|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
1-509 |
0e+00 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 918.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 1 MSHNLFETFAAKMRERaEADFITTRDGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGV 80
Cdd:PRK07514 1 MNNNLFDALRAAFADR-DAPFIETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 81 YLPLNTGYTGDEIRYFLNDAEPALFVCRPKIEEQALSLAAETGCPAVVTLGSAADGSLMETAQAAVPREDIVALGERDLA 160
Cdd:PRK07514 80 FLPLNTAYTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAAGAPHVETLDADGTGSLLEAAAAAPDDFETVPRGADDLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 161 AILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDADVIFE 240
Cdd:PRK07514 160 AILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDPDAVLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 241 ELPRGTVMMGVPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNMNLSNPYDGARR 320
Cdd:PRK07514 240 LMPRATVMMGVPTFYTRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTETNMNTSNPYDGERR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 321 AGTVGMPLPGVEMRITNRETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRD 400
Cdd:PRK07514 320 AGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 401 KDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADlgenqLEEEKVITHLDGRLAKYKQPK 480
Cdd:PRK07514 400 KDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAA-----LDEAAILAALKGRLARFKQPK 474
|
490 500
....*....|....*....|....*....
gi 2136495511 481 RVFFVDELPRNTMGKVQKNELRKRFNDTY 509
Cdd:PRK07514 475 RVFFVDELPRNTMGKVQKNLLREQYADLF 503
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
26-503 |
0e+00 |
|
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: 579.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 26 DGRRYRYTDALTISAQLAGALTELG-VKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPAL 104
Cdd:cd05941 8 DGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 105 FVcrpkieeqalslaaetgcpavvtlgsaadgslmetaqaavpredivalgerDLAAILYTSGTTGRSKGAMLTHKNLAS 184
Cdd:cd05941 88 VL---------------------------------------------------DPALILYTSGTTGRPKGVVLTHANLAA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 185 NAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDADVIF--EELPRGTVMMGVPTFYTRLVQDE 262
Cdd:cd05941 117 NVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAisRLMPSITVFMGVPTIYTRLLQYY 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 263 RLTP--------EATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNMNLSNPYDGARRAGTVGMPLPGVEMR 334
Cdd:cd05941 197 EAHFtdpqfaraAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGERRPGTVGMPLPGVQAR 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 335 ITNRETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVI-SGGYNVYP 413
Cdd:cd05941 277 IVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIkSGGYKVSA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 414 KEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGAdlgeNQLEEEKVITHLDGRLAKYKQPKRVFFVDELPRNTM 493
Cdd:cd05941 357 LEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGA----AALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAM 432
|
490
....*....|
gi 2136495511 494 GKVQKNELRK 503
Cdd:cd05941 433 GKVNKKELRK 442
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
5-507 |
0e+00 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 517.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 5 LFETFAAKMRERAEADFITtRDGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPL 84
Cdd:COG0318 1 LADLLRRAAARHPDRPALV-FGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 85 NTGYTGDEIRYFLNDAEPALFVCrpkieeqalslaaetgcpavvtlgsaadgslmetaqaavpredivalgerdlAAILY 164
Cdd:COG0318 80 NPRLTAEELAYILEDSGARALVT----------------------------------------------------ALILY 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 165 TSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDADVIFEELP- 243
Cdd:COG0318 108 TSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVLELIEr 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 244 -RGTVMMGVPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNMNLS-NPYD-GARR 320
Cdd:COG0318 188 eRVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTvNPEDpGERR 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 321 AGTVGMPLPGVEMRITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELlDDGFFITGDLAMVDEQGYVHIVGRD 400
Cdd:COG0318 268 PGSVGRPLPGVEVRIVD-EDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRK 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 401 KDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADlgenqLEEEKVITHLDGRLAKYKQPK 480
Cdd:COG0318 346 KDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAE-----LDAEELRAFLRERLARYKVPR 420
|
490 500
....*....|....*....|....*..
gi 2136495511 481 RVFFVDELPRNTMGKVQKNELRKRFND 507
Cdd:COG0318 421 RVEFVDELPRTASGKIDRRALRERYAA 447
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
26-502 |
2.93e-156 |
|
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: 453.17 E-value: 2.93e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 26 DGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALF 105
Cdd:cd05936 21 MGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 106 VCrpkieeqALSLAaetgcpavvtlgsaadgSLMETAQAAVPRediVALGERDLAAILYTSGTTGRSKGAMLTHKNLASN 185
Cdd:cd05936 101 IV-------AVSFT-----------------DLLAAGAPLGER---VALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVAN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 186 AKTlARAW---HFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDADVIFEEL--PRGTVMMGVPTFYTRLVQ 260
Cdd:cd05936 154 ALQ-IKAWledLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVLKEIrkHRVTIFPGVPTMYIALLN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 261 DERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNMNLS-NPYDGARRAGTVGMPLPGVEMRITNRE 339
Cdd:cd05936 233 APEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAvNPLDGPRKPGSIGIPLPGTEVKIVDDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 340 tGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTrEELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQV 419
Cdd:cd05936 313 -GEELPPGEVGELWVRGPQVMKGYWNRPEET-AEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 420 IDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGENQLeeekvITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKN 499
Cdd:cd05936 391 LYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEI-----IAFCREQLAGYKVPRQVEFRDELPKSAVGKILRR 465
|
...
gi 2136495511 500 ELR 502
Cdd:cd05936 466 ELR 468
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
4-507 |
1.67e-144 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 424.98 E-value: 1.67e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 4 NLFETFAAKMRERAEADfITTRDGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLP 83
Cdd:PRK06187 7 TIGRILRHGARKHPDKE-AVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 84 LNTGYTGDEIRYFLNDAEPALFVCRPKIEEQALSLAAE-TGCPAVVTLGSAADGSLMETAQ-------AAVPREDIVALG 155
Cdd:PRK06187 86 INIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQlPTVRTVIVEGDGPAAPLAPEVGeyeellaAASDTFDFPDID 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 156 ERDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVaCNVTLMAGASMLFLPKFDA 235
Cdd:PRK06187 166 ENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGL-PYLALMAGAKQVIPRRFDP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 236 DVIFE--ELPRGTVMMGVPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETN----M 309
Cdd:PRK06187 245 ENLLDliETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSpvvsV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 310 NLSNPYDGAR--RAGTVGMPLPGVEMRITNrETGAEVP--FGEIGMLQIRGPNVFIGYWRMPEKTrEELLDDGFFITGDL 385
Cdd:PRK06187 325 LPPEDQLPGQwtKRRSAGRPLPGVEARIVD-DDGDELPpdGGEVGEIIVRGPWLMQGYWNRPEAT-AETIDGGWLHTGDV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 386 AMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGENQLEEekv 465
Cdd:PRK06187 403 GYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAKELRA--- 479
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2136495511 466 itHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRKRFND 507
Cdd:PRK06187 480 --FLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQYAE 519
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
26-504 |
4.32e-144 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 423.55 E-value: 4.32e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 26 DGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAE-PAL 104
Cdd:PRK07656 27 GDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDaKAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 105 FVCRPKIeeqALSLAAETGCPAVVTLGSAADGSLMETAQAAVPREDIVALGER----------DLAAILYTSGTTGRSKG 174
Cdd:PRK07656 107 FVLGLFL---GVDYSATTRLPALEHVVICETEEDDPHTEKMKTFTDFLAAGDPaerapevdpdDVADILFTSGTTGRPKG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 175 AMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDADVIFE--ELPRGTVMMGVP 252
Cdd:PRK07656 184 AMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLPVFDPDEVFRliETERITVLPGPP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 253 TFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTG-HAILERYGMTETN-MNLSNPYDGARR--AGTVGMPL 328
Cdd:PRK07656 264 TMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGvDIVLTGYGLSEASgVTTFNRLDDDRKtvAGTIGTAI 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 329 PGVEMRITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGG 408
Cdd:PRK07656 344 AGVENKIVN-ELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGG 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 409 YNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGAdlgenQLEEEKVITHLDGRLAKYKQPKRVFFVDEL 488
Cdd:PRK07656 423 FNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGA-----ELTEEELIAYCREHLAKYKVPRSIEFLDEL 497
|
490
....*....|....*.
gi 2136495511 489 PRNTMGKVQKNELRKR 504
Cdd:PRK07656 498 PKNATGKVLKRALREK 513
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
26-498 |
9.52e-140 |
|
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: 409.69 E-value: 9.52e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 26 DGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALF 105
Cdd:cd17631 17 GGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 106 VcrpkieeqalslaaetgcpavvtlgsaadgslmetaqaavpredivalgeRDLAAILYTSGTTGRSKGAMLTHKNLASN 185
Cdd:cd17631 97 F--------------------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNLLWN 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 186 AKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDADVIFE--ELPRGTVMMGVPTFYTRLVQDER 263
Cdd:cd17631 127 AVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDliERHRVTSFFLVPTMIQALLQHPR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 264 LTPEATANMRLFVSGSAPLTAETHEAFEAKtGHAILERYGMTETNMNLS--NPYDGARRAGTVGMPLPGVEMRITnRETG 341
Cdd:cd17631 207 FATTDLSSLRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTflSPEDHRRKLGSAGRPVFFVEVRIV-DPDG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 342 AEVPFGEIGMLQIRGPNVFIGYWRMPEKTrEELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVID 421
Cdd:cd17631 285 REVPPGEVGEIVVRGPHVMAGYWNRPEAT-AAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLY 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2136495511 422 ELDQVAESAVIGLPHPDFGEGVTAVVVRQQGAdlgenQLEEEKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQK 498
Cdd:cd17631 364 EHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGA-----ELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
21-497 |
5.99e-123 |
|
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: 368.85 E-value: 5.99e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 21 FITTRDGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDA 100
Cdd:cd05911 2 QIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 101 EPALFVCRPKIEEQALSLAAETGC-PAVVTLGSAADG------SLMETAQAAVPREDIV-ALGERDLAAILYTSGTTGRS 172
Cdd:cd05911 82 KPKVIFTDPDGLEKVKEAAKELGPkDKIIVLDDKPDGvlsiedLLSPTLGEEDEDLPPPlKDGKDDTAAILYSSGTTGLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 173 KGAMLTHKNLASNAK--TLARAWHFSADDRLIHALPIFHTHGLFvACNVTLMAGASMLFLPKFDADVIFEELP--RGTVM 248
Cdd:cd05911 162 KGVCLSHRNLIANLSqvQTFLYGNDGSNDVILGFLPLYHIYGLF-TTLASLLNGATVIIMPKFDSELFLDLIEkyKITFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 249 MGVPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHA-ILERYGMTETNMNLSNPYDGARRAGTVGMP 327
Cdd:cd05911 241 YLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNAtIKQGYGMTETGGILTVNPDGDDKPGSVGRL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 328 LPGVEMRITNRETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISG 407
Cdd:cd05911 321 LPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKYK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 408 GYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGAdlgenQLEEEKVITHLDGRLAKYKQ-PKRVFFVD 486
Cdd:cd05911 401 GFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGE-----KLTEKEVKDYVAKKVASYKQlRGGVVFVD 475
|
490
....*....|.
gi 2136495511 487 ELPRNTMGKVQ 497
Cdd:cd05911 476 EIPKSASGKIL 486
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
158-497 |
2.97e-122 |
|
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: 361.60 E-value: 2.97e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 158 DLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVAcNVTLMAGASMLFLPKFDADV 237
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGL-LGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 238 IFEELP--RGTVMMGVPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNMNLS--N 313
Cdd:cd04433 80 ALELIEreKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVAtgP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 314 PYDGARRAGTVGMPLPGVEMRITNRETGaEVPFGEIGMLQIRGPNVFIGYWRMPEKTrEELLDDGFFITGDLAMVDEQGY 393
Cdd:cd04433 160 PDDDARKPGSVGRPVPGVEVRIVDPDGG-ELPPGEIGELVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDEDGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 394 VHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADlgenqLEEEKVITHLDGRL 473
Cdd:cd04433 238 LYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGAD-----LDAEELRAHVRERL 312
|
330 340
....*....|....*....|....
gi 2136495511 474 AKYKQPKRVFFVDELPRNTMGKVQ 497
Cdd:cd04433 313 APYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
34-502 |
3.20e-122 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 366.24 E-value: 3.20e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 34 DALTIS------AQLAGALTEL--GVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALF 105
Cdd:PRK07787 17 DAVRIGgrvlsrSDLAGAATAVaeRVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAW 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 106 VCRPKIEEQALslaaetgcPAV-VTLGSAADGSLMEtaqaavPREDIVALgerdlaaILYTSGTTGRSKGAMLTHKNLAS 184
Cdd:PRK07787 97 LGPAPDDPAGL--------PHVpVRLHARSWHRYPE------PDPDAPAL-------IVYTSGTTGPPKGVVLSRRAIAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 185 NAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDADVIFEELP-RGTVMMGVPTFYTRLVQDER 263
Cdd:PRK07787 156 DLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPEAYAQALSeGGTLYFGVPTVWSRIAADPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 264 LtPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNMNLSNPYDGARRAGTVGMPLPGVEMRITNrETGAE 343
Cdd:PRK07787 236 A-ARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVD-EDGGP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 344 VPF-GE-IGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRDK-DLVISGGYNVYPKEVEQVI 420
Cdd:PRK07787 314 VPHdGEtVGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETAL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 421 DELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGEnqleeekVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNE 500
Cdd:PRK07787 394 LGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAADE-------LIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQ 466
|
..
gi 2136495511 501 LR 502
Cdd:PRK07787 467 LL 468
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
5-504 |
3.04e-118 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 359.70 E-value: 3.04e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 5 LFETFAAKMRERAEADFIttrdGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPL 84
Cdd:PRK05605 37 LYDNAVARFGDRPALDFF----GATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 85 NTGYTGDEIRYFLNDAEPALFVCRPKIEEQALSLAAETGCPAVVTLG--------------------SAADGSLMETAQA 144
Cdd:PRK05605 113 NPLYTAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTPLETIVSVNmiaampllqrlalrlpipalRKARAALTGPAPG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 145 AVPREDIVALGE--------------RDLAAILYTSGTTGRSKGAMLTHKNLASNAKtLARAW---HFSADDRLIHALPI 207
Cdd:PRK05605 193 TVPWETLVDAAIggdgsdvshprptpDDVALILYTSGTTGKPKGAQLTHRNLFANAA-QGKAWvpgLGDGPERVLAALPM 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 208 FHTHGLFVACNVTLMAGASMLFLPKFDADVIFEELPRG--TVMMGVPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAE 285
Cdd:PRK05605 272 FHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHppTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGAMALPVS 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 286 THEAFEAKTGHAILERYGMTETN-MNLSNPYDGARRAGTVGMPLPGVEMRITNRETGAE-VPFGEIGMLQIRGPNVFIGY 363
Cdd:PRK05605 352 TVELWEKLTGGLLVEGYGLTETSpIIVGNPMSDDRRPGYVGVPFPDTEVRIVDPEDPDEtMPDGEEGELLVRGPQVFKGY 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 364 WRMPEKTREELLdDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGV 443
Cdd:PRK05605 432 WNRPEETAKSFL-DGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEV 510
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2136495511 444 TAVVVRQQGADlgenqLEEEKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRKR 504
Cdd:PRK05605 511 VAAVVLEPGAA-----LDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREE 566
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
6-407 |
4.10e-117 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 351.23 E-value: 4.10e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 6 FETFAAKMRERAeadFITTRDGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLN 85
Cdd:pfam00501 1 LERQAARTPDKT---ALEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 86 TGYTGDEIRYFLNDAEP-ALFVCRPKIEEQALSLAAETGCPAVVTLGSAADGSLMETAQAAVPREDI-----VALGERDL 159
Cdd:pfam00501 78 PRLPAEELAYILEDSGAkVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVpppppPPPDPDDL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 160 AAILYTSGTTGRSKGAMLTHKNLASNAKTLA----RAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKF-- 233
Cdd:pfam00501 158 AYIIYTSGTTGKPKGVMLTHRNLVANVLSIKrvrpRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFpa 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 234 -DADVIFEELPRG--TVMMGVPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNMN 310
Cdd:pfam00501 238 lDPAALLELIERYkvTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 311 LSNPYDG---ARRAGTVGMPLPGVEMRITNRETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAM 387
Cdd:pfam00501 318 VTTPLPLdedLRSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGR 397
|
410 420
....*....|....*....|
gi 2136495511 388 VDEQGYVHIVGRDKDLVISG 407
Cdd:pfam00501 398 RDEDGYLEIVGRKKDQIKLG 417
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
21-503 |
1.34e-114 |
|
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: 347.38 E-value: 1.34e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 21 FITTRDGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDA 100
Cdd:cd05926 6 LVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 101 EPALfVCRPKIEEQALSLAAETGCPAVVTLGSAA--------DGSL-METAQAAVPREDIVALGErDLAAILYTSGTTGR 171
Cdd:cd05926 86 GSKL-VLTPKGELGPASRAASKLGLAILELALDVgvlirapsAESLsNLLADKKNAKSEGVPLPD-DLALILHTSGTTGR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 172 SKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDADVIFEELP--RGTVMM 249
Cdd:cd05926 164 PKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVRdyNATWYT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 250 GVPTFYTRLVQDERLTPEATANMRLFV-SGSAPLTAETHEAFEAKTGHAILERYGMTETNMNL-SNPYD-GARRAGTVGM 326
Cdd:cd05926 244 AVPTIHQILLNRPEPNPESPPPKLRFIrSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMtSNPLPpGPRKPGSVGK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 327 PLpGVEMRITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVIS 406
Cdd:cd05926 324 PV-GVEVRILD-EDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 407 GGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGAdlgenQLEEEKVITHLDGRLAKYKQPKRVFFVD 486
Cdd:cd05926 402 GGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGA-----SVTEEELRAFCRKHLAAFKVPKKVYFVD 476
|
490
....*....|....*..
gi 2136495511 487 ELPRNTMGKVQKNELRK 503
Cdd:cd05926 477 ELPKTATGKIQRRKVAE 493
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
27-510 |
8.83e-108 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 331.13 E-value: 8.83e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 27 GRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFV 106
Cdd:PRK08316 34 DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 107 CRPKIEEQALSLAAETGC-----PAVVTLGSAADG--SLMETAQAAVPREDIVALGERDLAAILYTSGTTGRSKGAMLTH 179
Cdd:PRK08316 114 VDPALAPTAEAALALLPVdtlilSLVLGGREAPGGwlDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTH 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 180 KNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDADVIFEELPRGTVMM--GVPTFYTR 257
Cdd:PRK08316 194 RALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAPDPELILRTIEAERITSffAPPTVWIS 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 258 LVQDERLTPEATANMRLFVSGSAPLTAET-HEAFEAKTGHAILERYGMTE---TNMNLsNPYDGARRAGTVGMPLPGVEM 333
Cdd:PRK08316 274 LLRHPDFDTRDLSSLRKGYYGASIMPVEVlKELRERLPGLRFYNCYGQTEiapLATVL-GPEEHLRRPGSAGRPVLNVET 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 334 RITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTrEELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYP 413
Cdd:PRK08316 353 RVVD-DDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKT-AEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVAS 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 414 KEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADlgenqLEEEKVITHLDGRLAKYKQPKRVFFVDELPRNTM 493
Cdd:PRK08316 431 REVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGAT-----VTEDELIAHCRARLAGFKVPKRVIFVDELPRNPS 505
|
490
....*....|....*..
gi 2136495511 494 GKVQKNELRKRFNDTYQ 510
Cdd:PRK08316 506 GKILKRELRERYAGAFT 522
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
48-507 |
3.04e-106 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 326.05 E-value: 3.04e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 48 ELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVCRPKIEEQALSLAAETGCPAV 127
Cdd:PRK06839 47 ELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 128 VTLGSaadgsLMETAQAAvpREDIVALGERDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPI 207
Cdd:PRK06839 127 ISITS-----LKEIEDRK--IDNFVEKNESASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 208 FHTHGLFVACNVTLMAGASMLFLPKFDAD--VIFEELPRGTVMMGVPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAE 285
Cdd:PRK06839 200 FHIGGIGLFAFPTLFAGGVIIVPRKFEPTkaLSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 286 THEAFEAKtGHAILERYGMTETN----MNLSNpyDGARRAGTVGMPLPGVEMRITNRETGaEVPFGEIGMLQIRGPNVFI 361
Cdd:PRK06839 280 LMREFIDR-GFLFGQGFGMTETSptvfMLSEE--DARRKVGSIGKPVLFCDYELIDENKN-KVEVGEVGELLIRGPNVMK 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 362 GYWRMPEKTrEELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGE 441
Cdd:PRK06839 356 EYWNRPDAT-EETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGE 434
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2136495511 442 GVTAVVVRQQGAdlgenQLEEEKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRKRFND 507
Cdd:PRK06839 435 IPIAFIVKKSSS-----VLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLKS 495
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
24-504 |
5.60e-105 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 325.14 E-value: 5.60e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 24 TRDGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPA 103
Cdd:COG0365 34 DGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 104 LFVC-------------RPKIEEqalslaAETGCP---AVVTLGSAADGSLMETA-------QAAVPREDIVALGERDLA 160
Cdd:COG0365 114 VLITadgglrggkvidlKEKVDE------ALEELPsleHVIVVGRTGADVPMEGDldwdellAAASAEFEPEPTDADDPL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 161 AILYTSGTTGRSKGAMLTHKNLASNAKTLARAWH-FSADDRLIHALPIF----HTHGLFVAcnvtLMAGASMLFL---PK 232
Cdd:COG0365 188 FILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLdLKPGDVFWCTADIGwatgHSYIVYGP----LLNGATVVLYegrPD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 233 F-DADVIFEELPR-G-TVMMGVPTFYTRLVQ--DERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTET 307
Cdd:COG0365 264 FpDPGRLWELIEKyGvTVFFTAPTAIRALMKagDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTET 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 308 NMN-LSNPYDGARRAGTVGMPLPGVEMRITNrETGAEVPFGEIGMLQIRG--PNVFIGYWRMPEKTREELLD--DGFFIT 382
Cdd:COG0365 344 GGIfISNLPGLPVKPGSMGKPVPGYDVAVVD-EDGNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETYFGrfPGWYRT 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 383 GDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGEnQLEE 462
Cdd:COG0365 423 GDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSD-ELAK 501
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2136495511 463 EkVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRKR 504
Cdd:COG0365 502 E-LQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKI 542
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
21-503 |
7.74e-104 |
|
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: 320.34 E-value: 7.74e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 21 FITTRDGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDA 100
Cdd:cd05904 24 LIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 101 EPALFVCRPKIEEQALSLAAEtgcpaVVTLGSAADGS------LMETAQAAVPREDIvalGERDLAAILYTSGTTGRSKG 174
Cdd:cd05904 104 GAKLAFTTAELAEKLASLALP-----VVLLDSAEFDSlsfsdlLFEADEAEPPVVVI---KQDDVAALLYSSGTTGRSKG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 175 AMLTHKNLASNAKTLARAW--HFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDADVIFEELPRGTVMMG-- 250
Cdd:cd05904 176 VMLTHRNLIAMVAQFVAGEgsNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPRFDLEELLAAIERYKVTHLpv 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 251 VPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHA-ILERYGMTETN----MNLsNPYDGARRAGTVG 325
Cdd:cd05904 256 VPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVdLGQGYGMTESTgvvaMCF-APEKDRAKYGSVG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 326 MPLPGVEMRITNRETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVI 405
Cdd:cd05904 335 RLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIK 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 406 SGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGENQleeekVITHLDGRLAKYKQPKRVFFV 485
Cdd:cd05904 415 YKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDE-----IMDFVAKQVAPYKKVRKVAFV 489
|
490
....*....|....*...
gi 2136495511 486 DELPRNTMGKVqkneLRK 503
Cdd:cd05904 490 DAIPKSPSGKI----LRK 503
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
27-502 |
2.31e-103 |
|
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: 316.16 E-value: 2.31e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 27 GRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFV 106
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 107 CrpkieeqalslaaetgcpavvtlgsaadgslmetaqaavpredivalgerDLAAILYTSGTTGRSKGAMLTHKNLASNA 186
Cdd:cd05934 81 V--------------------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 187 KTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDA-----DV------IFEELPrgtVMMGvptfy 255
Cdd:cd05934 111 YYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSAsrfwsDVrrygatVTNYLG---AMLS----- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 256 TRLVQDERltPEATANmRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNMNLSNPYDGARRAGTVGMPLPGVEMRI 335
Cdd:cd05934 183 YLLAQPPS--PDDRAH-RLRAAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRI 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 336 TNrETGAEVPFGEIGMLQIR---GPNVFIGYWRMPEKTrEELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVY 412
Cdd:cd05934 260 VD-DDGQELPAGEPGELVIRglrGWGFFKGYYNMPEAT-AEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENIS 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 413 PKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGAdlgenQLEEEKVITHLDGRLAKYKQPKRVFFVDELPRNT 492
Cdd:cd05934 338 SAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGE-----TLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTP 412
|
490
....*....|
gi 2136495511 493 MGKVQKNELR 502
Cdd:cd05934 413 TEKVAKAQLR 422
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
3-511 |
5.27e-97 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 304.65 E-value: 5.27e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 3 HNLFETFAAKMRERAEADFIttrdGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYL 82
Cdd:PRK06710 27 HKYVEQMASRYPEKKALHFL----GKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 83 PLNTGYTGDEIRYFLNDAEPALFVCRPKIEEQALSLAAETGCPAVVTLGSA------------------------ADGSL 138
Cdd:PRK06710 103 QTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSATKIEHVIVTRIAdflpfpknllypfvqkkqsnlvvkVSESE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 139 METAQAAVPRE-----DIVALGERDLAAILYTSGTTGRSKGAMLTHKNLASNAkTLARAWHFS---ADDRLIHALPIFHT 210
Cdd:PRK06710 183 TIHLWNSVEKEvntgvEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNT-LMGVQWLYNckeGEEVVLGVLPFFHV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 211 HGLFVACNVTLMAGASMLFLPKFDADVIFEELPRGTVMM--GVPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHE 288
Cdd:PRK06710 262 YGMTAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLfpGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 289 AFEAKTGHAILERYGMTETN-MNLSNPYDGARRAGTVGMPLPGVEMRITNRETGAEVPFGEIGMLQIRGPNVFIGYWRMP 367
Cdd:PRK06710 342 KFETVTGGKLVEGYGLTESSpVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKP 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 368 EKTrEELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVV 447
Cdd:PRK06710 422 EET-AAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFV 500
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2136495511 448 VRQQGADLGENQLEEekvitHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNEL---RKRFNDTYQT 511
Cdd:PRK06710 501 VLKEGTECSEEELNQ-----FARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLieeEKRKNEDEQT 562
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
39-503 |
3.21e-93 |
|
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: 289.63 E-value: 3.21e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 39 SAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALfvcrpkieeqalsl 118
Cdd:cd05912 11 VSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL-------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 119 aaetgcpavvtlgsaadgslmetaqaavprEDIvalgerdlAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSAD 198
Cdd:cd05912 77 ------------------------------DDI--------ATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTED 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 199 DRLIHALPIFHTHGLFVACNvTLMAGASMLFLPKFDADVIFEELPRG--TVMMGVPTFYTRLVqdERLTPEATANMRLFV 276
Cdd:cd05912 119 DNWLCALPLFHISGLSILMR-SVIYGMTVYLVDKFDAEQVLHLINSGkvTIISVVPTMLQRLL--EILGEGYPNNLRCIL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 277 SGSAPLTAETHEAFEAKtGHAILERYGMTETNMNLS--NPYDGARRAGTVGMPLPGVEMRITNretgAEVPFGEIGMLQI 354
Cdd:cd05912 196 LGGGPAPKPLLEQCKEK-GIPVYQSYGMTETCSQIVtlSPEDALNKIGSAGKPLFPVELKIED----DGQPPYEVGEILL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 355 RGPNVFIGYWRMPEKTrEELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGL 434
Cdd:cd05912 271 KGPNVTKGYLNRPDAT-EESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGI 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2136495511 435 PHPDFGEGVTAVVVRQQgadlgenQLEEEKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRK 503
Cdd:cd05912 350 PDDKWGQVPVAFVVSER-------PISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
29-503 |
5.22e-93 |
|
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: 290.05 E-value: 5.22e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 29 RYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVcr 108
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 109 pkieeqalslaaetgcpavvtlgsaadgslmetaqaaVPRE----DIVALGErDLAAILYTSGTTGRSKGAMLTHKNLAS 184
Cdd:cd05903 79 -------------------------------------VPERfrqfDPAAMPD-AVALLLFTSGTTGEPKGVMHSHNTLSA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 185 NAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDAD---VIFEElPRGTVMMGVPTFYTRLVQD 261
Cdd:cd05903 121 SIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDkalALMRE-HGVTFMMGATPFLTDLLNA 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 262 ERLTPEATANMRLFVSGSAP----LTAETHEAFEAKtghaILERYGMTETNMNLSNPYDG--ARRAGTVGMPLPGVEMRI 335
Cdd:cd05903 200 VEEAGEPLSRLRTFVCGGATvprsLARRAAELLGAK----VCSAYGSTECPGAVTSITPApeDRRLYTDGRPLPGVEIKV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 336 TNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELlDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKE 415
Cdd:cd05903 276 VD-DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAA-PEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 416 VEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGENQLEEekvitHLDG-RLAKYKQPKRVFFVDELPRNTMG 494
Cdd:cd05903 354 VEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVA-----YLDRqGVAKQYWPERLVHVDDLPRTPSG 428
|
....*....
gi 2136495511 495 KVQKNELRK 503
Cdd:cd05903 429 KVQKFRLRE 437
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
25-502 |
1.62e-92 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 291.19 E-value: 1.62e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 25 RDGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLND----- 99
Cdd:cd05959 25 DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDsrarv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 100 --AEPALFvcrPKIEEqALSLAAETGCPAVVTLGSAADGSLMETAQ---AAVPREDIVALGERDLAAILYTSGTTGRSKG 174
Cdd:cd05959 105 vvVSGELA---PVLAA-ALTKSEHTLVVLIVSGGAGPEAGALLLAElvaAEAEQLKPAATHADDPAFWLYSSGSTGRPKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 175 AMLTHKNLASNAKTLAR-AWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKF-DADVIFEELPRG--TVMMG 250
Cdd:cd05959 181 VVHLHADIYWTAELYARnVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERpTPAAVFKRIRRYrpTVFFG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 251 VPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTET-NMNLSNpYDGARRAGTVGMPLP 329
Cdd:cd05959 261 VPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMlHIFLSN-RPGRVRYGTTGKPVP 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 330 GVEMRITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLdDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGY 409
Cdd:cd05959 340 GYEVELRD-EDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ-GEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 410 NVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGENqLEEEkVITHLDGRLAKYKQPKRVFFVDELP 489
Cdd:cd05959 418 WVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEA-LEEE-LKEFVKDRLAPYKYPRWIVFVDELP 495
|
490
....*....|...
gi 2136495511 490 RNTMGKVQKNELR 502
Cdd:cd05959 496 KTATGKIQRFKLR 508
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
162-502 |
5.70e-92 |
|
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: 284.17 E-value: 5.70e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 162 ILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFL-PKFDADVIFE 240
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPsPSFDPLAVLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 241 EL--PRGTVMMGVPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTG-HAILERYGMTETN--MNLSNPY 315
Cdd:cd05917 87 AIekEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNmKDVTIAYGMTETSpvSTQTRTD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 316 DGA-RRAGTVGMPLPGVEMRITNRETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYV 394
Cdd:cd05917 167 DSIeKRVNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 395 HIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGAdlgenQLEEEKVITHLDGRLA 474
Cdd:cd05917 247 RIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGA-----ELTEEDIKAYCKGKIA 321
|
330 340
....*....|....*....|....*...
gi 2136495511 475 KYKQPKRVFFVDELPRNTMGKVQKNELR 502
Cdd:cd05917 322 HYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
16-504 |
2.07e-91 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 287.47 E-value: 2.07e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 16 RAEADFITTRD---GRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDE 92
Cdd:PRK09088 6 RLQPQRLAAVDlalGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 93 IRYFLNDAEPALFVcrpkieEQALSLAAETGCPAVVTLGSAADGSLMETAQAAVPreDIVALgerdlaaILYTSGTTGRS 172
Cdd:PRK09088 86 LDALLQDAEPRLLL------GDDAVAAGRTDVEDLAAFIASADALEPADTPSIPP--ERVSL-------ILFTSGTSGQP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 173 KGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDADVIFEELPRG----TVM 248
Cdd:PRK09088 151 KGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLGDPalgiTHY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 249 MGVPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKtGHAILERYGMTETNMNLSNPYDGAR---RAGTVG 325
Cdd:PRK09088 231 FCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMSEAGTVFGMSVDCDViraKAGAAG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 326 MPLPGVEMRITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVI 405
Cdd:PRK09088 310 IPTPTVQTRVVD-DQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 406 SGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGE-GVTAVVVRQQGAdlgenqLEEEKVITHLDGRLAKYKQPKRVFF 484
Cdd:PRK09088 389 SGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEvGYLAIVPADGAP------LDLERIRSHLSTRLAKYKVPKHLRL 462
|
490 500
....*....|....*....|
gi 2136495511 485 VDELPRNTMGKVQKNELRKR 504
Cdd:PRK09088 463 VDALPRTASGKLQKARLRDA 482
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
26-505 |
2.36e-91 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 288.42 E-value: 2.36e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 26 DGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALF 105
Cdd:PRK06188 34 GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGISTL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 106 VCRP-KIEEQALSLAAE-TGCPAVVTLGSAADGS-LMETAQAAVPREDIVALGERDLAAILYTSGTTGRSKGAMLTHKNL 182
Cdd:PRK06188 114 IVDPaPFVERALALLARvPSLKHVLTLGPVPDGVdLLAAAAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 183 ASNAKTLARAWHFSADDRLIHALPIFHTHGLFVAcnVTLMAGASMLFLPKFDA----DVIFEElpRGTVMMGVPTFYTRL 258
Cdd:PRK06188 194 ATMAQIQLAEWEWPADPRFLMCTPLSHAGGAFFL--PTLLRGGTVIVLAKFDPaevlRAIEEQ--RITATFLVPTMIYAL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 259 VQDERLTPEATANMRLFVSGSAPLT----AETHEAFeaktGHAILERYGMTETNMNLS------NPYDGARRAGTVGMPL 328
Cdd:PRK06188 270 LDHPDLRTRDLSSLETVYYGASPMSpvrlAEAIERF----GPIFAQYYGQTEAPMVITylrkrdHDPDDPKRLTSCGRPT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 329 PGVEMRITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTrEELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGG 408
Cdd:PRK06188 346 PGLRVALLD-EDGREVAQGEVGEICVRGPLVMDGYWNRPEET-AEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGG 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 409 YNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGENQLEEekvitHLDGRLAKYKQPKRVFFVDEL 488
Cdd:PRK06188 424 FNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQA-----HVKERKGSVHAPKQVDFVDSL 498
|
490
....*....|....*..
gi 2136495511 489 PRNTMGKVQKNELRKRF 505
Cdd:PRK06188 499 PLTALGKPDKKALRARY 515
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
5-504 |
6.28e-90 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 285.94 E-value: 6.28e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 5 LFETFAAKMRERaeaDFITTRD-GRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLP 83
Cdd:PRK08315 21 LLDRTAARYPDR---EALVYRDqGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 84 LNTGYTGDEIRYFLNDAEPALFVC----------------RPKIEEQALSLAAETGCPA---VVTLGSAADGSLMETAQ- 143
Cdd:PRK08315 98 INPAYRLSELEYALNQSGCKALIAadgfkdsdyvamlyelAPELATCEPGQLQSARLPElrrVIFLGDEKHPGMLNFDEl 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 144 ----AAVPREDIVALGER----DLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFV 215
Cdd:PRK08315 178 lalgRAVDDAELAARQATldpdDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPLYHCFGMVL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 216 ACNVTLMAGASMLF-LPKFDA----DVIFEElpRGTVMMGVPT-FYTRLVQDER----LTPEATANMrlfvSGSaPLTAE 285
Cdd:PRK08315 258 GNLACVTHGATMVYpGEGFDPlatlAAVEEE--RCTALYGVPTmFIAELDHPDFarfdLSSLRTGIM----AGS-PCPIE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 286 THEAFEAKTG-HAILERYGMTETN--MNLSNPYDG-ARRAGTVGMPLPGVEMRITNRETGAEVPFGEIGMLQIRGPNVFI 361
Cdd:PRK08315 331 VMKRVIDKMHmSEVTIAYGMTETSpvSTQTRTDDPlEKRVTTVGRALPHLEVKIVDPETGETVPRGEQGELCTRGYSVMK 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 362 GYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGE 441
Cdd:PRK08315 411 GYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGE 490
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2136495511 442 GVTAVVVRQQGADlgenqLEEEKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRKR 504
Cdd:PRK08315 491 EVCAWIILRPGAT-----LTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREM 548
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
7-504 |
2.40e-87 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 278.96 E-value: 2.40e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 7 ETFAAKMRERAEADFITTRD-GRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLN 85
Cdd:PRK12583 22 DAFDATVARFPDREALVVRHqALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNIN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 86 TGYTGDEIRYFLNDAEPALFVCRPK-------------IEEQALSLAAETGCP------AVVTLGSAADGSL-----MET 141
Cdd:PRK12583 102 PAYRASELEYALGQSGVRWVICADAfktsdyhamlqelLPGLAEGQPGALACErlpelrGVVSLAPAPPPGFlawheLQA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 142 AQAAVPREDI----VALGERDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVAc 217
Cdd:PRK12583 182 RGETVSREALaerqASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLA- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 218 NVTLMAGASMLFLPK--FDADVIFE--ELPRGTVMMGVPT-FYTRLVQDERLTPEATAnMRLFVSGSAP--------LTA 284
Cdd:PRK12583 261 NLGCMTVGACLVYPNeaFDPLATLQavEEERCTALYGVPTmFIAELDHPQRGNFDLSS-LRTGIMAGAPcpievmrrVMD 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 285 ETHEAfeaktghAILERYGMTETN--MNLSNPYDG-ARRAGTVGMPLPGVEMRITNREtGAEVPFGEIGMLQIRGPNVFI 361
Cdd:PRK12583 340 EMHMA-------EVQIAYGMTETSpvSLQTTAADDlERRVETVGRTQPHLEVKVVDPD-GATVPRGEIGELCTRGYSVMK 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 362 GYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGE 441
Cdd:PRK12583 412 GYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGE 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2136495511 442 GVTAVVVRQQGadlgeNQLEEEKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRKR 504
Cdd:PRK12583 492 EIVAWVRLHPG-----HAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREI 549
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
39-504 |
3.85e-87 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 276.46 E-value: 3.85e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 39 SAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEpALFVcrpkieeqalsL 118
Cdd:PRK03640 37 VVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAE-VKCL-----------I 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 119 AAETGCPAVVTLGSAADGSLMETAQAAV-PREDIvalGERDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSA 197
Cdd:PRK03640 105 TDDDFEAKLIPGISVKFAELMNGPKEEAeIQEEF---DLDEVATIMYTSGTTGKPKGVIQTYGNHWWSAVGSALNLGLTE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 198 DDRLIHALPIFHTHGLFVACNvTLMAGASMLFLPKFDADVIFEELPRG--TVMMGVPTFYTRLVQDerlTPEAT--ANMR 273
Cdd:PRK03640 182 DDCWLAAVPIFHISGLSILMR-SVIYGMRVVLVEKFDAEKINKLLQTGgvTIISVVSTMLQRLLER---LGEGTypSSFR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 274 LFVSGSAPLTAETHEAFEAKtGHAILERYGMTETNMNLS--NPYDGARRAGTVGMPLPGVEMRItnRETGAEVPFGEIGM 351
Cdd:PRK03640 258 CMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETASQIVtlSPEDALTKLGSAGKPLFPCELKI--EKDGVVVPPFEEGE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 352 LQIRGPNVFIGYWRMPEKTrEELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAV 431
Cdd:PRK03640 335 IVVKGPNVTKGYLNREDAT-RETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGV 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2136495511 432 IGLPHPDFGEGVTAVVVRQQGADlgenqleEEKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRKR 504
Cdd:PRK03640 414 VGVPDDKWGQVPVAFVVKSGEVT-------EEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
14-503 |
2.66e-86 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 276.24 E-value: 2.66e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 14 RERAEADFITTRDGRRYRYTDAL--TISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGD 91
Cdd:PRK06087 32 TARAMPDKIAVVDNHGASYTYSAldHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 92 EIRYFLNDAEPALFVCRPKI-----EEQALSLAAE----TGCPAVVTLGSA-ADGSLMETAQAAVPREDIVALGERDLAA 161
Cdd:PRK06087 112 ELVWVLNKCQAKMFFAPTLFkqtrpVDLILPLQNQlpqlQQIVGVDKLAPAtSSLSLSQIIADYEPLTTAITTHGDELAA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 162 ILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDADVIFEE 241
Cdd:PRK06087 192 VLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLAL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 242 LPRG--TVMMGVPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAE-THEAFEAktGHAILERYGMTETN----MNLSNP 314
Cdd:PRK06087 272 LEQQrcTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKvARECQQR--GIKLLSVYGSTESSphavVNLDDP 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 315 YDgaRRAGTVGMPLPGVEMRITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYV 394
Cdd:PRK06087 350 LS--RFMHTDGYAAAGVEIKVVD-EARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYI 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 395 HIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQgadlGENQLEEEKVITHL-DGRL 473
Cdd:PRK06087 427 KITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKA----PHHSLTLEEVVAFFsRKRV 502
|
490 500 510
....*....|....*....|....*....|
gi 2136495511 474 AKYKQPKRVFFVDELPRNTMGKVQKNELRK 503
Cdd:PRK06087 503 AKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
39-505 |
5.36e-86 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 275.12 E-value: 5.36e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 39 SAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVCRPKIEEQALSL 118
Cdd:PRK07786 52 VAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAPVATAV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 119 -AAETGCPAVVTLGSAADGSLM---ETAQAAVPREDIVALGERDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWH 194
Cdd:PRK07786 132 rDIVPLLSTVVVAGGSSDDSVLgyeDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 195 -FSADDRLIHALPIFHTHGLFvACNVTLMAGASMLFLP--KFDADVIFE--ELPRGTVMMGVPTFYTRLVQDERLTPEAT 269
Cdd:PRK07786 212 aDINSDVGFVGVPLFHIAGIG-SMLPGLLLGAPTVIYPlgAFDPGQLLDvlEAEKVTGIFLVPAQWQAVCAEQQARPRDL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 270 AnMRLFVSGSAPLT-AETHEAFEAKTGHAILERYGMTE----TNMNLSNpyDGARRAGTVGMPLPGVEMRITNrETGAEV 344
Cdd:PRK07786 291 A-LRVLSWGAAPASdTLLRQMAATFPEAQILAAFGQTEmspvTCMLLGE--DAIRKLGSVGKVIPTVAARVVD-ENMNDV 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 345 PFGEIGMLQIRGPNVFIGYWRMPEKTREELlDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELD 424
Cdd:PRK07786 367 PVGEVGEIVYRAPTLMSGYWNNPEATAEAF-AGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHP 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 425 QVAESAVIGLPHPDFGE-GVTAVVVRQQGADLGENQLEEekvitHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRK 503
Cdd:PRK07786 446 DIVEVAVIGRADEKWGEvPVAVAAVRNDDAALTLEDLAE-----FLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRE 520
|
..
gi 2136495511 504 RF 505
Cdd:PRK07786 521 RY 522
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
26-505 |
5.69e-86 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 273.70 E-value: 5.69e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 26 DGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALF 105
Cdd:PRK08276 8 SGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 106 VCRPKIEEQALSLAAET--GCPAVVTLGSAADGSL-METAQAAVPREDI--VALGerdlAAILYTSGTTGRSKGAM--LT 178
Cdd:PRK08276 88 IVSAALADTAAELAAELpaGVPLLLVVAGPVPGFRsYEEALAAQPDTPIadETAG----ADMLYSSGTTGRPKGIKrpLP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 179 HK----NLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLfLPKFDADVIFE--ELPRGTVMMGVP 252
Cdd:PRK08276 164 GLdpdeAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAPLRFGMSALALGGTVVV-MEKFDAEEALAliERYRVTHSQLVP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 253 TFYTRLVqdeRLTPEATA-----NMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNM-NLSNPYDGARRAGTVGM 326
Cdd:PRK08276 243 TMFVRML---KLPEEVRArydvsSLRVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSEGGGvTVITSEDWLAHPGSVGK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 327 PLPGvEMRITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVIS 406
Cdd:PRK08276 320 AVLG-EVRILD-EDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIIS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 407 GGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGEnQLEEEkVITHLDGRLAKYKQPKRVFFVD 486
Cdd:PRK08276 398 GGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGD-ALAAE-LIAWLRGRLAHYKCPRSIDFED 475
|
490
....*....|....*....
gi 2136495511 487 ELPRNTMGKVQKNELRKRF 505
Cdd:PRK08276 476 ELPRTPTGKLYKRRLRDRY 494
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
42-503 |
8.94e-85 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 271.53 E-value: 8.94e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 42 LAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVCRPKIEEQA-LSLAA 120
Cdd:PRK07470 45 LAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMICHADFPEHAaAVRAA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 121 ETGCPAVVTLGSAADGSLMETAQAAVP--REDIVALGERDLAAILYTSGTTGRSKGAMLTHKNLA---SNaktlarawHF 195
Cdd:PRK07470 125 SPDLTHVVAIGGARAGLDYEALVARHLgaRVANAAVDHDDPCWFFFTSGTTGRPKAAVLTHGQMAfviTN--------HL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 196 -------SADDRLIHALPIFHTHGLFVACNVTlmAGASMLFLP--KFDADVIFE--ELPRGTVMMGVPTFYTRLVQDERL 264
Cdd:PRK07470 197 adlmpgtTEQDASLVVAPLSHGAGIHQLCQVA--RGAATVLLPseRFDPAEVWAlvERHRVTNLFTVPTILKMLVEHPAV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 265 TPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNMN-------LSNPYDG-ARRAGTVGMPLPGVEMRIT 336
Cdd:PRK07470 275 DRYDHSSLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVTGNitvlppaLHDAEDGpDARIGTCGFERTGMEVQIQ 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 337 NREtGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTrEELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEV 416
Cdd:PRK07470 355 DDE-GRELPPGETGEICVIGPAVFAGYYNNPEAN-AKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREI 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 417 EQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGAdlgenQLEEEKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKV 496
Cdd:PRK07470 433 EEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGA-----PVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKI 507
|
....*..
gi 2136495511 497 QKNELRK 503
Cdd:PRK07470 508 TKKMVRE 514
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
39-503 |
1.22e-84 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 268.05 E-value: 1.22e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 39 SAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVCrpkieeqalsl 118
Cdd:cd05972 10 SAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT----------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 119 aaetgcpavvtlgsaadgslmetaqaavpredivalGERDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSAD 198
Cdd:cd05972 79 ------------------------------------DAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 199 DrlIH---ALPIFHTHGLFVACNVTLMAGASMLF-LPKFDADVIFEELPR--GTVMMGVPTFYTRLVQdERLTPEATANM 272
Cdd:cd05972 123 D--IHwniADPGWAKGAWSSFFGPWLLGATVFVYeGPRFDAERILELLERygVTSFCGPPTAYRMLIK-QDLSSYKFSHL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 273 RLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNMNLSNPYDGARRAGTVGMPLPGVEMRITNREtGAEVPFGEIGML 352
Cdd:cd05972 200 RLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDD-GRELPPGEEGDI 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 353 QIRGPNV--FIGYWRMPEKTREELLDDgFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESA 430
Cdd:cd05972 279 AIKLPPPglFLGYVGDPEKTEASIRGD-YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAA 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2136495511 431 VIGLPHPDFGEGVTAVVVRQQGAdLGENQLEEEkVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRK 503
Cdd:cd05972 358 VVGSPDPVRGEVVKAFVVLTSGY-EPSEELAEE-LQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
32-496 |
2.32e-83 |
|
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: 264.73 E-value: 2.32e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 32 YTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPAlfvcrpki 111
Cdd:cd05935 4 YLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAK-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 112 eeqalslaaetgcpaVVTLGSAADgslmetaqaavpredivalgerDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLAR 191
Cdd:cd05935 76 ---------------VAVVGSELD----------------------DLALIPYTSGTTGLPKGCMHTHFSAAANALQSAV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 192 AWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDADVIFE--ELPRGTVMMGVPTFYTRLVQDERLTPEAT 269
Cdd:cd05935 119 WTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALEliEKYKVTFWTNIPTMLVDLLATPEFKTRDL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 270 ANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTET-NMNLSNPYdGARRAGTVGMPLPGVEMRITNRETGAEVPFGE 348
Cdd:cd05935 199 SSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETmSQTHTNPP-LRPKLQCLGIP*FGVDARVIDIETGRELPPNE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 349 IGMLQIRGPNVFIGYWRMPEKTREELLDDG---FFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQ 425
Cdd:cd05935 278 VGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPA 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2136495511 426 VAESAVIGLPHPDFGEGVTAVVVRQQGAdlgENQLEEEKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKV 496
Cdd:cd05935 358 I*EVCVISVPDERVGEEVKAFIVLRPEY---RGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKI 425
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
3-487 |
3.16e-83 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 269.66 E-value: 3.16e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 3 HNLFETFAAKMRERAEADFITTRDGRRYR---YTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGG 79
Cdd:COG1022 11 DTLPDLLRRRAARFPDRVALREKEDGIWQsltWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 80 VYLPLNTGYTGDEIRYFLNDAEP-ALFVCRPKIEEQALSLAAEtgCPA---VVTLgsaaDGSLMETAQAAVPREDIVALG 155
Cdd:COG1022 91 VTVPIYPTSSAEEVAYILNDSGAkVLFVEDQEQLDKLLEVRDE--LPSlrhIVVL----DPRGLRDDPRLLSLDELLALG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 156 ER-----------------DLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHT--HGLFVA 216
Cdd:COG1022 165 REvadpaelearraavkpdDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVfeRTVSYY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 217 CnvtLMAGASMLFLPkfDADVIFEELP--RGTVMMGVP----TFYTRLVQ------------------------DERLTP 266
Cdd:COG1022 245 A---LAAGATVAFAE--SPDTLAEDLRevKPTFMLAVPrvweKVYAGIQAkaeeagglkrklfrwalavgrryaRARLAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 267 EATA------------------------NMRLFVSGSAPLTAETHEAFEAkTGHAILERYGMTET----NMNlsnpYDGA 318
Cdd:COG1022 320 KSPSlllrlkhaladklvfsklrealggRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETspviTVN----RPGD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 319 RRAGTVGMPLPGVEMRItnretgaevpfGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVG 398
Cdd:COG1022 395 NRIGTVGPPLPGVEVKI-----------AEDGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITG 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 399 RDKDLVI-SGGYNVYPKEVEQVIDELDQVAESAVIglphpdfGEG---VTAVVV----------RQQG------ADLGEN 458
Cdd:COG1022 464 RKKDLIVtSGGKNVAPQPIENALKASPLIEQAVVV-------GDGrpfLAALIVpdfealgewaEENGlpytsyAELAQD 536
|
570 580 590
....*....|....*....|....*....|..
gi 2136495511 459 Q--LEE-EKVITHLDGRLAKYKQPKRVFFVDE 487
Cdd:COG1022 537 PevRALiQEEVDRANAGLSRAEQIKRFRLLPK 568
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
32-487 |
7.90e-83 |
|
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: 264.07 E-value: 7.90e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 32 YTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEpalfvcrpki 111
Cdd:cd05907 8 WAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSE---------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 112 eeqalslaaetgcpAVVTLGSAADgslmetaqaavpredivalgerDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLAR 191
Cdd:cd05907 78 --------------AKALFVEDPD----------------------DLATIIYTSGTTGRPKGVMLSHRNILSNALALAE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 192 AWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPkfDADVIFEELP--RGTVMMGVPTFYTRLVQDER--LTPE 267
Cdd:cd05907 122 RLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFAS--SAETLLDDLSevRPTVFLAVPRVWEKVYAAIKvkAVPG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 268 ---------ATANMRLFVSGSAPLTAEThEAFEAKTGHAILERYGMTETN--MNLSNPydGARRAGTVGMPLPGVEMRIT 336
Cdd:cd05907 200 lkrklfdlaVGGRLRFAASGGAPLPAEL-LHFFRALGIPVYEGYGLTETSavVTLNPP--GDNRIGTVGKPLPGVEVRIA 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 337 NRetgaevpfGEIgmlQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVI-SGGYNVYPKE 415
Cdd:cd05907 277 DD--------GEI---LVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIItSGGKNISPEP 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 416 VEQVIDELDQVAESAVIG--LPH------PDFgEGVTAVVVRQQGAD------LGENQLEE--EKVITHLDGRLAKYKQP 479
Cdd:cd05907 346 IENALKASPLISQAVVIGdgRPFlvalivPDP-EALEAWAEEHGIAYtdvaelAANPAVRAeiEAAVEAANARLSRYEQI 424
|
....*...
gi 2136495511 480 KRVFFVDE 487
Cdd:cd05907 425 KKFLLLPE 432
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
28-502 |
8.34e-83 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 266.92 E-value: 8.34e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 28 RRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVC 107
Cdd:PRK13295 54 RRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 108 rPKI------EEQALSLAAETgcPA---VVTLGSAADGS----LMETAQAAVPREDIVALGER----DLAAILYTSGTTG 170
Cdd:PRK13295 134 -PKTfrgfdhAAMARRLRPEL--PAlrhVVVVGGDGADSfealLITPAWEQEPDAPAILARLRpgpdDVTQLIYTSGTTG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 171 RSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFL----PKFDADVIFEElpRGT 246
Cdd:PRK13295 211 EPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQdiwdPARAAELIRTE--GVT 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 247 VMMGVPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNM-NLSNPYDGARRAGTV- 324
Cdd:PRK13295 289 FTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAvTLTKLDDPDERASTTd 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 325 GMPLPGVEMRITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREEllDDGFFITGDLAMVDEQGYVHIVGRDKDLV 404
Cdd:PRK13295 369 GCPLPGVEVRVVD-ADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTD--ADGWFDTGDLARIDADGYIRISGRSKDVI 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 405 ISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGenqLEEekVITHLDG-RLAKYKQPKRVF 483
Cdd:PRK13295 446 IRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLD---FEE--MVEFLKAqKVAKQYIPERLV 520
|
490
....*....|....*....
gi 2136495511 484 FVDELPRNTMGKVQKNELR 502
Cdd:PRK13295 521 VRDALPRTPSGKIQKFRLR 539
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
40-502 |
1.81e-82 |
|
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: 262.78 E-value: 1.81e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 40 AQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVcrpkieeqalsla 119
Cdd:cd05919 21 NRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVV------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 120 aetgcpavvtlgSAADgslmetaqaavpredivalgerDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLAR-AWHFSAD 198
Cdd:cd05919 88 ------------TSAD----------------------DIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAReALGLTPG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 199 DRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKF-DADVIFEELPR--GTVMMGVPTFYTRLVQDERLTPEATANMRLF 275
Cdd:cd05919 134 DRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWpTAERVLATLARfrPTVLYGVPTFYANLLDSCAGSPDALRSLRLC 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 276 VSGSAPLTAETHEAFEAKTGHAILERYGMTET-NMNLSNpYDGARRAGTVGMPLPGVEMRITNREtGAEVPFGEIGMLQI 354
Cdd:cd05919 214 VSAGEALPRGLGERWMEHFGGPILDGIGATEVgHIFLSN-RPGAWRLGSTGRPVPGYEIRLVDEE-GHTIPPGEEGDLLV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 355 RGPNVFIGYWRMPEKTREELLDdGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGL 434
Cdd:cd05919 292 RGPSAAVGYWNNPEKSRATFNG-GWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAV 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2136495511 435 PHPDFGEGVTAVVVRQQGADlgENQLEEEKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELR 502
Cdd:cd05919 371 PESTGLSRLTAFVVLKSPAA--PQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
48-502 |
4.24e-82 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 265.38 E-value: 4.24e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 48 ELGVKQGDRVAVQVdksPEaILLY----LACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVCRPKIEEQALSLAAETG 123
Cdd:PRK08974 68 GLGLKKGDRVALMM---PN-LLQYpialFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKTP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 124 CPAVV--TLG---SAADGSLMETA----QAAVPREDI---------VALGER-----------DLAAILYTSGTTGRSKG 174
Cdd:PRK08974 144 VKHVIltRMGdqlSTAKGTLVNFVvkyiKRLVPKYHLpdaisfrsaLHKGRRmqyvkpelvpeDLAFLQYTGGTTGVAKG 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 175 AMLTHKNLASN---AKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFL--PKfDADVIFEELPRG--TV 247
Cdd:PRK08974 224 AMLTHRNMLANleqAKAAYGPLLHPGKELVVTALPLYHIFALTVNCLLFIELGGQNLLItnPR-DIPGFVKELKKYpfTA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 248 MMGVPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNMNLS-NPYDGARRAGTVGM 326
Cdd:PRK08974 303 ITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSvNPYDLDYYSGSIGL 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 327 PLPGVEMRITNREtGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTrEELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVIS 406
Cdd:PRK08974 383 PVPSTEIKLVDDD-GNEVPPGEPGELWVKGPQVMLGYWQRPEAT-DEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILV 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 407 GGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQqgadlgENQLEEEKVITHLDGRLAKYKQPKRVFFVD 486
Cdd:PRK08974 461 SGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKK------DPSLTEEELITHCRRHLTGYKVPKLVEFRD 534
|
490
....*....|....*.
gi 2136495511 487 ELPRNTMGKVQKNELR 502
Cdd:PRK08974 535 ELPKSNVGKILRRELR 550
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
39-501 |
7.79e-82 |
|
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: 261.23 E-value: 7.79e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 39 SAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVCRPKIEE---QA 115
Cdd:TIGR01923 9 AAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSLLEEkdfQA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 116 LSLAaETGCPavvtlgSAADGSLmetaQAAVPREDIvalgerdlAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHF 195
Cdd:TIGR01923 89 DSLD-RIEAA------GRYETSL----SASFNMDQI--------ATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 196 SADDRLIHALPIFHTHGLFVACNvTLMAGASMLFLPKFDAdvIFEELPRGTVMMG--VPTFYTRLVqDERLTPEataNMR 273
Cdd:TIGR01923 150 TEDDNWLLSLPLYHISGLSILFR-WLIEGATLRIVDKFNQ--LLEMIANERVTHIslVPTQLNRLL-DEGGHNE---NLR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 274 LFVSGSAPLTAETHEafEAKT-GHAILERYGMTETN---MNLSNPYDGARraGTVGMPLPGVEMRITNREtgaEVPFGEI 349
Cdd:TIGR01923 223 KILLGGSAIPAPLIE--EAQQyGLPIYLSYGMTETCsqvTTATPEMLHAR--PDVGRPLAGREIKIKVDN---KEGHGEI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 350 gmlQIRGPNVFIGYWRmPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAES 429
Cdd:TIGR01923 296 ---MVKGANLMKGYLY-QGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEA 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2136495511 430 AVIGLPHPDFGEGVTAVVVrqqgadlGENQLEEEKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNEL 501
Cdd:TIGR01923 372 VVVPKPDAEWGQVPVAYIV-------SESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
27-502 |
4.52e-81 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 262.78 E-value: 4.52e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 27 GRRYRYTDALTISAQLAGALT-ELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALF 105
Cdd:PRK05677 47 GKTLTYGELYKLSGAFAAWLQqHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKAL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 106 VCRPKIEEQALSLAAETGCPAVVT-----LGSAADGSLMETA-------------QAAVPREDIVALGER---------- 157
Cdd:PRK05677 127 VCLANMAHLAEKVLPKTGVKHVIVtevadMLPPLKRLLINAVvkhvkkmvpayhlPQAVKFNDALAKGAGqpvteanpqa 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 158 -DLAAILYTSGTTGRSKGAMLTHKNLASN---AKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPK- 232
Cdd:PRK05677 207 dDVAVLQYTGGTTGVAKGAMLTHRNLVANmlqCRALMGSNLNEGCEILIAPLPLYHIYAFTFHCMAMMLIGNHNILISNp 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 233 FDADVIFEELP--RGTVMMGVPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNMN 310
Cdd:PRK05677 287 RDLPAMVKELGkwKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPV 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 311 LS-NPYDGARrAGTVGMPLPGVEMRITNREtGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVD 389
Cdd:PRK05677 367 VSvNPSQAIQ-VGTIGIPVPSTLCKVIDDD-GNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQ 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 390 EQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGENQLEEekvitHL 469
Cdd:PRK05677 445 EDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVME-----HM 519
|
490 500 510
....*....|....*....|....*....|...
gi 2136495511 470 DGRLAKYKQPKRVFFVDELPRNTMGKVQKNELR 502
Cdd:PRK05677 520 RANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
7-507 |
7.62e-81 |
|
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: 261.23 E-value: 7.62e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 7 ETFAAKMRERAEA--DFITTRDG-RRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVylP 83
Cdd:COG1021 25 ETLGDLLRRRAERhpDRIAVVDGeRRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI--P 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 84 LNT--GYTGDEIRYFLNDAEPALFVCRPKIEE-QALSLAAE--TGCPA---VVTLGSAADG-SLMETAQAAVPrEDIVAL 154
Cdd:COG1021 103 VFAlpAHRRAEISHFAEQSEAVAYIIPDRHRGfDYRALARElqAEVPSlrhVLVVGDAGEFtSLDALLAAPAD-LSEPRP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 155 GERDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLfvACNV---TLMAGASMLFLP 231
Cdd:COG1021 182 DPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHNFPL--SSPGvlgVLYAGGTVVLAP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 232 KFDADVIFE--ELPRGTVMMGVPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNM 309
Cdd:COG1021 260 DPSPDTAFPliERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAEGLV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 310 NLSNPYDGA-RRAGTVGMPL-PGVEMRITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAM 387
Cdd:COG1021 340 NYTRLDDPEeVILTTQGRPIsPDDEVRIVD-EDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVR 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 388 VDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRqQGADLGENQLEEekvit 467
Cdd:COG1021 419 RTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVP-RGEPLTLAELRR----- 492
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2136495511 468 HLDGR-LAKYKQPKRVFFVDELPRNTMGKVQKNELRKRFND 507
Cdd:COG1021 493 FLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALAA 533
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
15-503 |
1.39e-80 |
|
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: 260.26 E-value: 1.39e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 15 ERAEADF----ITTRDG----RRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNT 86
Cdd:cd12119 3 EHAARLHgdreIVSRTHegevHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 87 GYTGDEIRYFLNDAEP-ALFVCR---PKIEEQALSLAAETgcpAVVTLGSAADGSLMETAQ---------AAVPREDIVA 153
Cdd:cd12119 83 RLFPEQIAYIINHAEDrVVFVDRdflPLLEAIAPRLPTVE---HVVVMTDDAAMPEPAGVGvlayeellaAESPEYDWPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 154 LGERDLAAILYTSGTTGRSKGAMLTHKNL------ASNAKTLArawhFSADDRLIHALPIFHTH--GL-FVAcnvtLMAG 224
Cdd:cd12119 160 FDENTAAAICYTSGTTGNPKGVVYSHRSLvlhamaALLTDGLG----LSESDVVLPVVPMFHVNawGLpYAA----AMVG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 225 ASMLFL-PKFDADVIFE--ELPRGTVMMGVPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAK---TGHAi 298
Cdd:cd12119 232 AKLVLPgPYLDPASLAEliEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEERgvrVIHA- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 299 lerYGMTETN------------MNLSNPYDGARRAGTvGMPLPGVEMRITNRETGaEVPF--GEIGMLQIRGPNVFIGYW 364
Cdd:cd12119 311 ---WGMTETSplgtvarppsehSNLSEDEQLALRAKQ-GRPVPGVELRIVDDDGR-ELPWdgKAVGELQVRGPWVTKSYY 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 365 RMPEKTrEELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVT 444
Cdd:cd12119 386 KNDEES-EALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPL 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2136495511 445 AVVVRQQGADLGenqleEEKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRK 503
Cdd:cd12119 465 AVVVLKEGATVT-----AEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
5-502 |
1.30e-79 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 258.80 E-value: 1.30e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 5 LFETFAAKMRERAEadFITTRDGRRYRYTDALtiSAQLAGALTELGVKQGDRVAV---QVDKSPEAILlylACLRIGGVY 81
Cdd:PRK07059 28 LLEESFRQYADRPA--FICMGKAITYGELDEL--SRALAAWLQSRGLAKGARVAImmpNVLQYPVAIA---AVLRAGYVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 82 LPLNTGYTGDEIRYFLND--AEpALFVcrpkIE------EQALslaAETGCPAVVTlgsAADGSLM-----------ETA 142
Cdd:PRK07059 101 VNVNPLYTPRELEHQLKDsgAE-AIVV----LEnfattvQQVL---AKTAVKHVVV---ASMGDLLgfkghivnfvvRRV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 143 QAAVPREDI--------------------VALGERDLAAILYTSGTTGRSKGAMLTHKNLASNaKTLARAWHFSADDR-- 200
Cdd:PRK07059 170 KKMVPAWSLpghvrfndalaegarqtfkpVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVAN-VLQMEAWLQPAFEKkp 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 201 ------LIHALPIFHTHGLFVACNVTLMAGASMLFLPK-FDADVIFEELPRGTVMM--GVPTFYTRLVQDERLTPEATAN 271
Cdd:PRK07059 249 rpdqlnFVCALPLYHIFALTVCGLLGMRTGGRNILIPNpRDIPGFIKELKKYQVHIfpAVNTLYNALLNNPDFDKLDFSK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 272 MRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNMNLS-NPYDGARRAGTVGMPLPGVEMRITNrETGAEVPFGEIG 350
Cdd:PRK07059 329 LIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSPVATcNPVDATEFSGTIGLPLPSTEVSIRD-DDGNDLPLGEPG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 351 MLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESA 430
Cdd:PRK07059 408 EICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVA 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2136495511 431 VIGLPHPDFGEGVTAVVVRQQGAdlgenqLEEEKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELR 502
Cdd:PRK07059 488 AVGVPDEHSGEAVKLFVVKKDPA------LTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| pimA |
TIGR03205 |
dicarboxylate--CoA ligase PimA; PimA, a member of a large family of acyl-CoA ligases, is found ... |
125-502 |
4.62e-79 |
|
dicarboxylate--CoA ligase PimA; PimA, a member of a large family of acyl-CoA ligases, is found in a characteristic operon pimFABCDE for the metabolism of pimelate and related compounds. It is found, so far, in Bradyrhizobium japonicum and several strains of Rhodopseudomonas palustris. PimA from R. palustris was shown to be active as a CoA ligase for C(7) to C(14) dicarboxylates and fatty acids.
Pssm-ID: 132249 [Multi-domain] Cd Length: 541 Bit Score: 257.20 E-value: 4.62e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 125 PAVVTLGSAADGSlmeTAQAAVPredivALGERDLAAILYTSGTTGRSKGAMLTHKNLASnAKTLARAWHFSAD------ 198
Cdd:TIGR03205 168 PRIVTYADFVKGA---AAPAEWP-----AVTPDDVALLQYTGGTTGLPKGAMLTHGNLTS-AVSIYDVWGKPSRatrgdv 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 199 DRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDADVIFE--ELPRGTVMMGVPTFYTRLVQDERLTPEATANMRLFV 276
Cdd:TIGR03205 239 ERVICVLPLFHIYALTVILLRSLRRGDLISLHQRFDVAAVFRdiEEKRATVFPGVPTMWIALANDPSLEKRDLSSLATIG 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 277 SGSAPLTAETHEAFEAKTGHAILERYGMTET-NMNLSNPYDGARRAGTVGMPLPGVEMRITNRETGAEV-PFGEIGMLQI 354
Cdd:TIGR03205 319 SGGAPLPVEVANFFERKTGLKLKSGWGMTETcSPGTGHPPEGPDKPGSIGLMLPGIELDVVSLDDPTKVlPPGEVGELRI 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 355 RGPNVFIGYWRMPEKTREELLDDGfFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGL 434
Cdd:TIGR03205 399 RGPNVTRGYWNRPEESAEAFVGDR-FLTGDIGYMDTDGYFFLVDRKKDMIISGGFNVYPQMIEQAIYEHPGVQEVIVIGI 477
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2136495511 435 PHPDFGEGVTAVVVRQQGAD-LGENQLEEEkvithLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELR 502
Cdd:TIGR03205 478 PDQYRGEAAKAFVKLRPGAKpFSLDELRAF-----LAGKLGKHELPVAVEFVDELPRTPVGKLSRHELR 541
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
158-496 |
2.21e-78 |
|
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: 248.72 E-value: 2.21e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 158 DLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACnVTLMAGASMLFLPKFD--- 234
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLAL-ATFHAGGANVVMEKFDpae 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 235 -ADVIFEElpRGTVMMGVPTFYTRLVQDERLTPEATANMRLfVSG-SAPltaETHEAFEAKTGHAILERYGMTETNMNLS 312
Cdd:cd17637 80 aLELIEEE--KVTLMGSFPPILSNLLDAAEKSGVDLSSLRH-VLGlDAP---ETIQRFEETTGATFWSLYGQTETSGLVT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 313 -NPYDgaRRAGTVGMPLPGVEMRITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTrEELLDDGFFITGDLAMVDEQ 391
Cdd:cd17637 154 lSPYR--ERPGSAGRPGPLVRVRIVD-DNDRPVPAGETGEIVVRGPLVFQGYWNLPELT-AYTFRNGWHHTGDLGRFDED 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 392 GYVHIVGR--DKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGAdlgenQLEEEKVITHL 469
Cdd:cd17637 230 GYLWYAGRkpEKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGA-----TLTADELIEFV 304
|
330 340
....*....|....*....|....*..
gi 2136495511 470 DGRLAKYKQPKRVFFVDELPRNTMGKV 496
Cdd:cd17637 305 GSRIARYKKPRYVVFVEALPKTADGSI 331
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
27-504 |
6.84e-78 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 254.11 E-value: 6.84e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 27 GRRYRYTDALTISAQLAGAL-TELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALF 105
Cdd:PRK08314 33 GRAISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 106 VCRPKIEEQALSLAAETGCPAVV------TLGSAADGSLMETAQAAVPREDIV---------ALGER-----------DL 159
Cdd:PRK08314 113 IVGSELAPKVAPAVGNLRLRHVIvaqysdYLPAEPEIAVPAWLRAEPPLQALApggvvawkeALAAGlappphtagpdDL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 160 AAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDADVIF 239
Cdd:PRK08314 193 AVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMPRWDREAAA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 240 E--ELPRGTVMMGVPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTET-NMNLSNPYD 316
Cdd:PRK08314 273 RliERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTETmAQTHSNPPD 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 317 GARRaGTVGMPLPGVEMRITNRETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLD-DG--FFITGDLAMVDEQGY 393
Cdd:PRK08314 353 RPKL-QCLGIPTFGVDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFIEiDGkrFFRTGDLGRMDEEGY 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 394 VHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGAdlgENQLEEEKVITHLDGRL 473
Cdd:PRK08314 432 FFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEA---RGKTTEEEIIAWAREHM 508
|
490 500 510
....*....|....*....|....*....|.
gi 2136495511 474 AKYKQPKRVFFVDELPRNTMGKVQKNELRKR 504
Cdd:PRK08314 509 AAYKYPRIVEFVDSLPKSGSGKILWRQLQEQ 539
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
41-504 |
1.37e-75 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 250.26 E-value: 1.37e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 41 QLAGALTELGVKQGDRVAVQVDKSPEAILLYLAClRIGGVYLPLNtgytgdeiryflndaepalfvcrPKIE-EQALSLA 119
Cdd:PRK07529 70 RTANLLHSLGVGPGDVVAFLLPNLPETHFALWGG-EAAGIANPIN-----------------------PLLEpEQIAELL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 120 AETGCPAVVTLGSAADGSLMETAQAAV--------------------PREDIVALGER---------------------- 157
Cdd:PRK07529 126 RAAGAKVLVTLGPFPGTDIWQKVAEVLaalpelrtvvevdlarylpgPKRLAVPLIRRkaharildfdaelarqpgdrlf 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 158 --------DLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLF 229
Cdd:PRK07529 206 sgrpigpdDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 230 LPKF---DADVI--FEELP---RGTVMMGVPTFYTRLVQderlTPEATAN---MRLFVSGSAPLTAETHEAFEAKTGHAI 298
Cdd:PRK07529 286 ATPQgyrGPGVIanFWKIVeryRINFLSGVPTVYAALLQ----VPVDGHDissLRYALCGAAPLPVEVFRRFEAATGVRI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 299 LERYGMTETNMNLS-NPYDGARRAGTVGMPLPGVEMRITNR-ETGA---EVPFGEIGMLQIRGPNVFIGYWRmPEKTREE 373
Cdd:PRK07529 362 VEGYGLTEATCVSSvNPPDGERRIGSVGLRLPYQRVRVVILdDAGRylrDCAVDEVGVLCIAGPNVFSGYLE-AAHNKGL 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 374 LLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGA 453
Cdd:PRK07529 441 WLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGA 520
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2136495511 454 DLGENQLEEEkVITHLDGRLAkykQPKRVFFVDELPRNTMGKVQKNELRKR 504
Cdd:PRK07529 521 SATEAELLAF-ARDHIAERAA---VPKHVRILDALPKTAVGKIFKPALRRD 567
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
26-504 |
2.37e-75 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 247.36 E-value: 2.37e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 26 DGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALF 105
Cdd:PRK06155 43 GGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 106 VCR-PKIEEQALSLAAETGCPAVVTLGSAADGSLmETAQAAVP------REDIVALGERDLAAILYTSGTTGRSKGAMLT 178
Cdd:PRK06155 123 VVEaALLAALEAADPGDLPLPAVWLLDAPASVSV-PAGWSTAPlppldaPAPAAAVQPGDTAAILYTSGTTGPSKGVCCP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 179 HKNLASNAKTLARAWHFSADDRLIHALPIFHTHGL--FVAcnvTLMAGASMLFLPKFDADVIFEELPR--GTVMMGVPTF 254
Cdd:PRK06155 202 HAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALnaFFQ---ALLAGATYVLEPRFSASGFWPAVRRhgATVTYLLGAM 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 255 YTRLVQDERLTPEATANMRLFVSGSAPltAETHEAFEAKTGHAILERYGMTETNMNLSNPYdGARRAGTVGMPLPGVEMR 334
Cdd:PRK06155 279 VSILLSQPARESDRAHRVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTH-GSQRPGSMGRLAPGFEAR 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 335 ITNrETGAEVPFGEIGMLQIRG--PNVFI-GYWRMPEKTREElLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNV 411
Cdd:PRK06155 356 VVD-EHDQELPDGEPGELLLRAdePFAFAtGYFGMPEKTVEA-WRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENI 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 412 YPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGAdlgenQLEEEKVITHLDGRLAKYKQPKRVFFVDELPRN 491
Cdd:PRK06155 434 SSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGT-----ALEPVALVRHCEPRLAYFAVPRYVEFVAALPKT 508
|
490
....*....|...
gi 2136495511 492 TMGKVQKNELRKR 504
Cdd:PRK06155 509 ENGKVQKFVLREQ 521
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
39-502 |
2.00e-72 |
|
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: 237.34 E-value: 2.00e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 39 SAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGG----VYLPLNTGYTGDEIRYFLNDAEPALFVCRPKIEEQ 114
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGrlglVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 115 ALSLAAETGCPAVVTLGSAADGSlmETAQAAVPREDivalgeRDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWH 194
Cdd:cd05922 83 LRDALPASPDPGTVLDADGIRAA--RASAPAHEVSH------EDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 195 FSADDRLIHALPIFHTHGLFVaCNVTLMAGASMLFLPKFDADVIFEELPR---GTVMMGVPTFYTRLvqdERLT--PEAT 269
Cdd:cd05922 155 ITADDRALTVLPLSYDYGLSV-LNTHLLRGATLVLTNDGVLDDAFWEDLRehgATGLAGVPSTYAML---TRLGfdPAKL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 270 ANMRLFVSGSAPLTAETHEAF-EAKTGHAILERYGMTETNMNLS--NPYDGARRAGTVGMPLPGVEMRITNREtGAEVPF 346
Cdd:cd05922 231 PSLRYLTQAGGRLPQETIARLrELLPGAQVYVMYGQTEATRRMTylPPERILEKPGSIGLAIPGGEFEILDDD-GTPTPP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 347 GEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQV 426
Cdd:cd05922 310 GEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2136495511 427 AESAVIGLPhPDFGEGVTAVVVRQQGADLGEnqleeekVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELR 502
Cdd:cd05922 390 IEAAAVGLP-DPLGEKLALFVTAPDKIDPKD-------VLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
158-498 |
2.24e-71 |
|
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: 230.47 E-value: 2.24e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 158 DLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDADV 237
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 238 IFE--ELPRGTVMMGVPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTG-HAILERYGMTETNM-NLSN 313
Cdd:cd17638 81 ILEaiERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGfETVLTAYGLTEAGVaTMCR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 314 PYDGARR-AGTVGMPLPGVEMRItnretgaevpfGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQG 392
Cdd:cd17638 161 PGDDAETvATTCGRACPGFEVRI-----------ADDGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 393 YVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGAdlgenQLEEEKVITHLDGR 472
Cdd:cd17638 230 YLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGV-----TLTEEDVIAWCRER 304
|
330 340
....*....|....*....|....*.
gi 2136495511 473 LAKYKQPKRVFFVDELPRNTMGKVQK 498
Cdd:cd17638 305 LANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
27-505 |
4.53e-71 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 236.03 E-value: 4.53e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 27 GRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFV 106
Cdd:PLN02246 48 GRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLII 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 107 CRPKIEEQALSLAAETGCPaVVTLGSAADG-----SLMETAQAAVPREDIVAlgeRDLAAILYTSGTTGRSKGAMLTHKN 181
Cdd:PLN02246 128 TQSCYVDKLKGLAEDDGVT-VVTIDDPPEGclhfsELTQADENELPEVEISP---DDVVALPYSSGTTGLPKGVMLTHKG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 182 LASNAKTLARA----WHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDADVIFEELPRGTVMMG--VPTFY 255
Cdd:PLN02246 204 LVTSVAQQVDGenpnLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPKFEIGALLELIQRHKVTIApfVPPIV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 256 TRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAIL-ERYGMTET----NMNLS---NPYDgaRRAGTVGMP 327
Cdd:PLN02246 284 LAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMTEAgpvlAMCLAfakEPFP--VKSGSCGTV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 328 LPGVEMRITNRETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISG 407
Cdd:PLN02246 362 VRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYK 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 408 GYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGENQLEEekvitHLDGRLAKYKQPKRVFFVDE 487
Cdd:PLN02246 442 GFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQ-----FVAKQVVFYKRIHKVFFVDS 516
|
490
....*....|....*...
gi 2136495511 488 LPRNTMGKVQKNELRKRF 505
Cdd:PLN02246 517 IPKAPSGKILRKDLRAKL 534
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
32-502 |
5.43e-71 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 236.26 E-value: 5.43e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 32 YTDALTISAQLAGAL---TELgvKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVCR 108
Cdd:PRK12492 52 YAELERHSAAFAAYLqqhTDL--VPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 109 PKIEEQALSLAAETGCPAVVT-----LGSAADGSLMETA----QAAVP--------------------REDIVALGERDL 159
Cdd:PRK12492 130 NMFGKLVQEVLPDTGIEYLIEakmgdLLPAAKGWLVNTVvdkvKKMVPayhlpqavpfkqalrqgrglSLKPVPVGLDDI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 160 AAILYTSGTTGRSKGAMLTHKNLASNA-KTLARAWHFSAD---------DRLIHALPIFHTHGLFVACNVTLMAGA-SML 228
Cdd:PRK12492 210 AVLQYTGGTTGLAKGAMLTHGNLVANMlQVRACLSQLGPDgqplmkegqEVMIAPLPLYHIYAFTANCMCMMVSGNhNVL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 229 FLPKFDADVIFEELP--RGTVMMGVPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTE 306
Cdd:PRK12492 290 ITNPRDIPGFIKELGkwRFSALLGLNTLFVALMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 307 TN-MNLSNPYDGARRAGTVGMPLPGVEMRITNREtGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDL 385
Cdd:PRK12492 370 TSpVASTNPYGELARLGTVGIPVPGTALKVIDDD-GNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDI 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 386 AMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGAdlgenqLEEEKV 465
Cdd:PRK12492 449 AVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPG------LSVEEL 522
|
490 500 510
....*....|....*....|....*....|....*..
gi 2136495511 466 ITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELR 502
Cdd:PRK12492 523 KAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
49-502 |
1.30e-70 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 234.19 E-value: 1.30e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 49 LGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVCRPKIEEQALSLAAETGCP--- 125
Cdd:PRK08008 57 LGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPlrh 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 126 -AVVTLGSAADGSLM----ETAQAAVPREDIVALGERDLAAILYTSGTTGRSKGAMLTHKNLASNAktLARAWH--FSAD 198
Cdd:PRK08008 137 iCLTRVALPADDGVSsftqLKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAG--YYSAWQcaLRDD 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 199 DRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDADVIFEELP--RGTVMMGVPTFY-TRLVQ----DERltPEATAN 271
Cdd:PRK08008 215 DVYLTVMPAFHIDCQCTAAMAAFSAGATFVLLEKYSARAFWGQVCkyRATITECIPMMIrTLMVQppsaNDR--QHCLRE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 272 MRLFVsgsaPLTAETHEAFEAKTGHAILERYGMTETNMNL-SNPYDGARRAGTVGMPLPGVEMRITNrETGAEVPFGEIG 350
Cdd:PRK08008 293 VMFYL----NLSDQEKDAFEERFGVRLLTSYGMTETIVGIiGDRPGDKRRWPSIGRPGFCYEAEIRD-DHNRPLPAGEIG 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 351 MLQIRG---PNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVA 427
Cdd:PRK08008 368 EICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQ 447
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2136495511 428 ESAVIGLPHPDFGEGVTAVVVRQQGAdlgenQLEEEKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELR 502
Cdd:PRK08008 448 DIVVVGIKDSIRDEAIKAFVVLNEGE-----TLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
5-502 |
3.10e-70 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 234.39 E-value: 3.10e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 5 LFETFAAKMRER-AEADFITTRDgrrYRYTDALTisAQLAG-ALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYL 82
Cdd:PRK08751 30 VFATSVAKFADRpAYHSFGKTIT---YREADQLV--EQFAAyLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 83 PLNTGYTGDEIRYFLNDAEPALFVCRPKIEEQALSLAAETGCPAVVTLGSaadGSLMETAQAA------------VPRED 150
Cdd:PRK08751 105 NVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQVIADTPVKQVITTGL---GDMLGFPKAAlvnfvvkyvkklVPEYR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 151 I---------VALGER-----------DLAAILYTSGTTGRSKGAMLTHKNLASNAKTlARAWHFSAD------DRLIHA 204
Cdd:PRK08751 182 IngairfreaLALGRKhsmptlqiepdDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQ-AHQWLAGTGkleegcEVVITA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 205 LPIFHTHGLfVACNVTLM--AGASMLFLPKFDADVIFEELP--RGTVMMGVPTFYTRLVQDERLTPEATANMRLFVSGSA 280
Cdd:PRK08751 261 LPLYHIFAL-TANGLVFMkiGGCNHLISNPRDMPGFVKELKktRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGM 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 281 PLTAETHEAFEAKTGHAILERYGMTETNMNLS-NPYDGARRAGTVGMPLPGVEMRITNrETGAEVPFGEIGMLQIRGPNV 359
Cdd:PRK08751 340 AVQRSVAERWKQVTGLTLVEAYGLTETSPAACiNPLTLKEYNGSIGLPIPSTDACIKD-DAGTVLAIGEIGELCIKGPQV 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 360 FIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDF 439
Cdd:PRK08751 419 MKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKS 498
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2136495511 440 GEGVTAVVVRQQGAdlgenqLEEEKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELR 502
Cdd:PRK08751 499 GEIVKVVIVKKDPA------LTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
10-505 |
3.11e-70 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 234.55 E-value: 3.11e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 10 AAKMRERAEADFIttrdGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYT 89
Cdd:PRK06178 43 ARERPQRPAIIFY----GHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 90 GDEIRYFLNDAEPALFVC--------RPKIEEQALSLAAETG----CPAVVTL---------GSAADG--SLMEtAQAAV 146
Cdd:PRK06178 119 EHELSYELNDAGAEVLLAldqlapvvEQVRAETSLRHVIVTSladvLPAEPTLplpdslrapRLAAAGaiDLLP-ALRAC 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 147 PREDIVALGERD-LAAILYTSGTTGRSKGAMLTHKNLASNAKT-LARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAG 224
Cdd:PRK06178 198 TAPVPLPPPALDaLAALNYTGGTTGMPKGCEHTQRDMVYTAAAaYAVAVVGGEDSVFLSFLPEFWIAGENFGLLFPLFSG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 225 ASMLFLPKFDADVIFEELPRG--TVMMGVPTFYTRLVQderlTPEATA-NMRLF-----VSGSAPLTAETHEAFEAKTGH 296
Cdd:PRK06178 278 ATLVLLARWDAVAFMAAVERYrvTRTVMLVDNAVELMD----HPRFAEyDLSSLrqvrvVSFVKKLNPDYRQRWRALTGS 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 297 AILE-RYGMTETNMNLS-------NPYDGARRAGTVGMPLPGVEMRITNRETGAEVPFGEIGMLQIRGPNVFIGYWRMPE 368
Cdd:PRK06178 354 VLAEaAWGMTETHTCDTftagfqdDDFDLLSQPVFVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPE 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 369 KTREeLLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVV 448
Cdd:PRK06178 434 ATAE-ALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQ 512
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2136495511 449 RQQGADLGENQLEEEKVithldGRLAKYKQPKrVFFVDELPRNTMGKVQKNELRKRF 505
Cdd:PRK06178 513 LKPGADLTAAALQAWCR-----ENMAVYKVPE-IRIVDALPMTATGKVRKQDLQALA 563
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
29-502 |
1.26e-69 |
|
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: 229.24 E-value: 1.26e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 29 RYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPAlfvcr 108
Cdd:cd05971 6 KVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 109 pkieeqalslaaetgcpAVVTlgsaaDGSlmetaqaavpredivalgeRDLAAILYTSGTTGRSKGAMLTHKNLASNAKT 188
Cdd:cd05971 81 -----------------ALVT-----DGS-------------------DDPALIIYTSGTTGPPKGALHAHRVLLGHLPG 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 189 LARAWHF----------SADDRLIHAL-----PIFHtHGL-FVACNVTlmagasmlflpKFDADVIFEELPRGTVMMGV- 251
Cdd:cd05971 120 VQFPFNLfprdgdlywtPADWAWIGGLldvllPSLY-FGVpVLAHRMT-----------KFDPKAALDLMSRYGVTTAFl 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 252 -PTFYTRLVQDERLTPEATANMRLFVSGSAPLTAE----THEAFeaktGHAILERYGMTETNMNLSNPYD-GARRAGTVG 325
Cdd:cd05971 188 pPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEEllgwAREQF----GVEVNEFYGQTECNLVIGNCSAlFPIKPGSMG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 326 MPLPGVEMRITNREtGAEVPFGEIGMLQIRGPN--VFIGYWRMPEKTREELLDDgFFITGDLAMVDEQGYVHIVGRDKDL 403
Cdd:cd05971 264 KPIPGHRVAIVDDN-GTPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDDV 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 404 VISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGaDLGENQLEEEkVITHLDGRLAKYKQPKRVF 483
Cdd:cd05971 342 ITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPG-ETPSDALARE-IQELVKTRLAAHEYPREIE 419
|
490
....*....|....*....
gi 2136495511 484 FVDELPRNTMGKVQKNELR 502
Cdd:cd05971 420 FVNELPRTATGKIRRRELR 438
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
27-502 |
2.50e-69 |
|
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: 228.52 E-value: 2.50e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 27 GRRYRYTDALTISAQLAGALT-ELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALF 105
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 106 VCRPKIeeqalslaaetgcpavvtlgSAADgslmetaqaavpredivalgerDLAAILYTSGTTGRSKGAMLTHKNLASN 185
Cdd:cd05958 88 LCAHAL--------------------TASD----------------------DICILAFTSGTTGAPKATMHFHRDPLAS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 186 AKTLAR-AWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDADVIFEELPR--GTVMMGVPTFYTRLVQDE 262
Cdd:cd05958 126 ADRYAVnVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARykPTVLFTAPTAYRAMLAHP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 263 RLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTET-NMNLSNPYDGARrAGTVGMPLPGVEMRITNREtG 341
Cdd:cd05958 206 DAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMfHIFISARPGDAR-PGATGKPVPGYEAKVVDDE-G 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 342 AEVPFGEIGMLQIRGPNvfiGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVID 421
Cdd:cd05958 284 NPVPDGTIGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 422 ELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGENQLEEEKviTHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNEL 501
Cdd:cd05958 361 QHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARELQ--DHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
.
gi 2136495511 502 R 502
Cdd:cd05958 439 R 439
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
26-505 |
3.58e-69 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 229.97 E-value: 3.58e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 26 DGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALF 105
Cdd:PRK12406 8 GDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 106 V--------CRPKIEEQALSLAAETgcPAVVTLGSAADGSLMETAQAAVPREDIVALGE-------RDLAAILYTSGTTG 170
Cdd:PRK12406 88 IahadllhgLASALPAGVTVLSVPT--PPEIAAAYRISPALLTPPAGAIDWEGWLAQQEpydgppvPQPQSMIYTSGTTG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 171 RSKG---AMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHT----HGLFVAcnvtlMAGASMLFLPKFDADVIFE--E 241
Cdd:PRK12406 166 HPKGvrrAAPTPEQAAAAEQMRALIYGLKPGIRALLTGPLYHSapnaYGLRAG-----RLGGVLVLQPRFDPEELLQliE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 242 LPRGTVMMGVPTFYTRLVQ--DERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETN-MNLSNPYDGA 318
Cdd:PRK12406 241 RHRITHMHMVPTMFIRLLKlpEEVRAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGaVTFATSEDAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 319 RRAGTVGMPLPGVEMRITNrETGAEVPFGEIGMLQIRGP-NVFIGYWRMPEKtREELLDDGFFITGDLAMVDEQGYVHIV 397
Cdd:PRK12406 321 SHPGTVGKAAPGAELRFVD-EDGRPLPQGEIGEIYSRIAgNPDFTYHNKPEK-RAEIDRGGFITSGDVGYLDADGYLFLC 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 398 GRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGAdlgenQLEEEKVITHLDGRLAKYK 477
Cdd:PRK12406 399 DRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGA-----TLDEADIRAQLKARLAGYK 473
|
490 500
....*....|....*....|....*...
gi 2136495511 478 QPKRVFFVDELPRNTMGKVQKNELRKRF 505
Cdd:PRK12406 474 VPKHIEIMAELPREDSGKIFKRRLRDPY 501
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
41-506 |
4.87e-69 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 229.39 E-value: 4.87e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 41 QLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVCRpkiEEQALSLAA 120
Cdd:PRK06145 39 QAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVD---EEFDAIVAL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 121 ETgcpAVVTLGSAADGSLMETAQAAVPREDIVALGERDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDR 200
Cdd:PRK06145 116 ET---PKIVIDAAAQADSRRLAQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASER 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 201 LIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDADVIFEELPRGTVMMG--VPTFYTRLVQDERLTPEATANMRLFVSG 278
Cdd:PRK06145 193 LLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLAAIERHRLTCAwmAPVMLSRVLTVPDRDRFDLDSLAWCIGG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 279 SAPLTAETHEAF-EAKTGHAILERYGMTE-----TNMNLSNPYDgarRAGTVGMPLPGVEMRITNrETGAEVPFGEIGML 352
Cdd:PRK06145 273 GEKTPESRIRDFtRVFTRARYIDAYGLTEtcsgdTLMEAGREIE---KIGSTGRALAHVEIRIAD-GAGRWLPPNMKGEI 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 353 QIRGPNVFIGYWRMPEKTREELLDDgFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVI 432
Cdd:PRK06145 349 CMRGPKVTKGYWKDPEKTAEAFYGD-WFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVI 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2136495511 433 GLPHPDFGEGVTAVVVRQQGAdlgenQLEEEKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRKRFN 506
Cdd:PRK06145 428 GVHDDRWGERITAVVVLNPGA-----TLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDELN 496
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
26-504 |
4.99e-68 |
|
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: 226.44 E-value: 4.99e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 26 DGRRYRYTDALTiSAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVylPLNTGYTG--DEIRYFLNDAE-P 102
Cdd:cd05909 4 LGTSLTYRKLLT-GAIALARKLAKMTKEGENVGVMLPPSAGGALANFALALSGKV--PVMLNYTAglRELRACIKLAGiK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 103 ALFVCRPKIEEQALSLAAETGCPA-VVTLG------SAADGSLMETAQAAVPREDIVALG-----ERDLAAILYTSGTTG 170
Cdd:cd05909 81 TVLTSKQFIEKLKLHHLFDVEYDArIVYLEdlrakiSKADKCKAFLAGKFPPKWLLRIFGvapvqPDDPAVILFTSGSEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 171 RSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPK-FDADVIFE--ELPRGTV 247
Cdd:cd05909 161 LPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNpLDYKKIPEliYDKKATI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 248 MMGVPTFYTRLVQdeRLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETN----MNLSNPydgARRAGT 323
Cdd:cd05909 241 LLGTPTFLRGYAR--AAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSpvisVNTPQS---PNKEGT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 324 VGMPLPGVEMRITNRETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTrEELLDDGFFITGDLAMVDEQGYVHIVGRDKDL 403
Cdd:cd05909 316 VGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELT-SFAFGDGWYDTGDIGKIDGEGFLTITGRLSRF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 404 VISGGYNVYPKEVEQVIDE-LDQVAESAVIGLPHPDFGEGVTAVVVRqqgadlgeNQLEEEKVITHLD-GRLAKYKQPKR 481
Cdd:cd05909 395 AKIAGEMVSLEAIEDILSEiLPEDNEVAVVSVPDGRKGEKIVLLTTT--------TDTDPSSLNDILKnAGISNLAKPSY 466
|
490 500
....*....|....*....|...
gi 2136495511 482 VFFVDELPRNTMGKVQKNELRKR 504
Cdd:cd05909 467 IHQVEEIPLLGTGKPDYVTLKAL 489
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
42-503 |
2.12e-67 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 226.35 E-value: 2.12e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 42 LAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEI---------RYFLNDAEPAlfvcrpkie 112
Cdd:PRK07788 87 LARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLaevaaregvKALVYDDEFT--------- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 113 eqALSLAAETGCPAVVTLGSAADGSLMETAQAAVPREDIVALGERDLAA-------ILYTSGTTGRSKGAMLTH-KNLAS 184
Cdd:PRK07788 158 --DLLSALPPDLGRLRAWGGNPDDDEPSGSTDETLDDLIAGSSTAPLPKppkpggiVILTSGTTGTPKGAPRPEpSPLAP 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 185 NAKTLARAwHFSADDRLIHALPIFHTHGlFVACNVTLMAGASMLFLPKFDADVIFEELP--RGTVMMGVPTFYTRLVqde 262
Cdd:PRK07788 236 LAGLLSRV-PFRAGETTLLPAPMFHATG-WAHLTLAMALGSTVVLRRRFDPEATLEDIAkhKATALVVVPVMLSRIL--- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 263 RLTPEA-----TANMRL-FVSGSApLTAETHEAFEAKTGHAILERYGMTETN-MNLSNPYDGARRAGTVGMPLPGVEMRI 335
Cdd:PRK07788 311 DLGPEVlakydTSSLKIiFVSGSA-LSPELATRALEAFGPVLYNLYGSTEVAfATIATPEDLAEAPGTVGRPPKGVTVKI 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 336 TNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREelldDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKE 415
Cdd:PRK07788 390 LD-ENGNEVPRGVVGRIFVGNGFPFEGYTDGRDKQII----DGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAE 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 416 VEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGENQLEeekviTHLDGRLAKYKQPKRVFFVDELPRNTMGK 495
Cdd:PRK07788 465 VEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIK-----DYVRDNLARYKVPRDVVFLDELPRNPTGK 539
|
....*...
gi 2136495511 496 VQKNELRK 503
Cdd:PRK07788 540 VLKRELRE 547
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
39-504 |
4.38e-67 |
|
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: 225.04 E-value: 4.38e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 39 SAQLAGALTEL-GVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVCRPKIEEQALS 117
Cdd:cd05928 51 SRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 118 LAAEtgCPAVVT--LGSAA--DG--SLMETAQAAVPREDIVALGERDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLAR 191
Cdd:cd05928 131 VASE--CPSLKTklLVSEKsrDGwlNFKELLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 192 AW-HFSADDrlihalpIFHT---HGLFVACNVTLMA----GASMLF--LPKFDADVIFEELPRG--TVMMGVPTFYTRLV 259
Cdd:cd05928 209 YWlDLTASD-------IMWNtsdTGWIKSAWSSLFEpwiqGACVFVhhLPRFDPLVILKTLSSYpiTTFCGAPTVYRMLV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 260 QDErLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNMNLSNPYDGARRAGTVGMPLPGVEMRITNrE 339
Cdd:cd05928 282 QQD-LSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIID-D 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 340 TGAEVPFGEIGMLQIR-GPN----VFIGYWRMPEKTREELLDDgFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPK 414
Cdd:cd05928 360 NGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRGD-FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPF 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 415 EVEQVIDELDQVAESAVIGLPHPDFGEGVTA-VVVRQQGADLGENQLEEEkVITHLDGRLAKYKQPKRVFFVDELPRNTM 493
Cdd:cd05928 439 EVESALIEHPAVVESAVVSSPDPIRGEVVKAfVVLAPQFLSHDPEQLTKE-LQQHVKSVTAPYKYPRKVEFVQELPKTVT 517
|
490
....*....|.
gi 2136495511 494 GKVQKNELRKR 504
Cdd:cd05928 518 GKIQRNELRDK 528
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
39-431 |
5.45e-67 |
|
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: 221.37 E-value: 5.45e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 39 SAQLAGAL-TELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVCRPKIEEQALS 117
Cdd:TIGR01733 9 ANRLARHLrAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSALASRLAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 118 LAAETGCPAVVTLGSAADGSLMETAQAAVpredivalGERDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSA 197
Cdd:TIGR01733 89 LVLPVILLDPLELAALDDAPAPPPPDAPS--------GPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 198 DDRLIHalpiFHTHGlFVACN----VTLMAGASMLFLPKFDADVIFEELPRG------TVMMGVPTFYTRLVQDErltPE 267
Cdd:TIGR01733 161 DDRVLQ----FASLS-FDASVeeifGALLAGATLVVPPEDEERDDAALLAALiaehpvTVLNLTPSLLALLAAAL---PP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 268 ATANMRLFVSGSAPLTAETHEAFEAKTGHA-ILERYGMTET---NMNLSNPYDGARRAGTV--GMPLPGVEMRITNREtG 341
Cdd:TIGR01733 233 ALASLRLVILGGEALTPALVDRWRARGPGArLINLYGPTETtvwSTATLVDPDDAPRESPVpiGRPLANTRLYVLDDD-L 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 342 AEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGF--------FITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYP 413
Cdd:TIGR01733 312 RPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFaggdgarlYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIEL 391
|
410
....*....|....*...
gi 2136495511 414 KEVEQVIDELDQVAESAV 431
Cdd:TIGR01733 392 GEIEAALLRHPGVREAVV 409
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
7-501 |
1.44e-66 |
|
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: 222.59 E-value: 1.44e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 7 ETFAAKMRERAE--ADFITTRDG-RRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVylP 83
Cdd:cd05920 15 EPLGDLLARSAArhPDRIAVVDGdRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 84 LNT--GYTGDEIRYFLNDAEPALFVcrpkieeqalslaaetgcpavvtlgsaADGSLMETAQAAVPREdiVALGERDLAA 161
Cdd:cd05920 93 VLAlpSHRRSELSAFCAHAEAVAYI---------------------------VPDRHAGFDHRALARE--LAESIPEVAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 162 ILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIfhTHGLFVACNV---TLMAGASMLFLPKFDADVI 238
Cdd:cd05920 144 FLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPA--AHNFPLACPGvlgTLLAGGRVVLAPDPSPDAA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 239 FEELPRGTVMMG--VPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNMNLSNPYD 316
Cdd:cd05920 222 FPLIEREGVTVTalVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTRLDD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 317 -GARRAGTVGMPL-PGVEMRITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYV 394
Cdd:cd05920 302 pDEVIIHTQGRPMsPDDEIRVVD-EEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 395 HIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQgadlgeNQLEEEKVITHLDGR-L 473
Cdd:cd05920 381 VVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRD------PPPSAAQLRRFLRERgL 454
|
490 500
....*....|....*....|....*...
gi 2136495511 474 AKYKQPKRVFFVDELPRNTMGKVQKNEL 501
Cdd:cd05920 455 AAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
27-503 |
2.31e-66 |
|
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: 222.17 E-value: 2.31e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 27 GRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFV 106
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 107 CRPKIEEQALsLAAETGCPAVvtlgsaadgslmetaqaavpredIVALGERDLAAILYTSGTTGRSKGAMLTHKNLASNA 186
Cdd:cd12118 107 VDREFEYEDL-LAEGDPDFEW-----------------------IPPADEWDPIALNYTSGTTGRPKGVVYHHRGAYLNA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 187 KTLARAWHFSADDRLIHALPIFHTHGLfvaCNVTLMA--GASMLFLPKFDADVIFE--ELPRGTVMMGVPTFYTRLV--Q 260
Cdd:cd12118 163 LANILEWEMKQHPVYLWTLPMFHCNGW---CFPWTVAavGGTNVCLRKVDAKAIYDliEKHKVTHFCGAPTVLNMLAnaP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 261 DERLTPeATANMRLFVSGSAPlTAETHEAFEAKTGHaILERYGMTET--------------NMNLSNPYDGARRAGtVGM 326
Cdd:cd12118 240 PSDARP-LPHRVHVMTAGAPP-PAAVLAKMEELGFD-VTHVYGLTETygpatvcawkpewdELPTEERARLKARQG-VRY 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 327 PLPGvEMRITNRETGAEVP-----FGEIGMlqiRGPNVFIGYWRMPEKTREeLLDDGFFITGDLAMVDEQGYVHIVGRDK 401
Cdd:cd12118 316 VGLE-EVDVLDPETMKPVPrdgktIGEIVF---RGNIVMKGYLKNPEATAE-AFRGGWFHSGDLAVIHPDGYIEIKDRSK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 402 DLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADlgenqLEEEKVITHLDGRLAKYKQPKR 481
Cdd:cd12118 391 DIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAK-----VTEEEIIAFCREHLAGFMVPKT 465
|
490 500
....*....|....*....|..
gi 2136495511 482 VFFvDELPRNTMGKVQKNELRK 503
Cdd:cd12118 466 VVF-GELPKTSTGKIQKFVLRD 486
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
21-505 |
4.00e-66 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 222.26 E-value: 4.00e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 21 FITTRDGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDA 100
Cdd:PRK13391 16 VIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 101 EP-ALFVCRPKIEEQAlslAAETGCPAV---VTLGSAADGSLMETAQAAV------PREDivalgERDLAAILYTSGTTG 170
Cdd:PRK13391 96 GArALITSAAKLDVAR---ALLKQCPGVrhrLVLDGDGELEGFVGYAEAVaglpatPIAD-----ESLGTDMLYSSGTTG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 171 RSKG--AMLTHKNLASN---AKTLARAWHFSADDRLIHALPIFHTHGLFvACNVTLMAGASMLFLPKFDADVIFE--ELP 243
Cdd:PRK13391 168 RPKGikRPLPEQPPDTPlplTAFLQRLWGFRSDMVYLSPAPLYHSAPQR-AVMLVIRLGGTVIVMEHFDAEQYLAliEEY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 244 RGTVMMGVPTFYTRLVQderlTPEAT------ANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETN-MNLSNPYD 316
Cdd:PRK13391 247 GVTHTQLVPTMFSRMLK----LPEEVrdkydlSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGLgFTACDSEE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 317 GARRAGTVGMPLPGVeMRITNrETGAEVPFGEIGMLQIRGPNVFiGYWRMPEKTREELLDDGFFIT-GDLAMVDEQGYVH 395
Cdd:PRK13391 323 WLAHPGTVGRAMFGD-LHILD-DDGAELPPGEPGTIWFEGGRPF-EYLNDPAKTAEARHPDGTWSTvGDIGYVDEDGYLY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 396 IVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGEnQLEEEkVITHLDGRLAK 475
Cdd:PRK13391 400 LTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGP-ALAAE-LIAFCRQRLSR 477
|
490 500 510
....*....|....*....|....*....|
gi 2136495511 476 YKQPKRVFFVDELPRNTMGKVQKNELRKRF 505
Cdd:PRK13391 478 QKCPRSIDFEDELPRLPTGKLYKRLLRDRY 507
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
27-505 |
5.06e-65 |
|
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: 218.08 E-value: 5.06e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 27 GRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEP-ALF 105
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAkAIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 106 VCRPKieeqalslaaetgcpavvtlgsaadgslmetaqaavpredivalgerDLAAILYTSGTTGRSKGAMLTHKNLASN 185
Cdd:cd05914 85 VSDED-----------------------------------------------DVALINYTSGTTGNSKGVMLTYRNIVSN 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 186 AKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDAD-VIFEELPRGTVMMGVPTFY--------- 255
Cdd:cd05914 118 VDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAkIIALAFAQVTPTLGVPVPLviekifkmd 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 256 -------TRLVQDERLTPEAT---------------ANMRLFVSGSAPLTAEThEAFEAKTGHAILERYGMTETNMNLSN 313
Cdd:cd05914 198 iipkltlKKFKFKLAKKINNRkirklafkkvheafgGNIKEFVIGGAKINPDV-EEFLRTIGFPYTIGYGMTETAPIISY 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 314 PYDGARRAGTVGMPLPGVEMRITnretgAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGY 393
Cdd:cd05914 277 SPPNRIRLGSAGKVIDGVEVRID-----SPDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGY 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 394 VHIVGRDKDLVISG-GYNVYPKEVEQVIDELDQVAESAVI---------GLPHPDFgEGVTAVVVRqqgaDLGENQLEEe 463
Cdd:cd05914 352 LYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVLESLVVvqekklvalAYIDPDF-LDVKALKQR----NIIDAIKWE- 425
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2136495511 464 kVITHLDGRLAKYKQPKRVFFV-DELPRNTMGKVqknelrKRF 505
Cdd:cd05914 426 -VRDKVNQKVPNYKKISKVKIVkEEFEKTPKGKI------KRF 461
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
39-501 |
9.93e-65 |
|
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: 216.62 E-value: 9.93e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 39 SAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVCRPkieeqalsl 118
Cdd:cd05930 22 ANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLVLTDP--------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 119 aaetgcpavvtlgsaadgslmetaqaavpredivalgeRDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSAD 198
Cdd:cd05930 93 --------------------------------------DDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 199 DRLIH-ALPIF--HTHGLFVAcnvtLMAGASMLFLPKFD-------ADVIFEElpRGTVMMGVPTFYTRLVQDerLTPEA 268
Cdd:cd05930 135 DRVLQfTSFSFdvSVWEIFGA----LLAGATLVVLPEEVrkdpealADLLAEE--GITVLHLTPSLLRLLLQE--LELAA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 269 TANMRLFVSGSAPLTAET-HEAFEAKTGHAILERYGMTETNMNLS----NPYDGARRAGTVGMPLPGVEMRITNrETGAE 343
Cdd:cd05930 207 LPSLRLVLVGGEALPPDLvRRWRELLPGARLVNLYGPTEATVDATyyrvPPDDEEDGRVPIGRPIPNTRVYVLD-ENLRP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 344 VPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFI------TGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVE 417
Cdd:cd05930 286 VPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPgermyrTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 418 QVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGENQLEEekvitHLDGRLAKYKQPKRVFFVDELPRNTMGKVQ 497
Cdd:cd05930 366 AALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRA-----HLAERLPDYMVPSAFVVLDALPLTPNGKVD 440
|
....
gi 2136495511 498 KNEL 501
Cdd:cd05930 441 RKAL 444
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
158-505 |
4.76e-64 |
|
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: 211.04 E-value: 4.76e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 158 DLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVAcNVTLMAGASMLFLPKFDADV 237
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAIL-VRSLLAGAELVLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 238 IFEELPRGTVMMGVPTFYTRLVqDERLTPEATANMRLFVSGSAPLTAETHEAFEAKtGHAILERYGMTETNMNLSNPYDG 317
Cdd:cd17630 80 EDLAPPGVTHVSLVPTQLQRLL-DSGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTETASQVATKRPD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 318 ARRAGTVGMPLPGVEMRITNRetgaevpfgeiGMLQIRGPNVFIGYWRMPEktREELLDDGFFITGDLAMVDEQGYVHIV 397
Cdd:cd17630 158 GFGRGGVGVLLPGRELRIVED-----------GEIWVGGASLAMGYLRGQL--VPEFNEDGWFTTKDLGELHADGRLTVL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 398 GRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVrqqgadlGENQLEEEKVITHLDGRLAKYK 477
Cdd:cd17630 225 GRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIV-------GRGPADPAELRAWLKDKLARFK 297
|
330 340
....*....|....*....|....*...
gi 2136495511 478 QPKRVFFVDELPRNTMGKVQKNELRKRF 505
Cdd:cd17630 298 LPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
158-496 |
1.54e-62 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 221.34 E-value: 1.54e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 158 DLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLP-----K 232
Cdd:PRK08633 783 DTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYHPdptdaL 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 233 FDADVIFEElpRGTVMMGVPTF---YTRlvqDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETN- 308
Cdd:PRK08633 863 GIAKLVAKH--RATILLGTPTFlrlYLR---NKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSp 937
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 309 ---MNLSNPYDG------ARRAGTVGMPLPGVEMRITNRETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTRE---ELLD 376
Cdd:PRK08633 938 vasVNLPDVLAAdfkrqtGSKEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEvikDIDG 1017
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 377 DGFFITGDLAMVDEQGYVHIVGRdkdlvIS-----GGYNVYPKEVEQVIDEL--DQVAESAVIGLPHPDFGEGVtAVVVR 449
Cdd:PRK08633 1018 IGWYVTGDKGHLDEDGFLTITDR-----YSrfakiGGEMVPLGAVEEELAKAlgGEEVVFAVTAVPDEKKGEKL-VVLHT 1091
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2136495511 450 QQGADLGEnqLEEEkvitHLDGRLAKYKQPKRVFFVDELPRNTMGKV 496
Cdd:PRK08633 1092 CGAEDVEE--LKRA----IKESGLPNLWKPSRYFKVEALPLLGSGKL 1132
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
8-512 |
7.41e-62 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 211.49 E-value: 7.41e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 8 TFAAkmRERAEADFITTR---DGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPL 84
Cdd:PRK07008 17 AHAA--RHAGDTEIVSRRvegDIHRYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 85 NTGYTGDEIRYFLNDAEPAlFVC-----RPKIEeqalSLAAEtgCPAV---VTLGSAAdgSLMETAQAAVPREDIV---- 152
Cdd:PRK07008 95 NPRLFPEQIAYIVNHAEDR-YVLfdltfLPLVD----ALAPQ--CPNVkgwVAMTDAA--HLPAGSTPLLCYETLVgaqd 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 153 ------ALGERDLAAILYTSGTTGRSKGAMLTHKN--LASNAKTLARAWHFSADDRLIHALPIFHTH--GLFVACNVTlm 222
Cdd:PRK07008 166 gdydwpRFDENQASSLCYTSGTTGNPKGALYSHRStvLHAYGAALPDAMGLSARDAVLPVVPMFHVNawGLPYSAPLT-- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 223 aGASMLFL-PKFDADVIFE--ELPRGTVMMGVPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAIL 299
Cdd:PRK07008 244 -GAKLVLPgPDLDGKSLYEliEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 300 ERYGMTE----------TNMNLSNPYDGARRAGT-VGMPLPGVEMRITNrETGAEVP-----FGEigmLQIRGPNVFIGY 363
Cdd:PRK07008 323 HAWGMTEmsplgtlcklKWKHSQLPLDEQRKLLEkQGRVIYGVDMKIVG-DDGRELPwdgkaFGD---LQVRGPWVIDRY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 364 WRmpekTREELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGV 443
Cdd:PRK07008 399 FR----GDASPLVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERP 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2136495511 444 TAVVVRQQGADlgenqLEEEKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRKRFNDtYQTP 512
Cdd:PRK07008 475 LLVVVKRPGAE-----VTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQFRD-YVLP 537
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
21-503 |
2.46e-61 |
|
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: 210.08 E-value: 2.46e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 21 FITTRDGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDA 100
Cdd:cd17642 36 FTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNIS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 101 EPALFVCRPKIEEQALSLAAE-TGCPAVVTLGSAADGSLMETAQAAVPREDIVALGERD-----------LAAILYTSGT 168
Cdd:cd17642 116 KPTIVFCSKKGLQKVLNVQKKlKIIKTIIILDSKEDYKGYQCLYTFITQNLPPGFNEYDfkppsfdrdeqVALIMNSSGS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 169 TGRSKGAMLTHKNLA---SNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNvTLMAGASMLFLPKFDADVIFEELPRG 245
Cdd:cd17642 196 TGLPKGVQLTHKNIVarfSHARDPIFGNQIIPDTAILTVIPFHHGFGMFTTLG-YLICGFRVVLMYKFEEELFLRSLQDY 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 246 TVMMG--VPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTG-HAILERYGMTETNMNLSNPYDGARRAG 322
Cdd:cd17642 275 KVQSAllVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKlPGIRQGYGLTETTSAILITPEGDDKPG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 323 TVGMPLPGVEMRITNRETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRDKD 402
Cdd:cd17642 355 AVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKS 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 403 LVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGAdlgenQLEEEKVITHLDGRLAKYKQPK-R 481
Cdd:cd17642 435 LIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGK-----TMTEKEVMDYVASQVSTAKRLRgG 509
|
490 500
....*....|....*....|..
gi 2136495511 482 VFFVDELPRNTMGKVQKNELRK 503
Cdd:cd17642 510 VKFVDEVPKGLTGKIDRRKIRE 531
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
30-504 |
2.49e-61 |
|
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: 207.74 E-value: 2.49e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 30 YRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVCRP 109
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 110 KIEEqalslaaetgcpavvtlgsaadgslmetaqaavpREDIvalgeRDLAAILYTSGTTGRSKGAMLTHKNLASNAKTl 189
Cdd:cd05969 81 ELYE----------------------------------RTDP-----EDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFT- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 190 aRAWHFS--ADDRLIH-ALPIFHThGLFVACNVTLMAGASMLFLP-KFDADVIFEELPRG--TVMMGVPTFYTRLVQ--D 261
Cdd:cd05969 121 -GKYVLDlhPDDIYWCtADPGWVT-GTVYGIWAPWLNGVTNVVYEgRFDAESWYGIIERVkvTVWYTAPTAIRMLMKegD 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 262 ERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNMNLSNPYDGAR-RAGTVGMPLPGVEMRITNREt 340
Cdd:cd05969 199 ELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYPCMPiKPGSMGKPLPGVKAAVVDEN- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 341 GAEVPFGEIGMLQIRG--PNVFIGYWRMPEKTREELLDdGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQ 418
Cdd:cd05969 278 GNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSFID-GWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVES 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 419 VIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGEnQLEEEkVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQK 498
Cdd:cd05969 357 ALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSD-ELKEE-IINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMR 434
|
....*.
gi 2136495511 499 NELRKR 504
Cdd:cd05969 435 RVLKAK 440
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
25-501 |
3.25e-61 |
|
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: 208.52 E-value: 3.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 25 RDGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAE-PA 103
Cdd:cd05923 24 ARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEmTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 104 LFVC--RPKIEEQALSLAAETGCPAVVTLGSAADGSLMETAQAAVPREDivalgerdlAAILYTSGTTGRSKGAMLTHKN 181
Cdd:cd05923 104 AVIAvdAQVMDAIFQSGVRVLALSDLVGLGEPESAGPLIEDPPREPEQP---------AFVFYTSGTTGLPKGAVIPQRA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 182 LASNAKTLAR--AWHFSADDRLIHALPIFHTHGLFvACNVTLMAGASMLFLPK-FDADVIFE--ELPRGTVMMGVPTFYT 256
Cdd:cd05923 175 AESRVLFMSTqaGLRHGRHNVVLGLMPLYHVIGFF-AVLVAALALDGTYVVVEeFDPADALKliEQERVTSLFATPTHLD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 257 RLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETnMNlsNPYDGARRAGTVGMPLPGVEMRIT 336
Cdd:cd05923 254 ALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEA-MN--SLYMRDARTGTEMRPGFFSEVRIV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 337 NRETGAE--VPFGEIGMLQIR--GPNVFIGYWRMPEKTREELlDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVY 412
Cdd:cd05923 331 RIGGSPDeaLANGEEGELIVAaaADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIH 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 413 PKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGaDLGENQLEEekviTHLDGRLAKYKQPKRVFFVDELPRNT 492
Cdd:cd05923 410 PSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG-TLSADELDQ----FCRASELADFKRPRRYFFLDELPKNA 484
|
....*....
gi 2136495511 493 MGKVQKNEL 501
Cdd:cd05923 485 MNKVLRRQL 493
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
30-503 |
1.31e-60 |
|
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: 205.44 E-value: 1.31e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 30 YRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVC-- 107
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTda 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 108 --RPKIeeqalslaaetgcpavvtlgsaADGSLMEtaqaavpredivalgerdlaaiLYTSGTTGRSKGAMLTHKNLASN 185
Cdd:cd05973 81 anRHKL----------------------DSDPFVM----------------------MFTSGTTGLPKGVPVPLRALAAF 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 186 AKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAG-ASMLFLPKFDADVIFEELPRG--TVMMGVPTFYTRLVQDE 262
Cdd:cd05973 117 GAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGhPTILLEGGFSVESTWRVIERLgvTNLAGSPTAYRLLMAAG 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 263 RLTPEA-TANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNMNLSNPYDGAR--RAGTVGMPLPGVEMRITNrE 339
Cdd:cd05973 197 AEVPARpKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEHpvHAGSAGRAMPGWRVAVLD-D 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 340 TGAEVPFGEIGMLQI---RGPNV-FIGYWRMPEKTreelLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKE 415
Cdd:cd05973 276 DGDELGPGEPGRLAIdiaNSPLMwFRGYQLPDTPA----IDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFD 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 416 VEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADlGENQLEEEkVITHLDGRLAKYKQPKRVFFVDELPRNTMGK 495
Cdd:cd05973 352 VESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHE-GTPALADE-LQLHVKKRLSAHAYPRTIHFVDELPKTPSGK 429
|
....*...
gi 2136495511 496 VQKNELRK 503
Cdd:cd05973 430 IQRFLLRR 437
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
22-503 |
1.81e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 206.55 E-value: 1.81e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 22 ITTRDgRRYRYTDALTISAQLAGALTELGVKQgDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAE 101
Cdd:PRK07638 20 IKEND-RVLTYKDWFESVCKVANWLNEKESKN-KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 102 PALFVCrpkiEEQALSLAAETGCPavVTLGSAADGSLMETAQAAVPREDIvalgERDLAAILYTSGTTGRSKGAMLTHKN 181
Cdd:PRK07638 98 ADMIVT----ERYKLNDLPDEEGR--VIEIDEWKRMIEKYLPTYAPIENV----QNAPFYMGFTSGSTGKPKAFLRAQQS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 182 LASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNvTLMAGASMLFLPKFDADVIFEELPRG--TVMMGVPTFYTRLV 259
Cdd:PRK07638 168 WLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAIS-TLYVGQTVHLMRKFIPNQVLDKLETEniSVMYTVPTMLESLY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 260 QDERlTPEATanMRLFVSGsAPLTAETHEAFEAKTGHAIL-ERYGMTETN-MNLSNPYDGARRAGTVGMPLPGVEMRITN 337
Cdd:PRK07638 247 KENR-VIENK--MKIISSG-AKWEAEAKEKIKNIFPYAKLyEFYGASELSfVTALVDEESERRPNSVGRPFHNVQVRICN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 338 rETGAEVPFGEIGMLQIRGPNVFIGYwRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVE 417
Cdd:PRK07638 323 -EAGEEVQKGEIGTVYVKSPQFFMGY-IIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 418 QVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGAdlgenqleeEKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQ 497
Cdd:PRK07638 401 SVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSATK---------QQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIA 471
|
....*.
gi 2136495511 498 KNELRK 503
Cdd:PRK07638 472 RMEAKS 477
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
8-502 |
4.88e-60 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 205.63 E-value: 4.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 8 TFAAKMRERAEADFITTRDGRRYRYTDalTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTG 87
Cdd:PRK13390 5 THAQIAPDRPAVIVAETGEQVSYRQLD--DDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 88 YTGDEIRYFLNDAEPALFVCRPKIEeqalSLAAETGCPAVVTL--GSAADG--SLMETAQAAVPRedivaLGERDLAAI- 162
Cdd:PRK13390 83 LTAPEADYIVGDSGARVLVASAALD----GLAAKVGADLPLRLsfGGEIDGfgSFEAALAGAGPR-----LTEQPCGAVm 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 163 LYTSGTTGRSKGAM--LTHKNLASNAK---TLARAWH-FSADDRLIHALPIFHTHGLfVACNVTLMAGASMLFLPKFDAD 236
Cdd:PRK13390 154 LYSSGTTGFPKGIQpdLPGRDVDAPGDpivAIARAFYdISESDIYYSSAPIYHAAPL-RWCSMVHALGGTVVLAKRFDAQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 237 VIFE--ELPRGTVMMGVPTFYTRLVQ--DERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETN-MNL 311
Cdd:PRK13390 233 ATLGhvERYRITVTQMVPTMFVRLLKldADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEAHgMTF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 312 SNPYDGARRAGTVGMPLPGvEMRITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFIT--GDLAMVD 389
Cdd:PRK13390 313 IDSPDWLAHPGSVGRSVLG-DLHICD-DDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHPFWTtvGDLGSVD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 390 EQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADlGENQLEEEkVITHL 469
Cdd:PRK13390 391 EDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIR-GSDELARE-LIDYT 468
|
490 500 510
....*....|....*....|....*....|...
gi 2136495511 470 DGRLAKYKQPKRVFFVDELPRNTMGKVQKNELR 502
Cdd:PRK13390 469 RSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
10-505 |
3.04e-59 |
|
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: 204.78 E-value: 3.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 10 AAKMRERAEADFITTRDGRRYRYTDA-LTISAQ-LAGALTELGvKQGDRVAVQVDKSPEAILLYLACLRIGGV----YLP 83
Cdd:cd05931 3 AAARPDRPAYTFLDDEGGREETLTYAeLDRRARaIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIavplPPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 84 LNTGYTGDeIRYFLNDAEPALFVCRPkiEEQALSLAAETGCPAVVTLGSAADGSLMETAQAAVPRediVALGERDLAAIL 163
Cdd:cd05931 82 TPGRHAER-LAAILADAGPRVVLTTA--AALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPP---PSPDPDDIAYLQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 164 YTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDadviFEELP 243
Cdd:cd05931 156 YTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAA----FLRRP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 244 ---------RGTVMMGVPTFYTRLVQDeRLTPEATA-----NMRLFVSGSAPLTAETHEAFEAKTG------HAILERYG 303
Cdd:cd05931 232 lrwlrlisrYRATISAAPNFAYDLCVR-RVRDEDLEgldlsSWRVALNGAEPVRPATLRRFAEAFApfgfrpEAFRPSYG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 304 MTET-------------------NMNLSNPYDGARRAGT-------VGMPLPGVEMRITNRETGAEVPFGEIGMLQIRGP 357
Cdd:cd05931 311 LAEAtlfvsggppgtgpvvlrvdRDALAGRAVAVAADDPaarelvsCGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGP 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 358 NVFIGYWRMPEKTREELL------DDGFFITGDLAMVDEqGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQV---AE 428
Cdd:cd05931 391 SVASGYWGRPEATAETFGalaatdEGGWLRTGDLGFLHD-GELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPAlrpGC 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 429 SAVIGLPHPDfGEGVTAVVVRQQGADlgenQLEEEKVITHLDGRLAKYKQ--PKRVFFV--DELPRNTMGKVQKNELRKR 504
Cdd:cd05931 470 VAAFSVPDDG-EERLVVVAEVERGAD----PADLAAIAAAIRAAVAREHGvaPADVVLVrpGSIPRTSSGKIQRRACRAA 544
|
.
gi 2136495511 505 F 505
Cdd:cd05931 545 Y 545
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
158-503 |
3.04e-59 |
|
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: 199.63 E-value: 3.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 158 DLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFL-PK-FDA 235
Cdd:cd05944 3 DVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAgPAgYRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 236 DVIFEEL------PRGTVMMGVPTFYTRLVQdeRLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNM 309
Cdd:cd05944 83 PGLFDNFwklverYRITSLSTVPTVYAALLQ--VPVNADISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 310 NLS-NPYDGARRAGTVGMPLP--GVEMRITNRETGAEVPFG--EIGMLQIRGPNVFIGYWRMpEKTREELLDDGFFITGD 384
Cdd:cd05944 161 LVAvNPPDGPKRPGSVGLRLPyaRVRIKVLDGVGRLLRDCApdEVGEICVAGPGVFGGYLYT-EGNKNAFVADGWLNTGD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 385 LAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGENQLEEEk 464
Cdd:cd05944 240 LGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEELLAW- 318
|
330 340 350
....*....|....*....|....*....|....*....
gi 2136495511 465 VITHLDGRLAkykQPKRVFFVDELPRNTMGKVQKNELRK 503
Cdd:cd05944 319 ARDHVPERAA---VPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
24-501 |
4.13e-59 |
|
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: 202.52 E-value: 4.13e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 24 TRDGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPA 103
Cdd:cd12116 7 RDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 104 LFVCRPKIEEQAlslaaeTGCPAVVTLGSAADGSLMETAQAAVPredivalgERDLAAILYTSGTTGRSKGAMLTHKNLA 183
Cdd:cd12116 87 LVLTDDALPDRL------PAGLPVLLLALAAAAAAPAAPRTPVS--------PDDLAYVIYTSGSTGRPKGVVVSHRNLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 184 SNAKTLARAWHFSADDRL---------IHALPIFhthglfvacnVTLMAGASMLFLPKFD-------ADVIfeELPRGTV 247
Cdd:cd12116 153 NFLHSMRERLGLGPGDRLlavttyafdISLLELL----------LPLLAGARVVIAPRETqrdpealARLI--EAHSITV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 248 MMGVPTFYTRLVQDErltPEATANMRLFVSGSApLTAETHEAFEAKTGhAILERYGMTETNM-NLSNPYDGARRAGTVGM 326
Cdd:cd12116 221 MQATPATWRMLLDAG---WQGRAGLTALCGGEA-LPPDLAARLLSRVG-SLWNLYGPTETTIwSTAARVTAAAGPIPIGR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 327 PLPGVEMRITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGF-------FITGDLAMVDEQGYVHIVGR 399
Cdd:cd12116 296 PLANTQVYVLD-AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFagpgsrlYRTGDLVRRRADGRLEYLGR 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 400 DKDLVISGGYNVYPKEVEQVIDELDQVAESAVIgLPHPDFGEGVTAVVVRQQGADLGENQLEEekvitHLDGRLAKYKQP 479
Cdd:cd12116 375 ADGQVKIRGHRIELGEIEAALAAHPGVAQAAVV-VREDGGDRRLVAYVVLKAGAAPDAAALRA-----HLRATLPAYMVP 448
|
490 500
....*....|....*....|..
gi 2136495511 480 KRVFFVDELPRNTMGKVQKNEL 501
Cdd:cd12116 449 SAFVRLDALPLTANGKLDRKAL 470
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
42-503 |
1.15e-58 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 203.49 E-value: 1.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 42 LAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVcrpkIEEQALSLAAE 121
Cdd:PLN02860 45 LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLV----TDETCSSWYEE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 122 ---TGCPAV---VTLGSAADGSLMETAQ----------AAVPREDIVALGERDLAAILYTSGTTGRSKGAMLTHKNLAsn 185
Cdd:PLN02860 121 lqnDRLPSLmwqVFLESPSSSVFIFLNSflttemlkqrALGTTELDYAWAPDDAVLICFTSGTTGRPKGVTISHSALI-- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 186 AKTLAR--AWHFSADDRLIHALPIFHTHGLfVACNVTLMAGASMLFLPKFDADVIFEELP--RGTVMMGVPTFYTRLVQD 261
Cdd:PLN02860 199 VQSLAKiaIVGYGEDDVYLHTAPLCHIGGL-SSALAMLMVGACHVLLPKFDAKAALQAIKqhNVTSMITVPAMMADLISL 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 262 ERL--TPEATANMRLFVSGSAPLTAE-THEAFEAKTGHAILERYGMTE-----TNMNLSNPYDGARRA------------ 321
Cdd:PLN02860 278 TRKsmTWKVFPSVRKILNGGGSLSSRlLPDAKKLFPNAKLFSAYGMTEacsslTFMTLHDPTLESPKQtlqtvnqtksss 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 322 -----GT-VGMPLPGVEMRITNRETGaevpfgEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVH 395
Cdd:PLN02860 358 vhqpqGVcVGKPAPHVELKIGLDESS------RVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLW 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 396 IVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGENQLEEEK-------VITH 468
Cdd:PLN02860 432 LIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGWIWSDNEKENAKknltlssETLR 511
|
490 500 510
....*....|....*....|....*....|....*....
gi 2136495511 469 LDGR---LAKYKQPKR-VFFVDELPRNTMGKVQKNELRK 503
Cdd:PLN02860 512 HHCReknLSRFKIPKLfVQWRKPFPLTTTGKIRRDEVRR 550
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
38-505 |
2.09e-58 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 202.76 E-value: 2.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 38 ISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVCRPKIEEQALS 117
Cdd:PLN02574 76 VKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSP 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 118 LAAET-GCPAVVTLGSAADG-----SLMETAQAAVPREDIvalGERDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLAR 191
Cdd:PLN02574 156 LGVPViGVPENYDFDSKRIEfpkfyELIKEDFDFVPKPVI---KQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVR 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 192 ----AWHFSADDRL-IHALPIFHTHGLFVACNVTLMAGASMLFLPKFDADVIFEELPRGTVMMG--VPTFYTRLVQDER- 263
Cdd:PLN02574 233 feasQYEYPGSDNVyLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFpvVPPILMALTKKAKg 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 264 LTPEATANMRLFVSGSAPLTAETHEAFEAKTGHA-ILERYGMTETNMNLSNPYDGA--RRAGTVGMPLPGVEMRITNRET 340
Cdd:PLN02574 313 VCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVdFIQGYGMTESTAVGTRGFNTEklSKYSSVGLLAPNMQAKVVDWST 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 341 GAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVI 420
Cdd:PLN02574 393 GCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVL 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 421 DELDQVAESAVIGLPHPDFGEGVTAVVVRQQGAdlgenQLEEEKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNE 500
Cdd:PLN02574 473 ISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGS-----TLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRE 547
|
....*
gi 2136495511 501 LRKRF 505
Cdd:PLN02574 548 LKRSL 552
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
39-504 |
1.07e-57 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 200.37 E-value: 1.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 39 SAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLN-DAEPALFvcrpkIEEQALS 117
Cdd:PRK13382 78 SDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTrEGVDTVI-----YDEEFSA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 118 LA--AETGCPAVVTLGSAADGSLMETAQA--AVPREDIVALGERDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAW 193
Cdd:PRK13382 153 TVdrALADCPQATRIVAWTDEDHDLTVEVliAAHAGQRPEPTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKAILDRT 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 194 HFSADDRLIHALPIFHTHGlFVACNVTLMAGASMLFLPKFD--ADVIFEELPRGTVMMGVPTFYTRLVQ--DERLTPEAT 269
Cdd:PRK13382 233 PWRAEEPTVIVAPMFHAWG-FSQLVLAASLACTIVTRRRFDpeATLDLIDRHRATGLAVVPVMFDRIMDlpAEVRNRYSG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 270 ANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNM-NLSNPYDGARRAGTVGMPLPGVEMRITNREtGAEVPFGE 348
Cdd:PRK13382 312 RSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMiATATPADLRAAPDTAGRPAEGTEIRILDQD-FREVPTGE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 349 IGMLQIRGPNVFIGYwrMPEKTREelLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAE 428
Cdd:PRK13382 391 VGTIFVRNDTQFDGY--TSGSTKD--FHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAE 466
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2136495511 429 SAVIGLPHPDFGEGVTAVVVRQQGAdlgenQLEEEKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRKR 504
Cdd:PRK13382 467 AAVIGVDDEQYGQRLAAFVVLKPGA-----SATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
24-501 |
1.88e-57 |
|
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: 198.65 E-value: 1.88e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 24 TRDGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPA 103
Cdd:cd17646 18 VDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 104 LFVCRPkieEQALSLAAEtgcPAVVTLGSAADGSLMETAQAAVPREDivalgerDLAAILYTSGTTGRSKGAMLTHKNLA 183
Cdd:cd17646 98 VVLTTA---DLAARLPAG---GDVALLGDEALAAPPATPPLVPPRPD-------NLAYVIYTSGSTGRPKGVMVTHAGIV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 184 SNAKTLARAWHFSADDRLIHALPI-FHTHG--LFVAcnvtLMAGASMLFL-------PKFDADVIFEElpRGTVMMGVPT 253
Cdd:cd17646 165 NRLLWMQDEYPLGPGDRVLQKTPLsFDVSVweLFWP----LVAGARLVVArpgghrdPAYLAALIREH--GVTTCHFVPS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 254 FYTRLVQDerLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNMNLSN-PYDGARRAGTV--GMPLPG 330
Cdd:cd17646 239 MLRVFLAE--PAAGSCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHwPVRGPAETPSVpiGRPVPN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 331 VEMRITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGF------FITGDLAMVDEQGYVHIVGRDKDLV 404
Cdd:cd17646 317 TRLYVLD-DALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFgpgsrmYRTGDLARWRPDGALEFLGRSDDQV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 405 ISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVrqqgADLGENQLEEEKVITHLDGRLAKYKQPKRVFF 484
Cdd:cd17646 396 KIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVV----PAAGAAGPDTAALRAHLAERLPEYMVPAAFVV 471
|
490
....*....|....*..
gi 2136495511 485 VDELPRNTMGKVQKNEL 501
Cdd:cd17646 472 LDALPLTANGKLDRAAL 488
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
42-505 |
4.82e-57 |
|
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: 198.66 E-value: 4.82e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 42 LAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPA-------LFVCRPKIEEQ 114
Cdd:cd05906 52 LAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPNARLRKLRHIwqllgspVVLTDAELVAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 115 ALSLAAETGCPAVVTLGSAadgSLMETAQAAvpreDIVALGERDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWH 194
Cdd:cd05906 132 FAGLETLSGLPGIRVLSIE---ELLDTAADH----DLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 195 FSADDRLIHALPIFHTHGLfVACNV-TLMAGASMLFLPkfdADVIFEELP---------RGTVMMGVPTFYTRLVQDERL 264
Cdd:cd05906 205 LTPQDVFLNWVPLDHVGGL-VELHLrAVYLGCQQVHVP---TEEILADPLrwldlidryRVTITWAPNFAFALLNDLLEE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 265 TPEATAN---MRLFVSGSAPLTAETHEAFE---AKTG---HAILERYGMTET----NMNLSNPYDGARRAGT---VGMPL 328
Cdd:cd05906 281 IEDGTWDlssLRYLVNAGEAVVAKTIRRLLrllEPYGlppDAIRPAFGMTETcsgvIYSRSFPTYDHSQALEfvsLGRPI 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 329 PGVEMRITnRETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEqGYVHIVGRDKDLVISGG 408
Cdd:cd05906 361 PGVSMRIV-DDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDN-GNLTITGRTKDTIIVNG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 409 YNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVV----RQQGADLGENQLEE-EKVITHLDGRLAKYKQPKRvf 483
Cdd:cd05906 439 VNYYSHEIEAAVEEVPGVEPSFTAAFAVRDPGAETEELAIffvpEYDLQDALSETLRAiRSVVSREVGVSPAYLIPLP-- 516
|
490 500
....*....|....*....|..
gi 2136495511 484 fVDELPRNTMGKVQKNELRKRF 505
Cdd:cd05906 517 -KEEIPKTSLGKIQRSKLKAAF 537
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
26-496 |
1.07e-56 |
|
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: 195.54 E-value: 1.07e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 26 DGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALF 105
Cdd:cd05945 13 GGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 106 VCRPKieeqalslaaetgcpavvtlgsaadgslmetaqaavpredivalgerDLAAILYTSGTTGRSKGAMLTHKNLASN 185
Cdd:cd05945 93 IADGD-----------------------------------------------DNAYIIFTSGSTGRPKGVQISHDNLVSF 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 186 AKTLARAWHFSADDRLIHALPiFH----THGLFVAcnvtLMAGASMLFLPKfDADVIFEELPRG------TVMMGVPTFY 255
Cdd:cd05945 126 TNWMLSDFPLGPGDVFLNQAP-FSfdlsVMDLYPA----LASGATLVPVPR-DATADPKQLFRFlaehgiTVWVSTPSFA 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 256 TRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKT-GHAILERYGMTETNMNLS------NPYDGARRAgTVGMPL 328
Cdd:cd05945 200 AMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATVAVTyievtpEVLDGYDRL-PIGYAK 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 329 PGVEMRITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREEL-LDDGF--FITGDLAMVDEQGYVHIVGRDKDLVI 405
Cdd:cd05945 279 PGAKLVILD-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFfPDEGQraYRTGDLVRLEADGLLFYRGRLDFQVK 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 406 SGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGenQLEEEKviTHLDGRLAKYKQPKRVFFV 485
Cdd:cd05945 358 LNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAG--LTKAIK--AELAERLPPYMIPRRFVYL 433
|
490
....*....|.
gi 2136495511 486 DELPRNTMGKV 496
Cdd:cd05945 434 DELPLNANGKI 444
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
40-484 |
1.30e-56 |
|
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: 195.66 E-value: 1.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 40 AQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVcrpkieeqalsla 119
Cdd:cd17640 16 LDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 120 aetgcpavvtlgsaadgslmetaqaavprediVALGERDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADD 199
Cdd:cd17640 83 --------------------------------VENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 200 RLIHALPIFHTHGLfvACNVTLMA-GASMLF--LPKFDADVifeELPRGTVMMGVP----TFYTRlVQDERLTPEATANM 272
Cdd:cd17640 131 RFLSILPIWHSYER--SAEYFIFAcGCSQAYtsIRTLKDDL---KRVKPHYIVSVPrlweSLYSG-IQKQVSKSSPIKQF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 273 --RLFVS-----------GSAPLTAETHeaFEAkTGHAILERYGMTETNMNLSnpydgARR-----AGTVGMPLPGVEMR 334
Cdd:cd17640 205 lfLFFLSggifkfgisggGALPPHVDTF--FEA-IGIEVLNGYGLTETSPVVS-----ARRlkcnvRGSVGRPLPGTEIK 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 335 ITNRETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRDKD-LVISGGYNVYP 413
Cdd:cd17640 277 IVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDtIVLSNGENVEP 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2136495511 414 KEVEQVIDELDQVAESAVIG--------LPHPDFGEGVTAVVVRQQGADLGENQLEEEKVITHLDGRLAKYKQPKRVFF 484
Cdd:cd17640 357 QPIEEALMRSPFIEQIMVVGqdqkrlgaLIVPNFEELEKWAKESGVKLANDRSQLLASKKVLKLYKNEIKDEISNRPGF 435
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
1-495 |
6.07e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 195.49 E-value: 6.07e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 1 MSHN---LFETFAAKMRERAeadfITTRDGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRI 77
Cdd:PRK07798 1 MAWNiadLFEAVADAVPDRV----ALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 78 GGVYLPLNTGYTGDEIRYFLNDAEP-ALFVCR---PKIEEqalsLAAETgcPAVVTLGSAADGSLMETAQAAVPREDIVA 153
Cdd:PRK07798 77 RAVPVNVNYRYVEDELRYLLDDSDAvALVYERefaPRVAE----VLPRL--PKLRTLVVVEDGSGNDLLPGAVDYEDALA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 154 LG--ERDLAA-------ILYTSGTTGRSKGAMLTHKNL---------------ASNAKTLARAWHFSADDRLIHALPIFH 209
Cdd:PRK07798 151 AGspERDFGErspddlyLLYTGGTTGMPKGVMWRQEDIfrvllggrdfatgepIEDEEELAKRAAAGPGMRRFPAPPLMH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 210 THGLFVACNvTLMAGASMLFLP--KFDADVIFEELPRG--TVMMGVPTFYTRLVQDERLTPEAT--ANMRLFVSGSAPLT 283
Cdd:PRK07798 231 GAGQWAAFA-ALFSGQTVVLLPdvRFDADEVWRTIEREkvNVITIVGDAMARPLLDALEARGPYdlSSLFAIASGGALFS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 284 AETHEAF-EAKTGHAILERYGMTET-NMNLSNPYDGARRAGTvgmplPGVEMRITNR---ETGAEVPFG--EIGMLQIRG 356
Cdd:PRK07798 310 PSVKEALlELLPNVVLTDSIGSSETgFGGSGTVAKGAVHTGG-----PRFTIGPRTVvldEDGNPVEPGsgEIGWIARRG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 357 PnVFIGYWRMPEKTREELLD-DG--FFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIG 433
Cdd:PRK07798 385 H-IPLGYYKDPEKTAETFPTiDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVG 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2136495511 434 LPHPDFGEGVTAVVVRQQGADlgenqLEEEKVITHLDGRLAKYKQPKRVFFVDELPRNTMGK 495
Cdd:PRK07798 464 VPDERWGQEVVAVVQLREGAR-----PDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
10-505 |
1.48e-55 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 194.72 E-value: 1.48e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 10 AAKMRERAEAdFITTRDGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYT 89
Cdd:PRK05852 25 AATRLPEAPA-LVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 90 GDEIRYFLNDAEP-ALFVCRPKIEEQALslAAETGCPAVVTLGS---AADGSLMETAQAAV-PREDIVA-LGER-DLAAI 162
Cdd:PRK05852 104 IAEQRVRSQAAGArVVLIDADGPHDRAE--PTTRWWPLTVNVGGdsgPSGGTLSVHLDAATePTPATSTpEGLRpDDAMI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 163 LYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLfLP---KFDADVIF 239
Cdd:PRK05852 182 MFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVL-LPargRFSAHTFW 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 240 EELP--RGTVMMGVPTFYTRLVQ--DERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTE-TNMNLSNP 314
Cdd:PRK05852 261 DDIKavGATWYTAVPTIHQILLEraATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEaTHQVTTTQ 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 315 YDGARRAGTVGMPL------PGVEMRITnRETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELlDDGFFITGDLAMV 388
Cdd:PRK05852 341 IEGIGQTENPVVSTglvgrsTGAQIRIV-GSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 389 DEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGENQLEEekvitH 468
Cdd:PRK05852 419 SAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQ-----F 493
|
490 500 510
....*....|....*....|....*....|....*..
gi 2136495511 469 LDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRKRF 505
Cdd:PRK05852 494 CRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQF 530
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
7-502 |
3.14e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 193.81 E-value: 3.14e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 7 ETFAAKMRE--RAEADFITTRD-GRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLP 83
Cdd:PRK06164 10 DTLASLLDAhaRARPDAVALIDeDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 84 LNTGYTGDEIRYFLNDAEPALFVCRPKIEE-------QALSLAAETGCPAVVTLGSAAD---------------GSLMET 141
Cdd:PRK06164 90 VNTRYRSHEVAHILGRGRARWLVVWPGFKGidfaailAAVPPDALPPLRAIAVVDDAADatpapapgarvqlfaLPDPAP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 142 AQAAVPREDIValgerDLAAILYT-SGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNvT 220
Cdd:PRK06164 170 PAAAGERAADP-----DAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLG-A 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 221 LMAGASMLFLPKFDADVIFEELPRGTV--MMGVPTFYTRLVQderLTPEATANMRLFVSGSAPLTAETHE-AFEAKT-GH 296
Cdd:PRK06164 244 LAGGAPLVCEPVFDAARTARALRRHRVthTFGNDEMLRRILD---TAGERADFPSARLFGFASFAPALGElAALARArGV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 297 AILERYGMTE-----TNMNLSNPYDGARRAGtvGMPL-PGVEMRITNRETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKT 370
Cdd:PRK06164 321 PLTGLYGSSEvqalvALQPATDPVSVRIEGG--GRPAsPEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDAT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 371 REELLDDGFFITGDLA-MVDEQGYVHiVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVtAVVVR 449
Cdd:PRK06164 399 ARALTDDGYFRTGDLGyTRGDGQFVY-QTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPV-AFVIP 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2136495511 450 QQGAdlgenQLEEEKVITHLDGRLAKYKQPKRVFFVDELPRNTMG---KVQKNELR 502
Cdd:PRK06164 477 TDGA-----SPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLR 527
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
28-504 |
7.70e-55 |
|
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: 192.71 E-value: 7.70e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 28 RRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVC 107
Cdd:cd05970 46 RIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 108 --RPKIEEQALSLAAETGCPAVVTL--GSAADG------SLMETAQAAVPREDIVALGERDLAAILYTSGTTGRSKgaML 177
Cdd:cd05970 126 iaEDNIPEEIEKAAPECPSKPKLVWvgDPVPEGwidfrkLIKNASPDFERPTANSYPCGEDILLVYFSSGTTGMPK--MV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 178 THKNLASNAKTL-ARAWHFSADDRLiHaLPIFHTH------GLFVAcnvTLMAGASMLF--LPKFDADVIFEELP--RGT 246
Cdd:cd05970 204 EHDFTYPLGHIVtAKYWQNVREGGL-H-LTVADTGwgkavwGKIYG---QWIAGAAVFVydYDKFDPKALLEKLSkyGVT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 247 VMMGVPTFYTRLVQdERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNMNLSNPYDGARRAGTVGM 326
Cdd:cd05970 279 TFCAPPTIYRFLIR-EDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGK 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 327 PLPGVEMRITNREtGAEVPFGEIGMLQIRGPN-----VFIGYWRMPEKTrEELLDDGFFITGDLAMVDEQGYVHIVGRDK 401
Cdd:cd05970 358 PAPGYEIDLIDRE-GRSCEAGEEGEIVIRTSKgkpvgLFGGYYKDAEKT-AEVWHDGYYHTGDAAWMDEDGYLWFVGRTD 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 402 DLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGEnQLEEEkVITHLDGRLAKYKQPKR 481
Cdd:cd05970 436 DLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSE-ELKKE-LQDHVKKVTAPYKYPRI 513
|
490 500
....*....|....*....|...
gi 2136495511 482 VFFVDELPRNTMGKVQKNELRKR 504
Cdd:cd05970 514 VEFVDELPKTISGKIRRVEIRER 536
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
21-508 |
1.12e-54 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 192.50 E-value: 1.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 21 FITTRDGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDA 100
Cdd:PLN02330 47 FVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 101 EPALFVCRPKIEEQALSLaaetGCPaVVTLGSAADGS------LMETAQAAVPREDIVALGERDLAAILYTSGTTGRSKG 174
Cdd:PLN02330 127 GAKLIVTNDTNYGKVKGL----GLP-VIVLGEEKIEGavnwkeLLEAADRAGDTSDNEEILQTDLCALPFSSGTTGISKG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 175 AMLTHKNLASN-AKTLarawhFSADDRLIHA------LPIFHTHGLFVACNVTLMAGASMLFLPKFDADVIFEELPRGTV 247
Cdd:PLN02330 202 VMLTHRNLVANlCSSL-----FSVGPEMIGQvvtlglIPFFHIYGITGICCATLRNKGKVVVMSRFELRTFLNALITQEV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 248 MMG--VPTFYTRLVQDERLTPEATANMRL--FVSGSAPLTAETHEAFEAK-TGHAILERYGMTE---TNMNLSNPYDG-- 317
Cdd:PLN02330 277 SFApiVPPIILNLVKNPIVEEFDLSKLKLqaIMTAAAPLAPELLTAFEAKfPGVQVQEAYGLTEhscITLTHGDPEKGhg 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 318 -ARRaGTVGMPLPGVEMRITNRETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHI 396
Cdd:PLN02330 357 iAKK-NSVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFI 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 397 VGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGAdlgenQLEEEKVITHLDGRLAKY 476
Cdd:PLN02330 436 VDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKA-----KESEEDILNFVAANVAHY 510
|
490 500 510
....*....|....*....|....*....|..
gi 2136495511 477 KQPKRVFFVDELPRNTMGKVQKNELRKRFNDT 508
Cdd:PLN02330 511 KKVRVVQFVDSIPKSLSGKIMRRLLKEKMLSI 542
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
27-504 |
1.21e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 192.08 E-value: 1.21e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 27 GRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFV 106
Cdd:PRK08162 41 DRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 107 CRPKIEEQALSLAAETGCPAVVTLGsAADGSLMETAQA-AVPREDIVALGERDLAAIL-----------YTSGTTGRSKG 174
Cdd:PRK08162 121 VDTEFAEVAREALALLPGPKPLVID-VDDPEYPGGRFIgALDYEAFLASGDPDFAWTLpadewdaialnYTSGTTGNPKG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 175 AMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGAsMLFLPKFDADVIFEELPRGTV--MMGVP 252
Cdd:PRK08162 200 VVYHHRGAYLNALSNILAWGMPKHPVYLWTLPMFHCNGWCFPWTVAARAGT-NVCLRKVDPKLIFDLIREHGVthYCGAP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 253 TFYTRLVQderlTPEATAN-----MRLFVSGSAPLTAeTHEAFEAkTGHAILERYGMTET----NMNLSNPY-------D 316
Cdd:PRK08162 279 IVLSALIN----APAEWRAgidhpVHAMVAGAAPPAA-VIAKMEE-IGFDLTHVYGLTETygpaTVCAWQPEwdalpldE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 317 GARRAGTVGMPLPGVE-MRITNRETGAEVPF-GE-IGMLQIRGPNVFIGYWRMPEKTrEELLDDGFFITGDLAMVDEQGY 393
Cdd:PRK08162 353 RAQLKARQGVRYPLQEgVTVLDPDTMQPVPAdGEtIGEIMFRGNIVMKGYLKNPKAT-EEAFAGGWFHTGDLAVLHPDGY 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 394 VHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGAdlgenQLEEEKVITHLDGRL 473
Cdd:PRK08162 432 IKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGA-----SATEEEIIAHCREHL 506
|
490 500 510
....*....|....*....|....*....|.
gi 2136495511 474 AKYKQPKRVFFvDELPRNTMGKVQKNELRKR 504
Cdd:PRK08162 507 AGFKVPKAVVF-GELPKTSTGKIQKFVLREQ 536
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
38-502 |
7.32e-54 |
|
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: 188.36 E-value: 7.32e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 38 ISAQLAGALTELGVKQGDRVAVQVDKS--PEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVCRPKIEEQA 115
Cdd:cd05929 4 RDLDRAQVFHQRRLLLLDVYSIALNRNarAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEACA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 116 LSLAAetGCPAVV---TLGSAADG-SLMETAQAAVPREDIVALGERDlaAILYTSGTTGRSKGAMLTHKNLASNAKTLaR 191
Cdd:cd05929 84 IIEIK--AAALVCglfTGGGALDGlEDYEAAEGGSPETPIEDEAAGW--KMLYSGGTTGRPKGIKRGLPGGPPDNDTL-M 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 192 AWH----FSADDRLIHALPIFHTHGlFVACNVTLMAGASMLFLPKFDADVIFEELPRGTVMMG--VPTFYTRLVQDERLT 265
Cdd:cd05929 159 AAAlgfgPGADSVYLSPAPLYHAAP-FRWSMTALFMGGTLVLMEKFDPEEFLRLIERYRVTFAqfVPTMFVRLLKLPEAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 266 PEA--TANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETN-MNLSNPYDGARRAGTVGMPLPGvEMRITNrETGA 342
Cdd:cd05929 238 RNAydLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQgLTIINGEEWLTHPGSVGRAVLG-KVHILD-EDGN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 343 EVPFGEIGMLQIRGPNVFIgYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDE 422
Cdd:cd05929 316 EVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 423 LDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGEnQLEEEkVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELR 502
Cdd:cd05929 395 HPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGT-ALAEE-LIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
29-512 |
2.40e-52 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 186.11 E-value: 2.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 29 RYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPAL---- 104
Cdd:PRK06018 39 RTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVvitd 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 105 --FVcrPKIEEQALSLaaetgcPAVVTLGSAADGSLM--ETAQAAVPREDIVA----------LGERDLAAILYTSGTTG 170
Cdd:PRK06018 119 ltFV--PILEKIADKL------PSVERYVVLTDAAHMpqTTLKNAVAYEEWIAeadgdfawktFDENTAAGMCYTSGTTG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 171 RSKGAMLTHKN--LASNAKTLARAWHFSADDRLIHALPIFHTHGLFVAcnvtlMAGASM---LFLP--KFDADVIFEEL- 242
Cdd:PRK06018 191 DPKGVLYSHRSnvLHALMANNGDALGTSAADTMLPVVPLFHANSWGIA-----FSAPSMgtkLVMPgaKLDGASVYELLd 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 243 -PRGTVMMGVPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEaKTGHAILERYGMTETN---------MNLS 312
Cdd:PRK06018 266 tEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFE-DMGVEVRHAWGMTEMSplgtlaalkPPFS 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 313 NPYDGAR--RAGTVGMPLPGVEMRITNREtGAEVPFG--EIGMLQIRGPNVFIGYWRMPEKTreeLLDDGFFITGDLAMV 388
Cdd:PRK06018 345 KLPGDARldVLQKQGYPPFGVEMKITDDA-GKELPWDgkTFGRLKVRGPAVAAAYYRVDGEI---LDDDGFFDTGDVATI 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 389 DEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADlgenqLEEEKVITH 468
Cdd:PRK06018 421 DAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGET-----ATREEILKY 495
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2136495511 469 LDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRKRFNDtYQTP 512
Cdd:PRK06018 496 MDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQFKD-YKLP 538
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
164-496 |
6.51e-52 |
|
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: 179.14 E-value: 6.51e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 164 YTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFvACNVTLMAGASMLFLPKFDA----DVIF 239
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLY-GAISALYLGGTFIGQRKFNPkswiRKIN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 240 EElpRGTVMMGVPTFYTRLVQDERltPEATanMRLFVSGSAPLTAETHEAFEAKTGHA-ILERYGMTETNMNLSNPYDGA 318
Cdd:cd17633 86 QY--NATVIYLVPTMLQALARTLE--PESK--IKSIFSSGQKLFESTKKKLKNIFPKAnLIEFYGTSELSFITYNFNQES 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 319 RRAGTVGMPLPGVEMRITNRETGaevpfgEIGMLQIRGPNVFIGYWRMPEKTReelldDGFFITGDLAMVDEQGYVHIVG 398
Cdd:cd17633 160 RPPNSVGRPFPNVEIEIRNADGG------EIGKIFVKSEMVFSGYVRGGFSNP-----DGWMSVGDIGYVDEEGYLYLVG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 399 RDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVrqqgadlgENQLEEEKVITHLDGRLAKYKQ 478
Cdd:cd17633 229 RESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS--------GDKLTYKQLKRFLKQKLSRYEI 300
|
330
....*....|....*...
gi 2136495511 479 PKRVFFVDELPRNTMGKV 496
Cdd:cd17633 301 PKKIIFVDSLPYTSSGKI 318
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
162-496 |
6.85e-52 |
|
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: 179.42 E-value: 6.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 162 ILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASmLFLPKFDA----DV 237
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTN-VFVRRVDAeevlEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 238 IFEELPRGTVMMGvPTF--YTRLVQDERL---TPEATANMRLFvsgSAPLTAETHEAFEAKTGhailerYGMTETNMNLS 312
Cdd:cd17636 84 IEAERCTHAFLLP-PTIdqIVELNADGLYdlsSLRSSPAAPEW---NDMATVDTSPWGRKPGG------YGQTEVMGLAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 313 NPYDGARRAGTVGMPLPGVEMRITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPE----KTReelldDGFFITGDLAMV 388
Cdd:cd17636 154 FAALGGGAIGGAGRPSPLVQVRILD-EDGREVPDGEVGEIVARGPTVMAGYWNRPEvnarRTR-----GGWHHTNDLGRR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 389 DEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGAdlgenQLEEEKVITH 468
Cdd:cd17636 228 EPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGA-----SVTEAELIEH 302
|
330 340
....*....|....*....|....*...
gi 2136495511 469 LDGRLAKYKQPKRVFFVDELPRNTMGKV 496
Cdd:cd17636 303 CRARIASYKKPKSVEFADALPRTAGGAD 330
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
157-498 |
2.97e-51 |
|
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: 177.84 E-value: 2.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 157 RDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARA-WHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDA 235
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEgLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 236 DVIFEELP----RGTVMmgVPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNMNL 311
Cdd:cd17635 81 KSLFKILTtnavTTTCL--VPTLLSKLVSELKSANATVPSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 312 SNPY-DGARRAGTVGMPLPGVEMRITNREtGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDdGFFITGDLAMVDE 390
Cdd:cd17635 159 CLPTdDDSIEINAVGRPYPGVDVYLAATD-GIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLID-GWVNTGDLGERRE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 391 QGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQqgADLGENQLEEEKVIthLD 470
Cdd:cd17635 237 DGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAS--AELDENAIRALKHT--IR 312
|
330 340
....*....|....*....|....*...
gi 2136495511 471 GRLAKYKQPKRVFFVDELPRNTMGKVQK 498
Cdd:cd17635 313 RELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-512 |
3.20e-51 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 188.83 E-value: 3.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 3 HNLFETFAAKMRERAEADFittrDGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYL 82
Cdd:PRK12467 515 HQLIEAQARQHPERPALVF----GEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYV 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 83 PLNTGYTGDEIRYFLNDAEPALFVCRPkieEQALSLAAETGCPAVVTlgsAADGSLMETAQAAVPRediVALGERDLAAI 162
Cdd:PRK12467 591 PLDPEYPQDRLAYMLDDSGVRLLLTQS---HLLAQLPVPAGLRSLCL---DEPADLLCGYSGHNPE---VALDPDNLAYV 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 163 LYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIH----ALPIFHTHgLFVAcnvtLMAGASMLFLPK---FDA 235
Cdd:PRK12467 662 IYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMvstfAFDLGVTE-LFGA----LASGATLHLLPPdcaRDA 736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 236 DVIFEELPRG--TVMMGVPTFYTRLVQDERLTPeATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNMNLS- 312
Cdd:PRK12467 737 EAFAALMADQgvTVLKIVPSHLQALLQASRVAL-PRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSt 815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 313 -NPYDGARRAGTV--GMPLPGVEMRITNRETgAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGF-------FIT 382
Cdd:PRK12467 816 yELSDEERDFGNVpiGQPLANLGLYILDHYL-NPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFgadggrlYRT 894
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 383 GDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHpDFGEGVTAVVVRQQGADLGENQLEE 462
Cdd:PRK12467 895 GDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPG-DAGLQLVAYLVPAAVADGAEHQATR 973
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2136495511 463 EKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRK----RFNDTYQTP 512
Cdd:PRK12467 974 DELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKpdasAVQATFVAP 1027
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
39-502 |
3.46e-50 |
|
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: 177.95 E-value: 3.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 39 SAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALfvcrpkieeqalsL 118
Cdd:cd17649 22 ANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGL-------------L 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 119 AAETGcpavvtlgsaadgslmetaqaavpredivalgeRDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSAD 198
Cdd:cd17649 89 LTHHP---------------------------------RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 199 DRLIHALPI----FHtHGLFVAcnvtLMAGASMLFLPK---FDADVIFEELPRGTV-MMGVPTFYTR-LVQD-ERLTPEA 268
Cdd:cd17649 136 DRELQFASFnfdgAH-EQLLPP----LICGACVVLRPDelwASADELAEMVRELGVtVLDLPPAYLQqLAEEaDRTGDGR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 269 TANMRLFVSGSAPLTAEtHEAFEAKTGHAILERYGMTETNMN--LSNPYDGARRAGT---VGMPLPGVEMRITNrETGAE 343
Cdd:cd17649 211 PPSLRLYIFGGEALSPE-LLRRWLKAPVRLFNAYGPTEATVTplVWKCEAGAARAGAsmpIGRPLGGRSAYILD-ADLNP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 344 VPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFI-------TGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEV 416
Cdd:cd17649 289 VPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGApgsrlyrTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 417 EQVIDELDQVAESAVIGLPHPDfGEGVTAVVVRQQGADLGENQleeEKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKV 496
Cdd:cd17649 369 EAALLEHPGVREAAVVALDGAG-GKQLVAYVVLRAAAAQPELR---AQLRTALRASLPDYMVPAHLVFLARLPLTPNGKL 444
|
....*.
gi 2136495511 497 QKNELR 502
Cdd:cd17649 445 DRKALP 450
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
15-502 |
2.44e-49 |
|
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: 176.77 E-value: 2.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 15 ERAEADFITTRDGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIR 94
Cdd:cd17651 6 ARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 95 YFLNDAEPALFVCrpkieEQALSLAAETGCPAVVTLgsaadgsLMETAQAAVPREDIVALGERDLAAILYTSGTTGRSKG 174
Cdd:cd17651 86 FMLADAGPVLVLT-----HPALAGELAVELVAVTLL-------DQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 175 AMLTHKNLASNAKTLARAWHFSADDRLIHALPI---FHTHGLFvacnVTLMAGASMLFLP---KFDADVIFEEL-PRGTV 247
Cdd:cd17651 154 VVMPHRSLANLVAWQARASSLGPGARTLQFAGLgfdVSVQEIF----STLCAGATLVLPPeevRTDPPALAAWLdEQRIS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 248 MMGVPTFYTR-LVQDERLTPEATANMR-LFVSGSA-PLTAETHEAFEAKTGHAILERYGMTETNM----NLSNPYDGARR 320
Cdd:cd17651 230 RVFLPTVALRaLAEHGRPLGVRLAALRyLLTGGEQlVLTEDLREFCAGLPGLRLHNHYGPTETHVvtalSLPGDPAAWPA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 321 AGTVGMPLPGVEMRITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGF------FITGDLAMVDEQGYV 394
Cdd:cd17651 310 PPPIGRPIDNTRVYVLD-AALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFvpgarmYRTGDLARWLPDGEL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 395 HIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLgenQLEEEKviTHLDGRLA 474
Cdd:cd17651 389 EFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPV---DAAELR--AALATHLP 463
|
490 500
....*....|....*....|....*...
gi 2136495511 475 KYKQPKRVFFVDELPRNTMGKVQKNELR 502
Cdd:cd17651 464 EYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
32-508 |
6.15e-49 |
|
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: 176.64 E-value: 6.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 32 YTDALTISAQLAGALTELGVKQ--GDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVCRP 109
Cdd:cd05927 8 YKEVAERADNIGSALRSLGGKPapASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCDA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 110 KIEeqalslaaetgcpaVVTLgsaadgslmetaqaavprEDIVALGER-----------DLAAILYTSGTTGRSKGAMLT 178
Cdd:cd05927 88 GVK--------------VYSL------------------EEFEKLGKKnkvpppppkpeDLATICYTSGTTGNPKGVMLT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 179 HKNLASNA----KTLARAWHFSADDRLIHALPIFHTHGLFVACnVTLMAGASMLFlpkFDADV--IFEELP--RGTVMMG 250
Cdd:cd05927 136 HGNIVSNVagvfKILEILNKINPTDVYISYLPLAHIFERVVEA-LFLYHGAKIGF---YSGDIrlLLDDIKalKPTVFPG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 251 VPTFYTRL-------VQD-----ERLTPEATA-------------------------------NMRLFVSGSAPLTAETH 287
Cdd:cd05927 212 VPRVLNRIydkifnkVQAkgplkRKLFNFALNyklaelrsgvvraspfwdklvfnkikqalggNVRLMLTGSAPLSPEVL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 288 EAFEAKTGHAILERYGMTETN--MNLSNPYDgaRRAGTVGMPLPGVEMRIT-----NRETGAEVPFGEIgmlQIRGPNVF 360
Cdd:cd05927 292 EFLRVALGCPVLEGYGQTECTagATLTLPGD--TSVGHVGGPLPCAEVKLVdvpemNYDAKDPNPRGEV---CIRGPNVF 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 361 IGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRDKDLV-ISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDF 439
Cdd:cd05927 367 SGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIENIYARSPFVAQIFVYGDSLKSF 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 440 gegVTAVVV----------RQQG------ADLGENQ------LEEEKVITHLDGrLAKYKQPKRVFFVDEL--PRNTM-- 493
Cdd:cd05927 447 ---LVAIVVpdpdvlkewaASKGggtgsfEELCKNPevkkaiLEDLVRLGKENG-LKGFEQVKAIHLEPEPfsVENGLlt 522
|
570
....*....|....*..
gi 2136495511 494 --GKVQKNELRKRFNDT 508
Cdd:cd05927 523 ptFKLKRPQLKKYYKKQ 539
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
41-487 |
8.84e-49 |
|
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: 175.73 E-value: 8.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 41 QLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAE-PALFVcrPKIEEQAlslA 119
Cdd:cd05932 18 RLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSEsKALFV--GKLDDWK---A 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 120 AETGCPAVVTLGSAADGSLM------ETAQA-AVPREDIVALGERDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARA 192
Cdd:cd05932 93 MAPGVPEGLISISLPPPSAAncqyqwDDLIAqHPPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEH 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 193 WHFSADDRLIHALPIFH-THGLFVACNvTLMAGASMLF---LPKFDADVifeELPRGTVMMGVPTFYTRL---VQDErlT 265
Cdd:cd05932 173 IGTEENDRMLSYLPLAHvTERVFVEGG-SLYGGVLVAFaesLDTFVEDV---QRARPTLFFSVPRLWTKFqqgVQDK--I 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 266 PEATANM------------------------RLFVSGSAPLTAETHEAFEaKTGHAILERYGMTEtNMNLSN-PYDGARR 320
Cdd:cd05932 247 PQQKLNLllkipvvnslvkrkvlkglgldqcRLAGCGSAPVPPALLEWYR-SLGLNILEAYGMTE-NFAYSHlNYPGRDK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 321 AGTVGMPLPGVEMRItnretgaevpfGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRD 400
Cdd:cd05932 325 IGTVGNAGPGVEVRI-----------SEDGEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 401 KDLV-ISGGYNVYPKEVEQVIDELDQVAESAVIG--LPHPdFGEGVTAVVVRQQGADLGENQLEE--EKVITHLDGRLAK 475
Cdd:cd05932 394 KDIFkTSKGKYVAPAPIENKLAEHDRVEMVCVIGsgLPAP-LALVVLSEEARLRADAFARAELEAslRAHLARVNSTLDS 472
|
490
....*....|..
gi 2136495511 476 YKQPKRVFFVDE 487
Cdd:cd05932 473 HEQLAGIVVVKD 484
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
22-507 |
1.27e-48 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 176.51 E-value: 1.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 22 ITTRDGRRYRYTDALTISAQ---LAGAL-TELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFL 97
Cdd:PRK05620 28 VTTWGGAEQEQTTFAAIGARaaaLAHALhDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHII 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 98 NDAEPALFVCRPKIEEQALSLAAEtgCP---AVVTLGsaadGSLMETAQAAVPRE-----------------DIVALGER 157
Cdd:PRK05620 108 NHAEDEVIVADPRLAEQLGEILKE--CPcvrAVVFIG----PSDADSAAAHMPEGikvysyealldgrstvyDWPELDET 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 158 DLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSA--DDRLIHALPIFH--THGLFVAcnvTLMAGASMLFlPKF 233
Cdd:PRK05620 182 TAAAICYSTGTTGAPKGVVYSHRSLYLQSLSLRTTDSLAVthGESFLCCVPIYHvlSWGVPLA---AFMSGTPLVF-PGP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 234 D------ADVIFEELPRgtVMMGVPTFYTRL-VQDERLTPEATANMRLFVSGSaPLTAETHEAFEAKTGHAILERYGMTE 306
Cdd:PRK05620 258 DlsaptlAKIIATAMPR--VAHGVPTLWIQLmVHYLKNPPERMSLQEIYVGGS-AVPPILIKAWEERYGVDVVHVWGMTE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 307 TNMnlsnpydgarrAGTVGMPLPGV--EMRITNRETGAEVPF---------GEI--------GMLQIRGPNVFIGYWRMP 367
Cdd:PRK05620 335 TSP-----------VGTVARPPSGVsgEARWAYRVSQGRFPAsleyrivndGQVmestdrneGEIQVRGNWVTASYYHSP 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 368 ----------------EKTREELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAV 431
Cdd:PRK05620 404 teegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAV 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2136495511 432 IGLPHPDFGEGVTAVVVRQQGADlgENQLEEEKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRKRFND 507
Cdd:PRK05620 484 IGYPDDKWGERPLAVTVLAPGIE--PTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHLAD 557
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
1-506 |
1.83e-48 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 175.58 E-value: 1.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 1 MSH---NLFETFAAKMRERAEADFITTRDG-RRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLR 76
Cdd:PRK05857 9 MPQlpsTVLDRVFEQARQQPEAIALRRCDGtSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 77 IGGVYLPLNTGYTGDEIRYFLNDAEPALFVCRPKIEEQALSLA-AETGCPAVVTLGSAADGSLMETAQAAVPREDIvALG 155
Cdd:PRK05857 89 LGAIAVMADGNLPIAAIERFCQITDPAAALVAPGSKMASSAVPeALHSIPVIAVDIAAVTRESEHSLDAASLAGNA-DQG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 156 ERDLAAILYTSGTTGRSKGAMLTHKNLASNAKTL---ARAW-HFSADDRLIHALPIFHTHGLFVACNvTLMAGASMLFLP 231
Cdd:PRK05857 168 SEDPLAMIFTSGTTGEPKAVLLANRTFFAVPDILqkeGLNWvTWVVGETTYSPLPATHIGGLWWILT-CLMHGGLCVTGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 232 KFDADVIfEELPRGTVMMG--VPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAkTGHAILERYGMTETNM 309
Cdd:PRK05857 247 ENTTSLL-EILTTNAVATTclVPTLLSKLVSELKSANATVPSLRLVGYGGSRAIAADVRFIEA-TGVRTAQVYGLSETGC 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 310 N-LSNPYDGAR----RAGTVGMPLPGVEMRITNRETGAEV-----PFGEIGMLQIRGPNVFIGYWRMPEKTREeLLDDGF 379
Cdd:PRK05857 325 TaLCLPTDDGSivkiEAGAVGRPYPGVDVYLAATDGIGPTapgagPSASFGTLWIKSPANMLGYWNNPERTAE-VLIDGW 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 380 FITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGENQ 459
Cdd:PRK05857 404 VNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESAAR 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2136495511 460 LEEEKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRKRFN 506
Cdd:PRK05857 484 ALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAAT 530
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
39-496 |
5.02e-48 |
|
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: 178.90 E-value: 5.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 39 SAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVCrpkiEEQALSL 118
Cdd:COG1020 511 ANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLT----QSALAAR 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 119 AAETGCPaVVTLgsaaDGSLMETAQAAVPredIVALGERDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSAD 198
Cdd:COG1020 587 LPELGVP-VLAL----DALALAAEPATNP---PVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPG 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 199 DRLIHALPI---FHTHGLFVAcnvtLMAGASMLFLPK---FDADVIFEELPRG--TVMMGVPTFYTRLVQDErltPEATA 270
Cdd:COG1020 659 DRVLQFASLsfdASVWEIFGA----LLSGATLVLAPPearRDPAALAELLARHrvTVLNLTPSLLRALLDAA---PEALP 731
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 271 NMRLFVSGSAPLTAETHEAFEAKTGHAILE-RYGMTET----NMNLSNPYDGARRAGTVGMPLPGVEMRITNrETGAEVP 345
Cdd:COG1020 732 SLRLVLVGGEALPPELVRRWRARLPGARLVnLYGPTETtvdsTYYEVTPPDADGGSVPIGRPIANTRVYVLD-AHLQPVP 810
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 346 FGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFI-------TGDLAMVDEQGYVHIVGRDKDLV-ISgGYNVYPKEVE 417
Cdd:COG1020 811 VGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFpgarlyrTGDLARWLPDGNLEFLGRADDQVkIR-GFRIELGEIE 889
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2136495511 418 QVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGENQLEEekvitHLDGRLAKYKQPKRVFFVDELPRNTMGKV 496
Cdd:COG1020 890 AALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRL-----ALALLLPPYMVPAAVVLLLPLPLTGNGKL 963
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
5-501 |
1.24e-47 |
|
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: 172.00 E-value: 1.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 5 LFETFAAKMRERAEAdfitTRDGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPL 84
Cdd:cd12117 2 LFEEQAARTPDAVAV----VYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 85 NTGYTGDEIRYFLNDAEPALFVCRPKIEEQALSLaaetgCPAVVTLGSAadgslmETAQAAVPRediVALGERDLAAILY 164
Cdd:cd12117 78 DPELPAERLAFMLADAGAKVLLTDRSLAGRAGGL-----EVAVVIDEAL------DAGPAGNPA---VPVSPDDLAYVMY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 165 TSGTTGRSKGAMLTHKNLASNAKTlARAWHFSADDRLIHALPI-FH--THGLFVAcnvtLMAGASMLFLPK---FDADVI 238
Cdd:cd12117 144 TSGSTGRPKGVAVTHRGVVRLVKN-TNYVTLGPDDRVLQTSPLaFDasTFEIWGA----LLNGARLVLAPKgtlLDPDAL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 239 FEELPRG--TVM-MGVPTFytRLVQDERltPEATANMR-LFVSGSAPLTAETHEAFEAKTGHAILERYGMTEtNMNLSNP 314
Cdd:cd12117 219 GALIAEEgvTVLwLTAALF--NQLADED--PECFAGLReLLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTE-NTTFTTS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 315 Y---DGARRAGTV--GMPLPGVEMRITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGF------FITG 383
Cdd:cd12117 294 HvvtELDEVAGSIpiGRPIANTRVYVLD-EDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFgpgerlYRTG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 384 DLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVrqqgadlGENQLEEE 463
Cdd:cd12117 373 DLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVV-------AEGALDAA 445
|
490 500 510
....*....|....*....|....*....|....*...
gi 2136495511 464 KVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNEL 501
Cdd:cd12117 446 ELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
32-487 |
5.07e-47 |
|
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: 170.86 E-value: 5.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 32 YTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGgvyLPLNTGYTgdeiryflNDAEPALFvcrpki 111
Cdd:cd17639 8 YAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYA--------TLGEDALI------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 112 eeQALSlaaETGCPAVVTLGSAadgslmetaqaavpredivalgeRDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLAR 191
Cdd:cd17639 71 --HSLN---ETECSAIFTDGKP-----------------------DDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 192 --AWHFSADDRLIHALPIFHTHGlFVACNVTLMAGASMLF-LPKFDADVIFEElPRG-------TVMMGVP--------- 252
Cdd:cd17639 123 rvPELLGPDDRYLAYLPLAHIFE-LAAENVCLYRGGTIGYgSPRTLTDKSKRG-CKGdltefkpTLMVGVPaiwdtirkg 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 253 ------------------TFYTRLVQDERL--TP-----------EATA-NMRLFVSGSAPLTAETHEaFEAKTGHAILE 300
Cdd:cd17639 201 vlaklnpmgglkrtlfwtAYQSKLKALKEGpgTPlldelvfkkvrAALGgRLRYMLSGGAPLSADTQE-FLNIVLCPVIQ 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 301 RYGMTET--NMNLSNPYDgaRRAGTVGMPLPGVEMRITNRE-----TGAEVPFGEIgmlQIRGPNVFIGYWRMPEKTREE 373
Cdd:cd17639 280 GYGLTETcaGGTVQDPGD--LETGRVGPPLPCCEIKLVDWEeggysTDKPPPRGEI---LIRGPNVFKGYYKNPEKTKEA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 374 LLDDGFFITGDLAMVDEQGYVHIVGRDKDLV-ISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFgegVTAVVVRQQG 452
Cdd:cd17639 355 FDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVkLQNGEYIALEKLESIYRSNPLVNNICVYADPDKSY---PVAIVVPNEK 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2136495511 453 A------------DLGENQLEEEKVI---------THLDGRLAKYKQPKRVFFVDE 487
Cdd:cd17639 432 HltklaekhgvinSEWEELCEDKKLQkavlkslaeTARAAGLEKFEIPQGVVLLDE 487
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
28-504 |
2.66e-46 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 170.08 E-value: 2.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 28 RRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEailLY---LACLRIGGVYLPLNTGYTGDEIRYFLNDAEPAL 104
Cdd:PRK04319 72 EKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPE---LYfalLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 105 FVCRPKIEEQALslAAETgcPAVVTL------GSAADG--SLMETAQAAVPREDIVALGERDLAAILYTSGTTGRSKGAM 176
Cdd:PRK04319 149 LITTPALLERKP--ADDL--PSLKHVllvgedVEEGPGtlDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 177 LTHKNLASNAKTLARAWHFSADDRL-IHALPIFHT---HGLFVAcnvtLMAGASMLFL-PKFDADV---IFEELpRGTVM 248
Cdd:PRK04319 225 HVHNAMLQHYQTGKYVLDLHEDDVYwCTADPGWVTgtsYGIFAP----WLNGATNVIDgGRFSPERwyrILEDY-KVTVW 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 249 MGVPTFYTRLVQ--DERLTPEATANMRLFVSGSAPLTAET----HEAFeaktGHAILERYGMTETNMNL-SNPYDGARRA 321
Cdd:PRK04319 300 YTAPTAIRMLMGagDDLVKKYDLSSLRHILSVGEPLNPEVvrwgMKVF----GLPIHDNWWMTETGGIMiANYPAMDIKP 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 322 GTVGMPLPGVEMRITNREtGAEVPFGEIGMLQIRG--PNVFIGYWRMPEKTREELLDdGFFITGDLAMVDEQGYVHIVGR 399
Cdd:PRK04319 376 GSMGKPLPGIEAAIVDDQ-GNELPPNRMGNLAIKKgwPSMMRGIWNNPEKYESYFAG-DWYVSGDSAYMDEDGYFWFQGR 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 400 DKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGEnQLEEEkVITHLDGRLAKYKQP 479
Cdd:PRK04319 454 VDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSE-ELKEE-IRGFVKKGLGAHAAP 531
|
490 500
....*....|....*....|....*
gi 2136495511 480 KRVFFVDELPRNTMGKVQKNELRKR 504
Cdd:PRK04319 532 REIEFKDKLPKTRSGKIMRRVLKAW 556
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
30-501 |
8.30e-46 |
|
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: 166.33 E-value: 8.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 30 YRYTDALtiSAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVCRP 109
Cdd:cd17643 15 YGELDAR--ANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLLLTDP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 110 KieeqalslaaetgcpavvtlgsaadgslmetaqaavpredivalgerDLAAILYTSGTTGRSKGAMLTHKNLASNAKTL 189
Cdd:cd17643 93 D-----------------------------------------------DLAYVIYTSGSTGRPKGVVVSHANVLALFAAT 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 190 ARAWHFSADDRLIhalpIFHTHG-------LFVAcnvtLMAGASMLFLPK-------FDADVIFEElpRGTVMMGVPTFY 255
Cdd:cd17643 126 QRWFGFNEDDVWT----LFHSYAfdfsvweIWGA----LLHGGRLVVVPYevarspeDFARLLRDE--GVTVLNQTPSAF 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 256 TRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHA---ILERYGMTETNMN-----LSNPYDGARRAGTVGMP 327
Cdd:cd17643 196 YQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLDrpqLVNMYGITETTVHvtfrpLDAADLPAAAASPIGRP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 328 LPGVEMRITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGF-------FITGDLAMVDEQGYVHIVGRD 400
Cdd:cd17643 276 LPGLRVYVLD-ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFggpgsrmYRTGDLARRLPDGELEYLGRA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 401 KDLVISGGYNVYPKEVEQVIDELDQVAESAVIglPHpDFGEGVT---AVVVRQQGADLGENQLEEekvitHLDGRLAKYK 477
Cdd:cd17643 355 DEQVKIRGFRIELGEIEAALATHPSVRDAAVI--VR-EDEPGDTrlvAYVVADDGAAADIAELRA-----LLKELLPDYM 426
|
490 500
....*....|....*....|....
gi 2136495511 478 QPKRVFFVDELPRNTMGKVQKNEL 501
Cdd:cd17643 427 VPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
165-512 |
1.09e-44 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 163.24 E-value: 1.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 165 TSGTTGRSKGAMLTHKNLASNAKTLARawHFSADDrlIHA---LPIFHTHGLFVACNvTLMAGASMLFLPkfdadviFEE 241
Cdd:PRK07445 128 TGGSSGQIRFAIHTWETLTASVQGFQR--YFQLQQ--VNSfcvLPLYHVSGLMQFMR-SFLTGGKLVILP-------YKR 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 242 LPRGTVM-MGVPTFYTRLV--QDERLTPEAT---ANMRLFVSGSAPLTAETHEafEAKTGHAILE-RYGMTETNMNLSNP 314
Cdd:PRK07445 196 LKSGQELpPNPSDFFLSLVptQLQRLLQLRPqwlAQFRTILLGGAPAWPSLLE--QARQLQLRLApTYGMTETASQIATL 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 315 YDGARRAG--TVGMPLPGVEMRITNretgaevpfGEIGMLQIRGPNVFIGYWrmPEktreeLLD-DGFFITGDLAMVDEQ 391
Cdd:PRK07445 274 KPDDFLAGnnSSGQVLPHAQITIPA---------NQTGNITIQAQSLALGYY--PQ-----ILDsQGIFETDDLGYLDAQ 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 392 GYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGadlgenQLEEEKVITHLDG 471
Cdd:PRK07445 338 GYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP------SISLEELKTAIKD 411
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2136495511 472 RLAKYKQPKRVFFVDELPRNTMGKVQKNELRKRFNDTYQTP 512
Cdd:PRK07445 412 QLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQRLGLP 452
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
28-496 |
1.22e-44 |
|
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: 165.83 E-value: 1.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 28 RRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVC 107
Cdd:cd17634 83 RTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLIT 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 108 -----RP-------KIEEQALSLAAeTGCPAVVTL---GSAADGS------LMETAQAAVPREDIVALGERDLAAILYTS 166
Cdd:cd17634 163 adggvRAgrsvplkKNVDDALNPNV-TSVEHVIVLkrtGSDIDWQegrdlwWRDLIAKASPEHQPEAMNAEDPLFILYTS 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 167 GTTGRSKGAMLTHKNLASNAKTLAR---------AWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDADV 237
Cdd:cd17634 242 GTTGKPKGVLHTTGGYLVYAATTMKyvfdygpgdIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNWPTPARMWQV 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 238 IFEElprgtvmmGVPTFYTRLVQDERLTPEAT--------ANMRLFVSGSAPLTAETHEAFEAKTGHA---ILERYGMTE 306
Cdd:cd17634 322 VDKH--------GVNILYTAPTAIRALMAAGDdaiegtdrSSLRILGSVGEPINPEAYEWYWKKIGKEkcpVVDTWWQTE 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 307 TNMNLSNPYDGAR--RAGTVGMPLPGVEMRITNREtGAEVPFGEIGMLQIRG--PNVFIGYWRMPEKTREELLD--DGFF 380
Cdd:cd17634 394 TGGFMITPLPGAIelKAGSATRPVFGVQPAVVDNE-GHPQPGGTEGNLVITDpwPGQTRTLFGDHERFEQTYFStfKGMY 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 381 ITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGENQL 460
Cdd:cd17634 473 FSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELY 552
|
490 500 510
....*....|....*....|....*....|....*...
gi 2136495511 461 EE--EKVITHLdGRLAkykQPKRVFFVDELPRNTMGKV 496
Cdd:cd17634 553 AElrNWVRKEI-GPLA---TPDVVHWVDSLPKTRSGKI 586
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
39-501 |
7.08e-44 |
|
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: 161.73 E-value: 7.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 39 SAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEpALFVCrpkIEEQALSL 118
Cdd:cd17655 32 ANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSG-ADILL---TQSHLQPP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 119 AAETGcpaVVTLGSAADGSLMETAQAAVPREdivalgERDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSAD 198
Cdd:cd17655 108 IAFIG---LIDLLDEDTIYHEESENLEPVSK------SDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEH 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 199 DRLIHALP---------IFHT----HGLFVACNVTLMAGASML-FLPKFDADVIFeelprgtvmmGVPTfYTRLVQDERL 264
Cdd:cd17655 179 LRVALFASisfdasvteIFASllsgNTLYIVRKETVLDGQALTqYIRQNRITIID----------LTPA-HLKLLDAADD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 265 TPEatANMRLFVSGSAPLTAETHEAFEAKTGHA--ILERYGMTETNMNLS-NPYDGARRAGT---VGMPLPGVEMRITNr 338
Cdd:cd17655 248 SEG--LSLKHLIVGGEALSTELAKKIIELFGTNptITNAYGPTETTVDASiYQYEPETDQQVsvpIGKPLGNTRIYILD- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 339 ETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGF------FITGDLAMVDEQGYVHIVGRDKDLVISGGYNVY 412
Cdd:cd17655 325 QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFvpgermYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 413 PKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVrqqgadlGENQLEEEKVITHLDGRLAKYKQPKrvFFV--DELPR 490
Cdd:cd17655 405 LGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIV-------SEKELPVAQLREFLARELPDYMIPS--YFIklDEIPL 475
|
490
....*....|.
gi 2136495511 491 NTMGKVQKNEL 501
Cdd:cd17655 476 TPNGKVDRKAL 486
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
3-448 |
1.40e-43 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 163.73 E-value: 1.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 3 HNLFETFAAKMREraeADFITTR---DGR--RYR---YTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLAC 74
Cdd:PLN02736 47 HDNFVYAVETFRD---YKYLGTRirvDGTvgEYKwmtYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHAC 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 75 LRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVCRPKIEEQALSLAAEtgCPAV---VTLGsAADGSLMETAQAA----VP 147
Cdd:PLN02736 124 SAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQTLNTLLSCLSE--IPSVrliVVVG-GADEPLPSLPSGTgveiVT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 148 REDIVALGER-----------DLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHthgLFVA 216
Cdd:PLN02736 201 YSKLLAQGRSspqpfrppkpeDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAH---IYER 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 217 CNVTLM--AGASMLFlpkFDADVI-----FEELpRGTVMMGVPTFYTRL-------VQD-----ERLTPEATA------- 270
Cdd:PLN02736 278 VNQIVMlhYGVAVGF---YQGDNLklmddLAAL-RPTIFCSVPRLYNRIydgitnaVKEsgglkERLFNAAYNakkqale 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 271 -----------------------NMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNMNLSNPYDGARRAGTVGMP 327
Cdd:PLN02736 354 ngknpspmwdrlvfnkikaklggRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSP 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 328 LPGVE--------MRITNREtgAEVPFGEIGmlqIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGR 399
Cdd:PLN02736 434 NPACEvklvdvpeMNYTSED--QPYPRGEIC---VRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDR 508
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2136495511 400 DKDLV-ISGGYNVYPKEVEQVIDELDQVAESAVIGlphPDFGEGVTAVVV 448
Cdd:PLN02736 509 KKNIFkLAQGEYIAPEKIENVYAKCKFVAQCFVYG---DSLNSSLVAVVV 555
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
41-502 |
4.27e-43 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 161.34 E-value: 4.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 41 QLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPA-LFVCR---PKIEEQAL 116
Cdd:PLN03102 51 RLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKiLFVDRsfePLAREVLH 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 117 SLAAETGCPAV----------VTLGSAADGSLMETAQAAVPREDIVAL-----GERDLAAILYTSGTTGRSKGAMLTHKN 181
Cdd:PLN03102 131 LLSSEDSNLNLpvifiheidfPKRPSSEELDYECLIQRGEPTPSLVARmfriqDEHDPISLNYTSGTTADPKGVVISHRG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 182 LASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLfLPKFDADVIFE--ELPRGTVMMGVPTFYTRLV 259
Cdd:PLN03102 211 AYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVC-MRHVTAPEIYKniEMHNVTHMCCVPTVFNILL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 260 QDERLT-PEATANMRLFVSGSAPLTAETHEAfeAKTGHAILERYGMTETN--------------MNLSNPYDGARRAGTV 324
Cdd:PLN03102 290 KGNSLDlSPRSGPVHVLTGGSPPPAALVKKV--QRLGFQVMHAYGLTEATgpvlfcewqdewnrLPENQQMELKARQGVS 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 325 GMPLPGVEMRitNRETGAEVP-----FGEIgmlQIRGPNVFIGYWRMPEKTREELlDDGFFITGDLAMVDEQGYVHIVGR 399
Cdd:PLN03102 368 ILGLADVDVK--NKETQESVPrdgktMGEI---VIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDR 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 400 DKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADlgENQLEEEKVITHlDGRLAKYKQ- 478
Cdd:PLN03102 442 SKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGET--TKEDRVDKLVTR-ERDLIEYCRe 518
|
490 500 510
....*....|....*....|....*....|.
gi 2136495511 479 -------PKRVFFVDELPRNTMGKVQKNELR 502
Cdd:PLN03102 519 nlphfmcPRKVVFLQELPKNGNGKILKPKLR 549
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
28-503 |
6.17e-43 |
|
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: 161.33 E-value: 6.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 28 RRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALF-- 105
Cdd:cd05967 81 RTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLIvt 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 106 ----------VCRPKIEEQALSLAAETG----------CPAV-VTLGSAAD-GSLMETAQaavpREDIVALGERDLAAIL 163
Cdd:cd05967 161 ascgiepgkvVPYKPLLDKALELSGHKPhhvlvlnrpqVPADlTKPGRDLDwSELLAKAE----PVDCVPVAATDPLYIL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 164 YTSGTTGRSKGAMLTHKNLAsnaktLARAWHFsaddRLIHALPIFHThgLFVACNV------------TLMAGAsmlflp 231
Cdd:cd05967 237 YTSGTTGKPKGVVRDNGGHA-----VALNWSM----RNIYGIKPGDV--WWAASDVgwvvghsyivygPLLHGA------ 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 232 kfdADVIFEELPRGTVMMGVptfYTRLVQDERLT-----PEATANMR-------------------LFVSGSaPLTAETH 287
Cdd:cd05967 300 ---TTVLYEGKPVGTPDPGA---FWRVIEKYQVNalftaPTAIRAIRkedpdgkyikkydlsslrtLFLAGE-RLDPPTL 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 288 EAFEAKTGHAILERYGMTETN----MNLSNPYDGARRAGTVGMPLPGVEMRITNrETGAEVPFGEIGMLQIRGP---NVF 360
Cdd:cd05967 373 EWAENTLGVPVIDHWWQTETGwpitANPVGLEPLPIKAGSPGKPVPGYQVQVLD-EDGEPVGPNELGNIVIKLPlppGCL 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 361 IGYWRMPEKTREELL--DDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPD 438
Cdd:cd05967 452 LTLWKNDERFKKLYLskFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDEL 531
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2136495511 439 FGEGVTAVVVRQQGADLGENQLEEEkVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRK 503
Cdd:cd05967 532 KGQVPLGLVVLKEGVKITAEELEKE-LVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRK 595
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
7-503 |
1.60e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 158.69 E-value: 1.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 7 ETFAAKMRERAE-ADFITTRDGRRYRYTDALTISAQLAGALTELGVKQGDR-VAVQVDKSPEAILLYLACLRIGGVYLPL 84
Cdd:PRK07867 5 PTVAELLLPLAEdDDRGLYFEDSFTSWREHIRGSAARAAALRARLDPTRPPhVGVLLDNTPEFSLLLGAAALSGIVPVGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 85 NTGYTGDEIRYFLNDAEpalfvCRPKIEEQA---LSLAAETGCPAVVTLGSAADGSLMETAQAAVPREDIVAlgeRDLAA 161
Cdd:PRK07867 85 NPTRRGAALARDIAHAD-----CQLVLTESAhaeLLDGLDPGVRVINVDSPAWADELAAHRDAEPPFRVADP---DDLFM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 162 ILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDADVIFEE 241
Cdd:PRK07867 157 LIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRKFSASGFLPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 242 LPR--GTVM--MGVPTFY---TRLVQDERLTPeatanMRLFVSGSAplTAETHEAFEAKTGHAILERYGMTETNMNLSNP 314
Cdd:PRK07867 237 VRRygATYAnyVGKPLSYvlaTPERPDDADNP-----LRIVYGNEG--APGDIARFARRFGCVVVDGFGSTEGGVAITRT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 315 YDGarRAGTVGMPLPGVEmrITNRETGAEVPFGEIG-------------MLQIRGPNVFIGYWRMPEKTREELlDDGFFI 381
Cdd:PRK07867 310 PDT--PPGALGPLPPGVA--IVDPDTGTECPPAEDAdgrllnadeaigeLVNTAGPGGFEGYYNDPEADAERM-RGGVYW 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 382 TGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGENQLE 461
Cdd:PRK07867 385 SGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFA 464
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2136495511 462 EekvitHLDGR--LAKYKQPKRVFFVDELPRNTMGKVQKNELRK 503
Cdd:PRK07867 465 E-----FLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
4-501 |
1.82e-42 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 158.62 E-value: 1.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 4 NLFETFAAKMRERAEADFITTRDGRrYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLP 83
Cdd:PRK13383 36 NPYTLLAVTAARWPGRTAIIDDDGA-LSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 84 LNTGYTGDEIRYFLNDAEPALFVCRPKIEEQalsLAAETGCPAVVTLGSAadgslmeTAQAAVPREDIVALGErdlaAIL 163
Cdd:PRK13383 115 ISTEFRSDALAAALRAHHISTVVADNEFAER---IAGADDAVAVIDPATA-------GAEESGGRPAVAAPGR----IVL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 164 YTSGTTGRSKGAMLTHKnLASNAK---TLARAWHFSADDRLIHALPIFHTHGLFVACnVTLMAGASMLFLPKFDADVIFE 240
Cdd:PRK13383 181 LTSGTTGKPKGVPRAPQ-LRSAVGvwvTILDRTRLRTGSRISVAMPMFHGLGLGMLM-LTIALGGTVLTHRHFDAEAALA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 241 E--LPRGTVMMGVPTFYTRLVQderLTPEATAN-----MRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNMN-LS 312
Cdd:PRK13383 259 QasLHRADAFTAVPVVLARILE---LPPRVRARnplpqLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIGaLA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 313 NPYDGARRAGTVGMPLPGVEMRI---TNRETGAEVpfgeIGMLQIRGPNVFIGYWRMPEKTreelLDDGFFITGDLAMVD 389
Cdd:PRK13383 336 TPADLRDAPETVGKPVAGCPVRIldrNNRPVGPRV----TGRIFVGGELAGTRYTDGGGKA----VVDGMTSTGDMGYLD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 390 EQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGENQLEEekvitHL 469
Cdd:PRK13383 408 NAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRD-----YL 482
|
490 500 510
....*....|....*....|....*....|..
gi 2136495511 470 DGRLAKYKQPKRVFFVDELPRNTMGKVQKNEL 501
Cdd:PRK13383 483 KDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
7-512 |
3.05e-42 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 160.20 E-value: 3.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 7 ETFAAKMRERA-EADFIttrDGRRYRYTDALTI------SAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGG 79
Cdd:PRK06060 4 GNLAGLLAEQAsEAGWY---DRPAFYAADVVTHgqihdgAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 80 VYLPLNTGYTGDEIRYFLNDAEPALFVCRPKIEEQALSlaaetgcpavVTLGSAADgsLMETAQAAVPrEDIVALGERDL 159
Cdd:PRK06060 81 MAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQP----------SRVAEAAE--LMSEAARVAP-GGYEPMGGDAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 160 AAILYTSGTTGRSKGAMLTHKNLASNAKTLAR-AWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLP-KFDADV 237
Cdd:PRK06060 148 AYATYTSGTTGPPKAAIHRHADPLTFVDAMCRkALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSaPVTPEA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 238 I------FEElprgTVMMGVPTFYTRLVqdERLTPEATANMRLFVSGSAPLTAETHEAF-EAKTGHAILERYGMTETNMN 310
Cdd:PRK06060 228 AailsarFGP----SVLYGVPNFFARVI--DSCSPDSFRSLRCVVSAGEALELGLAERLmEFFGGIPILDGIGSTEVGQT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 311 -LSNPYDgARRAGTVGMPLPGVEMRITNRETGAEVPFGEiGMLQIRGPNVFIGYWRMPEKTreeLLDDGFFITGDLAMVD 389
Cdd:PRK06060 302 fVSNRVD-EWRLGTLGRVLPPYEIRVVAPDGTTAGPGVE-GDLWVRGPAIAKGYWNRPDSP---VANEGWLDTRDRVCID 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 390 EQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGENQLEEekVITHL 469
Cdd:PRK06060 377 SDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRD--LHRGL 454
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2136495511 470 DGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRKrfndtyQTP 512
Cdd:PRK06060 455 LNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRK------QSP 491
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
41-501 |
6.24e-42 |
|
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: 155.10 E-value: 6.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 41 QLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALfvcrpkieeqalslaa 120
Cdd:cd17652 24 RLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPAL---------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 121 etgcpaVVTLGSaadgslmetaqaavpredivalgerDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDR 200
Cdd:cd17652 88 ------LLTTPD-------------------------NLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 201 -LIHALPIFhtHGLFVACNVTLMAGASmLFLPkfdadvifeelPRGTVMMGVPtfYTRLVQDER-----LTPEATANM-- 272
Cdd:cd17652 137 vLQFASPSF--DASVWELLMALLAGAT-LVLA-----------PAEELLPGEP--LADLLREHRithvtLPPAALAALpp 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 273 ------RLFVSGSAPLTAETHEAFeaKTGHAILERYGMTETNMN--LSNPyDGARRAGTVGMPLPGVEMRITNRETgAEV 344
Cdd:cd17652 201 ddlpdlRTLVVAGEACPAELVDRW--APGRRMINAYGPTETTVCatMAGP-LPGGGVPPIGRPVPGTRVYVLDARL-RPV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 345 PFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGF-------FITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVE 417
Cdd:cd17652 277 PPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgapgsrmYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVE 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 418 QVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGENQLEEekvitHLDGRLAKYKQPKRVFFVDELPRNTMGKVQ 497
Cdd:cd17652 357 AALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRA-----HLAERLPGYMVPAAFVVLDALPLTPNGKLD 431
|
....
gi 2136495511 498 KNEL 501
Cdd:cd17652 432 RRAL 435
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
158-503 |
4.85e-41 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 158.21 E-value: 4.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 158 DLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDADV 237
Cdd:PRK06814 794 DPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYPSPLHYR 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 238 IFEELPRG---TVMMGVPTF---YTRLVQderltPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETN--M 309
Cdd:PRK06814 874 IIPELIYDtnaTILFGTDTFlngYARYAH-----PYDFRSLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETApvI 948
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 310 NLSNPYdgARRAGTVGMPLPGVEMRITnretgaEVP-FGEIGMLQIRGPNVFIGYWRmPEKTRE-ELLDDGFFITGDLAM 387
Cdd:PRK06814 949 ALNTPM--HNKAGTVGRLLPGIEYRLE------PVPgIDEGGRLFVRGPNVMLGYLR-AENPGVlEPPADGWYDTGDIVT 1019
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 388 VDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEgvtAVVVRQQGADLGENQLeeekvIT 467
Cdd:PRK06814 1020 IDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGE---RIILLTTASDATRAAF-----LA 1091
|
330 340 350
....*....|....*....|....*....|....*..
gi 2136495511 468 HLDGR-LAKYKQPKRVFFVDELPRNTMGKVQKNELRK 503
Cdd:PRK06814 1092 HAKAAgASELMVPAEIITIDEIPLLGTGKIDYVAVTK 1128
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
28-502 |
1.06e-40 |
|
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: 154.96 E-value: 1.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 28 RRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPAL--- 104
Cdd:cd05968 90 RTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKAlit 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 105 ---FVCRPK-IEEQALSLAAETGCPAV----------VTLGSAADGSLMETAQAAVPREDIVALGERDLAAILYTSGTTG 170
Cdd:cd05968 170 adgFTRRGReVNLKEEADKACAQCPTVekvvvvrhlgNDFTPAKGRDLSYDEEKETAGDGAERTESEDPLMIIYTSGTTG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 171 RSKGAMLTHKNLA-SNAKTLARAWHFSADDRLIHAL-------PIFHTHGLFVACNVTLMAGAsmlflPKFD-ADVIFEE 241
Cdd:cd05968 250 KPKGTVHVHAGFPlKAAQDMYFQFDLKPGDLLTWFTdlgwmmgPWLIFGGLILGATMVLYDGA-----PDHPkADRLWRM 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 242 LPR-GTVMMGV-PTFYTRLV--QDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHA---ILERYGMTETNMN-LSN 313
Cdd:cd05968 325 VEDhEITHLGLsPTLIRALKprGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGrnpIINYSGGTEISGGiLGN 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 314 PYDGARRAGTVGMPLPGVEMRITNrETGAEVPfGEIGMLQIRGPNVFI--GYWRMPEKTREELLD--DGFFITGDLAMVD 389
Cdd:cd05968 405 VLIKPIKPSSFNGPVPGMKADVLD-ESGKPAR-PEVGELVLLAPWPGMtrGFWRDEDRYLETYWSrfDNVWVHGDFAYYD 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 390 EQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGEnQLEEEkVITHL 469
Cdd:cd05968 483 EEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTE-ALAEE-LMERV 560
|
490 500 510
....*....|....*....|....*....|...
gi 2136495511 470 DGRLAKYKQPKRVFFVDELPRNTMGKVQKNELR 502
Cdd:cd05968 561 ADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
6-503 |
1.71e-40 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 154.26 E-value: 1.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 6 FETFAAKMRERaeaDFITTrDGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLN 85
Cdd:PRK08279 43 FEEAAARHPDR---PALLF-EDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 86 TGYTGDEIRYFLNDAEPALFV----CRPKIEEqALSLAAETGCPAVVTLGSAADGSLME---TAQAAVP------REDIV 152
Cdd:PRK08279 119 TQQRGAVLAHSLNLVDAKHLIvgeeLVEAFEE-ARADLARPPRLWVAGGDTLDDPEGYEdlaAAAAGAPttnpasRSGVT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 153 AlgeRDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPK 232
Cdd:PRK08279 198 A---KDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 233 FDA-----DVIFE---------ELPRgtvmmgvptfYTrLVQDErlTPEATANmRLFVSGSAPLTAETHEAFEAKTG-HA 297
Cdd:PRK08279 275 FSAsrfwdDVRRYratafqyigELCR----------YL-LNQPP--KPTDRDH-RLRLMIGNGLRPDIWDEFQQRFGiPR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 298 ILERYGMTETNMNLSNpYDGarRAGTVGMpLPGVEM---RIT--NRETGA----------EVPFGEIGML--QIRGPNVF 360
Cdd:PRK08279 341 ILEFYAASEGNVGFIN-VFN--FDGTVGR-VPLWLAhpyAIVkyDVDTGEpvrdadgrciKVKPGEVGLLigRITDRGPF 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 361 IGYwRMPEKTREELLDDGF------FITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGL 434
Cdd:PRK08279 417 DGY-TDPEASEKKILRDVFkkgdawFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGV 495
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2136495511 435 PHPDFG--EGVTAVVVRQQGAdlgenqLEEEKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRK 503
Cdd:PRK08279 496 EVPGTDgrAGMAAIVLADGAE------FDLAALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRK 560
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
26-501 |
2.78e-40 |
|
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: 151.08 E-value: 2.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 26 DGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALF 105
Cdd:cd17650 9 ATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 106 VCRPKieeqalslaaetgcpavvtlgsaadgslmetaqaavpredivalgerDLAAILYTSGTTGRSKGAMLTHKNLASN 185
Cdd:cd17650 89 LTQPE-----------------------------------------------DLAYVIYTSGTTGKPKGVMVEHRNVAHA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 186 AKTLARAWHFsadDRLIHALPIFHTHGLFVACN---VTLMAGASMLFLP---KFDADVIFEEL--PRGTVMMGVPTFYTR 257
Cdd:cd17650 122 AHAWRREYEL---DSFPVRLLQMASFSFDVFAGdfaRSLLNGGTLVICPdevKLDPAALYDLIlkSRITLMESTPALIRP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 258 L---VQDERLTPEAtanMRLFVSGSAPLTAETHEAFEAKTGHA--ILERYGMTETNMNlSNPYDGAR----RAGTV--GM 326
Cdd:cd17650 199 VmayVYRNGLDLSA---MRLLIVGSDGCKAQDFKTLAARFGQGmrIINSYGVTEATID-STYYEEGRdplgDSANVpiGR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 327 PLPGVEMRITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGF------FITGDLAMVDEQGYVHIVGRD 400
Cdd:cd17650 275 PLPNTAMYVLD-ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRV 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 401 KDLVISGGYNVYPKEVEQVIDELDQVAESAVIgLPHPDFGE-GVTAVVVRQQGADLgeNQLEEekvitHLDGRLAKYKQP 479
Cdd:cd17650 354 DHQVKIRGFRIELGEIESQLARHPAIDEAVVA-VREDKGGEaRLCAYVVAAATLNT--AELRA-----FLAKELPSYMIP 425
|
490 500
....*....|....*....|..
gi 2136495511 480 KRVFFVDELPRNTMGKVQKNEL 501
Cdd:cd17650 426 SYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1-503 |
3.67e-40 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 155.89 E-value: 3.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 1 MSHNLFETFAAKMRERAEADFittrDGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGV 80
Cdd:PRK12316 4552 CVHQLVAERARMTPDAVAVVF----DEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGA 4627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 81 YLPLNTGYTGDEIRYFLNDAEPALFVCRPKIEEQaLSLAAETGCPAVVTLGSAADGSlmetaqAAVPRediVALGERDLA 160
Cdd:PRK12316 4628 YVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQR-LPIPDGLASLALDRDEDWEGFP------AHDPA---VRLHPDNLA 4697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 161 AILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIH----ALPIFHtHGLFVAcnvtLMAGASMLFLPK--FD 234
Cdd:PRK12316 4698 YVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQfmsfSFDGSH-EGLYHP----LINGASVVIRDDslWD 4772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 235 ADVIFEELPRGTVMMGV--PTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNMNLS 312
Cdd:PRK12316 4773 PERLYAEIHEHRVTVLVfpPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVL 4852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 313 ----NPYDGARRAGT-VGMPLPGVEMRITNREtGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGF-------F 380
Cdd:PRK12316 4853 lwkaRDGDACGAAYMpIGTPLGNRSGYVLDGQ-LNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapggrlY 4931
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 381 ITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPdFGEGVTAVVVRQQG--ADLGEN 458
Cdd:PRK12316 4932 RTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGA-VGKQLVGYVVPQDPalADADEA 5010
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2136495511 459 QLEEEKVI-THLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRK 503
Cdd:PRK12316 5011 QAELRDELkAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQ 5056
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
26-504 |
4.07e-40 |
|
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: 153.10 E-value: 4.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 26 DGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALF 105
Cdd:cd05966 81 QSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKLV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 106 VC------RPK-IEEQALSLAAETGCPAV-------VTLGSAA--DG------SLMETAQAAVPREDIVAlgeRDLAAIL 163
Cdd:cd05966 161 ITadggyrGGKvIPLKEIVDEALEKCPSVekvlvvkRTGGEVPmtEGrdlwwhDLMAKQSPECEPEWMDS---EDPLFIL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 164 YTSGTTGRSKGAMLTHKNLASNAKTLARaWHFSaddrlIHALPIF-----------HTHGLFVAcnvtLMAGAsmlflpk 232
Cdd:cd05966 238 YTSGSTGKPKGVVHTTGGYLLYAATTFK-YVFD-----YHPDDIYwctadigwitgHSYIVYGP----LANGA------- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 233 fdADVIFEelprgtvmmGVPTF-----YTRLVQDERLT-----PEA----------------TANMRLFVSGSAPLTAET 286
Cdd:cd05966 301 --TTVMFE---------GTPTYpdpgrYWDIVEKHKVTifytaPTAiralmkfgdewvkkhdLSSLRVLGSVGEPINPEA 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 287 HEAFEAKTGH---AILERYGMTETNMNLSNPYDGAR--RAGTVGMPLPGVEMRITNrETGAEVPFGEIGMLQIRG--PNV 359
Cdd:cd05966 370 WMWYYEVIGKercPIVDTWWQTETGGIMITPLPGATplKPGSATRPFFGIEPAILD-EEGNEVEGEVEGYLVIKRpwPGM 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 360 FIGYWRMPEKTREELLDD--GFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHP 437
Cdd:cd05966 449 ARTIYGDHERYEDTYFSKfpGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHD 528
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2136495511 438 DFGEGVTAVVVRQQGADlGENQLEEEkVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRKR 504
Cdd:cd05966 529 IKGEAIYAFVTLKDGEE-PSDELRKE-LRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKI 593
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
29-505 |
4.13e-40 |
|
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: 151.49 E-value: 4.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 29 RYRYTDALtisaQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLrIGGvYLPLNTGYTGDEiryflnDAEPALFVCR 108
Cdd:cd05908 19 RHLREEAL----GYLGALQELGIKPGQEVVFQITHNNKFLYLFWACL-LGG-MIAVPVSIGSNE------EHKLKLNKVW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 109 PKIEEqalslaaetgcPAVVTlgsaadgslMETAQAAVPREdivalgerdLAAILYTSGTTGRSKGAMLTHKNLASNAKT 188
Cdd:cd05908 87 NTLKN-----------PYLIT---------EEEVLCELADE---------LAFIQFSSGSTGDPKGVMLTHENLVHNMFA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 189 LARAWHFSADDRLIHALPIFHTHGLfVACNVT-LMAGASMLFLPKfdadVIFEELP---------RGTVMMGVPTFYTRL 258
Cdd:cd05908 138 ILNSTEWKTKDRILSWMPLTHDMGL-IAFHLApLIAGMNQYLMPT----RLFIRRPilwlkkaseHKATIVSSPNFGYKY 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 259 VQDeRLTPEATAN-----MRLFVSGSAPLTAE-THEAFEAKTGH-----AILERYGMTETNMNLSNPYDGAR-------- 319
Cdd:cd05908 213 FLK-TLKPEKANDwdlssIRMILNGAEPIDYElCHEFLDHMSKYglkrnAILPVYGLAEASVGASLPKAQSPfktitlgr 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 320 --------------------RAGTVGMPLPGVEMRITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGF 379
Cdd:cd05908 292 rhvthgepepevdkkdseclTFVEVGKPIDETDIRICD-EDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGW 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 380 FITGDLAMVdEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQV--AESAVIGLPHPDF-GEGVTAVVVRQQGAD-- 454
Cdd:cd05908 371 LKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVelGRVVACGVNNSNTrNEEIFCFIEHRKSEDdf 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2136495511 455 --LGenqleeEKVITHLDGRlaKYKQPKRVFFVDELPRNTMGKVQKNELRKRF 505
Cdd:cd05908 450 ypLG------KKIKKHLNKR--GGWQINEVLPIRRIPKTTSGKVKRYELAQRY 494
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2-503 |
4.99e-40 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 155.50 E-value: 4.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 2 SHNLFETFAAKMRERAEADFITTrDGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVY 81
Cdd:PRK12316 2002 GPGVHQRIAEQAARAPEAIAVVF-GDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAY 2080
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 82 LPLNTGYTGDEIRYFLNDAEPALFVCRPKIEEQaLSLAAEtgcpaVVTLGSAADGSLMETAQAAvPRediVALGERDLAA 161
Cdd:PRK12316 2081 VPLDPNYPAERLAYMLEDSGAALLLTQRHLLER-LPLPAG-----VARLPLDRDAEWADYPDTA-PA---VQLAGENLAY 2150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 162 ILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPiFHTHGLFVACNVTLMAGASMLFLPK--FDADVIF 239
Cdd:PRK12316 2151 VIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMS-FSFDGAHEQWFHPLLNGARVLIRDDelWDPEQLY 2229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 240 EELPRGTVMMGV-PTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHE-AFEAKTGHAILERYGMTETNMNLSnpYDG 317
Cdd:PRK12316 2230 DEMERHGVTILDfPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRlAWEALRPVYLFNGYGPTEAVVTPL--LWK 2307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 318 ARRAGTVGMPLPGVEMRITNRET---GAE---VPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGF-------FITGD 384
Cdd:PRK12316 2308 CRPQDPCGAAYVPIGRALGNRRAyilDADlnlLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsasgerlYRTGD 2387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 385 LAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDfGEGVTAVVVrqqGADLGENQLEEEK 464
Cdd:PRK12316 2388 LARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGAS-GKQLVAYVV---PDDAAEDLLAELR 2463
|
490 500 510
....*....|....*....|....*....|....*....
gi 2136495511 465 viTHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRK 503
Cdd:PRK12316 2464 --AWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
158-505 |
1.33e-39 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 147.11 E-value: 1.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 158 DLAAILYTSGTTGRSKGAMLTHKNLASNAKtlarAWHfsadDRL------IHALPIFHTHGLFVACNvTLMAGASMLFLp 231
Cdd:PRK07824 36 DVALVVATSGTTGTPKGAMLTAAALTASAD----ATH----DRLggpgqwLLALPAHHIAGLQVLVR-SVIAGSEPVEL- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 232 kfDADVIFE--ELPRGTVMMGVPTFYTRLVQDERL----TPEATANMRLF---VSGSAPLTAETHEAfEAKTGHAILERY 302
Cdd:PRK07824 106 --DVSAGFDptALPRAVAELGGGRRYTSLVPMQLAkaldDPAATAALAELdavLVGGGPAPAPVLDA-AAAAGINVVRTY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 303 GMTETNmnlsnpydgarrAGTV--GMPLPGVEMRITNretgaevpfgeiGMLQIRGPNVFIGYWRMPEKtrEELLDDGFF 380
Cdd:PRK07824 183 GMSETS------------GGCVydGVPLDGVRVRVED------------GRIALGGPTLAKGYRNPVDP--DPFAEPGWF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 381 ITGDLAMVDEqGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGENQL 460
Cdd:PRK07824 237 RTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLEAL 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2136495511 461 EEekvitHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRKRF 505
Cdd:PRK07824 316 RA-----HVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRF 355
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
2-501 |
3.85e-39 |
|
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: 147.85 E-value: 3.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 2 SHNLFETFAAKmreRAEADFITTRDgRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVY 81
Cdd:cd12115 1 LHDLVEAQAAR---TPDAIALVCGD-ESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 82 LPLNTGYTGDEIRYFLNDAEPALFVCRPKieeqalslaaetgcpavvtlgsaadgslmetaqaavpredivalgerDLAA 161
Cdd:cd12115 77 VPLDPAYPPERLRFILEDAQARLVLTDPD-----------------------------------------------DLAY 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 162 ILYTSGTTGRSKGAMLTHKNLASNAKTLARawHFSADDR--------LIHALPIFHthgLFvacnVTLMAGASMLFLPKF 233
Cdd:cd12115 110 VIYTSGSTGRPKGVAIEHRNAAAFLQWAAA--AFSAEELagvlastsICFDLSVFE---LF----GPLATGGKVVLADNV 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 234 DADVIFEELPRGTVMMGVPTFYTRLVQDERLTPEATAnmrLFVSGSaPLTAE-THEAFEAKTGHAILERYGMTE-TNMNL 311
Cdd:cd12115 181 LALPDLPAAAEVTLINTVPSAAAELLRHDALPASVRV---VNLAGE-PLPRDlVQRLYARLQVERVVNLYGPSEdTTYST 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 312 SNPYD-GARRAGTVGMPLPGVEMRITNREtGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGF------FITGD 384
Cdd:cd12115 257 VAPVPpGASGEVSIGRPLANTQAYVLDRA-LQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFgpgarlYRTGD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 385 LAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGAdlgenQLEEEK 464
Cdd:cd12115 336 LVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGA-----AGLVED 410
|
490 500 510
....*....|....*....|....*....|....*..
gi 2136495511 465 VITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNEL 501
Cdd:cd12115 411 LRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
14-391 |
5.85e-39 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 150.03 E-value: 5.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 14 RERAEADFITTRDG----RRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGY- 88
Cdd:PRK08180 50 QEAPDRVFLAERGAdggwRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAYs 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 89 --TGD--EIRYFLNDAEPAL-FVCRPKIEEQALSLAAETGCPAVVTLGSAADG------SLMETAQAAVPREDIVALGER 157
Cdd:PRK08180 130 lvSQDfgKLRHVLELLTPGLvFADDGAAFARALAAVVPADVEVVAVRGAVPGRaatpfaALLATPPTAAVDAAHAAVGPD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 158 DLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDR--LIHALPIFHTHGLFVACNVTLMAGASMLF-----L 230
Cdd:PRK08180 210 TIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEPpvLVDWLPWNHTFGGNHNLGIVLYNGGTLYIddgkpT 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 231 PKfdadvIFEELPR------GTVMMGVPTFYTRLV----QDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILE 300
Cdd:PRK08180 290 PG-----GFDETLRnlreisPTVYFNVPKGWEMLVpaleRDAALRRRFFSRLKLLFYAGAALSQDVWDRLDRVAEATCGE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 301 R------YGMTETN---MNLSNPYDgarRAGTVGMPLPGVEMRItnretgaeVPFGeiGMLQIR--GPNVFIGYWRMPEK 369
Cdd:PRK08180 365 RirmmtgLGMTETApsaTFTTGPLS---RAGNIGLPAPGCEVKL--------VPVG--GKLEVRvkGPNVTPGYWRAPEL 431
|
410 420
....*....|....*....|...
gi 2136495511 370 TREELLDDGFFITGD-LAMVDEQ 391
Cdd:PRK08180 432 TAEAFDEEGYYRSGDaVRFVDPA 454
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
40-479 |
1.50e-38 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 146.56 E-value: 1.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 40 AQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNtgytgdeiryflndaePALfvCRPKIEEQALSLA 119
Cdd:PRK09029 39 DQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLN----------------PQL--PQPLLEELLPSLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 120 AETgcpAVVTLGSAADGSLMETAQAAVPREDIVALGERDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADD 199
Cdd:PRK09029 101 LDF---ALVLEGENTFSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 200 RLIHALPIFHTHGLFVacnVT--LMAGASMLFLPK--FDADVIfeelprgtvmmG------VPTFYTRLVQDERltpEAT 269
Cdd:PRK09029 178 SWLLSLPLFHVSGQGI---VWrwLYAGATLVVRDKqpLEQALA-----------GcthaslVPTQLWRLLDNRS---EPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 270 ANMRLFVSGSAPLTAETHEAfEAK-----TGhailerYGMTETNmnlSN----PYDGarRAGtVGMPLPGVEMRITNret 340
Cdd:PRK09029 241 SLKAVLLGGAAIPVELTEQA-EQQgircwCG------YGLTEMA---STvcakRADG--LAG-VGSPLPGREVKLVD--- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 341 gaevpfGEIgmlQIRGPNVFIGYWR----MPektreeLLD-DGFFITGDLAMVDeQGYVHIVGRDKDLVISGGYNVYPKE 415
Cdd:PRK09029 305 ------GEI---WLRGASLALGYWRqgqlVP------LVNdEGWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEE 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2136495511 416 VEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLgeNQLEEekvitHLDGRLAKYKQP 479
Cdd:PRK09029 369 IERVINQHPLVQQVFVVPVADAEFGQRPVAVVESDSEAAV--VNLAE-----WLQDKLARFQQP 425
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
39-504 |
3.08e-38 |
|
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: 145.02 E-value: 3.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 39 SAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYflndaepalfvcRPKIEEQALSL 118
Cdd:cd05974 10 SSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRD------------RVDRGGAVYAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 119 AAETgcpavvtlgSAADGSLMetaqaavpredivalgerdlaaILYTSGTTGRSKGAMLTHKNL-ASNAKTLARA----- 192
Cdd:cd05974 78 VDEN---------THADDPML----------------------LYFTSGTTSKPKLVEHTHRSYpVGHLSTMYWIglkpg 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 193 ---WHFSADDRLIHALPIFhthglFVACNvtlmAGASMLFL--PKFDADVIFEELPRG--TVMMGVPTFYTRLVQdERLT 265
Cdd:cd05974 127 dvhWNISSPGWAKHAWSCF-----FAPWN----AGATVFLFnyARFDAKRVLAALVRYgvTTLCAPPTVWRMLIQ-QDLA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 266 PEATAnMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNMNLSNPYDGARRAGTVGMPLPGVEMRITNREtGAEVP 345
Cdd:cd05974 197 SFDVK-LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPD-GAPAT 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 346 FGEIGML--QIRGPNVFIGYWRMPEKTREeLLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDEL 423
Cdd:cd05974 275 EGEVALDlgDTRPVGLMKGYAGDPDKTAH-AMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEH 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 424 DQVAESAVIGLPHPDFGEGVTAVVVRQQGADLG-ENQLEeekVITHLDGRLAKYKQPKRVFFVdELPRNTMGKVQKNELR 502
Cdd:cd05974 354 PAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSpETALE---IFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRRVELR 429
|
..
gi 2136495511 503 KR 504
Cdd:cd05974 430 RR 431
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
26-501 |
3.79e-38 |
|
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: 145.49 E-value: 3.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 26 DGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEpalf 105
Cdd:cd12114 9 GDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAG---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 106 vCRPKIEEQALSLAAETGCPAVVTLGSAADGSLMETAQAAVPredivalgeRDLAAILYTSGTTGRSKGAMLTHKNLASN 185
Cdd:cd12114 85 -ARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAP---------DDLAYVIFTSGSTGTPKGVMISHRAALNT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 186 AKTLARAWHFSADDRLIhALPIFH----THGLFVAcnvtLMAGASmLFLP----KFDADVIFEELPRG--TVMMGVPTFY 255
Cdd:cd12114 155 ILDINRRFAVGPDDRVL-ALSSLSfdlsVYDIFGA----LSAGAT-LVLPdearRRDPAHWAELIERHgvTLWNSVPALL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 256 TRLVQDERLTPEATANMRL-FVSG---SAPLTAETHEAFEAKTGHAIlerYGMTETNMnLSNPY-----DGARRAGTVGM 326
Cdd:cd12114 229 EMLLDVLEAAQALLPSLRLvLLSGdwiPLDLPARLRALAPDARLISL---GGATEASI-WSIYHpidevPPDWRSIPYGR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 327 PLPGVEMRITNREtGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDG----FFITGDLAMVDEQGYVHIVGRDKD 402
Cdd:cd12114 305 PLANQRYRVLDPR-GRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHPdgerLYRTGDLGRYRPDGTLEFLGRRDG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 403 LVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDfGEGVTAVVVrqqgADLGENQLEEEKVITHLDGRLAKYKQPKRV 482
Cdd:cd12114 384 QVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPG-GKRLAAFVV----PDNDGTPIAPDALRAFLAQTLPAYMIPSRV 458
|
490
....*....|....*....
gi 2136495511 483 FFVDELPRNTMGKVQKNEL 501
Cdd:cd12114 459 IALEALPLTANGKVDRAAL 477
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
10-384 |
9.96e-38 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 145.65 E-value: 9.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 10 AAKMRERAEADFITTRDG----RRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLN 85
Cdd:cd05921 2 AHWARQAPDRTWLAEREGnggwRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 86 TGYT-----GDEIRYFLNDAEPAL-FVCRPKIEEQALSLAAETGCPAVVTLGSAAD------GSLMETAQAAVPREDIVA 153
Cdd:cd05921 82 PAYSlmsqdLAKLKHLFELLKPGLvFAQDAAPFARALAAIFPLGTPLVVSRNAVAGrgaisfAELAATPPTAAVDAAFAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 154 LGERDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADD--RLIHALPIFHTHGLFVACNVTLMAGASMLFLP 231
Cdd:cd05921 162 VGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFNLVLYNGGTLYIDD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 232 KFDADVIFEELPRG------TVMMGVPTFYTRLVQ----DERLTPEATANMRLFVSGSAPLTAETHEAFEA----KTGHA 297
Cdd:cd05921 242 GKPMPGGFEETLRNlreispTVYFNVPAGWEMLVAalekDEALRRRFFKRLKLMFYAGAGLSQDVWDRLQAlavaTVGER 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 298 I--LERYGMTETNMNLSNPYDGARRAGTVGMPLPGVEMRItnretgaeVPFGEIGMLQIRGPNVFIGYWRMPEKTREELL 375
Cdd:cd05921 322 IpmMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKL--------VPSGGKYEVRVKGPNVTPGYWRQPELTAQAFD 393
|
....*....
gi 2136495511 376 DDGFFITGD 384
Cdd:cd05921 394 EEGFYCLGD 402
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
162-495 |
1.64e-37 |
|
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: 141.37 E-value: 1.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 162 ILYTSGTTGRSKGAMLTHKNLASNAKT--------------LARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASM 227
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIFRMLMGgadfgtgeftpsedAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 228 LFLPKFDADVIFEELPRG--TVMMGVPTFYTRLVQDE--RLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAIL-ERY 302
Cdd:cd05924 88 LPDDRFDPEEVWRTIEKHkvTSMTIVGDAMARPLIDAlrDAGPYDLSSLFAISSGGALLSPEVKQGLLELVPNITLvDAF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 303 GMTETNMNLSN-PYDGARRAGTVGMPLPGVemrITNRETGAEVPFGEIGMLQI-RGPNVFIGYWRMPEKTRE---ELLDD 377
Cdd:cd05924 168 GSSETGFTGSGhSAGSGPETGPFTRANPDT---VVLDDDGRVVPPGSGGVGWIaRRGHIPLGYYGDEAKTAEtfpEVDGV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 378 GFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADlge 457
Cdd:cd05924 245 RYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREGAG--- 321
|
330 340 350
....*....|....*....|....*....|....*...
gi 2136495511 458 nqLEEEKVITHLDGRLAKYKQPKRVFFVDELPRNTMGK 495
Cdd:cd05924 322 --VDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
7-507 |
8.00e-37 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 142.82 E-value: 8.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 7 ETFAAKMRER---------------AEADFITTRDG-RRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILL 70
Cdd:PRK10946 10 EEFARRYREKgywqdlpltdiltrhAASDAIAVICGeRQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYIT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 71 YLACLRIGGVylPLNTGYTGD--EIRYFLNDAEPALFVCRpkiEEQALslaaetgcpavvtlgsAADGSLMETAQAAVPR 148
Cdd:PRK10946 90 FFALLKLGVA--PVNALFSHQrsELNAYASQIEPALLIAD---RQHAL----------------FSDDDFLNTLVAEHSS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 149 EDIVAL----GERDLAAILYTS---------------------GTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIH 203
Cdd:PRK10946 149 LRVVLLlnddGEHSLDDAINHPaedftatpspadevaffqlsgGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLC 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 204 ALPIFHTHGLFV--ACNVtLMAGASMLFLPKFDADVIFEELPRGTVMMG--VPTFYTRLVQ--DERLTPEATANMRLFVS 277
Cdd:PRK10946 229 ALPAAHNYPMSSpgALGV-FLAGGTVVLAPDPSATLCFPLIEKHQVNVTalVPPAVSLWLQaiAEGGSRAQLASLKLLQV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 278 GSAPLTAETHEAFEAKTGHAILERYGMTETNMNLSNPYDGARRA-GTVGMPL-PGVEMRITNrETGAEVPFGEIGMLQIR 355
Cdd:PRK10946 308 GGARLSETLARRIPAELGCQLQQVFGMAEGLVNYTRLDDSDERIfTTQGRPMsPDDEVWVAD-ADGNPLPQGEVGRLMTR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 356 GPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLP 435
Cdd:PRK10946 387 GPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSME 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2136495511 436 HPDFGEGVTAVVVRQqgadlgeNQLEEEKVITHLDGR-LAKYKQPKRVFFVDELPRNTMGKVQKNELRKRFND 507
Cdd:PRK10946 467 DELMGEKSCAFLVVK-------EPLKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLAS 532
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-501 |
1.17e-35 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 142.40 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 3 HNLFETFAAKMRERAEADFITTRDGrrYRYTDALtiSAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYL 82
Cdd:PRK12316 514 HRLFEEQVERTPEAPALAFGEETLD--YAELNRR--ANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYV 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 83 PLNTGYTGDEIRYFLNDAEPALFVCRPKIEEQaLSLAAETgcpAVVTLGsaaDGSLMETAQAAVPREdiVALGERDLAAI 162
Cdd:PRK12316 590 PLDPEYPAERLAYMLEDSGVQLLLSQSHLGRK-LPLAAGV---QVLDLD---RPAAWLEGYSEENPG--TELNPENLAYV 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 163 LYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHG---LFvacnVTLMAGASMLFLPK---FDAD 236
Cdd:PRK12316 661 IYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSvweFF----WPLMSGARLVVAAPgdhRDPA 736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 237 VIFEELPRG--TVMMGVPTFYTRLVQDERltPEATANMRLFVSGSAPLTAETHEAFEAKTGHA-ILERYGMTETNMNLSn 313
Cdd:PRK12316 737 KLVELINREgvDTLHFVPSMLQAFLQDED--VASCTSLRRIVCSGEALPADAQEQVFAKLPQAgLYNLYGPTEAAIDVT- 813
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 314 pYDGARRAG----TVGMPLPGVEMRITNRETGAeVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGF------FITG 383
Cdd:PRK12316 814 -HWTCVEEGgdsvPIGRPIANLACYILDANLEP-VPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFvagermYRTG 891
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 384 DLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLphpDFGEGVTAVVVRQQGADLgenqleEE 463
Cdd:PRK12316 892 DLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV---DGKQLVGYVVLESEGGDW------RE 962
|
490 500 510
....*....|....*....|....*....|....*...
gi 2136495511 464 KVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNEL 501
Cdd:PRK12316 963 ALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
4-391 |
2.80e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 139.41 E-value: 2.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 4 NLFETFAAKMRERAEADFITTRDG-----RRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIG 78
Cdd:PRK12582 50 SIPHLLAKWAAEAPDRPWLAQREPghgqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 79 GVYLPLNTGYT-----GDEIRYFLNDAEPAL-FVCRPKIEEQALSLAAETGCPaVVTLGSAADGS-------LMETAQAA 145
Cdd:PRK12582 130 VPAAPVSPAYSlmshdHAKLKHLFDLVKPRVvFAQSGAPFARALAALDLLDVT-VVHVTGPGEGIasiafadLAATPPTA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 146 VPREDIVALGERDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHAL---PIFHTHGLFVACNVTLM 222
Cdd:PRK12582 209 AVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPVSLdwmPWNHTMGGNANFNGLLW 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 223 AGASMLFLPKFDADVIFEELPRG------TVMMGVPTFYTRLV----QDERLTPEATANMRLFVSGSAPLTAETHEAFEA 292
Cdd:PRK12582 289 GGGTLYIDDGKPLPGMFEETIRNlreispTVYGNVPAGYAMLAeameKDDALRRSFFKNLRLMAYGGATLSDDLYERMQA 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 293 ----KTGHAIL--ERYGMTETNMNLSNPYDGARRAGTVGMPLPGVEMRItnretgaeVPFGEIGMLQIRGPNVFIGYWRM 366
Cdd:PRK12582 369 lavrTTGHRIPfyTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKL--------APVGDKYEVRVKGPNVTPGYHKD 440
|
410 420
....*....|....*....|....*.
gi 2136495511 367 PEKTREELLDDGFFITGDLA-MVDEQ 391
Cdd:PRK12582 441 PELTAAAFDEEGFYRLGDAArFVDPD 466
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-512 |
3.84e-35 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 140.68 E-value: 3.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 3 HNLFEtfaAKMRERAEADFITTrDGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYL 82
Cdd:PRK12467 1577 HQLIE---DQAAATPEAVALVF-GEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYV 1652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 83 PLNTGYTGDEIRYFLNDAEPALFVCRPKIEEQalsLAAETGCPAVVTlgsAADGSLMETAQAAVPredIVALGERDLAAI 162
Cdd:PRK12467 1653 PLDPEYPRERLAYMIEDSGIELLLTQSHLQAR---LPLPDGLRSLVL---DQEDDWLEGYSDSNP---AVNLAPQNLAYV 1723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 163 LYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPI---FHTHGLFVAcnvtLMAGASMLFL-------PK 232
Cdd:PRK12467 1724 IYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFafdVSVWELFWP----LINGARLVIAppgahrdPE 1799
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 233 FDADVIFEElpRGTVMMGVPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNMN-- 310
Cdd:PRK12467 1800 QLIQLIERQ--QVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDvt 1877
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 311 ---LSNPYDGARRAGTVGMPLPGVEMRITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGF-------F 380
Cdd:PRK12467 1878 hwtCRRKDLEGRDSVPIGQPIANLSTYILD-ASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgtvgsrlY 1956
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 381 ITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDfGEGVTAVVVRQQGADLGEN-- 458
Cdd:PRK12467 1957 RTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGAN-GKQLVAYVVPTDPGLVDDDea 2035
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2136495511 459 -QLEEEKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRK----RFNDTYQTP 512
Cdd:PRK12467 2036 qVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPApdasELQQAYVAP 2094
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
41-447 |
4.83e-35 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 138.21 E-value: 4.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 41 QLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVY--LPLNTGYTG-----DEIRYFLNDAEPALFVCRPKIEE 113
Cdd:PRK09192 61 AGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPvpLPLPMGFGGresyiAQLRGMLASAQPAAIITPDELLP 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 114 qaLSLAAETGCPAVVTlGSAADGSLMETAQAAVPREDivalgERDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLAR-A 192
Cdd:PRK09192 141 --WVNEATHGNPLLHV-LSHAWFKALPEADVALPRPT-----PDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHdG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 193 WHFSADDRLIHALPIFHTHGLfVACNVTLMA-GASMLFLPKFDadviFEELP----------RGTVMMGvPTF-Y---TR 257
Cdd:PRK09192 213 LKVRPGDRCVSWLPFYHDMGL-VGFLLTPVAtQLSVDYLPTRD----FARRPlqwldlisrnRGTISYS-PPFgYelcAR 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 258 LVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAK------TGHAILERYGMTETNMNLS------------------- 312
Cdd:PRK09192 287 RVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAfapagfDDKAFMPSYGLAEATLAVSfsplgsgivveevdrdrle 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 313 ------NPYDGARRAGTV---GMPLPGVEMRITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTReELLDDGFFITG 383
Cdd:PRK09192 367 yqgkavAPGAETRRVRTFvncGKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGYFRDEESQD-VLAADGWLDTG 444
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2136495511 384 DLA-MVDeqGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQV--AESAVIGLPHPDfGEGVTAVV 447
Cdd:PRK09192 445 DLGyLLD--GYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELrsGDAAAFSIAQEN-GEKIVLLV 508
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
30-503 |
1.52e-34 |
|
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: 134.74 E-value: 1.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 30 YRYTDAltISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVCRP 109
Cdd:cd17653 25 YGELDA--ASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLLTTD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 110 KieeqalslaaetgcpavvtlgsaadgslmetaqaavpredivalgERDLAAILYTSGTTGRSKGAMLTHKNLASNAKTL 189
Cdd:cd17653 103 S---------------------------------------------PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 190 ARAWHFSADDRLIHALPIfhthgLFVACN----VTLMAGASMLFLpkfDADVIFEELPRG-TVMMGVPTFYTrlvqdeRL 264
Cdd:cd17653 138 PARLDVGPGSRVAQVLSI-----AFDACIgeifSTLCNGGTLVLA---DPSDPFAHVARTvDALMSTPSILS------TL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 265 TPEATANMRLFVSGSAPLTAETHEAFeaKTGHAILERYGMTETNMNLSNPYDGARRAGTVGMPLPGVEMRITNRETgAEV 344
Cdd:cd17653 204 SPQDFPNLKTIFLGGEAVPPSLLDRW--SPGRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCYILDADL-QPV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 345 PFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGF------FITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQ 418
Cdd:cd17653 281 PEGVVGEICISGVQVARGYLGNPALTASKFVPDPFwpgsrmYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 419 VIDELDQVAESAviglphpdfgegvTAVVVRQQ------GADLGENQLEEEkvithLDGRLAKYKQPKRVFFVDELPRNT 492
Cdd:cd17653 361 VVLQSQPEVTQA-------------AAIVVNGRlvafvtPETVDVDGLRSE-----LAKHLPSYAVPDRIIALDSFPLTA 422
|
490
....*....|.
gi 2136495511 493 MGKVQKNELRK 503
Cdd:cd17653 423 NGKVDRKALRE 433
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
39-463 |
2.16e-34 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 136.18 E-value: 2.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 39 SAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVCRPKieEQALSL 118
Cdd:PRK09274 51 SDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIGIPK--AHLARR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 119 AAETGCPAVVTLGSAADGSLMETAQAAVPRED-------IVALGERDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLAR 191
Cdd:PRK09274 129 LFGWGKPSVRRLVTVGGRLLWGGTTLATLLRDgaaapfpMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALRE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 192 AWHFSADDRLIHALPIFHTHGLfvACNVTLMagasmlfLPKFDA--------DVIFEELPRG--TVMMGVPTFYTRLVQD 261
Cdd:PRK09274 209 DYGIEPGEIDLPTFPLFALFGP--ALGMTSV-------IPDMDPtrpatvdpAKLFAAIERYgvTNLFGSPALLERLGRY 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 262 ERLTPEATANMRLFVSGSAPLTAETHEAFEA--KTGHAILERYGMTE--------TNMNLSNPYDGARR-AGT-VGMPLP 329
Cdd:PRK09274 280 GEANGIKLPSLRRVISAGAPVPIAVIERFRAmlPPDAEILTPYGATEalpissieSREILFATRAATDNgAGIcVGRPVD 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 330 GVEMRITNRETGA--------EVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDG----FFITGDLAMVDEQGYVHIV 397
Cdd:PRK09274 360 GVEVRIIAISDAPipewddalRLATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDGqgdvWHRMGDLGYLDAQGRLWFC 439
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2136495511 398 GRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPdfGEGVTAVVV-RQQGADLGENQLEEE 463
Cdd:PRK09274 440 GRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVP--GAQRPVLCVeLEPGVACSKSALYQE 504
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
41-505 |
4.11e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 135.12 E-value: 4.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 41 QLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNT--------GYTGDEIRYFLNDAEPALFVCRPKie 112
Cdd:PRK07768 41 RIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQptprtdlaVWAEDTLRVIGMIGAKAVVVGEPF-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 113 EQALSLAAETGCpAVVTLGSAADGslmetaqaavPREDIVALGERDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARA 192
Cdd:PRK07768 119 LAAAPVLEEKGI-RVLTVADLLAA----------DPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 193 WHFSAD-DRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFD--AD-VIFEELP---RGTVMMGvPTF-YT----RLvq 260
Cdd:PRK07768 188 AEFDVEtDVMVSWLPLFHDMGMVGFLTVPMYFGAELVKVTPMDflRDpLLWAELIskyRGTMTAA-PNFaYAllarRL-- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 261 dERLTPEATAN---MRLFVSGSAPLTAETHEAF-EAKTGH-----AILERYGMTETNMNLSNP----------------- 314
Cdd:PRK07768 265 -RRQAKPGAFDlssLRFALNGAEPIDPADVEDLlDAGARFglrpeAILPAYGMAEATLAVSFSpcgaglvvdevdadlla 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 315 ---------YDGARRAGTVGMPLPGVEMRITNREtGAEVPFGEIGMLQIRGPNVFIGYWRM--PEKTREElldDGFFITG 383
Cdd:PRK07768 344 alrravpatKGNTRRLATLGPPLPGLEVRVVDED-GQVLPPRGVGVIELRGESVTPGYLTMdgFIPAQDA---DGWLDTG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 384 DLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQV-AESAV-IGLPHPDFGEGVtAVVVRQQGADLGE--NQ 459
Cdd:PRK07768 420 DLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVrPGNAVaVRLDAGHSREGF-AVAVESNAFEDPAevRR 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2136495511 460 LEEE---KVITHLDGRlakykqPKRVFFVD--ELPRNTMGKVQKNELRKRF 505
Cdd:PRK07768 499 IRHQvahEVVAEVGVR------PRNVVVLGpgSIPKTPSGKLRRANAAELV 543
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
30-501 |
5.87e-34 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 136.71 E-value: 5.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 30 YRYTDALTISaqLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVcrp 109
Cdd:PRK10252 486 YREMREQVVA--LANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLI--- 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 110 KIEEQALSLAaetgcpavvtlgsAADGSLMETAQAAVPREDIVALGER---DLAAILYTSGTTGRSKGAMLTHKNLASNA 186
Cdd:PRK10252 561 TTADQLPRFA-------------DVPDLTSLCYNAPLAPQGAAPLQLSqphHTAYIIFTSGSTGRPKGVMVGQTAIVNRL 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 187 KTLARAWHFSADDRLIHALPifhthglfVACNVT-------LMAGASMLFL-------PKFDADVIFEElpRGTVMMGVP 252
Cdd:PRK10252 628 LWMQNHYPLTADDVVLQKTP--------CSFDVSvweffwpFIAGAKLVMAepeahrdPLAMQQFFAEY--GVTTTHFVP 697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 253 TFYTRLVQ--DERLTPEATANMR-LFVSGSApLTAETHEAFEAKTGHAILERYGMTETNMNLS----NPYDGARRAGT-- 323
Cdd:PRK10252 698 SMLAAFVAslTPEGARQSCASLRqVFCSGEA-LPADLCREWQQLTGAPLHNLYGPTEAAVDVSwypaFGEELAAVRGSsv 776
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 324 -VGMPLPGVEMRITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGF------FITGDLAMVDEQGYVHI 396
Cdd:PRK10252 777 pIGYPVWNTGLRILD-ARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLDDGAVEY 855
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 397 VGRDKDLVISGGYNVYPKEVEQVIDEL---DQVAESAVIGLPHPDFGEGVT---AVVVRQQGADLGENQLEeekviTHLD 470
Cdd:PRK10252 856 LGRSDDQLKIRGQRIELGEIDRAMQALpdvEQAVTHACVINQAAATGGDARqlvGYLVSQSGLPLDTSALQ-----AQLR 930
|
490 500 510
....*....|....*....|....*....|.
gi 2136495511 471 GRLAKYKQPKRVFFVDELPRNTMGKVQKNEL 501
Cdd:PRK10252 931 ERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
147-460 |
2.63e-33 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 134.07 E-value: 2.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 147 PREDIVALGERDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGAS 226
Cdd:PRK08043 355 PRLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 227 MLFLPKFDADVIFEEL---PRGTVMMGVPTF---YTRLVQderltPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILE 300
Cdd:PRK08043 435 VFLYPSPLHYRIVPELvydRNCTVLFGTSTFlgnYARFAN-----PYDFARLRYVVAGAEKLQESTKQLWQDKFGLRILE 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 301 RYGMTETNMNLSNPYDGARRAGTVGMPLPGVEMRITNretgaeVP-FGEIGMLQIRGPNVFIGYWRM--------PEKTR 371
Cdd:PRK08043 510 GYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLS------VPgIEQGGRLQLKGPNIMNGYLRVekpgvlevPTAEN 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 372 EE-LLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEgvtAVVVRQ 450
Cdd:PRK08043 584 ARgEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGE---ALVLFT 660
|
330
....*....|
gi 2136495511 451 QGADLGENQL 460
Cdd:PRK08043 661 TDSELTREKL 670
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-512 |
3.80e-33 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 134.90 E-value: 3.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 3 HNLFETFAAKmreRAEADFITTRDgRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYL 82
Cdd:PRK12467 3098 HQLIEAQVAR---TPEAPALVFGD-QQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYV 3173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 83 PLNTGYTGDEIRYFLNDAEPALFVCRPKIEEQalsLAAETGCPAVvTLGSAADGSLMEtaqaAVPreDIVALGErDLAAI 162
Cdd:PRK12467 3174 PLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQ---LPAPAGDTAL-TLDRLDLNGYSE----NNP--STRVMGE-NLAYV 3242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 163 LYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPiFHTHGLFVACNVTLMAGASMLFLPK--FDADVIFE 240
Cdd:PRK12467 3243 IYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMS-FSFDGAQERFLWTLICGGCLVVRDNdlWDPEELWQ 3321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 241 EL--PRGTVMMGVPTFYTRLVQDERltPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILER-YGMTETNMN---LSNP 314
Cdd:PRK12467 3322 AIhaHRISIACFPPAYLQQFAEDAG--GADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNgYGPTEAVVTvtlWKCG 3399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 315 YDGARRAGTV--GMPLPGVEMRITNRETGAeVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGF-------FITGDL 385
Cdd:PRK12467 3400 GDAVCEAPYApiGRPVAGRSIYVLDGQLNP-VPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFsgsggrlYRTGDL 3478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 386 AMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGenqleeEKV 465
Cdd:PRK12467 3479 ARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPADPQGDWR------ETL 3552
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2136495511 466 ITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRK---RFNDTYQTP 512
Cdd:PRK12467 3553 RDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDpdaKGSREYVAP 3602
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
27-503 |
6.23e-33 |
|
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: 130.55 E-value: 6.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 27 GRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNdaepalfV 106
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLN-------V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 107 CRPKIeeqalslaaetgcpavvtlgsaadgslmetaqaavpredIVAlgerDLAAILYTSGTTGRSKGAMLTHKNlASNA 186
Cdd:cd05940 74 SSAKH---------------------------------------LVV----DAALYIYTSGTTGLPKAAIISHRR-AWRG 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 187 KTLARAWHFSAD-DRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDA-----DVIFEelpRGTVMMGVPTFYTRLVQ 260
Cdd:cd05940 110 GAFFAGSGGALPsDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSAsnfwdDIRKY---QATIFQYIGELCRYLLN 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 261 DERLTPEATANMRLfVSGSApLTAETHEAFEAKTGHA-ILERYGMTETNMNLSNpYDGARRAGTVGMPLPGVEMRIT--- 336
Cdd:cd05940 187 QPPKPTERKHKVRM-IFGNG-LRPDIWEEFKERFGVPrIAEFYAATEGNSGFIN-FFGKPGAIGRNPSLLRKVAPLAlvk 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 337 -NRETGA----------EVPFGEIGML--QIRGPNVFIGYWRmPEKTREELLDDGF------FITGDLAMVDEQGYVHIV 397
Cdd:cd05940 264 yDLESGEpirdaegrciKVPRGEPGLLisRINPLEPFDGYTD-PAATEKKILRDVFkkgdawFNTGDLMRLDGEGFWYFV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 398 GRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFG--EGVTAVVVRQqgadlgENQLEEEKVITHLDGRLAK 475
Cdd:cd05940 343 DRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDgrAGMAAIVLQP------NEEFDLSALAAHLEKNLPG 416
|
490 500
....*....|....*....|....*...
gi 2136495511 476 YKQPKRVFFVDELPRNTMGKVQKNELRK 503
Cdd:cd05940 417 YARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
28-433 |
6.33e-33 |
|
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: 132.16 E-value: 6.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 28 RRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVC 107
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 108 RPkiEEQA---LSLAAETgcPAVV----------------TLGSAADgsLMETAQAAVPREDivALGERDLAA------- 161
Cdd:cd17641 90 ED--EEQVdklLEIADRI--PSVRyviycdprgmrkyddpRLISFED--VVALGRALDRRDP--GLYEREVAAgkgedva 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 162 -ILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPI-----------------FHTHglFVACNVTLMA 223
Cdd:cd17641 162 vLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLpwigeqmysvgqalvcgFIVN--FPEEPETMME 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 224 -----GASMLFLPK------------------------FD---------ADVIFEELPRGTVMMGVPTFYTRLVQD---E 262
Cdd:cd17641 240 dlreiGPTFVLLPPrvwegiaadvrarmmdatpfkrfmFElgmklglraLDRGKRGRPVSLWLRLASWLADALLFRplrD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 263 RLtpeATANMRLFVSGSAPLTAETHEAFEAkTGHAILERYGMTETNMNLSNPYDGARRAGTVGMPLPGVEMRITNRetga 342
Cdd:cd17641 320 RL---GFSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEV---- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 343 evpfGEIgmlQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRDKDL-VISGGYNVYPKEVEQVID 421
Cdd:cd17641 392 ----GEI---LVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVgTTSDGTRFSPQFIENKLK 464
|
490
....*....|..
gi 2136495511 422 ELDQVAESAVIG 433
Cdd:cd17641 465 FSPYIAEAVVLG 476
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
5-505 |
9.10e-33 |
|
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: 130.36 E-value: 9.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 5 LFETFAAKMRERAEADFITTRDGR-RYRYTDALtiSAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLP 83
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSlTYAELDRL--SSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 84 LNTGYTGDEIRYflndaepalfvcrpkieeqalsLAAETGCPAVVTlgSAADgslmetaqaavpredivalgerDLAAIL 163
Cdd:cd05918 79 LDPSHPLQRLQE----------------------ILQDTGAKVVLT--SSPS----------------------DAAYVI 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 164 YTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRL---------IHALPIFhthglfvacnVTLMAGASMLFLPKFD 234
Cdd:cd05918 113 FTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVlqfasytfdVSILEIF----------TTLAAGGCLCIPSEED 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 235 -----ADVIfEELpRGTVMMGVPTFyTRLvqderLTPEATANMRLFVSGSAPLTAETHEAFEAKTghAILERYGMTETNM 309
Cdd:cd05918 183 rlndlAGFI-NRL-RVTWAFLTPSV-ARL-----LDPEDVPSLRTLVLGGEALTQSDVDTWADRV--RLINAYGPAECTI 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 310 N-LSNPYDGARRAGTVGMPLPGVeMRITNRETGAE-VPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFI------ 381
Cdd:cd05918 253 AaTVSPVVPSTDPRNIGRPLGAT-CWVVDPDNHDRlVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAWLkqegsg 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 382 -------TGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVT--AVVVRQQG 452
Cdd:cd05918 332 rgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPqlVAFVVLDG 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2136495511 453 ADLGENQLEE-------------EKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRKRF 505
Cdd:cd05918 412 SSSGSGDGDSlflepsdefralvAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELA 477
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
7-502 |
9.92e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 131.30 E-value: 9.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 7 ETFAAKMRERAEADFITTR-DGRRYRYTDALTISAQLAGALTELGVKQGD-RVAVQVDKSPEAILLYLACLRIGGVYLPL 84
Cdd:PRK13388 3 DTIAQLLRDRAGDDTIAVRyGDRTWTWREVLAEAAARAAALIALADPDRPlHVGVLLGNTPEMLFWLAAAALGGYVLVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 85 NTGYTGDE----IRY-----FLNDAEPalfvcRPKIeeQALSLAAETgcpaVVTLGSAADGSLMETAQAAVPREDIvalG 155
Cdd:PRK13388 83 NTTRRGAAlaadIRRadcqlLVTDAEH-----RPLL--DGLDLPGVR----VLDVDTPAYAELVAAAGALTPHREV---D 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 156 ERDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDA 235
Cdd:PRK13388 149 AMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKFSA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 236 DVIFEELPR--GTVM--MGVPTFYTrLVQDERltPEATAN--MRLFVSGSAPltaETHEAFEAKTGHAILERYGMTETNM 309
Cdd:PRK13388 229 SGFLDDVRRygATYFnyVGKPLAYI-LATPER--PDDADNplRVAFGNEASP---RDIAEFSRRFGCQVEDGYGSSEGAV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 310 NLSNPyDGARrAGTVGMPLPGVEmrITNRETGAEVP---FGEIG-----------MLQIRGPNVFIGYWRMPEKTREELl 375
Cdd:PRK13388 303 IVVRE-PGTP-PGSIGRGAPGVA--IYNPETLTECAvarFDAHGallnadeaigeLVNTAGAGFFEGYYNNPEATAERM- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 376 DDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADL 455
Cdd:PRK13388 378 RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATF 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2136495511 456 GENQLEEekvitHLDGR--LAKYKQPKRVFFVDELPRNTMGKVQKNELR 502
Cdd:PRK13388 458 DPDAFAA-----FLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKRELI 501
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
160-433 |
1.58e-32 |
|
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: 131.33 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 160 AAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHF-SADDR---LIHALPIFHTHGLFVACNVTLMAGASMLF------ 229
Cdd:cd05933 153 CTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLrPATVGqesVVSYLPLSHIAAQILDIWLPIKVGGQVYFaqpdal 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 230 ---LPKFDADVifeelpRGTVMMGVPTFYTRLvqDERLTPEAT-------------------ANMRL------------- 274
Cdd:cd05933 233 kgtLVKTLREV------RPTAFMGVPRVWEKI--QEKMKAVGAksgtlkrkiaswakgvgleTNLKLmggespsplfyrl 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 275 --------------------FVSGSAPLTAETHEAFEAkTGHAILERYGMTETN--MNLSNPYdgARRAGTVGMPLPGVE 332
Cdd:cd05933 305 akklvfkkvrkalgldrcqkFFTGAAPISRETLEFFLS-LNIPIMELYGMSETSgpHTISNPQ--AYRLLSCGKALPGCK 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 333 MRITNRETGAevpfgeIGMLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVI-SGGYNV 411
Cdd:cd05933 382 TKIHNPDADG------IGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIItAGGENV 455
|
330 340
....*....|....*....|...
gi 2136495511 412 YPKEVEQVI-DELDQVAESAVIG 433
Cdd:cd05933 456 PPVPIEDAVkKELPIISNAMLIG 478
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
3-501 |
1.82e-32 |
|
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: 129.48 E-value: 1.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 3 HNLFETFAAKMRE----RAEADFITTRDgrryrytdaLTISA-QLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRI 77
Cdd:cd17644 3 HQLFEEQVERTPDavavVFEDQQLTYEE---------LNTKAnQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 78 GGVYLPLNTGYTGDEIRYFLNDAEPALFVCRPKieeqalslaaetgcpavvtlgsaadgslmetaqaavpredivalger 157
Cdd:cd17644 74 GGAYVPLDPNYPQERLTYILEDAQISVLLTQPE----------------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 158 DLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIhalpIFHTHGLFVACN---VTLMAGASMLFLPKfd 234
Cdd:cd17644 107 NLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVL----QFASIAFDVAAEeiyVTLLSGATLVLRPE-- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 235 advifEELPRGTVM-----------MGVPTFYTRLVQDERLTPEAT--ANMRLFVSGSAPLTAETHEAFEAKTGHAI--L 299
Cdd:cd17644 181 -----EMRSSLEDFvqyiqqwqltvLSLPPAYWHLLVLELLLSTIDlpSSLRLVIVGGEAVQPELVRQWQKNVGNFIqlI 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 300 ERYGMTE-----TNMNLSNPYDGARRAGTVGMPLPGVEMRITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREEL 374
Cdd:cd17644 256 NVYGPTEatiaaTVCRLTQLTERNITSVPIGRPIANTQVYILD-ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKF 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 375 LDDGF--------FITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAV 446
Cdd:cd17644 335 ISHPFnsseserlYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAY 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2136495511 447 VVRQQGADLGENQLEEekvitHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNEL 501
Cdd:cd17644 415 IVPHYEESPSTVELRQ-----FLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
28-504 |
9.27e-32 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 128.81 E-value: 9.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 28 RRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVC 107
Cdd:PLN02479 44 VRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 108 RPK---IEEQALSLAAETGC-----PAVVTLG--SAADGSLMET-AQAAVPREDIVALGERDLA-----------AILYT 165
Cdd:PLN02479 124 DQEfftLAEEALKILAEKKKssfkpPLLIVIGdpTCDPKSLQYAlGKGAIEYEKFLETGDPEFAwkppadewqsiALGYT 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 166 SGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLfLPKFDADVIFEELPRG 245
Cdd:PLN02479 204 SGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNGWCFTWTLAALCGTNIC-LRQVTAKAIYSAIANY 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 246 TV--MMGVPTFYTRLV---QDERLTPEATAnMRLFVSGSAPlTAETHEAFEAKtGHAILERYGMTET-----------NM 309
Cdd:PLN02479 283 GVthFCAAPVVLNTIVnapKSETILPLPRV-VHVMTAGAAP-PPSVLFAMSEK-GFRVTHTYGLSETygpstvcawkpEW 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 310 NLSNPYDGARRAGTVGMPLPGVE-MRITNRETGAEVP-----FGEIGMlqiRGPNVFIGYWRMPeKTREELLDDGFFITG 383
Cdd:PLN02479 360 DSLPPEEQARLNARQGVRYIGLEgLDVVDTKTMKPVPadgktMGEIVM---RGNMVMKGYLKNP-KANEEAFANGWFHSG 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 384 DLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGENQLEEE 463
Cdd:PLN02479 436 DLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEAALAE 515
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2136495511 464 KVITHLDGRLAKYKQPKRVFFvDELPRNTMGKVQKNELRKR 504
Cdd:PLN02479 516 DIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRAK 555
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
15-496 |
1.11e-31 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 128.91 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 15 ERAEAD---FITTRDGRRYRYTdaltiSAQL-------AGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPL 84
Cdd:PRK10524 65 KRPEQLaliAVSTETDEERTYT-----FRQLhdevnrmAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 85 NTGYTGDEIRYFLNDAEPALFVC-------------RPKIEEqALSLAAETgcPAVVTLgsaADGSLMETAQAAVPREDI 151
Cdd:PRK10524 140 FGGFASHSLAARIDDAKPVLIVSadagsrggkvvpyKPLLDE-AIALAQHK--PRHVLL---VDRGLAPMARVAGRDVDY 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 152 VALGERDLAA--------------ILYTSGTTGRSKG----------AmlthknLASNAKTL----ARAWHFSADDrlI- 202
Cdd:PRK10524 214 ATLRAQHLGArvpvewlesnepsyILYTSGTTGKPKGvqrdtggyavA------LATSMDTIfggkAGETFFCASD--Ig 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 203 ----HALPIFhthglfvacnVTLMAGAsmlflpkfdADVIFEELP---------------RGTVMMGVPTfYTRLV--QD 261
Cdd:PRK10524 286 wvvgHSYIVY----------APLLAGM---------ATIMYEGLPtrpdagiwwrivekyKVNRMFSAPT-AIRVLkkQD 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 262 -ERLTPEATANMR-LFVSGSaPLTAETHEAFEAKTGHAILERYGMTETN---MNLSNPY-DGARRAGTVGMPLPGVEMRI 335
Cdd:PRK10524 346 pALLRKHDLSSLRaLFLAGE-PLDEPTASWISEALGVPVIDNYWQTETGwpiLAIARGVeDRPTRLGSPGVPMYGYNVKL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 336 TNRETGAEVPFGEIGMLQIRGP-------------NVFIG-YWRmpektreeLLDDGFFITGDLAMVDEQGYVHIVGRDK 401
Cdd:PRK10524 425 LNEVTGEPCGPNEKGVLVIEGPlppgcmqtvwgddDRFVKtYWS--------LFGRQVYSTFDWGIRDADGYYFILGRTD 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 402 DLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADL--GENQLEEEK-VITHLDGRLAKYKQ 478
Cdd:PRK10524 497 DVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLadREARLALEKeIMALVDSQLGAVAR 576
|
570
....*....|....*...
gi 2136495511 479 PKRVFFVDELPRNTMGKV 496
Cdd:PRK10524 577 PARVWFVSALPKTRSGKL 594
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
27-480 |
1.29e-31 |
|
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: 127.79 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 27 GRRYRYTDALTISAQLAGAL-TELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEI---------RYF 96
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALlAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLlhcfrccgaKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 97 LNDAE--PALFVCRPKIEEQALS---LAAETGCPAVVTLGSAADGSLMEtaqaAVPREDIVALGERDLAAILYTSGTTGR 171
Cdd:cd05938 83 VVAPElqEAVEEVLPALRADGVSvwyLSHTSNTEGVISLLDKVDAASDE----PVPASLRAHVTIKSPALYIYTSGTTGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 172 SKGAMLTH-KNLASNAktLARAWHFSADDRLIHALPIFHTHGL---FVACnvtLMAGASMLFLPKFDADVIFEELP--RG 245
Cdd:cd05938 159 PKAARISHlRVLQCSG--FLSLCGVTADDVIYITLPLYHSSGFllgIGGC---IELGATCVLKPKFSASQFWDDCRkhNV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 246 TVMMGVPTFYTRLVQDERLTPEATANMRLFVsGSApLTAETHEAFEAKTGH-AILERYGMTETNMNLSNpYDGarRAGTV 324
Cdd:cd05938 234 TVIQYIGELLRYLCNQPQSPNDRDHKVRLAI-GNG-LRADVWREFLRRFGPiRIREFYGSTEGNIGFFN-YTG--KIGAV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 325 G---------MPLPGVEMRITNRE-----TG--AEVPFGEIGML--QIRGPNVFIGYWRMPEKTREELLDDGF------F 380
Cdd:cd05938 309 GrvsylykllFPFELIKFDVEKEEpvrdaQGfcIPVAKGEPGLLvaKITQQSPFLGYAGDKEQTEKKLLRDVFkkgdvyF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 381 ITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDF-GE-GVTAVVVRQqgadlgEN 458
Cdd:cd05938 389 NTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHeGRiGMAAVKLKP------GH 462
|
490 500
....*....|....*....|..
gi 2136495511 459 QLEEEKVITHLDGRLAKYKQPK 480
Cdd:cd05938 463 EFDGKKLYQHVREYLPAYARPR 484
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
3-501 |
8.04e-31 |
|
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: 124.20 E-value: 8.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 3 HNLFETFAAKMRERAEADFittrDGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYL 82
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVD----RGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 83 PLNTGYTGDEIRYFLNDAEPALFVCRPKieeqalslaaetgcpavvtlgsaadgslmetaqaavpredivalgerDLAAI 162
Cdd:cd17645 77 PIDPDYPGERIAYMLADSSAKILLTNPD-----------------------------------------------DLAYV 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 163 LYTSGTTGRSKGAMLTHKNLASNAktlarAWHFSA------DDRLIHAlpIFHTHGLFVACNVTLMAGASMLFLP---KF 233
Cdd:cd17645 110 IYTSGSTGLPKGVMIEHHNLVNLC-----EWHRPYfgvtpaDKSLVYA--SFSFDASAWEIFPHLTAGAALHVVPserRL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 234 DADVI---FEElpRGTVMMGVPTFYTrlvqdERLTPEATANMRLFVSGSAPLtaethEAFEAKtGHAILERYGMTE-TNM 309
Cdd:cd17645 183 DLDALndyFNQ--EGITISFLPTGAA-----EQFMQLDNQSLRVLLTGGDKL-----KKIERK-GYKLVNNYGPTEnTVV 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 310 NLSNPYDGARRAGTVGMPLPGVEMRITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGF------FITG 383
Cdd:cd17645 250 ATSFEIDKPYANIPIGKPIDNTRVYILD-EALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFvpgermYRTG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 384 DLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVrqqgadlGENQLEEE 463
Cdd:cd17645 329 DLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT-------APEEIPHE 401
|
490 500 510
....*....|....*....|....*....|....*...
gi 2136495511 464 KVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNEL 501
Cdd:cd17645 402 ELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-503 |
1.90e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 126.61 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 3 HNLFETFAAKMRERAEADFittrDGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYL 82
Cdd:PRK12316 3060 HRLFEEQVERTPDAVALAF----GEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYV 3135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 83 PLNTGYTGDEIRYFLNDAEPALFVCRPKieeqaLSLAAETGCpAVVTLGSAADGSLMETAQAAVPREdivalgerDLAAI 162
Cdd:PRK12316 3136 PLDPEYPEERLAYMLEDSGAQLLLSQSH-----LRLPLAQGV-QVLDLDRGDENYAEANPAIRTMPE--------NLAYV 3201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 163 LYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPiFHTHGLFVACNVTLMAGASMLFLPKFDAD--VIFE 240
Cdd:PRK12316 3202 IYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTT-FSFDVFVEELFWPLMSGARVVLAGPEDWRdpALLV 3280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 241 ELPRGTVmMGVPTFYTRLVQD--ERLTPEATANMRLFVSGSAPLTAETHEAFEAktGHAILERYGMTETNMNLS--NPYD 316
Cdd:PRK12316 3281 ELINSEG-VDVLHAYPSMLQAflEEEDAHRCTSLKRIVCGGEALPADLQQQVFA--GLPLYNLYGPTEATITVThwQCVE 3357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 317 GARRAGTVGMPLPGVEMRITNrETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGF------FITGDLAMVDE 390
Cdd:PRK12316 3358 EGKDAVPIGRPIANRACYILD-GSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRA 3436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 391 QGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLphpDFGEGVTAVVVRQQGADLgenqleEEKVITHLD 470
Cdd:PRK12316 3437 DGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAV---DGRQLVAYVVPEDEAGDL------REALKAHLK 3507
|
490 500 510
....*....|....*....|....*....|...
gi 2136495511 471 GRLAKYKQPKRVFFVDELPRNTMGKVQKNELRK 503
Cdd:PRK12316 3508 ASLPEYMVPAHLLFLERMPLTPNGKLDRKALPR 3540
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
39-501 |
1.56e-29 |
|
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: 121.04 E-value: 1.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 39 SAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDaepalfvcrpkieeqalsl 118
Cdd:cd17656 23 SNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLD------------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 119 aaeTGCPAVVTLGSAADgSLMETAQAAVPREDIVALG----------ERDLAAILYTSGTTGRSKGAMLTHKNLASNAK- 187
Cdd:cd17656 84 ---SGVRVVLTQRHLKS-KLSFNKSTILLEDPSISQEdtsnidyinnSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHf 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 188 TLARAWHFSADDRLIHALPIFHT--HGLFvacnVTLMAGASMLFLP---KFDADVIFEELPRGTV-MMGVPTFYTRLVQD 261
Cdd:cd17656 160 EREKTNINFSDKVLQFATCSFDVcyQEIF----STLLSGGTLYIIReetKRDVEQLFDLVKRHNIeVVFLPVAFLKFIFS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 262 ER-LTPEATANMRLFVSGSAPL--TAETHEAFEAKTGHaILERYGMTETN---MNLSNPYDGARRAGTVGMPLPGVEMRI 335
Cdd:cd17656 236 EReFINRFPTCVKHIITAGEQLviTNEFKEMLHEHNVH-LHNHYGPSETHvvtTYTINPEAEIPELPPIGKPISNTWIYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 336 TNREtGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGF------FITGDLAMVDEQGYVHIVGRDKDLVISGGY 409
Cdd:cd17656 315 LDQE-QQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKIRGY 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 410 NVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQgaDLGENQLEEekvitHLDGRLAKYKQPKRVFFVDELP 489
Cdd:cd17656 394 RIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQ--ELNISQLRE-----YLAKQLPEYMIPSFFVPLDQLP 466
|
490
....*....|..
gi 2136495511 490 RNTMGKVQKNEL 501
Cdd:cd17656 467 LTPNGKVDRKAL 478
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
46-404 |
2.34e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 122.39 E-value: 2.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 46 LTELGVKQGDRVAVQVDKSPEAILLYLAC----LRIGGVYLPLNTgytgDEIRYFLNDAEPALFVCRPKIEEQALSLAAE 121
Cdd:PTZ00216 138 LAELGLTKGSNVAIYEETRWEWLASIYGIwsqsMVAATVYANLGE----DALAYALRETECKAIVCNGKNVPNLLRLMKS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 122 TGCPA--VVTLGSAADGSLMETAQAaVPREDIVALGER--------------DLAAILYTSGTTGRSKGAMLTHKNLASN 185
Cdd:PTZ00216 214 GGMPNttIIYLDSLPASVDTEGCRL-VAWTDVVAKGHSagshhplnipenndDLALIMYTSGTTGDPKGVMHTHGSLTAG 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 186 AKTLARAW-----HFSADDRLIHALPIFHTHGlFVACNVTLMAGASMLF--------------------LPKFDADV--I 238
Cdd:PTZ00216 293 ILALEDRLndligPPEEDETYCSYLPLAHIME-FGVTNIFLARGALIGFgsprtltdtfarphgdltefRPVFLIGVprI 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 239 FEEL---------PRGTVMMGV--PTFYTRL--VQDERLTP-----------EATA-NMRLFVSGSAPLTAETHEAFEAK 293
Cdd:PTZ00216 372 FDTIkkaveaklpPVGSLKRRVfdHAYQSRLraLKEGKDTPywnekvfsaprAVLGgRVRAMLSGGGPLSAATQEFVNVV 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 294 TGhAILERYGMTETNMNLSNPYDGARRAGTVGMPLPGVEMRITNRE----TGAEVPFGEIgmlQIRGPNVFIGYWRMPEK 369
Cdd:PTZ00216 452 FG-MVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEeykhTDTPEPRGEI---LLRGPFLFKGYYKQEEL 527
|
410 420 430
....*....|....*....|....*....|....*
gi 2136495511 370 TREELLDDGFFITGDLAMVDEQGYVHIVGRDKDLV 404
Cdd:PTZ00216 528 TREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALA 562
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
10-507 |
8.28e-29 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 121.43 E-value: 8.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 10 AAKMRERAEADFITTRDGRR----YRYTD--ALTISAQLAGAltelgVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLP 83
Cdd:PRK05691 19 AAQTPDRLALRFLADDPGEGvvlsYRDLDlrARTIAAALQAR-----ASFGDRAVLLFPSGPDYVAAFFGCLYAGVIAVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 84 lntGYTGDEIR--------YFLNDAEPALF-----VCRPKIEEQALSLAAETGCPAVVTLgsaaDGSLMETAQA-AVPRE 149
Cdd:PRK05691 94 ---AYPPESARrhhqerllSIIADAEPRLLltvadLRDSLLQMEELAAANAPELLCVDTL----DPALAEAWQEpALQPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 150 DIvalgerdlAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAW--HFSADDRLIHALPIFHTHGL--------FVACNV 219
Cdd:PRK05691 167 DI--------AFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFgiDLNPDDVIVSWLPLYHDMGLiggllqpiFSGVPC 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 220 TLMAGASMLFLPKFDADVIFEElpRGTVMMGvPTFYTRLVQdERLTPEATANM-----RLFVSGSAPLTAETHEAFEAK- 293
Cdd:PRK05691 239 VLMSPAYFLERPLRWLEAISEY--GGTISGG-PDFAYRLCS-ERVSESALERLdlsrwRVAYSGSEPIRQDSLERFAEKf 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 294 -----TGHAILERYGMTETNMNLSNPYDG--------------ARRA----GTV----GMPLPGVEMRITNRETGAEVPF 346
Cdd:PRK05691 315 aacgfDPDSFFASYGLAEATLFVSGGRRGqgipaleldaealaRNRAepgtGSVlmscGRSQPGHAVLIVDPQSLEVLGD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 347 GEIGMLQIRGPNVFIGYWRMPEKTREELLD-DG--FFITGDLAMVDEqGYVHIVGRDKDLVISGGYNVYPKEVEQVID-E 422
Cdd:PRK05691 395 NRVGEIWASGPSIAHGYWRNPEASAKTFVEhDGrtWLRTGDLGFLRD-GELFVTGRLKDMLIVRGHNLYPQDIEKTVErE 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 423 LDQVAESAVIGLPHPDFGE---GVTAVVVRQQgadlgENQLEEEKVITHLDGRLAKYKQ--PKRVFFVD--ELPRNTMGK 495
Cdd:PRK05691 474 VEVVRKGRVAAFAVNHQGEegiGIAAEISRSV-----QKILPPQALIKSIRQAVAEACQeaPSVVLLLNpgALPKTSSGK 548
|
570
....*....|..
gi 2136495511 496 VQKNELRKRFND 507
Cdd:PRK05691 549 LQRSACRLRLAD 560
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
27-503 |
9.54e-29 |
|
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: 118.68 E-value: 9.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 27 GRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAepalfv 106
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVS------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 107 crpkieeqalslaaetGCPAVVTLGSAAdgsLMETAQAAVPREDIValGERDLAAILYTSGTTGRSKGAMLTHKNLASNA 186
Cdd:cd05939 75 ----------------KAKALIFNLLDP---LLTQSSTEPPSQDDV--NFRDKLFYIYTSGTTGLPKAAVIVHSRYYRIA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 187 KTLARAWHFSADDRLIHALPIFHTHGLFVACNVTLMAGASMLFLPKFDADVIFEELPR--GTVMMGVPTFYTRLVQDERL 264
Cdd:cd05939 134 AGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKynCTIVQYIGEICRYLLAQPPS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 265 TPEATANMRLFVSGSapLTAETHEAFEAKTGHA-ILERYGMTETNMNLSNpYDGarRAGTVG-MP--LPGV-EMRI--TN 337
Cdd:cd05939 214 EEEQKHNVRLAVGNG--LRPQIWEQFVRRFGIPqIGEFYGATEGNSSLVN-IDN--HVGACGfNSriLPSVyPIRLikVD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 338 RETG-----------AEVPfGEIGML--QIRGPNV---FIGYWRMPEKTREELLD-----DGFFITGDLAMVDEQGYVHI 396
Cdd:cd05939 289 EDTGelirdsdglciPCQP-GEPGLLvgKIIQNDPlrrFDGYVNEGATNKKIARDvfkkgDSAFLSGDVLVMDELGYLYF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 397 VGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIG--LPHPDFGEGVTAVVVRQQGADLgenqleeEKVITHLDGRLA 474
Cdd:cd05939 368 KDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGveVPGVEGRAGMAAIVDPERKVDL-------DRFSAVLAKSLP 440
|
490 500
....*....|....*....|....*....
gi 2136495511 475 KYKQPKRVFFVDELPRNTMGKVQKNELRK 503
Cdd:cd05939 441 PYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
5-501 |
3.52e-28 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 119.50 E-value: 3.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 5 LFETFAAKMRERAEADFITTrDGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPL 84
Cdd:PRK05691 2190 LHGLFAAQAARTPQAPALTF-AGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPL 2268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 85 NTGYTGDEIRYFLNDAEPALFVcrpkieEQALSLAAETGCPAVVTLGSAADGSLMETAQAAVPREDIValGERDLAAILY 164
Cdd:PRK05691 2269 DPEYPLERLHYMIEDSGIGLLL------SDRALFEALGELPAGVARWCLEDDAAALAAYSDAPLPFLS--LPQHQAYLIY 2340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 165 TSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPI-FH--THGLFVAcnvtLMAGASMLFLP--KFDADVIF 239
Cdd:PRK05691 2341 TSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSInFDaaSERLLVP----LLCGARVVLRAqgQWGAEEIC 2416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 240 EELPRGTV-MMG-VPTFYTRLVQdERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAIL-ERYGMTET-NMNLSNPY 315
Cdd:PRK05691 2417 QLIREQQVsILGfTPSYGSQLAQ-WLAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQLFfNAYGPTETvVMPLACLA 2495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 316 DGARRAGTVGMPLPGVemrITNR------ETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGF-------FIT 382
Cdd:PRK05691 2496 PEQLEEGAASVPIGRV---VGARvayildADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFaadggrlYRT 2572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 383 GDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGENQLEE 462
Cdd:PRK05691 2573 GDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVSAVAGQDDEAQAALR 2652
|
490 500 510
....*....|....*....|....*....|....*....
gi 2136495511 463 EKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNEL 501
Cdd:PRK05691 2653 EALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
15-503 |
2.77e-27 |
|
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: 114.84 E-value: 2.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 15 ERAEADFITTRDGR-RYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEI 93
Cdd:cd05915 9 GRKEVVSRLHTGEVhRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 94 RYFLNDAEPALFVcrpkIEEQALSLAAETgcpavvtLGSAADGSLMETAQAAVPR-EDIVALG-----------ERDLAA 161
Cdd:cd05915 89 AYILNHAEDKVLL----FDPNLLPLVEAI-------RGELKTVQHFVVMDEKAPEgYLAYEEAlgeeadpvrvpERAACG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 162 ILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIH--ALPIFHTHGLFVACNVTLMAGASMLFLPKFDADVIF 239
Cdd:cd05915 158 MAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKDVVlpVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPASLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 240 EELPRGTV--MMGVPTFYTrLVQDERLTPEATA--NMRLFVSGSAP----LTAETHEAFEAKTGHAILERYGMtetnmnl 311
Cdd:cd05915 238 ELFDGEGVtfTAGVPTVWL-ALADYLESTGHRLktLRRLVVGGSAAprslIARFERMGVEVRQGYGLTETSPV------- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 312 snpydgarraGTVGMPLPGVE-------MRITNRE--------------TGAEVPFG--EIGMLQIRGPNVFIGYWRMPE 368
Cdd:cd05915 310 ----------VVQNFVKSHLEslseeekLTLKAKTglpiplvrlrvadeEGRPVPKDgkALGEVQLKGPWITGGYYGNEE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 369 KTREELLDDGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVv 448
Cdd:cd05915 380 ATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVV- 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2136495511 449 rqqgaDLGENQLEEEKVITHLDGRLAKYKQ-PKRVFFVDELPRNTMGKVQKNELRK 503
Cdd:cd05915 459 -----VPRGEKPTPEELNEHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
28-501 |
3.71e-27 |
|
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: 114.03 E-value: 3.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 28 RRYRYTDALTISAQLAGALTELGVKQGD-RVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDaepalfv 106
Cdd:cd17648 11 KRLTYRELNERANRLAHYLLSVAEIRPDdLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILED------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 107 crpkieeqalslaaeTGCPAVVTlgsaadgslmetaqaavpredivalGERDLAAILYTSGTTGRSKGAMLTHKNLASNA 186
Cdd:cd17648 84 ---------------TGARVVIT-------------------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 187 KTLARawHFSADDRLIHALPIF-------HTHGLFVAcnvtLMAGASMLFLP---KFDADVIFE--ELPRGTVMMGVPTF 254
Cdd:cd17648 124 TSLSE--RYFGRDNGDEAVLFFsnyvfdfFVEQMTLA----LLNGQKLVVPPdemRFDPDRFYAyiNREKVTYLSGTPSV 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 255 YTRLVQDERltpeaTANMRLFVSGSApLTAETHEAFEAKTGHAILERYGMTETNM-NLSNPYDGARRA-GTVGMPLPGVE 332
Cdd:cd17648 198 LQQYDLARL-----PHLKRVDAAGEE-FTAPVFEKLRSRFAGLIINAYGPTETTVtNHKRFFPGDQRFdKSLGRPVRNTK 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 333 MRITNRETgAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGF--------------FITGDLAMVDEQGYVHIVG 398
Cdd:cd17648 272 CYVLNDAM-KRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFqteqerargrnarlYKTGDLVRWLPSGELEYLG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 399 RDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGvtavvvRQQGADLG-----ENQLEEEKVITHLDGRL 473
Cdd:cd17648 351 RNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQS------RIQKYLVGyylpePGHVPESDLLSFLRAKL 424
|
490 500
....*....|....*....|....*...
gi 2136495511 474 AKYKQPKRVFFVDELPRNTMGKVQKNEL 501
Cdd:cd17648 425 PRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
26-503 |
1.00e-26 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 114.08 E-value: 1.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 26 DGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALF 105
Cdd:PRK00174 95 DSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEALADRIIDAGAKLV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 106 VC--------RP----KIEEQALSlaaetGCPAV-------VTLGSAA--DG------SLMETAQAAVPREdivALGERD 158
Cdd:PRK00174 175 ITadegvrggKPiplkANVDEALA-----NCPSVekvivvrRTGGDVDwvEGrdlwwhELVAGASDECEPE---PMDAED 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 159 LAAILYTSGTTGRSKG-----------AMLTHKnlasnaktlaraWHFsadDrlIHALPIF-----------HTHGLFVA 216
Cdd:PRK00174 247 PLFILYTSGSTGKPKGvlhttggylvyAAMTMK------------YVF---D--YKDGDVYwctadvgwvtgHSYIVYGP 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 217 cnvtLMAGASMlflpkfdadVIFEelprgtvmmGVPT------------------FYT-----R-LVQDERLTPEAT--A 270
Cdd:PRK00174 310 ----LANGATT---------LMFE---------GVPNypdpgrfwevidkhkvtiFYTaptaiRaLMKEGDEHPKKYdlS 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 271 NMRLFVSGSAPLTAETHEAFEAKTGH---AILERYGMTETNMNLSNPYDGAR--RAGTVGMPLPGVEMRITNrETGAEVP 345
Cdd:PRK00174 368 SLRLLGSVGEPINPEAWEWYYKVVGGercPIVDTWWQTETGGIMITPLPGATplKPGSATRPLPGIQPAVVD-EEGNPLE 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 346 FGEIGML--------QIRG----PNVFI-GYWRmPEKtreellddGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVY 412
Cdd:PRK00174 447 GGEGGNLvikdpwpgMMRTiygdHERFVkTYFS-TFK--------GMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLG 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 413 PKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADlGENQLEEE------KVIthldGRLAKykqPKRVFFVD 486
Cdd:PRK00174 518 TAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEE-PSDELRKElrnwvrKEI----GPIAK---PDVIQFAP 589
|
570
....*....|....*..
gi 2136495511 487 ELPRNTMGKVQKNELRK 503
Cdd:PRK00174 590 GLPKTRSGKIMRRILRK 606
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
25-503 |
6.27e-26 |
|
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: 110.60 E-value: 6.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 25 RDGRRYRYTDALTISAQLAGAL-TELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNdaepa 103
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLhDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLK----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 104 lfVCRPKIeeqalslaaetgcpavvtlgsaadgslmetaqaavprediVALGERDLAAILYTSGTTGRSKGAMLTHKNLA 183
Cdd:cd05937 76 --LSGSRF----------------------------------------VIVDPDDPAILIYTSGTTGLPKAAAISWRRTL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 184 SNAKTLARAWHFSADDRLIHALPIFH-THGLFVACNVtLMAGASMLFLPKFDADVIFEE--LPRGTVMMGVPTFYTRLVQ 260
Cdd:cd05937 114 VTSNLLSHDLNLKNGDRTYTCMPLYHgTAAFLGACNC-LMSGGTLALSRKFSASQFWKDvrDSGATIIQYVGELCRYLLS 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 261 DERLTPEATANMRLfVSGSApLTAETHEAFEAKTG-HAILERYGMTETNMNLSNPYDGARRAGTVGM--PL--------- 328
Cdd:cd05937 193 TPPSPYDRDHKVRV-AWGNG-LRPDIWERFRERFNvPEIGEFYAATEGVFALTNHNVGDFGAGAIGHhgLIrrwkfenqv 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 329 ------PGVEMRITNRETG--AEVPFGEIG--MLQIRGPNV--FIGYWRMPEKTREELLDDGF------FITGDLAMVDE 390
Cdd:cd05937 271 vlvkmdPETDDPIRDPKTGfcVRAPVGEPGemLGRVPFKNReaFQGYLHNEDATESKLVRDVFrkgdiyFRTGDLLRQDA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 391 QGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIG--LPHPDFGEGVTAVVVRQQGADlgENQLEEEKVITH 468
Cdd:cd05937 351 DGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGvkVPGHDGRAGCAAITLEESSAV--PTEFTKSLLASL 428
|
490 500 510
....*....|....*....|....*....|....*
gi 2136495511 469 LDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRK 503
Cdd:cd05937 429 ARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
39-482 |
1.07e-25 |
|
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: 109.47 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 39 SAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVCRPKIEEQAlsl 118
Cdd:cd05910 12 SDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFIGIPKADEPA--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 119 aaetgcpavvtlgsaadgslmetaqaavpredivalgerdlaAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSAD 198
Cdd:cd05910 89 ------------------------------------------AILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 199 DRLIHALPIFhthGLF-VACNVTLMAGAsMLFLPKFDAD----VIFEELPRGTVMMGVPTFYTRLVQDERLTPEATANMR 273
Cdd:cd05910 127 EVDLATFPLF---ALFgPALGLTSVIPD-MDPTRPARADpqklVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 274 LFVSGSAPLTAETHEAFEA--KTGHAILERYGMTET---------NMNLSNPYDGARRAGT-VGMPLPGVEMRITNRETG 341
Cdd:cd05910 203 RVLSAGAPVPIALAARLRKmlSDEAEILTPYGATEAlpvssigsrELLATTTAATSGGAGTcVGRPIPGVRVRIIEIDDE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 342 A--------EVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDG----FFITGDLAMVDEQGYVHIVGRDKDLVISGGY 409
Cdd:cd05910 283 PiaewddtlELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGG 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2136495511 410 NVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVtAVVVRQQGADLGENQLEEEkvithLDGRLAKYKQPKRV 482
Cdd:cd05910 363 TLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPV-LCVEPLPGTITPRARLEQE-----LRALAKDYPHTQRI 429
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
155-422 |
2.00e-25 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 109.52 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 155 GERDLAAILYTSGTTGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGlFVACNV-TLMAGASMLFL--- 230
Cdd:PRK06334 181 DPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYG-FNSCTLfPLLSGVPVVFAynp 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 231 --PKFDADVIFEElpRGTVMMGVPTFYTRLVQDERLTPEATANMRLFVSGSAPLTAETHEAFEAKTGHAILER-YGMTET 307
Cdd:PRK06334 260 lyPKKIVEMIDEA--KVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQgYGTTEC 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 308 NMNLS-NPYDGARRAGTVGMPLPGVEMRITNRETGAEVPFGEIGMLQIRGPNVFIGYW-RMPEKTREELLDDGFFITGDL 385
Cdd:PRK06334 338 SPVITiNTVNSPKHESCVGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDL 417
|
250 260 270
....*....|....*....|....*....|....*..
gi 2136495511 386 AMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDE 422
Cdd:PRK06334 418 GYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILME 454
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
26-501 |
5.10e-25 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 109.87 E-value: 5.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 26 DGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALF 105
Cdd:PRK05691 1153 DGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELL 1232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 106 VcrpkieEQALSLAAETGCPAVVTLgsAADGSLMETAQAAVPRediVALGERDLAAILYTSGTTGRSKGAMLTHKNLASN 185
Cdd:PRK05691 1233 L------TQSHLLERLPQAEGVSAI--ALDSLHLDSWPSQAPG---LHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAER 1301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 186 AKTLARAWHFSADDRLIHALPIFHTHGLFvACNVTLMAGASMLFL-------PKFDADVIFEElpRGTVMMGVPTFYTRL 258
Cdd:PRK05691 1302 LQWMQATYALDDSDVLMQKAPISFDVSVW-ECFWPLITGCRLVLAgpgehrdPQRIAELVQQY--GVTTLHFVPPLLQLF 1378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 259 VqDERLTPEATANMRLFvSGSAPLTAETHE-AFEAKTGHAILERYGMTETNMNLSNPY----DGARraGTVGMPLPGVEM 333
Cdd:PRK05691 1379 I-DEPLAAACTSLRRLF-SGGEALPAELRNrVLQRLPQVQLHNRYGPTETAINVTHWQcqaeDGER--SPIGRPLGNVLC 1454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 334 RITNRETgAEVPFGEIGMLQIRGPNVFIGYWRMPEKTREELLDDGF-------FITGDLAMVDEQGYVHIVGRDKDLVIS 406
Cdd:PRK05691 1455 RVLDAEL-NLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLgedgarlYRTGDRARWNADGALEYLGRLDQQVKL 1533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 407 GGYNVYPKEVEQVIDELDQVAESAVIglphpdfgegVTAVVVRQQ--GADLGENQLEE--EKVITHLDGRLAKYKQPKRV 482
Cdd:PRK05691 1534 RGFRVEPEEIQARLLAQPGVAQAAVL----------VREGAAGAQlvGYYTGEAGQEAeaERLKAALAAELPEYMVPAQL 1603
|
490
....*....|....*....
gi 2136495511 483 FFVDELPRNTMGKVQKNEL 501
Cdd:PRK05691 1604 IRLDQMPLGPSGKLDRRAL 1622
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
32-502 |
1.16e-24 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 108.01 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 32 YTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPAL-FVCRPK 110
Cdd:PLN02861 80 YKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIaFVQESK 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 111 IEEqalSLAAETGCPA----VVTLGSAADGSLMETAQAAVP---REDIVALGER----------DLAAILYTSGTTGRSK 173
Cdd:PLN02861 160 ISS---ILSCLPKCSSnlktIVSFGDVSSEQKEEAEELGVScfsWEEFSLMGSLdcelppkqktDICTIMYTSGTTGEPK 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 174 GAMLTHKNLASNAKTLARAWHFS-----ADDRLIHALPIFHTHGLFVAcNVTLMAGASMLFlpkFDADVIF-----EELp 243
Cdd:PLN02861 237 GVILTNRAIIAEVLSTDHLLKVTdrvatEEDSYFSYLPLAHVYDQVIE-TYCISKGASIGF---WQGDIRYlmedvQAL- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 244 RGTVMMGVPTFYTR----------------------------------LVQDE------RLTPEAT-----ANMRLFVSG 278
Cdd:PLN02861 312 KPTIFCGVPRVYDRiytgimqkissggmlrkklfdfaynyklgnlrkgLKQEEasprldRLVFDKIkeglgGRVRLLLSG 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 279 SAPLTAETHEAFEAKTGHAILERYGMTETN----MNLSNPYDgarRAGTVGMPLPGVEMRITN-RETG----AEVPFGEI 349
Cdd:PLN02861 392 AAPLPRHVEEFLRVTSCSVLSQGYGLTESCggcfTSIANVFS---MVGTVGVPMTTIEARLESvPEMGydalSDVPRGEI 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 350 GMlqiRGPNVFIGYWRMPEKTrEELLDDGFFITGDLAMVDEQGYVHIVGRDKDLV-ISGGYNVYPKEVEQVIDELDQVAE 428
Cdd:PLN02861 469 CL---RGNTLFSGYHKRQDLT-EEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLIAS 544
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2136495511 429 SAVIGLPHPDFgegVTAVVVRQQGAdlgenqLEEEKVITHLDGRLAKY-KQPK-RVFFVDELprNTMGKvqKNELR 502
Cdd:PLN02861 545 IWVYGNSFESF---LVAVVVPDRQA------LEDWAANNNKTGDFKSLcKNLKaRKYILDEL--NSTGK--KLQLR 607
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
14-404 |
1.61e-24 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 107.51 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 14 RERAEADFITTRDGRRYR-----------YTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLR----IG 78
Cdd:PLN02387 80 RKLISREFETSSDGRKFEklhlgeyewitYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRqnitVV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 79 GVYLPLntgytGDE-IRYFLNDAEPALFVCRPKIEEQALSLAAETGCPAVVTL----GSAADGSLMETAQAAVPR-EDIV 152
Cdd:PLN02387 160 TIYASL-----GEEaLCHSLNETEVTTVICDSKQLKKLIDISSQLETVKRVIYmddeGVDSDSSLSGSSNWTVSSfSEVE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 153 ALGER-----------DLAAILYTSGTTGRSKGAMLTHKN-LASNAKTLARAWHFSADDRLIHALPIFHTHGLfVACNVT 220
Cdd:PLN02387 235 KLGKEnpvdpdlpspnDIAVIMYTSGSTGLPKGVMMTHGNiVATVAGVMTVVPKLGKNDVYLAYLPLAHILEL-AAESVM 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 221 LMAGASM-----LFL----------PKFDADVIfeelpRGTVMMGVPTFYTRlVQD------------------------ 261
Cdd:PLN02387 314 AAVGAAIgygspLTLtdtsnkikkgTKGDASAL-----KPTLMTAVPAILDR-VRDgvrkkvdakgglakklfdiaykrr 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 262 --------------ERLTPEATA----------NMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTET--NMNLSNPY 315
Cdd:PLN02387 388 laaiegswfgawglEKLLWDALVfkkiravlggRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETcaGATFSEWD 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 316 DGArrAGTVGMPLPGVEMRITNRETG------AEVPFGEIgmlQIRGPNVFIGYWRMPEKTREELLDDG----FFITGDL 385
Cdd:PLN02387 468 DTS--VGRVGPPLPCCYVKLVSWEEGgylisdKPMPRGEI---VIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGDI 542
|
490
....*....|....*....
gi 2136495511 386 AMVDEQGYVHIVGRDKDLV 404
Cdd:PLN02387 543 GQFHPDGCLEIIDRKKDIV 561
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
38-385 |
2.62e-23 |
|
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: 103.30 E-value: 2.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 38 ISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVCRPKIEEQALS 117
Cdd:cd17632 77 VGAVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAEHLDLAVE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 118 LAAETGCPA-VVTLG------------------SAADGSLMETAQAAVPREDIVALGERD--------LAAILYTSGTTG 170
Cdd:cd17632 157 AVLEGGTPPrLVVFDhrpevdahraalesarerLAAVGIPVTTLTLIAVRGRDLPPAPLFrpepdddpLALLIYTSGSTG 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 171 RSKGAMLTHKNlasnaktLARAWHFSA---DDR-----LIHALPIFHTHG---LFvacnVTLMAGASMLFLPKFDADVIF 239
Cdd:cd17632 237 TPKGAMYTERL-------VATFWLKVSsiqDIRppasiTLNFMPMSHIAGrisLY----GTLARGGTAYFAAASDMSTLF 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 240 EELP--RGTVMMGVPTFYTRLVQ------DERLTPEATA------------------NMRLFVSGSAPLTAETHEAFEAK 293
Cdd:cd17632 306 DDLAlvRPTELFLVPRVCDMLFQryqaelDRRSVAGADAetlaervkaelrervlggRLLAAVCGSAPLSAEMKAFMESL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 294 TGHAILERYGMTETNMNLSNpydgarraGTVGMPlPGVEMRITNR------ETGAEVPFGEigmLQIRGPNVFIGYWRMP 367
Cdd:cd17632 386 LDLDLHDGYGSTEAGAVILD--------GVIVRP-PVLDYKLVDVpelgyfRTDRPHPRGE---LLVKTDTLFPGYYKRP 453
|
410
....*....|....*...
gi 2136495511 368 EKTREELLDDGFFITGDL 385
Cdd:cd17632 454 EVTAEVFDEDGFYRTGDV 471
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
20-417 |
5.27e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 102.50 E-value: 5.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 20 DFITTRDG--RRYRYTDALTISAQLAGALTELGvKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPL----NTGYTGdEI 93
Cdd:PRK07769 44 DFSTERDGvaRDLTWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfdpaEPGHVG-RL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 94 RYFLNDAEPALFVCRPKIEEQALSL-----AAETgcPAVVTLGSAADgSLMETAQAAVPREDivalgerDLAAILYTSGT 168
Cdd:PRK07769 122 HAVLDDCTPSAILTTTDSAEGVRKFfrarpAKER--PRVIAVDAVPD-EVGATWVPPEANED-------TIAYLQYTSGS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 169 TGRSKGAMLTHKNLASNAKTLARAWHFSADDRLIHALPIFHTHGLFVAC-------NVTLMAGASMLFLP-KFDADVIFE 240
Cdd:PRK07769 192 TRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLlpallghYITFMSPAAFVRRPgRWIRELARK 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 241 ELPRGTVMMGVPTFY-----TRLVQDERLTPEATANMRLFVSGSAPLTAET----HEAFE----AKTghAILERYGMTET 307
Cdd:PRK07769 272 PGGTGGTFSAAPNFAfehaaARGLPKDGEPPLDLSNVKGLLNGSEPVSPASmrkfNEAFApyglPPT--AIKPSYGMAEA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 308 NMNLSN-PYD-------------GARR----------------AGTVGMPLPGVemrITNRETGAEVPFGEIGMLQIRGP 357
Cdd:PRK07769 350 TLFVSTtPMDeeptviyvdrdelNAGRfvevpadapnavaqvsAGKVGVSEWAV---IVDPETASELPDGQIGEIWLHGN 426
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2136495511 358 NVFIGYWRMPEKTREELL-----------------DDGFFITGDLAmVDEQGYVHIVGRDKDLVISGGYNVYPKEVE 417
Cdd:PRK07769 427 NIGTGYWGKPEETAATFQnilksrlseshaegapdDALWVRTGDYG-VYFDGELYITGRVKDLVIIDGRNHYPQDLE 502
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
32-503 |
1.18e-22 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 101.51 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 32 YTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDaepalfvCRPKI 111
Cdd:PLN02654 123 YSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVD-------CKPKV 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 112 eeqALSLAAETGCPAVVTLGSAADGSLMETA--------------QAAVPREDIVALGERDL------------------ 159
Cdd:PLN02654 196 ---VITCNAVKRGPKTINLKDIVDAALDESAkngvsvgicltyenQLAMKREDTKWQEGRDVwwqdvvpnyptkcevewv 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 160 -----AAILYTSGTTGRSKGAMLTHKN-LASNAKTLARAWHF--------SADDRLI--HAlpiFHTHGlfvacnvTLMA 223
Cdd:PLN02654 273 daedpLFLLYTSGSTGKPKGVLHTTGGyMVYTATTFKYAFDYkptdvywcTADCGWItgHS---YVTYG-------PMLN 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 224 GASMLflpkfdadvIFEELP---------------RGTVMMGVPTFYTRLVQD--ERLTPEATANMRLFVSGSAPLTAET 286
Cdd:PLN02654 343 GATVL---------VFEGAPnypdsgrcwdivdkyKVTIFYTAPTLVRSLMRDgdEYVTRHSRKSLRVLGSVGEPINPSA 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 287 HEAFEAKTGHA---ILERYGMTETNMNLSNPYDGA--RRAGTVGMPLPGVEMRITNrETGAEVPfGEI-GMLQIRG--PN 358
Cdd:PLN02654 414 WRWFFNVVGDSrcpISDTWWQTETGGFMITPLPGAwpQKPGSATFPFFGVQPVIVD-EKGKEIE-GECsGYLCVKKswPG 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 359 VFIGYWRMPEKTREELLD--DGFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPH 436
Cdd:PLN02654 492 AFRTLYGDHERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEH 571
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2136495511 437 PDFGEGVTAVVVRQQGADLGEnQLEEEKVIThLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRK 503
Cdd:PLN02654 572 EVKGQGIYAFVTLVEGVPYSE-ELRKSLILT-VRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 636
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
164-501 |
1.91e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 99.34 E-value: 1.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 164 YTSGTTGrskgamlthknlasNAKTLARAWH------------FSADDRL--IHALPIFHTHGLFVACNVTLMAGASMLF 229
Cdd:PRK08308 108 YSSGTTG--------------EPKLIRRSWTeidreieayneaLNCEQDEtpIVACPVTHSYGLICGVLAALTRGSKPVI 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 230 L----PKFdADVIFEELPRgTVMMGVPTFYTRLVqdeRLTPEATANMRLFVSGsAPLTAETHEAFEAKTGHaILERYGMT 305
Cdd:PRK08308 174 ItnknPKF-ALNILRNTPQ-HILYAVPLMLHILG---RLLPGTFQFHAVMTSG-TPLPEAWFYKLRERTTY-MMQQYGCS 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 306 ET-----NMNLSNPYDgarragtVGMPLPGVEMRI-TNRETGAEVPFgEIGMLQIRgpnvfigywrmpektreellddgf 379
Cdd:PRK08308 247 EAgcvsiCPDMKSHLD-------LGNPLPHVSVSAgSDENAPEEIVV-KMGDKEIF------------------------ 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 380 fiTGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLgeNQ 459
Cdd:PRK08308 295 --TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDP--VQ 370
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2136495511 460 LEEEKVithldGRLAKYKQPKRVFFVDELPRNTMGKVQKNEL 501
Cdd:PRK08308 371 LREWCI-----QHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
32-433 |
5.90e-22 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 99.71 E-value: 5.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 32 YTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVcrpkI 111
Cdd:PLN02614 82 YQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVF----V 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 112 EEQALSLAAETgCP-------AVVTLGSAADGSLMETAQAAV---PREDIVALGE-----------RDLAAILYTSGTTG 170
Cdd:PLN02614 158 EEKKISELFKT-CPnsteymkTVVSFGGVSREQKEEAETFGLviyAWDEFLKLGEgkqydlpikkkSDICTIMYTSGTTG 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 171 RSKGAMLTHKNLASnakTLARAWHF--------SADDRLIHALPIFHT-----------HG------------------- 212
Cdd:PLN02614 237 DPKGVMISNESIVT---LIAGVIRLlksanaalTVKDVYLSYLPLAHIfdrvieecfiqHGaaigfwrgdvklliedlge 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 213 ----LFVACNVTLMAGASML--------FLPKFDADVIFE----ELPRGTVMMGVPTFYTRLVQDeRLTPEATANMRLFV 276
Cdd:PLN02614 314 lkptIFCAVPRVLDRVYSGLqkklsdggFLKKFVFDSAFSykfgNMKKGQSHVEASPLCDKLVFN-KVKQGLGGNVRIIL 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 277 SGSAPLTAETHEAFEAKTGHAILERYGMTETNMN--LSNPyDGARRAGTVGMPLPGVEMRI-----TNRETGAEVPFGEI 349
Cdd:PLN02614 393 SGAAPLASHVESFLRVVACCHVLQGYGLTESCAGtfVSLP-DELDMLGTVGPPVPNVDIRLesvpeMEYDALASTPRGEI 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 350 GmlqIRGPNVFIGYWRMPEKTREELLdDGFFITGDLAMVDEQGYVHIVGRDKDLV-ISGGYNVYPKEVEQVIDELDQVAE 428
Cdd:PLN02614 472 C---IRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPNGSMKIIDRKKNIFkLSQGEYVAVENIENIYGEVQAVDS 547
|
....*
gi 2136495511 429 SAVIG 433
Cdd:PLN02614 548 VWVYG 552
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
6-506 |
3.29e-21 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 96.50 E-value: 3.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 6 FETFAakmreRAEADFITTRD-GRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPL 84
Cdd:PRK04813 8 IEEFA-----QTQPDFPAYDYlGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 85 NTGYTGDEIRYFLNDAEPALFVCrpkIEEQALSLaaeTGCPaVVTLGSAADGSLmetAQAAVPREDIValGERDLAAILY 164
Cdd:PRK04813 83 DVSSPAERIEMIIEVAKPSLIIA---TEELPLEI---LGIP-VITLDELKDIFA---TGNPYDFDHAV--KGDDNYYIIF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 165 TSGTTGRSKGAMLTHKNLAS-------------NAKTLARAwHFSADDRLIHALPifhthglfvacnvTLMAGASMLFLP 231
Cdd:PRK04813 151 TSGTTGKPKGVQISHDNLVSftnwmledfalpeGPQFLNQA-PYSFDLSVMDLYP-------------TLASGGTLVALP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 232 KfdaDVI------FEELPRGTV-----------M-MGVPTFytrlvqDERLTPEATanmRLFVSGSApLTAETHEAFEAK 293
Cdd:PRK04813 217 K---DMTanfkqlFETLPQLPInvwvstpsfadMcLLDPSF------NEEHLPNLT---HFLFCGEE-LPHKTAKKLLER 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 294 TGHA-ILERYGMTETNMNLS---------NPYDGArragTVGMPLPGVEMRITNrETGAEVPFGEIGMLQIRGPNVFIGY 363
Cdd:PRK04813 284 FPSAtIYNTYGPTEATVAVTsieitdemlDQYKRL----PIGYAKPDSPLLIID-EEGTKLPDGEQGEIVISGPSVSKGY 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 364 WRMPEKTREELLD-DG--FFITGDLAMVDEqGYVHIVGRdKDLVIS-GGYNVYPKEVEQVIDELDQVaESAVIgLPHPDf 439
Cdd:PRK04813 359 LNNPEKTAEAFFTfDGqpAYHTGDAGYLED-GLLFYQGR-IDFQIKlNGYRIELEEIEQNLRQSSYV-ESAVV-VPYNK- 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2136495511 440 GEGVT---AVVVrqqgadLGENQLEEEKVITH-----LDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRKRFN 506
Cdd:PRK04813 434 DHKVQyliAYVV------PKEEDFEREFELTKaikkeLKERLMEYMIPRKFIYRDSLPLTPNGKIDRKALIEEVN 502
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
120-503 |
8.52e-21 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 95.60 E-value: 8.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 120 AETGCPAVVTLGSAADgsLMETAQAAVPREDIVALG--ERDLA---------AILY-TSGTTGRSKGAMLTHKNLASNAK 187
Cdd:PRK05851 105 AGIGVRTVLSHGSHLE--RLRAVDSSVTVHDLATAAhtNRSASltppdsggpAVLQgTAGSTGTPRTAILSPGAVLSNLR 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 188 TL-ARAWHFSADDRLIHALPIFHTHGL-FVACNVtlMAGASMLFLPK--FDADViFEELP----RGTVMMGVPTF----- 254
Cdd:PRK05851 183 GLnARVGLDAATDVGCSWLPLYHDMGLaFLLTAA--LAGAPLWLAPTtaFSASP-FRWLSwlsdSRATLTAAPNFaynli 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 255 --YTRLVQDERLtpeatANMRLFVSGSAPLTAETHEAFEAKTGH------AILERYGMTETNMNLSNPYDGA-------- 318
Cdd:PRK05851 260 gkYARRVSDVDL-----GALRVALNGGEPVDCDGFERFATAMAPfgfdagAAAPSYGLAESTCAVTVPVPGIglrvdevt 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 319 -------RRAGTVGMPLPGVEMRITNRETGAEVPFGEIGMLQIRGPNVFIGYwrmpekTREELLD-DGFFITGDLAMVDE 390
Cdd:PRK05851 335 tddgsgaRRHAVLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGY------LGQAPIDpDDWFPTGDLGYLVD 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 391 QGYVhIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLphpDFGEGVT----AVVVRQQGADLGENQLEEEKVI 466
Cdd:PRK05851 409 GGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAV---GTGEGSArpglVIAAEFRGPDEAGARSEVVQRV 484
|
410 420 430
....*....|....*....|....*....|....*....
gi 2136495511 467 THLDGRLakykqPKRVFFVD--ELPRNTMGKVQKNELRK 503
Cdd:PRK05851 485 ASECGVV-----PSDVVFVApgSLPRTSSGKLRRLAVKR 518
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
41-448 |
9.56e-21 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 95.65 E-value: 9.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 41 QLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAE-PALFVCRPKIEEQalsLA 119
Cdd:PLN02430 88 QIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEiDFVFVQDKKIKEL---LE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 120 AETGCP----AVVTLGSAADGSLMETAQAAVPR---EDIVALGER-----------DLAAILYTSGTTGRSKGAMLTHKN 181
Cdd:PLN02430 165 PDCKSAkrlkAIVSFTSVTEEESDKASQIGVKTyswIDFLHMGKEnpsetnppkplDICTIMYTSGTSGDPKGVVLTHEA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 182 LASNAKTLARAWH-----FSADDRLIHALPIFHTHGLFVAcNVTLMAGASMLFLPKfDADVIFEELP--RGTVMMGVPTF 254
Cdd:PLN02430 245 VATFVRGVDLFMEqfedkMTHDDVYLSFLPLAHILDRMIE-EYFFRKGASVGYYHG-DLNALRDDLMelKPTLLAGVPRV 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 255 YTRLVQD-----ERLTP-----------EATANM-----------------------------RLFVSGSAPLTAETHEA 289
Cdd:PLN02430 323 FERIHEGiqkalQELNPrrrlifnalykYKLAWMnrgyshkkaspmadflafrkvkaklggrlRLLISGGAPLSTEIEEF 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 290 FEAKTGHAILERYGMTETNMNLSNPY-DGARRAGTVGMPLPGVEMRITNRETGAEVPFGE--IGMLQIRGPNVFIGYWRM 366
Cdd:PLN02430 403 LRVTSCAFVVQGYGLTETLGPTTLGFpDEMCMLGTVGAPAVYNELRLEEVPEMGYDPLGEppRGEICVRGKCLFSGYYKN 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 367 PEKTReELLDDGFFITGDLAMVDEQGYVHIVGRDKDLV-ISGGYNVYPKEVEQVIDELDQVAESAVIGlphPDFGEGVTA 445
Cdd:PLN02430 483 PELTE-EVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEYLENVYGQNPIVEDIWVYG---DSFKSMLVA 558
|
...
gi 2136495511 446 VVV 448
Cdd:PLN02430 559 VVV 561
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
30-501 |
1.15e-18 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 88.30 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 30 YRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNTGYTGDEIRYFLNDAEPALFVcrp 109
Cdd:cd17654 17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 110 kiEEQALSLAAETGCPAVVTLGSAADGSlmetaqaavpredivalgerdLAAILYTSGTTGRSKGAMLTHKNLASNAKTL 189
Cdd:cd17654 94 --QNKELDNAPLSFTPEHRHFNIRTDEC---------------------LAYVIHTSGTTGTPKIVAVPHKCILPNIQHF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 190 ARAWHFSADDRLIHAlPIFHTHGLFVACNVTLMAGASMLF-------LPKFDADVIFeELPRGTVMMGVPT----FYTRL 258
Cdd:cd17654 151 RSLFNITSEDILFLT-SPLTFDPSVVEIFLSLSSGATLLIvptsvkvLPSKLADILF-KRHRITVLQATPTlfrrFGSQS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 259 VQDERLTpeATANMRLFVSGSAPLTAETHEAFEAKTGHA--ILERYGMTETNMnLSNPYDGARRAGTV--GMPLPGVEMR 334
Cdd:cd17654 229 IKSTVLS--ATSSLRVLALGGEPFPSLVILSSWRGKGNRtrIFNIYGITEVSC-WALAYKVPEEDSPVqlGSPLLGTVIE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 335 ITNrETGAEVPfgeiGMLQIRGPNvfIGYWRMPEKTREELLddgFFITGDLAMVdEQGYVHIVGRDKDLVISGGYNVYPK 414
Cdd:cd17654 306 VRD-QNGSEGT----GQVFLGGLN--RVCILDDEVTVPKGT---MRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 415 EVEQVIDELDQVAESAVIGLPHpdfgEGVTAVVVrqqgaDLGENQLEEEKVITHLdgrLAKYKQPKRVFFVDELPRNTMG 494
Cdd:cd17654 375 LIQQVIESCLGVESCAVTLSDQ----QRLIAFIV-----GESSSSRIHKELQLTL---LSSHAIPDTFVQIDKLPLTSHG 442
|
....*..
gi 2136495511 495 KVQKNEL 501
Cdd:cd17654 443 KVDKSEL 449
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
5-501 |
6.47e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 87.92 E-value: 6.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 5 LFETFAAKMRERAEADFIttrdGRRYRYTDALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPL 84
Cdd:PRK05691 3725 LFEAQVAAHPQRIAASCL----DQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPL 3800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 85 NTGYTGDEIRYFLNDAEPALFVCRPKIEEQALSLAAETGCpavvtlgsAADGSLM---ETAQAAVPREDI-VALGERDLA 160
Cdd:PRK05691 3801 DPGLPAQRLQRIIELSRTPVLVCSAACREQARALLDELGC--------ANRPRLLvweEVQAGEVASHNPgIYSGPDNLA 3872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 161 AILYTSGTTGRSKGAMLTHKNLASN----------------AKTLARAWHFSADDRLihALPIFhthGLFVACNVTLMAG 224
Cdd:PRK05691 3873 YVIYTSGSTGLPKGVMVEQRGMLNNqlskvpylalseadviAQTASQSFDISVWQFL--AAPLF---GARVEIVPNAIAH 3947
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 225 ASMLFLPKFDADVIfeelprgTVMMGVPTFYTRLVQDERLTPEATANMrlfvsgsapltAETHEAFEAKTGHAILERYgm 304
Cdd:PRK05691 3948 DPQGLLAHVQAQGI-------TVLESVPSLIQGMLAEDRQALDGLRWM-----------LPTGEAMPPELARQWLQRY-- 4007
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 305 teTNMNLSNPYDGAR-----------RAGTVGMPLPGVEMRITNR-----ETGAEVPFGEIGMLQIRGPNVFIGYWRMPE 368
Cdd:PRK05691 4008 --PQIGLVNAYGPAEcsddvaffrvdLASTRGSYLPIGSPTDNNRlylldEALELVPLGAVGELCVAGTGVGRGYVGDPL 4085
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 369 KTREELLDDGF-------FITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDfGE 441
Cdd:PRK05691 4086 RTALAFVPHPFgapgerlYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVN-GK 4164
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 442 GVTAVVVRQQGADLGENQLEEEKviTHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKNEL 501
Cdd:PRK05691 4165 HLVGYLVPHQTVLAQGALLERIK--QRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
20-422 |
1.26e-17 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 85.95 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 20 DFITTRDGRRYRYT-DALTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYLPLNT----GYTgDEIR 94
Cdd:PRK12476 57 DHSHSAAGCAVELTwTQLGVRLRAVGARLQQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFApelpGHA-ERLD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 95 YFLNDAEPALF----VCRPKIEEQALSLAAETGcPAVVTLGSAADgSLMETAQAAVPREDivalgerDLAAILYTSGTTG 170
Cdd:PRK12476 136 TALRDAEPTVVltttAAAEAVEGFLRNLPRLRR-PRVIAIDAIPD-SAGESFVPVELDTD-------DVSHLQYTSGSTR 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 171 RSKGAMLTHKNLASNAKTLArawhFSAD--DRLIHA---LPIFHTHGL----FVAC---NVTLMAGASMLFLPKFDADVI 238
Cdd:PRK12476 207 PPVGVEITHRAVGTNLVQMI----LSIDllDRNTHGvswLPLYHDMGLsmigFPAVyggHSTLMSPTAFVRRPQRWIKAL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 239 FEELPRGTVMMGVPTFYTRLVQdERLTPEATANMRL----FVSGSAPLTAETHEAFEAKTG------HAILERYGMTETN 308
Cdd:PRK12476 283 SEGSRTGRVVTAAPNFAYEWAA-QRGLPAEGDDIDLsnvvLIIGSEPVSIDAVTTFNKAFApyglprTAFKPSYGIAEAT 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 309 MNLSN-PYD-------------GARRAGTV-------------GMPLPGVEMRITNRETGAEVPFGEIGMLQIRGPNVFI 361
Cdd:PRK12476 362 LFVATiAPDaepsvvyldreqlGAGRAVRVaadapnavahvscGQVARSQWAVIVDPDTGAELPDGEVGEIWLHGDNIGR 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 362 GYWRMPEKTREEL-------LDDG-----------FFITGDLAM-VDeqGYVHIVGRDKDLVISGGYNVYPKEVEQVIDE 422
Cdd:PRK12476 442 GYWGRPEETERTFgaklqsrLAEGshadgaaddgtWLRTGDLGVyLD--GELYITGRIADLIVIDGRNHYPQDIEATVAE 519
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
11-423 |
3.52e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 84.61 E-value: 3.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 11 AKMRERAEadfiTTRDGRRYRYTD----------ALTISaQL-------AGALTELGVKqGDRVAVQVDKSPEAILLYLA 73
Cdd:PRK05850 5 SLLRERAS----LQPDDAAFTFIDyeqdpagvaeTLTWS-QLyrrtlnvAEELRRHGST-GDRAVILAPQGLEYIVAFLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 74 CLRIGGVYLPLNTGYTG--DE-IRYFLNDAEPAlfvcrpkieeqalslaaetgcpaVVTLGSAADGSLMETAQAA----- 145
Cdd:PRK05850 79 ALQAGLIAVPLSVPQGGahDErVSAVLRDTSPS-----------------------VVLTTSAVVDDVTEYVAPQpgqsa 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 146 ------------VPREDIVALGERDLAAIL-YTSGTTGRSKGAMLTHKNLASNAKTLARAWH------FSADDRLIHALP 206
Cdd:PRK05850 136 ppvievdlldldSPRGSDARPRDLPSTAYLqYTSGSTRTPAGVMVSHRNVIANFEQLMSDYFgdtggvPPPDTTVVSWLP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 207 IFHTHGLFVACNVTLMAG-ASMLFLPkfdadVIFEELP-RGTVMMG--------VPTF----YTRLVQDERLTPEATANM 272
Cdd:PRK05850 216 FYHDMGLVLGVCAPILGGcPAVLTSP-----VAFLQRPaRWMQLLAsnphafsaAPNFafelAVRKTSDDDMAGLDLGGV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 273 RLFVSGSAPLTAETHEAFEAKTGH------AILERYGMTETNMNLSNPYDG-----------------ARR----AGT-- 323
Cdd:PRK05850 291 LGIISGSERVHPATLKRFADRFAPfnlretAIRPSYGLAEATVYVATREPGqppesvrfdyeklsaghAKRcetgGGTpl 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 324 --VGMPLPGVeMRITNRETGAEVPFGEIGMLQIRGPNVFIGYWRMPEKTRE----ELLD------DGFFI-TGDLAMVDE 390
Cdd:PRK05850 371 vsYGSPRSPT-VRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERtfgaTLVDpspgtpEGPWLrTGDLGFISE 449
|
490 500 510
....*....|....*....|....*....|...
gi 2136495511 391 qGYVHIVGRDKDLVISGGYNVYPKEVEQVIDEL 423
Cdd:PRK05850 450 -GELFIVGRIKDLLIVDGRNHYPDDIEATIQEI 481
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
415-495 |
4.20e-17 |
|
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: 75.66 E-value: 4.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 415 EVEQVIDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADlgenqLEEEKVITHLDGRLAKYKQPKRVFFVDELPRNTMG 494
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVE-----LLEEELVAHVREELGPYAVPKEVVFVDELPKTRSG 75
|
.
gi 2136495511 495 K 495
Cdd:pfam13193 76 K 76
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
162-512 |
1.38e-14 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 76.32 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 162 ILYTSGTTGRSKGAMLTHknlASNAKTLARAWHFSADDRLIHalpIFHTH-------------GLFVACNvTLMAGASML 228
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVRSN---GPHLVGLKYYWRSIIEKDIPT---VVFSHssigwvsfhgflyGSLSLGN-TFVMFEGGI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 229 FLPKFDADVIFEELPRGTVMMGV--PTFYTRLVQDErltPEAT--------ANMRLFVSGSAPLTAETHEAFEAKTGHAI 298
Cdd:PTZ00237 332 IKNKHIEDDLWNTIEKHKVTHTLtlPKTIRYLIKTD---PEATiirskydlSNLKEIWCGGEVIEESIPEYIENKLKIKS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 299 LERYGMTETNM-------NLSNPYDgarragTVGMPLPGVEMRITNrETGAEVPFGEIGMLQIR---GPNVFIGYWRMPE 368
Cdd:PTZ00237 409 SRGYGQTEIGItylycygHINIPYN------ATGVPSIFIKPSILS-EDGKELNVNEIGEVAFKlpmPPSFATTFYKNDE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 369 KTREeLLDD--GFFITGDLAMVDEQGYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQVAESAVIGLPHPDFGEGVTAV 446
Cdd:PTZ00237 482 KFKQ-LFSKfpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGL 560
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2136495511 447 VVRQQGAD---LGENQLEEE--KVITHldgRLAKYKQPKRVFFVDELPRNTMGKVQKNELRKRFNDT-YQTP 512
Cdd:PTZ00237 561 LVLKQDQSnqsIDLNKLKNEinNIITQ---DIESLAVLRKIIIVNQLPKTKTGKIPRQIISKFLNDSnYQLP 629
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
9-503 |
4.43e-13 |
|
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: 71.53 E-value: 4.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 9 FAAKMRERAEADF----ITTRDGRRYRYTDA--LTISAQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYL 82
Cdd:cd05943 72 YAENLLRHADADDpaaiYAAEDGERTEVTWAelRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 83 ---PlNTGYTGDEIRyfLNDAEPA-LFVC------------RPKIEE--QAL-SLAAETGCPAVVT-----LGSAADGSL 138
Cdd:cd05943 152 scsP-DFGVPGVLDR--FGQIEPKvLFAVdaytyngkrhdvREKVAElvKGLpSLLAVVVVPYTVAagqpdLSKIAKALT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 139 ME--TAQAAVPREDIVALGERDLAAILYTSGTTGRSK-------GAMLTHKnlasnaKTLARAWHFSADDRLihalpIFH 209
Cdd:cd05943 229 LEdfLATGAAGELEFEPLPFDHPLYILYSSGTTGLPKcivhgagGTLLQHL------KEHILHCDLRPGDRL-----FYY 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 210 T-----------HGLFVACNVTLMAGAsmLFLPKFDA--DVIFEElprGTVMMGVPTFYTRLVQDERLTPEATANM---R 273
Cdd:cd05943 298 TtcgwmmwnwlvSGLAVGATIVLYDGS--PFYPDTNAlwDLADEE---GITVFGTSAKYLDALEKAGLKPAETHDLsslR 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 274 LFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNMN----LSNPYDGARRaGTVGMPLPGVEMRITNrETGAEVPfGEI 349
Cdd:cd05943 373 TILSTGSPLKPESFDYVYDHIKPDVLLASISGGTDIIscfvGGNPLLPVYR-GEIQCRGLGMAVEAFD-EEGKPVW-GEK 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 350 GMLQIRG--PNVFIGYWRMPEKTREElldDGFFIT-------GDLAMVDEQGYVHIVGRdKDLVIS-GGYNVYPKEVEQV 419
Cdd:cd05943 450 GELVCTKpfPSMPVGFWNDPDGSRYR---AAYFAKypgvwahGDWIEITPRGGVVILGR-SDGTLNpGGVRIGTAEIYRV 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 420 IDELDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLgENQLeEEKVITHLDGRLAKYKQPKRVFFVDELPRNTMGKVQKN 499
Cdd:cd05943 526 VEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVEL-DDEL-RKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEV 603
|
....
gi 2136495511 500 ELRK 503
Cdd:cd05943 604 AVKK 607
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
159-404 |
5.10e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 65.12 E-value: 5.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 159 LAAILYTSGTTGRSKGAMLTHKNL---------ASNAKTLARAWHFSAddrlihaLPIFHTHGLFVAcNVTLMAGASMLF 229
Cdd:PTZ00342 306 ITSIVYTSGTSGKPKGVMLSNKNLyntvvplckHSIFKKYNPKTHLSY-------LPISHIYERVIA-YLSFMLGGTINI 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 230 LPK----FDADvIFEElpRGTVMMGVPTFYTRLVQD-----------------------------------ERLT----- 265
Cdd:PTZ00342 378 WSKdinyFSKD-IYNS--KGNILAGVPKVFNRIYTNimteinnlpplkrflvkkilslrksnnnggfskflEGIThissk 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 266 --PEATANMRLFVSGSAPLTAETHEAFEAKTGHAILERYGMTETNMNLSNPYDGARRAGTVGMPL-PGVEMRITNRET-- 340
Cdd:PTZ00342 455 ikDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTGPIFVQHADDNNTESIGGPIsPNTKYKVRTWETyk 534
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2136495511 341 -GAEVPFGEigmLQIRGPNVFIGYWRMPEKTREELLDDGFFITGDLAMVDEQGYVHIVGRDKDLV 404
Cdd:PTZ00342 535 aTDTLPKGE---LLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLV 596
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
145-438 |
6.33e-10 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 61.32 E-value: 6.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 145 AVPREDIValgerDLAAilyTSGTTGRSKGAMLTHKNLASNAKTLARAWH---FSADDRLIHALPifhtHGLFVA----- 216
Cdd:COG1541 79 AVPLEEIV-----RIHA---SSGTTGKPTVVGYTRKDLDRWAELFARSLRaagVRPGDRVQNAFG----YGLFTGglglh 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 217 -------CNVTLMAGASmlflPKFDADVIFEELPrgTVMMGVPTFYTRLV---QDERLTPEATaNMRLFVSGSAPLTAET 286
Cdd:COG1541 147 ygaerlgATVIPAGGGN----TERQLRLMQDFGP--TVLVGTPSYLLYLAevaEEEGIDPRDL-SLKKGIFGGEPWSEEM 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 287 HEAFEAKTGHAILERYGMTETNMNLSN--PYDGarragtvGMPLPG----VEmrITNRETGAEVPFGEIGMLqirgpnVF 360
Cdd:COG1541 220 RKEIEERWGIKAYDIYGLTEVGPGVAYecEAQD-------GLHIWEdhflVE--IIDPETGEPVPEGEEGEL------VV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 361 IGywrmpektreeLLDDGF----FITGDLAMVDEQ----GYVH-----IVGRDKDLVISGGYNVYPKEVEQVIDELDQVA 427
Cdd:COG1541 285 TT-----------LTKEAMplirYRTGDLTRLLPEpcpcGRTHprigrILGRADDMLIIRGVNVFPSQIEEVLLRIPEVG 353
|
330
....*....|.
gi 2136495511 428 ESAVIGLPHPD 438
Cdd:COG1541 354 PEYQIVVDREG 364
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
145-427 |
1.87e-06 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 50.32 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 145 AVPREDIVALGErdlaailyTSGTTGRSKGAMLTHKNLASNAKTLARAWhFSADDRLIHALPIFHTHGLFVA-------- 216
Cdd:cd05913 74 AVPREKVVRIHA--------SSGTTGKPTVVGYTKNDLDVWAELVARCL-DAAGVTPGDRVQNAYGYGLFTGglgfhyga 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 217 ----CNVTLMAGAS----MLFLPKFDAdvifeelprgTVMMGVPTFYTRL---VQDERLTPEATaNMRLFVSGSAPLTAE 285
Cdd:cd05913 145 erlgALVIPAGGGNterqLQLIKDFGP----------TVLCCTPSYALYLaeeAEEEGIDPREL-SLKVGIFGAEPWTEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 286 THEAFEAKTGHAILERYGMTETnMNLSNPYDGARRAGTVGMPlPGVEMRITNRETGAEVPFGEIGMLqirgpnVF--IGY 363
Cdd:cd05913 214 MRKRIERRLGIKAYDIYGLTEI-IGPGVAFECEEKDGLHIWE-DHFIPEIIDPETGEPVPPGEVGEL------VFttLTK 285
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2136495511 364 WRMPektreeLLddgFFITGDLA-MVDEQ---GYVH-----IVGRDKDLVISGGYNVYPKEVEQVIDELDQVA 427
Cdd:cd05913 286 EAMP------LI---RYRTRDITrLLPGPcpcGRTHrridrITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLG 349
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
26-497 |
3.55e-06 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 49.79 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 26 DGRRYRYT-DALTIS-AQLAGALTELGVKQGDRVAVQVDKSPEAILLYLACLRIGGVYlplnTGYTGDeiryFLNDA--- 100
Cdd:PRK03584 109 DGPRRELSwAELRRQvAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIW----SSCSPD----FGVQGvld 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 101 -----EP-ALFVC------------RPKIEE--QAL-SLAAetgcpAVVT--LGSAADGSLMEtaqAAVPREDIVALGEr 157
Cdd:PRK03584 181 rfgqiEPkVLIAVdgyryggkafdrRAKVAElrAALpSLEH-----VVVVpyLGPAAAAAALP---GALLWEDFLAPAE- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 158 dlAA--------------ILYTSGTTGRSK-------GAMLTHknlasnAKTLARAWHFSADDRLIhalpIFHTHG---- 212
Cdd:PRK03584 252 --AAelefepvpfdhplwILYSSGTTGLPKcivhghgGILLEH------LKELGLHCDLGPGDRFF----WYTTCGwmmw 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 213 -LFVAcnvTLMAGASML------FLPKFDA--DVIFEElprGTVMMGV-PTFYTrLVQDERLTPEATANMR----LFVSG 278
Cdd:PRK03584 320 nWLVS---GLLVGATLVlydgspFYPDPNVlwDLAAEE---GVTVFGTsAKYLD-ACEKAGLVPGETHDLSalrtIGSTG 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 279 SaPLTAET----HEAFEAKTGHAILEryGMTE--TNMNLSNPYDGARRaGTVGMPLPGVEMRITNrETGAEVpFGEIGML 352
Cdd:PRK03584 393 S-PLPPEGfdwvYEHVKADVWLASIS--GGTDicSCFVGGNPLLPVYR-GEIQCRGLGMAVEAWD-EDGRPV-VGEVGEL 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 353 QIRG--PNVFIGYWRMPEKTReelLDDGFFIT-------GDLAMVDEQGYVHIVGRdKDLVIS-GGYNVYPKEVEQVIDE 422
Cdd:PRK03584 467 VCTKpfPSMPLGFWNDPDGSR---YRDAYFDTfpgvwrhGDWIEITEHGGVVIYGR-SDATLNrGGVRIGTAEIYRQVEA 542
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2136495511 423 LDQVAESAVIGLPHPDFGEGVTAVVVRQQGADLGEnQLEEE--KVI-THLDGRLAkykqPKRVFFVDELPRNTMGKVQ 497
Cdd:PRK03584 543 LPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDD-ALRARirTTIrTNLSPRHV----PDKIIAVPDIPRTLSGKKV 615
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
392-505 |
1.47e-04 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 44.68 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136495511 392 GYVHIVGRDKDLVISGGYNVYPKEVEQVIDELDQ-VAESAVIGLPHPDFGEGVTAVVVRQQGADLGENQLEEEKVI--TH 468
Cdd:PLN03052 603 GYYRAHGRADDTMNLGGIKVSSVEIERVCNAADEsVLETAAIGVPPPGGGPEQLVIAAVLKDPPGSNPDLNELKKIfnSA 682
|
90 100 110
....*....|....*....|....*....|....*..
gi 2136495511 469 LDGRLAKYKQPKRVFFVDELPRNTMGKVQKNELRKRF 505
Cdd:PLN03052 683 IQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQQL 719
|
|
| |
