05941 93 LILYTSGTTGRPKGVVLTHAN--LAANVRALVDAWR-WTEDDVLLHVLPLHHVHGLVNALLCPlFAGASVEFLPKFDPKE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 283 IWKLLKQEHITHFNAAPTVNTLLCNSKEAEPLP---------EPVHVTVAASPPTP-HLFEQMTNLNLHP-VHVYGMTET 351
Cdd:cd05941 170 VAISRLMPSITVFMGVPTIYTRLLQYYEAHFTDpqfaraaaaERLRLMVSGSAALPvPTLEEWEAITGHTlLERYGMTEI 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 352 ygpitkgyylpawdNLPSSERYKKMARQghGFVTS-LP---VRVIKTDVAEgtvidvARDGKEIGEIVFVGNICARGYYK 427
Cdd:cd05941 250 --------------GMALSNPLDGERRP--GTVGMpLPgvqARIVDEETGE------PLPRGEVGEIQVRGPSVFKEYWN 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 428 DPDATRKLF-AGGVLHSGDLAVWHADGSIQIQDRAK-DIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPK 505
Cdd:cd05941 308 KPEATKEEFtDDGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVV 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 169764941 506 AFVTVKPGKF-LTGSEVIEWARNAsdISKFMIPREVEVVAELPKTSTGKVRKNILRD 561
Cdd:cd05941 388 AVVVLRAGAAaLSLEELKEWAKQR--LAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
200-561 |
1.74e-43 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 163.25 E-value: 1.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 200 DDVIALAYTSGTTARPKGVEYTHRGCYL-AAMGNVIESGLNshRGRCRYLWTLPMFHACGWTFPWAVT-AVRGTHYCLRK 277
Cdd:PRK05605 219 DDVALILYTSGTTGKPKGAQLTHRNLFAnAAQGKAWVPGLG--DGPERVLAALPMFHAYGLTLCLTLAvSIGGELVLLPA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 278 IDYPQIWKLLKQEHITHFNAAPTVNTLLCNSKEAEPLP-EPVHVTV--AAS--PPTPHLFEQMTNLNLhpVHVYGMTETy 352
Cdd:PRK05605 297 PDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDlSGVRNAFsgAMAlpVSTVELWEKLTGGLL--VEGYGLTET- 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 353 GPITKGyylpawdNLPSSERykkmaRQGHGFVT--SLPVRVIKTDvaegtviDVAR---DGKEiGEIVFVGNICARGYYK 427
Cdd:PRK05605 374 SPIIVG-------NPMSDDR-----RPGYVGVPfpDTEVRIVDPE-------DPDEtmpDGEE-GELLVRGPQVFKGYWN 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 428 DPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAF 507
Cdd:PRK05605 434 RPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAA 513
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 169764941 508 VTVKPGKFLTGSEVIEWARnaSDISKFMIPREVEVVAELPKTSTGKVRKNILRD 561
Cdd:PRK05605 514 VVLEPGAALDPEGLRAYCR--EHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
58-561 |
1.90e-43 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 162.62 E-value: 1.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 58 RRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVD 134
Cdd:PRK06155 46 RWTYAEAARAAAAAAHALAAAGVKrgdRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 135 QEFLSLLQSYRASRPSIPIIVDMDTdATEGELSGPFDEVVLEGLTYDLDTGAKGwPGleaqaasedDVIALAYTSGTTAR 214
Cdd:PRK06155 126 AALLAALEAADPGDLPLPAVWLLDA-PASVSVPAGWSTAPLPPLDAPAPAAAVQ-PG---------DTAAILYTSGTTGP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 215 PKGVEYTHR-----GCYLAAMGNVIESGLnshrgrcrYLWTLPMFH--ACGWTFPWAVTavrGTHYCL-RKIDYPQIWKL 286
Cdd:PRK06155 195 SKGVCCPHAqfywwGRNSAEDLEIGADDV--------LYTTLPLFHtnALNAFFQALLA---GATYVLePRFSASGFWPA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 287 LkQEH---ITHFNAApTVNTLLcnSKEAEPLPEPVHVTVAASPPTP-HLFEQMT-NLNLHPVHVYGMTETYGPItkgyYL 361
Cdd:PRK06155 264 V-RRHgatVTYLLGA-MVSILL--SQPARESDRAHRVRVALGPGVPaALHAAFReRFGVDLLDGYGSTETNFVI----AV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 362 PawdnlPSSERYKKMARQGHGFVtslpVRViktdVAEGtviDVARDGKEIGEIVFVGN---ICARGYYKDPDATRKLFAG 438
Cdd:PRK06155 336 T-----HGSQRPGSMGRLAPGFE----ARV----VDEH---DQELPDGEPGELLLRADepfAFATGYFGMPEKTVEAWRN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 439 GVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTG 518
Cdd:PRK06155 400 LWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEP 479
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 169764941 519 SEVIEWARnaSDISKFMIPREVEVVAELPKTSTGKVRKNILRD 561
Cdd:PRK06155 480 VALVRHCE--PRLAYFAVPRYVEFVAALPKTENGKVQKFVLRE 520
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
208-563 |
1.26e-42 |
|
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: 155.57 E-value: 1.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 208 TSGTTARPKGVEYTHRGCYLAAMGnviesgLNSH---RGRCRYLWTLPMFHACGWTFPWAVTAVRGTHYCLRKIdypqiW 284
Cdd:cd17630 8 TSGSTGTPKAVVHTAANLLASAAG------LHSRlgfGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERN-----Q 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 285 KLLKQEH---ITHFNAAPT-VNTLLCNSKEAEPLPEPVHVTVAASPPTPHLFEQMTNLNLHPVHVYGMTETYGPITKGyy 360
Cdd:cd17630 77 ALAEDLAppgVTHVSLVPTqLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADRGIPLYTTYGMTETASQVATK-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 361 lpawdnlpsseRYKKMARQGHGFVtsLPvrviktdvaeGTVIDVARDGKeigeiVFVGNICARGYYKDPDATRKLFAGGV 440
Cdd:cd17630 155 -----------RPDGFGRGGVGVL--LP----------GRELRIVEDGE-----IWVGGASLAMGYLRGQLVPEFNEDGW 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 441 LHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGkfLTGSE 520
Cdd:cd17630 207 FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGP--ADPAE 284
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 169764941 521 VIEWARNAsdISKFMIPREVEVVAELPKTSTGKVRKNILRDWA 563
Cdd:cd17630 285 LRAWLKDK--LARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
60-559 |
1.39e-42 |
|
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: 158.03 E-value: 1.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 60 TYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQE 136
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRkgdRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 137 FlsllqsyrasrpsipiivdmdtdategelsgpfdevvlegltydldtgakgwpgleaqaaseDDVIALAYTSGTTARPK 216
Cdd:cd05935 83 L--------------------------------------------------------------DDLALIPYTSGTTGLPK 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 217 GVEYTHRGCYLAAMGNVIESGLNshrGRCRYLWTLPMFHACGWTFPW-AVTAVRGTHYCLRKIDYPQIWKLLKQEHITHF 295
Cdd:cd05935 101 GCMHTHFSAAANALQSAVWTGLT---PSDVILACLPLFHVTGFVGSLnTAVYVGGTYVLMARWDRETALELIEKYKVTFW 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 296 NAAPT-VNTLLCNSK-EAEPLPEPVHVTVAASPPTPHLFEQMTNL-NLHPVHVYGMTETYGPITKgyylpawdNLPSSER 372
Cdd:cd05935 178 TNIPTmLVDLLATPEfKTRDLSSLKVLTGGGAPMPPAVAEKLLKLtGLRFVEGYGLTETMSQTHT--------NPPLRPK 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 373 ykkmaRQGHGFVTS-LPVRVIktDVAEGTVIDVArdgkEIGEIVFVGNICARGYYKDPDATRKLFA--GG--VLHSGDLA 447
Cdd:cd05935 250 -----LQCLGIP*FgVDARVI--DIETGRELPPN----EVGEIVVRGPQIFKGYWNRPEETEESFIeiKGrrFFRTGDLG 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 448 VWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGSE--VIEWA 525
Cdd:cd05935 319 YMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEedIIEWA 398
|
490 500 510
....*....|....*....|....*....|....
gi 169764941 526 RnaSDISKFMIPREVEVVAELPKTSTGKVRKNIL 559
Cdd:cd05935 399 R--EQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
33-559 |
3.51e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 159.43 E-value: 3.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 33 FLPRAAAIEPEAVAIHHVTANnqvlrRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVA 109
Cdd:PRK06710 29 YVEQMASRYPEKKALHFLGKD-----ITFSVFHDKVKRFANYLQKLGVEkgdRVAIMLPNCPQAVIGYYGTLLAGGIVVQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 110 VNYRLKEDDIAYIFTHSDVEAIIVDQEFLSLLQSYRASRPSIPIIVDMDTD--ATEGELSGPFDEVVLEGLTYDLDTGA- 186
Cdd:PRK06710 104 TNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSATKIEHVIVTRIADflPFPKNLLYPFVQKKQSNLVVKVSESEt 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 187 -KGWPGLEAQAAS--------EDDVIALAYTSGTTARPKGVEYTHRGCYL-AAMGnvIESGLNSHRGRCRYLWTLPMFHA 256
Cdd:PRK06710 184 iHLWNSVEKEVNTgvevpcdpENDLALLQYTGGTTGFPKGVMLTHKNLVSnTLMG--VQWLYNCKEGEEVVLGVLPFFHV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 257 CGWTFPWAVTAVRGTHYCL-RKIDYPQIWKLLKQEHITHFNAAPTVNTLLCNS---KEAEplPEPVHVTVAASPPTP--- 329
Cdd:PRK06710 262 YGMTAVMNLSIMQGYKMVLiPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSpllKEYD--ISSIRACISGSAPLPvev 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 330 -HLFEQMTNLNLhpVHVYGMTETyGPITKGYYLpaWDN-LPSSerykkmarqghgfvTSLP-----VRVIKTDVAEgtvi 402
Cdd:PRK06710 340 qEKFETVTGGKL--VEGYGLTES-SPVTHSNFL--WEKrVPGS--------------IGVPwpdteAMIMSLETGE---- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 403 dVARDGkEIGEIVFVGNICARGYYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLV 482
Cdd:PRK06710 397 -ALPPG-EIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLY 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169764941 483 THPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIEWARNAsdISKFMIPREVEVVAELPKTSTGKVRKNIL 559
Cdd:PRK06710 475 EHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKY--LAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
33-563 |
5.83e-42 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 159.74 E-value: 5.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 33 FLPRAAAIEPEAVAI---HHVTANNQVLRRTYAETADRARGLAYYLKKHGFKR---VGVLCPNTPaflESIF-------- 98
Cdd:PRK07529 30 LLSRAAARHPDAPALsflLDADPLDRPETWTYAELLADVTRTANLLHSLGVGPgdvVAFLLPNLP---ETHFalwggeaa 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 99 GIAAAGAVnvavnyRLKEDDIAYIFTHSDVEAIIV-----DQEFLSLLQSYRASRPSIPIIVDMD---TDATEGELSGPF 170
Cdd:PRK07529 107 GIANPINP------LLEPEQIAELLRAAGAKVLVTlgpfpGTDIWQKVAEVLAALPELRTVVEVDlarYLPGPKRLAVPL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 171 DEVVLEGLTYDLDTGAKGWPG---LEAQAASEDDVIALAYTSGTTARPKGVEYTHRGcyLAAMGNVIESGLNSHRGRCRy 247
Cdd:PRK07529 181 IRRKAHARILDFDAELARQPGdrlFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGN--EVANAWLGALLLGLGPGDTV- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 248 LWTLPMFHacgwtfpwaVTAV---------RGTHYCL------RKID-YPQIWKLLKQEHITHFNAAPTV-NTLL---CN 307
Cdd:PRK07529 258 FCGLPLFH---------VNALlvtglaplaRGAHVVLatpqgyRGPGvIANFWKIVERYRINFLSGVPTVyAALLqvpVD 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 308 SKE----------AEPLPepvhVTVAASpptphlFEQMTNLNLhpVHVYGMTET---------YGPITKGyylpaWDNLP 368
Cdd:PRK07529 329 GHDisslryalcgAAPLP----VEVFRR------FEAATGVRI--VEGYGLTEAtcvssvnppDGERRIG-----SVGLR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 369 sserykkmarqghgfvtsLP---VRVIKTDVAEGTVIDVARDgkEIGEI------VFVGnicargyYKDPDATRKLFAGG 439
Cdd:PRK07529 392 ------------------LPyqrVRVVILDDAGRYLRDCAVD--EVGVLciagpnVFSG-------YLEAAHNKGLWLED 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 440 V-LHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTG 518
Cdd:PRK07529 445 GwLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATE 524
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 169764941 519 SEVIEWARnaSDIS-KFMIPREVEVVAELPKTSTGKVRKNILRDWA 563
Cdd:PRK07529 525 AELLAFAR--DHIAeRAAVPKHVRILDALPKTAVGKIFKPALRRDA 568
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
201-556 |
9.30e-42 |
|
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: 153.04 E-value: 9.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 201 DVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLNSHRgrcRYLWTLPMFHACGWTFPWAVTAVRG-THYCLRKID 279
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDD---RYLIINPFFHTFGYKAGIVACLLTGaTVVPVAVFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 280 YPQIWKLLKQEHITHFNAAPTV-NTLLC--NSKEAEPLPEPVHVTVAASPPtPHLFEQM-TNLNLHPVHV-YGMTETyGP 354
Cdd:cd17638 78 VDAILEAIERERITVLPGPPTLfQSLLDhpGRKKFDLSSLRAAVTGAATVP-VELVRRMrSELGFETVLTaYGLTEA-GV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 355 ITkgyylpawdnlpsserykkMARQGHGFVTslpvrviktdVAegTVIDVARDGKEI-----GEIVFVGNICARGYYKDP 429
Cdd:cd17638 156 AT-------------------MCRPGDDAET----------VA--TTCGRACPGFEVriaddGEVLVRGYNVMQGYLDDP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 430 DATRKLF-AGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFV 508
Cdd:cd17638 205 EATAEAIdADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFV 284
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 169764941 509 TVKPGKFLTGSEVIEWARnaSDISKFMIPREVEVVAELPKTSTGKVRK 556
Cdd:cd17638 285 VARPGVTLTEEDVIAWCR--ERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
33-561 |
7.42e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 155.20 E-value: 7.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 33 FLPRAAAIEPEAVAIHHVTAnnqvlRRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVA 109
Cdd:PRK07470 12 FLRQAARRFPDRIALVWGDR-----SWTWREIDARVDALAAALAARGVRkgdRILVHSRNCNQMFESMFAAFRLGAVWVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 110 VNYRLKEDDIAYIFTHSDVEAIIVDQEFLSLLQSYRASRPSIPIIVDMDtdATEGELSgpFDEVVLEGLtydldtGAKGw 189
Cdd:PRK07470 87 TNFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHVVAIG--GARAGLD--YEALVARHL------GARV- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 190 pglEAQAASEDDVIALAYTSGTTARPKGVEYTHrgcylAAMGNVIESGL------NSHRGRCryLWTLPMFHACGWTfpw 263
Cdd:PRK07470 156 ---ANAAVDHDDPCWFFFTSGTTGRPKAAVLTH-----GQMAFVITNHLadlmpgTTEQDAS--LVVAPLSHGAGIH--- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 264 AVTAV-RGTHYCL---RKIDYPQIWKLLKQEHITHFNAAPTVNTLLCNSKEAEPLPEPV--HVTVAASPPTPHlfEQMTN 337
Cdd:PRK07470 223 QLCQVaRGAATVLlpsERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSlrYVIYAGAPMYRA--DQKRA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 338 LN-LHPVHV--YGMTETYGPITkgyYLPAWDNLPSSErykKMARQGH-GFvtslpvrviktdvaEGTVIDVA---RDGKE 410
Cdd:PRK07470 301 LAkLGKVLVqyFGLGEVTGNIT---VLPPALHDAEDG---PDARIGTcGF--------------ERTGMEVQiqdDEGRE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 411 I--GEivfVGNICARG------YYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLV 482
Cdd:PRK07470 361 LppGE---TGEICVIGpavfagYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLL 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169764941 483 THPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIEWArnASDISKFMIPREVEVVAELPKTSTGKVRKNILRD 561
Cdd:PRK07470 438 THPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAELLAWL--DGKVARYKLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
34-564 |
2.24e-40 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 154.87 E-value: 2.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 34 LPRAAAIEPEAVAIHHVtANNQVLRRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIaaagavnvav 110
Cdd:COG1022 17 LRRRAARFPDRVALREK-EDGIWQSLTWAEFAERVRALAAGLLALGVKpgdRVAILSDNRPEWVIADLAI---------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 111 nyrLK-------------EDDIAYIFTHSDVEAIIV-DQEFLSLLQSYRASRPSIPIIVDMDTDATEGELSG-PFDEVVL 175
Cdd:COG1022 86 ---LAagavtvpiyptssAEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDELPSLRHIVVLDPRGLRDDPRLlSLDELLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 176 EGLTYDLDTGAKGWpgleAQAASEDDVIALAYTSGTTARPKGVEYTHRgCYLAAMGNVIESGlnSHRGRCRYLWTLPMFH 255
Cdd:COG1022 163 LGREVADPAELEAR----RAAVKPDDLATIIYTSGTTGRPKGVMLTHR-NLLSNARALLERL--PLGPGDRTLSFLPLAH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 256 ACGWTFPWAVTAVRGTHYCLRKIDY----------------PQIWKLLKQEHITHFNAAPTV---------------NTL 304
Cdd:COG1022 236 VFERTVSYYALAAGATVAFAESPDTlaedlrevkptfmlavPRVWEKVYAGIQAKAEEAGGLkrklfrwalavgrryARA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 305 LCNSKEAEPLPEPVH------------------VTVAAS---PPTPHLFEQMTNLNLHPVHVYGMTETYGPITkgyYLPA 363
Cdd:COG1022 316 RLAGKSPSLLLRLKHaladklvfsklrealggrLRFAVSggaALGPELARFFRALGIPVLEGYGLTETSPVIT---VNRP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 364 WDNLPSSerykkmarqghgfvtslpV-RVIktdvaEGTVIDVARDGkEI---GEIVFvgnicaRGYYKDPDATRKLF-AG 438
Cdd:COG1022 393 GDNRIGT------------------VgPPL-----PGVEVKIAEDG-EIlvrGPNVM------KGYYKNPEATAEAFdAD 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 439 GVLHSGDLAVWHADGSIQIQDRAKDIII-SGGENISSVALESMLVTHPDILEAGVVA----------VPD----SHWGER 503
Cdd:COG1022 443 GWLHTGDIGELDEDGFLRITGRKKDLIVtSGGKNVAPQPIENALKASPLIEQAVVVGdgrpflaaliVPDfealGEWAEE 522
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169764941 504 -PKAFVTVKpgKFLTGSEVIEWARNA-----SDISKFMIPREVEVVA--------ELpkTSTGKV-RKNILRDWAK 564
Cdd:COG1022 523 nGLPYTSYA--ELAQDPEVRALIQEEvdranAGLSRAEQIKRFRLLPkeftiengEL--TPTLKLkRKVILEKYAD 594
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
31-559 |
6.37e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 153.27 E-value: 6.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 31 TSFLPRAAAIEPEAVAIH---HVTannqvlrrTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAG 104
Cdd:PRK06178 36 TEYLRAWARERPQRPAIIfygHVI--------TYAELDELSDRFAALLRQRGVGagdRVAVFLPNCPQFHIVFFGILKLG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 105 AVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQEFLSLLQSYRASRPSIPIIV----DMDTDATEGELSGPFDE-VVLEGLT 179
Cdd:PRK06178 108 AVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHVIVtslaDVLPAEPTLPLPDSLRApRLAAAGA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 180 YDLDTGAKGWPGLEAQAASE-DDVIALAYTSGTTARPKGVEYTHRG-CYLAAMGNVIESGLNSHRgrcRYLWTLPMFHAC 257
Cdd:PRK06178 188 IDLLPALRACTAPVPLPPPAlDALAALNYTGGTTGMPKGCEHTQRDmVYTAAAAYAVAVVGGEDS---VFLSFLPEFWIA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 258 GWTFPWAVTAVRG-THYCLRKIDYPQIWKLLKQEHITHfnAAPTVNTLlcnskeAEPLPEP----------VHVTVAA-- 324
Cdd:PRK06178 265 GENFGLLFPLFSGaTLVLLARWDAVAFMAAVERYRVTR--TVMLVDNA------VELMDHPrfaeydlsslRQVRVVSfv 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 325 ---SPPTPHLFEQMTNLNLHPVhVYGMTETY--GPITKGYYLPAWD--NLPSserykkmarqghgFVtSLPVrviktdva 397
Cdd:PRK06178 337 kklNPDYRQRWRALTGSVLAEA-AWGMTETHtcDTFTAGFQDDDFDllSQPV-------------FV-GLPV-------- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 398 EGTVIDVArdGKEIGEIVFVG---NICAR------GYYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISG 468
Cdd:PRK06178 394 PGTEFKIC--DFETGELLPLGaegEIVVRtpsllkGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVN 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 469 GENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIEWARNASDISKfmIPrEVEVVAELPK 548
Cdd:PRK06178 472 GMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYK--VP-EIRIVDALPM 548
|
570
....*....|.
gi 169764941 549 TSTGKVRKNIL 559
Cdd:PRK06178 549 TATGKVRKQDL 559
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
24-561 |
1.51e-39 |
|
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: 151.49 E-value: 1.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 24 NFHTLSPTSF------LPRAAAIEPEAVAIHHVTANNQVLRRTYAETADRARGLAYYLKKHGFKR---VGVLCPNTPAFL 94
Cdd:cd05970 7 NFSINVPENFnfaydvVDAMAKEYPDKLALVWCDDAGEERIFTFAELADYSDKTANFFKAMGIGKgdtVMLTLKRRYEFW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 95 ESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQE--FLSLLQSYRASRPSIPIIVDMDTDATEGELSgpFDE 172
Cdd:cd05970 87 YSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEdnIPEEIEKAAPECPSKPKLVWVGDPVPEGWID--FRK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 173 VVlegltydlDTGAKGWPGLEAQAASEDDVIALAY-TSGTTARPKGVEYTHR---GCYLAAM--GNVIESGLN---SHRG 243
Cdd:cd05970 165 LI--------KNASPDFERPTANSYPCGEDILLVYfSSGTTGMPKMVEHDFTyplGHIVTAKywQNVREGGLHltvADTG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 244 RCRYLWTlpMFHAcGWTFPWAVTAvrgthYCLRKIDYPQIWKLLKQEHITHFNAAPTVNTLLCNSK-EAEPLPEPVHVTV 322
Cdd:cd05970 237 WGKAVWG--KIYG-QWIAGAAVFV-----YDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDlSRYDLSSLRYCTT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 323 AASPPTPHLFE---QMTNLNLhpVHVYGMTETYGPITKgyyLPAWDNLPSSerykkMARQGHGFvtslPVRVIKTDVA-- 397
Cdd:cd05970 309 AGEALNPEVFNtfkEKTGIKL--MEGFGQTETTLTIAT---FPWMEPKPGS-----MGKPAPGY----EIDLIDREGRsc 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 398 ----EGTVIDVARDGKEIGeiVFvgnicaRGYYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENIS 473
Cdd:cd05970 375 eageEGEIVIRTSKGKPVG--LF------GGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIG 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 474 SVALESMLVTHPDILEAGVVAVPDSHWGERPKAFV----TVKPGKFLTgSEVIEWARNASDISKFmiPREVEVVAELPKT 549
Cdd:cd05970 447 PFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIvlakGYEPSEELK-KELQDHVKKVTAPYKY--PRIVEFVDELPKT 523
|
570
....*....|..
gi 169764941 550 STGKVRKNILRD 561
Cdd:cd05970 524 ISGKIRRVEIRE 535
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
187-561 |
1.62e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 151.84 E-value: 1.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 187 KGWPGLEAQAASeDDVIALAYTSGTTARPKGVEYTHRGCYL------AAMGNVIESGlnshrgrCRYLWT-LPMFHACGW 259
Cdd:PRK05677 195 AGQPVTEANPQA-DDVAVLQYTGGTTGVAKGAMLTHRNLVAnmlqcrALMGSNLNEG-------CEILIApLPLYHIYAF 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 260 TFPWAVTAVRGTHYCL--RKIDYPQIWKLLKQEHITHFNAAPTVNTLLCNSKEAEPLP-EPVHVTV----AASPPTPHLF 332
Cdd:PRK05677 267 TFHCMAMMLIGNHNILisNPRDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDfSALKLTLsggmALQLATAERW 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 333 EQMTNLNLhpVHVYGMTETyGPITKGyylpawdNLPSSERYKKMARQghgfVTSLPVRVIKTDVAEGTVidvardgKEIG 412
Cdd:PRK05677 347 KEVTGCAI--CEGYGMTET-SPVVSV-------NPSQAIQVGTIGIP----VPSTLCKVIDDDGNELPL-------GEVG 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 413 EIVFVGNICARGYYKDPDATRKLF-AGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAG 491
Cdd:PRK05677 406 ELCVKGPQVMKGYWQRPEATDEILdSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCA 485
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 492 VVAVPDSHWGERPKAFVTVKPGKFLTGSEVIEWARnaSDISKFMIPREVEVVAELPKTSTGKVRKNILRD 561
Cdd:PRK05677 486 AIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMR--ANLTGYKVPKAVEFRDELPTTNVGKILRRELRD 553
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
31-559 |
5.39e-39 |
|
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: 149.01 E-value: 5.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 31 TSFLPRAAAIEPEAVAIhhVTANNQVlrrTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVN 107
Cdd:cd05920 18 GDLLARSAARHPDRIAV--VDGDRRL---TYRELDRRADRLAAGLRGLGIRpgdRVVVQLPNVAEFVVLFFALLRLGAVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 108 VAVNYRLKEDDIAYIFTHSDVEAIIVDQEFlsllqsyrasrpsipiivdmdtdategelsGPFDEVVLegltydldtgak 187
Cdd:cd05920 93 VLALPSHRRSELSAFCAHAEAVAYIVPDRH------------------------------AGFDHRAL------------ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 188 gwpgLEAQAASEDDVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLNSHrgrCRYLWTLPMFHacgwTFPWAVTA 267
Cdd:cd05920 131 ----ARELAESIPEVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQD---TVYLAVLPAAH----NFPLACPG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 268 VRGTHYC-----LRKIDYPQ-IWKLLKQEHITHFNAAPTVNTLLCNSKEAEPLPEPVH--VTVAASPPTPHLFEQmtnln 339
Cdd:cd05920 200 VLGTLLAggrvvLAPDPSPDaAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLrlLQVGGARLSPALARR----- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 340 LHPV------HVYGMTEtyGPITkgyyLPAWDNLPSseryKKMARQGHGFVTSLPVRVIK---TDVAEGtvidvardgkE 410
Cdd:cd05920 275 VPPVlgctlqQVFGMAE--GLLN----YTRLDDPDE----VIIHTQGRPMSPDDEIRVVDeegNPVPPG----------E 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 411 IGEIVFVGNICARGYYKDPDATRKLF-AGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILE 489
Cdd:cd05920 335 EGELLTRGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHD 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 490 AGVVAVPDSHWGERPKAFVTVKPGKfLTGSEVIEWARNASdISKFMIPREVEVVAELPKTSTGKVRKNIL 559
Cdd:cd05920 415 AAVVAMPDELLGERSCAFVVLRDPP-PSAAQLRRFLRERG-LAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
201-554 |
9.20e-39 |
|
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: 145.11 E-value: 9.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 201 DVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLNSHRgrcRYLWTLPMFHACGWTFPWAVTAVRGTHYCLRKIDY 280
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEAD---VYLNMLPLFHIAGLNLALATFHAGGANVVMEKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 281 PQIWKLLKQEHITHFNAAPTVNTLLCNSKEAEP--LPEPVHVTVAASPPTPHLFEQMTNLNLHPVhvYGMTETYGPITKG 358
Cdd:cd17637 78 AEALELIEEEKVTLMGSFPPILSNLLDAAEKSGvdLSSLRHVLGLDAPETIQRFEETTGATFWSL--YGQTETSGLVTLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 359 yylpawdnlPSSERYKKMARQGhgfvtsLPVRVIKTDVAEGTVidvaRDGkEIGEIVFVGNICARGYYKDPDATRKLFAG 438
Cdd:cd17637 156 ---------PYRERPGSAGRPG------PLVRVRIVDDNDRPV----PAG-ETGEIVVRGPLVFQGYWNLPELTAYTFRN 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 439 GVLHSGDLAVWHADGSIQIQDR--AKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFL 516
Cdd:cd17637 216 GWHHTGDLGRFDEDGYLWYAGRkpEKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATL 295
|
330 340 350
....*....|....*....|....*....|....*...
gi 169764941 517 TGSEVIEWArnASDISKFMIPREVEVVAELPKTSTGKV 554
Cdd:cd17637 296 TADELIEFV--GSRIARYKKPRYVVFVEALPKTADGSI 331
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
197-564 |
1.86e-38 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 148.74 E-value: 1.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 197 ASEDDVIALAYTSGTTARPKGVEYTHrgcylaamgNVIesgLNSHRGRCRYL---WTLPMF------HACGwtFPWAVTA 267
Cdd:PRK06087 184 THGDELAAVLFTSGTEGLPKGVMLTH---------NNI---LASERAYCARLnltWQDVFMmpaplgHATG--FLHGVTA 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 268 --VRGTHYCLRKIDYP-QIWKLLKQEHIT-HFNAAPTVNTLLCNSKEAEPLPEPVHVTVAASPPTP-HLFEQMTNLNLHP 342
Cdd:PRK06087 250 pfLIGARSVLLDIFTPdACLALLEQQRCTcMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPkKVARECQQRGIKL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 343 VHVYGMTETyGPITkgyYLPAWDNLPsseryKKMARQGHGFvTSLPVRVI---KTDVAEGTvidvarDGKEI--GEIVFV 417
Cdd:PRK06087 330 LSVYGSTES-SPHA---VVNLDDPLS-----RFMHTDGYAA-AGVEIKVVdeaRKTLPPGC------EGEEAsrGPNVFM 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 418 GnicargYYKDPDAT-RKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVP 496
Cdd:PRK06087 394 G------YLDEPELTaRALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMP 467
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 497 DSHWGERPKAFVTVK-PGKFLTGSEVIEWARNaSDISKFMIPREVEVVAELPKTSTGKVRKNILR-DWAK 564
Cdd:PRK06087 468 DERLGERSCAYVVLKaPHHSLTLEEVVAFFSR-KRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRkDIMR 536
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
30-561 |
2.61e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 145.46 E-value: 2.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 30 PTSFLPRAAAIE-PEAVAI--HHVTannqvlrRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAA 103
Cdd:PRK07788 50 PFAGLVAHAARRaPDRAALidERGT-------LTYAELDEQSNALARGLLALGVRagdGVAVLARNHRGFVLALYAAGKV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 104 GAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQEFLSLLQSYRASRPSIPIIVDmdtDATEGELSGP----FDEVVleglt 179
Cdd:PRK07788 123 GARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGRLRAWGG---NPDDDEPSGStdetLDDLI----- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 180 ydlDTGAKGWPGLEAQAASeddVIALayTSGTTARPKGVEYTHrgcylaAMGNVIESGLNSH---RGRCRYLWTLPMFHA 256
Cdd:PRK07788 195 ---AGSSTAPLPKPPKPGG---IVIL--TSGTTGTPKGAPRPE------PSPLAPLAGLLSRvpfRAGETTLLPAPMFHA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 257 CGWTFPWAVTAVRGTHYCLRKIDYPQIWKLLKQEHIThfnAAPTVNTLLcnsKEAEPLPEPVH----------VTVAASP 326
Cdd:PRK07788 261 TGWAHLTLAMALGSTVVLRRRFDPEATLEDIAKHKAT---ALVVVPVML---SRILDLGPEVLakydtsslkiIFVSGSA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 327 PTPHLfeqmtnlnlhpvhVYGMTETYGPITkgyYlpawdNLPSSerykkmarqghgfvTSLPVRVIKT--DVAE--GTV- 401
Cdd:PRK07788 335 LSPEL-------------ATRALEAFGPVL---Y-----NLYGS--------------TEVAFATIATpeDLAEapGTVg 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 402 -----IDVA---RDGKEI--GEI--VFVGNICA-RGYYKDPDatrKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISG 468
Cdd:PRK07788 380 rppkgVTVKildENGNEVprGVVgrIFVGNGFPfEGYTDGRD---KQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSG 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 469 GENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIEWARNasDISKFMIPREVEVVAELPK 548
Cdd:PRK07788 457 GENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRD--NLARYKVPRDVVFLDELPR 534
|
570
....*....|...
gi 169764941 549 TSTGKVRKNILRD 561
Cdd:PRK07788 535 NPTGKVLKRELRE 547
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
60-560 |
6.41e-37 |
|
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: 142.22 E-value: 6.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 60 TYAETADRARGLAYYLKKHGF---KRVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQe 136
Cdd:cd05919 12 TYGQLHDGANRLGSALRNLGVssgDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 137 flsllqsyrasrpsipiivdmdtdategelsgpfdevvlegltydldtgakgwpgleaqaaseDDVIALAYTSGTTARPK 216
Cdd:cd05919 91 ---------------------------------------------------------------DDIAYLLYSSGTTGPPK 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 217 GVEYTHRGCYLAA--MGNVIESGLNSHRGRCrylwTLPMFHACGW----TFPWAVTAVrgthyCLRKIDYP---QIWKLL 287
Cdd:cd05919 108 GVMHAHRDPLLFAdaMAREALGLTPGDRVFS----SAKMFFGYGLgnslWFPLAVGAS-----AVLNPGWPtaeRVLATL 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 288 KQEHITHFNAAPTVNTLLCNSKEAEP-LPEPVHVTVAASPPTPH-LFEQMTnlnlhpvhvygmtETYG-PITKGyylpaw 364
Cdd:cd05919 179 ARFRPTVLYGVPTFYANLLDSCAGSPdALRSLRLCVSAGEALPRgLGERWM-------------EHFGgPILDG------ 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 365 dnLPSSErykkmarQGHGFVTSLP--VRVIKTD-VAEGTVID-VARDGKEI-----GEIVFVGNICARGYYKDPDATRKL 435
Cdd:cd05919 240 --IGATE-------VGHIFLSNRPgaWRLGSTGrPVPGYEIRlVDEEGHTIppgeeGDLLVRGPSAAVGYWNNPEKSRAT 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 436 FAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKF 515
Cdd:cd05919 311 FNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAA 390
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 169764941 516 LTGSEVIEWARNASD-ISKFMIPREVEVVAELPKTSTGKVRKNILR 560
Cdd:cd05919 391 PQESLARDIHRHLLErLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
60-565 |
8.33e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 143.29 E-value: 8.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 60 TYAETADRARGLAYYLKKHGFKR---VGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQE 136
Cdd:PRK13391 26 TYRELDERSNRLAHLFRSLGLKRgdhVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 137 FLSLLQSYRASRPSIPIIVDMDTDATegelsgpfdevvLEGLtYDLDTGAKGWPglEAQAASEDDVIALAYTSGTTARPK 216
Cdd:PRK13391 106 KLDVARALLKQCPGVRHRLVLDGDGE------------LEGF-VGYAEAVAGLP--ATPIADESLGTDMLYSSGTTGRPK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 217 GV--EYTHRG----CYLAAMGNviesGLNSHRGRCRYLWTLPMFHACGWTFPWAVTAVRGTHYCLRKIDYPQIWKLLKQE 290
Cdd:PRK13391 171 GIkrPLPEQPpdtpLPLTAFLQ----RLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVMEHFDAEQYLALIEEY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 291 HITHFNAAPTVNTLLCNskeaepLPEPVH----------VTVAASPPTPHLFEQMTnlnlhpvhvygmtETYGPITKGYY 360
Cdd:PRK13391 247 GVTHTQLVPTMFSRMLK------LPEEVRdkydlsslevAIHAAAPCPPQVKEQMI-------------DWWGPIIHEYY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 361 LPAWDN----LPSSERYKKMARQGHGFVTSLpvRVIKTDVAEGTVidvardgKEIGEIVFVGNICARgYYKDPDATRKLF 436
Cdd:PRK13391 308 AATEGLgftaCDSEEWLAHPGTVGRAMFGDL--HILDDDGAELPP-------GEPGTIWFEGGRPFE-YLNDPAKTAEAR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 437 A--GGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVT----V 510
Cdd:PRK13391 378 HpdGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQpvdgV 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 169764941 511 KPGKFLtGSEVIEWARNasDISKFMIPREVEVVAELPKTSTGKVRKNILRD--WAKG 565
Cdd:PRK13391 458 DPGPAL-AAELIAFCRQ--RLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDryWGNK 511
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
58-561 |
1.94e-36 |
|
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: 142.29 E-value: 1.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 58 RRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVD 134
Cdd:TIGR02262 30 SLSYGELEAQVRRLAAALRRLGVKreeRVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 135 QEFLSLLQSYRASRPSIPIIVdMDTDATEGELSgpFDEVVlegltydldtgAKGWPGLEAQAASEDDVIALAYTSGTTAR 214
Cdd:TIGR02262 110 GALLPVIKAALGKSPHLEHRV-VVGRPEAGEVQ--LAELL-----------ATESEQFKPAATQADDPAFWLYSSGSTGM 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 215 PKGVEYTHRGCYLAA---MGNVIesglnSHRGRCRYLWTLPMFHACG----WTFPWAVTAvrgTHYCLRKIDYP-QIWKL 286
Cdd:TIGR02262 176 PKGVVHTHSNPYWTAelyARNTL-----GIREDDVCFSAAKLFFAYGlgnaLTFPMSVGA---TTVLMGERPTPdAVFDR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 287 LKQEHITHFNAAPT----------------VNTLLCNSKeAEPLPEPVH-----------VTVAASPPTPHLFeqMTNLN 339
Cdd:TIGR02262 248 LRRHQPTIFYGVPTlyaamladpnlpsedqVRLRLCTSA-GEALPAEVGqrwqarfgvdiVDGIGSTEMLHIF--LSNLP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 340 lHPVHvYGmteTYGPITKGYYLpawdnlpsserykKMARQGHGfvtslpvrviktDVAEGtvidvardgkEIGEIVFVGN 419
Cdd:TIGR02262 325 -GDVR-YG---TSGKPVPGYRL-------------RLVGDGGQ------------DVADG----------EPGELLISGP 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 420 ICARGYYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSH 499
Cdd:TIGR02262 365 SSATMYWNNRAKSRDTFQGEWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADED 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169764941 500 WGERPKAFVTVKPGKFLTGSEVIEWARNAsdISKFMIPREVEVVAELPKTSTGKVRKNILRD 561
Cdd:TIGR02262 445 GLIKPKAFVVLRPGQTALETELKEHVKDR--LAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
167-561 |
2.64e-36 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 142.67 E-value: 2.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 167 SGPFDEVVLEGLTYDLDTGAKGWPGLeAQAASEDDVIALAYTSGTTARPKGVEYTHRGcYLAAMGNVI--ESGLNSHRGR 244
Cdd:PLN02574 166 NYDFDSKRIEFPKFYELIKEDFDFVP-KPVIKQDDVAAIMYSSGTTGASKGVVLTHRN-LIAMVELFVrfEASQYEYPGS 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 245 CR-YLWTLPMFHACGWT-FPWAVTAVRGTHYCLRKIDYPQIWKLLKQEHITHFNAAPTVNTLLCNSKE---AEPLPEPVH 319
Cdd:PLN02574 244 DNvYLAALPMFHIYGLSlFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKgvcGEVLKSLKQ 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 320 VTVAASPPTPHLFEQMTNLNLHP--VHVYGMTETYGPITKGYylpawdnlpSSERYKKMARQGHgFVTSLPVRVIktDVA 397
Cdd:PLN02574 324 VSCGAAPLSGKFIQDFVQTLPHVdfIQGYGMTESTAVGTRGF---------NTEKLSKYSSVGL-LAPNMQAKVV--DWS 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 398 EGTVIDVArdgkEIGEIVFVGNICARGYYKDPDATR-KLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVA 476
Cdd:PLN02574 392 TGCLLPPG----NCGELWIQGPGVMKGYLNNPKATQsTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPAD 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 477 LESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIEWArnASDISKFMIPREVEVVAELPKTSTGKVRK 556
Cdd:PLN02574 468 LEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYV--AKQVAPYKKVRKVVFVQSIPKSPAGKILR 545
|
....*
gi 169764941 557 NILRD 561
Cdd:PLN02574 546 RELKR 550
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
165-561 |
3.81e-36 |
|
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: 140.98 E-value: 3.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 165 ELSGPFDEVVLEGLTYDLDtgakGWPGLEAQAASEDDVI--------ALAYTSGTTARPKGVEYTHRGCYLAAMGNVIES 236
Cdd:cd05929 86 EIKAAALVCGLFTGGGALD----GLEDYEAAEGGSPETPiedeaagwKMLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 237 GLNSHRGRCRYLWTLPMFHACGwtFPWAVTAVR--GTHYCLRKIDYPQIWKLLKQEHITHFNAAPTV-NTLLcnskeaeP 313
Cdd:cd05929 162 LGFGPGADSVYLSPAPLYHAAP--FRWSMTALFmgGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMfVRLL-------K 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 314 LPEPVH----------VTVAASPPTPHLFEQMTNLnlhpvhvygmtetYGPITKGYYlpawdnlPSSERykkmarQGHGF 383
Cdd:cd05929 233 LPEAVRnaydlsslkrVIHAAAPCPPWVKEQWIDW-------------GGPIIWEYY-------GGTEG------QGLTI 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 384 VTSL-----PVRVIKtdVAEGTVIDVARDGKE-----IGEIVFVGNiCARGYYKDPDATRKLF-AGGVLHSGDLAVWHAD 452
Cdd:cd05929 287 INGEewlthPGSVGR--AVLGKVHILDEDGNEvppgeIGEVYFANG-PGFEYTNDPEKTAAARnEGGWSTLGDVGYLDED 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 453 GSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKF---LTGSEVIEWARNAs 529
Cdd:cd05929 364 GYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADagtALAEELIAFLRDR- 442
|
410 420 430
....*....|....*....|....*....|..
gi 169764941 530 dISKFMIPREVEVVAELPKTSTGKVRKNILRD 561
Cdd:cd05929 443 -LSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
200-560 |
4.21e-35 |
|
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: 135.69 E-value: 4.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 200 DDVIALAYTSGTTARPKGVEYTHRG-CYLAAMGNViesgLNSHRGRCRYLWTLPMFHACGWTFPWAVTAVRGTHYCL--- 275
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNeVYNAWMLAL----NSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLagp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 276 ----RKIDYPQIWKLLKQEHITHFNAAPTVNTLLCNSKEAEPLPEPVHVTVAASPPTPHL---FEQMTNLNLhpVHVYGM 348
Cdd:cd05944 78 agyrNPGLFDNFWKLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVELrarFEDATGLPV--VEGYGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 349 TETYGPITKgyylpawdNLPSSEryKKMARQGHGFvTSLPVRVIKTDVAEGTVIDVARDgkEIGEIVFVGNICARGYYKD 428
Cdd:cd05944 156 TEATCLVAV--------NPPDGP--KRPGSVGLRL-PYARVRIKVLDGVGRLLRDCAPD--EVGEICVAGPGVFGGYLYT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 429 PDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFV 508
Cdd:cd05944 223 EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYV 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 169764941 509 TVKPGKFLTGSEVIEWARNASDiSKFMIPREVEVVAELPKTSTGKVRKNILR 560
Cdd:cd05944 303 QLKPGAVVEEEELLAWARDHVP-ERAAVPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
193-562 |
6.02e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 137.63 E-value: 6.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 193 EAQAASEDDVIALAYTSGTTARPKGVEYTHRGCYLAAmgnvIESGLNSHRG-RCRYLWTLPMFHACGwtfpwAVTAVRGT 271
Cdd:PRK09088 128 DTPSIPPERVSLILFTSGTSGQPKGVMLSERNLQQTA----HNFGVLGRVDaHSSFLCDAPMFHIIG-----LITSVRPV 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 272 ---------------HYCLRKIDYPQIwkllkqeHITHFNAAPTVNTLLcnskEAEPLPEPV---HVTVAASPPTPHLFE 333
Cdd:PRK09088 199 lavggsilvsngfepKRTLGRLGDPAL-------GITHYFCVPQMAQAF----RAQPGFDAAalrHLTALFTGGAPHAAE 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 334 QMT---NLNLHPVHVYGMTETyGPItkgYYLPAWDNLPSSerykKMARQGhgfvtsLPVRVIKTDVAEGTVIDVArdGKE 410
Cdd:PRK09088 268 DILgwlDDGIPMVDGFGMSEA-GTV---FGMSVDCDVIRA----KAGAAG------IPTPTVQTRVVDDQGNDCP--AGV 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 411 IGEIVFVGNICARGYYKDPDATRKLFAG-GVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILE 489
Cdd:PRK09088 332 PGELLLRGPNLSPGYWRRPQATARAFTGdGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRE 411
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169764941 490 AGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIEWArnASDISKFMIPREVEVVAELPKTSTGKVRKNILRDW 562
Cdd:PRK09088 412 CAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHL--STRLAKYKVPKHLRLVDALPRTASGKLQKARLRDA 482
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
62-561 |
9.98e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 134.81 E-value: 9.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 62 AETADRARGLAYYLKKHGFKRVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQEFLSLL 141
Cdd:PRK07867 36 RGSAARAAALRARLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 142 QSyraSRPSIPIiVDMDTDATEGELSGPFDEVVlegltydldtgakgwpglEAQAASEDDVIALAYTSGTTARPKGVEYT 221
Cdd:PRK07867 116 DG---LDPGVRV-INVDSPAWADELAAHRDAEP------------------PFRVADPDDLFMLIFTSGTSGDPKAVRCT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 222 HRgcYLAAMGNViesgLNSHRGRCR----YLwTLPMFHACGWTFPWAVTAVRGTHYCLR-KIDYPQIWKLLKQEHITHFN 296
Cdd:PRK07867 174 HR--KVASAGVM----LAQRFGLGPddvcYV-SMPLFHSNAVMAGWAVALAAGASIALRrKFSASGFLPDVRRYGATYAN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 297 aapTVNTLLCNSKEAEPLPEPVHVTV------AASPPTPHLFEqmTNLNLHPVHVYGMTETYGPITKGYYLPAwdnlpss 370
Cdd:PRK07867 247 ---YVGKPLSYVLATPERPDDADNPLrivygnEGAPGDIARFA--RRFGCVVVDGFGSTEGGVAITRTPDTPP------- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 371 erykkmarqghGFVTSLPVRVIKTDVAEGT-----VIDVARDG---KEIGEIV-FVGNICARGYYKDPDATRKLFAGGVL 441
Cdd:PRK07867 315 -----------GALGPLPPGVAIVDPDTGTecppaEDADGRLLnadEAIGELVnTAGPGGFEGYYNDPEADAERMRGGVY 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 442 HSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEV 521
Cdd:PRK07867 384 WSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAF 463
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 169764941 522 IEWARNASDISKFMIPREVEVVAELPKTSTGKVRKNILRD 561
Cdd:PRK07867 464 AEFLAAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
58-564 |
1.56e-32 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 130.97 E-value: 1.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 58 RRTYAETADRARGLAYYLKKHGFKR---VGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVD 134
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLAALGVRPgdcVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 135 QEFLsllqsyRASRPSIPIIVDMDTDATEGELSGPFdevvleGLTYDLDT---GAKGWPG-LEAQAASEDDVIA----LA 206
Cdd:PRK12406 91 ADLL------HGLASALPAGVTVLSVPTPPEIAAAY------RISPALLTppaGAIDWEGwLAQQEPYDGPPVPqpqsMI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 207 YTSGTTARPKGVEYTHRGCYLAA-MGNVIESGLNSHRGrCRYLWTLPMFHACGWTFPWAVTAVRGTHYCLRKIDYPQIWK 285
Cdd:PRK12406 159 YTSGTTGHPKGVRRAAPTPEQAAaAEQMRALIYGLKPG-IRALLTGPLYHSAPNAYGLRAGRLGGVLVLQPRFDPEELLQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 286 LLKQEHITHFNAAPTVNTLLCNskeaepLPEPV----------HVTVAASPPTPHLFEQMTNLnLHPV--HVYGMTETyG 353
Cdd:PRK12406 238 LIERHRITHMHMVPTMFIRLLK------LPEEVrakydvsslrHVIHAAAPCPADVKRAMIEW-WGPViyEYYGSTES-G 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 354 PITkgyylpawdnLPSSERYkkmarqghgfvTSLPVRVIKtdVAEGTVID-VARDGKE--IGEIvfvGNICAR------- 423
Cdd:PRK12406 310 AVT----------FATSEDA-----------LSHPGTVGK--AAPGAELRfVDEDGRPlpQGEI---GEIYSRiagnpdf 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 424 GYYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGER 503
Cdd:PRK12406 364 TYHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEA 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169764941 504 PKAFVTVKPGKFLTGSEVIEWARNAsdISKFMIPREVEVVAELPKTSTGKVRKNILRD--WAK 564
Cdd:PRK12406 444 LMAVVEPQPGATLDEADIRAQLKAR--LAGYKVPKHIEIMAELPREDSGKIFKRRLRDpyWAN 504
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
190-561 |
1.86e-32 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 130.77 E-value: 1.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 190 PGLEAQAASEDDVIALAYTSGTTARPKGVEYTHrgcylaamGNVIESGLNSH-----RGRCRYLWTLPMFHACGWTFPWA 264
Cdd:PRK07514 146 DDFETVPRGADDLAAILYTSGTTGRSKGAMLSH--------GNLLSNALTLVdywrfTPDDVLIHALPIFHTHGLFVATN 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 265 VT-AVRGTHYCLRKIDYPQIWKLLKQEhiTHFNAAPTVNT-LLCNSKEAEPLPEPVHVTVAASPP----TPHLFEQMTNl 338
Cdd:PRK07514 218 VAlLAGASMIFLPKFDPDAVLALMPRA--TVMMGVPTFYTrLLQEPRLTREAAAHMRLFISGSAPllaeTHREFQERTG- 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 339 nlHPV-HVYGMTETygpitkgyylpawdNLPSSERYKKMARQGH-GFvtSLP---VRVikTDVAEGTVidVARDgkEIGE 413
Cdd:PRK07514 295 --HAIlERYGMTET--------------NMNTSNPYDGERRAGTvGF--PLPgvsLRV--TDPETGAE--LPPG--EIGM 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 414 I------VFvgnicaRGYYKDPDATRKLF-AGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPD 486
Cdd:PRK07514 351 IevkgpnVF------KGYWRMPEKTAEEFrADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPG 424
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169764941 487 ILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIewARNASDISKFMIPREVEVVAELPKTSTGKVRKNILRD 561
Cdd:PRK07514 425 VVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAIL--AALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLRE 497
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
42-554 |
6.98e-32 |
|
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: 128.03 E-value: 6.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 42 PEAVAihhVTANNQVLrrTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIaaagavnvavnyrLK--- 115
Cdd:cd05930 1 PDAVA---VVDGDQSL--TYAELDARANRLARYLRERGVGpgdLVAVLLERSLEMVVAILAV-------------LKaga 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 116 ----------EDDIAYIFTHSDVEAIIVDQeflsllqsyrasrpsipiivdmdtdategelsgpfdevvlegltydldtg 185
Cdd:cd05930 63 ayvpldpsypAERLAYILEDSGAKLVLTDP-------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 186 akgwpgleaqaaseDDVIALAYTSGTTARPKGVEYTHRGC--YLAAMGNVIESGlnshrGRCRYL-WTLPMFHACGWTFP 262
Cdd:cd05930 93 --------------DDLAYVIYTSGSTGKPKGVMVEHRGLvnLLLWMQEAYPLT-----PGDRVLqFTSFSFDVSVWEIF 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 263 WAVTAvRGTHYCLRK---IDYPQIWKLLKQEHITHFNAAPTVNTLLCNSKEAEPLPEPVHVTVAASPPTPHLFEQMTNLN 339
Cdd:cd05930 154 GALLA-GATLVVLPEevrKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSLRLVLVGGEALPPDLVRRWRELL 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 340 LHP--VHVYGMTE-----TYGPITKGyylpawdnlpsserykkmaRQGHGFVTslpvrvIKTDVAeGTVIDVaRDGK--- 409
Cdd:cd05930 233 PGArlVNLYGPTEatvdaTYYRVPPD-------------------DEEDGRVP------IGRPIP-NTRVYV-LDENlrp 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 410 ----EIGEIVFVGNICARGYYKDPDATRKLF------AGGVLH-SGDLAVWHADGSIQIQDRAKDII-ISG-----GEni 472
Cdd:cd05930 286 vppgVPGELYIGGAGLARGYLNRPELTAERFvpnpfgPGERMYrTGDLVRWLPDGNLEFLGRIDDQVkIRGyrielGE-- 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 473 ssvaLESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIEWARNAsdISKFMIPREVEVVAELPKTSTG 552
Cdd:cd05930 364 ----IEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAER--LPDYMVPSAFVVLDALPLTPNG 437
|
..
gi 169764941 553 KV 554
Cdd:cd05930 438 KV 439
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
127-561 |
2.04e-31 |
|
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: 126.78 E-value: 2.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 127 DVEAIIVDQEF---LSLLQSYRASRPSIPIIVDMDTDATEGELSgpfdevvlegltydlDTGAKGWPGLEAqaaseDDVI 203
Cdd:cd05971 32 DRVGVFLSQGPecaIAHIAILRSGAIAVPLFALFGPEALEYRLS---------------NSGASALVTDGS-----DDPA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 204 ALAYTSGTTARPKGVEYTHRgCYLAAMGNViESGLNSHRGRCRYLWTLPMFhacGWT-------FPWAVTAVRGTHYCLR 276
Cdd:cd05971 92 LIIYTSGTTGPPKGALHAHR-VLLGHLPGV-QFPFNLFPRDGDLYWTPADW---AWIgglldvlLPSLYFGVPVLAHRMT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 277 KIDYPQIWKLLKQEHITHFNAAPTVNTLLcnsKEAEPLPEPVHVTVAA------SPPTPHLFEQMTNLNLHPVHVYGMTE 350
Cdd:cd05971 167 KFDPKAALDLMSRYGVTTAFLPPTALKMM---RQQGEQLKHAQVKLRAiatggeSLGEELLGWAREQFGVEVNEFYGQTE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 351 TYGPITKGyylPAWdnlpSSERYKKMARQGHGFVtslpVRVIKtdvAEGTVIdvardgkEIGEivfVGNICAR------- 423
Cdd:cd05971 244 CNLVIGNC---SAL----FPIKPGSMGKPIPGHR----VAIVD---DNGTPL-------PPGE---VGEIAVElpdpvaf 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 424 -GYYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGE 502
Cdd:cd05971 300 lGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGE 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169764941 503 RPKAFVTVKPGkfLTGSEVIewarnASDISKFM--------IPREVEVVAELPKTSTGKVRKNILRD 561
Cdd:cd05971 380 IVKAFVVLNPG--ETPSDAL-----AREIQELVktrlaaheYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
178-560 |
2.90e-31 |
|
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: 126.44 E-value: 2.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 178 LTYDLDTGAKGWPGLEAQAASEDDVIALAYTSGTTARPKGVEYTHRGCYLAAMG---NVIESglnshRGRCRYLWTLPMF 254
Cdd:cd05958 75 LAYILDKARITVALCAHALTASDDICILAFTSGTTGAPKATMHFHRDPLASADRyavNVLRL-----REDDRFVGSPPLA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 255 HACGW----TFPWAVTAvrgTHYCLRKIDYPQIWKLLKQEHITHFNAAPTV-NTLLCNSKEAEPLPEPVHVTVAASPPTP 329
Cdd:cd05958 150 FTFGLggvlLFPFGVGA---SGVLLEEATPDLLLSAIARYKPTVLFTAPTAyRAMLAHPDAAGPDLSSLRKCVSAGEALP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 330 hlfeqmtnlnlHPVHvYGMTETYGpitkgyyLPAWDNLPSSERYkkmarqgHGFVTSLP--VRVIKTdvaeGTVID---- 403
Cdd:cd05958 227 -----------AALH-RAWKEATG-------IPIIDGIGSTEMF-------HIFISARPgdARPGAT----GKPVPgyea 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 404 --VARDGKEI--GEIvfvGNICARG----YYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSV 475
Cdd:cd05958 277 kvVDDEGNPVpdGTI---GRLAVRGptgcRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPP 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 476 ALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKflTGSEVIewARNASD-----ISKFMIPREVEVVAELPKTS 550
Cdd:cd05958 354 EVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGV--IPGPVL--ARELQDhakahIAPYKYPRAIEFVTELPRTA 429
|
410
....*....|
gi 169764941 551 TGKVRKNILR 560
Cdd:cd05958 430 TGKLQRFALR 439
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
60-564 |
4.21e-31 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 127.44 E-value: 4.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 60 TYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVN--YRLKEddIAYIFTHSDVEAIIVD 134
Cdd:PRK07059 50 TYGELDELSRALAAWLQSRGLAkgaRVAIMMPNVLQYPVAIAAVLRAGYVVVNVNplYTPRE--LEHQLKDSGAEAIVVL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 135 QEFLSLLQSYRASRPSIPIIVdmdtdATEGELSG--------------------------PFDEVVLEGltydldtgakG 188
Cdd:PRK07059 128 ENFATTVQQVLAKTAVKHVVV-----ASMGDLLGfkghivnfvvrrvkkmvpawslpghvRFNDALAEG----------A 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 189 WPGLEAQAASEDDVIALAYTSGTTARPKGVEYTHRGcylaAMGNVIESGL-----NSHRGRCRYLWT---LPMFHACGWT 260
Cdd:PRK07059 193 RQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRN----IVANVLQMEAwlqpaFEKKPRPDQLNFvcaLPLYHIFALT 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 261 FPWAVTAVRGTHYCL----RkiDYPQIWKLLKQEHITHFnaaPTVNTL---LCNSKEAEPLP-EPVHVT----VAASPPT 328
Cdd:PRK07059 269 VCGLLGMRTGGRNILipnpR--DIPGFIKELKKYQVHIF---PAVNTLynaLLNNPDFDKLDfSKLIVAngggMAVQRPV 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 329 PHLFEQMTNLnlhpvhvygmtetygPITKGYYLpawdnlpsSErykkmarqghgfvTSLPVRVIKTDVAE--GTV----- 401
Cdd:PRK07059 344 AERWLEMTGC---------------PITEGYGL--------SE-------------TSPVATCNPVDATEfsGTIglplp 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 402 -IDVA-RD--GKE--IGEivfVGNICARG------YYKDPDATRK-LFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISG 468
Cdd:PRK07059 388 sTEVSiRDddGNDlpLGE---PGEICIRGpqvmagYWNRPDETAKvMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVS 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 469 GENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVtVKPGKFLTGSEVIEWArnASDISKFMIPREVEVVAELPK 548
Cdd:PRK07059 465 GFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFV-VKKDPALTEEDVKAFC--KERLTNYKRPKFVEFRTELPK 541
|
570
....*....|....*.
gi 169764941 549 TSTGKVRKNILRDWAK 564
Cdd:PRK07059 542 TNVGKILRRELRDGKA 557
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
199-560 |
3.80e-30 |
|
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: 123.01 E-value: 3.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 199 EDDVIALAYTSGTTARPKGVEYTHRgcYLAAMGNVIESGLNSHRGRCryLWTL--PmfhacGWTFP--WAVTA--VRGTH 272
Cdd:cd05973 87 DSDPFVMMFTSGTTGLPKGVPVPLR--ALAAFGAYLRDAVDLRPEDS--FWNAadP-----GWAYGlyYAITGplALGHP 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 273 YCLRKIDY--PQIWKLLKQEHITHFNAAPTVNTLLCNSKEAEPLPEPVHVTVAAS---PPTPHLFEQM-TNLNLhPVH-V 345
Cdd:cd05973 158 TILLEGGFsvESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPKGRLRRVSSagePLTPEVIRWFdAALGV-PIHdH 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 346 YGMTETYGPI-------------TKGYYLPAWdnlpsseRYKKMARQGHGFVTSLPVRViktdvaegtVIDVARDGKeig 412
Cdd:cd05973 237 YGQTELGMVLanhhalehpvhagSAGRAMPGW-------RVAVLDDDGDELGPGEPGRL---------AIDIANSPL--- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 413 eivfvgnICARGYYKDPDATrklFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGV 492
Cdd:cd05973 298 -------MWFRGYQLPDTPA---IDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAV 367
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169764941 493 VAVPDSHWGERPKAFVTVKPGKFLTGSEVIEWARNA-SDISKFMIPREVEVVAELPKTSTGKVRKNILR 560
Cdd:cd05973 368 IGVPDPERTEVVKAFVVLRGGHEGTPALADELQLHVkKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
60-494 |
5.34e-30 |
|
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: 122.70 E-value: 5.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 60 TYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDqe 136
Cdd:cd05907 7 TWAEFAEEVRALAKGLIALGVEpgdRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 137 flsllqsyrasrpsipiivdmdtdategelsgpfdevvlegltydldtgakgWPgleaqaaseDDVIALAYTSGTTARPK 216
Cdd:cd05907 85 ----------------------------------------------------DP---------DDLATIIYTSGTTGRPK 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 217 GVEYTHRgCYLAAMGNVIEsgLNSHRGRCRYLWTLPMFHacgwtfpwaVTAVRGTHYclrkidYPqiwkLLKQEHITHfn 296
Cdd:cd05907 104 GVMLSHR-NILSNALALAE--RLPATEGDRHLSFLPLAH---------VFERRAGLY------VP----LLAGARIYF-- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 297 aAPTVNTLLCNSKEAEP--------LPEPVH--------------------------VTVAASPPTPHLFEQMTNLNLhP 342
Cdd:cd05907 160 -ASSAETLLDDLSEVRPtvflavprVWEKVYaaikvkavpglkrklfdlavggrlrfAASGGAPLPAELLHFFRALGI-P 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 343 VH-VYGMTETYGPITkgyYLPAWDNlpsserykKMARQGHgfvtslpvrviktdVAEGTVIDVARDGkeigEIVFVGNIC 421
Cdd:cd05907 238 VYeGYGLTETSAVVT---LNPPGDN--------RIGTVGK--------------PLPGVEVRIADDG----EILVRGPNV 288
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169764941 422 ARGYYKDPDATRK-LFAGGVLHSGDLAVWHADGSIQIQDRAKDIII-SGGENISSVALESMLVTHPDILEAGVVA 494
Cdd:cd05907 289 MLGYYKNPEATAEaLDADGWLHTGDLGEIDEDGFLHITGRKKDLIItSGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
32-559 |
9.70e-30 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 122.97 E-value: 9.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 32 SFLPRAAAIEPEAVAIHHvtaNNQVLrrTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNV 108
Cdd:TIGR03098 4 HLLEDAAARLPDATALVH---HDRTL--TYAALSERVLALASGLRGLGLArgeRVAIYLDKRLETVTAMFGAALAGGVFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 109 AVNYRLKEDDIAYIFTHSDVEAIIVDQEFLSLLQSYRASRPSIPIIVDMDtDATEGELSGPFDEVVlegltyDLDTGAKG 188
Cdd:TIGR03098 79 PINPLLKAEQVAHILADCNVRLLVTSSERLDLLHPALPGCHDLRTLIIVG-DPAHASEGHPGEEPA------SWPKLLAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 189 WPGLEAQAASEDDVIALAYTSGTTARPKGVEYTHRGCYLAAMgnVIESGLNSHRGRcRYLWTLPMFHACGwtFPWAVTAV 268
Cdd:TIGR03098 152 GDADPPHPVIDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQ--SVATYLENRPDD-RLLAVLPLSFDYG--FNQLTTAF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 269 R-GTHYCLRKIDYPQ-IWKLLKQEHITHFNAAPTVNTLLCNSK---EAEPLPEPVHVTVAASPP--TPHLFEQMTNLNLH 341
Cdd:TIGR03098 227 YvGATVVLHDYLLPRdVLKALEKHGITGLAAVPPLWAQLAQLDwpeSAAPSLRYLTNSGGAMPRatLSRLRSFLPNARLF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 342 PvhVYGMTETYgpitKGYYLPA--WDNLPSSerykkMARQghgfVTSLPVRVIKTDVAEGTVidvardgKEIGEIVFVGN 419
Cdd:TIGR03098 307 L--MYGLTEAF----RSTYLPPeeVDRRPDS-----IGKA----IPNAEVLVLREDGSECAP-------GEEGELVHRGA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 420 ICARGYYKDPDATRKLFA-----GGVLHSGDLAVWHAD-------GSIQIQDRAKDIIISGGENISSVALESMLVTHPDI 487
Cdd:TIGR03098 365 LVAMGYWNDPEKTAERFRplppfPGELHLPELAVWSGDtvrrdeeGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLV 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169764941 488 LEAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIEWARNAsdISKFMIPREVEVVAELPKTSTGKVRKNIL 559
Cdd:TIGR03098 445 AEAVAFGVPDPTLGQAIVLVVTPPGGEELDRAALLAECRAR--LPNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
200-555 |
1.16e-29 |
|
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: 119.33 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 200 DDVIALaYTSGTTARPKGVEYTHRGcyLAAMgNVIESGLNSHRGRCRYLWTLPMFHACGWTFPWAVTAVRGTHYCLRKID 279
Cdd:cd17636 1 DPVLAI-YTAAFSGRPNGALLSHQA--LLAQ-ALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFVRRVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 280 YPQIWKLLKQEHITH-FNAAPTVNTLLCNSKEAEPlpepvHVTVAASPPTPHLFEQMTNLNLHPVHV----YGMTETYGP 354
Cdd:cd17636 77 AEEVLELIEAERCTHaFLLPPTIDQIVELNADGLY-----DLSSLRSSPAAPEWNDMATVDTSPWGRkpggYGQTEVMGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 355 ITKGYYlpAWDNLPSSERYKKMARqghgfvtslpVRVIKTDVAEgtvidVArDGkEIGEIVFVGNICARGYYKDPDATRK 434
Cdd:cd17636 152 ATFAAL--GGGAIGGAGRPSPLVQ----------VRILDEDGRE-----VP-DG-EVGEIVARGPTVMAGYWNRPEVNAR 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 435 LFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGK 514
Cdd:cd17636 213 RTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGA 292
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 169764941 515 FLTGSEVIEWARNAsdISKFMIPREVEVVAELPKTSTGKVR 555
Cdd:cd17636 293 SVTEAELIEHCRAR--IASYKKPKSVEFADALPRTAGGADD 331
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
192-564 |
2.95e-29 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 121.91 E-value: 2.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 192 LEAQAASEDDVIALAYTSGTTARPKGVEYTHR---------GCYLAAMGNVIEsglnshrGRCRYLWTLPMFHACGWTFP 262
Cdd:PRK08751 200 MPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRnlvanmqqaHQWLAGTGKLEE-------GCEVVITALPLYHIFALTAN 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 263 WAVTAVRG--THYCLRKIDYPQIWKLLKQehiTHFNAAPTVNTL---LCNSKEAEPLP-EPVHVTV----AASPPTPHLF 332
Cdd:PRK08751 273 GLVFMKIGgcNHLISNPRDMPGFVKELKK---TRFTAFTGVNTLfngLLNTPGFDQIDfSSLKMTLgggmAVQRSVAERW 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 333 EQMTNLNLhpVHVYGMTETYgpitkgyylPAWDNLPsserykkMARQGHGFVTSLPV----RVIKTDvaEGTVIDVArdg 408
Cdd:PRK08751 350 KQVTGLTL--VEAYGLTETS---------PAACINP-------LTLKEYNGSIGLPIpstdACIKDD--AGTVLAIG--- 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 409 kEIGEIVFVGNICARGYYKDPDATRKLF-AGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDI 487
Cdd:PRK08751 407 -EIGELCIKGPQVMKGYWKRPEETAKVMdADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGV 485
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169764941 488 LEAGVVAVPDSHWGERPKAfVTVKPGKFLTGSEVIEWARnaSDISKFMIPREVEVVAELPKTSTGKVRKNILRDWAK 564
Cdd:PRK08751 486 LEVAAVGVPDEKSGEIVKV-VIVKKDPALTAEDVKAHAR--ANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAAK 559
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
17-563 |
3.33e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 121.39 E-value: 3.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 17 PGAEQRVNFHTLsptsfLPRAAAIEPEAVAIhhvTANNQVLrrTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAF 93
Cdd:PRK06164 4 DAAPRADTLASL-----LDAHARARPDAVAL---IDEDRPL--SRAELRALVDRLAAWLAAQGVRrgdRVAVWLPNCIEW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 94 LESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQEFLSLLQSYR------ASRPSIP--IIVDMDTDATEGE 165
Cdd:PRK06164 74 VVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPGFKGIDFAAIlaavppDALPPLRaiAVVDDAADATPAP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 166 LsgPFDEVVLEGLTYDLDTGAKGWPgleaqaASEDDVIALAYT-SGTTARPKGVeyTHRGCYLAAMGNVIESGLNSHRGR 244
Cdd:PRK06164 154 A--PGARVQLFALPDPAPPAAAGER------AADPDAGALLFTtSGTTSGPKLV--LHRQATLLRHARAIARAYGYDPGA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 245 CrYLWTLPMFHACGWTFPWAVTAVRGTHYCLRKIDYPQIWKLLKQEHITH-FNAAPTVNTLLCNSKEAEPLPEPVHVTVA 323
Cdd:PRK06164 224 V-LLAALPFCGVFGFSTLLGALAGGAPLVCEPVFDAARTARALRRHRVTHtFGNDEMLRRILDTAGERADFPSARLFGFA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 324 ASPPTPHLFEQMTNLNLHPVH-VYGMTETYGPITkgyylpAWD-NLPSSERYkkmarQGHGFVTSLPVRVIKTDVAEGTV 401
Cdd:PRK06164 303 SFAPALGELAALARARGVPLTgLYGSSEVQALVA------LQPaTDPVSVRI-----EGGGRPASPEARVRARDPQDGAL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 402 IDvarDGkEIGEIVFVGNICARGYYKDPDATRKLF-AGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESM 480
Cdd:PRK06164 372 LP---DG-ESGEIEIRAPSLMRGYLDNPDATARALtDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHA 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 481 LVTHPDILEAGVVAVpdSHWGE-RPKAFVTVKPGKFLTGSEVIEWARNAsdISKFMIPREVEVVAELPKTSTG---KVRK 556
Cdd:PRK06164 448 LEALPGVAAAQVVGA--TRDGKtVPVAFVIPTDGASPDEAGLMAACREA--LAGFKVPARVQVVEAFPVTESAngaKIQK 523
|
....*..
gi 169764941 557 NILRDWA 563
Cdd:PRK06164 524 HRLREMA 530
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
9-561 |
3.60e-29 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 121.40 E-value: 3.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 9 SGLLGHFVP-------GAEQRVNFhtlSPTSFLPRAAAIEPEAVAIhhvtaNNQVLRRTYAETADRARGLAYYLKKHGF- 80
Cdd:PRK13382 20 AGLIAPMRPdrylrivAAMRREGM---GPTSGFAIAAQRCPDRPGL-----IDELGTLTWRELDERSDALAAALQALPIg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 81 --KRVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQEFLSLLQSYRASRPSIPIIVDMD 158
Cdd:PRK13382 92 epRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEEFSATVDRALADCPQATRIVAWT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 159 TDAtegelsgpfDEVVLEGLTydlDTGAkgwpGLEAQAASED-DVIALayTSGTTARPKGVEYTHRGCYLAAMGNVIESG 237
Cdd:PRK13382 172 DED---------HDLTVEVLI---AAHA----GQRPEPTGRKgRVILL--TSGTTGTPKGARRSGPGGIGTLKAILDRTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 238 LNSHRgrcRYLWTLPMFHACGWTFPWAVTAVRGTHYCLRKIDYPQIWKLLKQEHITHFNAAPTVNTLLCNskeaepLPEP 317
Cdd:PRK13382 234 WRAEE---PTVIVAPMFHAWGFSQLVLAASLACTIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMD------LPAE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 318 VH-------VTVAASPPTPhlfeqmtnlnLHPVHVYGMTETYGPITkgyylpaWDNLPSSEryKKMArqghgfVTSLPV- 389
Cdd:PRK13382 305 VRnrysgrsLRFAAASGSR----------MRPDVVIAFMDQFGDVI-------YNNYNATE--AGMI------ATATPAd 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 390 --RVIKT--DVAEGTVIDVA-RDGKEI--GEivfVGNICAR------GYykdPDATRKLFAGGVLHSGDLAVWHADGSIQ 456
Cdd:PRK13382 360 lrAAPDTagRPAEGTEIRILdQDFREVptGE---VGTIFVRndtqfdGY---TSGSTKDFHDGFMASGDVGYLDENGRLF 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 457 IQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIEWARNasDISKFMI 536
Cdd:PRK13382 434 VVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRD--NLANYKV 511
|
570 580
....*....|....*....|....*
gi 169764941 537 PREVEVVAELPKTSTGKVRKNILRD 561
Cdd:PRK13382 512 PRDIVVLDELPRGATGKILRRELQA 536
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
60-561 |
7.30e-29 |
|
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: 120.32 E-value: 7.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 60 TYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQE 136
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKqndRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 137 FLSLLQSYRASRPSIPIIVDMDTDATEGELSGPFDEVvleglTYDLDTGAKGWPGLEAQAASEDDVIALAYTSGTTARPK 216
Cdd:cd17642 126 GLQKVLNVQKKLKIIKTIIILDSKEDYKGYQCLYTFI-----TQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGSTGLPK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 217 GVEYTHRG-------CYLAAMGNVIESGLNshrgrcrYLWTLPMFHACGwtfpwaVTAVRGTHYC------LRKIDYPQI 283
Cdd:cd17642 201 GVQLTHKNivarfshARDPIFGNQIIPDTA-------ILTVIPFHHGFG------MFTTLGYLICgfrvvlMYKFEEELF 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 284 WKLLKQEHITHFNAAPTVNTLLCNSK--EAEPLPEPVHVTVAASPPTPHLFEQMTN-LNLHPVHV-YGMTETYGPItkgy 359
Cdd:cd17642 268 LRSLQDYKVQSALLVPTLFAFFAKSTlvDKYDLSNLHEIASGGAPLSKEVGEAVAKrFKLPGIRQgYGLTETTSAI---- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 360 ylpawdnLPSSERYKKMARQGHgFVTSLPVRVIktDVAEGTVIDVardgKEIGEIVFVGNICARGYYKDPDATRKLF-AG 438
Cdd:cd17642 344 -------LITPEGDDKPGAVGK-VVPFFYAKVV--DLDTGKTLGP----NERGELCVKGPMIMKGYVNNPEATKALIdKD 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 439 GVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTG 518
Cdd:cd17642 410 GWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTE 489
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 169764941 519 SEVIEW-ARNASDISKfmIPREVEVVAELPKTSTGKVRKNILRD 561
Cdd:cd17642 490 KEVMDYvASQVSTAKR--LRGGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
27-552 |
1.13e-28 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 119.99 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 27 TLSPTSFLPR-------AAAIEPEAVAIHhVTANNQVLrrTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLES 96
Cdd:PRK05852 8 APMASDFGPRiadlvevAATRLPEAPALV-VTADRIAI--SYRDLARLVDDLAGQLTRSGLLpgdRVALRMGSNAEFVVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 97 IFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQEFLSllQSYRASRPSIPIIVDM--DTDATEGELSgpfdevv 174
Cdd:PRK05852 85 LLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADGPH--DRAEPTTRWWPLTVNVggDSGPSGGTLS------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 175 legltYDLDTGAKGWPGLEAQAASEDDVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLNShrgRCRYLWTLPMF 254
Cdd:PRK05852 156 -----VHLDAATEPTPATSTPEGLRPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSP---RDATVAVMPLY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 255 HACGWTFPWAVTAVRGTHYCLR---KIDYPQIWKLLKQEHITHFNAAPTVNTLLCNSKEAEPLPEPVH----VTVAASPP 327
Cdd:PRK05852 228 HGHGLIAALLATLASGGAVLLPargRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAalrfIRSCSAPL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 328 TPHLFEQMTNLNLHPV-HVYGMTETYGPITkgyylpawdnlpsSERYKKMARQGHGFVTSLPVrviktDVAEGTVIDVAR 406
Cdd:PRK05852 308 TAETAQALQTEFAAPVvCAFGMTEATHQVT-------------TTQIEGIGQTENPVVSTGLV-----GRSTGAQIRIVG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 407 -DGKE-----IGEIVFVGNICARGYYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESM 480
Cdd:PRK05852 370 sDGLPlpagaVGEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGV 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169764941 481 LVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIEWARNAsdISKFMIPREVEVVAELPKTSTG 552
Cdd:PRK05852 450 LASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQFCRER--LAAFEIPASFQEASGLPHTAKG 519
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
60-563 |
1.19e-28 |
|
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: 118.76 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 60 TYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQE 136
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGkgdRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 137 FlsllqsYRASRPSIPIIvdmdtdategelsgpfdevvlegltydldtgakgwpgleaqaaseddviaLAYTSGTTARPK 216
Cdd:cd05969 82 L------YERTDPEDPTL--------------------------------------------------LHYTSGTTGTPK 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 217 GVEYTHRGCYLAAMGNVIESGLnshRGRCRYL------WTLPMFHACgWTfPWA----VTAVRGthyclrKIDYPQIWKL 286
Cdd:cd05969 106 GVLHVHDAMIFYYFTGKYVLDL---HPDDIYWctadpgWVTGTVYGI-WA-PWLngvtNVVYEG------RFDAESWYGI 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 287 LKQEHITHFNAAPTVNTLLCNS----KEAEPLPEPVHVTVAASPPTPHLFE-QMTNLNLhPVH-VYGMTETYGPITKGYy 360
Cdd:cd05969 175 IERVKVTVWYTAPTAIRMLMKEgdelARKYDLSSLRFIHSVGEPLNPEAIRwGMEVFGV-PIHdTWWQTETGSIMIANY- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 361 lPAWDNLPSSerykkMARQGHGfvtslpvrviktdvAEGTVIDVARDGKEIGEivfVGNIC--------ARGYYKDPDAT 432
Cdd:cd05969 253 -PCMPIKPGS-----MGKPLPG--------------VKAAVVDENGNELPPGT---KGILAlkpgwpsmFRGIWNDEERY 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 433 RKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKP 512
Cdd:cd05969 310 KNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKE 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 169764941 513 GkFLTGS----EVIEWARNAsdISKFMIPREVEVVAELPKTSTGKVRKNILRDWA 563
Cdd:cd05969 390 G-FEPSDelkeEIINFVRQK--LGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
9-558 |
2.78e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 118.56 E-value: 2.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 9 SGLLGHFVPGAEQRVNFHT----LSPTSFLPRAAAIEPEAVAIhhvTANNQVLrrTYAETADRARGLAYYLKKHGF---K 81
Cdd:PRK13383 12 SGLLNPPSPRAVLRLLREAsrggTNPYTLLAVTAARWPGRTAI---IDDDGAL--SYRELQRATESLARRLTRDGVapgR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 82 RVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQEFLSLLqsyrASRPSIPIIVDMDTda 161
Cdd:PRK13383 87 AVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERI----AGADDAVAVIDPAT-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 162 tegelsgpfdevvlegltydldTGAKGWPGLEAQAASEDDVIalaYTSGTTARPKGVEythRGCYLAAMGNVIESGLNSH 241
Cdd:PRK13383 161 ----------------------AGAEESGGRPAVAAPGRIVL---LTSGTTGKPKGVP---RAPQLRSAVGVWVTILDRT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 242 RGRC--RYLWTLPMFHACGWTFPWAVTAVRGTHYCLRKIDYPQIwklLKQEHITHFNAAPTVNTLLCNSKEAEPlpepvh 319
Cdd:PRK13383 213 RLRTgsRISVAMPMFHGLGLGMLMLTIALGGTVLTHRHFDAEAA---LAQASLHRADAFTAVPVVLARILELPP------ 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 320 vTVAASPPTPHLFEQMTNLN-LHPVHVYGMTETYGPITKGYYLP---AWDNLPSSERYKKMARQGHGFVTSLPVRVIKtd 395
Cdd:PRK13383 284 -RVRARNPLPQLRVVMSSGDrLDPTLGQRFMDTYGDILYNGYGStevGIGALATPADLRDAPETVGKPVAGCPVRILD-- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 396 vaegtvidvaRDGKEIGEIV----FVGNICARGYYKDPDAtrKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGEN 471
Cdd:PRK13383 361 ----------RNNRPVGPRVtgriFVGGELAGTRYTDGGG--KAVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGEN 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 472 ISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIEWARNAsdISKFMIPREVEVVAELPKTST 551
Cdd:PRK13383 429 VYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDR--VSRFEQPRDINIVSSIPRNPT 506
|
....*...
gi 169764941 552 GKV-RKNI 558
Cdd:PRK13383 507 GKVlRKEL 514
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
181-562 |
6.77e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 117.01 E-value: 6.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 181 DLDTGAKGWPgleAQAASEDDVIALA-YTSGTTARPKGVEYTHRGcyLAAMGNVIESGlnshrgrcrYLWT--------L 251
Cdd:PRK07787 111 PVRLHARSWH---RYPEPDPDAPALIvYTSGTTGPPKGVVLSRRA--IAADLDALAEA---------WQWTaddvlvhgL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 252 PMFHACGwtfpwavtAVRGTHYCLR---------KIDyPQIWKLLKQEHITHFNAAPTVNTLLCNSKEAEPLPEPVHVTV 322
Cdd:PRK07787 177 PLFHVHG--------LVLGVLGPLRignrfvhtgRPT-PEAYAQALSEGGTLYFGVPTVWSRIAADPEAARALRGARLLV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 323 AASPPTP-HLFEQMTNLNLH-PVHVYGMTETYgpITkgyylpawdnlpSSERYKKMARQGhgfVTSLPVRVIKTDVAEGT 400
Cdd:PRK07787 248 SGSAALPvPVFDRLAALTGHrPVERYGMTETL--IT------------LSTRADGERRPG---WVGLPLAGVETRLVDED 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 401 VIDVARDGKEIGEIVFVGNICARGYYKDPDATRKLF-AGGVLHSGDLAVWHADGSIQIQDR-AKDIIISGGENISSVALE 478
Cdd:PRK07787 311 GGPVPHDGETVGELQVRGPTLFDGYLNRPDATAAAFtADGWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 479 SMLVTHPDILEAGVVAVPDSHWGERPKAFVTvkPGKFLTGSEVIEWArnASDISKFMIPREVEVVAELPKTSTGKVRKNI 558
Cdd:PRK07787 391 TALLGHPGVREAAVVGVPDDDLGQRIVAYVV--GADDVAADELIDFV--AQQLSVHKRPREVRFVDALPRNAMGKVLKKQ 466
|
....
gi 169764941 559 LRDW 562
Cdd:PRK07787 467 LLSE 470
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
62-568 |
1.33e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 116.66 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 62 AETADRARGLAYYLKKHGFKRVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQEFLSLL 141
Cdd:PRK13388 34 AEAAARAAALIALADPDRPLHVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLVTDAEHRPLL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 142 QSYRAsrPSIPIIvDMDTDATEGELSGPFDEVvlegltydldtgakgwpglEAQAASEDDVIALAYTSGTTARPKGVEYT 221
Cdd:PRK13388 114 DGLDL--PGVRVL-DVDTPAYAELVAAAGALT-------------------PHREVDAMDPFMLIFTSGTTGAPKAVRCS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 222 HRGCYLAAMGNVIESGLnsHRGRCRYLwTLPMFHACGWTFPWAVTAVRGTHYCLR-KIDYPQIWKLLKQEHITHFN-AAP 299
Cdd:PRK13388 172 HGRLAFAGRALTERFGL--TRDDVCYV-SMPLFHSNAVMAGWAPAVASGAAVALPaKFSASGFLDDVRRYGATYFNyVGK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 300 TVNTLLCNSKEAEPLPEPVHVTVA--ASPPTPHLFEQmtNLNLHPVHVYGMTETYGPITKGYYLPawdnlPSSerykkMA 377
Cdd:PRK13388 249 PLAYILATPERPDDADNPLRVAFGneASPRDIAEFSR--RFGCQVEDGYGSSEGAVIVVREPGTP-----PGS-----IG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 378 RQGHGFVTSLPVRVIKTDVAE----GTVIDVArdgKEIGEIVFV-GNICARGYYKDPDATRKLFAGGVLHSGDLAVWHAD 452
Cdd:PRK13388 317 RGAPGVAIYNPETLTECAVARfdahGALLNAD---EAIGELVNTaGAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDAD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 453 GSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIEWARNASDIS 532
Cdd:PRK13388 394 GWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFLAAQPDLG 473
|
490 500 510
....*....|....*....|....*....|....*...
gi 169764941 533 KFMIPREVEVVAELPKTSTGKVRKNILRD--WAKGANR 568
Cdd:PRK13388 474 TKAWPRYVRIAADLPSTATNKVLKRELIAqgWATGDPV 511
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
32-560 |
1.36e-27 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 117.21 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 32 SFLPRAAAIEPEAVAIHHVTANNQVLRRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNV 108
Cdd:cd05968 65 QLLDKWLADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGLRALGVGkgdRVGIYLPMIPEIVPAFLAVARIGGIVV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 109 AVNYRLKEDDIAYIFTHSDVEAIIVDQEFlsllqsYRASRPsipiiVDMDTDATEGELSGP-FDEVVLEGLTYDLDTGAK 187
Cdd:cd05968 145 PIFSGFGKEAAATRLQDAEAKALITADGF------TRRGRE-----VNLKEEADKACAQCPtVEKVVVVRHLGNDFTPAK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 188 G---WPGLEAQAA-------SEDDVIALAYTSGTTARPKGVEYTHRGCYLAAMGNvIESGLNSHRGRcRYLWTLPMfhac 257
Cdd:cd05968 214 GrdlSYDEEKETAgdgaertESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQD-MYFQFDLKPGD-LLTWFTDL---- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 258 GWTF-PWAVTA---VRGTHYCLRKI-DYP---QIWKLLKQEHITHFNAAPTVNTLLCNSKEAeplPEPVH----VTVAAS 325
Cdd:cd05968 288 GWMMgPWLIFGgliLGATMVLYDGApDHPkadRLWRMVEDHEITHLGLSPTLIRALKPRGDA---PVNAHdlssLRVLGS 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 326 PPTP-------HLFEQMTNLNLHPVHVYGMTETYGPITKGYYLpawdnlpssERYKKMarqghGFVTSLPvrviktdvae 398
Cdd:cd05968 365 TGEPwnpepwnWLFETVGKGRNPIINYSGGTEISGGILGNVLI---------KPIKPS-----SFNGPVP---------- 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 399 GTVIDVA-RDGK----EIGEIV----FVGniCARGYYKDPDatRKL------FAGGVLHsGDLAVWHADGSIQIQDRAKD 463
Cdd:cd05968 421 GMKADVLdESGKparpEVGELVllapWPG--MTRGFWRDED--RYLetywsrFDNVWVH-GDFAYYDEEGYFYILGRSDD 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 464 IIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGS---EVIEwaRNASDISKFMIPREV 540
Cdd:cd05968 496 TINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEAlaeELME--RVADELGKPLSPERI 573
|
570 580
....*....|....*....|
gi 169764941 541 EVVAELPKTSTGKVRKNILR 560
Cdd:cd05968 574 LFVKDLPKTRNAKVMRRVIR 593
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
200-561 |
1.95e-27 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 116.31 E-value: 1.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 200 DDVIALAYTSGTTARPKGVEYTHRgcylaamgNVIESGLNS--------HRGRCRYLWTLPMFHAcgwtfpWAVTAvrgt 271
Cdd:PRK08974 206 EDLAFLQYTGGTTGVAKGAMLTHR--------NMLANLEQAkaaygpllHPGKELVVTALPLYHI------FALTV---- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 272 hYCLRKI-------------DYPQIWKLLKQEHithFNAAPTVNTL---LCNSKEAEPLP-----------EPVHVTVAA 324
Cdd:PRK08974 268 -NCLLFIelggqnllitnprDIPGFVKELKKYP---FTAITGVNTLfnaLLNNEEFQELDfsslklsvgggMAVQQAVAE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 325 SpptphlFEQMTNLNLhpVHVYGMTETYGPITKGYYlpawdNLpsserykkmarQGH----GF-VTSLPVRVIKTDvaeG 399
Cdd:PRK08974 344 R------WVKLTGQYL--LEGYGLTECSPLVSVNPY-----DL-----------DYYsgsiGLpVPSTEIKLVDDD---G 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 400 TviDVARDgkEIGEIVFVGNICARGYYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALES 479
Cdd:PRK08974 397 N--EVPPG--EPGELWVKGPQVMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIED 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 480 MLVTHPDILEAGVVAVPDSHWGERPKAFVtVKPGKFLTGSEVIEWARNasDISKFMIPREVEVVAELPKTSTGKVRKNIL 559
Cdd:PRK08974 473 VVMLHPKVLEVAAVGVPSEVSGEAVKIFV-VKKDPSLTEEELITHCRR--HLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
..
gi 169764941 560 RD 561
Cdd:PRK08974 550 RD 551
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
177-554 |
3.34e-27 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 114.46 E-value: 3.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 177 GLTYDLDTGAKGWPGLEAQAASEDDVIALAYTSGTTARPKGVEYTHRGcyLAAMGNVIESGLNSHrGRCRYLWTLPmFHA 256
Cdd:cd05922 94 GTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQN--LLANARSIAEYLGIT-ADDRALTVLP-LSY 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 257 CGWTFPWAVTAVRGTHYCLRKIDYP--QIWKLLKQEHITHFNAAPTVNTLLCNSKEA-EPLPEPVHVT-VAASPPTPHLF 332
Cdd:cd05922 170 DYGLSVLNTHLLRGATLVLTNDGVLddAFWEDLREHGATGLAGVPSTYAMLTRLGFDpAKLPSLRYLTqAGGRLPQETIA 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 333 EQMTNLNLHPVHV-YGMTETYGPITkgyYLPA--WDNLPSSerykkmarqghgfvtslpvrvIKTDVAEGTVIDVARDG- 408
Cdd:cd05922 250 RLRELLPGAQVYVmYGQTEATRRMT---YLPPerILEKPGS---------------------IGLAIPGGEFEILDDDGt 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 409 ----KEIGEIVFVGNICARGYYKDPDATRKLFAGG-VLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVT 483
Cdd:cd05922 306 ptppGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGgVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARS 385
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169764941 484 HPDILEAGVVAVPDShWGERPKAFVTVKPGkfLTGSEVIEWArnASDISKFMIPREVEVVAELPKTSTGKV 554
Cdd:cd05922 386 IGLIIEAAAVGLPDP-LGEKLALFVTAPDK--IDPKDVLRSL--AERLPPYKVPATVRVVDELPLTASGKV 451
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
191-563 |
1.06e-26 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 114.15 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 191 GLEAQAASEDDVIALAYTSGTTARPKGVEYTHrGCYLAAMGNViESGLNSHRGRCRYLWT---------LPMFHACGWTF 261
Cdd:PRK12492 198 SLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTH-GNLVANMLQV-RACLSQLGPDGQPLMKegqevmiapLPLYHIYAFTA 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 262 PWAVTAVRGTHYCLrkIDYPQ-IWKLLKQEHITHFNAAPTVNTL---LCNSKEAEPLP-EPVHVT----VAASPPTPHLF 332
Cdd:PRK12492 276 NCMCMMVSGNHNVL--ITNPRdIPGFIKELGKWRFSALLGLNTLfvaLMDHPGFKDLDfSALKLTnsggTALVKATAERW 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 333 EQMTNLNLhpVHVYGMTETyGPITkgyylpawdnlpSSERYKKMARQGhgfVTSLPVrviktdvaEGTVIDVARD-GKEI 411
Cdd:PRK12492 354 EQLTGCTI--VEGYGLTET-SPVA------------STNPYGELARLG---TVGIPV--------PGTALKVIDDdGNEL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 412 -----GEIVFVGNICARGYYKDPDATRK-LFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHP 485
Cdd:PRK12492 408 plgerGELCIKGPQVMKGYWQQPEATAEaLDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHP 487
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169764941 486 DILEAGVVAVPDSHWGERPKAFVTVKPGKfLTGSEVIEWARnaSDISKFMIPREVEVVAELPKTSTGKVRKNILRDWA 563
Cdd:PRK12492 488 KVANCAAIGVPDERSGEAVKLFVVARDPG-LSVEELKAYCK--ENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDIA 562
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
197-553 |
2.08e-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: 110.93 E-value: 2.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 197 ASEDDVIALaYTSGTTARPKGVEYTHRGCYLAAMG-------NVIESGLNSHR----GRCRYLWTLPMFHACGWtfpWAV 265
Cdd:cd05924 1 RSADDLYIL-YTGGTTGMPKGVMWRQEDIFRMLMGgadfgtgEFTPSEDAHKAaaaaAGTVMFPAPPLMHGTGS---WTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 266 TAV--RGTHYCL--RKIDYPQIWKLLKQEHITHFN------AAPTVNTLlcNSKEAEPLPEPVHVTVAASPPTPHLFEQM 335
Cdd:cd05924 77 FGGllGGQTVVLpdDRFDPEEVWRTIEKHKVTSMTivgdamARPLIDAL--RDAGPYDLSSLFAISSGGALLSPEVKQGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 336 TNL--NLHPVHVYGMTETYGpitKGYYLPAwdnlpsserykKMARQGHGFVTSLPVRVIKTDvaEGTVIDVARDGkeIGE 413
Cdd:cd05924 155 LELvpNITLVDAFGSSETGF---TGSGHSA-----------GSGPETGPFTRANPDTVVLDD--DGRVVPPGSGG--VGW 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 414 IVFVGNIcARGYYKDPDATRKLF--AGGVLHS--GDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILE 489
Cdd:cd05924 217 IARRGHI-PLGYYGDEAKTAETFpeVDGVRYAvpGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYD 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169764941 490 AGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIEWARnaSDISKFMIPREVEVVAELPKTSTGK 553
Cdd:cd05924 296 VLVVGRPDERWGQEVVAVVQLREGAGVDLEELREHCR--TRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
114-561 |
2.14e-26 |
|
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: 112.94 E-value: 2.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 114 LKEDDIAYIFTHSDVEAIIVDQEFLSLLQSYRASRPSIPIIVDMDTDATEGELSgpFDEVVlegltydldtgakgwpgle 193
Cdd:cd05928 101 LTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLN--FKELL------------------- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 194 aQAASED---------DVIALAYTSGTTARPKGVEYTHRgcyLAAMGNVIESGLNSHRGRCRYLWTLPmfhACGWTF--- 261
Cdd:cd05928 160 -NEASTEhhcvetgsqEPMAIYFTSGTTGSPKMAEHSHS---SLGLGLKVNGRYWLDLTASDIMWNTS---DTGWIKsaw 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 262 -----PWAVTAVRGTHYcLRKIDYPQIWKLLKQEHITHFNAAPTV-NTLLCNSKEAEPLPEPVHVTVAASPPTPHLFEQ- 334
Cdd:cd05928 233 sslfePWIQGACVFVHH-LPRFDPLVILKTLSSYPITTFCGAPTVyRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKw 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 335 --MTNLNLHpvHVYGMTETyGPITKgyylpawdnlpsseRYKKMA-RQGHGFVTSLPVRVIKTDVaEGTVIDvarDGKEi 411
Cdd:cd05928 312 kaQTGLDIY--EGYGQTET-GLICA--------------NFKGMKiKPGSMGKASPPYDVQIIDD-NGNVLP---PGTE- 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 412 geivfvGNICAR-----------GYYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESM 480
Cdd:cd05928 370 ------GDIGIRvkpirpfglfsGYVDNPEKTAATIRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESA 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 481 LVTHPDILEAGVVAVPDSHWGERPKAFVTVKPG------KFLTgSEVIEWARNASDISKFmiPREVEVVAELPKTSTGKV 554
Cdd:cd05928 444 LIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQflshdpEQLT-KELQQHVKSVTAPYKY--PRKVEFVQELPKTVTGKI 520
|
....*..
gi 169764941 555 RKNILRD 561
Cdd:cd05928 521 QRNELRD 527
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
60-561 |
2.29e-26 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 113.15 E-value: 2.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 60 TYAETADRARGLAYYLKKHGFKR---VGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQE 136
Cdd:PLN02330 57 TYGEVVRDTRRFAKALRSLGLRKgqvVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDT 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 137 FLSLLQSYrasrpSIPIIVdmdtdATEGELSGPFDEVVLegltydLDTGAKGWPGLEAQAASEDDVIALAYTSGTTARPK 216
Cdd:PLN02330 137 NYGKVKGL-----GLPVIV-----LGEEKIEGAVNWKEL------LEAADRAGDTSDNEEILQTDLCALPFSSGTTGISK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 217 GVEYTHRGcYLAAMGNVIESGLNSHRGRCRYLWTLPMFHACGWT-FPWAVTAVRGTHYCLRKIDYPQIWKLLKQEHITHf 295
Cdd:PLN02330 201 GVMLTHRN-LVANLCSSLFSVGPEMIGQVVTLGLIPFFHIYGITgICCATLRNKGKVVVMSRFELRTFLNALITQEVSF- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 296 naAPTVNTLLCNSKEaEPLPEPVHVT--------VAASPPTPHLFEQMTNL--NLHPVHVYGMTE------TYGPITKGY 359
Cdd:PLN02330 279 --APIVPPIILNLVK-NPIVEEFDLSklklqaimTAAAPLAPELLTAFEAKfpGVQVQEAYGLTEhscitlTHGDPEKGH 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 360 YLPawdnlpsserykkmARQGHGFV-TSLPVRVIKTDVAEGTVIDVArdgkeiGEIVFVGNICARGYYKDPDAT-RKLFA 437
Cdd:PLN02330 356 GIA--------------KKNSVGFIlPNLEVKFIDPDTGRSLPKNTP------GELCVRSQCVMQGYYNNKEETdRTIDE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 438 GGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLT 517
Cdd:PLN02330 416 DGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKES 495
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 169764941 518 GSEVIEWArnASDISKFMIPREVEVVAELPKTSTGKVRKNILRD 561
Cdd:PLN02330 496 EEDILNFV--AANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
45-562 |
9.08e-26 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 111.53 E-value: 9.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 45 VAIHHVTANnQVLRRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIaaagavnvavnyrLK------ 115
Cdd:PRK04319 61 VALRYLDAS-RKEKYTYKELKELSNKFANVLKELGVEkgdRVFIFMPRIPELYFALLGA-------------LKngaivg 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 116 -------EDDIAYIFTHSDVEAIIVDQEFLSllqsyRASRPSIP-----IIVDMDTDATEGELSgpFDEVVlegltydld 183
Cdd:PRK04319 127 plfeafmEEAVRDRLEDSEAKVLITTPALLE-----RKPADDLPslkhvLLVGEDVEEGPGTLD--FNALM--------- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 184 tgAKGWPGLEAQAASEDDVIALAYTSGTTARPKGVEYTHrgcylaamGNVIEsglnsHRGRCRYLWTLpmfHA-----C- 257
Cdd:PRK04319 191 --EQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVH--------NAMLQ-----HYQTGKYVLDL---HEddvywCt 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 258 ---GWtfpwavtaVRGTHY------------CLRKIDY-PQIW-KLLKQEHITHFNAAPTVNTLLCNSKE---------- 310
Cdd:PRK04319 253 adpGW--------VTGTSYgifapwlngatnVIDGGRFsPERWyRILEDYKVTVWYTAPTAIRMLMGAGDdlvkkydlss 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 311 -------AEPL-PEPVHVTVAAspptphlfeqmtnLNLhPVH-VYGMTETYGPITKGYylPAWDNLPSSerykkMARqgh 381
Cdd:PRK04319 325 lrhilsvGEPLnPEVVRWGMKV-------------FGL-PIHdNWWMTETGGIMIANY--PAMDIKPGS-----MGK--- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 382 gfvtslPVRVIktdvaEGTVIDVARDGKEIGEivfVGNICA--------RGYYKDPDATRKLFAGGVLHSGDLAVWHADG 453
Cdd:PRK04319 381 ------PLPGI-----EAAIVDDQGNELPPNR---MGNLAIkkgwpsmmRGIWNNPEKYESYFAGDWYVSGDSAYMDEDG 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 454 SIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGkFLTGSEVIEwarnasDISK 533
Cdd:PRK04319 447 YFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPG-YEPSEELKE------EIRG 519
|
570 580 590
....*....|....*....|....*....|....*..
gi 169764941 534 F--------MIPREVEVVAELPKTSTGKVRKNILRDW 562
Cdd:PRK04319 520 FvkkglgahAAPREIEFKDKLPKTRSGKIMRRVLKAW 556
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
195-560 |
1.37e-25 |
|
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: 109.58 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 195 QAASEDDVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLNshRGRCRYLWTLPMFHACGWT---FPWAVTAVRGT 271
Cdd:cd05974 80 ENTHADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLK--PGDVHWNISSPGWAKHAWScffAPWNAGATVFL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 272 hYCLRKIDYPQIWKLLKQEHITHFNAAPTVNTLLCNSKEAEPLPEPVHVTVAASPPTPHLFEQMTNL-NLHPVHVYGMTE 350
Cdd:cd05974 158 -FNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVKLREVVGAGEPLNPEVIEQVRRAwGLTIRDGYGQTE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 351 TYGPITKGyylPAWDNLPSSerykkMARQGHGFvtslpvRVIKTD-----VAEGTVIDVARDGKEIGEIvfvgnicaRGY 425
Cdd:cd05974 237 TTALVGNS---PGQPVKAGS-----MGRPLPGY------RVALLDpdgapATEGEVALDLGDTRPVGLM--------KGY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 426 YKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPK 505
Cdd:cd05974 295 AGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPK 374
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 169764941 506 AFVTVKPGKFLTGSEVIEWARNASD-ISKFMIPREVEvVAELPKTSTGKVRKNILR 560
Cdd:cd05974 375 AFIVLRAGYEPSPETALEIFRFSRErLAPYKRIRRLE-FAELPKTISGKIRRVELR 429
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
423-564 |
2.52e-25 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 109.69 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 423 RGYYKDPDATRKLF-AGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWG 501
Cdd:PRK10946 392 RGYYKSPQHNASAFdANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMG 471
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169764941 502 ERPKAFVTVKPGkfLTGSEVIEWARnASDISKFMIPREVEVVAELPKTSTGKVRKNILRDWAK 564
Cdd:PRK10946 472 EKSCAFLVVKEP--LKAVQLRRFLR-EQGIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLA 531
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
36-556 |
6.17e-25 |
|
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: 109.95 E-value: 6.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 36 RAAAIEPEAVAihhVTANNQVLrrTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIaaagavnvavny 112
Cdd:COG1020 484 AQAARTPDAVA---VVFGDQSL--TYAELNARANRLAHHLRALGVGpgdLVGVCLERSLEMVVALLAV------------ 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 113 rLK-------------EDDIAYIFTHSDVEAIIVDQEFLSLLQSYRASrpsipiIVDMDTDATEGELSGPfdevvleglt 179
Cdd:COG1020 547 -LKagaayvpldpaypAERLAYMLEDAGARLVLTQSALAARLPELGVP------VLALDALALAAEPATN---------- 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 180 ydldtgakgwpgLEAQAASEDdviaLAY---TSGTTARPKGVEYTHRG--CYLAAMGNVIesGLNSHRgrcRYLWTLPM- 253
Cdd:COG1020 610 ------------PPVPVTPDD----LAYviyTSGSTGRPKGVMVEHRAlvNLLAWMQRRY--GLGPGD---RVLQFASLs 668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 254 FHACGWTFPWA-------VTAVRGTHYclrkiDYPQIWKLLKQEHITHFNAAPTVNTLLCNSkEAEPLPEPVHVTVAASP 326
Cdd:COG1020 669 FDASVWEIFGAllsgatlVLAPPEARR-----DPAALAELLARHRVTVLNLTPSLLRALLDA-APEALPSLRLVLVGGEA 742
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 327 PTPHLFEQMTNLNLHP--VHVYGMTE-----TYGPITKGyyLPAWDNLPsserykkmarqghgfvtslpvrvIKTDVAeG 399
Cdd:COG1020 743 LPPELVRRWRARLPGArlVNLYGPTEttvdsTYYEVTPP--DADGGSVP-----------------------IGRPIA-N 796
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 400 T---VIDvaRDGK-----EIGEIvFVGNIC-ARGYYKDPDATRK-------LFAGGVL-HSGDLAVWHADGSIQIQDRA- 461
Cdd:COG1020 797 TrvyVLD--AHLQpvpvgVPGEL-YIGGAGlARGYLNRPELTAErfvadpfGFPGARLyRTGDLARWLPDGNLEFLGRAd 873
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 462 ---KdiiISG-----GEnissvaLESMLVTHPDILEAGVVAVPDSHwGERPKAFVTVKPGKFLTGSEVIEWARNASDiSK 533
Cdd:COG1020 874 dqvK---IRGfrielGE------IEAALLQHPGVREAVVVAREDAP-GDKRLVAYVVPEAGAAAAAALLRLALALLL-PP 942
|
570 580
....*....|....*....|...
gi 169764941 534 FMIPREVEVVAELPKTSTGKVRK 556
Cdd:COG1020 943 YMVPAAVVLLLPLPLTGNGKLDR 965
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
36-554 |
1.08e-24 |
|
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: 107.29 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 36 RAAAIEPEAVAihhVTANNQVLrrTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNY 112
Cdd:cd12117 5 EQAARTPDAVA---VVYGDRSL--TYAELNERANRLARRLRAAGVGpgdVVGVLAERSPELVVALLAVLKAGAAYVPLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 113 RLKEDDIAYIFTHSDVEAIIVDQeflsllqsyrasrpsipiivdmdtdATEGELSGPFDEVVLEGltyDLDTGAkgwPGL 192
Cdd:cd12117 80 ELPAERLAFMLADAGAKVLLTDR-------------------------SLAGRAGGLEVAVVIDE---ALDAGP---AGN 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 193 EAQAASEDDVIALAYTSGTTARPKGVEYTHRGcylaAMGNVIESGLNSHRGRCRYLWTLPM-FHACgwTFP-WA------ 264
Cdd:cd12117 129 PAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRG----VVRLVKNTNYVTLGPDDRVLQTSPLaFDAS--TFEiWGallnga 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 265 --VTAVRGThyclrKIDYPQIWKLLKQEHIT-HFNAAPTVNTLlcnskeAEPLPEPV----HVTV---AASPPTPHLFeq 334
Cdd:cd12117 203 rlVLAPKGT-----LLDPDALGALIAEEGVTvLWLTAALFNQL------ADEDPECFaglrELLTggeVVSPPHVRRV-- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 335 mtnLNLHP----VHVYGMTE-----TYGPITKGYYLPawdnlpsserykkmarqghgfvTSLPvrvIKTDVAEGTVIDVA 405
Cdd:cd12117 270 ---LAACPglrlVNGYGPTEnttftTSHVVTELDEVA----------------------GSIP---IGRPIANTRVYVLD 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 406 RDGK-----EIGEIVFVGNICARGYYKDPDATRKLFA------GGVLH-SGDLAVWHADGSIQIQDRAKDIIISGGENIS 473
Cdd:cd12117 322 EDGRpvppgVPGELYVGGDGLALGYLNRPALTAERFVadpfgpGERLYrTGDLARWLPDGRLEFLGRIDDQVKIRGFRIE 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 474 SVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGkfLTGSEVIEWARnaSDISKFMIPREVEVVAELPKTSTGK 553
Cdd:cd12117 402 LGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGA--LDAAELRAFLR--ERLPAYMVPAAFVVLDELPLTANGK 477
|
.
gi 169764941 554 V 554
Cdd:cd12117 478 V 478
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
58-560 |
2.97e-24 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 106.81 E-value: 2.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 58 RRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNYR--LKEDDIAYIFthsdVEAI- 131
Cdd:PLN02860 32 RRTGHEFVDGVLSLAAGLLRLGLRngdVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRwsFEEAKSAMLL----VRPVm 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 132 -IVDQEFLSLLQSYRASR-PSIPIIVDMDTDATEGelsGPFDEVVLEglTYDLDTGAKGWPGLEAQAASEDDVIaLAYTS 209
Cdd:PLN02860 108 lVTDETCSSWYEELQNDRlPSLMWQVFLESPSSSV---FIFLNSFLT--TEMLKQRALGTTELDYAWAPDDAVL-ICFTS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 210 GTTARPKGVEYTHRGCYLAAMGNVIESGLNSHRgrcRYLWTLPMFHACGWTFPWAVTAVRGTHYCLRKIDYPQIWKLLKQ 289
Cdd:PLN02860 182 GTTGRPKGVTISHSALIVQSLAKIAIVGYGEDD---VYLHTAPLCHIGGLSSALAMLMVGACHVLLPKFDAKAALQAIKQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 290 EHITHFNAAPTVNTLLcnskeaeplpepvhVTVAASPPTPHLFEQMTNL----------------NLHP----VHVYGMT 349
Cdd:PLN02860 259 HNVTSMITVPAMMADL--------------ISLTRKSMTWKVFPSVRKIlngggslssrllpdakKLFPnaklFSAYGMT 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 350 ETYGPITkgyYLPAWDnlPSSERYKKmARQGHGFVTSLPVRViktdvAEGTVIDVARDGKEIG----EIVFVGNICARG- 424
Cdd:PLN02860 325 EACSSLT---FMTLHD--PTLESPKQ-TLQTVNQTKSSSVHQ-----PQGVCVGKPAPHVELKigldESSRVGRILTRGp 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 425 ----YYKD--PDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDS 498
Cdd:PLN02860 394 hvmlGYWGqnSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDS 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169764941 499 HWGERPKAFVTVKPG-------------KFLTGSEVIEWARNASDISKFMIPREVEVVAE-LPKTSTGKVRKNILR 560
Cdd:PLN02860 474 RLTEMVVACVRLRDGwiwsdnekenakkNLTLSSETLRHHCREKNLSRFKIPKLFVQWRKpFPLTTTGKIRRDEVR 549
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
38-560 |
3.23e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 106.25 E-value: 3.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 38 AAIEPEAVAIHHVTANNQVlrrTYAETADRARGLAYYLKKHGFKR---VGVLCPNTPAFLESIFGIAAAGAVNVAVNYRL 114
Cdd:PRK13390 7 AQIAPDRPAVIVAETGEQV---SYRQLDDDSAALARVLYDAGLRTgdvVALLSDNSPEALVVLWAALRSGLYITAINHHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 115 KEDDIAYIFTHSDVEAIIVDQEFLSLlqsyrASRPSIPIIVDMdtdATEGELSGPFDevvlegltYDLDTGAKGwPGLEA 194
Cdd:PRK13390 84 TAPEADYIVGDSGARVLVASAALDGL-----AAKVGADLPLRL---SFGGEIDGFGS--------FEAALAGAG-PRLTE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 195 QAASEddviALAYTSGTTARPKGVEYTHRGCYLAAMGN---VIESGLNSHRGRCRYLWTLPMFHACGWTFPWAVTAVRGT 271
Cdd:PRK13390 147 QPCGA----VMLYSSGTTGFPKGIQPDLPGRDVDAPGDpivAIARAFYDISESDIYYSSAPIYHAAPLRWCSMVHALGGT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 272 HYCLRKIDYPQIWKLLKQEHITHFNAAPT--VNTLLCNS--KEAEPLPEPVHVTVAASPPtphlfeqmtnlnlhPVHV-Y 346
Cdd:PRK13390 223 VVLAKRFDAQATLGHVERYRITVTQMVPTmfVRLLKLDAdvRTRYDVSSLRAVIHAAAPC--------------PVDVkH 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 347 GMTETYGPITKGYYlpawdnlpSSERYKKMARQGHGFVTSLPVRVIKTDVAEGTVIDvaRDGKE-----IGEIVFVGNIC 421
Cdd:PRK13390 289 AMIDWLGPIVYEYY--------SSTEAHGMTFIDSPDWLAHPGSVGRSVLGDLHICD--DDGNElpagrIGTVYFERDRL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 422 ARGYYKDPDATRKlfAGGVLHS-----GDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVP 496
Cdd:PRK13390 359 PFRYLNDPEKTAA--AQHPAHPfwttvGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVP 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169764941 497 DSHWGERPKAFVTVKPGkfLTGS-----EVIEWARnaSDISKFMIPREVEVVAELPKTSTGKVRKNILR 560
Cdd:PRK13390 437 DPEMGEQVKAVIQLVEG--IRGSdelarELIDYTR--SRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
36-561 |
5.05e-24 |
|
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: 105.78 E-value: 5.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 36 RAAAIEPEAVAIHHVT-ANNQVLRRTYAETADRARGLAYYLKKHGFK--RVGVLCPNTPAFLESIFG--------IAAAG 104
Cdd:cd05931 1 RRAAARPDRPAYTFLDdEGGREETLTYAELDRRARAIAARLQAVGKPgdRVLLLAPPGLDFVAAFLGclyagaiaVPLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 105 AVNVAVNYRLkeddiAYIFTHSDVEAIIVDQEFLSLLQSYRASRPSIPIIVDMDTDATEgelsgpfdevvlegltydlDT 184
Cdd:cd05931 81 PTPGRHAERL-----AAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLP-------------------DT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 185 GAKGWPGleaQAASEDDVIALAYTSGTTARPKGVEYTHRGCY--LAAMGNVIESGLNSHRGrcryLWtLPMFHACGWTFP 262
Cdd:cd05931 137 SAADWPP---PSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLanVRQIRRAYGLDPGDVVV----SW-LPLYHDMGLIGG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 263 WAVTAVRGTHyC--------LRKidyPQIW-KLLKQEHITHfNAAPTVNTLLC----NSKEAEPL-----------PEPV 318
Cdd:cd05931 209 LLTPLYSGGP-SvlmspaafLRR---PLRWlRLISRYRATI-SAAPNFAYDLCvrrvRDEDLEGLdlsswrvalngAEPV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 319 HV-TVAAspptphLFEQMTNLNLHP-VHV--YGMTE-----TYGPITKGyylpawdnlPSSERYKKMARQGHGFVTSLPV 389
Cdd:cd05931 284 RPaTLRR------FAEAFAPFGFRPeAFRpsYGLAEatlfvSGGPPGTG---------PVVLRVDRDALAGRAVAVAADD 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 390 RVIKTDVAEGTVID-------------VARDGkEIGEIVFVGNICARGYYKDPDATRKLF-------AGGVLHSGDLAVW 449
Cdd:cd05931 349 PAARELVSCGRPLPdqevrivdpetgrELPDG-EVGEIWVRGPSVASGYWGRPEATAETFgalaatdEGGWLRTGDLGFL 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 450 HaDGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVA---VPDSHwGERPKAFVTVKPGKfltgsEVIEWAR 526
Cdd:cd05931 428 H-DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRPGCVAafsVPDDG-EERLVVVAEVERGA-----DPADLAA 500
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 169764941 527 NASDI-----SKF-MIPREVEVVA--ELPKTSTGKVRKNILRD 561
Cdd:cd05931 501 IAAAIraavaREHgVAPADVVLVRpgSIPRTSSGKIQRRACRA 543
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
60-556 |
2.84e-23 |
|
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: 102.91 E-value: 2.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 60 TYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVdqe 136
Cdd:cd05914 9 TYKDLADNIAKFALLLKINGVGtgdRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 137 flsllqsyrasrpsipiivdmdtdategelsgpfdevvlegltydldtgakgwpgleaqaASEDDVIALAYTSGTTARPK 216
Cdd:cd05914 86 ------------------------------------------------------------SDEDDVALINYTSGTTGNSK 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 217 GVEYTHRGCyLAAMGNVIESGLNSHRGRCryLWTLPMFHACGWTFPWAVTAVRGTH-YCLRKIDYPQIW----------- 284
Cdd:cd05914 106 GVMLTYRNI-VSNVDGVKEVVLLGKGDKI--LSILPLHHIYPLTFTLLLPLLNGAHvVFLDKIPSAKIIalafaqvtptl 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 285 ---KLLKQEHITHFNAAPTVN---------TLLCNSKEAEPLPEPVH---------VTVAASPPTPHLFEQMTNLNLHPV 343
Cdd:cd05914 183 gvpVPLVIEKIFKMDIIPKLTlkkfkfklaKKINNRKIRKLAFKKVHeafggnikeFVIGGAKINPDVEEFLRTIGFPYT 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 344 HVYGMTETyGPITKGyylpawdNLPSSERYKKMarqghGFVTS-LPVRVIKTDVAEGTvidvardgkeiGEIVFVGNICA 422
Cdd:cd05914 263 IGYGMTET-APIISY-------SPPNRIRLGSA-----GKVIDgVEVRIDSPDPATGE-----------GEIIVRGPNVM 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 423 RGYYKDPDATRKLF-AGGVLHSGDLAVWHADGSIQIQDRAKDIIISG-GENISSVALESMLVTHPDILEAGVV------- 493
Cdd:cd05914 319 KGYYKNPEATAEAFdKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVLESLVVvqekklv 398
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169764941 494 --AVPDShwgerpkAFVTVKPGKFLTGSEVIEWA------RNASD---ISKFMIPREvevvaELPKTSTGKVRK 556
Cdd:cd05914 399 alAYIDP-------DFLDVKALKQRNIIDAIKWEvrdkvnQKVPNykkISKVKIVKE-----EFEKTPKGKIKR 460
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
60-558 |
3.91e-23 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 103.14 E-value: 3.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 60 TYAETADRARGLAYYLKKHGFKRVGV---LCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQE 136
Cdd:PLN02246 52 TYADVELLSRRVAAGLHKLGIRQGDVvmlLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSC 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 137 FLSLLQSYRASRPSIPIIVDmdtDATEGELSgpFDEVVlegltyDLDTGAkgwpgLEAQAASEDDVIALAYTSGTTARPK 216
Cdd:PLN02246 132 YVDKLKGLAEDDGVTVVTID---DPPEGCLH--FSELT------QADENE-----LPEVEISPDDVVALPYSSGTTGLPK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 217 GVEYTHRGCYLAAMGNVieSGLNSH---RGRCRYLWTLPMFHA--------CGwtfpwavTAVRGTHYCLRKIDYPQIWK 285
Cdd:PLN02246 196 GVMLTHKGLVTSVAQQV--DGENPNlyfHSDDVILCVLPMFHIyslnsvllCG-------LRVGAAILIMPKFEIGALLE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 286 LLKQEHIThfnAAPTVntllcnskeaeplPePVHVTVAASPptphlfeQMTNLNLHPVHV-------------------- 345
Cdd:PLN02246 267 LIQRHKVT---IAPFV-------------P-PIVLAIAKSP-------VVEKYDLSSIRMvlsgaaplgkeledafrakl 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 346 --------YGMTETyGPItkgyylpawdnLPSSERYKKmarqghgfvTSLPVR------VIKTdvAEGTVID------VA 405
Cdd:PLN02246 323 pnavlgqgYGMTEA-GPV-----------LAMCLAFAK---------EPFPVKsgscgtVVRN--AELKIVDpetgasLP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 406 RDgkEIGEIVFVGNICARGYYKDPDATRKLF-AGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTH 484
Cdd:PLN02246 380 RN--QPGEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISH 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169764941 485 PDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIEWarnasdISKFMI----PREVEVVAELPKTSTGKV-RKNI 558
Cdd:PLN02246 458 PSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQF------VAKQVVfykrIHKVFFVDSIPKAPSGKIlRKDL 530
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
201-556 |
5.68e-23 |
|
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: 100.41 E-value: 5.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 201 DVIALAYTSGTTARPKGVEYTHRgCYLAAMGNVIESGLNSHRGRCRYLwTLPMFHACGwtFPWAVTAVRGTHYCL---RK 277
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANK-TFFAVPDILQKEGLNWVVGDVTYL-PLPATHIGG--LWWILTCLIHGGLCVtggEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 278 IDYPQIWKLLKQEHITHFNAAPT-----VNTLLCNSKEAEPLPepvHVTVAASPP---TPHLFEQMTNLNLhpVHVYGMT 349
Cdd:cd17635 78 TTYKSLFKILTTNAVTTTCLVPTllsklVSELKSANATVPSLR---LIGYGGSRAiaaDVRFIEATGLTNT--AQVYGLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 350 ETygpiTKGYYLPAWDNLpsseryKKMARQGHGFvTSLPVRVIKTDVAEGTvidvardGKEIGEIVFVGNICARGYYKDP 429
Cdd:cd17635 153 ET----GTALCLPTDDDS------IEINAVGRPY-PGVDVYLAATDGIAGP-------SASFGTIWIKSPANMLGYWNNP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 430 DATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVT 509
Cdd:cd17635 215 ERTAEVLIDGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVV 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 169764941 510 VKPGKFLTGSEVIEWARNASdISKFMIPREVEVVAELPKTSTGKVRK 556
Cdd:cd17635 295 ASAELDENAIRALKHTIRRE-LEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
477-553 |
8.15e-23 |
|
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: 92.22 E-value: 8.15e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169764941 477 LESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIEWARnaSDISKFMIPREVEVVAELPKTSTGK 553
Cdd:pfam13193 2 VESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVR--EELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
144-554 |
4.11e-22 |
|
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: 100.34 E-value: 4.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 144 YRASRpSIPIIVDMDtDATEGELSGPFDEVVL--EGLTYDLDTGAKGW---------PGLEAQAASEDDVIALAYTSGTT 212
Cdd:cd17634 167 VRAGR-SVPLKKNVD-DALNPNVTSVEHVIVLkrTGSDIDWQEGRDLWwrdliakasPEHQPEAMNAEDPLFILYTSGTT 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 213 ARPKGVEYTHRGCYLAA---MGNVIESGLNShrgrcRYLWTLPMfhacGWTF--PWAV---TAVRGTHYCLR-KIDYP-- 281
Cdd:cd17634 245 GKPKGVLHTTGGYLVYAattMKYVFDYGPGD-----IYWCTADV----GWVTghSYLLygpLACGATTLLYEgVPNWPtp 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 282 -QIWKLLKQEHITHFNAAPTV-----------------NTLLCNSKEAEPL-PEPV-----HVTVAASPPTPHlfeqmtn 337
Cdd:cd17634 316 aRMWQVVDKHGVNILYTAPTAiralmaagddaiegtdrSSLRILGSVGEPInPEAYewywkKIGKEKCPVVDT------- 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 338 lnlhpvhvYGMTETYGPITKgyylpawdNLPSSERYKkmarQGHGFVTSLPVRVIKTDvAEGTVIDvardGKEIGEIVFV 417
Cdd:cd17634 389 --------WWQTETGGFMIT--------PLPGAIELK----AGSATRPVFGVQPAVVD-NEGHPQP----GGTEGNLVIT 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 418 GNI--CARGYYKDPD----ATRKLFAGGVLHsGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAG 491
Cdd:cd17634 444 DPWpgQTRTLFGDHErfeqTYFSTFKGMYFS-GDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAA 522
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169764941 492 VVAVPDSHWGERPKAFVTVKPGKFLT---GSEVIEWARNasDISKFMIPREVEVVAELPKTSTGKV 554
Cdd:cd17634 523 VVGIPHAIKGQAPYAYVVLNHGVEPSpelYAELRNWVRK--EIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
36-554 |
6.52e-22 |
|
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: 98.96 E-value: 6.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 36 RAAAIEPEAVAihhVTANNQVLrrTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNY 112
Cdd:cd17651 3 RQAARTPDAPA---LVAEGRRL--TYAELDRRANRLAHRLRARGVGpgdLVALCARRSAELVVALLAILKAGAAYVPLDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 113 RLKEDDIAYIFTHSDVEAIIVDQEFLSLLqsyrASRPSIPIIVDMDTDATEGELSgpfdevvlegltydldtgakgwPGL 192
Cdd:cd17651 78 AYPAERLAFMLADAGPVLVLTHPALAGEL----AVELVAVTLLDQPGAAAGADAE----------------------PDP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 193 EAQAASEDDVIalaYTSGTTARPKGVEYTHRGcyLAAMGNVIESGLNSHRGRCRYLWTLPMFHACGW-TFPwavTAVRGT 271
Cdd:cd17651 132 ALDADDLAYVI---YTSGSTGRPKGVVMPHRS--LANLVAWQARASSLGPGARTLQFAGLGFDVSVQeIFS---TLCAGA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 272 HYCLR----KIDYPQIWKLLKQEHITHFNAAPTVNTLLCNSKEAEPLPEPV--HVTVA-----ASPPTPHLFEQMTNLNL 340
Cdd:cd17651 204 TLVLPpeevRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAAlrYLLTGgeqlvLTEDLREFCAGLPGLRL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 341 HpvHVYGMTETYgpITKGYYLPA----WDNLPSSERYKKMARqghgfvtslpVRVIKTD---VAEGTVidvardgkeiGE 413
Cdd:cd17651 284 H--NHYGPTETH--VVTALSLPGdpaaWPAPPPIGRPIDNTR----------VYVLDAAlrpVPPGVP----------GE 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 414 IVFVGNICARGYYKDPDATRKLF------AGGVLH-SGDLAVWHADGSIQIQDRAKD-IIISG-----GEnissvaLESM 480
Cdd:cd17651 340 LYIGGAGLARGYLNRPELTAERFvpdpfvPGARMYrTGDLARWLPDGELEFLGRADDqVKIRGfrielGE------IEAA 413
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169764941 481 LVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVieWARNASDISKFMIPREVEVVAELPKTSTGKV 554
Cdd:cd17651 414 LARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAEL--RAALATHLPEYMVPSAFVLLDALPLTPNGKL 485
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
60-563 |
1.22e-21 |
|
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: 98.17 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 60 TYAETADRARGLAYYLKKHGF--KRVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQEF 137
Cdd:cd05909 9 TYRKLLTGAIALARKLAKMTKegENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 138 LSLLqsyrasrpSIPIIVDMDTdategelsgPFDEVVLEGLTYDLDTGAKGWPGLEAQA-------------ASEDDVIA 204
Cdd:cd05909 89 IEKL--------KLHHLFDVEY---------DARIVYLEDLRAKISKADKCKAFLAGKFppkwllrifgvapVQPDDPAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 205 LAYTSGTTARPKGVEYTHRGCY--LAAMGNVIESGLNShrgrcRYLWTLPMFHACGWTFPWAVTAVRGTH--YCLRKIDY 280
Cdd:cd05909 152 ILFTSGSEGLPKGVVLSHKNLLanVEQITAIFDPNPED-----VVFGALPFFHSFGLTGCLWLPLLSGIKvvFHPNPLDY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 281 PQIWKLLKQEHITHFNAAPTVNTLLCNSKEAEPLPEPVHVTVAASPPTPHLFEQMTNL-NLHPVHVYGMTETYGPITKgy 359
Cdd:cd05909 227 KKIPELIYDKKATILLGTPTFLRGYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKfGIRILEGYGTTECSPVISV-- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 360 ylpawdNLPSSERYkkmarqgHGFV-TSLPVRVIKTDVAEGTVIDVARDGkeiGEIVFVGNICARGYYKDPDATRKLFAG 438
Cdd:cd05909 305 ------NTPQSPNK-------EGTVgRPLPGMEVKIVSVETHEEVPIGEG---GLLLVRGPNVMLGYLNEPELTSFAFGD 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 439 GVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTH-PDILEAGVVAVPDSHWGERPKAFVTvkpGKFLT 517
Cdd:cd05909 369 GWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTT---TTDTD 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 169764941 518 GSEVIEWARNaSDISKFMIPREVEVVAELPKTSTGKVRKNILRDWA 563
Cdd:cd05909 446 PSSLNDILKN-AGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
53-487 |
4.29e-21 |
|
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: 96.77 E-value: 4.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 53 NNQVLRRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVE 129
Cdd:cd05932 1 GGQVVEFTWGEVADKARRLAAALRALGLEpgsKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 130 AIIVDQeflslLQSYRASRP----SIPIIVDMDTDAtegelsGPFDEvvleglTYDlDTGAKGWPGLEAQAASEDDVIAL 205
Cdd:cd05932 81 ALFVGK-----LDDWKAMAPgvpeGLISISLPPPSA------ANCQY------QWD-DLIAQHPPLEERPTRFPEQLATL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 206 AYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLNshrGRCRYLWTLPMFHAC-------GW--------------TFPWA 264
Cdd:cd05932 143 IYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTE---ENDRMLSYLPLAHVTervfvegGSlyggvlvafaesldTFVED 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 265 VTAVRGTHYclrkIDYPQIWKLLKQEHITHFNAA--------PTVNTLLcNSKEAEPLPEPvHVTVAAS---PPTPHLFE 333
Cdd:cd05932 220 VQRARPTLF----FSVPRLWTKFQQGVQDKIPQQklnlllkiPVVNSLV-KRKVLKGLGLD-QCRLAGCgsaPVPPALLE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 334 QMTNLNLHPVHVYGMTETYGpitkgyylpawdnlpsserYKKMARQGhgfvtslpvrviktDVAEGTVIDvARDGKEI-- 411
Cdd:cd05932 294 WYRSLGLNILEAYGMTENFA-------------------YSHLNYPG--------------RDKIGTVGN-AGPGVEVri 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 412 ---GEIVFVGNICARGYYKDPDATRKLF-AGGVLHSGDLAVWHADGSIQIQDRAKDII-ISGGENISSVALESMLVTHPD 486
Cdd:cd05932 340 sedGEILVRSPALMMGYYKDPEATAEAFtADGFLRTGDKGELDADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDR 419
|
.
gi 169764941 487 I 487
Cdd:cd05932 420 V 420
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
42-556 |
9.12e-21 |
|
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: 95.44 E-value: 9.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 42 PEAVAihhVTANNQVLrrTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDD 118
Cdd:cd12116 1 PDATA---VRDDDRSL--SYAELDERANRLAARLRARGVGpgdRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 119 IAYIFTHSDVEAIIVDQEflsLLQSYRASRPSIPIIVDmdtdategelsgpfdevvlegltydldtgAKGWPGLEAQAAS 198
Cdd:cd12116 76 LRYILEDAEPALVLTDDA---LPDRLPAGLPVLLLALA-----------------------------AAAAAPAAPRTPV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 199 EDDVIA-LAYTSGTTARPKGVEYTHRG--CYLAAMGNviESGLnshRGRCRYLW-TLPMFH----------ACGWTfpwA 264
Cdd:cd12116 124 SPDDLAyVIYTSGSTGRPKGVVVSHRNlvNFLHSMRE--RLGL---GPGDRLLAvTTYAFDisllelllplLAGAR---V 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 265 VTAVRGTHYclrkiDYPQIWKLLKQEHITHFNAAPTVNTLLCNSkeAEPLPEPVHVTVAASPPTPHLFEQMTNLNLHPVH 344
Cdd:cd12116 196 VIAPRETQR-----DPEALARLIEAHSITVMQATPATWRMLLDA--GWQGRAGLTALCGGEALPPDLAARLLSRVGSLWN 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 345 VYGMTET------------YGPITKGYYLPAwdnlpsserykkmarqghgfvtslpVRVIKTD-----VAEGtvidvard 407
Cdd:cd12116 269 LYGPTETtiwstaarvtaaAGPIPIGRPLAN-------------------------TQVYVLDaalrpVPPG-------- 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 408 gkEIGEIVFVGNICARGYYKDPDATRKLF-------AGGVLH-SGDLAVWHADGSIQIQDRAKDIIISGGENISSVALES 479
Cdd:cd12116 316 --VPGELYIGGDGVAQGYLGRPALTAERFvpdpfagPGSRLYrTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEA 393
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169764941 480 MLVTHPDILEAGVVAVPDSHwGERPKAFVTVKPGKFLTGSEVIEWARNAsdISKFMIPREVEVVAELPKTSTGKV-RK 556
Cdd:cd12116 394 ALAAHPGVAQAAVVVREDGG-DRRLVAYVVLKAGAAPDAAALRAHLRAT--LPAYMVPSAFVRLDALPLTANGKLdRK 468
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
407-567 |
1.85e-20 |
|
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: 95.32 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 407 DGKEIGEIVfVGNIC--------ARGYYKDPDATRKLFAG---GVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSV 475
Cdd:cd05966 427 EGNEVEGEV-EGYLVikrpwpgmARTIYGDHERYEDTYFSkfpGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTA 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 476 ALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTG---SEVIEWARNasDISKFMIPREVEVVAELPKTSTG 552
Cdd:cd05966 506 EVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDelrKELRKHVRK--EIGPIATPDKIQFVPGLPKTRSG 583
|
170
....*....|....*
gi 169764941 553 KVRKNILRDWAKGAN 567
Cdd:cd05966 584 KIMRRILRKIAAGEE 598
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
33-559 |
2.02e-20 |
|
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: 93.92 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 33 FLPRAAAIEPEAVAIhhVTANNQVlrrTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVA 109
Cdd:cd12115 4 LVEAQAARTPDAIAL--VCGDESL---TYAELNRRANRLAARLRAAGVGpesRVGVCLERTPDLVVALLAVLKAGAAYVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 110 VNYRLKEDDIAYIFTHSDVEAIIVDQeflsllqsyrasrpsipiivdmdtdategelsgpfdevvlegltydldtgakgw 189
Cdd:cd12115 79 LDPAYPPERLRFILEDAQARLVLTDP------------------------------------------------------ 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 190 pgleaqaaseDDVIALAYTSGTTARPKGVEYTHRGC------YLAAMGNVIESGLNSHRGRCRYLWTLPMFH--ACGWTF 261
Cdd:cd12115 105 ----------DDLAYVIYTSGSTGRPKGVAIEHRNAaaflqwAAAAFSAEELAGVLASTSICFDLSVFELFGplATGGKV 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 262 PWAVTAvrgthycLRKIDYPqiwkllKQEHITHFNAAPTVNTLLCnskEAEPLPEPVH-VTVAASPPTPHLFEQMTNlNL 340
Cdd:cd12115 175 VLADNV-------LALPDLP------AAAEVTLINTVPSAAAELL---RHDALPASVRvVNLAGEPLPRDLVQRLYA-RL 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 341 HPVHVYGMtetYGPITKGYYlpawdnlpssERYKKMARQGHGFVTslpvrvIKTDVAeGTVIDVARDGKE------IGEI 414
Cdd:cd12115 238 QVERVVNL---YGPSEDTTY----------STVAPVPPGASGEVS------IGRPLA-NTQAYVLDRALQpvplgvPGEL 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 415 VFVGNICARGYYKDPDATRKLF------AGGVLHS-GDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDI 487
Cdd:cd12115 298 YIGGAGVARGYLGRPGLTAERFlpdpfgPGARLYRtGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGV 377
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169764941 488 LEAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIEWARnaSDISKFMIPREVEVVAELPKTSTGKVRKNIL 559
Cdd:cd12115 378 REAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLG--TRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
38-556 |
9.41e-20 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 91.92 E-value: 9.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 38 AAIEPEAVAIHHvtannQVLRRTYAETADRARGLAYYLKKHGF---KRVGVLCPNTPAFLESIFGiaaagavnvavnyrl 114
Cdd:cd05945 1 AAANPDRPAVVE-----GGRTLTYRELKERADALAAALASLGLdagDPVVVYGHKSPDAIAAFLA--------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 115 keddiayifthsdveaiivdqeflsllqSYRASRPSIPIIVDMDTDATEG--ELSGPfdEVVLegltydldtgakgwpgl 192
Cdd:cd05945 61 ----------------------------ALKAGHAYVPLDASSPAERIREilDAAKP--ALLI----------------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 193 eaqaASEDDVIALAYTSGTTARPKGVEYTHRG--CYLAAMgnVIESGLNSHrgrCRYLWTLPM-FHACgwTFPWAVTAVR 269
Cdd:cd05945 94 ----ADGDDNAYIIFTSGSTGRPKGVQISHDNlvSFTNWM--LSDFPLGPG---DVFLNQAPFsFDLS--VMDLYPALAS 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 270 G-THYCLRK---IDYPQIWKLLKQEHITHFNAAPTVNTLLCNSKE---------------AEPLPEPVHVTVAASPPTPH 330
Cdd:cd05945 163 GaTLVPVPRdatADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTftpeslpslrhflfcGEVLPHKTARALQQRFPDAR 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 331 LFeqmtnlNLhpvhvYGMTETYGPITkgYYlpAWDNLPSSErykkmarqghgfVTSLPVRVIKTDvAEGTVID---VARD 407
Cdd:cd05945 243 IY------NT-----YGPTEATVAVT--YI--EVTPEVLDG------------YDRLPIGYAKPG-AKLVILDedgRPVP 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 408 GKEIGEIVFVGNICARGYYKDPDATRKLF----AGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVT 483
Cdd:cd05945 295 PGEKGELVISGPSVSKGYLNNPEKTAAAFfpdeGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQ 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 484 HPDILEAGVVAVPDSHWGERPKAFVTVKPGkfltgseviEWARNASDISKF--------MIPREVEVVAELPKTSTGKV- 554
Cdd:cd05945 375 VPGVKEAVVVPKYKGEKVTELIAFVVPKPG---------AEAGLTKAIKAElaerlppyMIPRRFVYLDELPLNANGKId 445
|
..
gi 169764941 555 RK 556
Cdd:cd05945 446 RK 447
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
207-554 |
7.66e-19 |
|
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: 89.23 E-value: 7.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 207 YTSGTTARPKGVEYTHRGcyLAAMGNVIESGLNSHRGRCRYLWTLPMFHACGWTFPWAVTAvrGTHYCL----RKIDYPQ 282
Cdd:cd17652 100 YTSGSTGRPKGVVVTHRG--LANLAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLA--GATLVLapaeELLPGEP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 283 IWKLLKQEHITHFNAAPTVNTLLcnskEAEPLPEPVHVTVAASPPTPHLFEQ------MTNlnlhpvhVYGMTETYGPIT 356
Cdd:cd17652 176 LADLLREHRITHVTLPPAALAAL----PPDDLPDLRTLVVAGEACPAELVDRwapgrrMIN-------AYGPTETTVCAT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 357 KGYYLPAWDNLPsserykkmarqghgfvtslpvrvIKTDVAeGTVIDVARDGKE------IGEIVFVGNICARGYYKDPD 430
Cdd:cd17652 245 MAGPLPGGGVPP-----------------------IGRPVP-GTRVYVLDARLRpvppgvPGELYIAGAGLARGYLNRPG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 431 ATRKLF-------AGGVLH-SGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGE 502
Cdd:cd17652 301 LTAERFvadpfgaPGSRMYrTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDK 380
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 169764941 503 RPKAFVTVKPGKFLTGSEVIEWARNasDISKFMIPREVEVVAELPKTSTGKV 554
Cdd:cd17652 381 RLVAYVVPAPGAAPTAAELRAHLAE--RLPGYMVPAAFVVLDALPLTPNGKL 430
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
38-559 |
9.75e-19 |
|
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: 89.31 E-value: 9.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 38 AAIEPEAVAihhVTANNQVLrrTYAETADRARGLAYYLKKHGFKR---VGVLCPNTPAFLESIFGIaaagavnvavnyrL 114
Cdd:cd17655 7 AEKTPDHTA---VVFEDQTL--TYRELNERANQLARTLREKGVGPdtiVGIMAERSLEMIVGILGI-------------L 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 115 K-------------EDDIAYIFTHSDVEaIIVDQEFLSLLQSYRASrpsipIIVDMDTDATEGELSGpfdevvlegltyd 181
Cdd:cd17655 69 KaggaylpidpdypEERIQYILEDSGAD-ILLTQSHLQPPIAFIGL-----IDLLDEDTIYHEESEN------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 182 ldtgakgwpgLEAQAASEDdviaLAY---TSGTTARPKGVEYTHRGC--YLAAMGNVIESGLNSHrgrcrylwtLPMFHA 256
Cdd:cd17655 130 ----------LEPVSKSDD----LAYviyTSGSTGKPKGVMIEHRGVvnLVEWANKVIYQGEHLR---------VALFAS 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 257 cgWTFPWAVTAV------RGTHYCLRK---IDYPQIWKLLKQEHITHFNAAPTVNTLLCNSKEAEPLPEPvHVTVAASPP 327
Cdd:cd17655 187 --ISFDASVTEIfasllsGNTLYIVRKetvLDGQALTQYIRQNRITIIDLTPAHLKLLDAADDSEGLSLK-HLIVGGEAL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 328 TPHLFEQMTNLNLHPV---HVYGMTETYGPITKGYYLPAWDNLPSSERYKKMARqghgfvtslpVRVIKTDvAEGTVIDV 404
Cdd:cd17655 264 STELAKKIIELFGTNPtitNAYGPTETTVDASIYQYEPETDQQVSVPIGKPLGN----------TRIYILD-QYGRPQPV 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 405 ArdgkEIGEIVFVGNICARGYYKDPDATRKLF------AGGVLH-SGDLAVWHADGSIQIQDRAKDIIISGGENISSVAL 477
Cdd:cd17655 333 G----VAGELYIGGEGVARGYLNRPELTAEKFvddpfvPGERMYrTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEI 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 478 ESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKpgKFLTGSEVIEWArnASDISKFMIPREVEVVAELPKTSTGKVRKN 557
Cdd:cd17655 409 EARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSE--KELPVAQLREFL--ARELPDYMIPSYFIKLDEIPLTPNGKVDRK 484
|
..
gi 169764941 558 IL 559
Cdd:cd17655 485 AL 486
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
58-493 |
9.93e-19 |
|
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: 88.96 E-value: 9.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 58 RRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVD 134
Cdd:cd17640 5 RITYKDLYQEILDFAAGLRSLGVKageKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 135 QeflsllqsyrasrpsipiivdmdtdategelsgpfdevvlegltydldtgakgwpgleaqaaSEDDVIALAYTSGTTAR 214
Cdd:cd17640 85 N--------------------------------------------------------------DSDDLATIIYTSGTTGN 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 215 PKGVEYTHRGcYLAAMGNvIESGLNSHRGRcRYLWTLPMFH----ACGWT-FPWAVTAVRGTHYCLRK----------ID 279
Cdd:cd17640 103 PKGVMLTHAN-LLHQIRS-LSDIVPPQPGD-RFLSILPIWHsyerSAEYFiFACGCSQAYTSIRTLKDdlkrvkphyiVS 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 280 YPQIWKLLKQEHITHFNAAPTVNTLLC-------NSKEAeplpepvhVTVAASPPtPHL---FEQmtnLNLHPVHVYGMT 349
Cdd:cd17640 180 VPRLWESLYSGIQKQVSKSSPIKQFLFlfflsggIFKFG--------ISGGGALP-PHVdtfFEA---IGIEVLNGYGLT 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 350 ETyGPITkgyylpawdnlpSSERYKKMARQGHGfvTSLPVRVIKtdvaegtVIDVarDGKEI---GE--IVFV-GNICAR 423
Cdd:cd17640 248 ET-SPVV------------SARRLKCNVRGSVG--RPLPGTEIK-------IVDP--EGNVVlppGEkgIVWVrGPQVMK 303
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169764941 424 GYYKDPDATRK-LFAGGVLHSGDLAVWHADGSIQIQDRAKD-IIISGGENISSVALESMLVTHPDILEAGVV 493
Cdd:cd17640 304 GYYKNPEATSKvLDSDGWFNTGDLGWLTCGGELVLTGRAKDtIVLSNGENVEPQPIEEALMRSPFIEQIMVV 375
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
60-492 |
1.23e-18 |
|
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: 88.09 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 60 TYAETADRARGLAYYLKKHGF----KRVGVLCPNTPAFLESIFGIaaagavnvavnyrLK-------------EDDIAYI 122
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGvgpgDRVAVLLERSAELVVAILAV-------------LKagaayvpldpaypAERLAFI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 123 FTHSDVEAIIVDQEFLSLLqsyrasrpsipiivdmdtdategelsgpfDEVVLEGLTYDLDTGAKGWPGL-EAQAASEDD 201
Cdd:TIGR01733 68 LEDAGARLLLTDSALASRL-----------------------------AGLVLPVILLDPLELAALDDAPaPPPPDAPSG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 202 VIALAY---TSGTTARPKGVEYTHRGC--YLAAMGNVIESGLNShrgrcRYLWTLPM-FHACGWTF--PWAVTAvrgthy 273
Cdd:TIGR01733 119 PDDLAYviyTSGSTGRPKGVVVTHRSLvnLLAWLARRYGLDPDD-----RVLQFASLsFDASVEEIfgALLAGA------ 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 274 CL-------RKIDyPQIWKLLKQEH-ITHFNAAPTVNTLLcnSKEAEPLPEPV-HVTVAASPPTPHLFEQMTNL--NLHP 342
Cdd:TIGR01733 188 TLvvppedeERDD-AALLAALIAEHpVTVLNLTPSLLALL--AAALPPALASLrLVILGGEALTPALVDRWRARgpGARL 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 343 VHVYGMTETYGPITKGYYLPAWDNLPSSERYkkmarqGHGFvTSLPVRVIK---TDVAEGtvidvardgkEIGEIVFVGN 419
Cdd:TIGR01733 265 INLYGPTETTVWSTATLVDPDDAPRESPVPI------GRPL-ANTRLYVLDddlRPVPVG----------VVGELYIGGP 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 420 ICARGYYKDPDATRKLF--------AGGVLH-SGDLAVWHADGSIQIQDRAKDII-ISG-----GEnissvaLESMLVTH 484
Cdd:TIGR01733 328 GVARGYLNRPELTAERFvpdpfaggDGARLYrTGDLVRYLPDGNLEFLGRIDDQVkIRGyrielGE------IEAALLRH 401
|
....*...
gi 169764941 485 PDILEAGV 492
Cdd:TIGR01733 402 PGVREAVV 409
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
42-556 |
1.36e-18 |
|
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: 88.87 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 42 PEAVAIHHvtaNNQVLrrTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDD 118
Cdd:cd12114 1 PDATAVIC---GDGTL--TYGELAERARRVAGALKAAGVRpgdLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 119 IAYIFTHSDVEAIIVDQEFLSLLQsyrasRPSIPIIVDMDTDATEGELSGPfdEVVLEGLTYdldtgakgwpgleaqaas 198
Cdd:cd12114 76 REAILADAGARLVLTDGPDAQLDV-----AVFDVLILDLDALAAPAPPPPV--DVAPDDLAY------------------ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 199 eddVIalaYTSGTTARPKGVEYTHRGCYlaamgNVIESgLNSHrgrcrylwtlpmfhacgwtfpWAVT------AVRGTH 272
Cdd:cd12114 131 ---VI---FTSGSTGTPKGVMISHRAAL-----NTILD-INRR---------------------FAVGpddrvlALSSLS 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 273 YCLRKIDY--------------------PQIWKLLKQEH-ITHFNAAPTVNTLLCNSKEAEPLPEPVHVTVAAS------ 325
Cdd:cd12114 178 FDLSVYDIfgalsagatlvlpdearrrdPAHWAELIERHgVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSgdwipl 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 326 --PPTPH-LFEqmtnlNLHPVHVYGMTET-----YGPITKgyYLPAWDNLP-----SSERYKKMARQGHgfvtslpvrvi 392
Cdd:cd12114 258 dlPARLRaLAP-----DARLISLGGATEAsiwsiYHPIDE--VPPDWRSIPygrplANQRYRVLDPRGR----------- 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 393 ktDVAEGTVidvardgkeiGEIVFVGNICARGYYKDPDATRKLF----AGGVLH-SGDLAVWHADGSIQIQDRAKDIIIS 467
Cdd:cd12114 320 --DCPDWVP----------GELWIGGRGVALGYLGDPELTAARFvthpDGERLYrTGDLGRYRPDGTLEFLGRRDGQVKV 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 468 GGENISSVALESMLVTHPDILEAGVVAVPDSHwGERPKAFVTVKPGKFLTGSEVIEwARNASDISKFMIPREVEVVAELP 547
Cdd:cd12114 388 RGYRIELGEIEAALQAHPGVARAVVVVLGDPG-GKRLAAFVVPDNDGTPIAPDALR-AFLAQTLPAYMIPSRVIALEALP 465
|
....*....
gi 169764941 548 KTSTGKVRK 556
Cdd:cd12114 466 LTANGKVDR 474
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
60-561 |
1.69e-18 |
|
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: 89.02 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 60 TYAETADRARGLAYYLKKHGFKR---VGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIV-DQ 135
Cdd:cd17641 13 TWADYADRVRAFALGLLALGVGRgdvVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAeDE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 136 EFLSLLQSYRASRPSIPIIVDMDTDATEGELSG---PFDEVVLEGLTYDldtgaKGWPGL---EAQAASEDDVIALAYTS 209
Cdd:cd17641 93 EQVDKLLEIADRIPSVRYVIYCDPRGMRKYDDPrliSFEDVVALGRALD-----RRDPGLyerEVAAGKGEDVAVLCTTS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 210 GTTARPKGVEYTHRgcylaamgNVIESGLNSHR--GRCR---YLWTLPMfhacgwtfPWA---VTAVRGTHYCLRKIDYP 281
Cdd:cd17641 168 GTTGKPKLAMLSHG--------NFLGHCAAYLAadPLGPgdeYVSVLPL--------PWIgeqMYSVGQALVCGFIVNFP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 282 QiwkllkqehithfnaapTVNTLLCNSKEAEPlpepvHVTVAAspptPHLFEQMtnlnLHPVHVYGMTETygPITKGYY- 360
Cdd:cd17641 232 E-----------------EPETMMEDLREIGP-----TFVLLP----PRVWEGI----AADVRARMMDAT--PFKRFMFe 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 361 ------------------LPAWDNLPSSERYKKMARQ-----GHGFVTS--------------------LPVRVI--KTD 395
Cdd:cd17641 280 lgmklglraldrgkrgrpVSLWLRLASWLADALLFRPlrdrlGFSRLRSaatggaalgpdtfrffhaigVPLKQLygQTE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 396 VAEGTVIDvaRDGK------------------EIGEIVFVGNICARGYYKDPDATRKLF-AGGVLHSGDLAVWHADGSIQ 456
Cdd:cd17641 360 LAGAYTVH--RDGDvdpdtvgvpfpgtevridEVGEILVRSPGVFVGYYKNPEATAEDFdEDGWLHTGDAGYFKENGHLV 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 457 IQDRAKDI-IISGGENISSVALESMLVTHPDILEAGVVAvpdshwGERP--KAFVTVKPgkfltgSEVIEWARNA----- 528
Cdd:cd17641 438 VIDRAKDVgTTSDGTRFSPQFIENKLKFSPYIAEAVVLG------AGRPylTAFICIDY------AIVGKWAEQRgiaft 505
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169764941 529 --SDISKF-----MIPREVEVV-AELPK---------------------TSTGKVRKNILRD 561
Cdd:cd17641 506 tyTDLASRpevyeLIRKEVEKVnASLPEaqrirrflllykeldaddgelTRTRKVRRGVIAE 567
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
320-563 |
1.71e-18 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 88.13 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 320 VTVAASPPTPHLFEQMTNLNLHPVHVYGMTETYGPItkgyylpawdnlpsserykkmarqghgfVTSLPVRVIKTDVAEG 399
Cdd:PRK07445 235 ILLGGAPAWPSLLEQARQLQLRLAPTYGMTETASQI----------------------------ATLKPDDFLAGNNSSG 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 400 TVIDVAR---DGKEIGEIVFVGNICARGYYKDPDATRKLFAggvlhSGDLAVWHADGSIQIQDRAKDIIISGGENISSVA 476
Cdd:PRK07445 287 QVLPHAQitiPANQTGNITIQAQSLALGYYPQILDSQGIFE-----TDDLGYLDAQGYLHILGRNSQKIITGGENVYPAE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 477 LESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFlTGSEVIEWArnASDISKFMIPREVEVVAELPKTSTGKVRK 556
Cdd:PRK07445 362 VEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSI-SLEELKTAI--KDQLSPFKQPKHWIPVPQLPRNPQGKINR 438
|
....*..
gi 169764941 557 NILRDWA 563
Cdd:PRK07445 439 QQLQQIA 445
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
42-559 |
2.95e-18 |
|
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: 87.53 E-value: 2.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 42 PEAVAIhhVTANNQVlrrTYAETADRARGLAYYLKKHGFKR---VGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDD 118
Cdd:cd17656 2 PDAVAV--VFENQKL---TYRELNERSNQLARFLREKGVKKdsiVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 119 IAYIFTHSDVEAIivdqeflsLLQSYRASRPSIpiivdmdtdatEGELSGPFDEVVLEGLTYDLDTgakgwpgleaqAAS 198
Cdd:cd17656 77 RIYIMLDSGVRVV--------LTQRHLKSKLSF-----------NKSTILLEDPSISQEDTSNIDY-----------INN 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 199 EDDVIALAYTSGTTARPKGVEYTHRgcylaAMGNVIE-----SGLNSHRGRCRYlwTLPMFHACgWTFPWAVTAVRGTHY 273
Cdd:cd17656 127 SDDLLYIIYTSGTTGKPKGVQLEHK-----NMVNLLHferekTNINFSDKVLQF--ATCSFDVC-YQEIFSTLLSGGTLY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 274 CLR---KIDYPQIWKLLKQEHITHFNAAPTVNTLLCNSKEA-EPLPEPVHVTVAASPP---TPHLFEQMTNLNLHPVHVY 346
Cdd:cd17656 199 IIReetKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFiNRFPTCVKHIITAGEQlviTNEFKEMLHEHNVHLHNHY 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 347 GMTETYgpITKGYYL---PAWDNLPsserykkmarqghgfvtslPV--RVIKTDV----AEGTVIDVArdgkEIGEIVFV 417
Cdd:cd17656 279 GPSETH--VVTTYTInpeAEIPELP-------------------PIgkPISNTWIyildQEQQLQPQG----IVGELYIS 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 418 GNICARGYYKDPDATRKLFAGG-------VLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEA 490
Cdd:cd17656 334 GASVARGYLNRQELTAEKFFPDpfdpnerMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEA 413
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169764941 491 GVVAVPDSHWGERPKAFVTvkPGKFLTGSEVIEWArnASDISKFMIPREVEVVAELPKTSTGKVRKNIL 559
Cdd:cd17656 414 VVLDKADDKGEKYLCAYFV--MEQELNISQLREYL--AKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
407-554 |
4.93e-18 |
|
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: 85.15 E-value: 4.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 407 DGKEIGEI------VFVGNICARGYYKDpdatrklfagGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESM 480
Cdd:cd17633 180 DGGEIGKIfvksemVFSGYVRGGFSNPD----------GWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESV 249
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169764941 481 LVTHPDILEAGVVAVPDSHWGERPKAFVTvkpGKFLTGSEVIEWARNasDISKFMIPREVEVVAELPKTSTGKV 554
Cdd:cd17633 250 LKAIPGIEEAIVVGIPDARFGEIAVALYS---GDKLTYKQLKRFLKQ--KLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
424-564 |
7.69e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 86.37 E-value: 7.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 424 GYYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGER 503
Cdd:PRK07638 346 GYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEK 425
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169764941 504 PKAFVtvkpgkflTGSEVIEWARNA--SDISKFMIPREVEVVAELPKTSTGKVRKNILRDWAK 564
Cdd:PRK07638 426 PVAII--------KGSATKQQLKSFclQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIE 480
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
38-556 |
2.58e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 86.16 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 38 AAIEPEAVAihhVTANNQVLrrTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRL 114
Cdd:PRK12316 4561 ARMTPDAVA---VVFDEEKL--TYAELNRRANRLAHALIARGVGpevLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEY 4635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 115 KEDDIAYIFTHSDVEaiivdqefLSLLQSYRASRPSIPiivdmdtdatEGelsgpfdevvLEGLTYDLDTGAKGWPGLEA 194
Cdd:PRK12316 4636 PRERLAYMMEDSGAA--------LLLTQSHLLQRLPIP----------DG----------LASLALDRDEDWEGFPAHDP 4687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 195 QAASEDDVIA-LAYTSGTTARPKGVEYTHRGC--YLAAMGNVIESGLNShrgrCRYLWTLPMFHACGWTFPWAVTA---- 267
Cdd:PRK12316 4688 AVRLHPDNLAyVIYTSGSTGRPKGVAVSHGSLvnHLHATGERYELTPDD----RVLQFMSFSFDGSHEGLYHPLINgasv 4763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 268 -VRGTHYCLRKIDYPQIwkllKQEHITHFNAAPTVNTLLCNSKEAEPLPEPVHVTVAASPPTPHLFEQMTNLNLHPVHVY 346
Cdd:PRK12316 4764 vIRDDSLWDPERLYAEI----HEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLF 4839
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 347 gmtETYGPITKGYYLPAWDNLPSSERYKKMARQGhgfvTSLPVRviktdvaEGTVIDVARDGKEI---GEIVFVGNICAR 423
Cdd:PRK12316 4840 ---NGYGPTETTVTVLLWKARDGDACGAAYMPIG----TPLGNR-------SGYVLDGQLNPLPVgvaGELYLGGEGVAR 4905
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 424 GYYKDPDATRKLFA-------GGVLH-SGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAV 495
Cdd:PRK12316 4906 GYLERPALTAERFVpdpfgapGGRLYrTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQ 4985
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169764941 496 PDSHwGERPKAFVTVKPGKFLTGSEVIEWARN------ASDISKFMIPREVEVVAELPKTSTGKV-RK 556
Cdd:PRK12316 4986 EGAV-GKQLVGYVVPQDPALADADEAQAELRDelkaalRERLPEYMVPAHLVFLARMPLTPNGKLdRK 5052
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
42-554 |
3.00e-17 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 84.28 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 42 PEAVAihhVTANNQVLrrTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDD 118
Cdd:cd17643 1 PEAVA---VVDEDRRL--TYGELDARANRLARTLRAEGVGpgdRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 119 IAYIFTHSDVEAIIVDQEflsllqsyrasrpsipiivdmdtdategelsgpfdevvleGLTYdldtgakgwpgleaqaas 198
Cdd:cd17643 76 IAFILADSGPSLLLTDPD----------------------------------------DLAY------------------ 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 199 eddVIalaYTSGTTARPKGVEYTHRgcylaamgNVIesGLNSHRGRCRYL-----WTlpMFHACGWTFP----WAVTAVR 269
Cdd:cd17643 98 ---VI---YTSGSTGRPKGVVVSHA--------NVL--ALFAATQRWFGFneddvWT--LFHSYAFDFSvweiWGALLHG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 270 GT-----HYCLRKIDypQIWKLLKQEHITHFNAAPT-----VNTLLCNSKEAEPLP------EPVHVTVAASpptphLFE 333
Cdd:cd17643 160 GRlvvvpYEVARSPE--DFARLLRDEGVTVLNQTPSafyqlVEAADRDGRDPLALRyvifggEALEAAMLRP-----WAG 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 334 QMTNLNLHPVHVYGMTET-----YGPITKGYyLPAWDNLPSSERykkmarqghgfVTSLPVRVIKTDVAegtviDVARDG 408
Cdd:cd17643 233 RFGLDRPQLVNMYGITETtvhvtFRPLDAAD-LPAAAASPIGRP-----------LPGLRVYVLDADGR-----PVPPGV 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 409 keIGEIVFVGNICARGYYKDPDATRKLF----AGG----VLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESM 480
Cdd:cd17643 296 --VGELYVSGAGVARGYLGRPELTAERFvanpFGGpgsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAA 373
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169764941 481 LVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIEWARNAsdISKFMIPREVEVVAELPKTSTGKV 554
Cdd:cd17643 374 LATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKEL--LPDYMVPARYVPLDALPLTVNGKL 445
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
422-565 |
3.41e-17 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 84.81 E-value: 3.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 422 ARGYYKDPDATRKL----FAGGVLhSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPD 497
Cdd:PRK00174 463 MRTIYGDHERFVKTyfstFKGMYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPD 541
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169764941 498 SHWGERPKAFVTVKPGKflTGS-----EVIEWARnaSDISKFMIPREVEVVAELPKTSTGKVRKNILRDWAKG 565
Cdd:PRK00174 542 DIKGQGIYAFVTLKGGE--EPSdelrkELRNWVR--KEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEG 610
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
36-560 |
3.71e-17 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 84.93 E-value: 3.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 36 RAAAIEPEAVAIhhvTANNQVLrrTYAETADRARGLAYYLKKHGFKR---VGVLCPNTPAFLESIFGIAAAGAVNVAVNY 112
Cdd:PRK08279 45 EAAARHPDRPAL---LFEDQSI--SYAELNARANRYAHWAAARGVGKgdvVALLMENRPEYLAAWLGLAKLGAVVALLNT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 113 RLKEDDIAYIFTHSDVEAIIVDQEFLSLLQSYRA--SRPSIPIIVDMDTDATEGELSgpfdevvlegltyDLDTGAKGWP 190
Cdd:PRK08279 120 QQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARAdlARPPRLWVAGGDTLDDPEGYE-------------DLAAAAAGAP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 191 GLEAQAASE---DDVIALAYTSGTTARPKGVEYTHRG--CYLAAMGNVIESGLNShrgrcRYLWTLPMFHACGWTFPWAV 265
Cdd:PRK08279 187 TTNPASRSGvtaKDTAFYIYTSGTTGLPKAAVMSHMRwlKAMGGFGGLLRLTPDD-----VLYCCLPLYHNTGGTVAWSS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 266 TAVRGTHYCL-RKIDYPQIWKLLKQEHITHFNAAPTVNTLLCNskeaeplpepvhvtvaaSPPTP----HLFEQMTNLNL 340
Cdd:PRK08279 262 VLAAGATLALrRKFSASRFWDDVRRYRATAFQYIGELCRYLLN-----------------QPPKPtdrdHRLRLMIGNGL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 341 HP---------------VHVYGMTEtyGPITkgyyLPAWDNLPSSErykkmarqghGFVTSL---PVRVIKTDV------ 396
Cdd:PRK08279 325 RPdiwdefqqrfgipriLEFYAASE--GNVG----FINVFNFDGTV----------GRVPLWlahPYAIVKYDVdtgepv 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 397 --AEGTVIDVARDgkEIGEIvfVGNICARGY---YKDPDATRK-----LFAGG--VLHSGDLAVWHADGSIQIQDRAKDI 464
Cdd:PRK08279 389 rdADGRCIKVKPG--EVGLL--IGRITDRGPfdgYTDPEASEKkilrdVFKKGdaWFNTGDLMRDDGFGHAQFVDRLGDT 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 465 IISGGENISSVALESMLVTHPDILEAGV--VAVPDsHWGERPKAFVTVKPGKFLTGSEVieWARNASDISKFMIPREVEV 542
Cdd:PRK08279 465 FRWKGENVATTEVENALSGFPGVEEAVVygVEVPG-TDGRAGMAAIVLADGAEFDLAAL--AAHLYERLPAYAVPLFVRL 541
|
570
....*....|....*...
gi 169764941 543 VAELPKTSTGKVRKNILR 560
Cdd:PRK08279 542 VPELETTGTFKYRKVDLR 559
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
42-565 |
4.51e-17 |
|
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: 84.67 E-value: 4.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 42 PEAVAIHHVTANNQVLRR-TYAETADRARGLAYYLKKHGFK---RVGVLCPNTPaflESIFGIAAagavnvavnyrlked 117
Cdd:cd05967 65 GDQIALIYDSPVTGTERTyTYAELLDEVSRLAGVLRKLGVVkgdRVIIYMPMIP---EAAIAMLA--------------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 118 dIAYI-FTHSDV---------EAIIVDQEFLSLLQSYRASRPSIPI----IVDmdtDATEGELSGPFDEVVLEGLTYDLD 183
Cdd:cd05967 127 -CARIgAIHSVVfggfaakelASRIDDAKPKLIVTASCGIEPGKVVpykpLLD---KALELSGHKPHHVLVLNRPQVPAD 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 184 TGAKG----WPGLEAQAASEDDVIALA-------YTSGTTARPKGV-----------EYTHRGCYLAAMGNVIESGlnSH 241
Cdd:cd05967 203 LTKPGrdldWSELLAKAEPVDCVPVAAtdplyilYTSGTTGKPKGVvrdngghavalNWSMRNIYGIKPGDVWWAA--SD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 242 RGrcrylWTL--------PMFHACgwtfpwavTAVRGTHYCLRKIDYPQIWKLLKQEHITHFNAAPTVNTLLcnsKEAEP 313
Cdd:cd05967 281 VG-----WVVghsyivygPLLHGA--------TTVLYEGKPVGTPDPGAFWRVIEKYQVNALFTAPTAIRAI---RKEDP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 314 LPEPV---------HVTVA---ASPPTPHLFEQMTNLnlhPVH-VYGMTETYGPIT---KGYYLPAwdnLPSSERYKKMA 377
Cdd:cd05967 345 DGKYIkkydlsslrTLFLAgerLDPPTLEWAENTLGV---PVIdHWWQTETGWPITanpVGLEPLP---IKAGSPGKPVP 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 378 rqGHGfvtslpVRVIKTDVAEGTVidvardgKEIGEIVFVGNI---CARGYYKDPDATRKLFAG---GVLHSGDLAVWHA 451
Cdd:cd05967 419 --GYQ------VQVLDEDGEPVGP-------NELGNIVIKLPLppgCLLTLWKNDERFKKLYLSkfpGYYDTGDAGYKDE 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 452 DGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTG----SEVIEWARN 527
Cdd:cd05967 484 DGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAeeleKELVALVRE 563
|
570 580 590
....*....|....*....|....*....|....*...
gi 169764941 528 asDISKFMIPREVEVVAELPKTSTGKVRKNILRDWAKG 565
Cdd:cd05967 564 --QIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADG 599
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
197-561 |
5.80e-17 |
|
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: 83.64 E-value: 5.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 197 ASEDDVIALAYTSGTTARPKGVEYTHRGCYLAamGNVIESGLNSHRGRcRYLWTLPMFHACGWTFPWAVTAVRGTHYCL- 275
Cdd:cd05937 84 VDPDDPAILIYTSGTTGLPKAAAISWRRTLVT--SNLLSHDLNLKNGD-RTYTCMPLYHGTAAFLGACNCLMSGGTLALs 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 276 RKIDYPQIWKLLKQEHITHFN-AAPTVNTLLcnSKEAEPLPEPVHVTVA----ASPPTPHLFEQMTNLnlhPV--HVYGM 348
Cdd:cd05937 161 RKFSASQFWKDVRDSGATIIQyVGELCRYLL--STPPSPYDRDHKVRVAwgngLRPDIWERFRERFNV---PEigEFYAA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 349 TETYGPITKgYYLPAWdNLPSSERYKKMARQGHGFV---------TSLPVRVIKTDVAEgtVIDVARDGKEIGEIVFVGN 419
Cdd:cd05937 236 TEGVFALTN-HNVGDF-GAGAIGHHGLIRRWKFENQvvlvkmdpeTDDPIRDPKTGFCV--RAPVGEPGEMLGRVPFKNR 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 420 ICARGYYKDPDATRKLFAGGVLH-------SGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGV 492
Cdd:cd05937 312 EAFQGYLHNEDATESKLVRDVFRkgdiyfrTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANV 391
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169764941 493 --VAVPdSHWGERPKAFVTVKPGKflTGSEVIEWARNAS----DISKFMIPREVEVVAELPKTSTGKVRKNILRD 561
Cdd:cd05937 392 ygVKVP-GHDGRAGCAAITLEESS--AVPTEFTKSLLASlarkNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
26-559 |
6.80e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 84.83 E-value: 6.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 26 HTLSPTSFLPRA--------AAIEPEAVAIhhvTANNQVLrrTYAETADRARGLAYYLKKHGF---KRVGVLCPNTPAFL 94
Cdd:PRK12467 502 WNAPATEYAPDCvhqlieaqARQHPERPAL---VFGEQVL--SYAELNRQANRLAHVLIAAGVgpdVLVGIAVERSIEMV 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 95 ESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQEFLSLLqsyrasrpsipiivDMDTDATEGELSGPFDEVv 174
Cdd:PRK12467 577 VGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQL--------------PVPAGLRSLCLDEPADLL- 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 175 legltydldtgaKGWPGLEAQAASEDDVIALA-YTSGTTARPKGVEYTHRgcylaAMGNVIESGLNSHRGRCRYLW---T 250
Cdd:PRK12467 642 ------------CGYSGHNPEVALDPDNLAYViYTSGSTGQPKGVAISHG-----ALANYVCVIAERLQLAADDSMlmvS 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 251 LPMFHACGWTFPWAVTAVRGTHY----CLRkiDYPQIWKLLKQEHITHFNAAPTVNTLLCNSKEAEPLPEPVHVTVAASP 326
Cdd:PRK12467 705 TFAFDLGVTELFGALASGATLHLlppdCAR--DAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRALVCGGEA 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 327 PTPHLFEQMTNL--NLHPVHVYGMTET-----YGPITKgyylpawDNLPSSERYKKMArqghgfVTSLPVRVIKTDVAEG 399
Cdd:PRK12467 783 LQVDLLARVRALgpGARLINHYGPTETtvgvsTYELSD-------EERDFGNVPIGQP------LANLGLYILDHYLNPV 849
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 400 TVidvardgKEIGEIVFVGNICARGYYKDPDATRKLF-------AGGVLH-SGDLAVWHADGSIQIQDRAKDIIISGGEN 471
Cdd:PRK12467 850 PV-------GVVGELYIGGAGLARGYHRRPALTAERFvpdpfgaDGGRLYrTGDLARYRADGVIEYLGRMDHQVKIRGFR 922
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 472 ISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIEWARNA--SDISKFMIPREVEVVAELPKT 549
Cdd:PRK12467 923 IELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVPAAVADGAEHQATRDELKAQlrQVLPDYMVPAHLLLLDSLPLT 1002
|
570
....*....|
gi 169764941 550 STGKVRKNIL 559
Cdd:PRK12467 1003 PNGKLDRKAL 1012
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
36-554 |
1.60e-16 |
|
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: 82.32 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 36 RAAAIEPEAVAihhVTANNQVLrrTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIaaagavnvavny 112
Cdd:cd17646 6 EQAARTPDAPA---VVDEGRTL--TYRELDERANRLAHLLRARGVGpedRVAVLLPRSADLVVALLAV------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 113 rlkeddiayifthsdVEAIIVdqeFLSLLQSYRASRpsIPIIVDmDTDA----TEGELSGPFdeVVLEGLTYDLDTGAKG 188
Cdd:cd17646 69 ---------------LKAGAA---YLPLDPGYPADR--LAYMLA-DAGPavvlTTADLAARL--PAGGDVALLGDEALAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 189 WPGLEAQAASEDDVIA-LAYTSGTTARPKGVEYTHRGC--YLAAMGNviESGLNSHRgrcRYLWTLPM-FHACGWTFPWA 264
Cdd:cd17646 126 PPATPPLVPPRPDNLAyVIYTSGSTGRPKGVMVTHAGIvnRLLWMQD--EYPLGPGD---RVLQKTPLsFDVSVWELFWP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 265 -------VTAVRGTHyclRKIDYPQiwKLLKQEHIT--HFnaAPTVNTLLCNSKEAEPLPEPVHVTV---AASPPTPHLF 332
Cdd:cd17646 201 lvagarlVVARPGGH---RDPAYLA--ALIREHGVTtcHF--VPSMLRVFLAEPAAGSCASLRRVFCsgeALPPELAARF 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 333 EQMTNLNLHpvHVYGMTETYGPITKGYYLPAWDNLPsserykkmarqghgfvTSLPVRVIKTDVAegtVID----VARDG 408
Cdd:cd17646 274 LALPGAELH--NLYGPTEAAIDVTHWPVRGPAETPS----------------VPIGRPVPNTRLY---VLDdalrPVPVG 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 409 kEIGEIVFVGNICARGYYKDPDATRKLF------AGGVLH-SGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESML 481
Cdd:cd17646 333 -VPGELYLGGVQLARGYLGRPALTAERFvpdpfgPGSRMYrTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAAL 411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169764941 482 VTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKF-LTGSEVIEWARNAsdISKFMIPREVEVVAELPKTSTGKV 554
Cdd:cd17646 412 AAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAgPDTAALRAHLAER--LPEYMVPAAFVVLDALPLTANGKL 483
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
60-560 |
2.29e-16 |
|
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: 81.63 E-value: 2.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 60 TYAETADRARGLAYYLKKHGFKR---VGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQE 136
Cdd:cd05940 5 TYAELDAMANRYARWLKSLGLKPgdvVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVVDAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 137 FLsllqsyrasrpsipiivdmdtdategelsgpfdevvlegltydldtgakgwpgleaqaaseddvialAYTSGTTARPK 216
Cdd:cd05940 85 LY-------------------------------------------------------------------IYTSGTTGLPK 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 217 GVEYTHRGCYLAaMGNVIESGLNSHRGRCrYLwTLPMFHACGWTFPWAVTAVRGTHYCLR-KIDYPQIWKLLKQEHITHF 295
Cdd:cd05940 98 AAIISHRRAWRG-GAFFAGSGGALPSDVL-YT-CLPLYHSTALIVGWSACLASGATLVIRkKFSASNFWDDIRKYQATIF 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 296 NAAPTVNTLLCNSKEAEPlpEPVH-VTVA-ASPPTPHLFEQMTN-LNL-HPVHVYGMTEtyGPItkgyylpAWDNLPSSE 371
Cdd:cd05940 175 QYIGELCRYLLNQPPKPT--ERKHkVRMIfGNGLRPDIWEEFKErFGVpRIAEFYAATE--GNS-------GFINFFGKP 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 372 RykKMARQGHGFVTSLPVRVIKTDV--------AEGTVIDVARDgkEIGEIVfvGNICARGY---YKDPDAT-----RKL 435
Cdd:cd05940 244 G--AIGRNPSLLRKVAPLALVKYDLesgepirdAEGRCIKVPRG--EPGLLI--SRINPLEPfdgYTDPAATekkilRDV 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 436 FAGG--VLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGV--VAVPDsHWGERPKAFVTVK 511
Cdd:cd05940 318 FKKGdaWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPG-TDGRAGMAAIVLQ 396
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 169764941 512 PGKFLTGSEVIEWArnASDISKFMIPREVEVVAELPKTSTGKVRKNILR 560
Cdd:cd05940 397 PNEEFDLSALAAHL--EKNLPGYARPLFLRLQPEMEITGTFKQQKVDLR 443
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
60-561 |
1.11e-15 |
|
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: 79.95 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 60 TYAETADRARGLAYYLKKHGFK-----RVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVD 134
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGKpapasFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 135 qeflsllqsyrasrPSIPIIVdmdtdategelsgpFDEVvlegltydLDTGAKGWPglEAQAASEDDVIALAYTSGTTAR 214
Cdd:cd05927 87 --------------AGVKVYS--------------LEEF--------EKLGKKNKV--PPPPPKPEDLATICYTSGTTGN 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 215 PKGVEYTHRGcyLAAMGNVIESGLNSHRGRC---RYLWTLPMFH----ACGWTFPWA-----------------VTAVRG 270
Cdd:cd05927 129 PKGVMLTHGN--IVSNVAGVFKILEILNKINptdVYISYLPLAHiferVVEALFLYHgakigfysgdirlllddIKALKP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 271 THYC-----LRKIdYPQIWKLLKQEHI---THFNAAptVNTLLCNSKEAEPLPEPVH------------------VTVAA 324
Cdd:cd05927 207 TVFPgvprvLNRI-YDKIFNKVQAKGPlkrKLFNFA--LNYKLAELRSGVVRASPFWdklvfnkikqalggnvrlMLTGS 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 325 SPPTPHLFEQM-TNLNLHPVHVYGMTETYGPITKGYylpAWDNLPsserykkmarqGH--GFVTSLPVRVIktDVAEGTV 401
Cdd:cd05927 284 APLSPEVLEFLrVALGCPVLEGYGQTECTAGATLTL---PGDTSV-----------GHvgGPLPCAEVKLV--DVPEMNY 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 402 IdvARDGKEIGEIVFVGNICARGYYKDPDATRKLFA-GGVLHSGDLAVWHADGSIQIQDRAKDII-ISGGE-----NISS 474
Cdd:cd05927 348 D--AKDPNPRGEVCIRGPNVFSGYYKDPEKTAEALDeDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEyvapeKIEN 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 475 VALESMLVT----HPDILEAGVVA--VPDshwgerPKAFVtvkpgkfltgseviEWARnasdiSKFMIPREVEVVAELPk 548
Cdd:cd05927 426 IYARSPFVAqifvYGDSLKSFLVAivVPD------PDVLK--------------EWAA-----SKGGGTGSFEELCKNP- 479
|
570
....*....|...
gi 169764941 549 tstgKVRKNILRD 561
Cdd:cd05927 480 ----EVKKAILED 488
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
196-561 |
3.07e-15 |
|
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: 78.12 E-value: 3.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 196 AASEDDVIALAYTSGTTARPKGVEYTHRGC--YLAAMgnviESGLNSHRGRcRYLWTL-PMFHACGWTFpwAVTAVRGTH 272
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVlnYVSQP----PARLDVGPGS-RVAQVLsIAFDACIGEI--FSTLCNGGT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 273 YCLRkiDYPQIWKLLKQEhITHFNAAPTVNTLLcnskEAEPLPEPVHVTVAASPPTPHLFEQMTnLNLHPVHVYGMTET- 351
Cdd:cd17653 174 LVLA--DPSDPFAHVART-VDALMSTPSILSTL----SPQDFPNLKTIFLGGEAVPPSLLDRWS-PGRRLYNAYGPTECt 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 352 ----YG------PITKGYYLPawdnlpsserykkmarqghgfvtSLPVRVIKTDVAEGTVidvardgKEIGEIVFVGNIC 421
Cdd:cd17653 246 isstMTellpgqPVTIGKPIP-----------------------NSTCYILDADLQPVPE-------GVVGEICISGVQV 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 422 ARGYYKDPDATRKLFA-----GGVLH--SGDLAVWHADGSIQIQDRAKDIIISGG-----ENISSVALESMlvthPDILE 489
Cdd:cd17653 296 ARGYLGNPALTASKFVpdpfwPGSRMyrTGDYGRWTEDGGLEFLGREDNQVKVRGfrinlEEIEEVVLQSQ----PEVTQ 371
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169764941 490 AGVVAVpdshwGERPKAFVTvkpgkflTGSEVIEWARN--ASDISKFMIPREVEVVAELPKTSTGKVRKNILRD 561
Cdd:cd17653 372 AAAIVV-----NGRLVAFVT-------PETVDVDGLRSelAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
196-561 |
4.35e-15 |
|
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: 78.09 E-value: 4.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 196 AASEDDVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLNShrgRCRYLWTLPMFHacgwtfpwaVTAVrgTHYCL 275
Cdd:cd05906 163 QSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTP---QDVFLNWVPLDH---------VGGL--VELHL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 276 RKIDY---------------PQIWKLLKQEHITHFNAAPtvN---TLLCNSKEAEPLP--------------EPVHVTVA 323
Cdd:cd05906 229 RAVYLgcqqvhvpteeiladPLRWLDLIDRYRVTITWAP--NfafALLNDLLEEIEDGtwdlsslrylvnagEAVVAKTI 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 324 ASpptphLFEQMTNLNLHP---VHVYGMTETYGPITkgyylpaWDNLPSSERykkmARQGHGFVT-SLP-----VRVIKt 394
Cdd:cd05906 307 RR-----LLRLLEPYGLPPdaiRPAFGMTETCSGVI-------YSRSFPTYD----HSQALEFVSlGRPipgvsMRIVD- 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 395 dvAEGTVIDVArdgkEIGEIVFVGNICARGYYKDPDATRKLF-AGGVLHSGDLAVWHaDGSIQIQDRAKDIIISGGENIS 473
Cdd:cd05906 370 --DEGQLLPEG----EVGRLQVRGPVVTKGYYNNPEANAEAFtEDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYY 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 474 SVALESmLVTHPDILEAGVVAVpdshWGERPKA---------FVTVK--PGKFLTGSEVIE-WARNASDIS-KFMIPREV 540
Cdd:cd05906 443 SHEIEA-AVEEVPGVEPSFTAA----FAVRDPGaeteelaifFVPEYdlQDALSETLRAIRsVVSREVGVSpAYLIPLPK 517
|
410 420
....*....|....*....|.
gi 169764941 541 EvvaELPKTSTGKVRKNILRD 561
Cdd:cd05906 518 E---EIPKTSLGKIQRSKLKA 535
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
200-559 |
1.02e-14 |
|
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: 76.35 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 200 DDVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLNSHRGRcryLWTLPMFHACGWTFPWAVTAVRG-THY-CLR- 276
Cdd:cd17650 93 EDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVR---LLQMASFSFDVFAGDFARSLLNGgTLViCPDe 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 277 -KIDYPQIWKLLKQEHITHFNAAPTVNTLLCNSKEAEPL-PEPVHVTVAASPPTPHL--------FEQMTNLnlhpVHVY 346
Cdd:cd17650 170 vKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLdLSAMRLLIVGSDGCKAQdfktlaarFGQGMRI----INSY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 347 GMTETygPITKGYY------LPAWDNLPSSERYKKMarqgHGFVTSLPVRVIKTDVAegtvidvardgkeiGEIVFVGNI 420
Cdd:cd17650 246 GVTEA--TIDSTYYeegrdpLGDSANVPIGRPLPNT----AMYVLDERLQPQPVGVA--------------GELYIGGAG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 421 CARGYYKDPDATRKLF------AGGVLH-SGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVV 493
Cdd:cd17650 306 VARGYLNRPELTAERFvenpfaPGERMYrTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVA 385
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169764941 494 AVPDSHWGERPKAFVTvkPGKFLTGSEVIEWArnASDISKFMIPREVEVVAELPKTSTGKVRKNIL 559
Cdd:cd17650 386 VREDKGGEARLCAYVV--AAATLNTAELRAFL--AKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
36-561 |
1.02e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 77.89 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 36 RAAAIEPEAVAIhhVTANNQVlrrTYAETADRARGLAYYLKKHGF---KRVGVLCPNTPAFLESIFGIAAAGAVNVAVNY 112
Cdd:PRK12467 3103 AQVARTPEAPAL--VFGDQQL---SYAELNRRANRLAHRLIAIGVgpdVLVGVAVERSVEMIVALLAVLKAGGAYVPLDP 3177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 113 RLKEDDIAYIFTHSDVEAIIVDQeflSLLQsyRASRPSIPIIVDMDTDATEGEL-SGPFDEVVLEGLTYdldtgakgwpg 191
Cdd:PRK12467 3178 EYPRERLAYMIEDSGVKLLLTQA---HLLE--QLPAPAGDTALTLDRLDLNGYSeNNPSTRVMGENLAY----------- 3241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 192 leaqaaseddVIalaYTSGTTARPKGVEYTH-----RGCYLAAMgnvieSGLNSHRgrcRYLWTLPM-FHACGWTFPWAV 265
Cdd:PRK12467 3242 ----------VI---YTSGSTGKPKGVGVRHgalanHLCWIAEA-----YELDAND---RVLLFMSFsFDGAQERFLWTL 3300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 266 TA-----VRGTHYclrkIDYPQIWKLLKQEHITHFNAAPTVNTLLCNSKEAEPLPEPVHVTVAASPPTPHLFEQMTNlNL 340
Cdd:PRK12467 3301 ICggclvVRDNDL----WDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGADCASLDIYVFGGEAVPPAAFEQVKR-KL 3375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 341 HPVhvyGMTETYGPITKGYYLPAWDNLPSSERYKKMARQGHGfvtsLPVRVIKtdVAEGTVIDVARDgkEIGEIVFVGNI 420
Cdd:PRK12467 3376 KPR---GLTNGYGPTEAVVTVTLWKCGGDAVCEAPYAPIGRP----VAGRSIY--VLDGQLNPVPVG--VAGELYIGGVG 3444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 421 CARGYYKDPDATRKLF-------AGGVLH-SGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGV 492
Cdd:PRK12467 3445 LARGYHQRPSLTAERFvadpfsgSGGRLYrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVV 3524
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 493 VAVpDSHWGERPKAFVTVKPgkfLTGSEVIEWARN-ASDISKFMIPREVEVVAELPKTSTGKVRKNILRD 561
Cdd:PRK12467 3525 LAR-DGAGGKQLVAYVVPAD---PQGDWRETLRDHlAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPD 3590
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
25-566 |
1.24e-14 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 76.59 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 25 FHTLS--PTSFLPR---AAAIEPEAVAIHHVTANNQVlrrTYAETADRARGLAYYLK----KHGfKRVGVLCPNTPAFLE 95
Cdd:PRK05857 6 FQAMPqlPSTVLDRvfeQARQQPEAIALRRCDGTSAL---RYRELVAEVGGLAADLRaqsvSRG-SRVLVISDNGPETYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 96 SIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQEFLSLLQSYRASRPSIPII-VDMDTDATEGELSGPFDEVv 174
Cdd:PRK05857 82 SVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAPGSKMASSAVPEALHSIPVIaVDIAAVTRESEHSLDAASL- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 175 legltydldtgaKGWPGLEAqaaseDDVIALAYTSGTTARPKGVEYTHRgCYLAAMGNVIESGLNSHR---GRCRYLwTL 251
Cdd:PRK05857 161 ------------AGNADQGS-----EDPLAMIFTSGTTGEPKAVLLANR-TFFAVPDILQKEGLNWVTwvvGETTYS-PL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 252 PMFHACG-WtfpWAVTAVRGTHYCLRKIDY-PQIWKLLKQEHITHFNAAPTVNT-LLCNSKEAEPLPEPVHVTV-AASPP 327
Cdd:PRK05857 222 PATHIGGlW---WILTCLMHGGLCVTGGENtTSLLEILTTNAVATTCLVPTLLSkLVSELKSANATVPSLRLVGyGGSRA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 328 TPHLFEQMTNLNLHPVHVYGMTETYgpiTKGYYLPAWDNLPSSERYKKMARQGHGFVTSLPvrviKTDVAEGTVIDVArD 407
Cdd:PRK05857 299 IAADVRFIEATGVRTAQVYGLSETG---CTALCLPTDDGSIVKIEAGAVGRPYPGVDVYLA----ATDGIGPTAPGAG-P 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 408 GKEIGEIVFVGNICARGYYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDI 487
Cdd:PRK05857 371 SASFGTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGV 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 488 LEAGVVAVPDSHWGerpkAFV--TVKPGKFLTGSEVIEW-----ARNASDISKFMIPREVEVVAELPKTSTGKVRKNILR 560
Cdd:PRK05857 451 REAACYEIPDEEFG----ALVglAVVASAELDESAARALkhtiaARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLA 526
|
....*.
gi 169764941 561 DWAKGA 566
Cdd:PRK05857 527 AAATAD 532
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
192-564 |
1.47e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 75.47 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 192 LEAQAASEDDVIALAYTSGTTARPKGVEYThrgcylAAmgNVIESGLNSHR---GRCRYLWTLPMFHacgwtfpwavtaV 268
Cdd:PRK07824 27 LRVGEPIDDDVALVVATSGTTGTPKGAMLT------AA--ALTASADATHDrlgGPGQWLLALPAHH------------I 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 269 RGTHYCLRKI---DYPQIWKLLKQEHITHFNAA------PTVNTLLCNSKEAEPLPEPVHVTVAAS--------PPTPH- 330
Cdd:PRK07824 87 AGLQVLVRSViagSEPVELDVSAGFDPTALPRAvaelggGRRYTSLVPMQLAKALDDPAATAALAEldavlvggGPAPAp 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 331 LFEQMTNLNLHPVHVYGMTETYGpitkgyylpawdnlpsserykkmarqghgfvtslpvrviktdvaeGTVID-VARDGK 409
Cdd:PRK07824 167 VLDAAAAAGINVVRTYGMSETSG---------------------------------------------GCVYDgVPLDGV 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 410 EI----GEIVFVGNICARGYYK--DPDAtrklFAG-GVLHSGDLAVWHaDGSIQIQDRAKDIIISGGENISSVALESMLV 482
Cdd:PRK07824 202 RVrvedGRIALGGPTLAKGYRNpvDPDP----FAEpGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALA 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 483 THPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIewARNASDISKFMIPREVEVVAELPKTSTGKV-RKNILRD 561
Cdd:PRK07824 277 THPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLEALR--AHVARTLDRTAAPRELHVVDELPRRGIGKVdRRALVRR 354
|
...
gi 169764941 562 WAK 564
Cdd:PRK07824 355 FAG 357
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
200-497 |
9.69e-14 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 73.79 E-value: 9.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 200 DDVIALAYTSGTTARPKGVEYTHRGCYLAAMGnvIESGLNSHRGRC-RYLWTLPMFHACGWTFP-----WAVT------- 266
Cdd:cd17639 88 DDLACIMYTSGSTGNPKGVMLTHGNLVAGIAG--LGDRVPELLGPDdRYLAYLPLAHIFELAAEnvclyRGGTigygspr 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 267 -----AVRGTHYCLRK------IDYPQIWKLLKQEHITHFNAAPTV------------NTLLCNSKEAEPLPEPVHVTVA 323
Cdd:cd17639 166 tltdkSKRGCKGDLTEfkptlmVGVPAIWDTIRKGVLAKLNPMGGLkrtlfwtayqskLKALKEGPGTPLLDELVFKKVR 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 324 A----------------SPPTPhlfEQMTNLNLHPVHVYGMTETY--GPITKgyylpaWDNLPSSERykkmarqghGFVt 385
Cdd:cd17639 246 AalggrlrymlsggaplSADTQ---EFLNIVLCPVIQGYGLTETCagGTVQD------PGDLETGRV---------GPP- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 386 sLPVRVIK-TDVAEGTVIDvarDGKEI-GEIVFVGNICARGYYKDPDATRKLFAG-GVLHSGDLAVWHADGSIQIQDRAK 462
Cdd:cd17639 307 -LPCCEIKlVDWEEGGYST---DKPPPrGEILIRGPNVFKGYYKNPEKTKEAFDGdGWFHTGDIGEFHPDGTLKIIDRKK 382
|
330 340 350
....*....|....*....|....*....|....*.
gi 169764941 463 DII-ISGGENISSVALESMLVTHPDILEAGVVAVPD 497
Cdd:cd17639 383 DLVkLQNGEYIALEKLESIYRSNPLVNNICVYADPD 418
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
36-556 |
1.72e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 74.04 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 36 RAAAIEPEAVAihhVTANNQVLrrTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNY 112
Cdd:PRK12467 1582 DQAAATPEAVA---LVFGEQEL--TYGELNRRANRLAHRLIALGVGpevLVGIAVERSLEMVVGLLAILKAGGAYVPLDP 1656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 113 RLKEDDIAYIFTHSDVEaiivdqeflsLLQSYRASRPSIPIIvdmdtdatEGELSgpfdeVVLEGLTYDLDTGAKGWPGL 192
Cdd:PRK12467 1657 EYPRERLAYMIEDSGIE----------LLLTQSHLQARLPLP--------DGLRS-----LVLDQEDDWLEGYSDSNPAV 1713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 193 eaqAASEDDVIALAYTSGTTARPKGVEYTHrgcylaamGNVIEsglnshrgrcRYLWTLPMFHACG-------------- 258
Cdd:PRK12467 1714 ---NLAPQNLAYVIYTSGSTGRPKGAGNRH--------GALVN----------RLCATQEAYQLSAadvvlqftsfafdv 1772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 259 --WTFPWA-------VTAVRGTHYclrkiDYPQIWKLLKQEHITHFNAAPTVNTLLCNSKEAEPLPEPVHVTVAASPPTP 329
Cdd:PRK12467 1773 svWELFWPlingarlVIAPPGAHR-----DPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEALE 1847
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 330 -----HLFEQMTNLNLhpVHVYGMTE-----TYGPITKGyYLPAWDNLPSSErykkmarqghgfvtslPVRVIKTDVAEG 399
Cdd:PRK12467 1848 vealrPWLERLPDTGL--FNLYGPTEtavdvTHWTCRRK-DLEGRDSVPIGQ----------------PIANLSTYILDA 1908
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 400 TVIDVARdgKEIGEIVFVGNICARGYYKDPDATRKLF-------AGGVLH-SGDLAVWHADGSIQIQDRAKDIIISGGEN 471
Cdd:PRK12467 1909 SLNPVPI--GVAGELYLGGVGLARGYLNRPALTAERFvadpfgtVGSRLYrTGDLARYRADGVIEYLGRIDHQVKIRGFR 1986
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 472 ISSVALESMLVTHPDILEAGVVAVpDSHWGERPKAFVTVKPGKFLTGSEVIEWARNA------SDISKFMIPREVEVVAE 545
Cdd:PRK12467 1987 IELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVPTDPGLVDDDEAQVALRAIlknhlkASLPEYMVPAHLVFLAR 2065
|
570
....*....|..
gi 169764941 546 LPKTSTGKV-RK 556
Cdd:PRK12467 2066 MPLTPNGKLdRK 2077
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
32-523 |
3.32e-13 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 72.24 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 32 SFLPRAAAIEPEAVAI-------HHVTANNQvlRRTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIF--- 98
Cdd:PRK09274 10 RHLPRAAQERPDQLAVavpggrgADGKLAYD--ELSFAELDARSDAIAHGLNAAGIGrgmRAVLMVTPSLEFFALTFalf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 99 --GIAAAGAVNVAVNYRLKEddiayIFTHSDVEAII--VDQEFLSLLqsYRASRPSIPIIVDMDTdateGELSGpfdEVV 174
Cdd:PRK09274 88 kaGAVPVLVDPGMGIKNLKQ-----CLAEAQPDAFIgiPKAHLARRL--FGWGKPSVRRLVTVGG----RLLWG---GTT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 175 LEGLTYDLDTGAkgwpgLEAQAASEDDVIALAYTSGTTARPKGVEYTHRgcYLAAMgnvIESgLNSHRGRC---RYLWTL 251
Cdd:PRK09274 154 LATLLRDGAAAP-----FPMADLAPDDMAAILFTSGSTGTPKGVVYTHG--MFEAQ---IEA-LREDYGIEpgeIDLPTF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 252 PMFH----ACGwtfpwaVTAVrgthycLRKIDY-------PQ-IWKLLKQEHITHFNAAPTVNTLLCNSKEA--EPLPEP 317
Cdd:PRK09274 223 PLFAlfgpALG------MTSV------IPDMDPtrpatvdPAkLFAAIERYGVTNLFGSPALLERLGRYGEAngIKLPSL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 318 VHVTVAASPPTPHLFEQMTNLnLHP---VH-VYGMTETYgPITKgyylpawdnLPSSE---RYKKMARQGHGF-----VT 385
Cdd:PRK09274 291 RRVISAGAPVPIAVIERFRAM-LPPdaeILtPYGATEAL-PISS---------IESREilfATRAATDNGAGIcvgrpVD 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 386 SLPVRVIKTDVAEGTVID----VARDgkEIGEIVFVGNICARGYYKDPDATR--KLF--AGGVLH-SGDLAVWHADGSIQ 456
Cdd:PRK09274 360 GVEVRIIAISDAPIPEWDdalrLATG--EIGEIVVAGPMVTRSYYNRPEATRlaKIPdgQGDVWHrMGDLGYLDAQGRLW 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169764941 457 IQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHwGERPKAFVTVKPGKFLTGSEVIE 523
Cdd:PRK09274 438 FCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVPG-AQRPVLCVELEPGVACSKSALYQ 503
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
192-526 |
6.60e-13 |
|
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: 71.23 E-value: 6.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 192 LEAQAASEddVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLN---------------SHRGRCRY-LWTlPMFH 255
Cdd:cd05933 144 ISSQKPNQ--CCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRpatvgqesvvsylplSHIAAQILdIWL-PIKV 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 256 ----------ACGWTFPWAVTAVRGTHYClrkiDYPQIWKLLkQEHITHFNAAPT----------------VNTLLCNSK 309
Cdd:cd05933 221 ggqvyfaqpdALKGTLVKTLREVRPTAFM----GVPRVWEKI-QEKMKAVGAKSGtlkrkiaswakgvgleTNLKLMGGE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 310 EAEPLP---------EPV-------HVTV---AASPPTPHLFEQMTNLNLHPVHVYGMTETYGPITKgyylpawdNLPSS 370
Cdd:cd05933 296 SPSPLFyrlakklvfKKVrkalgldRCQKfftGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTI--------SNPQA 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 371 ERYKKMARQghgfVTSLPVRVIKTDvAEGtvidvardgkeIGEIVFVGNICARGYYKDPDAT-RKLFAGGVLHSGDLAVW 449
Cdd:cd05933 368 YRLLSCGKA----LPGCKTKIHNPD-ADG-----------IGEICFWGRHVFMGYLNMEDKTeEAIDEDGWLHSGDLGKL 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 450 HADGSIQIQDRAKDIII-SGGENISSVALESMLVTHPDILEAGVVAvpdshwGERPK---AFVTVK---------PGKFL 516
Cdd:cd05933 432 DEDGFLYITGRIKELIItAGGENVPPVPIEDAVKKELPIISNAMLI------GDKRKflsMLLTLKcevnpetgePLDEL 505
|
410
....*....|
gi 169764941 517 TgSEVIEWAR 526
Cdd:cd05933 506 T-EEAIEFCR 514
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
200-566 |
6.68e-13 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 71.88 E-value: 6.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 200 DDVIALAYTSGTTARPKGVEYTHR--GCYLAAMGNVIESGLNShrgrcRYLWTLPMFHACGWT----FPWAVTAVRGTHY 273
Cdd:PRK08633 782 DDTATIIFSSGSEGEPKGVMLSHHniLSNIEQISDVFNLRNDD-----VILSSLPFFHSFGLTvtlwLPLLEGIKVVYHP 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 274 clRKIDYPQIWKLLKQEHITHFNAAPTVNTLLCNSKEAEPLP-EPVHVTVAAS----PPTPHLFEQmtNLNLHPVHVYGM 348
Cdd:PRK08633 857 --DPTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMfASLRLVVAGAeklkPEVADAFEE--KFGIRILEGYGA 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 349 TETYGPITKgyylpawdNLPSSERyKKMARQ--------GHgfvtSLP---VRVIktDVAEGTVIDVARDGKeigeIVFV 417
Cdd:PRK08633 933 TETSPVASV--------NLPDVLA-ADFKRQtgskegsvGM----PLPgvaVRIV--DPETFEELPPGEDGL----ILIG 993
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 418 GNICARGYYKDPDAT----RKLFAGGVLHSGDLAVWHADGSIQIQDR----AKdiiIsGGENISSVALESMLVThpdILE 489
Cdd:PRK08633 994 GPQVMKGYLGDPEKTaeviKDIDGIGWYVTGDKGHLDEDGFLTITDRysrfAK---I-GGEMVPLGAVEEELAK---ALG 1066
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 490 AG-----VVAVPDSHWGERPKAFVTVKPGKFLTGSEVIEwarnASDISKFMIPREVEVVAELPKTSTGKVRKNILRDWAK 564
Cdd:PRK08633 1067 GEevvfaVTAVPDEKKGEKLVVLHTCGAEDVEELKRAIK----ESGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKELAL 1142
|
..
gi 169764941 565 GA 566
Cdd:PRK08633 1143 AL 1144
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
200-559 |
9.24e-13 |
|
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: 70.28 E-value: 9.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 200 DDVIALAYTSGTTARPKGVEYTHRGcylaamgnviesglnshrgrcrylwtlpMFHACGWTFP-WAVTAV-RGTHYCLRK 277
Cdd:cd17645 104 DDLAYVIYTSGSTGLPKGVMIEHHN----------------------------LVNLCEWHRPyFGVTPAdKSLVYASFS 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 278 IDyPQIWKLLkqehiTHFNAAPTVNTLLCNSK-EAEPLP---EPVHVTVAASPpTPhLFEQMTNLNLHPVHVYgmtetyg 353
Cdd:cd17645 156 FD-ASAWEIF-----PHLTAGAALHVVPSERRlDLDALNdyfNQEGITISFLP-TG-AAEQFMQLDNQSLRVL------- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 354 pITKGyylpawDNLPSSERYKKMARQGHG------FVTSLPVRVIKTDVAEGTVIDVAR-----DGKEI------GEIVF 416
Cdd:cd17645 221 -LTGG------DKLKKIERKGYKLVNNYGptentvVATSFEIDKPYANIPIGKPIDNTRvyildEALQLqpigvaGELCI 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 417 VGNICARGYYKDPDATRKLFAGG-------VLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILE 489
Cdd:cd17645 294 AGEGLARGYLNRPELTAEKFIVHpfvpgerMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIEL 373
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 490 AGVVAVPDSHWGERPKAFVTVKpgKFLTGSEVIEWARNasDISKFMIPREVEVVAELPKTSTGKVRKNIL 559
Cdd:cd17645 374 AAVLAKEDADGRKYLVAYVTAP--EEIPHEELREWLKN--DLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
38-560 |
2.58e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 70.37 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 38 AAIEPEAVAihhVTANNQVLrrTYAETADRARGLAYYLKKHGF---KRVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRL 114
Cdd:PRK12316 2013 AARAPEAIA---VVFGDQHL--SYAELDSRANRLAHRLRARGVgpeVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNY 2087
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 115 KEDDIAYIFTHSDVEAIIVDQEFLSLLqsyrasrpsiPIivdmdtdaTEGelsgpfdevvLEGLTYDLDTGAKGWP-GLE 193
Cdd:PRK12316 2088 PAERLAYMLEDSGAALLLTQRHLLERL----------PL--------PAG----------VARLPLDRDAEWADYPdTAP 2139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 194 AQAASEDDVIALAYTSGTTARPKGVEYTHrgcylAAMGNVIESGLNSHR---GRCRYLWTLPMFHAC--GWTFPWAVTA- 267
Cdd:PRK12316 2140 AVQLAGENLAYVIYTSGSTGLPKGVAVSH-----GALVAHCQAAGERYElspADCELQFMSFSFDGAheQWFHPLLNGAr 2214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 268 --VRGTHYCLRKIDYPQIwkllkQEH-ITHFNAAPTVNTLLCNSKEAEPLPEPVHVTVAASPPTPHLFEQMTNLNLHPVH 344
Cdd:PRK12316 2215 vlIRDDELWDPEQLYDEM-----ERHgVTILDFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVY 2289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 345 V---YGMTETYgpITKGYYLPAWDNlPSSERYKKMARqghgfvtslPVRVIKTDVAEGTVIDVARDGkeIGEIVFVGNIC 421
Cdd:PRK12316 2290 LfngYGPTEAV--VTPLLWKCRPQD-PCGAAYVPIGR---------ALGNRRAYILDADLNLLAPGM--AGELYLGGEGL 2355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 422 ARGYYKDPDATRKLF-------AGGVLH-SGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVV 493
Cdd:PRK12316 2356 ARGYLNRPGLTAERFvpdpfsaSGERLYrTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVV 2435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169764941 494 AVpDSHWGERPKAFVTVKPGKFLTGSEVIEWARNAsdISKFMIPREVEVVAELPKTSTGKV-RKNILR 560
Cdd:PRK12316 2436 AQ-DGASGKQLVAYVVPDDAAEDLLAELRAWLAAR--LPAYMVPAHWVVLERLPLNPNGKLdRKALPK 2500
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
207-559 |
4.81e-12 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 68.23 E-value: 4.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 207 YTSGTTARPKGVEYTHRGCYLAAMGNVIESGLNShRGRCRYLWTLPMFHACGWTFPwavTAVRGTHYCLR----KIDYPQ 282
Cdd:cd17644 113 YTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITS-SDRVLQFASIAFDVAAEEIYV---TLLSGATLVLRpeemRSSLED 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 283 IWKLLKQEHITHFNAAPTVNTLLCN--SKEAEPLPEPVHVTV----AASPPTPHLFEQMTNLNLHPVHVYGMTEtyGPIT 356
Cdd:cd17644 189 FVQYIQQWQLTVLSLPPAYWHLLVLelLLSTIDLPSSLRLVIvggeAVQPELVRQWQKNVGNFIQLINVYGPTE--ATIA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 357 KGYYLPAWDNlpsserykkmARQGHGFVTSLPVRVIKTDVAEGTVIDVARDGKeiGEIVFVGNICARGYYKDPDATRKLF 436
Cdd:cd17644 267 ATVCRLTQLT----------ERNITSVPIGRPIANTQVYILDENLQPVPVGVP--GELHIGGVGLARGYLNRPELTAEKF 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 437 AGGVLHS---------GDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAF 507
Cdd:cd17644 335 ISHPFNSseserlyktGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAY 414
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 169764941 508 VTVKPGKFLTGSEVIEWARNasDISKFMIPREVEVVAELPKTSTGKVRKNIL 559
Cdd:cd17644 415 IVPHYEESPSTVELRQFLKA--KLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
60-560 |
8.35e-12 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 68.13 E-value: 8.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 60 TYAETADRARGLAYYLKKHGF---KRVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDiaYIFTHSDVEA--IIVD 134
Cdd:PRK06060 32 THGQIHDGAARLGEVLRNRGLssgDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDD--HALAARNTEPalVVTS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 135 QEFLSLLQSYRASRPSipiivDMDTDATEgelSGPFDEVVLEGLTYDLDTgakgwpgleaqaaseddvialaYTSGTTAR 214
Cdd:PRK06060 110 DALRDRFQPSRVAEAA-----ELMSEAAR---VAPGGYEPMGGDALAYAT----------------------YTSGTTGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 215 PKGVeyTHRGC----YLAAM-GNVI-----ESGLNSHRgrcrylwtlpMFHACG-----WtFPWAVtavrgthyclrkid 279
Cdd:PRK06060 160 PKAA--IHRHAdpltFVDAMcRKALrltpeDTGLCSAR----------MYFAYGlgnsvW-FPLAT-------------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 280 ypqiwkllkqehithfNAAPTVNTLLCNSKEAEPLPEPVHVTVAASPP----------TPHLFEQMTNL-----NLHPVH 344
Cdd:PRK06060 213 ----------------GGSAVINSAPVTPEAAAILSARFGPSVLYGVPnffarvidscSPDSFRSLRCVvsageALELGL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 345 VYGMTETYGPItkgyylPAWDNLPSSErykkmarQGHGFVTS-------------LP---VRVIKTDVAegtvidVARDG 408
Cdd:PRK06060 277 AERLMEFFGGI------PILDGIGSTE-------VGQTFVSNrvdewrlgtlgrvLPpyeIRVVAPDGT------TAGPG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 409 KEiGEIVFVGNICARGYYKDPDATrkLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDIL 488
Cdd:PRK06060 338 VE-GDLWVRGPAIAKGYWNRPDSP--VANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVA 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169764941 489 EAGVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIEWARN-ASDISKFMIPREVEVVAELPKTSTGKVRKNILR 560
Cdd:PRK06060 415 EAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGlLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
38-559 |
2.63e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 66.90 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 38 AAIEPEAVAIHHvtaNNQVLrrTYAETADRARGLAYYLKKHGF---KRVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRL 114
Cdd:PRK12316 3067 VERTPDAVALAF---GEQRL--SYAELNRRANRLAHRLIERGVgpdVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEY 3141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 115 KEDDIAYIFTHSDVEaIIVDQEFLSLLQSYRASRpsipiiVDMDTDATEGELSGPFDEVVLEGLTYdldtgakgwpglea 194
Cdd:PRK12316 3142 PEERLAYMLEDSGAQ-LLLSQSHLRLPLAQGVQV------LDLDRGDENYAEANPAIRTMPENLAY-------------- 3200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 195 qaaseddviaLAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLNShrGRCRYLWTLPMFHACGWTFPWAVTAvrGTHYC 274
Cdd:PRK12316 3201 ----------VIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGV--GDRVLQFTTFSFDVFVEELFWPLMS--GARVV 3266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 275 LRKI----DYPQIWKLLKQEHITHFNAAPTVNTLLCNSKEAEPLPEpVHVTVAASPPTPHLFEQMTNLNLHPVHVYGMTE 350
Cdd:PRK12316 3267 LAGPedwrDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTS-LKRIVCGGEALPADLQQQVFAGLPLYNLYGPTE 3345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 351 TYGPITkgyylpAWDNLPSSERYKKMARqghgfvtSLPVRVIKTDVAEGTVIDVArdgkEIGEIVFVGNICARGYYKDPD 430
Cdd:PRK12316 3346 ATITVT------HWQCVEEGKDAVPIGR-------PIANRACYILDGSLEPVPVG----ALGELYLGGEGLARGYHNRPG 3408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 431 ATRKLF------AGGVLH-SGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPdshwGER 503
Cdd:PRK12316 3409 LTAERFvpdpfvPGERLYrTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVD----GRQ 3484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 169764941 504 PKAFVtVKPGKFLTGSEVIEWARNASdISKFMIPREVEVVAELPKTSTGKVRKNIL 559
Cdd:PRK12316 3485 LVAYV-VPEDEAGDLREALKAHLKAS-LPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
200-563 |
3.16e-11 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 66.07 E-value: 3.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 200 DDVIALAYTSGTTARPKGVEYThRGCYLAAMGNVIESGLNSHRGRCrYLWTLPmfhaCGW-------TF-PW----AVTA 267
Cdd:PLN02654 275 EDPLFLLYTSGSTGKPKGVLHT-TGGYMVYTATTFKYAFDYKPTDV-YWCTAD----CGWitghsyvTYgPMlngaTVLV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 268 VRGTHyclrkiDYP---QIWKLLKQEHITHFNAAPT-VNTLLCNSKEAEPLPEPVHVTVAAS---PPTPHLFEQMTNL-- 338
Cdd:PLN02654 349 FEGAP------NYPdsgRCWDIVDKYKVTIFYTAPTlVRSLMRDGDEYVTRHSRKSLRVLGSvgePINPSAWRWFFNVvg 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 339 -NLHPVH-VYGMTETYG-PITKgyyLP-AWDNLPSSERYKKMARQghgfvtslPVrviktdvaegtVIDvaRDGKEI-GE 413
Cdd:PLN02654 423 dSRCPISdTWWQTETGGfMITP---LPgAWPQKPGSATFPFFGVQ--------PV-----------IVD--EKGKEIeGE 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 414 IVfvGNICARGYYkdPDATRKLFA-------------GGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESM 480
Cdd:PLN02654 479 CS--GYLCVKKSW--PGAFRTLYGdheryettyfkpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESA 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 481 LVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKFLTG---SEVIEWARNasDISKFMIPREVEVVAELPKTSTGKVRKN 557
Cdd:PLN02654 555 LVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEelrKSLILTVRN--QIGAFAAPDKIHWAPGLPKTRSGKIMRR 632
|
....*.
gi 169764941 558 ILRDWA 563
Cdd:PLN02654 633 ILRKIA 638
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
205-560 |
3.89e-11 |
|
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: 65.47 E-value: 3.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 205 LAYTSGTTARPKGVEYTHRGcyLAAMGNVIESGLNSHRGRCRyLWTLPM----FHACgWTFPWAVTA---VRGthyclrk 277
Cdd:cd17649 99 VIYTSGSTGTPKGVAVSHGP--LAAHCQATAERYGLTPGDRE-LQFASFnfdgAHEQ-LLPPLICGAcvvLRP------- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 278 idyPQIW-------KLLKQEHITHFNAAPTVNTLLCNSKEAEP--LPEPVHVTVAASPP-TPHLFEQMTNLNLHPVHVYG 347
Cdd:cd17649 168 ---DELWasadelaEMVRELGVTVLDLPPAYLQQLAEEADRTGdgRPPSLRLYIFGGEAlSPELLRRWLKAPVRLFNAYG 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 348 MTETYgpITKGYYLP------AWDNLPSSerykkmarqghgfvTSLPVRVIKTDVAEGTVIDVARdgkeIGEIVFVGNIC 421
Cdd:cd17649 245 PTEAT--VTPLVWKCeagaarAGASMPIG--------------RPLGGRSAYILDADLNPVPVGV----TGELYIGGEGL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 422 ARGYYKDPDATRKLF-------AGGVLH-SGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVV 493
Cdd:cd17649 305 ARGYLGRPELTAERFvpdpfgaPGSRLYrTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVV 384
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169764941 494 AVPDSHwGERPKAFVTvkPGKFLTGSEVIEWARNA--SDISKFMIPREVEVVAELPKTSTGKVRKNILR 560
Cdd:cd17649 385 ALDGAG-GKQLVAYVV--LRAAAAQPELRAQLRTAlrASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
37-559 |
4.44e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 66.13 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 37 AAAIEPEAVAIHHVTaNNQVLRR-------------TYAETADRARGLAYYLKKHGF---KRVGVLCPNTPAFLESIFGI 100
Cdd:PRK12316 503 TAAEYPLQRGVHRLF-EEQVERTpeapalafgeetlDYAELNRRANRLAHALIERGVgpdVLVGVAMERSIEMVVALLAI 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 101 AAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQEFLSLLqsyrasrPSIPIIVDMDTDATEGELSGPFDEVvleglty 180
Cdd:PRK12316 582 LKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKL-------PLAAGVQVLDLDRPAAWLEGYSEEN------- 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 181 dldtgakgwPGLEAQAASEDDVIalaYTSGTTARPKGVEYTHRGC--YLAAMGNVIesGLNSHRgrcRYLWTLPM-FHAC 257
Cdd:PRK12316 648 ---------PGTELNPENLAYVI---YTSGSTGKPKGAGNRHRALsnRLCWMQQAY--GLGVGD---TVLQKTPFsFDVS 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 258 GWTFPWA-------VTAVRGTHYclrkiDYPQIWKLLKQEHITHFNAAPT-VNTLL-------CNSKEA-----EPLPEP 317
Cdd:PRK12316 711 VWEFFWPlmsgarlVVAAPGDHR-----DPAKLVELINREGVDTLHFVPSmLQAFLqdedvasCTSLRRivcsgEALPAD 785
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 318 VHVTVAASPPTPHLFeqmtNLnlhpvhvYGMTETYGPITKgyylpaWDNLPSSERYKKMARQghgfVTSLPVRVIKtdvA 397
Cdd:PRK12316 786 AQEQVFAKLPQAGLY----NL-------YGPTEAAIDVTH------WTCVEEGGDSVPIGRP----IANLACYILD---A 841
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 398 EGTVIDVArdgkEIGEIVFVGNICARGYYKDPDATRKLF------AGGVLH-SGDLAVWHADGSIQIQDRAKDIIISGGE 470
Cdd:PRK12316 842 NLEPVPVG----VLGELYLAGRGLARGYHGRPGLTAERFvpspfvAGERMYrTGDLARYRADGVIEYAGRIDHQVKLRGL 917
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 471 NISSVALESMLVTHPDILEAGVVAVPdshwGERPKAFVTVKPGKFLTGSEVIEWARnaSDISKFMIPREVEVVAELPKTS 550
Cdd:PRK12316 918 RIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVLESEGGDWREALKAHLA--ASLPEYMVPAQWLALERLPLTP 991
|
....*....
gi 169764941 551 TGKVRKNIL 559
Cdd:PRK12316 992 NGKLDRKAL 1000
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
140-553 |
4.92e-11 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 65.41 E-value: 4.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 140 LLQSYRASRPSIP-IIVDMDTDATEGeLSGPFdevvleGLTYDlDTGAKGWPGLEAQAASEDDVIALAYTSGTTARPKGV 218
Cdd:PRK09192 123 MLASAQPAAIITPdELLPWVNEATHG-NPLLH------VLSHA-WFKALPEADVALPRPTPDDIAYLQYSSGSTRFPRGV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 219 EYTHRgcylAAMGN---VIESGLNSHRG-RCrYLWtLPMFHACGWT--FPWAVTAVRGTHYcLRKIDY---PQIW-KLLK 288
Cdd:PRK09192 195 IITHR----ALMANlraISHDGLKVRPGdRC-VSW-LPFYHDMGLVgfLLTPVATQLSVDY-LPTRDFarrPLQWlDLIS 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 289 QEHIThFNAAPTVNTLLC----NSKEAEPL----------------PEPVHVTVAASPP---TPHLFeqmtnlnlhpVHV 345
Cdd:PRK09192 268 RNRGT-ISYSPPFGYELCarrvNSKDLAELdlscwrvagigadmirPDVLHQFAEAFAPagfDDKAF----------MPS 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 346 YGMTE-----TYGPITKG------------YYLPAWDNLPSSERYKKMARQGhgfvTSLPvrviktdvaeGTVIDV-ARD 407
Cdd:PRK09192 337 YGLAEatlavSFSPLGSGivveevdrdrleYQGKAVAPGAETRRVRTFVNCG----KALP----------GHEIEIrNEA 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 408 GKEIGEIVfVGNICARG------YYKDPDATRKLFAGGVLHSGDLAvWHADGSIQIQDRAKDIIISGGENISSVALESML 481
Cdd:PRK09192 403 GMPLPERV-VGHICVRGpslmsgYFRDEESQDVLAADGWLDTGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEWIA 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 482 VTHPDILEAGVVA-VPDSHWGERPKAFVTVKpgkfltGSEVIEWARNASDI-SKFMIPREVEVVAEL------PKTSTGK 553
Cdd:PRK09192 481 EQEPELRSGDAAAfSIAQENGEKIVLLVQCR------ISDEERRGQLIHALaALVRSEFGVEAAVELvpphslPRTSSGK 554
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
200-495 |
5.24e-11 |
|
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: 64.79 E-value: 5.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 200 DDVIALAYTSGTTARPKGVEYTHRgcYLAAMGNVIESGLNSHRGRcRYLWTLPMFHACGWTFPWAVTAVRGTHYCLRKID 279
Cdd:cd05910 85 DEPAAILFTSGSTGTPKGVVYRHG--TFAAQIDALRQLYGIRPGE-VDLATFPLFALFGPALGLTSVIPDMDPTRPARAD 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 280 YPQIWKLLKQEHITHFNAAPTVNTLLCNSKEAE--PLPEPVHVTVAASPPTPHLFEQMTNLnLHP----VHVYGMTETYg 353
Cdd:cd05910 162 PQKLVGAIRQYGVSIVFGSPALLERVARYCAQHgiTLPSLRRVLSAGAPVPIALAARLRKM-LSDeaeiLTPYGATEAL- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 354 PITkgyyLPAWDNLPSSERykKMARQGHGFVTSLPV-----RVIKTDVAEGTVIDVAR--DGKEIGEIVFVGNICARGYY 426
Cdd:cd05910 240 PVS----SIGSRELLATTT--AATSGGAGTCVGRPIpgvrvRIIEIDDEPIAEWDDTLelPRGEIGEITVTGPTVTPTYV 313
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169764941 427 KDPDATR--KL--FAGGVLH-SGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAV 495
Cdd:cd05910 314 NRPVATAlaKIddNSEGFWHrMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV 387
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
411-563 |
6.24e-11 |
|
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: 64.87 E-value: 6.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 411 IGEIVFVGNICARGYYKDPDATRKLF--------------AGGVLHSGDLAVWHADGSIQIQDRaKD--IIISG-----G 469
Cdd:cd05918 293 VGELLIEGPILARGYLNDPEKTAAAFiedpawlkqegsgrGRRLYRTGDLVRYNPDGSLEYVGR-KDtqVKIRGqrvelG 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 470 EnISSVALESMlvthPDILEAGVVAVPDSHWGERPK--AFVTVKP-------GKFLTGSEVIEWARNASDIS-------- 532
Cdd:cd05918 372 E-IEHHLRQSL----PGAKEVVVEVVKPKDGSSSPQlvAFVVLDGsssgsgdGDSLFLEPSDEFRALVAELRsklrqrlp 446
|
170 180 190
....*....|....*....|....*....|.
gi 169764941 533 KFMIPREVEVVAELPKTSTGKVRKNILRDWA 563
Cdd:cd05918 447 SYMVPSVFLPLSHLPLTASGKIDRRALRELA 477
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
166-556 |
6.84e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 64.63 E-value: 6.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 166 LSGPFDEV--VLEGLTYDLDTGAKGWPGLEAQ--AASEDDVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLNSH 241
Cdd:PRK07768 114 VGEPFLAAapVLEEKGIRVLTVADLLAADPIDpvETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 242 RGRCrYLWtLPMFHACG----WTFP--WAVTAVRGThyclrKIDY---PQIWKLLKQEHITHFNAAPT------------ 300
Cdd:PRK07768 194 TDVM-VSW-LPLFHDMGmvgfLTVPmyFGAELVKVT-----PMDFlrdPLLWAELISKYRGTMTAAPNfayallarrlrr 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 301 --------VNTLLCNSKEAEPL-PEPVHVTVAASPPtphlfeqmtnLNLHP---VHVYGMTET-----YGPITKGYYLPA 363
Cdd:PRK07768 267 qakpgafdLSSLRFALNGAEPIdPADVEDLLDAGAR----------FGLRPeaiLPAYGMAEAtlavsFSPCGAGLVVDE 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 364 WD-NLPSSERYKKMARQGHG--FVT------SLPVRVIKTDvaeGTVIDvARdgkEIGEIVFVGNICARGYyKDPDATRK 434
Cdd:PRK07768 337 VDaDLLAALRRAVPATKGNTrrLATlgpplpGLEVRVVDED---GQVLP-PR---GVGVIELRGESVTPGY-LTMDGFIP 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 435 LF-AGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAV--PDSHWGER------PK 505
Cdd:PRK07768 409 AQdADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVrlDAGHSREGfavaveSN 488
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 169764941 506 AFVTVKPGKFLTgSEVIEWARNASDISkfmiPREVEVVA--ELPKTSTGKVRK 556
Cdd:PRK07768 489 AFEDPAEVRRIR-HQVAHEVVAEVGVR----PRNVVVLGpgSIPKTPSGKLRR 536
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
59-500 |
1.12e-10 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 64.27 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 59 RTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQ 135
Cdd:PLN02614 80 QTYQEVYDIVIKLGNSLRSVGVKdeaKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 136 EFLS-LLQSYRASRPSIPIIVDMD----TDATEGELSG----PFDEVVL--EGLTYDLDTGAKgwpgleaqaaseDDVIA 204
Cdd:PLN02614 160 KKISeLFKTCPNSTEYMKTVVSFGgvsrEQKEEAETFGlviyAWDEFLKlgEGKQYDLPIKKK------------SDICT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 205 LAYTSGTTARPKGVEYTHRGCYLAAMG--NVIESGLNSHRGRCRYLWTLPMFHA-------CGWTFPWAVTAVRG----- 270
Cdd:PLN02614 228 IMYTSGTTGDPKGVMISNESIVTLIAGviRLLKSANAALTVKDVYLSYLPLAHIfdrvieeCFIQHGAAIGFWRGdvkll 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 271 ---------THYCL--RKID--YPQIWKLLK---------------------QEHITHFNAAPTVNTLLCNsKEAEPLPE 316
Cdd:PLN02614 308 iedlgelkpTIFCAvpRVLDrvYSGLQKKLSdggflkkfvfdsafsykfgnmKKGQSHVEASPLCDKLVFN-KVKQGLGG 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 317 PVHVTVAASPPTPHLFEQMTNL--NLHPVHVYGMTETygpiTKGYYLPAWDNLpsserykkmarqghGFVTSLPVRVIKT 394
Cdd:PLN02614 387 NVRIILSGAAPLASHVESFLRVvaCCHVLQGYGLTES----CAGTFVSLPDEL--------------DMLGTVGPPVPNV 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 395 DVAEGTVIDVARDG---KEIGEIVFVGNICARGYYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDII-ISGGE 470
Cdd:PLN02614 449 DIRLESVPEMEYDAlasTPRGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFkLSQGE 528
|
490 500 510
....*....|....*....|....*....|
gi 169764941 471 NISSVALESMLvthpdileaGVVAVPDSHW 500
Cdd:PLN02614 529 YVAVENIENIY---------GEVQAVDSVW 549
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
114-495 |
1.23e-10 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 64.35 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 114 LKEDDIAYIFTHSDVEAIIVDQEFLSLLQSYRASRPSIPIIVDMDTDatEGELSGPFDEVVLEGLTYDldtgakgwpGLE 193
Cdd:PLN02736 137 LGPDAVKFIVNHAEVAAIFCVPQTLNTLLSCLSEIPSVRLIVVVGGA--DEPLPSLPSGTGVEIVTYS---------KLL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 194 AQAAS---------EDDVIALAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLNSHRgrcRYLWTLPMFHA-------- 256
Cdd:PLN02736 206 AQGRSspqpfrppkPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSD---VHISYLPLAHIyervnqiv 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 257 ---CGWTFPW----------AVTAVRGTHYClrkiDYPQIW-------------------KLL-------KQEHITHFNA 297
Cdd:PLN02736 283 mlhYGVAVGFyqgdnlklmdDLAALRPTIFC----SVPRLYnriydgitnavkesgglkeRLFnaaynakKQALENGKNP 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 298 APTVNTLLCNSKEAEPLPEPVHVTVAASPPTPhlfEQMTNLNL----HPVHVYGMTETYGPITKgyyLPAWDNLpssery 373
Cdd:PLN02736 359 SPMWDRLVFNKIKAKLGGRVRFMSSGASPLSP---DVMEFLRIcfggRVLEGYGMTETSCVISG---MDEGDNL------ 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 374 kkmarQGHgfVTS-LPVRVIK-TDVAEgtvIDVARDGKEI--GEIVFVGNICARGYYKDPDATRKLF-AGGVLHSGDLAV 448
Cdd:PLN02736 427 -----SGH--VGSpNPACEVKlVDVPE---MNYTSEDQPYprGEICVRGPIIFKGYYKDEVQTREVIdEDGWLHTGDIGL 496
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 169764941 449 WHADGSIQIQDRAKDII-ISGG-----ENISSVALESMLVT----HPDILEAGVVAV 495
Cdd:PLN02736 497 WLPGGRLKIIDRKKNIFkLAQGeyiapEKIENVYAKCKFVAqcfvYGDSLNSSLVAV 553
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
408-508 |
3.08e-10 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 62.58 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 408 GKEI----GEIVFVGNICARGYYKDpdatRKLF----AGGVLHSGDLAVWHaDGSIQIQDRAKDIIISGGENISSVALES 479
Cdd:PRK09029 297 GREVklvdGEIWLRGASLALGYWRQ----GQLVplvnDEGWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIER 371
|
90 100
....*....|....*....|....*....
gi 169764941 480 MLVTHPDILEAGVVAVPDSHWGERPKAFV 508
Cdd:PRK09029 372 VINQHPLVQQVFVVPVADAEFGQRPVAVV 400
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
444-566 |
3.60e-10 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 63.06 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 444 GDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVT-HPDILEAgVVAVPDSHWGERpkaFVTVKPGKFLTGSEVI 522
Cdd:PRK06814 1015 GDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAElWPDALHA-AVSIPDARKGER---IILLTTASDATRAAFL 1090
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 169764941 523 EWARNAsDISKFMIPREVEVVAELPKTSTGKVRKNILRDWAKGA 566
Cdd:PRK06814 1091 AHAKAA-GASELMVPAEIITIDEIPLLGTGKIDYVAVTKLAEEA 1133
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
283-559 |
5.36e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 62.07 E-value: 5.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 283 IWKLLKQEHITHFNAAP-TVNTLLCNSKEAE------PLPEPVHVTVAASPPTPHLFEQMTN-LNLHPVHVYGMTET--- 351
Cdd:PTZ00237 341 LWNTIEKHKVTHTLTLPkTIRYLIKTDPEATiirskyDLSNLKEIWCGGEVIEESIPEYIENkLKIKSSRGYGQTEIgit 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 352 ----YGPITKGYYlpawdnlpsserykkmarqghgfVTSLPVRVIKTDVaegtvidVARDGKE-----IGEIVF---VGN 419
Cdd:PTZ00237 421 ylycYGHINIPYN-----------------------ATGVPSIFIKPSI-------LSEDGKElnvneIGEVAFklpMPP 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 420 ICARGYYKDPDATRKLFAG--GVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPD 497
Cdd:PTZ00237 471 SFATTFYKNDEKFKQLFSKfpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYD 550
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169764941 498 SHWGERPKAFVTVKPGKFLTGSEVIEWARN-----ASDISKFMIPREVEVVAELPKTSTGKVRKNIL 559
Cdd:PTZ00237 551 PDCYNVPIGLLVLKQDQSNQSIDLNKLKNEinniiTQDIESLAVLRKIIIVNQLPKTKTGKIPRQII 617
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
192-560 |
9.31e-10 |
|
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: 60.97 E-value: 9.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 192 LEAQAASEDDVIALAYTSGTTARPKGVEYTHRGCY--LAAMGNVIESGLNShrgrcRYLWTLPMFHACGWTFPWAVTAVR 269
Cdd:cd05908 98 EEVLCELADELAFIQFSSGSTGDPKGVMLTHENLVhnMFAILNSTEWKTKD-----RILSWMPLTHDMGLIAFHLAPLIA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 270 G-THYCLRK---IDYPQIWklLKQ--EHITHFNAAPT------VNTLLCNSKEAEPLPEPVHVTVAASPPTP----HLFE 333
Cdd:cd05908 173 GmNQYLMPTrlfIRRPILW--LKKasEHKATIVSSPNfgykyfLKTLKPEKANDWDLSSIRMILNGAEPIDYelchEFLD 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 334 QMTNLNLHP---VHVYGMTETygpiTKGYYLPawdnlPSSERYKKMARQGHGFVTSLPVR-VIKTDVAEGTVIDVardGK 409
Cdd:cd05908 251 HMSKYGLKRnaiLPVYGLAEA----SVGASLP-----KAQSPFKTITLGRRHVTHGEPEPeVDKKDSECLTFVEV---GK 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 410 EIGE----IV----------FVGNICARG------YYKDPDATRKLF-AGGVLHSGDLAVWHaDGSIQIQDRAKDIIISG 468
Cdd:cd05908 319 PIDEtdirICdednkilpdgYIGHIQIRGknvtpgYYNNPEATAKVFtDDGWLKTGDLGFIR-NGRLVITGREKDIIFVN 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 469 GENISSVALESMLVTHPDILEAGVVA--VPDSHWGERpKAFVTVKPGKfltgsEVIEWARNASDISKFMIPR------EV 540
Cdd:cd05908 398 GQNVYPHDIERIAEELEGVELGRVVAcgVNNSNTRNE-EIFCFIEHRK-----SEDDFYPLGKKIKKHLNKRggwqinEV 471
|
410 420
....*....|....*....|
gi 169764941 541 EVVAELPKTSTGKVRKNILR 560
Cdd:cd05908 472 LPIRRIPKTTSGKVKRYELA 491
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
441-556 |
2.35e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 59.66 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 441 LHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPGkfLTGSE 520
Cdd:PRK08308 293 IFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEE--IDPVQ 370
|
90 100 110
....*....|....*....|....*....|....*..
gi 169764941 521 VIEWARnaSDISKFMIPREVEVVAELPKTSTGKV-RK 556
Cdd:PRK08308 371 LREWCI--QHLAPYQVPHEIESVTEIPKNANGKVsRK 405
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
412-487 |
2.38e-09 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 60.24 E-value: 2.38e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169764941 412 GEIVFVGNICARGYYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDII-ISGGENISSVALESMLVTHPDI 487
Cdd:PLN02861 466 GEICLRGNTLFSGYHKRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLI 542
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
346-485 |
5.61e-09 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 59.06 E-value: 5.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 346 YGMTETYGPITKGYylpawdnlPSserykKMARQGhgfvtSLPVRVIKTDVAEGTVIDVARD---GKEIGEIVFVGNICA 422
Cdd:PLN02430 415 YGLTETLGPTTLGF--------PD-----EMCMLG-----TVGAPAVYNELRLEEVPEMGYDplgEPPRGEICVRGKCLF 476
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169764941 423 RGYYKDPDATRKLFAGGVLHSGDLAVWHADGSIQIQDRAKDII-ISGGENISSVALESMLVTHP 485
Cdd:PLN02430 477 SGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEYLENVYGQNP 540
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
60-556 |
1.34e-08 |
|
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: 57.69 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 60 TYAETADRARGLAYYLKKHGFKR----VGVLCPNTPAFLESIFGIAAAGAVNVAVNYRLKEDDIAYIFTHSDVEAIIVDQ 135
Cdd:cd05938 7 TYRDVDRRSNQAARALLAHAGLRpgdtVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 136 EFLSLLQsyrasrpsiPIIVDMDTDATEGELSGPfdEVVLEGLTYDLDtgakgwpglEAQAASEDDVIALA--------- 206
Cdd:cd05938 87 ELQEAVE---------EVLPALRADGVSVWYLSH--TSNTEGVISLLD---------KVDAASDEPVPASLrahvtiksp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 207 ----YTSGTTARPKGVEYTHRGCyLAAMGNVIESGLNSHrgRCRYLwTLPMFHACGwtfpwavtAVRGTHYCL------- 275
Cdd:cd05938 147 alyiYTSGTTGLPKAARISHLRV-LQCSGFLSLCGVTAD--DVIYI-TLPLYHSSG--------FLLGIGGCIelgatcv 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 276 --RKIDYPQIWKLLKQEHITHFNAAPTVNTLLCNSKEAeplPEPVHVTV---AASPPTPHLFEQMTNL--NLHPVHVYGM 348
Cdd:cd05938 215 lkPKFSASQFWDDCRKHNVTVIQYIGELLRYLCNQPQS---PNDRDHKVrlaIGNGLRADVWREFLRRfgPIRIREFYGS 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 349 TE----------TYGPITKGYYLpawdnlpsserYKKMarqghgfvtsLPVRVIKTDV--------AEGTVIDVARDgkE 410
Cdd:cd05938 292 TEgnigffnytgKIGAVGRVSYL-----------YKLL----------FPFELIKFDVekeepvrdAQGFCIPVAKG--E 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 411 IGEIV--------FVgnicarGYYKDPDAT-RKLFA-----GGV-LHSGDLAVWHADGSIQIQDRAKDIIISGGENISSV 475
Cdd:cd05938 349 PGLLVakitqqspFL------GYAGDKEQTeKKLLRdvfkkGDVyFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATT 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 476 ALESMLVTHPDILEAGV--VAVPDsHWGERPKAFVTVKPGKFLTGSEVIEWARNAsdISKFMIPREVEVVAELPKTSTGK 553
Cdd:cd05938 423 EVADVLGLLDFLQEVNVygVTVPG-HEGRIGMAAVKLKPGHEFDGKKLYQHVREY--LPAYARPRFLRIQDSLEITGTFK 499
|
...
gi 169764941 554 VRK 556
Cdd:cd05938 500 QQK 502
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
196-554 |
1.51e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 57.43 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 196 AASEDDVIALAYTSGTTARPKGVEYTHRgcylAAMGNVIE--SGLNSHRGRCRYLWtLPMFHACGW---TFPwavtAVRG 270
Cdd:PRK07769 176 EANEDTIAYLQYTSGSTRIPAGVQITHL----NLPTNVLQviDALEGQEGDRGVSW-LPFFHDMGLitvLLP----ALLG 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 271 THYCLRK----IDYPQIW--KLLKQEHITH--FNAAPTVNTLLCNS----KEAEPL------------PEPvhVTVAAsp 326
Cdd:PRK07769 247 HYITFMSpaafVRRPGRWirELARKPGGTGgtFSAAPNFAFEHAAArglpKDGEPPldlsnvkgllngSEP--VSPAS-- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 327 pTPHLFEQMTNLNLHPVHV---YGMTETygpiTKGYYLPAWDNLPS----------SERYKKMARQGHGFVTSlpVRVIK 393
Cdd:PRK07769 323 -MRKFNEAFAPYGLPPTAIkpsYGMAEA----TLFVSTTPMDEEPTviyvdrdelnAGRFVEVPADAPNAVAQ--VSAGK 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 394 TDVAEGTVIDVARDGKE-----IGEIVFVGNICARGYYKDPDATRKLF------------AGGV------LHSGDLAVWH 450
Cdd:PRK07769 396 VGVSEWAVIVDPETASElpdgqIGEIWLHGNNIGTGYWGKPEETAATFqnilksrlseshAEGApddalwVRTGDYGVYF 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 451 aDGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVA---VP----------DSHWG------ERPKAFVTV- 510
Cdd:PRK07769 476 -DGELYITGRVKDLVIIDGRNHYPQDLEYTAQEATKALRTGYVAafsVPanqlpqvvfdDSHAGlkfdpeDTSEQLVIVa 554
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 169764941 511 --KPG-KFLTGSEVIEWARNASDISKFMIPREVEVVA--ELPKTSTGKV 554
Cdd:PRK07769 555 erAPGaHKLDPQPIADDIRAAIAVRHGVTVRDVLLVPagSIPRTSSGKI 603
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
114-492 |
3.42e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 56.52 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 114 LKEDDIAYIFTHSDVEAIIVDQE----FLSLLQSYRASRPSIpIIVD---MDTDATEGELSgPFDEVVLEGLTYDLDTGA 186
Cdd:PTZ00216 180 LGEDALAYALRETECKAIVCNGKnvpnLLRLMKSGGMPNTTI-IYLDslpASVDTEGCRLV-AWTDVVAKGHSAGSHHPL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 187 KGwpgleaqAASEDDVIALAYTSGTTARPKGVEYTHRGCY--LAAMGNVIESGLNSHRGRCRYLWTLPMFHacgwTFPWA 264
Cdd:PTZ00216 258 NI-------PENNDDLALIMYTSGTTGDPKGVMHTHGSLTagILALEDRLNDLIGPPEEDETYCSYLPLAH----IMEFG 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 265 VTAV---RGTHYC-----------------LRK------IDYPQIWKLLK---QEHIthfnaaPTVNTL----------- 304
Cdd:PTZ00216 327 VTNIflaRGALIGfgsprtltdtfarphgdLTEfrpvflIGVPRIFDTIKkavEAKL------PPVGSLkrrvfdhayqs 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 305 ----LCNSKEAEPLPEPVHVTVAA----------------SPPTphlfEQMTNLNLHPV-HVYGMTETY--GPItkgyyl 361
Cdd:PTZ00216 401 rlraLKEGKDTPYWNEKVFSAPRAvlggrvramlsgggplSAAT----QEFVNVVFGMViQGWGLTETVccGGI------ 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 362 pawdnlpsserykkmarQGHGFVTSLPV-RVIKTdvAEGTVIDVAR----DGKEI-GEIVFVGNICARGYYKDPDATRK- 434
Cdd:PTZ00216 471 -----------------QRTGDLEPNAVgQLLKG--VEMKLLDTEEykhtDTPEPrGEILLRGPFLFKGYYKQEELTREv 531
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169764941 435 LFAGGVLHSGDLAVWHADGSIQIQDR----AKDIIisgGENISSVALESMLVTHPDILEAGV 492
Cdd:PTZ00216 532 LDEDGWFHTGDVGSIAANGTLRIIGRvkalAKNCL---GEYIALEALEALYGQNELVVPNGV 590
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
183-554 |
6.27e-08 |
|
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: 55.10 E-value: 6.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 183 DTGAKGwpgleaQAASEDDVIALAYTSGTTARPKGVEYTHRGCylaamgnviesgLNSHRGRC-RYLWTLPMFHA----C 257
Cdd:cd17648 83 DTGARV------VITNSTDLAYAIYTSGTTGKPKGVLVEHGSV------------VNLRTSLSeRYFGRDNGDEAvlffS 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 258 GWTFPWAVT----AVRGTHYCL-----RKIDYPQIWKLLKQEHITHFNAAPTVNTLLcnskEAEPLPEPVHVTVAASPPT 328
Cdd:cd17648 145 NYVFDFFVEqmtlALLNGQKLVvppdeMRFDPDRFYAYINREKVTYLSGTPSVLQQY----DLARLPHLKRVDAAGEEFT 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 329 PHLFEQMTNLNLHP-VHVYGMTETYGPITKGYYlpawdnlPSSERYKKMARQghgfvtslPVRVIKTDVAEGTVIDVARD 407
Cdd:cd17648 221 APVFEKLRSRFAGLiINAYGPTETTVTNHKRFF-------PGDQRFDKSLGR--------PVRNTKCYVLNDAMKRVPVG 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 408 GkeIGEIvFVGNIC-ARGYYKDPDATRKLF-----------AGGV----LHSGDLAVWHADGSIQIQDRAKDIIISGGEN 471
Cdd:cd17648 286 A--VGEL-YLGGDGvARGYLNRPELTAERFlpnpfqteqerARGRnarlYKTGDLVRWLPSGELEYLGRNDFQVKIRGQR 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 472 ISSVALESMLVTHPDILEAGVVA--VPDSHWGERPKAFVtvkpGKFLTGSEVIEwarnASDISKF--------MIPREVE 541
Cdd:cd17648 363 IEPGEVEAALASYPGVRECAVVAkeDASQAQSRIQKYLV----GYYLPEPGHVP----ESDLLSFlraklpryMVPARLV 434
|
410
....*....|...
gi 169764941 542 VVAELPKTSTGKV 554
Cdd:cd17648 435 RLEGIPVTINGKL 447
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
403-556 |
3.77e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 52.85 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 403 DVARDGKEIGEIVFVGNICARGYYKDPdatrKLFAGGVLHSGDLAvWHADGSIQIQDRAKDIIISGGENISSVALESMLV 482
Cdd:PRK05851 364 AAGVAGREIGEIEIRGASMMSGYLGQA----PIDPDDWFPTGDLG-YLVDGGLVVCGRAKELITVAGRNIFPTEIERVAA 438
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169764941 483 THPDILEAGVVAVPDSHWGERPKAFVTVK---PGKFLTGSEVIEwaRNASDISkfMIPREVEVVA--ELPKTSTGKVRK 556
Cdd:PRK05851 439 QVRGVREGAVVAVGTGEGSARPGLVIAAEfrgPDEAGARSEVVQ--RVASECG--VVPSDVVFVApgSLPRTSSGKLRR 513
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
120-559 |
5.78e-07 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 52.20 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 120 AYI--FTHSDVEAI--IVDqeflsllqsyrASRPSIPI-IVDMDTDATEGELsgpfdeVVLEGLTydlDTGAKGWPGLEA 194
Cdd:PRK04813 78 AYIpvDVSSPAERIemIIE-----------VAKPSLIIaTEELPLEILGIPV------ITLDELK---DIFATGNPYDFD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 195 QAASEDDVIALAYTSGTTARPKGVEYTHRGcyLAAMGNVIESgLNSHRGRCRYLWTLPmfhacgWTFPWAVTAVR----- 269
Cdd:PRK04813 138 HAVKGDDNYYIIFTSGTTGKPKGVQISHDN--LVSFTNWMLE-DFALPEGPQFLNQAP------YSFDLSVMDLYptlas 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 270 -GTHYCLRK--IDYP-QIWKLLKQehiTHFNAapTVNT-------LLCNSKEAEPLPEPVH---------VTVAASpptp 329
Cdd:PRK04813 209 gGTLVALPKdmTANFkQLFETLPQ---LPINV--WVSTpsfadmcLLDPSFNEEHLPNLTHflfcgeelpHKTAKK---- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 330 hLFEQMTnlNLHPVHVYGMTETYGPITkgyylpawdnlpSSERYKKMARQghgfVTSLPVRVIKTDVaEGTVID----VA 405
Cdd:PRK04813 280 -LLERFP--SATIYNTYGPTEATVAVT------------SIEITDEMLDQ----YKRLPIGYAKPDS-PLLIIDeegtKL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 406 RDGKEiGEIVFVGNICARGYYKDPDATRKLF---AG-GVLHSGDLAVWhADGSIQIQDRAKDIIISGGENISSVALESML 481
Cdd:PRK04813 340 PDGEQ-GEIVISGPSVSKGYLNNPEKTAEAFftfDGqPAYHTGDAGYL-EDGLLFYQGRIDFQIKLNGYRIELEEIEQNL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 482 VTHPDILEAGVVAVPDSHWGERPKAFVTVKPGKF---LTGSEVIEwARNASDISKFMIPREVEVVAELPKTSTGKV-RKN 557
Cdd:PRK04813 418 RQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFereFELTKAIK-KELKERLMEYMIPRKFIYRDSLPLTPNGKIdRKA 496
|
..
gi 169764941 558 IL 559
Cdd:PRK04813 497 LI 498
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
200-554 |
6.71e-07 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 52.05 E-value: 6.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 200 DDVIALAYTSGTTARPKGVEYTHRgcylAAMGNVIE---SGLNSHRGRCRYLWtLPMFHACGWT---FPwavtAVRGTHY 273
Cdd:PRK12476 193 DDVSHLQYTSGSTRPPVGVEITHR----AVGTNLVQmilSIDLLDRNTHGVSW-LPLYHDMGLSmigFP----AVYGGHS 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 274 CLRK----IDYPQIW-KLLKQEHITH--FNAAPTVNTLLCNSKeaePLPEP--------VHVTVAASPPTPHLFEQMTN- 337
Cdd:PRK12476 264 TLMSptafVRRPQRWiKALSEGSRTGrvVTAAPNFAYEWAAQR---GLPAEgddidlsnVVLIIGSEPVSIDAVTTFNKa 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 338 ---LNLHPVHV---YGMTE------TYGP-------------ITKGYYLPAWDNLPSSerykkMARQGHGFVTSLPVRVI 392
Cdd:PRK12476 341 fapYGLPRTAFkpsYGIAEatlfvaTIAPdaepsvvyldreqLGAGRAVRVAADAPNA-----VAHVSCGQVARSQWAVI 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 393 KTDVAEgtviDVARDGkEIGEIVFVGNICARGYYKDPDATRKLF-------------AGGV------LHSGDLAVWhADG 453
Cdd:PRK12476 416 VDPDTG----AELPDG-EVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegshADGAaddgtwLRTGDLGVY-LDG 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 454 SIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVA---VPdshwGERPKAFVTVKPGKFLTG----SEVIEWAR 526
Cdd:PRK12476 490 ELYITGRIADLIVIDGRNHYPQDIEATVAEASPMVRRGYVTaftVP----AEDNERLVIVAERAAGTSradpAPAIDAIR 565
|
410 420 430
....*....|....*....|....*....|
gi 169764941 527 NASDISKFMIPREVEVVAE--LPKTSTGKV 554
Cdd:PRK12476 566 AAVSRRHGLAVADVRLVPAgaIPRTTSGKL 595
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
119-487 |
6.83e-07 |
|
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: 52.07 E-value: 6.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 119 IAYIFTHSDVEAIIVDQEFLSLLQSYRASRPSIPIIVDMD----TDATEGELSGPFDEVVLEGLTYDLDT-----GAKGW 189
Cdd:cd17632 132 LAPILAETEPRLLAVSAEHLDLAVEAVLEGGTPPRLVVFDhrpeVDAHRAALESARERLAAVGIPVTTLTliavrGRDLP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 190 PGLEAQAASEDDVIA-LAYTSGTTARPKGVEYTHRGCYLAAMGNVIESGLNSHRGRCryLWTLPMFHACGWTFPWAVTAV 268
Cdd:cd17632 212 PAPLFRPEPDDDPLAlLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASIT--LNFMPMSHIAGRISLYGTLAR 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 269 RGTHYCLRKIDY------------------PQIWKLLKQEHIThfnaapTVNTLLCNSKEAEPLPEPVHV---------- 320
Cdd:cd17632 290 GGTAYFAAASDMstlfddlalvrptelflvPRVCDMLFQRYQA------ELDRRSVAGADAETLAERVKAelrervlggr 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 321 ---TVAASPPtphLFEQMTN-----LNLHPVHVYGMTETYGPITKGyylpawdnlpsserykkmarqghgfvtslpvRVI 392
Cdd:cd17632 364 llaAVCGSAP---LSAEMKAfmeslLDLDLHDGYGSTEAGAVILDG-------------------------------VIV 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 393 KTDVAEGTVIDVARDG-------KEIGEIVFVGNICARGYYKDPDATRKLF-AGGVLHSGDLAVWHADGSIQIQDRAKDI 464
Cdd:cd17632 410 RPPVLDYKLVDVPELGyfrtdrpHPRGELLVKTDTLFPGYYKRPEVTAEVFdEDGFYRTGDVMAELGPDRLVYVDRRNNV 489
|
410 420
....*....|....*....|....
gi 169764941 465 I-ISGGENISSVALESMLVTHPDI 487
Cdd:cd17632 490 LkLSQGEFVTVARLEAVFAASPLV 513
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
34-560 |
1.03e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 52.09 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 34 LPRAAAIEPEAVAIHHVT-ANNQVLRRTYAETADRARGLAYYLKKHGF--KRVGVLCPNTPAFLESIFG-----IAAAGA 105
Cdd:PRK05691 15 LQRRAAQTPDRLALRFLAdDPGEGVVLSYRDLDLRARTIAAALQARASfgDRAVLLFPSGPDYVAAFFGclyagVIAVPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 106 VNVAVNYRLKEDDIAYIFTHSDVEAIIVDQEFL-SLLQSYRASRPSIPIIVDMDTdategelsgpfdevvlegltydLDT 184
Cdd:PRK05691 95 YPPESARRHHQERLLSIIADAEPRLLLTVADLRdSLLQMEELAAANAPELLCVDT----------------------LDP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 185 G-AKGWPGLEAQAaseDDVIALAYTSGTTARPKGVEYTHRGcyLAAMGNVIESGLNSHRGRCRYL--WtLPMFHACGWT- 260
Cdd:PRK05691 153 AlAEAWQEPALQP---DDIAFLQYTSGSTALPKGVQVSHGN--LVANEQLIRHGFGIDLNPDDVIvsW-LPLYHDMGLIg 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 261 ------FPWAVTAVRGTHYCLRKidyPQIWkllkQEHITHF----NAAPTVNTLLCNSKEAEPLPEPVHVT---VAASPP 327
Cdd:PRK05691 227 gllqpiFSGVPCVLMSPAYFLER---PLRW----LEAISEYggtiSGGPDFAYRLCSERVSESALERLDLSrwrVAYSGS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 328 TP------HLF-EQMTNLNLHP---VHVYGMTETYGPIT---KGYYLPAWDnLPSSERYKKMARQGHGFV-----TSLPV 389
Cdd:PRK05691 300 EPirqdslERFaEKFAACGFDPdsfFASYGLAEATLFVSggrRGQGIPALE-LDAEALARNRAEPGTGSVlmscgRSQPG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 390 RVIKtdVAEGTVIDVARDGKeIGEIVFVGNICARGYYKDPDATRKLF---AGGV-LHSGDLAvWHADGSIQIQDRAKDII 465
Cdd:PRK05691 379 HAVL--IVDPQSLEVLGDNR-VGEIWASGPSIAHGYWRNPEASAKTFvehDGRTwLRTGDLG-FLRDGELFVTGRLKDML 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 466 ISGGENISSVALESMLVTHPDILEAGVVAV-PDSHWGERP---KAFVTVKPGKFLTGSEVIEWARNASDISKFMIPREVE 541
Cdd:PRK05691 455 IVRGHNLYPQDIEKTVEREVEVVRKGRVAAfAVNHQGEEGigiAAEISRSVQKILPPQALIKSIRQAVAEACQEAPSVVL 534
|
570 580
....*....|....*....|.
gi 169764941 542 VV--AELPKTSTGKVRKNILR 560
Cdd:PRK05691 535 LLnpGALPKTSSGKLQRSACR 555
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
15-553 |
1.05e-06 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 51.50 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 15 FVPGAeqRVNF--HTLSPTSflpraaaiEPEAVAIHHVTaNNQVLRRTYAETADRARGLAYYLKKHGFK---RVGVLCPN 89
Cdd:cd05943 64 WFPGA--RLNYaeNLLRHAD--------ADDPAAIYAAE-DGERTEVTWAELRRRVARLAAALRALGVKpgdRVAGYLPN 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 90 TP----AFL--ESI----------FGIAAAGAvnvavnyRLKEDDIAYIFThsdVEAIIVDQEFLSLLQSYRASRPSIP- 152
Cdd:cd05943 133 IPeavvAMLatASIgaiwsscspdFGVPGVLD-------RFGQIEPKVLFA---VDAYTYNGKRHDVREKVAELVKGLPs 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 153 ----IIVDMDTDATEGELSGPFDEVVLEGLtydLDTGAKGWPGLEAqaASEDDVIALAYTSGTTARPKGVEYTHRGCYLA 228
Cdd:cd05943 203 llavVVVPYTVAAGQPDLSKIAKALTLEDF---LATGAAGELEFEP--LPFDHPLYILYSSGTTGLPKCIVHGAGGTLLQ 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 229 AMGNVIESGlNSHRGRcRYLWtlpmFHACGWT-FPWAVTAV-RGTHYCLrkID----YPQ---IWKLLKQEHITHFNAAP 299
Cdd:cd05943 278 HLKEHILHC-DLRPGD-RLFY----YTTCGWMmWNWLVSGLaVGATIVL--YDgspfYPDtnaLWDLADEEGITVFGTSA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 300 TvntLLCNSKEAEplpepvhvtvaASPPTPHlfeqmtnlNLHPVHVygMTETYGPITKGYYLPAWDNLPSSERYKKMARQ 379
Cdd:cd05943 350 K---YLDALEKAG-----------LKPAETH--------DLSSLRT--ILSTGSPLKPESFDYVYDHIKPDVLLASISGG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 380 ---GHGFV---TSLPV-------RVIKTDVA----EGT-VIDvardgkEIGEIVfvgniCAR-------GYYKDPDATR- 433
Cdd:cd05943 406 tdiISCFVggnPLLPVyrgeiqcRGLGMAVEafdeEGKpVWG------EKGELV-----CTKpfpsmpvGFWNDPDGSRy 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 434 --KLFA--GGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVT 509
Cdd:cd05943 475 raAYFAkyPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVK 554
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 169764941 510 VKPGKFLTgSEVIEWARNA--SDISKFMIPREVEVVAELPKTSTGK 553
Cdd:cd05943 555 LREGVELD-DELRKRIRSTirSALSPRHVPAKIIAVPDIPRTLSGK 599
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
434-554 |
2.09e-06 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 50.72 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 434 KLFAGGVLHSGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAVPDSHWGERPKAFVTVKPG 513
Cdd:PRK10524 468 SLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDS 547
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 169764941 514 KFLTGSEVIE------WARNASDISKFMIPREVEVVAELPKTSTGKV 554
Cdd:PRK10524 548 DSLADREARLalekeiMALVDSQLGAVARPARVWFVSALPKTRSGKL 594
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
34-559 |
2.63e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 50.55 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 34 LPRAAAIEPEAVAIhhVTANNQVlrrTYAETADRARGLAYYLKKHGFK---RVGVLCPNTPAFLESIFGIAAAGAVNVAV 110
Cdd:PRK05691 1137 LNEQARQTPERIAL--VWDGGSL---DYAELHAQANRLAHYLRDKGVGpdvCVAIAAERSPQLLVGLLAILKAGGAYVPL 1211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 111 NYRLKEDDIAYIFTHSDVEAIIVDQEFLSllqsyRASRPSIPIIVDMDTdategelsgpfdevvlegltYDLDTGAKGWP 190
Cdd:PRK05691 1212 DPDYPAERLAYMLADSGVELLLTQSHLLE-----RLPQAEGVSAIALDS--------------------LHLDSWPSQAP 1266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 191 GLEAQAaseDDVIALAYTSGTTARPKGVEYTHrgcylAAMGNVIESGLNSHR--GRCRYLWTLPM-FHACGWTFPWA--- 264
Cdd:PRK05691 1267 GLHLHG---DNLAYVIYTSGSTGQPKGVGNTH-----AALAERLQWMQATYAldDSDVLMQKAPIsFDVSVWECFWPlit 1338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 265 ----VTAVRGTHYclrkiDYPQIWKLLKQEHITHFNAAPTVNTLL--------CNS-----KEAEPLPEPVHVTVaaspp 327
Cdd:PRK05691 1339 gcrlVLAGPGEHR-----DPQRIAELVQQYGVTTLHFVPPLLQLFideplaaaCTSlrrlfSGGEALPAELRNRV----- 1408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 328 tphlFEQMTNLNLHpvHVYGMTETYGPITKgyylpaWDNLPSSERYKKMARQGHGFVtslpVRVIKTD---VAEGTVidv 404
Cdd:PRK05691 1409 ----LQRLPQVQLH--NRYGPTETAINVTH------WQCQAEDGERSPIGRPLGNVL----CRVLDAElnlLPPGVA--- 1469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 405 ardgkeiGEIVFVGNICARGYYKDPDATRKLF-------AGGVLH-SGDLAVWHADGSIQIQDRAKDIIISGGENISSVA 476
Cdd:PRK05691 1470 -------GELCIGGAGLARGYLGRPALTAERFvpdplgeDGARLYrTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEE 1542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 477 LESMLVTHPDILEAgVVAVPDSHWGERPKAFVTVKPGKFLTGSEVIewARNASDISKFMIPREVEVVAELPKTSTGKVRK 556
Cdd:PRK05691 1543 IQARLLAQPGVAQA-AVLVREGAAGAQLVGYYTGEAGQEAEAERLK--AALAAELPEYMVPAQLIRLDQMPLGPSGKLDR 1619
|
...
gi 169764941 557 NIL 559
Cdd:PRK05691 1620 RAL 1622
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
38-559 |
6.94e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 49.40 E-value: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 38 AAIEPEAVAIhhvTANNQVLrrTYAETADRARGLAYYLKKHGFK---RVGVLCPNTpafLESIFGIAAAGAVNVAVN--- 111
Cdd:PRK05691 2198 AARTPQAPAL---TFAGQTL--SYAELDARANRLARALRERGVGpqvRVGLALERS---LEMVVGLLAILKAGGAYVpld 2269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 112 --YRLkeDDIAYIFTHSDVeaiivdqeflSLLQSYRAsrpsipiivdmdTDATEGELSgpfDEVVLEGLTYDLdtgakgw 189
Cdd:PRK05691 2270 peYPL--ERLHYMIEDSGI----------GLLLSDRA------------LFEALGELP---AGVARWCLEDDA------- 2315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 190 PGLEAQAASEDDVIA-------LAYTSGTTARPKGVEYTHrGCYLAAMGNVIES-GLNSHRgrCRYLWTLPMFHACgwTF 261
Cdd:PRK05691 2316 AALAAYSDAPLPFLSlpqhqayLIYTSGSTGKPKGVVVSH-GEIAMHCQAVIERfGMRADD--CELHFYSINFDAA--SE 2390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 262 PWAVTAVRGTHYCLR---KIDYPQIWKLLKQEHITHFNAAPTVNTLLCN--SKEAEPLPEPVHVTVAASPPTPHLfeQMT 336
Cdd:PRK05691 2391 RLLVPLLCGARVVLRaqgQWGAEEICQLIREQQVSILGFTPSYGSQLAQwlAGQGEQLPVRMCITGGEALTGEHL--QRI 2468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 337 NLNLHP---VHVYGMTETYgpitkgyylpawdNLPSSERYKKMARQGHGfvtSLPV-RVIKTDVAEGTVIDVARDGK-EI 411
Cdd:PRK05691 2469 RQAFAPqlfFNAYGPTETV-------------VMPLACLAPEQLEEGAA---SVPIgRVVGARVAYILDADLALVPQgAT 2532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 412 GEIVFVGNICARGYYKDPDATRKLF-------AGGVLH-SGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVT 483
Cdd:PRK05691 2533 GELYVGGAGLAQGYHDRPGLTAERFvadpfaaDGGRLYrTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLE 2612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 484 HPDILEAGVVAVpDSHWGERPKAFVTVKPGKflTGSEVIEWARNA------SDISKFMIPREVEVVAELPKTSTGKVRKN 557
Cdd:PRK05691 2613 HPAVREAVVLAL-DTPSGKQLAGYLVSAVAG--QDDEAQAALREAlkahlkQQLPDYMVPAHLILLDSLPLTANGKLDRR 2689
|
..
gi 169764941 558 IL 559
Cdd:PRK05691 2690 AL 2691
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
412-485 |
1.27e-05 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 48.19 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 412 GEIVFVGNICARGYYKDPDATRKLFA---GGV--LHSGDLAVWHADGSIQIQDRAKDII-ISGGENISSVALESMLVTHP 485
Cdd:PLN02387 503 GEIVIGGPSVTLGYFKNQEKTDEVYKvdeRGMrwFYTGDIGQFHPDGCLEIIDRKKDIVkLQHGEYVSLGKVEAALSVSP 582
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
388-560 |
2.68e-05 |
|
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: 47.03 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 388 PVRVIKTDVAEGTVIDvARDGKEI----GEI-VFVGNICAR-------GYYKDPDATRKL----FAGG--VLHSGDLAVW 449
Cdd:cd05939 281 PIRLIKVDEDTGELIR-DSDGLCIpcqpGEPgLLVGKIIQNdplrrfdGYVNEGATNKKIardvFKKGdsAFLSGDVLVM 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 450 HADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGV--VAVPDSHWGERPKAFVTVKPGKFLTgsevIEWARN 527
Cdd:cd05939 360 DELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVPGVEGRAGMAAIVDPERKVDLD----RFSAVL 435
|
170 180 190
....*....|....*....|....*....|...
gi 169764941 528 ASDISKFMIPREVEVVAELPKTSTGKVRKNILR 560
Cdd:cd05939 436 AKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
173-556 |
6.86e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 45.70 E-value: 6.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 173 VVLEGLTYDLDTGakgwPGLEAQAASEDDVIALAYTSGTTARPKGVEYTHRGC----------YLAAMGNVIESGLNShr 242
Cdd:PRK05850 137 PVIEVDLLDLDSP----RGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVianfeqlmsdYFGDTGGVPPPDTTV-- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 243 grcrYLWtLPMFH------------ACGW----TFPWAVtavrgthycLRKidyPQIWKLLKQEHITHFNAAP------- 299
Cdd:PRK05850 211 ----VSW-LPFYHdmglvlgvcapiLGGCpavlTSPVAF---------LQR---PARWMQLLASNPHAFSAAPnfafela 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 300 ---------------TVNTLLCNSkeaeplpEPVHvtvaasPPTPHLF-EQMTNLNLHPVHV---YGMTE-TYGPITkgy 359
Cdd:PRK05850 274 vrktsdddmagldlgGVLGIISGS-------ERVH------PATLKRFaDRFAPFNLRETAIrpsYGLAEaTVYVAT--- 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 360 ylPAWDNLPSSER--YKKMARqGH---------------GFVTSLPVRVIKTDvaegTVIDVArDGKeIGEIVFVGNICA 422
Cdd:PRK05850 338 --REPGQPPESVRfdYEKLSA-GHakrcetgggtplvsyGSPRSPTVRIVDPD----TCIECP-AGT-VGEIWVHGDNVA 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 423 RGYYKDPDATRKLFAGGV------------LHSGDLAVWHaDGSIQIQDRAKDIIISGGENissvalesmlvTHPDILEA 490
Cdd:PRK05850 409 AGYWQKPEETERTFGATLvdpspgtpegpwLRTGDLGFIS-EGELFIVGRIKDLLIVDGRN-----------HYPDDIEA 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 491 GV----------VAVPDSHwGERPKAFVTVKPgKFLTGSEVIEWARN-----ASDISKF--MIPREVEVVA--ELPKTST 551
Cdd:PRK05850 477 TIqeitggrvaaISVPDDG-TEKLVAIIELKK-RGDSDEEAMDRLRTvkrevTSAISKShgLSVADLVLVApgSIPITTS 554
|
....*
gi 169764941 552 GKVRK 556
Cdd:PRK05850 555 GKIRR 559
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
162-559 |
1.47e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 45.04 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 162 TEGELSGPFDEV-VLEGLTYD-LDTGAKGWPGLEAQAASEDDVIalaYTSGTTARPKGVEYTHRgcylaAMGNviesgln 239
Cdd:PRK10252 561 TTADQLPRFADVpDLTSLCYNaPLAPQGAAPLQLSQPHHTAYII---FTSGSTGRPKGVMVGQT-----AIVN------- 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 240 shrgrcRYLW----------------TLPMFHACGWTFPWA-------VTAVRGTHYclrkiDYPQIWKLLKQEHIT--H 294
Cdd:PRK10252 626 ------RLLWmqnhypltaddvvlqkTPCSFDVSVWEFFWPfiagaklVMAEPEAHR-----DPLAMQQFFAEYGVTttH 694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 295 FnaaptVNTLLcNSKEAEPLPEPVHVTVAA---------SPPTP--HLFEQMTNLNLHpvHVYGMTETYGPITkgyYLPA 363
Cdd:PRK10252 695 F-----VPSML-AAFVASLTPEGARQSCASlrqvfcsgeALPADlcREWQQLTGAPLH--NLYGPTEAAVDVS---WYPA 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 364 WdnlpsserykkmaRQGHGFVTSLPV----RVIKTDVaegTVID---------VArdgkeiGEIVFVGNICARGYYKDPD 430
Cdd:PRK10252 764 F-------------GEELAAVRGSSVpigyPVWNTGL---RILDarmrpvppgVA------GDLYLTGIQLAQGYLGRPD 821
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 431 ATRKLF------AGGVLH-SGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVTHPDILEAGVVAV----PDSH 499
Cdd:PRK10252 822 LTASRFiadpfaPGERMYrTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqAAAT 901
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169764941 500 WGE--RPKAFVTVKPGKFLTgSEVIEwARNASDISKFMIPREVEVVAELPKTSTGKVRKNIL 559
Cdd:PRK10252 902 GGDarQLVGYLVSQSGLPLD-TSALQ-AQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
114-255 |
3.22e-04 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 43.57 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 114 LKEDDIAYIFTHSDVEAIIVDQEFLSLLQSYRASRPSIPIIVDMDTDATEGELSGPFDEVVLEGLTYDLDTGAKGWPgLE 193
Cdd:PLN02387 165 LGEEALCHSLNETEVTTVICDSKQLKKLIDISSQLETVKRVIYMDDEGVDSDSSLSGSSNWTVSSFSEVEKLGKENP-VD 243
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169764941 194 AQAASEDDVIALAYTSGTTARPKGVEYTHrGCYLAAMGNV--IESGLNShrgRCRYLWTLPMFH 255
Cdd:PLN02387 244 PDLPSPNDIAVIMYTSGSTGLPKGVMMTH-GNIVATVAGVmtVVPKLGK---NDVYLAYLPLAH 303
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
443-563 |
8.06e-04 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 42.39 E-value: 8.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 443 SGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESM-LVTHPDILEAgVVAVPDSHWGErpkAFVTVKPGKFLTGSEV 521
Cdd:PRK08043 595 TGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLGVSPDKQHA-TAIKSDASKGE---ALVLFTTDSELTREKL 670
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 169764941 522 IEWARnASDISKFMIPREVEVVAELPKTSTGKVRKNILRDWA 563
Cdd:PRK08043 671 QQYAR-EHGVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSMV 711
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
411-559 |
8.57e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.46 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 411 IGEIVFVGNICARGYYKDPDATRKLF-------AGGVLH-SGDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLV 482
Cdd:PRK05691 4066 VGELCVAGTGVGRGYVGDPLRTALAFvphpfgaPGERLYrTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLH 4145
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169764941 483 THPDILEAgVVAVPDSHWGERPKAFVTVKPGkFLTGSEVIEWARN--ASDISKFMIPREVEVVAELPKTSTGKVRKNIL 559
Cdd:PRK05691 4146 EQAEVREA-AVAVQEGVNGKHLVGYLVPHQT-VLAQGALLERIKQrlRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
444-569 |
2.72e-03 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 40.83 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 444 GDLAVWHADGSIQIQDRAKDIIISGGENISSVALESMLVT-HPDILEAGVVAVPDSHWG-ERPKAFVTVKPGKFLTGS-E 520
Cdd:PLN03052 594 GDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCNAaDESVLETAAIGVPPPGGGpEQLVIAAVLKDPPGSNPDlN 673
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 169764941 521 VIEWARNASdISKFMIP----REVEVVAELPKTSTGKVRKNILRD-WAKGANRS 569
Cdd:PLN03052 674 ELKKIFNSA-IQKKLNPlfkvSAVVIVPSFPRTASNKVMRRVLRQqLAQELSRS 726
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
173-260 |
8.25e-03 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 38.92 E-value: 8.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169764941 173 VVLEGLTYDLDTGAKGW-------PGLEAQAASEDDVIALAYTSGTTARPKGVEYTHRgcylAAMGNV--IESgLNSHRG 243
Cdd:PRK08043 331 VYLEDLKDDVTTADKLWifahllmPRLAQVKQQPEDAALILFTSGSEGHPKGVVHSHK----SLLANVeqIKT-IADFTP 405
|
90
....*....|....*..
gi 169764941 244 RCRYLWTLPMFHACGWT 260
Cdd:PRK08043 406 NDRFMSALPLFHSFGLT 422
|
|
| |
