|
Name |
Accession |
Description |
Interval |
E-value |
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
7-501 |
1.01e-168 |
|
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: 483.65 E-value: 1.01e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 7 LQRAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFT 86
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 87 AAEASDVVENCTPRAFIggdgytgyarttpgfaaveafvalggpaagylgyEDLLarggtsrpphraaaadaaVLHFSSG 166
Cdd:cd17631 81 PPEVAYILADSGAKVLF----------------------------------DDLA------------------LLMYTSG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 167 STGRIKAAVQSYGNRMASLRKmlLGMDRQARPGDRLALIGPVTH--ASGMLMQPFLYCGATLVLFDRFEPAHFLAEVARL 244
Cdd:cd17631 109 TTGRPKGAMLTHRNLLWNAVN--ALAALDLGPDDVLLVVAPLFHigGLGVFTLPTLLRGGTVVILRKFDPETVLDLIERH 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 245 RITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMaPARIREAWERIGPILSQGYGASESTSGVTRLSTADHAEai 324
Cdd:cd17631 187 RVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPM-PERLLRALQARGVKFVQGYGMTETSPGVTFLSPEDHRR-- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 325 agrpgRLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDGWLRTGDLARVDEEGFIYL 404
Cdd:cd17631 264 -----KLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYI 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 405 VDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCRERIADYKTPRS 484
Cdd:cd17631 339 VDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKS 418
|
490
....*....|....*..
gi 1092251577 485 VEFVGELPKNPSGKVAR 501
Cdd:cd17631 419 VEFVDALPRNATGKILK 435
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
6-515 |
1.34e-167 |
|
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: 481.62 E-value: 1.34e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 6 FLQRAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRF 85
Cdd:COG0318 4 LLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 86 TAAEASDVVENCTPRAFIGgdgytgyarttpgfaaveafvalggpaagylgyedllarggtsrpphraaaadaAVLHFSS 165
Cdd:COG0318 84 TAEELAYILEDSGARALVT------------------------------------------------------ALILYTS 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 166 GSTGRIKAAVQSYGNRMASLRKMLLGMDrqARPGDRLALIGPVTHASGMLMQPF--LYCGATLVLFDRFEPAHFLAEVAR 243
Cdd:COG0318 110 GTTGRPKGVMLTHRNLLANAAAIAAALG--LTPGDVVLVALPLFHVFGLTVGLLapLLAGATLVLLPRFDPERVLELIER 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 244 LRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIREAWERIGPILSQGYGASESTSGVTrLSTADHAEA 323
Cdd:COG0318 188 ERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVT-VNPEDPGER 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 324 iagrpgRLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDGWLRTGDLARVDEEGFIY 403
Cdd:COG0318 267 ------RPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLY 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 404 LVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCRERIADYKTPR 483
Cdd:COG0318 341 IVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPR 420
|
490 500 510
....*....|....*....|....*....|..
gi 1092251577 484 SVEFVGELPKNPSGKVARKVVREPYWQGVARR 515
Cdd:COG0318 421 RVEFVDELPRTASGKIDRRALRERYAAGALEA 452
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
6-511 |
6.21e-142 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 418.82 E-value: 6.21e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 6 FLQRAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRF 85
Cdd:PRK06187 11 ILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 86 TAAEASDVVENCTPRAFIGGDGYTG-YARTTPGFAAVEAFVALGGPAAGYLG-----YEDLLARGGTSRPPHRAAAADAA 159
Cdd:PRK06187 91 KPEEIAYILNDAEDRVVLVDSEFVPlLAAILPQLPTVRTVIVEGDGPAAPLApevgeYEELLAAASDTFDFPDIDENDAA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 160 VLHFSSGSTGRIKAAV----QSYGNRMASLRKMLLgmdrqaRPGDRLALIGPV--THASGMLMQPFlYCGATLVLFDRFE 233
Cdd:PRK06187 171 AMLYTSGTTGHPKGVVlshrNLFLHSLAVCAWLKL------SRDDVYLVIVPMfhVHAWGLPYLAL-MAGAKQVIPRRFD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 234 PAHFLAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIREAWERIGPILSQGYGASESTSGVT 313
Cdd:PRK06187 244 PENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 314 RLSTADHAEAIAGRPGrlaSCGRPHGETEVRVVDEQGREVEGD--AIGEIVIRGEDVFQGYWGEPELTREVLVDGWLRTG 391
Cdd:PRK06187 324 VLPPEDQLPGQWTKRR---SAGRPLPGVEARIVDDDGDELPPDggEVGEIIVRGPWLMQGYWNRPEATAETIDGGWLHTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 392 DLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAH 471
Cdd:PRK06187 401 DVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAKELRAF 480
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1092251577 472 CRERIADYKTPRSVEFVGELPKNPSGKVARKVVREPYWQG 511
Cdd:PRK06187 481 LRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQYAEG 520
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
9-517 |
4.40e-140 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 414.00 E-value: 4.40e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 9 RAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAA 88
Cdd:PRK06188 20 SALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 89 EASDVVENCTPRAFIGGDG-YTGYART----TPGFAAVEAFvalgGPAAGYlgyEDLLARGGTSRP-PHRAAAADAAV-- 160
Cdd:PRK06188 100 DHAYVLEDAGISTLIVDPApFVERALAllarVPSLKHVLTL----GPVPDG---VDLLAAAAKFGPaPLVAAALPPDIag 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 161 LHFSSGSTGRIKAAVQSYGNrMASLRKMLLGmDRQARPGDRLALIGPVTHASGMLMQPFLYCGATLVLFDRFEPAHFLAE 240
Cdd:PRK06188 173 LAYTGGTTGKPKGVMGTHRS-IATMAQIQLA-EWEWPADPRFLMCTPLSHAGGAFFLPTLLRGGTVIVLAKFDPAEVLRA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 241 VARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIREAWERIGPILSQGYGASESTSGVTRLSTADH 320
Cdd:PRK06188 251 IEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDH 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 321 AeaiAGRPGRLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDGWLRTGDLARVDEEG 400
Cdd:PRK06188 331 D---PDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDGWLHTGDVAREDEDG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 401 FIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCRERIADYK 480
Cdd:PRK06188 408 FYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERKGSVH 487
|
490 500 510
....*....|....*....|....*....|....*..
gi 1092251577 481 TPRSVEFVGELPKNPSGKVARKVVREPYWQGVARRVN 517
Cdd:PRK06188 488 APKQVDFVDSLPLTALGKPDKKALRARYWEGRGRAVG 524
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
7-505 |
6.68e-136 |
|
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: 401.56 E-value: 6.68e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 7 LQRAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFT 86
Cdd:cd05936 5 LEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 87 AAEASDVVENCTPRAFIggdgytgyarttpgfaAVEAFvalggpaagylgyEDLLARGGTSRPPHRAAAADAAVLHFSSG 166
Cdd:cd05936 85 PRELEHILNDSGAKALI----------------VAVSF-------------TDLLAAGAPLGERVALTPEDVAVLQYTSG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 167 STGRIKAAVQSYGNRMASLRKMLLGMDRQARPGDRLALIGPVTHASGM---LMQPFlYCGATLVLFDRFEPAHFLAEVAR 243
Cdd:cd05936 136 TTGVPKGAMLTHRNLVANALQIKAWLEDLLEGDDVVLAALPLFHVFGLtvaLLLPL-ALGATIVLIPRFRPIGVLKEIRK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 244 LRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMaPARIREAWERI-GPILSQGYGASEsTSGVTRLSTADhae 322
Cdd:cd05936 215 HRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPL-PVEVAERFEELtGVPIVEGYGLTE-TSPVVAVNPLD--- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 323 aIAGRPGrlaSCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDGWLRTGDLARVDEEGFI 402
Cdd:cd05936 290 -GPRKPG---SIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYF 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 403 YLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCRERIADYKTP 482
Cdd:cd05936 366 FIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVP 445
|
490 500
....*....|....*....|...
gi 1092251577 483 RSVEFVGELPKNPSGKVARKVVR 505
Cdd:cd05936 446 RQVEFRDELPKSAVGKILRRELR 468
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
160-499 |
2.22e-129 |
|
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: 379.71 E-value: 2.22e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 160 VLHFSSGSTGRIKAAVQSYGNRMASLRKMLLgmDRQARPGDRLALIGPVTHASGM-LMQPFLYCGATLVLFDRFEPAHFL 238
Cdd:cd04433 4 LILYTSGTTGKPKGVVLSHRNLLAAAAALAA--SGGLTEGDVFLSTLPLFHIGGLfGLLGALLAGGTVVLLPKFDPEAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 239 AEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIREAWERIGPILSQGYGASESTSGVTRLSTA 318
Cdd:cd04433 82 ELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 319 DHAEaiagrpgRLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDGWLRTGDLARVDE 398
Cdd:cd04433 162 DDAR-------KPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 399 EGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCRERIAD 478
Cdd:cd04433 235 DGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAP 314
|
330 340
....*....|....*....|.
gi 1092251577 479 YKTPRSVEFVGELPKNPSGKV 499
Cdd:cd04433 315 YKVPRRVVFVDALPRTASGKI 335
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
7-506 |
1.01e-127 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 381.94 E-value: 1.01e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 7 LQRAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFT 86
Cdd:PRK07656 11 LARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 87 AAEASDVVENCTPRAFIGGDGYTGYARTTP-GFAAVEAFVALGGPAA-----GYLGYEDLLARGGTSRPPHRAAAADAAV 160
Cdd:PRK07656 91 ADEAAYILARGDAKALFVLGLFLGVDYSATtRLPALEHVVICETEEDdphteKMKTFTDFLAAGDPAERAPEVDPDDVAD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 161 LHFSSGSTGRIKAAVQSYGN--RMASLRKMLLGMdrqaRPGDRLALIGPVTHASGM---LMQPFLYcGATLVLFDRFEPA 235
Cdd:PRK07656 171 ILFTSGTTGRPKGAMLTHRQllSNAADWAEYLGL----TEGDRYLAANPFFHVFGYkagVNAPLMR-GATILPLPVFDPD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 236 HFLAEVARLRIThVFM-VPAMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIREAWERIG-PILSQGYGASEStSGVT 313
Cdd:PRK07656 246 EVFRLIETERIT-VLPgPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGvDIVLTGYGLSEA-SGVT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 314 RLSTADH-AEAIAGrpgrlaSCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVL-VDGWLRTG 391
Cdd:PRK07656 324 TFNRLDDdRKTVAG------TIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIdADGWLHTG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 392 DLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAH 471
Cdd:PRK07656 398 DLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEELIAY 477
|
490 500 510
....*....|....*....|....*....|....*
gi 1092251577 472 CRERIADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:PRK07656 478 CREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
1-506 |
1.64e-121 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 366.67 E-value: 1.64e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 1 MAFALFLQRAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAA 80
Cdd:PRK07470 7 MNLAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 81 LNPRFTAAEASDVVENCTPRAFIGGDGYTGYAR----TTPGFAAVeafVALGGPAAGyLGYEDLLARG-GTSRPPHRAAA 155
Cdd:PRK07470 87 TNFRQTPDEVAYLAEASGARAMICHADFPEHAAavraASPDLTHV---VAIGGARAG-LDYEALVARHlGARVANAAVDH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 156 ADAAVLHFSSGSTGRIKAAVQSYG-------NRMASLRkmllgmdrqarPG----DRLALIGPVTHASGM--LMQpfLYC 222
Cdd:PRK07470 163 DDPCWFFFTSGTTGRPKAAVLTHGqmafvitNHLADLM-----------PGtteqDASLVVAPLSHGAGIhqLCQ--VAR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 223 GATLVLF--DRFEPAHFLAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIREAWERIGPILS 300
Cdd:PRK07470 230 GAATVLLpsERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKVLV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 301 QGYGASESTSGVTRLSTADHAEAiAGRPGRLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTR 380
Cdd:PRK07470 310 QYFGLGEVTGNITVLPPALHDAE-DGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 381 EVLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPG 460
Cdd:PRK07470 389 KAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDG 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1092251577 461 RALEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:PRK07470 469 APVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
6-508 |
1.41e-112 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 343.45 E-value: 1.41e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 6 FLQRAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRF 85
Cdd:PRK08316 16 ILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFML 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 86 TAAEASDVVENCTPRAFIGGDGYTGYARTTPGFAAVEAFVAL-----GGPAAGYLGYEDLLARGGTSRPPHRAAAADAAV 160
Cdd:PRK08316 96 TGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSlvlggREAPGGWLDFADWAEAGSVAEPDVELADDDLAQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 161 LHFSSGSTGRIKAAVQSYGNRMASLRKMLLGMDrqARPGDRLALIGPVTHASGM--LMQPFLYCGATLVLFDRFEPAHFL 238
Cdd:PRK08316 176 ILYTSGTESLPKGAMLTHRALIAEYVSCIVAGD--MSADDIPLHALPLYHCAQLdvFLGPYLYVGATNVILDAPDPELIL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 239 AEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIREAWERIGPI-LSQGYGASESTSGVTRLST 317
Cdd:PRK08316 254 RTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERLPGLrFYNCYGQTEIAPLATVLGP 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 318 ADHAEaiagrpgRLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDGWLRTGDLARVD 397
Cdd:PRK08316 334 EEHLR-------RPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMD 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 398 EEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCRERIA 477
Cdd:PRK08316 407 EEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLA 486
|
490 500 510
....*....|....*....|....*....|.
gi 1092251577 478 DYKTPRSVEFVGELPKNPSGKVARKVVREPY 508
Cdd:PRK08316 487 GFKVPKRVIFVDELPRNPSGKILKRELRERY 517
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
25-516 |
4.20e-108 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 331.10 E-value: 4.20e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 25 RVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVENCTPRAFIG 104
Cdd:PRK08276 10 EVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 105 ----GDGYTGYARTTPgfAAVEAFVALGGPAAGYLGYEDLLARGGTSRPPHRAAAAdaaVLHFSSGSTGRIK----AAVQ 176
Cdd:PRK08276 90 saalADTAAELAAELP--AGVPLLLVVAGPVPGFRSYEEALAAQPDTPIADETAGA---DMLYSSGTTGRPKgikrPLPG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 177 SYGNRMASLRKMLLGMDRQARPGDRLALIGPVTHASgmlmqPFLYC------GATLVLFDRFEPAHFLAEVARLRITHVF 250
Cdd:PRK08276 165 LDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTA-----PLRFGmsalalGGTVVVMEKFDAEEALALIERYRVTHSQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 251 MVPAMIHMLLADPALEQA--DLSSLKTLSYGAAPMAPARIREAWERIGPILSQGYGASEStSGVTRLSTADHAEaiagRP 328
Cdd:PRK08276 240 LVPTMFVRMLKLPEEVRAryDVSSLRVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSEG-GGVTVITSEDWLA----HP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 329 GrlaSCGRPhGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVD-GWLRTGDLARVDEEGFIYLVDR 407
Cdd:PRK08276 315 G---SVGKA-VLGEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPhGWVTVGDVGYLDEDGYLYLTDR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 408 KKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPG---RALEAAALIAHCRERIADYKTPRS 484
Cdd:PRK08276 391 KSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGadaGDALAAELIAWLRGRLAHYKCPRS 470
|
490 500 510
....*....|....*....|....*....|..
gi 1092251577 485 VEFVGELPKNPSGKVARKVVREPYWQGVARRV 516
Cdd:PRK08276 471 IDFEDELPRTPTGKLYKRRLRDRYWEGRQRAI 502
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
25-499 |
4.98e-106 |
|
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: 325.32 E-value: 4.98e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 25 RVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVENCTPRAFIG 104
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 105 -GDGYTGYARTTPGFAAVEAFVALGGPAAGYLGYEDLL-ARGGTS---RPPHRAAAADAAV-LHFSSGSTGRIKAAVQSY 178
Cdd:cd05911 89 dPDGLEKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLsPTLGEEdedLPPPLKDGKDDTAaILYSSGTTGLPKGVCLSH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 179 GNRMASLRKMLLGMDRQARPGDRLALIGPVTHASGMLMQPF-LYCGATLVLFDRFEPAHFLAEVARLRITHVFMVPAMIH 257
Cdd:cd05911 169 RNLIANLSQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLAsLLNGATVIIMPKFDSELFLDLIEKYKITFLYLVPPIAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 258 MLLADPALEQADLSSLKTLSYGAAPMApARIREAWERIGP--ILSQGYGASESTSGVTRLSTADHaeaiagRPGrlaSCG 335
Cdd:cd05911 249 ALAKSPLLDKYDLSSLRVILSGGAPLS-KELQELLAKRFPnaTIKQGYGMTETGGILTVNPDGDD------KPG---SVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 336 RPHGETEVRVVDEQGREVEG-DAIGEIVIRGEDVFQGYWGEPELTREVLV-DGWLRTGDLARVDEEGFIYLVDRKKDMII 413
Cdd:cd05911 319 RLLPNVEAKIVDDDGKDSLGpNEPGEICVRGPQVMKGYYNNPEATKETFDeDGWLHTGDIGYFDEDGYLYIVDRKKELIK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 414 SGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCRERIADYKTPRS-VEFVGELP 492
Cdd:cd05911 399 YKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYKQLRGgVVFVDEIP 478
|
....*..
gi 1092251577 493 KNPSGKV 499
Cdd:cd05911 479 KSASGKI 485
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
7-514 |
5.72e-97 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 303.81 E-value: 5.72e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 7 LQRAARYWGDRPAVMHRERVLSFRQLDERSTRLANA-LLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRF 85
Cdd:PRK08314 16 LEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYlQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 86 TAAEASDVVENCTPR-AFIGGD--------------------GYTGYARTTPGFAaVEAFVALGGPA-----AGYLGYED 139
Cdd:PRK08314 96 REEELAHYVTDSGARvAIVGSElapkvapavgnlrlrhvivaQYSDYLPAEPEIA-VPAWLRAEPPLqalapGGVVAWKE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 140 LLARGGTSrPPHRAAAADAAVLHFSSGSTGRIKAAVQSYGNRMASLrkMLLGMDRQARPGDRLALIGPVTHASGML--MQ 217
Cdd:PRK08314 175 ALAAGLAP-PPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANA--VGSVLWSNSTPESVVLAVLPLFHVTGMVhsMN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 218 PFLYCGATLVLFDRFEPAHFLAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIREAWERIGP 297
Cdd:PRK08314 252 APIYAGATVVLMPRWDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMPEAVAERLKELTGL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 298 ILSQGYGASEsTSGVTRLSTADHAeaiagrpgRLASCGRPHGETEVRVVD-EQGREVEGDAIGEIVIRGEDVFQGYWGEP 376
Cdd:PRK08314 332 DYVEGYGLTE-TMAQTHSNPPDRP--------KLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFKGYWNRP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 377 ELTREVLV--DG--WLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVK 452
Cdd:PRK08314 403 EATAEAFIeiDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVK 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092251577 453 AVVALRPGRALEAAA--LIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVREPYWQGVAR 514
Cdd:PRK08314 483 AVVVLRPEARGKTTEeeIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKARAAK 546
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
4-501 |
1.17e-95 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 299.08 E-value: 1.17e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 4 ALFLQRAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGL-GLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALN 82
Cdd:PRK06839 5 AYWIEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 83 PRFTAAEASDVVENCTPRAFIGGDGYTGYARTTPGFAAVEAFVALGGPAAGYLGYEDLLARGGTSRPphraaaadaAVLH 162
Cdd:PRK06839 85 IRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVISITSLKEIEDRKIDNFVEKNESAS---------FIIC 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 163 FSSGSTGRIKAAVQSYGNRMASLRKMLLGMDRQARpgDRLALIGPVTHASG--MLMQPFLYCGATLVLFDRFEPAHFLAE 240
Cdd:PRK06839 156 YTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMH--DRSIVLLPLFHIGGigLFAFPTLFAGGVIIVPRKFEPTKALSM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 241 VARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIREAWERiGPILSQGYGASESTSGVTRLSTADH 320
Cdd:PRK06839 234 IEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETSPTVFMLSEEDA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 321 AEaiagRPGrlaSCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDGWLRTGDLARVDEEG 400
Cdd:PRK06839 313 RR----KVG---SIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 401 FIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCRERIADYK 480
Cdd:PRK06839 386 FVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYK 465
|
490 500
....*....|....*....|.
gi 1092251577 481 TPRSVEFVGELPKNPSGKVAR 501
Cdd:PRK06839 466 IPKEIVFLKELPKNATGKIQK 486
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
6-506 |
1.31e-94 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 298.18 E-value: 1.31e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 6 FLQRAARYWGDRPAVMHR-----ERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAA 80
Cdd:COG0365 14 CLDRHAEGRGDKVALIWEgedgeERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 81 LNPRFTAAEASDVVENCTPRAFIGGDGYTGYARTTPGFAAVEAFVAL---------------GGPAAGYLGYEDLLARGG 145
Cdd:COG0365 94 VFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEElpslehvivvgrtgaDVPMEGDLDWDELLAAAS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 146 TSRPPHRAAAADAAVLHFSSGSTGRIKAAVQSYGNRMASLRK-MLLGMDrqARPGDRL---ALIGPVTHASGMLMQPfLY 221
Cdd:COG0365 174 AEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATtAKYVLD--LKPGDVFwctADIGWATGHSYIVYGP-LL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 222 CGATLVLFDR----FEPAHFLAEVARLRITHVFMVPAMIHMLLA--DPALEQADLSSLKTLSYGAAPMAPARIREAWERI 295
Cdd:COG0365 251 NGATVVLYEGrpdfPDPGRLWELIEKYGVTVFFTAPTAIRALMKagDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 296 G-PILSqGYGASESTSGVtrlstadhaeaIAGRPG---RLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGED--VF 369
Cdd:COG0365 331 GvPIVD-GWGQTETGGIF-----------ISNLPGlpvKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPWpgMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 370 QGYWGEPELTREVLVD---GWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDAT 446
Cdd:COG0365 399 RGYWNDPERYRETYFGrfpGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEI 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092251577 447 WGESVKAVVALRPGRALE---AAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:COG0365 479 RGQVVKAFVVLKPGVEPSdelAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRK 541
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
7-508 |
1.85e-94 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 297.46 E-value: 1.85e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 7 LQRAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFT 86
Cdd:PRK07786 23 LARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 87 AAEASDVVENCTPRAFIGGDGYTGYA----RTTPGFAAVeaFVALGGPAAGYLGYEDLLARGGTSRPPHRAAAADAAVLH 162
Cdd:PRK07786 103 PPEIAFLVSDCGAHVVVTEAALAPVAtavrDIVPLLSTV--VVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 163 FSSGSTGRIKAAVQSYGNRMASLRKMLLGMdrQARPGDRLALIG-PVTHASGM-LMQPFLYCGATLVLF--DRFEPAHFL 238
Cdd:PRK07786 181 YTSGTTGRPKGAVLTHANLTGQAMTCLRTN--GADINSDVGFVGvPLFHIAGIgSMLPGLLLGAPTVIYplGAFDPGQLL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 239 AEVARLRITHVFMVPAMIHMLLADPALEQADLSsLKTLSYGAAPMAPARIREAWERI-GPILSQGYGASEsTSGVTRLST 317
Cdd:PRK07786 259 DVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLA-LRVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTE-MSPVTCMLL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 318 ADhaEAIAgrpgRLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDGWLRTGDLARVD 397
Cdd:PRK07786 337 GE--DAIR----KLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQD 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 398 EEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRA-LEAAALIAHCRERI 476
Cdd:PRK07786 411 EEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAaLTLEDLAEFLTDRL 490
|
490 500 510
....*....|....*....|....*....|..
gi 1092251577 477 ADYKTPRSVEFVGELPKNPSGKVARKVVREPY 508
Cdd:PRK07786 491 ARYKHPKALEIVDALPRNPAGKVLKTELRERY 522
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
7-415 |
8.69e-91 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 283.82 E-value: 8.69e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 7 LQRAARYWGDRPAVMHRE-RVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRF 85
Cdd:pfam00501 1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 86 TAAEASDVVENCTPRAFIGGDGYTGY----ARTTPGFAAVEAFVALGGPAAGYLGYEDLLARGGTSRPPHRAAAADAAVL 161
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKLEelleALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 162 HFSSGSTGRIKAAVQSYGNRMASLR--KMLLGMDRQARPGDRLALIGPVTHASGMLMQPF--LYCGATLVLFDRFE---P 234
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLsiKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLgpLLAGATVVLPPGFPaldP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 235 AHFLAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIREAWERIGPILSQGYGASESTSGVTR 314
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 315 LSTADHAEAIAGrpgrlaSCGRPHGETEVRVVDEQ-GREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLV-DGWLRTGD 392
Cdd:pfam00501 321 PLPLDEDLRSLG------SVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDeDGWYRTGD 394
|
410 420
....*....|....*....|...
gi 1092251577 393 LARVDEEGFIYLVDRKKDMIISG 415
Cdd:pfam00501 395 LGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
28-505 |
1.04e-89 |
|
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: 281.10 E-value: 1.04e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 28 SFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVENCTPRAfiggdg 107
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQL------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 108 ytgyarttpgfaaveafvALGGPAAgylgyedllarggtsrpphraaaadaavLHFSSGSTGRIKAAVQSYGNRMASLRK 187
Cdd:cd05934 79 ------------------VVVDPAS----------------------------ILYTSGTTGPPKGVVITHANLTFAGYY 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 188 MLLGMDrqARPGDRLALIGPVTHASGMLMQ--PFLYCGATLVLFDRFEPAHFLAEVARLRITHVFMVPAMIHMLLADPAL 265
Cdd:cd05934 113 SARRFG--LGEDDVYLTVLPLFHINAQAVSvlAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPS 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 266 EQADLSSLKTLsyGAAPMAPARIREAWERIGPILSQGYGASESTSGVtrLSTADHAeaiaGRPGrlaSCGRPHGETEVRV 345
Cdd:cd05934 191 PDDRAHRLRAA--YGAPNPPELHEEFEERFGVRLLEGYGMTETIVGV--IGPRDEP----RRPG---SIGRPAPGYEVRI 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 346 VDEQGREVEGDAIGEIVIRGED---VFQGYWGEPELTREVLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPT 422
Cdd:cd05934 260 VDDDGQELPAGEPGELVIRGLRgwgFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSA 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 423 EVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARK 502
Cdd:cd05934 340 EVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKA 419
|
...
gi 1092251577 503 VVR 505
Cdd:cd05934 420 QLR 422
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
16-512 |
1.98e-89 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 283.51 E-value: 1.98e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 16 DRPAV-MHRER-VLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDV 93
Cdd:PRK13391 12 DKPAViMASTGeVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 94 VENCTPRAFIGGDGYTGYARTTPGFA-AVEAFVALGGPAA--GYLGYEDLLARGGTSRPPHRAAAADaavLHFSSGSTGR 170
Cdd:PRK13391 92 VDDSGARALITSAAKLDVARALLKQCpGVRHRLVLDGDGEleGFVGYAEAVAGLPATPIADESLGTD---MLYSSGTTGR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 171 ---IKAAVQSYGNRMASLRKMLLGMDRQARPGDRLALIGPVTHA----SGMLMQPFlycGATLVLFDRFEPAHFLAEVAR 243
Cdd:PRK13391 169 pkgIKRPLPEQPPDTPLPLTAFLQRLWGFRSDMVYLSPAPLYHSapqrAVMLVIRL---GGTVIVMEHFDAEQYLALIEE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 244 LRITHVFMVPAM-IHML-LADPALEQADLSSLKTLSYGAAPmAPARIREA----WeriGPILSQGYGASEStSGVTRLST 317
Cdd:PRK13391 246 YGVTHTQLVPTMfSRMLkLPEEVRDKYDLSSLEVAIHAAAP-CPPQVKEQmidwW---GPIIHEYYAATEG-LGFTACDS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 318 AdhaEAIAgRPGrlaSCGRP-HGEteVRVVDEQGREVEGDAIGEIVIRGEDVFQgYWGEPELTREVLVD--GWLRTGDLA 394
Cdd:PRK13391 321 E---EWLA-HPG---TVGRAmFGD--LHILDDDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPdgTWSTVGDIG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 395 RVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALE---AAALIAH 471
Cdd:PRK13391 391 YVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGpalAAELIAF 470
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1092251577 472 CRERIADYKTPRSVEFVGELPKNPSGKVARKVVREPYWQGV 512
Cdd:PRK13391 471 CRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDRYWGNK 511
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
7-506 |
2.02e-88 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 282.66 E-value: 2.02e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 7 LQRAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFT 86
Cdd:PRK05605 38 YDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 87 AAEASDVVENCTPRAFIGGDGYTGYARTTPGFAAVEAFV----------------------------ALGGPAAGYLGYE 138
Cdd:PRK05605 118 AHELEHPFEDHGARVAIVWDKVAPTVERLRRTTPLETIVsvnmiaampllqrlalrlpipalrkaraALTGPAPGTVPWE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 139 DLLARG----GTSRPPHRAAAADAAVLHFSSGSTGRIKAAVQSYGNRMASLRKMLLGMDRQARPGDRLALIGPVTHASGM 214
Cdd:PRK05605 198 TLVDAAiggdGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPGLGDGPERVLAALPMFHAYGL 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 215 LMQPFL--YCGATLVLFDRFEPAHFLAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMaPARIREAW 292
Cdd:PRK05605 278 TLCLTLavSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGAMAL-PVSTVELW 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 293 E-RIGPILSQGYGASESTSGVTRLSTADHAeaiagRPGrlaSCGRPHGETEVRVVDEQ--GREVEGDAIGEIVIRGEDVF 369
Cdd:PRK05605 357 EkLTGGLLVEGYGLTETSPIIVGNPMSDDR-----RPG---YVGVPFPDTEVRIVDPEdpDETMPDGEEGELLVRGPQVF 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 370 QGYWGEPELTREVLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGE 449
Cdd:PRK05605 429 KGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSE 508
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1092251577 450 SVKAVVALRPGRALEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:PRK05605 509 EVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
5-506 |
6.10e-88 |
|
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: 278.80 E-value: 6.10e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 5 LFLQRAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPR 84
Cdd:cd12118 8 SFLERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 85 FTAAEASDVVENCTPRAFIggdgytgyarTTPGFAaveafvalggpaagylgYEDLLARGGTSRPPHRAAAADAAV-LHF 163
Cdd:cd12118 88 LDAEEIAFILRHSEAKVLF----------VDREFE-----------------YEDLLAEGDPDFEWIPPADEWDPIaLNY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 164 SSGSTGRIKAAVqsYGNRMASLRKMLLGMDRQARPGDRLALIGPVTHASGmlmqpflYC--------GATLVLFDRFEPA 235
Cdd:cd12118 141 TSGTTGRPKGVV--YHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNG-------WCfpwtvaavGGTNVCLRKVDAK 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 236 HFLAEVARLRITHVFMVPAMIHMLLADPALEQADLS-SLKTLSYGAAPmaPARIREAWERIGPILSQGYGASESTSGVT- 313
Cdd:cd12118 212 AIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPhRVHVMTAGAPP--PAAVLAKMEELGFDVTHVYGLTETYGPATv 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 314 --------RLSTADHAEAIAgRPGRlascgRPHGETEVRVVDEQG-REVEGDA--IGEIVIRGEDVFQGYWGEPELTREV 382
Cdd:cd12118 290 cawkpewdELPTEERARLKA-RQGV-----RYVGLEEVDVLDPETmKPVPRDGktIGEIVFRGNIVMKGYLKNPEATAEA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 383 LVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRA 462
Cdd:cd12118 364 FRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAK 443
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1092251577 463 LEAAALIAHCRERIADYKTPRSVEFvGELPKNPSGKVARKVVRE 506
Cdd:cd12118 444 VTEEEIIAFCREHLAGFMVPKTVVF-GELPKTSTGKIQKFVLRD 486
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
11-508 |
7.49e-88 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 278.69 E-value: 7.49e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 11 ARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEA 90
Cdd:PRK06145 12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 91 SDVVENCTPRAFIGGDGYtgyarttpgfaavEAFVALGGPAA--GYLGYEDL--LARGGTSRPPHRAAAADAAV-LHFSS 165
Cdd:PRK06145 92 AYILGDAGAKLLLVDEEF-------------DAIVALETPKIviDAAAQADSrrLAQGGLEIPPQAAVAPTDLVrLMYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 166 GSTGRIKAAVQSYGN-RMASLRKML-LGMDRQarpgDRLALIGPVTHAsGMLMQP---FLYCGATLVLFDRFEPAHFLAE 240
Cdd:PRK06145 159 GTTDRPKGVMHSYGNlHWKSIDHVIaLGLTAS----ERLLVVGPLYHV-GAFDLPgiaVLWVGGTLRIHREFDPEAVLAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 241 VARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIREAWERI-GPILSQGYGASESTSGVTRLSTAD 319
Cdd:PRK06145 234 IERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFtRARYIDAYGLTETCSGDTLMEAGR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 320 HAEAIAgrpgrlaSCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDGWLRTGDLARVDEE 399
Cdd:PRK06145 314 EIEKIG-------STGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 400 GFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCRERIADY 479
Cdd:PRK06145 387 GFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASF 466
|
490 500
....*....|....*....|....*....
gi 1092251577 480 KTPRSVEFVGELPKNPSGKVARKVVREPY 508
Cdd:PRK06145 467 KVPRQLKVRDELPRNPSGKVLKRVLRDEL 495
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
27-502 |
2.67e-87 |
|
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: 274.61 E-value: 2.67e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 27 LSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVENctprafiggd 106
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKD---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 107 gytgyarttpgfAAVeafvalggpaagylGYEDLlarggtsrpphraaaadaAVLHFSSGSTGRIKAAVQSYGNRMASLR 186
Cdd:cd05912 72 ------------SDV--------------KLDDI------------------ATIMYTSGTTGKPKGVQQTFGNHWWSAI 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 187 --KMLLGMDRQarpgDRLALIGPVTHASGM--LMQPFLYcGATLVLFDRFEPAHFLAEVARLRITHVFMVPAMIHMLLAD 262
Cdd:cd05912 108 gsALNLGLTED----DNWLCALPLFHISGLsiLMRSVIY-GMTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRLLEI 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 263 paLEQADLSSLKTLSYGAAPMAPARIREAWERIGPILsQGYGASESTSGVTRLSTADHAEaiagrpgRLASCGRPHGETE 342
Cdd:cd05912 183 --LGEGYPNNLRCILLGGGPAPKPLLEQCKEKGIPVY-QSYGMTETCSQIVTLSPEDALN-------KIGSAGKPLFPVE 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 343 VRVVDEQGREVEgdaIGEIVIRGEDVFQGYWGEPELTREVLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPT 422
Cdd:cd05912 253 LKIEDDGQPPYE---VGEILLKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPA 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 423 EVEAVLYQHPDVMEACVISVPDATWGE-SVKAVVALRPgraLEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVAR 501
Cdd:cd05912 330 EIEEVLLSHPAIKEAGVVGIPDDKWGQvPVAFVVSERP---ISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLR 406
|
.
gi 1092251577 502 K 502
Cdd:cd05912 407 H 407
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
24-516 |
7.00e-87 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 276.58 E-value: 7.00e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 24 ERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVENCTPRAFI 103
Cdd:PRK12406 9 DRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 104 G-GDGYTGYARTTPgfAAVEAFV---------------ALGGPAAGYLGYEDLLArggTSRPPHRAAAADAAVLHFSSGS 167
Cdd:PRK12406 89 AhADLLHGLASALP--AGVTVLSvptppeiaaayrispALLTPPAGAIDWEGWLA---QQEPYDGPPVPQPQSMIYTSGT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 168 TGRIK-----------AAVQsygnrmASLRKMLLGMdrqaRPGDRLALIGPVTHASgmlmqPFLY------CGATLVLFD 230
Cdd:PRK12406 164 TGHPKgvrraaptpeqAAAA------EQMRALIYGL----KPGIRALLTGPLYHSA-----PNAYglragrLGGVLVLQP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 231 RFEPAHFLAEVARLRITHVFMVPAMIHMLLADPALEQA--DLSSLKTLSYGAAPmAPARIREA----WeriGPILSQGYG 304
Cdd:PRK12406 229 RFDPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAkyDVSSLRHVIHAAAP-CPADVKRAmiewW---GPVIYEYYG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 305 ASEStsGVTRLSTADHAEAiagRPGrlaSCGRPHGETEVRVVDEQGREVEGDAIGEIVIR--GEDVFQgYWGEPELTREV 382
Cdd:PRK12406 305 STES--GAVTFATSEDALS---HPG---TVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRiaGNPDFT-YHNKPEKRAEI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 383 LVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRA 462
Cdd:PRK12406 376 DRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGAT 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1092251577 463 LEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVREPYWQGVARRV 516
Cdd:PRK12406 456 LDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPYWANAGRKI 509
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
26-506 |
1.16e-85 |
|
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: 273.03 E-value: 1.16e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 26 VLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASD-VVENCTPRAFIG 104
Cdd:cd05926 14 ALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFyLADLGSKLVLTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 105 GDGYTGYARTTPGF------AAVEAFVALGGPAAGYLGYEDLLARGGTSRPPHRAAAADAaVLHfSSGSTGRIKAAVQSY 178
Cdd:cd05926 94 KGELGPASRAASKLglaileLALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLPDDLAL-ILH-TSGTTGRPKGVPLTH 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 179 GNRMASLRKMLLGMdrQARPGDRLALIGPVTHASGML--MQPFLYCGATLVLFDRFEPAHFLAEVARLRITHVFMVPAMI 256
Cdd:cd05926 172 RNLAASATNITNTY--KLTPDDRTLVVMPLFHVHGLVasLLSTLAAGGSVVLPPRFSASTFWPDVRDYNATWYTAVPTIH 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 257 HMLLADP-ALEQADLSSLKTLSYGAAPMAPARIREAWERIG-PILsQGYGASESTSGVT--RLSTADHaeaiagRPGrla 332
Cdd:cd05926 250 QILLNRPePNPESPPPKLRFIRSCSASLPPAVLEALEATFGaPVL-EAYGMTEAAHQMTsnPLPPGPR------KPG--- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 333 SCGRPHGeTEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREV-LVDGWLRTGDLARVDEEGFIYLVDRKKDM 411
Cdd:cd05926 320 SVGKPVG-VEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAaFKDGWFRTGDLGYLDADGYLFLTGRIKEL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 412 IISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCRERIADYKTPRSVEFVGEL 491
Cdd:cd05926 399 INRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHLAAFKVPKKVYFVDEL 478
|
490
....*....|....*
gi 1092251577 492 PKNPSGKVARKVVRE 506
Cdd:cd05926 479 PKTATGKIQRRKVAE 493
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
3-506 |
2.16e-84 |
|
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: 270.86 E-value: 2.16e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 3 FALFLQRAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALN 82
Cdd:COG1021 27 LGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVFAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 83 PRFTAAEASDVVENCTPRAFIGGDGYTGY-----ART-TPGFAAVEAFVALGgPAAGYLGYEDLLARGGTSRPPhRAAAA 156
Cdd:COG1021 107 PAHRRAEISHFAEQSEAVAYIIPDRHRGFdyralARElQAEVPSLRHVLVVG-DAGEFTSLDALLAAPADLSEP-RPDPD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 157 DAAVLHFSSGSTGRIKAAVQSYGNRMASLRKM--LLGMDrqarPGDRLALIGPVTH----AS-GMLmqPFLYCGATLVLF 229
Cdd:COG1021 185 DVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASaeICGLD----ADTVYLAALPAAHnfplSSpGVL--GVLYAGGTVVLA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 230 DRFEPAHFLAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMAP---ARIREAWeriGPILSQGYGAS 306
Cdd:COG1021 259 PDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPelaRRVRPAL---GCTLQQVFGMA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 307 ESTSGVTRLstaDHAEAIagrpgRLASCGRPHGET-EVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVL-V 384
Cdd:COG1021 336 EGLVNYTRL---DDPEEV-----ILTTQGRPISPDdEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFtP 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 385 DGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRpGRALE 464
Cdd:COG1021 408 DGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPR-GEPLT 486
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1092251577 465 AAALIAHCRER-IADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:COG1021 487 LAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRA 529
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
169-501 |
5.90e-84 |
|
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: 263.36 E-value: 5.90e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 169 GRIKAAVQSYGNRMASLRKMLLGMdrQARPGDRLALIGPVTHASGM-LMQPFLYCGATLVLFDRFEPAHFLAEVARLRIT 247
Cdd:cd17637 13 GRPRGAVLSHGNLIAANLQLIHAM--GLTEADVYLNMLPLFHIAGLnLALATFHAGGANVVMEKFDPAEALELIEEEKVT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 248 HVFMVPAMIHMLLADPALEQADLSSLKTLSyGAApmAPARIrEAWERIGPilSQ---GYGASEsTSGVTRLSTADHAEAI 324
Cdd:cd17637 91 LMGSFPPILSNLLDAAEKSGVDLSSLRHVL-GLD--APETI-QRFEETTG--ATfwsLYGQTE-TSGLVTLSPYRERPGS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 325 AGRPGRLAscgrphgetEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDGWLRTGDLARVDEEGFIYL 404
Cdd:cd17637 164 AGRPGPLV---------RVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 405 VDRK--KDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCRERIADYKTP 482
Cdd:cd17637 235 AGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFVGSRIARYKKP 314
|
330
....*....|....*....
gi 1092251577 483 RSVEFVGELPKNPSGKVAR 501
Cdd:cd17637 315 RYVVFVEALPKTADGSIDR 333
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
11-506 |
4.73e-83 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 265.90 E-value: 4.73e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 11 ARYWGDRPAV--MHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAA 88
Cdd:PRK09088 5 ARLQPQRLAAvdLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 89 EASDVVENCTPRAFIGGDGYTGyARTTPgfaaveafVALGGPAAGYLGYEDLLARggtSRPPHRAAaadaaVLHFSSGST 168
Cdd:PRK09088 85 ELDALLQDAEPRLLLGDDAVAA-GRTDV--------EDLAAFIASADALEPADTP---SIPPERVS-----LILFTSGTS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 169 GRIKAAVQSYGNrmasLRKMLLGMDRQARPGDRLALI--GPVTHASGML--MQPFLYCGATLVLFDRFEPAHFLAEVA-- 242
Cdd:PRK09088 148 GQPKGVMLSERN----LQQTAHNFGVLGRVDAHSSFLcdAPMFHIIGLItsVRPVLAVGGSILVSNGFEPKRTLGRLGdp 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 243 RLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIReAWERIGPILSQGYGASESTsgvTRLSTADHAE 322
Cdd:PRK09088 224 ALGITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEDIL-GWLDDGIPMVDGFGMSEAG---TVFGMSVDCD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 323 AIAGRPGrlaSCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLV-DGWLRTGDLARVDEEGF 401
Cdd:PRK09088 300 VIRAKAG---AAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTgDGWFRTGDIARRDADGF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 402 IYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCRERIADYKT 481
Cdd:PRK09088 377 FWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKV 456
|
490 500
....*....|....*....|....*
gi 1092251577 482 PRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:PRK09088 457 PKHLRLVDALPRTASGKLQKARLRD 481
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
28-504 |
5.36e-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: 261.61 E-value: 5.36e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 28 SFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVENcTPRAFIggdg 107
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLED-LDVQLL---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 108 ytgyarTTPGFAAVEAFVALGGPAAGYLGYED--LLARGGTSRPphraaaadaAVLHFSSGSTGRIKAAVQSYGNRMASL 185
Cdd:TIGR01923 76 ------LTDSLLEEKDFQADSLDRIEAAGRYEtsLSASFNMDQI---------ATLMFTSGTTGKPKAVPHTFRNHYASA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 186 R--KMLLGMDrqarPGDRLALIGPVTHASG--MLMQpFLYCGATLVLFDRFepAHFLAEVARLRITHVFMVPAMIHMLLa 261
Cdd:TIGR01923 141 VgsKENLGFT----EDDNWLLSLPLYHISGlsILFR-WLIEGATLRIVDKF--NQLLEMIANERVTHISLVPTQLNRLL- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 262 dpaleQADLS--SLKTLSYGAAPMAPARIREAWERIGPILsQGYGASESTSGVTRLST-ADHAEAIAGRPgrLASCgrph 338
Cdd:TIGR01923 213 -----DEGGHneNLRKILLGGSAIPAPLIEEAQQYGLPIY-LSYGMTETCSQVTTATPeMLHARPDVGRP--LAGR---- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 339 gETEVRVVDEQGrevegdaIGEIVIRGEDVFQGYWGEPELTREVLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFN 418
Cdd:TIGR01923 281 -EIKIKVDNKEG-------HGEIMVKGANLMKGYLYQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGEN 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 419 VYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRpgRALEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGK 498
Cdd:TIGR01923 353 IYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSE--SDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGK 430
|
....*.
gi 1092251577 499 VARKVV 504
Cdd:TIGR01923 431 ILRNQL 436
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
7-502 |
5.85e-82 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 262.98 E-value: 5.85e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 7 LQRAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFT 86
Cdd:PRK03640 8 LKQRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 87 AAEASDVVENCTPRAFIGGDGYTgyARTTPG-FAAVEAFVALGGPAAGYLGYEDLlarggtsrpphraaaADAAVLHFSS 165
Cdd:PRK03640 88 REELLWQLDDAEVKCLITDDDFE--AKLIPGiSVKFAELMNGPKEEAEIQEEFDL---------------DEVATIMYTS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 166 GSTGRIKAAVQSYGNRMASLRKMLLGMDRQARpgDR-LALIgPVTHASGM--LMQPFLYcGATLVLFDRFEPAHFLAEVA 242
Cdd:PRK03640 151 GTTGKPKGVIQTYGNHWWSAVGSALNLGLTED--DCwLAAV-PIFHISGLsiLMRSVIY-GMRVVLVEKFDAEKINKLLQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 243 RLRITHVFMVPAMIHMLLADpaLEQADL-SSLKTLSYGAAPMAPARIREAWERIGPILsQGYGASESTSGVTRLSTADHA 321
Cdd:PRK03640 227 TGGVTIISVVSTMLQRLLER--LGEGTYpSSFRCMLLGGGPAPKPLLEQCKEKGIPVY-QSYGMTETASQIVTLSPEDAL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 322 EaiagrpgRLASCGRPHGETEVRVVDeQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDGWLRTGDLARVDEEGF 401
Cdd:PRK03640 304 T-------KLGSAGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWFKTGDIGYLDEEGF 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 402 IYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALrpGRALEAAALIAHCRERIADYKT 481
Cdd:PRK03640 376 LYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVTEEELRHFCEEKLAKYKV 453
|
490 500
....*....|....*....|.
gi 1092251577 482 PRSVEFVGELPKNPSGKVARK 502
Cdd:PRK03640 454 PKRFYFVEELPRNASGKLLRH 474
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
26-506 |
8.77e-81 |
|
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: 258.46 E-value: 8.77e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 26 VLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVENCTPRAFIGG 105
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 106 DGYTGYArttpgFAAVEAFVALggpaagylgyedllarggtsrpphraaaadaavLHFSSGSTGRIKAAVQSYGNRMASL 185
Cdd:cd05903 81 ERFRQFD-----PAAMPDAVAL---------------------------------LLFTSGTTGEPKGVMHSHNTLSASI 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 186 RKMLLGMdrQARPGDRLALIGPVTHASGML---MQPFLYcGATLVLFDRFEPAHFLAEVARLRITHVFMVPAMIHMLLAD 262
Cdd:cd05903 123 RQYAERL--GLGPGDVFLVASPMAHQTGFVygfTLPLLL-GAPVVLQDIWDPDKALALMREHGVTFMMGATPFLTDLLNA 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 263 PALEQADLSSLKTLSYGAAPMAPARIREAWERIGPILSQGYGASESTSGVTRLSTADhaeaiAGRpgRLASCGRPHGETE 342
Cdd:cd05903 200 VEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAP-----EDR--RLYTDGRPLPGVE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 343 VRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPT 422
Cdd:cd05903 273 IKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 423 EVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHC-RERIADYKTPRSVEFVGELPKNPSGKVAR 501
Cdd:cd05903 353 EVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKVQK 432
|
....*
gi 1092251577 502 KVVRE 506
Cdd:cd05903 433 FRLRE 437
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
6-506 |
9.81e-81 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 262.05 E-value: 9.81e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 6 FLQRAARYWGDRPAV--MHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNP 83
Cdd:PRK08315 21 LLDRTAARYPDREALvyRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 84 RFTAAEASDVVENCTPRAFIGGDGY--TGY-----------ARTTPGFAAVEAFVAL-------GGPAAGYLGYEDLLAR 143
Cdd:PRK08315 101 AYRLSELEYALNQSGCKALIAADGFkdSDYvamlyelapelATCEPGQLQSARLPELrrviflgDEKHPGMLNFDELLAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 144 GgTSRPPHRAAAADAAV-------LHFSSGSTGRIKAAVQSYGN-----RMASlRKMLLGmdrqarPGDRLALIGPVTHA 211
Cdd:PRK08315 181 G-RAVDDAELAARQATLdpddpinIQYTSGTTGFPKGATLTHRNilnngYFIG-EAMKLT------EEDRLCIPVPLYHC 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 212 SGMLMQpFLYC---GATLVLF-DRFEPAHFLAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTlsyGAapMA--- 284
Cdd:PRK08315 253 FGMVLG-NLACvthGATMVYPgEGFDPLATLAAVEEERCTALYGVPTMFIAELDHPDFARFDLSSLRT---GI--MAgsp 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 285 -PARI-REAWERIGpiLSQ---GYGASESTSGVTRLSTADHAEAiagrpgRLASCGRPHGETEVRVVD-EQGREVEGDAI 358
Cdd:PRK08315 327 cPIEVmKRVIDKMH--MSEvtiAYGMTETSPVSTQTRTDDPLEK------RVTTVGRALPHLEVKIVDpETGETVPRGEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 359 GEIVIRGEDVFQGYWGEPELTREVL-VDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEA 437
Cdd:PRK08315 399 GELCTRGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDV 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092251577 438 CVISVPDATWGESVKAVVALRPGRALEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:PRK08315 479 QVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMRE 547
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
3-508 |
5.81e-80 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 258.27 E-value: 5.81e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 3 FALFLQRAARywGDRPAVM-HRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAAL 81
Cdd:PRK07514 6 FDALRAAFAD--RDAPFIEtPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 82 NPRFTAAEASDVVENCTPRAFIGGDGYTGYARTTPGFAAVEAFVALGGPAAGYLgyEDLLARGGTSRPPHRAAAADAAVL 161
Cdd:PRK07514 84 NTAYTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAAGAPHVETLDADGTGSL--LEAAAAAPDDFETVPRGADDLAAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 162 HFSSGSTGRIKAAVQSYGNrMASLRKMLlgmdRQA---RPGDRL--ALigPVTHASGMlmqpF------LYCGATLVLFD 230
Cdd:PRK07514 162 LYTSGTTGRSKGAMLSHGN-LLSNALTL----VDYwrfTPDDVLihAL--PIFHTHGL----FvatnvaLLAGASMIFLP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 231 RFEPAHFLAEVARlriTHVFM-VPAMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIREAWERIG-PILSQgYGASEs 308
Cdd:PRK07514 231 KFDPDAVLALMPR---ATVMMgVPTFYTRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGhAILER-YGMTE- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 309 tsgvTRLSTAD--HAEAIAGrpgrlaSCGRPHGETEVRVVD-EQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVL-V 384
Cdd:PRK07514 306 ----TNMNTSNpyDGERRAG------TVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFrA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 385 DGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALE 464
Cdd:PRK07514 376 DGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALD 455
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1092251577 465 AAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVREPY 508
Cdd:PRK07514 456 EAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQY 499
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
7-506 |
7.39e-80 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 259.70 E-value: 7.39e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 7 LQRAARYWGDRPAVMHRERVL--SFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPR 84
Cdd:PRK12583 24 FDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 85 FTAAEASDVVENCTPRAFIGGDGYT-------------GYARTTPGFAAVEAF------VALGG-PAAGYLGYEDLLARG 144
Cdd:PRK12583 104 YRASELEYALGQSGVRWVICADAFKtsdyhamlqellpGLAEGQPGALACERLpelrgvVSLAPaPPPGFLAWHELQARG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 145 GTSRPPHRAAAADAAV------LHFSSGSTGRIKAAVQSYGN-----RMASLRkmlLGMDRQarpgDRLALIGPVTHASG 213
Cdd:PRK12583 184 ETVSREALAERQASLDrddpinIQYTSGTTGFPKGATLSHHNilnngYFVAES---LGLTEH----DRLCVPVPLYHCFG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 214 MLMQPfLYC---GATLVL-FDRFEPAHFLAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIR 289
Cdd:PRK12583 257 MVLAN-LGCmtvGACLVYpNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 290 EAWERIG-PILSQGYGASEsTSGVTRLSTADHAeaiagRPGRLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDV 368
Cdd:PRK12583 336 RVMDEMHmAEVQIAYGMTE-TSPVSLQTTAADD-----LERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSV 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 369 FQGYWGEPELTREVL-VDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATW 447
Cdd:PRK12583 410 MKGYWNNPEATAESIdEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKY 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1092251577 448 GESVKAVVALRPGRALEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:PRK12583 490 GEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMRE 548
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
10-502 |
1.28e-79 |
|
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: 257.55 E-value: 1.28e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 10 AARYWGDRPAVMHRE--RVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTA 87
Cdd:cd05904 14 FASAHPSRPALIDAAtgRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 88 AEASDVVENCTPR-AFIGGDgytgYARTTPGFAAveAFVALGGPAAGYLGYEDLLAR-GGTSRPPHRAAAADAAVLHFSS 165
Cdd:cd05904 94 AEIAKQVKDSGAKlAFTTAE----LAEKLASLAL--PVVLLDSAEFDSLSFSDLLFEaDEAEPPVVVIKQDDVAALLYSS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 166 GSTGRIKAAVQSYGNRMASLRKMLLGMDRQARPGDRLALIGPVTHASGM--LMQPFLYCGATLVLFDRFEPAHFLAEVAR 243
Cdd:cd05904 168 GTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSEDVFLCVLPMFHIYGLssFALGLLRLGATVVVMPRFDLEELLAAIER 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 244 LRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIREAWERI-GPILSQGYGASESTSGVTRLSTADHAe 322
Cdd:cd05904 248 YKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFpNVDLGQGYGMTESTGVVAMCFAPEKD- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 323 aiagrPGRLASCGRPHGETEVRVVD-EQGREVEGDAIGEIVIRGEDVFQGYWGEPELTRE-VLVDGWLRTGDLARVDEEG 400
Cdd:cd05904 327 -----RAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAAtIDKEGWLHTGDLCYIDEDG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 401 FIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCRERIADYK 480
Cdd:cd05904 402 YLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQVAPYK 481
|
490 500
....*....|....*....|..
gi 1092251577 481 TPRSVEFVGELPKNPSGKVARK 502
Cdd:cd05904 482 KVRKVAFVDAIPKSPSGKILRK 503
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
163-505 |
2.57e-78 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 249.12 E-value: 2.57e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 163 FSSGSTGRIKAAVQSYGNRMASLRkmLLGMDRQARPGDRLALIGPVTHASGMLMQpFLYC---GATLVLFDR-FEPAHFL 238
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGY--FIGERLGLTEQDRLCIPVPLFHCFGSVLG-VLAClthGATMVFPSPsFDPLAVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 239 AEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIREAWERIG-PILSQGYGASESTSGVTRLST 317
Cdd:cd05917 86 EAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNmKDVTIAYGMTETSPVSTQTRT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 318 ADHAEAiagrpgRLASCGRPHGETEVRVVDEQGREVEG-DAIGEIVIRGEDVFQGYWGEPELTREVL-VDGWLRTGDLAR 395
Cdd:cd05917 166 DDSIEK------RVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKTAEAIdGDGWLHTGDLAV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 396 VDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCRER 475
Cdd:cd05917 240 MDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKAYCKGK 319
|
330 340 350
....*....|....*....|....*....|
gi 1092251577 476 IADYKTPRSVEFVGELPKNPSGKVARKVVR 505
Cdd:cd05917 320 IAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
11-505 |
1.14e-77 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 252.62 E-value: 1.14e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 11 ARYWGDRPAVMHRE--RVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAA 88
Cdd:PRK13390 7 AQIAPDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 89 EASDVVENCTPRAFIGGDGYTGYARTTPGfaAVEAFVALGGPAAGYLGYEDLLARGGtsrpPHRAAAADAAVLHFSSGST 168
Cdd:PRK13390 87 EADYIVGDSGARVLVASAALDGLAAKVGA--DLPLRLSFGGEIDGFGSFEAALAGAG----PRLTEQPCGAVMLYSSGTT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 169 GRIKA--------AVQSYGNRMASLRKMLLGMDRQarpgDRLALIGPVTHASgmlmqPFLYC------GATLVLFDRFEP 234
Cdd:PRK13390 161 GFPKGiqpdlpgrDVDAPGDPIVAIARAFYDISES----DIYYSSAPIYHAA-----PLRWCsmvhalGGTVVLAKRFDA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 235 AHFLAEVARLRITHVFMVPAM-IHML-LADPALEQADLSSLKTLSYGAAPmAPARIREA---WerIGPILSQGYGASESt 309
Cdd:PRK13390 232 QATLGHVERYRITVTQMVPTMfVRLLkLDADVRTRYDVSSLRAVIHAAAP-CPVDVKHAmidW--LGPIVYEYYSSTEA- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 310 SGVTRLSTADHAeAIAGRPGRlASCGRPHgetevrVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDG--- 386
Cdd:PRK13390 308 HGMTFIDSPDWL-AHPGSVGR-SVLGDLH------ICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAhpf 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 387 WLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVAL----RPGRA 462
Cdd:PRK13390 380 WTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLvegiRGSDE 459
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1092251577 463 LeAAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVR 505
Cdd:PRK13390 460 L-ARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
10-506 |
4.62e-77 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 252.16 E-value: 4.62e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 10 AARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAE 89
Cdd:PRK07788 58 AARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 90 ASDVVENCTPRAFIGGDGYTGYARTTPgfAAVEAFVALGG-------PAAGYLGYEDLLARGGTSRPPHRAAAADAAVLh 162
Cdd:PRK07788 138 LAEVAAREGVKALVYDDEFTDLLSALP--PDLGRLRAWGGnpdddepSGSTDETLDDLIAGSSTAPLPKPPKPGGIVIL- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 163 fSSGSTGRIKAAVQSYGNRMASLRKMLlgmDRQA-RPGDRLALIGPVTHASGMLM-QPFLYCGATLVLFDRFEPAHFLAE 240
Cdd:PRK07788 215 -TSGTTGTPKGAPRPEPSPLAPLAGLL---SRVPfRAGETTLLPAPMFHATGWAHlTLAMALGSTVVLRRRFDPEATLED 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 241 VARLRITHVFMVPAMIHMLLADP--ALEQADLSSLKTLSYGAAPMAPARIREAWERIGPILSQGYGASEsTSGVTRLSTA 318
Cdd:PRK07788 291 IAKHKATALVVVPVMLSRILDLGpeVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTE-VAFATIATPE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 319 DHAEA--IAGRPgrlascgrPHGeTEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPEltrEVLVDGWLRTGDLARV 396
Cdd:PRK07788 370 DLAEApgTVGRP--------PKG-VTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGRD---KQIIDGLLSSGDVGYF 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 397 DEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCRERI 476
Cdd:PRK07788 438 DEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNL 517
|
490 500 510
....*....|....*....|....*....|
gi 1092251577 477 ADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:PRK07788 518 ARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
168-499 |
5.44e-77 |
|
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: 245.29 E-value: 5.44e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 168 TGRIKAAVQSYGNRMAslRKMLLGMDRQARPGDRLALIGPVTH-ASGMLMQPFLYCGATLVLFDRFEPAHFLAEVARLRI 246
Cdd:cd17636 12 SGRPNGALLSHQALLA--QALVLAVLQAIDEGTVFLNSGPLFHiGTLMFTLATFHAGGTNVFVRRVDAEEVLELIEAERC 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 247 THVFMVPAMIHMLLADPALEQADLSSLKTLSY--GAAPMAPARiREAWERIGPilsqGYGASESTSGVTRLSTADHAEAI 324
Cdd:cd17636 90 THAFLLPPTIDQIVELNADGLYDLSSLRSSPAapEWNDMATVD-TSPWGRKPG----GYGQTEVMGLATFAALGGGAIGG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 325 AGRPGRLAScgrphgeteVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDGWLRTGDLARVDEEGFIYL 404
Cdd:cd17636 165 AGRPSPLVQ---------VRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRGGWHHTNDLGRREPDGSLSF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 405 VDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCRERIADYKTPRS 484
Cdd:cd17636 236 VGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARIASYKKPKS 315
|
330
....*....|....*
gi 1092251577 485 VEFVGELPKNPSGKV 499
Cdd:cd17636 316 VEFADALPRTAGGAD 330
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
163-501 |
7.05e-77 |
|
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: 244.72 E-value: 7.05e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 163 FSSGSTGRIKaavqsyGNRMASLRKMLL----GMDRQARPGDRLALIGPVTHASGMlMQPFLYC---GATLVLFDRFEPA 235
Cdd:cd17638 7 FTSGTTGRSK------GVMCAHRQTLRAaaawADCADLTEDDRYLIINPFFHTFGY-KAGIVAClltGATVVPVAVFDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 236 HFLAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIREAWERIG-PILSQGYGASESTSgVTR 314
Cdd:cd17638 80 AILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGfETVLTAYGLTEAGV-ATM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 315 LSTADHAEAIAgrpgrlASCGRPHGETEVRVVDEqgrevegdaiGEIVIRGEDVFQGYWGEPELTREVL-VDGWLRTGDL 393
Cdd:cd17638 159 CRPGDDAETVA------TTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIdADGWLHTGDV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 394 ARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCR 473
Cdd:cd17638 223 GELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCR 302
|
330 340
....*....|....*....|....*...
gi 1092251577 474 ERIADYKTPRSVEFVGELPKNPSGKVAR 501
Cdd:cd17638 303 ERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
16-506 |
2.03e-76 |
|
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: 248.45 E-value: 2.03e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 16 DRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVE 95
Cdd:cd05929 7 DRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEACAIIE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 96 NCTPrafiggdgytgyarttpgfAAVEAFVALGGPAAGYLGYEDllARGGTSRPPHRAAAADAAVLhFSSGSTGRIKAAV 175
Cdd:cd05929 87 IKAA-------------------ALVCGLFTGGGALDGLEDYEA--AEGGSPETPIEDEAAGWKML-YSGGTTGRPKGIK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 176 QSYGNRM--ASLRKMLLGMDrQARPGDRLALIGPVTHASgmlmqPFLYC------GATLVLFDRFEPAHFLAEVARLRIT 247
Cdd:cd05929 145 RGLPGGPpdNDTLMAAALGF-GPGADSVYLSPAPLYHAA-----PFRWSmtalfmGGTLVLMEKFDPEEFLRLIERYRVT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 248 HVFMVPAMIHMLLADPALEQA--DLSSLKTLSYGAAPMaPARIREAW-ERIGPILSQGYGASEStSGVTRLSTADHAEai 324
Cdd:cd05929 219 FAQFVPTMFVRLLKLPEAVRNayDLSSLKRVIHAAAPC-PPWVKEQWiDWGGPIIWEYYGGTEG-QGLTIINGEEWLT-- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 325 agRPGrlaSCGRPhGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQgYWGEPELTRE-VLVDGWLRTGDLARVDEEGFIY 403
Cdd:cd05929 295 --HPG---SVGRA-VLGKVHILDEDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAaRNEGGWSTLGDVGYLDEDGYLY 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 404 LVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVV----ALRPGRALeAAALIAHCRERIADY 479
Cdd:cd05929 368 LTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVqpapGADAGTAL-AEELIAFLRDRLSRY 446
|
490 500
....*....|....*....|....*..
gi 1092251577 480 KTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:cd05929 447 KCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
160-504 |
2.42e-76 |
|
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: 246.62 E-value: 2.42e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 160 VLHFSSGSTGRIKAAVQSYGNRMASLrkMLLGMDRQARPGDRLALIGPVTHASGM--LMQPFLYCGATLVLFDRFEPAHF 237
Cdd:cd05935 88 LIPYTSGTTGLPKGCMHTHFSAAANA--LQSAVWTGLTPSDVILACLPLFHVTGFvgSLNTAVYVGGTYVLMARWDRETA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 238 LAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIREAWERIGPILSQGYGASESTSGVTrlsT 317
Cdd:cd05935 166 LELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTH---T 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 318 ADHaeaiaGRPgRLASCGRPHGETEVRVVD-EQGREVEGDAIGEIVIRGEDVFQGYWGEPELTRE--VLVDG--WLRTGD 392
Cdd:cd05935 243 NPP-----LRP-KLQCLGIP*FGVDARVIDiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEEsfIEIKGrrFFRTGD 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 393 LARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAA--LIA 470
Cdd:cd05935 317 LGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEedIIE 396
|
330 340 350
....*....|....*....|....*....|....
gi 1092251577 471 HCRERIADYKTPRSVEFVGELPKNPSGKVARKVV 504
Cdd:cd05935 397 WAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
16-506 |
2.33e-75 |
|
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: 244.51 E-value: 2.33e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 16 DRPAVMHRERVLSFRQLDERSTRLANA-LLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVV 94
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRlLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 95 ENCTPRAFIGGdgytgyarttpgfaaveafvalggpaagylgyedllarggtsrpphraaaadaAVLHFSSGSTGRIKAA 174
Cdd:cd05941 81 TDSEPSLVLDP-----------------------------------------------------ALILYTSGTTGRPKGV 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 175 VQSYGNRMASLRkmLLGMDRQARPGDRLALIGPVTHASGM---LMQPfLYCGATLVLFDRFEPAHFLAEVARLRIThVFM 251
Cdd:cd05941 108 VLTHANLAANVR--ALVDAWRWTEDDVLLHVLPLHHVHGLvnaLLCP-LFAGASVEFLPKFDPKEVAISRLMPSIT-VFM 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 252 -VPAMIHMLLADPALEQAD--------LSSLKTLSYGAAPMaPARIREAWERI-GPILSQGYGASEStsGVTrLSTADHA 321
Cdd:cd05941 184 gVPTIYTRLLQYYEAHFTDpqfaraaaAERLRLMVSGSAAL-PVPTLEEWEAItGHTLLERYGMTEI--GMA-LSNPLDG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 322 EAIAGrpgrlaSCGRPHGETEVRVVDEQ-GREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLV-DGWLRTGDLARVDEE 399
Cdd:cd05941 260 ERRPG------TVGMPLPGVQARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTdDGWFKTGDLGVVDED 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 400 GFIYLVDRKKDMII-SGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGR-ALEAAALIAHCRERIA 477
Cdd:cd05941 334 GYYWILGRSSVDIIkSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAaALSLEELKEWAKQRLA 413
|
490 500
....*....|....*....|....*....
gi 1092251577 478 DYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:cd05941 414 PYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
5-506 |
1.12e-74 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 246.12 E-value: 1.12e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 5 LFLQRAARYwGDRPAVMHRERVLSFRQLDERStRLANALLGLGLR--PGDRVAVQSRNcaeLVEIECALY---KSGLVKA 79
Cdd:PRK08974 28 MFEQAVARY-ADQPAFINMGEVMTFRKLEERS-RAFAAYLQNGLGlkKGDRVALMMPN---LLQYPIALFgilRAGMIVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 80 ALNPRFT----------------------AAEASDVVENCTPRAFI---GGDGYTGYARTTPGFAA--VEAFVA---Lgg 129
Cdd:PRK08974 103 NVNPLYTprelehqlndsgakaivivsnfAHTLEKVVFKTPVKHVIltrMGDQLSTAKGTLVNFVVkyIKRLVPkyhL-- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 130 PAAgyLGYEDLLARGGTS---RPphRAAAADAAVLHFSSGSTGRIKAAVQSYGNRMASLRKMLLGMDRQARPGDRLALIG 206
Cdd:PRK08974 181 PDA--ISFRSALHKGRRMqyvKP--ELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGPLLHPGKELVVTA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 207 -PVTHASGMLMQP--FLYCGATLVLFD--RFEPAhFLAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKtLSYGAA 281
Cdd:PRK08974 257 lPLYHIFALTVNCllFIELGGQNLLITnpRDIPG-FVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLK-LSVGGG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 282 pMAPAR-IREAWERI-GPILSQGYGASEStsgvtrlstadhAEAIAGRPGRLA----SCGRPHGETEVRVVDEQGREVEG 355
Cdd:PRK08974 335 -MAVQQaVAERWVKLtGQYLLEGYGLTEC------------SPLVSVNPYDLDyysgSIGLPVPSTEIKLVDDDGNEVPP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 356 DAIGEIVIRGEDVFQGYWGEPELTREVLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVM 435
Cdd:PRK08974 402 GEPGELWVKGPQVMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVL 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092251577 436 EACVISVPDATWGESVKAVVaLRPGRALEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:PRK08974 482 EVAAVGVPSEVSGEAVKIFV-VKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
15-498 |
1.35e-74 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 245.18 E-value: 1.35e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 15 GDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVV 94
Cdd:PRK07798 17 PDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 95 ENCTPRAFIGGDGYTG-YARTTPGFAAVEAFVALG-GPAAGYLG----YEDLLARGGTSRPPHRAAAADAAVLhFSSGST 168
Cdd:PRK07798 97 DDSDAVALVYEREFAPrVAEVLPRLPKLRTLVVVEdGSGNDLLPgavdYEDALAAGSPERDFGERSPDDLYLL-YTGGTT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 169 GRIKAAVQSYGN-RMASL--RKMLLG-----MDRQAR-----PGDRLALIGPVTHASGML--MQPFLyCGATLVLFD--R 231
Cdd:PRK07798 176 GMPKGVMWRQEDiFRVLLggRDFATGepiedEEELAKraaagPGMRRFPAPPLMHGAGQWaaFAALF-SGQTVVLLPdvR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 232 FEPAHFLAEVARLRITHVFMV-PAMIHMLLAdpALEQA---DLSSLKTLSYGAAPMAPArIREAWERIGP--ILSQGYGA 305
Cdd:PRK07798 255 FDADEVWRTIEREKVNVITIVgDAMARPLLD--ALEARgpyDLSSLFAIASGGALFSPS-VKEALLELLPnvVLTDSIGS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 306 SESTSGVTrLSTADHAEAIAGRPGRLAScgrphgetEVRVVDEQGREVE-GDAIGEIVIRGEDVFQGYWGEPELTREVL- 383
Cdd:PRK07798 332 SETGFGGS-GTVAKGAVHTGGPRFTIGP--------RTVVLDEDGNPVEpGSGEIGWIARRGHIPLGYYKDPEKTAETFp 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 384 -VDG--WLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPG 460
Cdd:PRK07798 403 tIDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREG 482
|
490 500 510
....*....|....*....|....*....|....*...
gi 1092251577 461 RALEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGK 498
Cdd:PRK07798 483 ARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
6-506 |
1.91e-74 |
|
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: 244.46 E-value: 1.91e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 6 FLQRAARYWGDRPAV----MHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAAL 81
Cdd:cd12119 1 LLEHAARLHGDREIVsrthEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 82 NPR-------FTAAEASDVVenctprAFIGGDGYTGYARTTPGFAAVEAFVALGGPAA-------GYLGYEDLLARGGTS 147
Cdd:cd12119 81 NPRlfpeqiaYIINHAEDRV------VFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAmpepagvGVLAYEELLAAESPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 148 RPPHRAAAADAAVLHFSSGSTGRIKAAVqsYGNR------MASLRKMLLGMdrqaRPGDRLALIGPVTHAS--GMlmqPF 219
Cdd:cd12119 155 YDWPDFDENTAAAICYTSGTTGNPKGVV--YSHRslvlhaMAALLTDGLGL----SESDVVLPVVPMFHVNawGL---PY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 220 --LYCGATLVLFDRF-EPAHFLAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIReAWERIG 296
Cdd:cd12119 226 aaAMVGAKLVLPGPYlDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIE-AFEERG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 297 PILSQGYGASEsTSG---VTRLSTADHAEAIAGRPGRLASCGRPHGETEVRVVDEQGREVE--GDAIGEIVIRGEDVFQG 371
Cdd:cd12119 305 VRVIHAWGMTE-TSPlgtVARPPSEHSNLSEDEQLALRAKQGRPVPGVELRIVDDDGRELPwdGKAVGELQVRGPWVTKS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 372 YWGEPELTREVLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESV 451
Cdd:cd12119 384 YYKNDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERP 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1092251577 452 KAVVALRPGRALEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:cd12119 464 LAVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
6-506 |
3.80e-73 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 241.77 E-value: 3.80e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 6 FLQRAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRF 85
Cdd:PRK08162 23 FLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 86 TAAEASDVVENCTPRAFIGGDGYTGYAR--------TTPGFAAVEAFVALGGPAAGYLGYEDLLARGGTSRPPHRAAAAD 157
Cdd:PRK08162 103 DAASIAFMLRHGEAKVLIVDTEFAEVARealallpgPKPLVIDVDDPEYPGGRFIGALDYEAFLASGDPDFAWTLPADEW 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 158 AAV-LHFSSGSTGRIKAAVqsYGNRMASLRKM----LLGMDRqarpgdrlaligpvtHASGMLMQPFLYC---------- 222
Cdd:PRK08162 183 DAIaLNYTSGTTGNPKGVV--YHHRGAYLNALsnilAWGMPK---------------HPVYLWTLPMFHCngwcfpwtva 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 223 --GATLVLFDRFEPAHFLAEVARLRITHVFMVPAMIHMLLADPALEQADLS-SLKTLSYGAAPmaPARIREAWERIGPIL 299
Cdd:PRK08162 246 arAGTNVCLRKVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDhPVHAMVAGAAP--PAAVIAKMEEIGFDL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 300 SQGYGASES---------TSGVTRLSTADHAeAIAGRPGRlascgRPHGETEVRVVD-EQGREV--EGDAIGEIVIRGED 367
Cdd:PRK08162 324 THVYGLTETygpatvcawQPEWDALPLDERA-QLKARQGV-----RYPLQEGVTVLDpDTMQPVpaDGETIGEIMFRGNI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 368 VFQGYWGEPELTREVLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATW 447
Cdd:PRK08162 398 VMKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKW 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1092251577 448 GESVKAVVALRPGRALEAAALIAHCRERIADYKTPRSVEFvGELPKNPSGKVARKVVRE 506
Cdd:PRK08162 478 GEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLRE 535
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
17-505 |
8.18e-73 |
|
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: 237.75 E-value: 8.18e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 17 RPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVEN 96
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 97 CTPRAFIggdgytgyarttpgfaaveafvaLGGPAAGYLGYedllarggtsrpphraaaadaavlhfSSGSTGRIKAAVQ 176
Cdd:cd05919 81 CEARLVV-----------------------TSADDIAYLLY--------------------------SSGTTGPPKGVMH 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 177 SYGNRMASLRKM---LLGMdrqaRPGDRLALIGPVTHASGM---LMQPfLYCGATLVLFD-RFEPAHFLAEVARLRITHV 249
Cdd:cd05919 112 AHRDPLLFADAMareALGL----TPGDRVFSSAKMFFGYGLgnsLWFP-LAVGASAVLNPgWPTAERVLATLARFRPTVL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 250 FMVPAMIHMLLADPALEQADLSSLKtLSYGAAPMAPARIREAW-ERIGPILSQGYGASEStsGVTRLSTadhaeaiagRP 328
Cdd:cd05919 187 YGVPTFYANLLDSCAGSPDALRSLR-LCVSAGEALPRGLGERWmEHFGGPILDGIGATEV--GHIFLSN---------RP 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 329 G--RLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDGWLRTGDLARVDEEGFIYLVD 406
Cdd:cd05919 255 GawRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 407 RKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALE---AAALIAHCRERIADYKTPR 483
Cdd:cd05919 335 RADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQeslARDIHRHLLERLSAHKVPR 414
|
490 500
....*....|....*....|..
gi 1092251577 484 SVEFVGELPKNPSGKVARKVVR 505
Cdd:cd05919 415 RIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
11-506 |
2.93e-72 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 239.26 E-value: 2.93e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 11 ARYWGDRPAVM-HRERVL-------SFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALN 82
Cdd:PRK06087 26 ADYWQQTARAMpDKIAVVdnhgasyTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 83 PRFTAAEASDVVENCTPRAFIGGdgyTGYARTTPGFAAVE-----------AFVALGGPAAGYLGYEDLLARGGT-SRPP 150
Cdd:PRK06087 106 PSWREAELVWVLNKCQAKMFFAP---TLFKQTRPVDLILPlqnqlpqlqqiVGVDKLAPATSSLSLSQIIADYEPlTTAI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 151 HRAAAADAAVLhFSSGSTGRIKAAVQSYGNRMASLRKMLLGMDRQARpgDRLALIGPVTHASGM---LMQPFLyCGATLV 227
Cdd:PRK06087 183 TTHGDELAAVL-FTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQ--DVFMMPAPLGHATGFlhgVTAPFL-IGARSV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 228 LFDRFEPAHFLAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIREAWERiGPILSQGYGASE 307
Cdd:PRK06087 259 LLDIFTPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 308 STSgvtrlstadHAEAIAGRPGRL--ASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVL-V 384
Cdd:PRK06087 338 SSP---------HAVVNLDDPLSRfmHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALdE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 385 DGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALR-PGRAL 463
Cdd:PRK06087 409 EGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKaPHHSL 488
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1092251577 464 EAAALIAH-CRERIADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:PRK06087 489 TLEEVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
6-503 |
3.25e-69 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 231.85 E-value: 3.25e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 6 FLQRAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRF 85
Cdd:PRK06178 38 YLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 86 TAAEASDVVENCTPRAFIGGDGY------------------TGYARTTPGFAAVEAFVALGGPAAGYLGYEDLLA--RGG 145
Cdd:PRK06178 118 REHELSYELNDAGAEVLLALDQLapvveqvraetslrhvivTSLADVLPAEPTLPLPDSLRAPRLAAAGAIDLLPalRAC 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 146 TSRPP-HRAAAADAAVLHFSSGSTGRIKAAVQSYGN---RMASLRKMLLGMDRQAR----------PGDRLALIGPvtha 211
Cdd:PRK06178 198 TAPVPlPPPALDALAALNYTGGTTGMPKGCEHTQRDmvyTAAAAYAVAVVGGEDSVflsflpefwiAGENFGLLFP---- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 212 sgmlmqpfLYCGATLVLFDRFEPAHFLAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTlsygaaPMAPA----- 286
Cdd:PRK06178 274 --------LFSGATLVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQ------VRVVSfvkkl 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 287 --RIREAW-ERIGPILSQG-YGASES-TSGVTRLSTADHAEAIAGRPgrlASCGRPHGETEVRVVD-EQGREVEGDAIGE 360
Cdd:PRK06178 340 npDYRQRWrALTGSVLAEAaWGMTEThTCDTFTAGFQDDDFDLLSQP---VFVGLPVPGTEFKICDfETGELLPLGAEGE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 361 IVIRGEDVFQGYWGEPELTREVLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVI 440
Cdd:PRK06178 417 IVVRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVV 496
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092251577 441 SVPDATWGESVKAVVALRPGRALEAAALIAHCRERIADYKTPrSVEFVGELPKNPSGKVaRKV 503
Cdd:PRK06178 497 GRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKV-RKQ 557
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
27-505 |
1.11e-68 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 226.83 E-value: 1.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 27 LSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVENCTPRAFIGGD 106
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 107 gytgyarttpgfaaveafvalggpaagylgyEDLLArggtsrpphraaaadaavLHFSSGSTGRIKAAVQSYGNRMASLR 186
Cdd:cd05972 81 -------------------------------EDPAL------------------IYFTSGTTGLPKGVLHTHSYPLGHIP 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 187 KMLLGMDrqARPGD---RLALIGPVTHASGMLMQPFLYcGATLVLF--DRFEPAHFLAEVARLRITHVFMVPAMIHMLLA 261
Cdd:cd05972 112 TAAYWLG--LRPDDihwNIADPGWAKGAWSSFFGPWLL-GATVFVYegPRFDAERILELLERYGVTSFCGPPTAYRMLIK 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 262 dPALEQADLSSLKTLSYGAAPMAPARIREAWERIGPILSQGYGASESTSGVTRLSTADHaeaiagRPGrlaSCGRPHGET 341
Cdd:cd05972 189 -QDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPV------KPG---SMGRPTPGY 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 342 EVRVVDEQGREVEGDAIGEIVIRGEDV--FQGYWGEPELTREVLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNV 419
Cdd:cd05972 259 DVAIIDDDGRELPPGEEGDIAIKLPPPglFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRI 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 420 YPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPG-RALEAAA--LIAHCRERIADYKTPRSVEFVGELPKNPS 496
Cdd:cd05972 339 GPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGyEPSEELAeeLQGHVKKVLAPYKYPREIEFVEELPKTIS 418
|
....*....
gi 1092251577 497 GKVARKVVR 505
Cdd:cd05972 419 GKIRRVELR 427
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
3-502 |
2.04e-68 |
|
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: 227.60 E-value: 2.04e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 3 FALFLQRAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALN 82
Cdd:cd05920 17 LGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 83 PRFTAAEASDVVENCTPRAFIGGDGYTGYartTPGFAAVEAFVALGGPAagylgyedllarggtsrpphraaaadaaVLH 162
Cdd:cd05920 97 PSHRRSELSAFCAHAEAVAYIVPDRHAGF---DHRALARELAESIPEVA----------------------------LFL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 163 FSSGSTGRIKAAVQSYGNRMASLRKM--LLGMDRQARpgdRLALIgPVTH-----ASGMLMQpfLYCGATLVLFDRFEPA 235
Cdd:cd05920 146 LSGGTTGTPKLIPRTHNDYAYNVRASaeVCGLDQDTV---YLAVL-PAAHnfplaCPGVLGT--LLAGGRVVLAPDPSPD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 236 HFLAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIREAWERIGPILSQGYGASESTSGVTRL 315
Cdd:cd05920 220 AAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTRL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 316 StaDHAEAIAGRPGRLAScgrPHgeTEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPEL-TREVLVDGWLRTGDLA 394
Cdd:cd05920 300 D--DPDEVIIHTQGRPMS---PD--DEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHnARAFTPDGFYRTGDLV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 395 RVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPgRALEAAALIAHCRE 474
Cdd:cd05920 373 RRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRD-PPPSAAQLRRFLRE 451
|
490 500
....*....|....*....|....*....
gi 1092251577 475 R-IADYKTPRSVEFVGELPKNPSGKVARK 502
Cdd:cd05920 452 RgLAAYKLPDRIEFVDSLPLTAVGKIDKK 480
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
5-502 |
5.33e-68 |
|
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: 226.62 E-value: 5.33e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 5 LFLQRAARYWGDRPAVMHRERV--LSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALN 82
Cdd:cd05923 5 EMLRRAASRAPDACAIADPARGlrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALIN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 83 PRFTAAEASDVVENCTPRAFIGGDGYTGYARTTPGFAAVEAFVALGGPAAGYlGYEDLLArggtsrPPHRAAAADAAVLh 162
Cdd:cd05923 85 PRLKAAELAELIERGEMTAAVIAVDAQVMDAIFQSGVRVLALSDLVGLGEPE-SAGPLIE------DPPREPEQPAFVF- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 163 FSSGSTGRIKAAVQSygNRMASLRKMLLGMDRQARPGDRLALIG--PVTHASGM--LMQPFLYCGATLVLFDRFEPAHFL 238
Cdd:cd05923 157 YTSGTTGLPKGAVIP--QRAAESRVLFMSTQAGLRHGRHNVVLGlmPLYHVIGFfaVLVAALALDGTYVVVEEFDPADAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 239 AEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMaPARIREAWERIGPILSQG-YGASEStsgVTRLST 317
Cdd:cd05923 235 KLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATM-PDAVLERVNQHLPGEKVNiYGTTEA---MNSLYM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 318 ADHAEAIAGRPGRLascgrphgeTEVRVVDEQGREVEGDAIGE----IVIRGED-VFQGYWGEPELTREVLVDGWLRTGD 392
Cdd:cd05923 311 RDARTGTEMRPGFF---------SEVRIVRIGGSPDEALANGEegelIVAAAADaAFTGYLNQPEATAKKLQDGWYRTGD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 393 LARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRaLEAAALIAHC 472
Cdd:cd05923 382 VGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGT-LSADELDQFC 460
|
490 500 510
....*....|....*....|....*....|.
gi 1092251577 473 RE-RIADYKTPRSVEFVGELPKNPSGKVARK 502
Cdd:cd05923 461 RAsELADFKRPRRYFFLDELPKNAMNKVLRR 491
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
11-505 |
3.77e-67 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 225.33 E-value: 3.77e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 11 ARYWGDRPAVMHRE-----RVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRF 85
Cdd:PRK08008 17 ADVYGHKTALIFESsggvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 86 TAAEASDVVENCTPRAFIGGDGYTG-YARTTPGFAAVEAFVALGGPAA----GYLGYEDLLARGGTS---RPPHRAAAAD 157
Cdd:PRK08008 97 LREESAWILQNSQASLLVTSAQFYPmYRQIQQEDATPLRHICLTRVALpaddGVSSFTQLKAQQPATlcyAPPLSTDDTA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 158 AAVlhFSSGSTGRIKAAVQSYGN-RMASLRKMLLGmdrQARPGDRLALIGPVTH-----ASGMlmqPFLYCGATLVLFDR 231
Cdd:PRK08008 177 EIL--FTSGTTSRPKGVVITHYNlRFAGYYSAWQC---ALRDDDVYLTVMPAFHidcqcTAAM---AAFSAGATFVLLEK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 232 FEPAHFLAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYgAAPMAPARIREAWERIGPILSQGYGASESTSG 311
Cdd:PRK08008 249 YSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHCLREVMF-YLNLSDQEKDAFEERFGVRLLTSYGMTETIVG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 312 VtrlstadhaeaIAGRPG---RLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGE---DVFQGYWGEPELTREVL-V 384
Cdd:PRK08008 328 I-----------IGDRPGdkrRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYYLDPKATAKVLeA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 385 DGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALE 464
Cdd:PRK08008 397 DGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLS 476
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1092251577 465 AAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVR 505
Cdd:PRK08008 477 EEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
7-506 |
8.09e-67 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 225.02 E-value: 8.09e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 7 LQRAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFT 86
Cdd:PRK06155 27 LARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 87 AAEASDVVENCTPRAFIGGDGYTGYARTT-PGFAAVEAFVALGGPAAGYL--GYEDL-LARGGTSRPPHRAAAADAAVLH 162
Cdd:PRK06155 107 GPQLEHILRNSGARLLVVEAALLAALEAAdPGDLPLPAVWLLDAPASVSVpaGWSTApLPPLDAPAPAAAVQPGDTAAIL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 163 FSSGSTGRIKAAV----QSY--GNRMASLrkmlLGMdrqaRPGDRLALIGPVTH--ASGMLMQPFLYcGATLVLFDRFEP 234
Cdd:PRK06155 187 YTSGTTGPSKGVCcphaQFYwwGRNSAED----LEI----GADDVLYTTLPLFHtnALNAFFQALLA-GATYVLEPRFSA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 235 AHFLAEVARLRITHVFMVPAMIHMLLADPALEQadlSSLKTLSYGAAPMAPARIREAW-ERIGPILSQGYGASESTSGVT 313
Cdd:PRK06155 258 SGFWPAVRRHGATVTYLLGAMVSILLSQPARES---DRAHRVRVALGPGVPAALHAAFrERFGVDLLDGYGSTETNFVIA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 314 rlstADHAEAIAGRPGRLAScgrphgETEVRVVDEQGREVEGDAIGEIVIRGEDVF---QGYWGEPELTREVLVDGWLRT 390
Cdd:PRK06155 335 ----VTHGSQRPGSMGRLAP------GFEARVVDEHDQELPDGEPGELLLRADEPFafaTGYFGMPEKTVEAWRNLWFHT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 391 GDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIA 470
Cdd:PRK06155 405 GDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVR 484
|
490 500 510
....*....|....*....|....*....|....*.
gi 1092251577 471 HCRERIADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:PRK06155 485 HCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLRE 520
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
160-506 |
2.48e-66 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 224.14 E-value: 2.48e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 160 VLHFSSGSTGRIKAAVQSYGNRMASlrkMLLGMD--RQARPGDRLAL-IGPVTHASGM--LMQPFLYCGATLVLFDRFEP 234
Cdd:PRK06710 210 LLQYTGGTTGFPKGVMLTHKNLVSN---TLMGVQwlYNCKEGEEVVLgVLPFFHVYGMtaVMNLSIMQGYKMVLIPKFDM 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 235 AHFLAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMaPARIREAWERI-GPILSQGYGASEStsgvt 313
Cdd:PRK06710 287 KMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPL-PVEVQEKFETVtGGKLVEGYGLTES----- 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 314 rlSTADHAEAIAGR--PGrlaSCGRPHGETEVRVVD-EQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDGWLRT 390
Cdd:PRK06710 361 --SPVTHSNFLWEKrvPG---SIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHT 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 391 GDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIA 470
Cdd:PRK06710 436 GDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQ 515
|
330 340 350
....*....|....*....|....*....|....*.
gi 1092251577 471 HCRERIADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:PRK06710 516 FARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIE 551
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
7-506 |
4.39e-66 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 223.49 E-value: 4.39e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 7 LQRAARYWGDRPAVMHRERVLSFRQLDERS-TRLANALLGLGLRPGDRVAVQSRNcaeLVEIECALY---KSGLVKAALN 82
Cdd:PRK05677 30 LKQSCQRFADKPAFSNLGKTLTYGELYKLSgAFAAWLQQHTDLKPGDRIAVQLPN---VLQYPVAVFgamRAGLIVVNTN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 83 PRFTA------------------AEASDVVENCTPRAFIGGDGYTGYARTTPGFA-----AVEAFVALGGPA---AGYLG 136
Cdd:PRK05677 107 PLYTAremehqfndsgakalvclANMAHLAEKVLPKTGVKHVIVTEVADMLPPLKrllinAVVKHVKKMVPAyhlPQAVK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 137 YEDLLARG-GTSRPPHRAAAADAAVLHFSSGSTGRIKAAVQSYGNRMASlrkMLlgmdrQARP--GDRL-----ALIGP- 207
Cdd:PRK05677 187 FNDALAKGaGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVAN---ML-----QCRAlmGSNLnegceILIAPl 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 208 -VTHASGMLMqpflYCGATLVLFD--------RFEPAhFLAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLK-TLS 277
Cdd:PRK05677 259 pLYHIYAFTF----HCMAMMLIGNhnilisnpRDLPA-MVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKlTLS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 278 YGAA-PMAPArirEAWERI-GPILSQGYGASEsTSGVTRLSTADHAeaiagrpgRLASCGRPHGETEVRVVDEQGREVEG 355
Cdd:PRK05677 334 GGMAlQLATA---ERWKEVtGCAICEGYGMTE-TSPVVSVNPSQAI--------QVGTIGIPVPSTLCKVIDDDGNELPL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 356 DAIGEIVIRGEDVFQGYWGEPELTREVL-VDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDV 434
Cdd:PRK05677 402 GEVGELCVKGPQVMKGYWQRPEATDEILdSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGV 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092251577 435 MEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:PRK05677 482 LQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRD 553
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
2-505 |
6.49e-66 |
|
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: 221.47 E-value: 6.49e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 2 AFALFLQRAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAAL 81
Cdd:cd05959 5 AATLVDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 82 NPRFTAAEASDVVENCTPRAFI-------------GGDGYTGYARTTPGFAaveafvalgGPAAGYLGYEDLLARGGTSR 148
Cdd:cd05959 85 NTLLTPDDYAYYLEDSRARVVVvsgelapvlaaalTKSEHTLVVLIVSGGA---------GPEAGALLLAELVAAEAEQL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 149 PPHRAAAADAAVLHFSSGSTGRIKAAVQSYGNRMASLR---KMLLGMdrqaRPGDRLALIGPVTHASGM---LMQPFLYC 222
Cdd:cd05959 156 KPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAElyaRNVLGI----REDDVCFSAAKLFFAYGLgnsLTFPLSVG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 223 GATLVLFDRFEPAHFLAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKtLSYGAAPMAPARIREAWE-RIGPILSQ 301
Cdd:cd05959 232 ATTVLMPERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLR-LCVSAGEALPAEVGERWKaRFGLDILD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 302 GYGASEstsgvtrlstADHAeAIAGRPG--RLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELT 379
Cdd:cd05959 311 GIGSTE----------MLHI-FLSNRPGrvRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 380 REVLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRP 459
Cdd:cd05959 380 RDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRP 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1092251577 460 GRALEAAA---LIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVR 505
Cdd:cd05959 460 GYEDSEALeeeLKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
8-507 |
1.01e-65 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 222.39 E-value: 1.01e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 8 QRAARYWGDRPAVMHRERVLSFRQLDERSTR-LANALLGLGLRPGDRVAVQSRNcaeLVEIECALY---KSGLVKAALNP 83
Cdd:PRK12492 31 ERSCKKFADRPAFSNLGVTLSYAELERHSAAfAAYLQQHTDLVPGDRIAVQMPN---VLQYPIAVFgalRAGLIVVNTNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 84 RFTAAEASDVVENCTPRAFIGGDGYTGYARTTPGFAAVEAFVA-----LGGPAAGYL---------------------GY 137
Cdd:PRK12492 108 LYTAREMRHQFKDSGARALVYLNMFGKLVQEVLPDTGIEYLIEakmgdLLPAAKGWLvntvvdkvkkmvpayhlpqavPF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 138 EDLLARG-GTSRPPHRAAAADAAVLHFSSGSTGRIKAAVQSYGNRMASLRKMLLGMDRQARPGDRLALIG--------PV 208
Cdd:PRK12492 188 KQALRQGrGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDGQPLMKEGqevmiaplPL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 209 TH-----ASGMLMqpfLYCGATLVLF-DRFEPAHFLAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAP 282
Cdd:PRK12492 268 YHiyaftANCMCM---MVSGNHNVLItNPRDIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDLDFSALKLTNSGGTA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 283 MAPArIREAWERI-GPILSQGYGASEsTSGVTrlSTADHaeaiaGRPGRLASCGRPHGETEVRVVDEQGREVEGDAIGEI 361
Cdd:PRK12492 345 LVKA-TAERWEQLtGCTIVEGYGLTE-TSPVA--STNPY-----GELARLGTVGIPVPGTALKVIDDDGNELPLGERGEL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 362 VIRGEDVFQGYWGEPELTREVL-VDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVI 440
Cdd:PRK12492 416 CIKGPQVMKGYWQQPEATAEALdAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAI 495
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092251577 441 SVPDATWGESVKA-VVALRPGRALEaaALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVREP 507
Cdd:PRK12492 496 GVPDERSGEAVKLfVVARDPGLSVE--ELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
6-505 |
5.42e-65 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 220.28 E-value: 5.42e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 6 FLQRAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRF 85
Cdd:PRK07059 28 LLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 86 T-----------AAEASDVVEN--CTPRAFIggdgytgyARTTPGFAAVEAFVALGG-----------------PA---A 132
Cdd:PRK07059 108 TprelehqlkdsGAEAIVVLENfaTTVQQVL--------AKTAVKHVVVASMGDLLGfkghivnfvvrrvkkmvPAwslP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 133 GYLGYEDLLARGG--TSRPPHrAAAADAAVLHFSSGSTGRIKAAVQSYGNRMASLRKMLLGMD----RQARPgDRLALIG 206
Cdd:PRK07059 180 GHVRFNDALAEGArqTFKPVK-LGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQpafeKKPRP-DQLNFVC 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 207 --PVTH-----ASGMLMqpfLYCGATLVLF--DRFEPAhFLAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKtLS 277
Cdd:PRK07059 258 alPLYHifaltVCGLLG---MRTGGRNILIpnPRDIPG-FIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLI-VA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 278 YGAApMAPAR-IREAW-ERIGPILSQGYGASESTSGVT--RLSTADHAEAIagrpgrlascGRPHGETEVRVVDEQGREV 353
Cdd:PRK07059 333 NGGG-MAVQRpVAERWlEMTGCPITEGYGLSETSPVATcnPVDATEFSGTI----------GLPLPSTEVSIRDDDGNDL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 354 EGDAIGEIVIRGEDVFQGYWGEPELTREVLV-DGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHP 432
Cdd:PRK07059 402 PLGEPGEICIRGPQVMAGYWNRPDETAKVMTaDGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHP 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092251577 433 DVMEACVISVPDATWGESVKAVVaLRPGRALEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVR 505
Cdd:PRK07059 482 GVLEVAAVGVPDEHSGEAVKLFV-VKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
6-506 |
1.75e-64 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 218.77 E-value: 1.75e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 6 FLQRAARYWGDRPAV-----MHRE-RVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGlvkA 79
Cdd:PRK13295 29 DLDACVASCPDKTAVtavrlGTGApRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIG---A 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 80 ALNP----------RFTAAEA-SDVVenCTPRAFIGGDGYTGYARTTPGFAAVEAFVALGGPAAGylGYEDLLARGGTSR 148
Cdd:PRK13295 106 VLNPlmpifrerelSFMLKHAeSKVL--VVPKTFRGFDHAAMARRLRPELPALRHVVVVGGDGAD--SFEALLITPAWEQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 149 PP--------HRAAAADAAVLHFSSGSTGRIKAAVQSYGNRMASLRKMLLGMDRQArpGDRLALIGPVTHASGM---LMQ 217
Cdd:PRK13295 182 EPdapailarLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGA--DDVILMASPMAHQTGFmygLMM 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 218 PfLYCGATLVLFDRFEPAHFLAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIREAWERIGP 297
Cdd:PRK13295 260 P-VMLGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 298 ILSQGYGASEsTSGVTRLSTADHAEAIAgrpgrlASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPE 377
Cdd:PRK13295 339 KIVSAWGMTE-NGAVTLTKLDDPDERAS------TTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQ 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 378 LTReVLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVAL 457
Cdd:PRK13295 412 LNG-TDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVP 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1092251577 458 RPGRALEAAALIAHCRE-RIADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:PRK13295 491 RPGQSLDFEEMVEFLKAqKVAKQYIPERLVVRDALPRTPSGKIQKFRLRE 540
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
1-507 |
8.91e-64 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 216.55 E-value: 8.91e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 1 MAFALFLQRAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAA 80
Cdd:PRK13382 43 MGPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 81 LNPRFTAAEASDVVEN--------------CTPRAFIGgdgytgyartTPGFAAVEAFVAlggpAAGYLGYEDLLARGGT 146
Cdd:PRK13382 123 LNTSFAGPALAEVVTRegvdtviydeefsaTVDRALAD----------CPQATRIVAWTD----EDHDLTVEVLIAAHAG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 147 SRPPHRAAAADAAVLhfSSGSTGRIKAAVQSYGNRMASLRKMllgMDRQA-RPGDRLALIGPVTHASG---MLMQPFLYC 222
Cdd:PRK13382 189 QRPEPTGRKGRVILL--TSGTTGTPKGARRSGPGGIGTLKAI---LDRTPwRAEEPTVIVAPMFHAWGfsqLVLAASLAC 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 223 gaTLVLFDRFEPAHFLAEVARLRITHVFMVPAMIHMLLADPAlEQADLSSLKTLSYGAA---PMAPARIREAWERIGPIL 299
Cdd:PRK13382 264 --TIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPA-EVRNRYSGRSLRFAAAsgsRMRPDVVIAFMDQFGDVI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 300 SQGYGASEstsgVTRLSTADHAEAIAGrpgrLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYwgEPELT 379
Cdd:PRK13382 341 YNNYNATE----AGMIATATPADLRAA----PDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGST 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 380 REvLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRP 459
Cdd:PRK13382 411 KD-FHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKP 489
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1092251577 460 GRALEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVREP 507
Cdd:PRK13382 490 GASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
6-499 |
5.00e-63 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 216.75 E-value: 5.00e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 6 FLQRAARYWGDRPAV--------MHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLV 77
Cdd:PRK07529 30 LLSRAAARHPDAPALsflldadpLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 78 kAALNPRF---------TAAEASDVVencTPRAFIGGDGY------------------TGYARTTPGFAAVEAFVALGGP 130
Cdd:PRK07529 110 -NPINPLLepeqiaellRAAGAKVLV---TLGPFPGTDIWqkvaevlaalpelrtvveVDLARYLPGPKRLAVPLIRRKA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 131 AAGYLGYEDLLAR--GGTSRPPHRAAAADAAVLHFSSGSTGRIKAAVQSYGNRMAslRKMLLGMDRQARPGDRLALIGPV 208
Cdd:PRK07529 186 HARILDFDAELARqpGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVA--NAWLGALLLGLGPGDTVFCGLPL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 209 THASGML---MQPFLYcGATLVL-----------FDRfepahFLAEVARLRITHVFMVPAMIHMLLADPAlEQADLSSLK 274
Cdd:PRK07529 264 FHVNALLvtgLAPLAR-GAHVVLatpqgyrgpgvIAN-----FWKIVERYRINFLSGVPTVYAALLQVPV-DGHDISSLR 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 275 TLSYGAAPMAPARIREAWERIGPILSQGYGASESTSGVTRlstadhaeAIAGRPGRLASCGRPHGETEVRVV--DEQG-- 350
Cdd:PRK07529 337 YALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSV--------NPPDGERRIGSVGLRLPYQRVRVVilDDAGry 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 351 -REVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLY 429
Cdd:PRK07529 409 lRDCAVDEVGVLCIAGPNVFSGYLEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALL 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092251577 430 QHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCRERIADYKT-PRSVEFVGELPKNPSGKV 499
Cdd:PRK07529 489 RHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLAFARDHIAERAAvPKHVRILDALPKTAVGKI 559
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
5-506 |
3.32e-62 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 213.20 E-value: 3.32e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 5 LFLQRAARYwGDRPAVMHRERVLSFRQLDERSTR-LANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNP 83
Cdd:PRK08751 30 VFATSVAKF-ADRPAYHSFGKTITYREADQLVEQfAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 84 RFTAAE-----------ASDVVEN-CTPRAFIGGDGYTGYARTTP-----GF--AAVEAFV-------ALGGPAAGYLGY 137
Cdd:PRK08751 109 LYTPRElkhqlidsgasVLVVIDNfGTTVQQVIADTPVKQVITTGlgdmlGFpkAALVNFVvkyvkklVPEYRINGAIRF 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 138 EDLLARGGTSR-PPHRAAAADAAVLHFSSGSTGRIKAAVQSYGNRMASLRKM--LLGMDRQARPGDRLALIG-PVTH--- 210
Cdd:PRK08751 189 REALALGRKHSmPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAhqWLAGTGKLEEGCEVVITAlPLYHifa 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 211 --ASGMLMQPFLYCGAtLVLFDRFEPAhFLAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLK-TLSYGaapMAPAR 287
Cdd:PRK08751 269 ltANGLVFMKIGGCNH-LISNPRDMPG-FVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKmTLGGG---MAVQR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 288 -IREAWERI-GPILSQGYGASESTSG--VTRLSTADHAEAIagrpgrlascGRPHGETEVRVVDEQGREVEGDAIGEIVI 363
Cdd:PRK08751 344 sVAERWKQVtGLTLVEAYGLTETSPAacINPLTLKEYNGSI----------GLPIPSTDACIKDDAGTVLAIGEIGELCI 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 364 RGEDVFQGYWGEPELTREVL-VDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISV 442
Cdd:PRK08751 414 KGPQVMKGYWKRPEETAKVMdADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGV 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092251577 443 PDATWGESVKAVVaLRPGRALEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:PRK08751 494 PDEKSGEIVKVVI-VKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRD 556
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
160-506 |
1.51e-61 |
|
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: 204.87 E-value: 1.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 160 VLHFSSGSTGRIKAAVQSYGNRMASLR--KMLLGMDrqarPGDRLALIGPVTHASGmLMQPF--LYCGATLVLFDRFEPA 235
Cdd:cd17630 4 TVILTSGSTGTPKAVVHTAANLLASAAglHSRLGFG----GGDSWLLSLPLYHVGG-LAILVrsLLAGAELVLLERNQAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 236 hfLAEVARLRITHVFMVPAMIHMLLADPAlEQADLSSLKTLSYGAAPMAPARIREAWERIGPILsQGYGASESTSGVTRL 315
Cdd:cd17630 79 --AEDLAPPGVTHVSLVPTQLQRLLDSGQ-GPAALKSLRAVLLGGAPIPPELLERAADRGIPLY-TTYGMTETASQVATK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 316 STADHAeaiagrpgrLASCGRPHGETEVRVVDEqgrevegdaiGEIVIRGEDVFQGYWgEPELTREVLVDGWLRTGDLAR 395
Cdd:cd17630 155 RPDGFG---------RGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYL-RGQLVPEFNEDGWFTTKDLGE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 396 VDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALeaAALIAHCRER 475
Cdd:cd17630 215 LHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADP--AELRAWLKDK 292
|
330 340 350
....*....|....*....|....*....|.
gi 1092251577 476 IADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:cd17630 293 LARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
16-502 |
9.68e-61 |
|
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: 206.22 E-value: 9.68e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 16 DRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVeieCALY---KSGLVKAALNPRFTAAEASD 92
Cdd:cd05930 2 DAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMV---VAILavlKAGAAYVPLDPSYPAERLAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 93 VVENCTPRAFIGGDGYTGYarttpgfaaveafvalggpaagylgyedllarggtsrpphraaaadaaVLhFSSGSTGRIK 172
Cdd:cd05930 79 ILEDSGAKLVLTDPDDLAY------------------------------------------------VI-YTSGSTGKPK 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 173 AAV---QSYGNRMASLRKMLlgmdrQARPGDRLALIGPVTH-ASGMLMQPFLYCGATLVLFD---RFEPAHFLAEVARLR 245
Cdd:cd05930 110 GVMvehRGLVNLLLWMQEAY-----PLTPGDRVLQFTSFSFdVSVWEIFGALLAGATLVVLPeevRKDPEALADLLAEEG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 246 ITHVFMVPAMIHMLLadPALEQADLSSLKTLSYGAAPMAPARIREaWERIGP--ILSQGYGASESTSGVTRLSTADHAEA 323
Cdd:cd05930 185 ITVLHLTPSLLRLLL--QELELAALPSLRLVLVGGEALPPDLVRR-WRELLPgaRLVNLYGPTEATVDATYYRVPPDDEE 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 324 IAGRPGrlascGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVD------GWL-RTGDLARV 396
Cdd:cd05930 262 DGRVPI-----GRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPnpfgpgERMyRTGDLVRW 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 397 DEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCRERI 476
Cdd:cd05930 337 LPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERL 416
|
490 500
....*....|....*....|....*.
gi 1092251577 477 ADYKTPRSVEFVGELPKNPSGKVARK 502
Cdd:cd05930 417 PDYMVPSAFVVLDALPLTPNGKVDRK 442
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
17-505 |
1.80e-60 |
|
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: 205.40 E-value: 1.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 17 RPAVMHRERVLSFRQLDERSTRLA-NALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEAsdvve 95
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIAnVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKEL----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 96 nctprafiggDGYTGYARTTpgfaaveafVALggpAAGYLGYEDLLArggtsrpphraaaadaaVLHFSSGSTGRIKAAv 175
Cdd:cd05958 76 ----------AYILDKARIT---------VAL---CAHALTASDDIC-----------------ILAFTSGTTGAPKAT- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 176 qsygnrMASLRKMLLGMDRQA------RPGDRLALIGPV--THASGMLMQPFLYCGATLVLFDRFEPAHFLAEVARLRIT 247
Cdd:cd05958 116 ------MHFHRDPLASADRYAvnvlrlREDDRFVGSPPLafTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPT 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 248 HVFMVPAMIHMLLADPALEQADLSSL-KTLSYGAApmAPARIREAW-ERIGPILSQGYGASESTSgVTRLSTADHAeaia 325
Cdd:cd05958 190 VLFTAPTAYRAMLAHPDAAGPDLSSLrKCVSAGEA--LPAALHRAWkEATGIPIIDGIGSTEMFH-IFISARPGDA---- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 326 gRPGRLascGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEdvfQGYWGEPELTREVLV-DGWLRTGDLARVDEEGFIYL 404
Cdd:cd05958 263 -RPGAT---GKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP---TGCRYLADKRQRTYVqGGWNITGDTYSRDPDGYFRH 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 405 VDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRA---LEAAALIAHCRERIADYKT 481
Cdd:cd05958 336 QGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIpgpVLARELQDHAKAHIAPYKY 415
|
490 500
....*....|....*....|....
gi 1092251577 482 PRSVEFVGELPKNPSGKVARKVVR 505
Cdd:cd05958 416 PRAIEFVTELPRTATGKLQRFALR 439
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
52-506 |
6.54e-60 |
|
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: 206.22 E-value: 6.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 52 DRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVENCTPR-AFIGGDGYTGYARTTPGFAAVEAFVALGGp 130
Cdd:cd17642 70 DRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTiVFCSKKGLQKVLNVQKKLKIIKTIIILDS- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 131 AAGYLGYEDL-------LARGGTS---RPPHRAAAADAAVLHFSSGSTGRIKAAVQSYGN---RMASLRKMLLGmdRQAR 197
Cdd:cd17642 149 KEDYKGYQCLytfitqnLPPGFNEydfKPPSFDRDEQVALIMNSSGSTGLPKGVQLTHKNivaRFSHARDPIFG--NQII 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 198 PGDRLALIGPVTHASGMLMQ-PFLYCGATLVLFDRFEPAHFLAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTL 276
Cdd:cd17642 227 PDTAILTVIPFHHGFGMFTTlGYLICGFRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEI 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 277 SYGAAPMAPARIREAWERIG-PILSQGYGASESTSGVtrLSTADHAEaiagRPGrlaSCGRPHGETEVRVVD-EQGREVE 354
Cdd:cd17642 307 ASGGAPLSKEVGEAVAKRFKlPGIRQGYGLTETTSAI--LITPEGDD----KPG---AVGKVVPFFYAKVVDlDTGKTLG 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 355 GDAIGEIVIRGEDVFQGYWGEPELTREVLV-DGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPD 433
Cdd:cd17642 378 PNERGELCVKGPMIMKGYVNNPEATKALIDkDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPK 457
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092251577 434 VMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCRERIADYKTPR-SVEFVGELPKNPSGKVARKVVRE 506
Cdd:cd17642 458 IFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
16-505 |
3.07e-59 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 203.47 E-value: 3.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 16 DRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPgDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVE 95
Cdd:PRK07638 16 NKIAIKENDRVLTYKDWFESVCKVANWLNEKESKN-KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 96 NCTPRAFIGGDGYTG--------------YARTTPGFAAVEAFVALGGPAAGYLGyedllarggtsrpphraaaadaavl 161
Cdd:PRK07638 95 ISNADMIVTERYKLNdlpdeegrvieideWKRMIEKYLPTYAPIENVQNAPFYMG------------------------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 162 hFSSGSTGRIKAAVQSYGNRMASLRKMLlgMDRQARPGDRLALIGPVTHaSGMLMQPF--LYCGATLVLFDRFEPAHFLA 239
Cdd:PRK07638 150 -FTSGSTGKPKAFLRAQQSWLHSFDCNV--HDFHMKREDSVLIAGTLVH-SLFLYGAIstLYVGQTVHLMRKFIPNQVLD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 240 EVARLRITHVFMVPAMIHMLL-ADPALEQadlsSLKTLSYGAAPMAPA--RIREAWERIGpiLSQGYGASEsTSGVTRLS 316
Cdd:PRK07638 226 KLETENISVMYTVPTMLESLYkENRVIEN----KMKIISSGAKWEAEAkeKIKNIFPYAK--LYEFYGASE-LSFVTALV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 317 TADHAEaiagRPgrlASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDGWLRTGDLARV 396
Cdd:PRK07638 299 DEESER----RP---NSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARELNADGWMTVRDVGYE 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 397 DEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVAlrpGRAlEAAALIAHCRERI 476
Cdd:PRK07638 372 DEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIK---GSA-TKQQLKSFCLQRL 447
|
490 500
....*....|....*....|....*....
gi 1092251577 477 ADYKTPRSVEFVGELPKNPSGKVARKVVR 505
Cdd:PRK07638 448 SSFKIPKEWHFVDEIPYTNSGKIARMEAK 476
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
163-501 |
3.08e-58 |
|
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: 196.09 E-value: 3.08e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 163 FSSGSTGRIKAAVQSYGNRMASL--RKMLLGMDRQarpgDRLALIGPVTHaSGML---MQPfLYCGATLVLFDRFEPAHF 237
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFvcNEDLFNISGE----DAILAPGPLSH-SLFLygaISA-LYLGGTFIGQRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 238 LAEVARLRITHVFMVPAMIHMLladpALEQADLSSLKTLSYGAAPMAP---ARIREAWERIGPILSqgYGASEsTSGVTR 314
Cdd:cd17633 81 IRKINQYNATVIYLVPTMLQAL----ARTLEPESKIKSIFSSGQKLFEstkKKLKNIFPKANLIEF--YGTSE-LSFITY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 315 LSTADhaeaiAGRPGrlaSCGRPHGETEVRVvdeqgREVEGDAIGEIVIRGEDVFQGYWGEPELTrevlVDGWLRTGDLA 394
Cdd:cd17633 154 NFNQE-----SRPPN---SVGRPFPNVEIEI-----RNADGGEIGKIFVKSEMVFSGYVRGGFSN----PDGWMSVGDIG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 395 RVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGEsvkAVVALRPGRALEAAALIAHCRE 474
Cdd:cd17633 217 YVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGE---IAVALYSGDKLTYKQLKRFLKQ 293
|
330 340
....*....|....*....|....*..
gi 1092251577 475 RIADYKTPRSVEFVGELPKNPSGKVAR 501
Cdd:cd17633 294 KLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
9-510 |
3.71e-58 |
|
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: 202.08 E-value: 3.71e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 9 RAARYWGDRPAVMH------RERVLSFRQLDERsTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAAL- 81
Cdd:cd05931 1 RRAAARPDRPAYTFlddeggREETLTYAELDRR-ARAIAARLQAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 82 --NPRFTAAEASDVVENCTPRAFIGGDGYtgYARTTPGFAAVEAFVALGGPAAgylgyeDLLARGGTSRPPHRAAAAD-A 158
Cdd:cd05931 80 ppTPGRHAERLAAILADAGPRVVLTTAAA--LAAVRAFAASRPAAGTPRLLVV------DLLPDTSAADWPPPSPDPDdI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 159 AVLHFSSGSTGRIKAAVQSYGNRMASLRKMLLGMDrqARPGDRLALIGPVTHASGM---LMQPfLYCGATLVLFDrfePA 235
Cdd:cd05931 152 AYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYG--LDPGDVVVSWLPLYHDMGLiggLLTP-LYSGGPSVLMS---PA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 236 HFLA-------EVARLRITHVFmVP----AMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIREAWERIGPI------ 298
Cdd:cd05931 226 AFLRrplrwlrLISRYRATISA-APnfayDLCVRRVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFAEAFAPFgfrpea 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 299 LSQGYGASESTSGVT--------------RLSTADHAEAIAGRPG---RLASCGRPHGETEVRVVDEQG-REVEGDAIGE 360
Cdd:cd05931 305 FRPSYGLAEATLFVSggppgtgpvvlrvdRDALAGRAVAVAADDPaarELVSCGRPLPDQEVRIVDPETgRELPDGEVGE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 361 IVIRGEDVFQGYWGEPELTREVLV-------DGWLRTGDLARVDeEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPD 433
Cdd:cd05931 385 IWVRGPSVASGYWGRPEATAETFGalaatdeGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 434 VME---ACVISVPDATWGESVKAVVALRPGRALEAAALIAHCRERIADYK--TPRSVEFV--GELPKNPSGKVARKVVRE 506
Cdd:cd05931 464 ALRpgcVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREHgvAPADVVLVrpGSIPRTSSGKIQRRACRA 543
|
....
gi 1092251577 507 PYWQ 510
Cdd:cd05931 544 AYLD 547
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
16-502 |
2.76e-57 |
|
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: 197.08 E-value: 2.76e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 16 DRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVE 95
Cdd:cd05945 6 DRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 96 NCTPRAFIGGDGYTGYarttpgfaaveafvalggpaagylgyedllarggtsrpphraaaadaavLHFSSGSTGRIKAAV 175
Cdd:cd05945 86 AAKPALLIADGDDNAY-------------------------------------------------IIFTSGSTGRPKGVQ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 176 QSYGNRMASLRKMLlgMDRQARPGDRLALIGPVT-HASGMLMQPFLYCGATLVLFDRFEPAHFLAEVARLR---ITHVFM 251
Cdd:cd05945 117 ISHDNLVSFTNWML--SDFPLGPGDVFLNQAPFSfDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAehgITVWVS 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 252 VPAMIHMLLADPALEQADLSSLKTLSYGAAPMaPARIREAWERIGP--ILSQGYGASESTSGVTrlstADH-AEAIAGRP 328
Cdd:cd05945 195 TPSFAAMCLLSPTFTPESLPSLRHFLFCGEVL-PHKTARALQQRFPdaRIYNTYGPTEATVAVT----YIEvTPEVLDGY 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 329 GRLaSCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVD----GWLRTGDLARVDEEGFIYL 404
Cdd:cd05945 270 DRL-PIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPdegqRAYRTGDLVRLEADGLLFY 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 405 VDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALI-AHCRERIADYKTPR 483
Cdd:cd05945 349 RGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGLTKAIkAELAERLPPYMIPR 428
|
490
....*....|....*....
gi 1092251577 484 SVEFVGELPKNPSGKVARK 502
Cdd:cd05945 429 RFVYLDELPLNANGKIDRK 447
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
7-506 |
1.80e-56 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 197.13 E-value: 1.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 7 LQRAARyWGDRPAVMHRE--RVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPR 84
Cdd:PLN02246 30 FERLSE-FSDRPCLIDGAtgRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 85 FTAAEASDVVENCTPRAFIggdGYTGYARTTPGFAAVEAF--VALGGPAAGYLGYEDLLARGGTSRPPHRAAAADAAVLH 162
Cdd:PLN02246 109 YTPAEIAKQAKASGAKLII---TQSCYVDKLKGLAEDDGVtvVTIDDPPEGCLHFSELTQADENELPEVEISPDDVVALP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 163 FSSGSTGRIKAAVQSYGNRMASLRKMLLGMDRQA--RPGDRLALIGPVTHASGM--LMQPFLYCGATLVLFDRFEPAHFL 238
Cdd:PLN02246 186 YSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLyfHSDDVILCVLPMFHIYSLnsVLLCGLRVGAAILIMPKFEIGALL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 239 AEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMAP-------ARIREAwerigpILSQGYGASESTSg 311
Cdd:PLN02246 266 ELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKeledafrAKLPNA------VLGQGYGMTEAGP- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 312 VTRLSTADHAEAIAGRPGrlaSCGRPHGETEVRVVD-EQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVL-VDGWLR 389
Cdd:PLN02246 339 VLAMCLAFAKEPFPVKSG---SCGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIdKDGWLH 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 390 TGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALI 469
Cdd:PLN02246 416 TGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIK 495
|
490 500 510
....*....|....*....|....*....|....*..
gi 1092251577 470 AHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:PLN02246 496 QFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRA 532
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
7-506 |
2.21e-56 |
|
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: 196.95 E-value: 2.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 7 LQRAARYWGDRPAVMH-----RERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAAL 81
Cdd:cd05970 23 VDAMAKEYPDKLALVWcddagEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 82 NPRFTAAEASDVVENCTPRAF--IGGDGYTG-YARTTPGFAAVEAFVALGGPAA-GYLGYEDLLARGGTS-RPPHRAAAA 156
Cdd:cd05970 103 THQLTAKDIVYRIESADIKMIvaIAEDNIPEeIEKAAPECPSKPKLVWVGDPVPeGWIDFRKLIKNASPDfERPTANSYP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 157 D---AAVLHFSSGSTGRIKAAVQsygNRMASLRKMLLGMDRQ-ARPGDRLALIGPVTHASGMLMQpfLY----CGATLVL 228
Cdd:cd05970 183 CgedILLVYFSSGTTGMPKMVEH---DFTYPLGHIVTAKYWQnVREGGLHLTVADTGWGKAVWGK--IYgqwiAGAAVFV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 229 FD--RFEPAHFLAEVARLRIThVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIREAWERIGPILSQGYGAS 306
Cdd:cd05970 258 YDydKFDPKALLEKLSKYGVT-TFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQT 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 307 ESTSGVTRLStadhaeAIAGRPGrlaSCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGED-----VFQGYWGEPELTRE 381
Cdd:cd05970 337 ETTLTIATFP------WMEPKPG---SMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKgkpvgLFGGYYKDAEKTAE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 382 VLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVAL---- 457
Cdd:cd05970 408 VWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLakgy 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1092251577 458 RPGRALEaAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:cd05970 488 EPSEELK-KELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
22-505 |
2.67e-55 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 191.49 E-value: 2.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 22 HRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFtaaeasdvvenctpra 101
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALF---------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 102 fiGGDgytgyarttpgfaAVEAFVALGGPAAgylgyedlLARGGTSRPphraaaadaAVLHFSSGSTGRIKAAVQSYGNR 181
Cdd:cd05971 66 --GPE-------------ALEYRLSNSGASA--------LVTDGSDDP---------ALIIYTSGTTGPPKGALHAHRVL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 182 MASLRKMLLGMDRQARPGDRL------ALIGpvthASGMLMQPFLYCGATLVL--FDRFEPAHFLAEVARLRITHVFMVP 253
Cdd:cd05971 114 LGHLPGVQFPFNLFPRDGDLYwtpadwAWIG----GLLDVLLPSLYFGVPVLAhrMTKFDPKAALDLMSRYGVTTAFLPP 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 254 AMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIREAWERIGPILSQGYGASEstsgvTRLSTADHAEAIAGRPGrlaS 333
Cdd:cd05971 190 TALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTE-----CNLVIGNCSALFPIKPG---S 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 334 CGRPHGETEVRVVDEQGREVEGDAIGEIVIRGED--VFQGYWGEPELTREVLVDGWLRTGDLARVDEEGFIYLVDRKKDM 411
Cdd:cd05971 262 MGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDV 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 412 IISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPG----RALeAAALIAHCRERIADYKTPRSVEF 487
Cdd:cd05971 342 ITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGetpsDAL-AREIQELVKTRLAAHEYPREIEF 420
|
490
....*....|....*...
gi 1092251577 488 VGELPKNPSGKVARKVVR 505
Cdd:cd05971 421 VNELPRTATGKIRRRELR 438
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
6-505 |
1.74e-54 |
|
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: 190.63 E-value: 1.74e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 6 FLQRAARYwGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRF 85
Cdd:cd17651 1 FERQAART-PDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 86 TAAEASDVVENCTPRAFIGGDGYTgyarttPGFAAVEAFVALggpaagyLGYEDLLARGGTSRPPHRAAAADAAVLhFSS 165
Cdd:cd17651 80 PAERLAFMLADAGPVLVLTHPALA------GELAVELVAVTL-------LDQPGAAAGADAEPDPALDADDLAYVI-YTS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 166 GSTGRIKAAVQSYgnrmASLRKMLLGMDR--QARPGDRLALIGPVT-HASGMLMQPFLYCGATLVLFD---RFEPAHFLA 239
Cdd:cd17651 146 GSTGRPKGVVMPH----RSLANLVAWQARasSLGPGARTLQFAGLGfDVSVQEIFSTLCAGATLVLPPeevRTDPPALAA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 240 EVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPM-APARIRE--AWERiGPILSQGYGASESTsgvtrLS 316
Cdd:cd17651 222 WLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLvLTEDLREfcAGLP-GLRLHNHYGPTETH-----VV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 317 TADHAEAIAGRPGRLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDG-------WLR 389
Cdd:cd17651 296 TALSLPGDPAAWPAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDpfvpgarMYR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 390 TGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALI 469
Cdd:cd17651 376 TGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELR 455
|
490 500 510
....*....|....*....|....*....|....*.
gi 1092251577 470 AHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVR 505
Cdd:cd17651 456 AALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
27-505 |
5.57e-54 |
|
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: 188.09 E-value: 5.57e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 27 LSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVENCTPRAFIGGD 106
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 107 GYtgYARTTPgfaaveafvalggpaagylgyEDLLarggtsrpphraaaadaaVLHFSSGSTGRIKAAVQSYgNRMAS-- 184
Cdd:cd05969 81 EL--YERTDP---------------------EDPT------------------LLHYTSGTTGTPKGVLHVH-DAMIFyy 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 185 -LRKMLLGMdrqaRPGDRL---ALIGPVTHASGMLMQPFLYcGATLVLFD-RFEPAHFLAEVARLRITHVFMVPAMIHML 259
Cdd:cd05969 119 fTGKYVLDL----HPDDIYwctADPGWVTGTVYGIWAPWLN-GVTNVVYEgRFDAESWYGIIERVKVTVWYTAPTAIRML 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 260 --LADPALEQADLSSLKTLSYGAAPMAPARIREAWERIGPILSQGYGASESTSgvtrlstadhaEAIAGRPG---RLASC 334
Cdd:cd05969 194 mkEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGS-----------IMIANYPCmpiKPGSM 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 335 GRPHGETEVRVVDEQGREVEGDAIGEIVIRGE--DVFQGYWGEPELTREVLVDGWLRTGDLARVDEEGFIYLVDRKKDMI 412
Cdd:cd05969 263 GKPLPGVKAAVVDENGNELPPGTKGILALKPGwpSMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDII 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 413 ISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPG-RALEA--AALIAHCRERIADYKTPRSVEFVG 489
Cdd:cd05969 343 KTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGfEPSDElkEEIINFVRQKLGAHVAPREIEFVD 422
|
490
....*....|....*.
gi 1092251577 490 ELPKNPSGKVARKVVR 505
Cdd:cd05969 423 NLPKTRSGKIMRRVLK 438
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
7-508 |
2.47e-52 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 185.86 E-value: 2.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 7 LQRAARYWGDRPA-VMHRERV-LSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPR 84
Cdd:PRK05852 22 VEVAATRLPEAPAlVVTADRIaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 85 FTAAEASDVVENCTPRA-FIGGDGYTGYARTTPGFAAVEAFValgGPAAGYLGYEDLLARGGTSRPPHRAAAADA----- 158
Cdd:PRK05852 102 LPIAEQRVRSQAAGARVvLIDADGPHDRAEPTTRWWPLTVNV---GGDSGPSGGTLSVHLDAATEPTPATSTPEGlrpdd 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 159 AVLHFSSGSTGRIKAAVQSYGNRMASLRKMLLGMdrQARPGDRLALIGPVTHASGML--MQPFLYCGATLVL--FDRFEP 234
Cdd:PRK05852 179 AMIMFTGGTTGLPKMVPWTHANIASSVRAIITGY--RLSPRDATVAVMPLYHGHGLIaaLLATLASGGAVLLpaRGRFSA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 235 AHFLAEVARLRITHVFMVPAMIHMLLADPALEQADLS--SLKTLSYGAAPMAPARIREAWERIGPILSQGYGASESTSGV 312
Cdd:PRK05852 257 HTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKpaALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 313 --TRLSTADHAEAIAGRPGRLASCGRPhgetEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDGWLRT 390
Cdd:PRK05852 337 ttTQIEGIGQTENPVVSTGLVGRSTGA----QIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWLRT 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 391 GDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIA 470
Cdd:PRK05852 413 GDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQ 492
|
490 500 510
....*....|....*....|....*....|....*...
gi 1092251577 471 HCRERIADYKTPRSVEFVGELPKNPSGKVARKVVREPY 508
Cdd:PRK05852 493 FCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQF 530
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
4-502 |
3.31e-52 |
|
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: 184.40 E-value: 3.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 4 ALFLQRAARYwGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNP 83
Cdd:cd17646 2 ALVAEQAART-PDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 84 RFTAAEASDVVENCTPRAFIGGDGytgyartTPGFAAVEAFVALGGPAAgylgyedlLARGGTSRPPHRAAAADAAVLHF 163
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTAD-------LAARLPAGGDVALLGDEA--------LAAPPATPPLVPPRPDNLAYVIY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 164 SSGSTGRIKAAVqsygNRMASLRKMLLGMDRQAR--PGDRLALIGPVTHASGM--LMQPFLyCGATLVLFD---RFEPAH 236
Cdd:cd17646 146 TSGSTGRPKGVM----VTHAGIVNRLLWMQDEYPlgPGDRVLQKTPLSFDVSVweLFWPLV-AGARLVVARpggHRDPAY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 237 FLAEVARLRITHVFMVPAMIHMLLADPALEQADlsSLKTLSYGAAPMAPARIREAWERIGPILSQGYGASESTSGVTrls 316
Cdd:cd17646 221 LAALIREHGVTTCHFVPSMLRVFLAEPAAGSCA--SLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVT--- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 317 tadHAEAIAGRPGRLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDGWL-------R 389
Cdd:cd17646 296 ---HWPVRGPAETPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFgpgsrmyR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 390 TGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRA-LEAAAL 468
Cdd:cd17646 373 TGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAgPDTAAL 452
|
490 500 510
....*....|....*....|....*....|....
gi 1092251577 469 IAHCRERIADYKTPRSVEFVGELPKNPSGKVARK 502
Cdd:cd17646 453 RAHLAERLPEYMVPAAFVVLDALPLTANGKLDRA 486
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
4-502 |
5.17e-52 |
|
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: 183.94 E-value: 5.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 4 ALFLQRAARyWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNP 83
Cdd:cd12117 1 ELFEEQAAR-TPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 84 RFTAAEASDVVENCTPRAFIGgdgytgyARTTPGfaaveafvALGGPAAGYLGYEDLLARGGTSrPPHRAAAADAAVLHF 163
Cdd:cd12117 80 ELPAERLAFMLADAGAKVLLT-------DRSLAG--------RAGGLEVAVVIDEALDAGPAGN-PAVPVSPDDLAYVMY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 164 SSGSTGRIKAAvqsygnrMASLRKML-LGMDR---QARPGDRLALIGPVT-HASGMLMQPFLYCGATLVLFDR---FEPA 235
Cdd:cd12117 144 TSGSTGRPKGV-------AVTHRGVVrLVKNTnyvTLGPDDRVLQTSPLAfDASTFEIWGALLNGARLVLAPKgtlLDPD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 236 HFLAEVARLRITHVFMVPAMIHMLL-ADPALeqadLSSLKTLSYGAAPMAPARIREAWERIGPI-LSQGYGASESTSGVT 313
Cdd:cd12117 217 ALGALIAEEGVTVLWLTAALFNQLAdEDPEC----FAGLRELLTGGEVVSPPHVRRVLAACPGLrLVNGYGPTENTTFTT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 314 RLSTADHAEAIAGRPgrlasCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDG------- 386
Cdd:cd12117 293 SHVVTELDEVAGSIP-----IGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADpfgpger 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 387 WLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGesvKAVVA-LRPGRALEA 465
Cdd:cd12117 368 LYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGD---KRLVAyVVAEGALDA 444
|
490 500 510
....*....|....*....|....*....|....*..
gi 1092251577 466 AALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARK 502
Cdd:cd12117 445 AELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRR 481
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
27-504 |
7.54e-52 |
|
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: 182.80 E-value: 7.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 27 LSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVENCTPRAFIGGD 106
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 107 GytgyarttpgfaaveafvalggpaagylgyEDLLarggtsrpphraaaadaaVLHFSSGSTGRIKAAVQSYGNRMASLR 186
Cdd:cd05907 86 P------------------------------DDLA------------------TIIYTSGTTGRPKGVMLSHRNILSNAL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 187 KMLLGMDrqARPGDRLALIGPVTHASGMLMQPF--LYCGATLVLFDRFEpaHFLAEVARLRITHVFMVP-------AMIH 257
Cdd:cd05907 118 ALAERLP--ATEGDRHLSFLPLAHVFERRAGLYvpLLAGARIYFASSAE--TLLDDLSEVRPTVFLAVPrvwekvyAAIK 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 258 MLLADPA----LEQADLSSLKTLSYGAAPMaPARIREAWERIG-PILsQGYGASESTSGVTrlstADHAEAIagrpgRLA 332
Cdd:cd05907 194 VKAVPGLkrklFDLAVGGRLRFAASGGAPL-PAELLHFFRALGiPVY-EGYGLTETSAVVT----LNPPGDN-----RIG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 333 SCGRPHGETEVRVVDEqgrevegdaiGEIVIRGEDVFQGYWGEPELTREVLV-DGWLRTGDLARVDEEGFIYLVDRKKDM 411
Cdd:cd05907 263 TVGKPLPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDaDGWLHTGDLGEIDEDGFLHITGRKKDL 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 412 II-SGGFNVYPTEVEAVLYQHPDVMEACVIsvpdatwGESVKAVVAL--------------------RPGRALEAAALIA 470
Cdd:cd05907 333 IItSGGKNISPEPIENALKASPLISQAVVI-------GDGRPFLVALivpdpealeawaeehgiaytDVAELAANPAVRA 405
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1092251577 471 HCRERI-------ADYKTPRSVEFV--------GELpkNPSGKVARKVV 504
Cdd:cd05907 406 EIEAAVeaanarlSRYEQIKKFLLLpepftienGEL--TPTLKLKRPVI 452
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
49-505 |
1.27e-51 |
|
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: 182.25 E-value: 1.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 49 RPGDRVAVQSRNCAELVEIECALYKSG----LVKAALNPRFTAAEASDVVENCTPRAFIGGDGYTgyARTTPGFAAVeaf 124
Cdd:cd05922 16 VRGERVVLILPNRFTYIELSFAVAYAGgrlgLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAA--DRLRDALPAS--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 125 valggPAAGYLGYEDLLARGGTSRPPHRAAAADAAVLHFSSGSTGRIKAAVQSYGNRMASLRKM--LLGMDrqarPGDRL 202
Cdd:cd05922 91 -----PDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIaeYLGIT----ADDRA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 203 ALIGPVTHASGM-LMQPFLYCGATLVLFDRFE-PAHFLAEVARLRITHVFMVPAMIHMLLAdPALEQADLSSLKTLSYGA 280
Cdd:cd05922 162 LTVLPLSYDYGLsVLNTHLLRGATLVLTNDGVlDDAFWEDLREHGATGLAGVPSTYAMLTR-LGFDPAKLPSLRYLTQAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 281 APMAPARIREAWERI-GPILSQGYGASESTSgvtRLSTADhAEAIAGRPGrlaSCGRPHGETEVRVVDEQGREVEGDAIG 359
Cdd:cd05922 241 GRLPQETIARLRELLpGAQVYVMYGQTEATR---RMTYLP-PERILEKPG---SIGLAIPGGEFEILDDDGTPTPPGEPG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 360 EIVIRGEDVFQGYW-GEPELTREVLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEAC 438
Cdd:cd05922 314 EIVHRGPNVMKGYWnDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAA 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092251577 439 VISVPDaTWGESVKAVVALRPGraLEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVR 505
Cdd:cd05922 394 AVGLPD-PLGEKLALFVTAPDK--IDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
49-506 |
6.29e-51 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 182.49 E-value: 6.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 49 RPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVENCTPRAFIGGDGYTGYARttpgfaaveafvALG 128
Cdd:PLN02330 78 RKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVK------------GLG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 129 GPA--------AGYLGYEDLLA---RGGTSRPPHRAAAADAAVLHFSSGSTGRIKAAVQSYGNRMASLRKMLLGMdrqar 197
Cdd:PLN02330 146 LPVivlgeekiEGAVNWKELLEaadRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSV----- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 198 pgdRLALIGPVThASGMLmqPFLY-------CGATL------VLFDRFEPAHFLAEVARLRITHVFMVPAMIHMLLADPA 264
Cdd:PLN02330 221 ---GPEMIGQVV-TLGLI--PFFHiygitgiCCATLrnkgkvVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPI 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 265 LEQADLSSLK--TLSYGAAPMAPaRIREAWERIGP--ILSQGYGASESTSGVTRLSTADHAEAIAGRpgrlASCGRPHGE 340
Cdd:PLN02330 295 VEEFDLSKLKlqAIMTAAAPLAP-ELLTAFEAKFPgvQVQEAYGLTEHSCITLTHGDPEKGHGIAKK----NSVGFILPN 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 341 TEVRVVD-EQGREVEGDAIGEIVIRGEDVFQGYWGEPELT-REVLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFN 418
Cdd:PLN02330 370 LEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETdRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQ 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 419 VYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGK 498
Cdd:PLN02330 450 VAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGK 529
|
....*...
gi 1092251577 499 VARKVVRE 506
Cdd:PLN02330 530 IMRRLLKE 537
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
196-498 |
6.64e-51 |
|
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: 177.96 E-value: 6.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 196 ARPGDRLALIGPVTHASGMLMQPFLYCGATLVLF--DRFEPAHFLAEVARLRITHVFMVPAMIHMLLADpALEQA---DL 270
Cdd:cd05924 55 AAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTVVLpdDRFDPEEVWRTIEKHKVTSMTIVGDAMARPLID-ALRDAgpyDL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 271 SSLKTLSYGAAPMAPaRIREAWERIGP--ILSQGYGASESTSGVTRLSTADHAEAiagrpgrlASCGRPHGETEVrvVDE 348
Cdd:cd05924 134 SSLFAISSGGALLSP-EVKQGLLELVPniTLVDAFGSSETGFTGSGHSAGSGPET--------GPFTRANPDTVV--LDD 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 349 QGREVE--GDAIGEIVIRGEdVFQGYWGEPELTRE--VLVDG--WLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPT 422
Cdd:cd05924 203 DGRVVPpgSGGVGWIARRGH-IPLGYYGDEAKTAEtfPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPE 281
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092251577 423 EVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGK 498
Cdd:cd05924 282 EVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
166-505 |
2.47e-49 |
|
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: 173.44 E-value: 2.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 166 GSTGRIKAAVQSYGNRMASLRKMLLGMDRQarPGDRLALIGPVTHASGMLMQPF--LYCGATLVLFDrfePA-------- 235
Cdd:cd05944 12 GTTGTPKLAQHTHSNEVYNAWMLALNSLFD--PDDVLLCGLPLFHVNGSVVTLLtpLASGAHVVLAG---PAgyrnpglf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 236 -HFLAEVARLRITHVFMVPAMIHMLLADPAleQADLSSLKTLSYGAAPMaPARIREAWE-RIGPILSQGYGASESTSGVT 313
Cdd:cd05944 87 dNFWKLVERYRITSLSTVPTVYAALLQVPV--NADISSLRFAMSGAAPL-PVELRARFEdATGLPVVEGYGLTEATCLVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 314 RlstadhaeAIAGRPGRLASCGR--PHGETEVRVVDEQG---REVEGDAIGEIVIRGEDVFQGYWgEPELTREVLV-DGW 387
Cdd:cd05944 164 V--------NPPDGPKRPGSVGLrlPYARVRIKVLDGVGrllRDCAPDEVGEICVAGPGVFGGYL-YTEGNKNAFVaDGW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 388 LRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAA 467
Cdd:cd05944 235 LNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEE 314
|
330 340 350
....*....|....*....|....*....|....*....
gi 1092251577 468 LIAHCRERIADY-KTPRSVEFVGELPKNPSGKVARKVVR 505
Cdd:cd05944 315 LLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
6-506 |
4.25e-49 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 176.57 E-value: 4.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 6 FLQR-AARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPR 84
Cdd:TIGR02262 9 LLDRnVVEGRGGKTAFIDDISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 85 FTAAEASDVVENCTPRA-FIGGDGYTGYARTTPGFAAVEAFVALGGPAAGYLGYEDLLARGGTSRPPHRAAAADAAVLHF 163
Cdd:TIGR02262 89 LTADDYAYMLEDSRARVvFVSGALLPVIKAALGKSPHLEHRVVVGRPEAGEVQLAELLATESEQFKPAATQADDPAFWLY 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 164 SSGSTGRIKAAVQSYGN--RMASLR-KMLLGMdrqaRPGDRLALIGPVTHASGM---LMQPfLYCGATLVLF-DRFEPAH 236
Cdd:TIGR02262 169 SSGSTGMPKGVVHTHSNpyWTAELYaRNTLGI----REDDVCFSAAKLFFAYGLgnaLTFP-MSVGATTVLMgERPTPDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 237 FLAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMaPARIREAWE-RIGPILSQGYGASEStsGVTRL 315
Cdd:TIGR02262 244 VFDRLRRHQPTIFYGVPTLYAAMLADPNLPSEDQVRLRLCTSAGEAL-PAEVGQRWQaRFGVDIVDGIGSTEM--LHIFL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 316 STADHAEaiagrpgRLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDGWLRTGDLAR 395
Cdd:TIGR02262 321 SNLPGDV-------RYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTFQGEWTRSGDKYV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 396 VDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCRER 475
Cdd:TIGR02262 394 RNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTALETELKEHVKDR 473
|
490 500 510
....*....|....*....|....*....|.
gi 1092251577 476 IADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:TIGR02262 474 LAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
163-516 |
2.61e-48 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 175.42 E-value: 2.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 163 FSSGSTGRIKAAVQSYGNRMASLRKMLLGMDRQ-ARPGDR---LALIgPVTHASGM--LMQPFLYCGATLVLFDRFEPAH 236
Cdd:PLN02574 205 YSSGTTGASKGVVLTHRNLIAMVELFVRFEASQyEYPGSDnvyLAAL-PMFHIYGLslFVVGLLSLGSTIVVMRRFDASD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 237 FLAEVARLRITHVFMVPAMIHMLL-ADPALEQADLSSLKTLSYGAAPMAPARIREAWERIGPI-LSQGYGASESTSGVTR 314
Cdd:PLN02574 284 MVKVIDRFKVTHFPVVPPILMALTkKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVdFIQGYGMTESTAVGTR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 315 -LSTAdhaeaiagRPGRLASCGRPHGETEVRVVD-EQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLV-DGWLRTG 391
Cdd:PLN02574 364 gFNTE--------KLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDkDGWLRTG 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 392 DLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAH 471
Cdd:PLN02574 436 DIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINY 515
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1092251577 472 CRERIADYKTPRSVEFVGELPKNPSGKVARKVVREPYWQGVARRV 516
Cdd:PLN02574 516 VAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLTNSVSSRL 560
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
7-502 |
6.00e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 173.64 E-value: 6.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 7 LQRAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVeieCALYKSGLVKA---ALNP 83
Cdd:PRK13383 41 LAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFV---TAVFAVGLLGAdvvPIST 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 84 RFTAAEASDVVENCTPRAFIGGDGYTGYarttpgFAAVEAFVALGGPAAgyLGYEDLLARGGTSrPPHRaaaadaaVLHF 163
Cdd:PRK13383 118 EFRSDALAAALRAHHISTVVADNEFAER------IAGADDAVAVIDPAT--AGAEESGGRPAVA-APGR-------IVLL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 164 SSGSTGRIKAAVQSYGNRMASLRKMLLGMDRQARPGDRLALIGPVTHA--SGMLMQPfLYCGATLVLFDRFEPAHFLAEV 241
Cdd:PRK13383 182 TSGTTGKPKGVPRAPQLRSAVGVWVTILDRTRLRTGSRISVAMPMFHGlgLGMLMLT-IALGGTVLTHRHFDAEAALAQA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 242 ARLRITHVFMVPAMIHMLLADPALEQA--DLSSLKTLSYGAAPMAPARIREAWERIGPILSQGYGASEStsGVTRLST-A 318
Cdd:PRK13383 261 SLHRADAFTAVPVVLARILELPPRVRArnPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEV--GIGALATpA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 319 DHAEAIAgrpgrlaSCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEpelTREVLVDGWLRTGDLARVDE 398
Cdd:PRK13383 339 DLRDAPE-------TVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDG---GGKAVVDGMTSTGDMGYLDN 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 399 EGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCRERIAD 478
Cdd:PRK13383 409 AGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSR 488
|
490 500
....*....|....*....|....
gi 1092251577 479 YKTPRSVEFVGELPKNPSGKVARK 502
Cdd:PRK13383 489 FEQPRDINIVSSIPRNPTGKVLRK 512
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
7-499 |
1.10e-47 |
|
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: 174.30 E-value: 1.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 7 LQRAARYWGDRPAVMH------RERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAA 80
Cdd:cd17634 59 LDRHLRENGDRTAIIYegddtsQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 81 LNPRFTAAEASDVVENCTPRAFIGGDGYTGYARTTPGFAAV-EAF-----------------VALGGPAAGYLGYEDLLA 142
Cdd:cd17634 139 IFGGFAPEAVAGRIIDSSSRLLITADGGVRAGRSVPLKKNVdDALnpnvtsvehvivlkrtgSDIDWQEGRDLWWRDLIA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 143 RGGTSRPPHRAAAADAAVLHFSSGSTGRIKAAVQSYGNR-MASLRKMLLGMDrqARPGD---RLALIGPVTHASGMLMQP 218
Cdd:cd17634 219 KASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYlVYAATTMKYVFD--YGPGDiywCTADVGWVTGHSYLLYGP 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 219 fLYCGATLVLFDRF----EPAHFLAEVARLRITHVFMVPAMIHMLLA--DPALEQADLSSLKTLSYGAAPMAPARIREAW 292
Cdd:cd17634 297 -LACGATTLLYEGVpnwpTPARMWQVVDKHGVNILYTAPTAIRALMAagDDAIEGTDRSSLRILGSVGEPINPEAYEWYW 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 293 ERIG----PILSQGYGASESTSGVTRLSTADhaeaiagrPGRLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGE-- 366
Cdd:cd17634 376 KKIGkekcPVVDTWWQTETGGFMITPLPGAI--------ELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwp 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 367 DVFQGYWGEPELTREVLV---DGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVP 443
Cdd:cd17634 448 GQTRTLFGDHERFEQTYFstfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIP 527
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1092251577 444 DATWGESVKAVVALRPGRALE---AAALIAHCRERIADYKTPRSVEFVGELPKNPSGKV 499
Cdd:cd17634 528 HAIKGQAPYAYVVLNHGVEPSpelYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
6-506 |
2.22e-47 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 173.28 E-value: 2.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 6 FLQRAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRF 85
Cdd:PLN03102 19 FLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 86 TAAEASDVVENCTPRAFIGGDGYTGYARTT------------PGFAAVEAFVALGGPAAGYLGYEDLLARGgtsRPPHRA 153
Cdd:PLN03102 99 DATSIAAILRHAKPKILFVDRSFEPLAREVlhllssedsnlnLPVIFIHEIDFPKRPSSEELDYECLIQRG---EPTPSL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 154 AAADAAV--------LHFSSGSTGRIKAAVQSYGNRMASLRKMLLGMDRQARPGDRLALigPVTHASG-MLMQPFLYCGA 224
Cdd:PLN03102 176 VARMFRIqdehdpisLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTL--PMFHCNGwTFTWGTAARGG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 225 TLVLFDRFEPAHFLAEVARLRITHVFMVPAMIHMLLADPALEQADLSS-LKTLSYGAAPmaPARIREAWERIGPILSQGY 303
Cdd:PLN03102 254 TSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGpVHVLTGGSPP--PAALVKKVQRLGFQVMHAY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 304 GASESTSGV---------TRLSTADHAEaIAGRPGRlascgRPHGETEVRVVDEQGREV---EGDAIGEIVIRGEDVFQG 371
Cdd:PLN03102 332 GLTEATGPVlfcewqdewNRLPENQQME-LKARQGV-----SILGLADVDVKNKETQESvprDGKTMGEIVIKGSSIMKG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 372 YWGEPELTREVLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESV 451
Cdd:PLN03102 406 YLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETP 485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092251577 452 KAVVALRPGRALEAAA----------LIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:PLN03102 486 CAFVVLEKGETTKEDRvdklvtrerdLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRD 550
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
9-505 |
5.49e-47 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 172.00 E-value: 5.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 9 RAARYWGDRpavmHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAA 88
Cdd:PRK04319 60 KVALRYLDA----SRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 89 EASDVVENCTPRAFIGGDgyTGYAR----TTPGFAAVEAFVALGGPAAGYLGYEDLLARGGTSRPPHRAAAADAAVLHFS 164
Cdd:PRK04319 136 AVRDRLEDSEAKVLITTP--ALLERkpadDLPSLKHVLLVGEDVEEGPGTLDFNALMEQASDEFDIEWTDREDGAILHYT 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 165 SGSTGRIKAAVQSYGnrmASLRKMLLGmdRQA---RPGDRL---ALIGPVTHASGMLMQPFLyCGATLVLF-DRFEPAHF 237
Cdd:PRK04319 214 SGSTGKPKGVLHVHN---AMLQHYQTG--KYVldlHEDDVYwctADPGWVTGTSYGIFAPWL-NGATNVIDgGRFSPERW 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 238 LAEVARLRITHVFMVPAMIHMLL--ADPALEQADLSSLK-TLSYGAaPMAPARIREAWERIG-PILSqgygasestsgvT 313
Cdd:PRK04319 288 YRILEDYKVTVWYTAPTAIRMLMgaGDDLVKKYDLSSLRhILSVGE-PLNPEVVRWGMKVFGlPIHD------------N 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 314 RLSTADHAEAIAGRPG---RLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGE--DVFQGYWGEPELTREVLVDGWL 388
Cdd:PRK04319 355 WWMTETGGIMIANYPAmdiKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGwpSMMRGIWNNPEKYESYFAGDWY 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 389 RTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAA-- 466
Cdd:PRK04319 435 VSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEElk 514
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1092251577 467 -ALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVR 505
Cdd:PRK04319 515 eEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
3-508 |
2.79e-46 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 170.67 E-value: 2.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 3 FALFLQRAARYwGDRPAVMHRE----RVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVK 78
Cdd:COG1022 14 PDLLRRRAARF-PDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 79 AALNPRFTAAEASDVVENCTPRAFIGGDGYTgYARTTP---GFAAVEAFVALGGPAA----GYLGYEDLLARGGTSRPPH 151
Cdd:COG1022 93 VPIYPTSSAEEVAYILNDSGAKVLFVEDQEQ-LDKLLEvrdELPSLRHIVVLDPRGLrddpRLLSLDELLALGREVADPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 152 RAAAADAAV-------LHFSSGSTGRIKAAVQSYGNrMASLRKMLLGMDrQARPGDRLALIGPVTHASG-MLMQPFLYCG 223
Cdd:COG1022 172 ELEARRAAVkpddlatIIYTSGTTGRPKGVMLTHRN-LLSNARALLERL-PLGPGDRTLSFLPLAHVFErTVSYYALAAG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 224 ATLVlFDRfEPAHFLAEVARLRITHVFMVP---------AMIHM--------LLADPALEQA-----------DLSSLKT 275
Cdd:COG1022 250 ATVA-FAE-SPDTLAEDLREVKPTFMLAVPrvwekvyagIQAKAeeagglkrKLFRWALAVGrryararlagkSPSLLLR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 276 LSY------------------------GAAPMAPaRIREAWERIG-PILsQGYGASEsTSGVTrlsTADHAEAIagRPGr 330
Cdd:COG1022 328 LKHaladklvfsklrealggrlrfavsGGAALGP-ELARFFRALGiPVL-EGYGLTE-TSPVI---TVNRPGDN--RIG- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 331 laSCGRPHGETEVRVVDEqgrevegdaiGEIVIRGEDVFQGYWGEPELTREVL-VDGWLRTGDLARVDEEGFIYLVDRKK 409
Cdd:COG1022 399 --TVGPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFdADGWLHTGDIGELDEDGFLRITGRKK 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 410 DMII-SGGFNVYPTEVEAVLYQHPDVMEACVIS----------VPD----ATWGESvKAVVALRPGRALEAAALIAHCRE 474
Cdd:COG1022 467 DLIVtSGGKNVAPQPIENALKASPLIEQAVVVGdgrpflaaliVPDfealGEWAEE-NGLPYTSYAELAQDPEVRALIQE 545
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1092251577 475 RIADYK-------TPRSVEFV--------GELpkNPSGKVARKVVREPY 508
Cdd:COG1022 546 EVDRANaglsraeQIKRFRLLpkeftienGEL--TPTLKLKRKVILEKY 592
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
49-505 |
8.12e-46 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 168.82 E-value: 8.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 49 RPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVENCTPRAFIGGDGYTGYAR--TTPGFAAVEAFVA 126
Cdd:PLN02860 55 RNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETCSSWYEelQNDRLPSLMWQVF 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 127 LGGP-------AAGYLGYEDLLARGGTSRPPHRAAAADAAVL-HFSSGSTGRIKAAVQSYGNRMA-SLRKM-LLGMDR-- 194
Cdd:PLN02860 135 LESPsssvfifLNSFLTTEMLKQRALGTTELDYAWAPDDAVLiCFTSGTTGRPKGVTISHSALIVqSLAKIaIVGYGEdd 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 195 ---QARPgdrLALIGPVTHASGMLMqpflyCGATLVLFDRFEPAHFLAEVARLRITHVFMVPAMIHMLLADPALEQADLS 271
Cdd:PLN02860 215 vylHTAP---LCHIGGLSSALAMLM-----VGACHVLLPKFDAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKV 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 272 --SLKTLSYGAAPMaPARIREAWERIGP---ILSqGYGASESTSGVT-------RLSTADHAEAIAGRPGRLA------S 333
Cdd:PLN02860 287 fpSVRKILNGGGSL-SSRLLPDAKKLFPnakLFS-AYGMTEACSSLTfmtlhdpTLESPKQTLQTVNQTKSSSvhqpqgV 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 334 C-GRPHGETEVRV-VDEQGREvegdaiGEIVIRGEDVFQGYWGEPELTREVLV-DGWLRTGDLARVDEEGFIYLVDRKKD 410
Cdd:PLN02860 365 CvGKPAPHVELKIgLDESSRV------GRILTRGPHVMLGYWGQNSETASVLSnDGWLDTGDIGWIDKAGNLWLIGRSND 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 411 MIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPG--------------RALEAAALIAHCRER- 475
Cdd:PLN02860 439 RIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGwiwsdnekenakknLTLSSETLRHHCREKn 518
|
490 500 510
....*....|....*....|....*....|.
gi 1092251577 476 IADYKTPRS-VEFVGELPKNPSGKVARKVVR 505
Cdd:PLN02860 519 LSRFKIPKLfVQWRKPFPLTTTGKIRRDEVR 549
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
223-502 |
4.71e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 164.78 E-value: 4.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 223 GATLVLFDRFEPAHFlAEVARLRITHVFMVPAMIHMLLADPALEQAdLSSLKTLSYGAAPM-AP--ARIREAwerIGPIL 299
Cdd:PRK07787 195 GNRFVHTGRPTPEAY-AQALSEGGTLYFGVPTVWSRIAADPEAARA-LRGARLLVSGSAALpVPvfDRLAAL---TGHRP 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 300 SQGYGASESTSGVTRLSTADHaeaiagRPGrlaSCGRPHGETEVRVVDEQGREV--EGDAIGEIVIRGEDVFQGYWGEPE 377
Cdd:PRK07787 270 VERYGMTETLITLSTRADGER------RPG---WVGLPLAGVETRLVDEDGGPVphDGETVGELQVRGPTLFDGYLNRPD 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 378 LTREVLV-DGWLRTGDLARVDEEGFIYLVDRKK-DMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVV 455
Cdd:PRK07787 341 ATAAAFTaDGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYV 420
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1092251577 456 AlrPGRALEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARK 502
Cdd:PRK07787 421 V--GADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKK 465
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
15-502 |
7.78e-45 |
|
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: 164.00 E-value: 7.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 15 GDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVV 94
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 95 ENCTPRAFI----GGDGYTGYARTTPgfaaveafvaLGGPAAGYLGyedlLARGGTSRPPHraaaadAAVLHFSSGSTGR 170
Cdd:cd12116 81 EDAEPALVLtddaLPDRLPAGLPVLL----------LALAAAAAAP----AAPRTPVSPDD------LAYVIYTSGSTGR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 171 IKAAVQSYGNRMASLRKM--LLGMdrqaRPGDRLALIGPVT-HASGMLMQPFLYCGATLVLFDR---FEPAHFLAEVARL 244
Cdd:cd12116 141 PKGVVVSHRNLVNFLHSMreRLGL----GPGDRLLAVTTYAfDISLLELLLPLLAGARVVIAPRetqRDPEALARLIEAH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 245 RITHVFMVPAMIHMLLADpalEQADLSSLKTLSYGAA---PMAP---ARIREAWerigpilsQGYGASEST--SGVTRLS 316
Cdd:cd12116 217 SITVMQATPATWRMLLDA---GWQGRAGLTALCGGEAlppDLAArllSRVGSLW--------NLYGPTETTiwSTAARVT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 317 TADHAEAIagrpgrlascGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDG--------WL 388
Cdd:cd12116 286 AAAGPIPI----------GRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDpfagpgsrLY 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 389 RTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVkAVVALRPGRALEAAAL 468
Cdd:cd12116 356 RTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVLKAGAAPDAAAL 434
|
490 500 510
....*....|....*....|....*....|....
gi 1092251577 469 IAHCRERIADYKTPRSVEFVGELPKNPSGKVARK 502
Cdd:cd12116 435 RAHLRATLPAYMVPSAFVRLDALPLTANGKLDRK 468
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
1-506 |
8.60e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 165.30 E-value: 8.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 1 MAFALFLQRAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAA 80
Cdd:PRK06164 10 DTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 81 LNPRFTAAEASDVVENCTPRAFIGGDGYTGY-------------ARTTPGFAAV-EAFVALGGPAAGylGYEDLLARGGT 146
Cdd:PRK06164 90 VNTRYRSHEVAHILGRGRARWLVVWPGFKGIdfaailaavppdaLPPLRAIAVVdDAADATPAPAPG--ARVQLFALPDP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 147 SRPP---HRAAAADAAVLHF-SSGSTGRIKAAVQSYGN--RMASLRKMLLGMDrqarPGDRLALIGPVTHASGMLMQ-PF 219
Cdd:PRK06164 168 APPAaagERAADPDAGALLFtTSGTTSGPKLVLHRQATllRHARAIARAYGYD----PGAVLLAALPFCGVFGFSTLlGA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 220 LYCGATLVLFDRFEPAHFLAEVARLRITHVFMVPAMIHMLLaDPALEQADLSSLKTLSYGAAPMAPARIREAWERIGPIL 299
Cdd:PRK06164 244 LAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRIL-DTAGERADFPSARLFGFASFAPALGELAALARARGVPL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 300 SQGYGASESTSGVTrLSTADHAEAIAGRPGrlascGRP-HGETEVRVVDEQGREVEGD-AIGEIVIRGEDVFQGYWGEPE 377
Cdd:PRK06164 323 TGLYGSSEVQALVA-LQPATDPVSVRIEGG-----GRPaSPEARVRARDPQDGALLPDgESGEIEIRAPSLMRGYLDNPD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 378 LTREVLV-DGWLRTGDLAR-VDEEGFIYlVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVkAVV 455
Cdd:PRK06164 397 ATARALTdDGYFRTGDLGYtRGDGQFVY-QTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPV-AFV 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1092251577 456 ALRPGRALEAAALIAHCRERIADYKTPRSVEFVGELPKNPSG---KVARKVVRE 506
Cdd:PRK06164 475 IPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLRE 528
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
133-509 |
1.84e-44 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 164.18 E-value: 1.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 133 GYLGYEDLLARGGTSRPPHRAAAADAAVLHFSSGSTGRIKAAVQSYGNrmaslrkMLLGMDRQAR------PGD---RLA 203
Cdd:cd05928 151 GWLNFKELLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSS-------LGLGLKVNGRywldltASDimwNTS 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 204 LIGPVTHASGMLMQPFLyCGATLV--LFDRFEPAHFLAEVARLRITHVFMVPAMIHMLLadpaleQADLSSLKTLSY--- 278
Cdd:cd05928 224 DTGWIKSAWSSLFEPWI-QGACVFvhHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLV------QQDLSSYKFPSLqhc 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 279 --GAAPMAPaRIREAW-ERIGPILSQGYGASEstsgvTRLSTADHaEAIAGRPGrlaSCGRPHGETEVRVVDEQGREVEG 355
Cdd:cd05928 297 vtGGEPLNP-EVLEKWkAQTGLDIYEGYGQTE-----TGLICANF-KGMKIKPG---SMGKASPPYDVQIIDDNGNVLPP 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 356 DAIGEIVIRGEDV-----FQGYWGEPELTREVLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQ 430
Cdd:cd05928 367 GTEGDIGIRVKPIrpfglFSGYVDNPEKTAATIRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIE 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 431 HPDVMEACVISVPDATWGESVKAVVALRP---GRALEA--AALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVR 505
Cdd:cd05928 447 HPAVVESAVVSSPDPIRGEVVKAFVVLAPqflSHDPEQltKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELR 526
|
....
gi 1092251577 506 EPYW 509
Cdd:cd05928 527 DKEW 530
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
9-505 |
2.35e-44 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 164.01 E-value: 2.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 9 RAARYWGDRP--------------AVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKS 74
Cdd:PRK10946 17 REKGYWQDLPltdiltrhaasdaiAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 75 GLvkAALNPRFT--AAEASDVVENCTPRAFIG--------GDGYTGYARTTPGFAAVeafVALGGpAAGYLGYEDLLARG 144
Cdd:PRK10946 97 GV--APVNALFShqRSELNAYASQIEPALLIAdrqhalfsDDDFLNTLVAEHSSLRV---VLLLN-DDGEHSLDDAINHP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 145 GTSRPPHRAAAADAAVLHFSSGSTGRIKAAVQSYGNRMASLRKM--LLGMDRQARpgdRL-ALigPVTHaSGMLMQP--- 218
Cdd:PRK10946 171 AEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSveICGFTPQTR---YLcAL--PAAH-NYPMSSPgal 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 219 -FLYCGATLVLFDRFEPAHFLAEVARLRITHVFMVPAMIHMLLADPALE--QADLSSLKTLSYGAAPMAPARIREAWERI 295
Cdd:PRK10946 245 gVFLAGGTVVLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGgsRAQLASLKLLQVGGARLSETLARRIPAEL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 296 GPILSQGYGASESTSGVTRLStaDHAEAIAGRPGRLAScgrphGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGE 375
Cdd:PRK10946 325 GCQLQQVFGMAEGLVNYTRLD--DSDERIFTTQGRPMS-----PDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 376 PELTREVL-VDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAV 454
Cdd:PRK10946 398 PQHNASAFdANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAF 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1092251577 455 VALRpgRALEAAALIAHCRER-IADYKTPRSVEFVGELPKNPSGKVARKVVR 505
Cdd:PRK10946 478 LVVK--EPLKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLR 527
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
27-505 |
8.45e-44 |
|
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: 160.38 E-value: 8.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 27 LSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGlvkAALNPRFTAAeasdvvencTPRAFiggd 106
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLG---AVYQPLFTAF---------GPKAI---- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 107 gytgyartTPGFAAVEAFVALGGPAAGYLGYEDLLarggtsrpphraaaadaaVLHFSSGSTGRIKAAVQSYGNRMASLR 186
Cdd:cd05973 65 --------EHRLRTSGARLVVTDAANRHKLDSDPF------------------VMMFTSGTTGLPKGVPVPLRALAAFGA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 187 KMLLGMDrqARPGDRLALIGPVTHASGM---LMQPFLYCGATLVLFDRFEPAHFLAEVARLRITHVFMVPAMIHMLLADP 263
Cdd:cd05973 119 YLRDAVD--LRPEDSFWNAADPGWAYGLyyaITGPLALGHPTILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAG 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 264 ALEQADLS-SLKTLSYGAAPMAPARIREAWERIGPILSQGYGASEstsgVTRLSTADHAEAiagRPGRLASCGRPHGETE 342
Cdd:cd05973 197 AEVPARPKgRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTE----LGMVLANHHALE---HPVHAGSAGRAMPGWR 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 343 VRVVDEQGREVEGDAIGEIVIrgeDV-------FQGYWGEPELTrevLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISG 415
Cdd:cd05973 270 VAVLDDDGDELGPGEPGRLAI---DIansplmwFRGYQLPDTPA---IDGGYYLTGDTVEFDPDGSFSFIGRADDVITMS 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 416 GFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPG-RALE--AAALIAHCRERIADYKTPRSVEFVGELP 492
Cdd:cd05973 344 GYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGhEGTPalADELQLHVKKRLSAHAYPRTIHFVDELP 423
|
490
....*....|...
gi 1092251577 493 KNPSGKVARKVVR 505
Cdd:cd05973 424 KTPSGKIQRFLLR 436
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
6-505 |
1.05e-43 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 162.71 E-value: 1.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 6 FLQRAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRF 85
Cdd:PLN02479 25 FLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 86 TAAEASDVVENCTPRAFIGGDGYTGYARTTPGFAAVEA--------FVALGGP-----------AAGYLGYEDLLARGGT 146
Cdd:PLN02479 105 NAPTIAFLLEHSKSEVVMVDQEFFTLAEEALKILAEKKkssfkpplLIVIGDPtcdpkslqyalGKGAIEYEKFLETGDP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 147 S---RPPhrAAAADAAVLHFSSGSTGRIKAAVQSY-GNRMASLRKMLL-GMDRQARPGDRLaligPVTHASGMLMQPFL- 220
Cdd:PLN02479 185 EfawKPP--ADEWQSIALGYTSGTTASPKGVVLHHrGAYLMALSNALIwGMNEGAVYLWTL----PMFHCNGWCFTWTLa 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 221 -YCGATLVLFDRFEPAHFLAeVARLRITHVFMVPAMIHMLLADPALEQA-DLSSL-KTLSYGAAPmaPARIREAWERIGP 297
Cdd:PLN02479 259 aLCGTNICLRQVTAKAIYSA-IANYGVTHFCAAPVVLNTIVNAPKSETIlPLPRVvHVMTAGAAP--PPSVLFAMSEKGF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 298 ILSQGYGASESTSGVTRLSTADHAEAIAgrpgrLASCGRPHGETEVRVVDEQGREV-----------EGDAIGEIVIRGE 366
Cdd:PLN02479 336 RVTHTYGLSETYGPSTVCAWKPEWDSLP-----PEEQARLNARQGVRYIGLEGLDVvdtktmkpvpaDGKTMGEIVMRGN 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 367 DVFQGYWGEPELTREVLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDAT 446
Cdd:PLN02479 411 MVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDER 490
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092251577 447 WGESVKAVVALRPG-----RALEAAALIAHCRERIADYKTPRSVEFvGELPKNPSGKVARKVVR 505
Cdd:PLN02479 491 WGESPCAFVTLKPGvdksdEAALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLR 553
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
28-439 |
3.32e-42 |
|
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: 155.50 E-value: 3.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 28 SFRQLDERSTRLANA-LLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVENCTPRAFIggd 106
Cdd:TIGR01733 1 TYRELDERANRLARHlRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 107 gytgyarTTPGFAAVEAFValgGPAAGYLGYEDLLARGGTSRPPHRAAAADAA----VLhFSSGSTGRIKAAVQSYG--- 179
Cdd:TIGR01733 78 -------TDSALASRLAGL---VLPVILLDPLELAALDDAPAPPPPDAPSGPDdlayVI-YTSGSTGRPKGVVVTHRslv 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 180 NRMASLRKMLLGmdrqaRPGDRLALIGPVTH-ASGMLMQPFLYCGATLVLFDRFEPAHFLAEVARLR----ITHVFMVPA 254
Cdd:TIGR01733 147 NLLAWLARRYGL-----DPDDRVLQFASLSFdASVEEIFGALLAGATLVVPPEDEERDDAALLAALIaehpVTVLNLTPS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 255 MIHMLLAdpaLEQADLSSLKTLSYGAAPMAPARIREAWERIGPI-LSQGYGASESTSGVTRLSTADHAEaiagRPGRLAS 333
Cdd:TIGR01733 222 LLALLAA---ALPPALASLRLVILGGEALTPALVDRWRARGPGArLINLYGPTETTVWSTATLVDPDDA----PRESPVP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 334 CGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDG---------WLRTGDLARVDEEGFIYL 404
Cdd:TIGR01733 295 IGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDpfaggdgarLYRTGDLVRYLPDGNLEF 374
|
410 420 430
....*....|....*....|....*....|....*
gi 1092251577 405 VDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACV 439
Cdd:TIGR01733 375 LGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
16-502 |
1.30e-41 |
|
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: 154.83 E-value: 1.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 16 DRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVE 95
Cdd:cd17649 2 DAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 96 NctprafiggdgytgyarttpgfAAVEAFVALGGPAAGYLGYedllarggtsrpphraaaadaavlhfSSGSTGRIKAAV 175
Cdd:cd17649 82 D----------------------SGAGLLLTHHPRQLAYVIY--------------------------TSGSTGTPKGVA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 176 QSYGNRMASLRKML--LGMdrqaRPGDRLALIGPVTH--ASGMLMQPfLYCGATLVLFD--RFEPAHFLAE-VARLRITH 248
Cdd:cd17649 114 VSHGPLAAHCQATAerYGL----TPGDRELQFASFNFdgAHEQLLPP-LICGACVVLRPdeLWASADELAEmVRELGVTV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 249 VFMVPAMIHMLLADPALEQADLS-SLKTLSYGAAPMAPARIReAWERIGPILSQGYGASESTsgVTrlSTADHAEAIAGR 327
Cdd:cd17649 189 LDLPPAYLQQLAEEADRTGDGRPpSLRLYIFGGEALSPELLR-RWLKAPVRLFNAYGPTEAT--VT--PLVWKCEAGAAR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 328 PGRLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDG--------WLRTGDLARVDEE 399
Cdd:cd17649 264 AGASMPIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDpfgapgsrLYRTGDLARWRDD 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 400 GFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATwGESVKAVVALRPGRALEA--AALIAHCRERIA 477
Cdd:cd17649 344 GVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG-GKQLVAYVVLRAAAAQPElrAQLRTALRASLP 422
|
490 500
....*....|....*....|....*
gi 1092251577 478 DYKTPRSVEFVGELPKNPSGKVARK 502
Cdd:cd17649 423 DYMVPAHLVFLARLPLTPNGKLDRK 447
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
163-501 |
1.51e-40 |
|
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: 149.33 E-value: 1.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 163 FSSGSTGRIKAAVQSYGNRMASLrKMLLGMDRQARPGDRLALIGPVTHASGML-MQPFLYCGATLVLF-DRFEPAHFLAE 240
Cdd:cd17635 8 FTSGTTGEPKAVLLANKTFFAVP-DILQKEGLNWVVGDVTYLPLPATHIGGLWwILTCLIHGGLCVTGgENTTYKSLFKI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 241 VARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIREAWERIGPILSQGYGASEsTSGVTRLSTADH 320
Cdd:cd17635 87 LTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSE-TGTALCLPTDDD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 321 AEAIAgrpgrlaSCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDGWLRTGDLARVDEEG 400
Cdd:cd17635 166 SIEIN-------AVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGERREDG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 401 FIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAA-ALIAHCRERIADY 479
Cdd:cd17635 239 FLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAIrALKHTIRRELEPY 318
|
330 340
....*....|....*....|..
gi 1092251577 480 KTPRSVEFVGELPKNPSGKVAR 501
Cdd:cd17635 319 ARPSTIVIVTDIPRTQSGKVKR 340
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
4-516 |
2.11e-40 |
|
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: 156.56 E-value: 2.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 4 ALFLQRAARYwGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVeieCALY---KSGlvkAA 80
Cdd:COG1020 480 ELFEAQAART-PDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMV---VALLavlKAG---AA 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 81 ---LNPRFTAAEASDVVENCTPRAFIggdgytgyarTTPGFAAveafvALGGPAAGYLGYEDLLARGGTSRPPHRAAAAD 157
Cdd:COG1020 553 yvpLDPAYPAERLAYMLEDAGARLVL----------TQSALAA-----RLPELGVPVLALDALALAAEPATNPPVPVTPD 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 158 AA--VLhFSSGSTGRIKAAVQSYG---NRMASLRKMLlgmdrQARPGDRLALIGPVTH-ASGMLMQPFLYCGATLVLFD- 230
Cdd:COG1020 618 DLayVI-YTSGSTGRPKGVMVEHRalvNLLAWMQRRY-----GLGPGDRVLQFASLSFdASVWEIFGALLSGATLVLAPp 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 231 --RFEPAHFLAEVARLRITHVFMVPAMIHMLLADPAleqADLSSLKTLSYGAAPMAPARIREAWERI-GPILSQGYGASE 307
Cdd:COG1020 692 eaRRDPAALAELLARHRVTVLNLTPSLLRALLDAAP---EALPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTE 768
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 308 STSGVTrLSTADHAEAIAGRPgrlaSCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDG- 386
Cdd:COG1020 769 TTVDST-YYEVTPPDADGGSV----PIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADp 843
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 387 -------WLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRP 459
Cdd:COG1020 844 fgfpgarLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEA 923
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1092251577 460 GRALEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVREPYWQGVARRV 516
Cdd:COG1020 924 GAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAA 980
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
12-506 |
8.26e-40 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 150.02 E-value: 8.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 12 RYW----GDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTA 87
Cdd:PRK09029 10 RHWaqvrPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 88 AEASDVVENCTPRafiggdgytgyarttpgfaaveaFVALGGPAAGYLGYEDLLARGGTSRPPHRAAAADAAVLHFSSGS 167
Cdd:PRK09029 90 PLLEELLPSLTLD-----------------------FALVLEGENTFSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 168 TGRIKAAVQSYGNRMASLRKMLLGMDRQArpGDRLALIGPVTHASGM-LMQPFLYCGATLVLFDrfePAHFLAEVARlrI 246
Cdd:PRK09029 147 TGLPKAAVHTAQAHLASAEGVLSLMPFTA--QDSWLLSLPLFHVSGQgIVWRWLYAGATLVVRD---KQPLEQALAG--C 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 247 THVFMVPAMIHMLLADPALEqadlSSLKTLSYGAApMAPARIREAWERIGpILSQ-GYGASESTSGVTrlstadhAEAIA 325
Cdd:PRK09029 220 THASLVPTQLWRLLDNRSEP----LSLKAVLLGGA-AIPVELTEQAEQQG-IRCWcGYGLTEMASTVC-------AKRAD 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 326 GRPGrlasCGRPHGETEVRVVDeqgrevegdaiGEIVIRGEDVFQGYWGEPELTreVLVD--GWLRTGDLARVDEeGFIY 403
Cdd:PRK09029 287 GLAG----VGSPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQLV--PLVNdeGWFATRDRGEWQN-GELT 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 404 LVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEaaALIAHCRERIADYKTPr 483
Cdd:PRK09029 349 ILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESDSEAAVV--NLAEWLQDKLARFQQP- 425
|
490 500
....*....|....*....|....*.
gi 1092251577 484 sVEFVgELP---KNPSGKVARKVVRE 506
Cdd:PRK09029 426 -VAYY-LLPpelKNGGIKISRQALKE 449
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
7-508 |
1.01e-39 |
|
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: 152.26 E-value: 1.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 7 LQRAARYWGDRPAVMHR-----ERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAAL 81
Cdd:cd05968 67 LDKWLADTRTRPALRWEgedgtSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 82 NPRFTAAEASDVVENCTPRAFIGGDGYT-------------GYARTTPGFAAVEAFVALGGPA----AGYLGYEDLLArg 144
Cdd:cd05968 147 FSGFGKEAAATRLQDAEAKALITADGFTrrgrevnlkeeadKACAQCPTVEKVVVVRHLGNDFtpakGRDLSYDEEKE-- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 145 gtSRPPH--RAAAADAAVLHFSSGSTGRIKAAVQSY-GNRMASLRKMLLGMDrqARPGDRLALIGPVthasGMLMQPFLY 221
Cdd:cd05968 225 --TAGDGaeRTESEDPLMIIYTSGTTGKPKGTVHVHaGFPLKAAQDMYFQFD--LKPGDLLTWFTDL----GWMMGPWLI 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 222 CG-----ATLVLFDRFePAHFLAE-----VARLRITHVFMVPAMIHMLLA--DPALEQADLSSLKTLSYGAAPMAPARIR 289
Cdd:cd05968 297 FGglilgATMVLYDGA-PDHPKADrlwrmVEDHEITHLGLSPTLIRALKPrgDAPVNAHDLSSLRVLGSTGEPWNPEPWN 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 290 EAWERIG----PILSQgygasestSGVTRLSTAdhaeaIAG----RPGRLASCGRPHGETEVRVVDEQGREVEGDaIGEI 361
Cdd:cd05968 376 WLFETVGkgrnPIINY--------SGGTEISGG-----ILGnvliKPIKPSSFNGPVPGMKADVLDESGKPARPE-VGEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 362 VIRGE--DVFQGYWGEPELTREVL---VDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVME 436
Cdd:cd05968 442 VLLAPwpGMTRGFWRDEDRYLETYwsrFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLE 521
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092251577 437 ACVISVPDATWGESVKAVVALRPGRAlEAAALIAHCRERIADYK----TPRSVEFVGELPKNPSGKVARKVVREPY 508
Cdd:cd05968 522 SAAIGVPHPVKGEAIVCFVVLKPGVT-PTEALAEELMERVADELgkplSPERILFVKDLPKTRNAKVMRRVIRAAY 596
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
16-510 |
1.95e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 150.22 E-value: 1.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 16 DRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDR-VAVQSRNCAELVEIECALYKSGLVKAALNP-RFTAAEASDV 93
Cdd:PRK07867 18 DDRGLYFEDSFTSWREHIRGSAARAAALRARLDPTRPPhVGVLLDNTPEFSLLLGAAALSGIVPVGLNPtRRGAALARDI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 94 VE-NCtpRAFIGGDGYTGYARTTPGFAAVeafVALGGPAagylgYEDLLARGGTSRPPHRAAAADAAV-LHFSSGSTGRI 171
Cdd:PRK07867 98 AHaDC--QLVLTESAHAELLDGLDPGVRV---INVDSPA-----WADELAAHRDAEPPFRVADPDDLFmLIFTSGTSGDP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 172 KAAVQSYGnRMASLRKMLLGMdRQARPGDRLALIGPVTHaSGMLMQ---PFLYCGATLVLFDRFEPAHFLAEVARLRITH 248
Cdd:PRK07867 168 KAVRCTHR-KVASAGVMLAQR-FGLGPDDVCYVSMPLFH-SNAVMAgwaVALAAGASIALRRKFSASGFLPDVRRYGATY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 249 VFMVPAMIHMLLADPAL-EQADlSSLKtLSYG--AAPMAPARIREaweRIGPILSQGYGASESTSGVTRlsTADhaeaia 325
Cdd:PRK07867 245 ANYVGKPLSYVLATPERpDDAD-NPLR-IVYGneGAPGDIARFAR---RFGCVVVDGFGSTEGGVAITR--TPD------ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 326 GRPGRLascGRPHGETEVR-----------VVDEQGREVEGDAIGEIV-IRGEDVFQGYWGEPELTREVLVDGWLRTGDL 393
Cdd:PRK07867 312 TPPGAL---GPLPPGVAIVdpdtgtecppaEDADGRLLNADEAIGELVnTAGPGGFEGYYNDPEADAERMRGGVYWSGDL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 394 ARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCR 473
Cdd:PRK07867 389 AYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLA 468
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1092251577 474 ERiADYKT---PRSVEFVGELPKNPSGKVARKVVREPYWQ 510
Cdd:PRK07867 469 AQ-PDLGPkqwPSYVRVCAELPRTATFKVLKRQLSAEGVD 507
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
22-501 |
2.22e-39 |
|
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: 148.74 E-value: 2.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 22 HRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVENCTPRA 101
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 102 FIGGDgytgyarttpgfaaveafvalggpaagylgyEDLLArggtsrpphraaaadaaVLHFSSGSTGRIKAAVQSYGN- 180
Cdd:cd05914 83 IFVSD-------------------------------EDDVA-----------------LINYTSGTTGNSKGVMLTYRNi 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 181 --RMASLRKMLLgmdrqARPGDRLALIGPVTHASGM---LMQPFLYcGATLVLFDRFEPAHFLAEvARLRITHVFMVPAM 255
Cdd:cd05914 115 vsNVDGVKEVVL-----LGKGDKILSILPLHHIYPLtftLLLPLLN-GAHVVFLDKIPSAKIIAL-AFAQVTPTLGVPVP 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 256 IHML-------------------LADPALEQADLS------------SLKTLSYGAAPMAPaRIREAWERIGPILSQGYG 304
Cdd:cd05914 188 LVIEkifkmdiipkltlkkfkfkLAKKINNRKIRKlafkkvheafggNIKEFVIGGAKINP-DVEEFLRTIGFPYTIGYG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 305 ASEStsgvtrlstadhAEAIAGRPG---RLASCGRPHGETEVRVVDEQGREVEGdaigEIVIRGEDVFQGYWGEPELTRE 381
Cdd:cd05914 267 MTET------------APIISYSPPnriRLGSAGKVIDGVEVRIDSPDPATGEG----EIIVRGPNVMKGYYKNPEATAE 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 382 VLV-DGWLRTGDLARVDEEGFIYLVDRKKDMIISG-GFNVYPTEVEAVLYQHPDVMEACVISVPDatwgeSVKAVVALRP 459
Cdd:cd05914 331 AFDkDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVLESLVVVQEK-----KLVALAYIDP 405
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1092251577 460 GRALEAAALIAHCRERI------------ADYKTPRSVEFVGE-LPKNPSGKVAR 501
Cdd:cd05914 406 DFLDVKALKQRNIIDAIkwevrdkvnqkvPNYKKISKVKIVKEeFEKTPKGKIKR 460
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
27-506 |
3.13e-39 |
|
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: 147.71 E-value: 3.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 27 LSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVEnctprafIGGD 106
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVD-------RGGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 107 GYtgyarttpgfAAVEAFVALGGPaagylgyedllarggtsrpphraaaadaAVLHFSSGSTGRIKAAVQSYGNR-MASL 185
Cdd:cd05974 74 VY----------AAVDENTHADDP----------------------------MLLYFTSGTTSKPKLVEHTHRSYpVGHL 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 186 RKML-LGMdrqaRPGD---RLALIGPVTHASGMLMQPfLYCGATLVLFD--RFEPAHFLAEVARLRITHVFMVPAMIHML 259
Cdd:cd05974 116 STMYwIGL----KPGDvhwNISSPGWAKHAWSCFFAP-WNAGATVFLFNyaRFDAKRVLAALVRYGVTTLCAPPTVWRML 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 260 LadpaleQADLSSLKT----LSYGAAPMAPA---RIREAWeriGPILSQGYGASESTSGVTRlstadhaeaIAGRPGRLA 332
Cdd:cd05974 191 I------QQDLASFDVklreVVGAGEPLNPEvieQVRRAW---GLTIRDGYGQTETTALVGN---------SPGQPVKAG 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 333 SCGRPHGETEVRVVDEQGREVegdAIGEIVI-----RGEDVFQGYWGEPELTREVLVDGWLRTGDLARVDEEGFIYLVDR 407
Cdd:cd05974 253 SMGRPLPGYRVALLDPDGAPA---TEGEVALdlgdtRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGR 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 408 KKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALR----PGRALeAAALIAHCRERIADYKTPR 483
Cdd:cd05974 330 ADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRagyePSPET-ALEIFRFSRERLAPYKRIR 408
|
490 500
....*....|....*....|...
gi 1092251577 484 SVEFvGELPKNPSGKVARKVVRE 506
Cdd:cd05974 409 RLEF-AELPKTISGKIRRVELRR 430
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
3-482 |
4.54e-39 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 150.02 E-value: 4.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 3 FALFLQRAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALN 82
Cdd:PRK08279 39 LGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 83 PRFTA---AEASDVVEnctPRAFIGGDGYTGYARTTPGFAAVEAFVALGGPAAGY--LGYEDLLARGGTSRPPHRAAAAD 157
Cdd:PRK08279 119 TQQRGavlAHSLNLVD---AKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDdpEGYEDLAAAAAGAPTTNPASRSG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 158 -----AAVLHFSSGSTGRIKAAVQSYGNRMASLRKMLLGMDrqARPGDRLALIGPVTHASGMLMQP--FLYCGATLVLFD 230
Cdd:PRK08279 196 vtakdTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLR--LTPDDVLYCCLPLYHNTGGTVAWssVLAAGATLALRR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 231 RFEPAHFLAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTlsygaapMAPARIR-EAWER------IGPILsQGY 303
Cdd:PRK08279 274 KFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLRL-------MIGNGLRpDIWDEfqqrfgIPRIL-EFY 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 304 GASESTSGVTRLSTADHAeaiAGR-PGRLASCGRP---HGETEVRVVDEQGREVE------GDAIGEIVIRGEdvFQGYw 373
Cdd:PRK08279 346 AASEGNVGFINVFNFDGT---VGRvPLWLAHPYAIvkyDVDTGEPVRDADGRCIKvkpgevGLLIGRITDRGP--FDGY- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 374 GEPELTREVLV-------DGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACV--ISVPD 444
Cdd:PRK08279 420 TDPEASEKKILrdvfkkgDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVygVEVPG 499
|
490 500 510
....*....|....*....|....*....|....*...
gi 1092251577 445 aTWGESVKAVVALRPGRALEAAALIAHCRERIADYKTP 482
Cdd:PRK08279 500 -TDGRAGMAAIVLADGAEFDLAALAAHLYERLPAYAVP 536
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
24-511 |
6.93e-39 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 149.39 E-value: 6.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 24 ERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALnPRFTA--------AEASDVVE 95
Cdd:PRK09192 47 EEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPL-PLPMGfggresyiAQLRGMLA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 96 NCTPRAFIGGDGYTGYARttpgfaavEAFVALGGPAAGYLGYEDLLARGGTSRPPhrAAAADAAVLHFSSGSTGRIKAAV 175
Cdd:PRK09192 126 SAQPAAIITPDELLPWVN--------EATHGNPLLHVLSHAWFKALPEADVALPR--PTPDDIAYLQYSSGSTRFPRGVI 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 176 QSYGNRMASLRKMLL-GMdrQARPGDRLALIGPVTH---ASGMLMQPfLYCGATLVL-----FDRfEPAHFLAEVARLRI 246
Cdd:PRK09192 196 ITHRALMANLRAISHdGL--KVRPGDRCVSWLPFYHdmgLVGFLLTP-VATQLSVDYlptrdFAR-RPLQWLDLISRNRG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 247 ThVFMVPAMIHMLLA----DPALEQADLSSLKTLSYGAAPMAPARIREAWERIGPI------LSQGYGASESTSGVT--- 313
Cdd:PRK09192 272 T-ISYSPPFGYELCArrvnSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAFAPAgfddkaFMPSYGLAEATLAVSfsp 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 314 -------------RLSTADHAEAIAGRPGRLAS---CGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPE 377
Cdd:PRK09192 351 lgsgivveevdrdRLEYQGKAVAPGAETRRVRTfvnCGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEE 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 378 LTREVLVDGWLRTGDLARVdEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVM--EACVISVPDATwGESVKAVV 455
Cdd:PRK09192 431 SQDVLAADGWLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQEN-GEKIVLLV 508
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1092251577 456 ALRPGRALEAAALIAHCRERI-ADYKTPRSVEFVG--ELPKNPSGKVARKVVREPYWQG 511
Cdd:PRK09192 509 QCRISDEERRGQLIHALAALVrSEFGVEAAVELVPphSLPRTSSGKLSRAKAKKRYLSG 567
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
5-507 |
3.09e-38 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 150.49 E-value: 3.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 5 LFLQRAARYwGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPR 84
Cdd:PRK12316 4556 LVAERARMT-PDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPE 4634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 85 FTAAEASDVVENCTPRAFIGgdgytgYARTTPGFAAVEAFVALG-GPAAGYLGYEDllarggtSRPPHRAAAADAAVLHF 163
Cdd:PRK12316 4635 YPRERLAYMMEDSGAALLLT------QSHLLQRLPIPDGLASLAlDRDEDWEGFPA-------HDPAVRLHPDNLAYVIY 4701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 164 SSGSTGRIKAAvqsyGNRMASLRKMLLGMDR--QARPGDRLALIGPVT-HASGMLMQPFLYCGATLVLFD--RFEPAHFL 238
Cdd:PRK12316 4702 TSGSTGRPKGV----AVSHGSLVNHLHATGEryELTPDDRVLQFMSFSfDGSHEGLYHPLINGASVVIRDdsLWDPERLY 4777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 239 AEVARLRITHVFMVPAMIHMLLADPAlEQADLSSLKTLSYGAAPMAPARIREAWERIGPI-LSQGYGASESTSGVTRLST 317
Cdd:PRK12316 4778 AEIHEHRVTVLVFPPVYLQQLAEHAE-RDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVyLFNGYGPTETTVTVLLWKA 4856
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 318 ADHAEAIAGrpgrLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLV-------DGWL-R 389
Cdd:PRK12316 4857 RDGDACGAA----YMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVpdpfgapGGRLyR 4932
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 390 TGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVV----ALRPGRALEA 465
Cdd:PRK12316 4933 TGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVpqdpALADADEAQA 5012
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1092251577 466 A---ALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVREP 507
Cdd:PRK12316 5013 ElrdELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQP 5057
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
7-506 |
6.96e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 146.00 E-value: 6.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 7 LQRAARYWGDRPAV-------MHRervLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKA 79
Cdd:PRK07008 16 IAHAARHAGDTEIVsrrvegdIHR---YTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 80 ALNPRFTAAEASDVVENCTprafiggDGY----TGYARTTPGFAA----VEAFVALGG----PAAG--YLGYEDLL-ARG 144
Cdd:PRK07008 93 TINPRLFPEQIAYIVNHAE-------DRYvlfdLTFLPLVDALAPqcpnVKGWVAMTDaahlPAGStpLLCYETLVgAQD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 145 GTSRPPhRAAAADAAVLHFSSGSTGRIKAAVqsYGNRMASLRKMLL----GMDRQARpgDRLALIGPVTHA-------SG 213
Cdd:PRK07008 166 GDYDWP-RFDENQASSLCYTSGTTGNPKGAL--YSHRSTVLHAYGAalpdAMGLSAR--DAVLPVVPMFHVnawglpySA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 214 MLMqpflycGATLV----------LFDRFEpahflAEvarlRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPM 283
Cdd:PRK07008 241 PLT------GAKLVlpgpdldgksLYELIE-----AE----RVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSAC 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 284 APARIREAWERIGPILSQGYGASE-STSGVT-RLSTADHAEAIAGRPGRLASCGRPHGETEVRVVDEQGREV--EGDAIG 359
Cdd:PRK07008 306 PPAMIRTFEDEYGVEVIHAWGMTEmSPLGTLcKLKWKHSQLPLDEQRKLLEKQGRVIYGVDMKIVGDDGRELpwDGKAFG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 360 EIVIRGEDVFQGYWGEPEltrEVLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACV 439
Cdd:PRK07008 386 DLQVRGPWVIDRYFRGDA---SPLVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAAC 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092251577 440 ISVPDATWGESVKAVVALRPGRALEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:PRK07008 463 IACAHPKWDERPLLVVVKRPGAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLRE 529
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
16-502 |
1.66e-37 |
|
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: 143.16 E-value: 1.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 16 DRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVE 95
Cdd:cd17652 2 DAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 96 NCTPRAFIggdgytgyarTTPGFAAveafvalggpaagYLGYedllarggtsrpphraaaadaavlhfSSGSTGRIKAAV 175
Cdd:cd17652 82 DARPALLL----------TTPDNLA-------------YVIY--------------------------TSGSTGRPKGVV 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 176 ---QSYGNRMASLRKMLlgmdrQARPGDR-LALIGPVTHASGMLMQPFLYCGATLVLFDRFE---PAHFLAEVARLRITH 248
Cdd:cd17652 113 vthRGLANLAAAQIAAF-----DVGPGSRvLQFASPSFDASVWELLMALLAGATLVLAPAEEllpGEPLADLLREHRITH 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 249 VFMVPAmihmllADPALEQADLSSLKTL-SYGAAPMAPARIREAWERIgpiLSQGYGASESTSGVTRlstadhaeAIAGR 327
Cdd:cd17652 188 VTLPPA------ALAALPPDDLPDLRTLvVAGEACPAELVDRWAPGRR---MINAYGPTETTVCATM--------AGPLP 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 328 PGRLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLV--------DGWLRTGDLARVDEE 399
Cdd:cd17652 251 GGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVadpfgapgSRMYRTGDLARWRAD 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 400 GFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCRERIADY 479
Cdd:cd17652 331 GQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGY 410
|
490 500
....*....|....*....|...
gi 1092251577 480 KTPRSVEFVGELPKNPSGKVARK 502
Cdd:cd17652 411 MVPAAFVVLDALPLTPNGKLDRR 433
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
163-505 |
1.01e-36 |
|
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: 143.47 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 163 FSSGSTGRIKAAVQSYGNRMA-SLRKMLLGMDrqARPGDRL---ALIGPVTHASGMLMQPfLYCGATLVLF----DRFEP 234
Cdd:cd05966 238 YTSGSTGKPKGVVHTTGGYLLyAATTFKYVFD--YHPDDIYwctADIGWITGHSYIVYGP-LANGATTVMFegtpTYPDP 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 235 AHFLAEVARLRITHVFMVPAMIHMLLA--DPALEQADLSSLKTLSYGAAPMAParirEAW----ERIG----PILSQgYG 304
Cdd:cd05966 315 GRYWDIVEKHKVTIFYTAPTAIRALMKfgDEWVKKHDLSSLRVLGSVGEPINP----EAWmwyyEVIGkercPIVDT-WW 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 305 ASEsTSG--VTRLstadhAEAIAGRPGrlaSCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGE--DVFQGYWGEPELTR 380
Cdd:cd05966 390 QTE-TGGimITPL-----PGATPLKPG---SATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDHERYE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 381 EVL---VDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVAL 457
Cdd:cd05966 461 DTYfskFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTL 540
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1092251577 458 RPGRALE---AAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVR 505
Cdd:cd05966 541 KDGEEPSdelRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILR 591
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
137-509 |
2.05e-36 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 141.70 E-value: 2.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 137 YEDLLARGGTSRPPHRAAAADAAVLHFSSGSTGRIKAAvqsygnRMASLRKMLLGMDRQARPG----DRLALIGPVTHAS 212
Cdd:PRK13388 131 YAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAV------RCSHGRLAFAGRALTERFGltrdDVCYVSMPLFHSN 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 213 GMLM--QPFLYCGATLVLFDRFEPAHFLAEVARLRITHVFMVPAMIHMLLADPalEQADlSSLKTLSYGAAPMA-PARIR 289
Cdd:PRK13388 205 AVMAgwAPAVASGAAVALPAKFSASGFLDDVRRYGATYFNYVGKPLAYILATP--ERPD-DADNPLRVAFGNEAsPRDIA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 290 EAWERIGPILSQGYGASESTSGVTRLSTAdhAEAIAGRPGRLASCGRPHGETE--VRVVDEQGREVEGD-AIGEIVIR-G 365
Cdd:PRK13388 282 EFSRRFGCQVEDGYGSSEGAVIVVREPGT--PPGSIGRGAPGVAIYNPETLTEcaVARFDAHGALLNADeAIGELVNTaG 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 366 EDVFQGYWGEPELTREVLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDA 445
Cdd:PRK13388 360 AGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDE 439
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092251577 446 TWGESVKAVVALRPGRALEAAALIAHCRERiADYKT---PRSVEFVGELPKNPSGKVARKVVREPYW 509
Cdd:PRK13388 440 RVGDQVMAALVLRDGATFDPDAFAAFLAAQ-PDLGTkawPRYVRIAADLPSTATNKVLKRELIAQGW 505
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
16-502 |
2.47e-36 |
|
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: 140.14 E-value: 2.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 16 DRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVE 95
Cdd:cd17643 2 EAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 96 NCTPRAFIggdgytgyarTTPGFAAveafvalggpaagYLGYedllarggtsrpphraaaadaavlhfSSGSTGRIKAAV 175
Cdd:cd17643 82 DSGPSLLL----------TDPDDLA-------------YVIY--------------------------TSGSTGRPKGVV 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 176 QSYGNrmasLRKMLLGMDRQAR--PGDRLALIgpvtHASGM------LMQPFLYcGATLVLFD---RFEPAHFLAEVARL 244
Cdd:cd17643 113 VSHAN----VLALFAATQRWFGfnEDDVWTLF----HSYAFdfsvweIWGALLH-GGRLVVVPyevARSPEDFARLLRDE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 245 RITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIREAWERIG---PILSQGYGASESTSGVT--RLSTAD 319
Cdd:cd17643 184 GVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGldrPQLVNMYGITETTVHVTfrPLDAAD 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 320 HAEAIAGrpgrlaSCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDG--------WLRTG 391
Cdd:cd17643 264 LPAAAAS------PIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANpfggpgsrMYRTG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 392 DLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAH 471
Cdd:cd17643 338 DLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRAL 417
|
490 500 510
....*....|....*....|....*....|.
gi 1092251577 472 CRERIADYKTPRSVEFVGELPKNPSGKVARK 502
Cdd:cd17643 418 LKELLPDYMVPARYVPLDALPLTVNGKLDRA 448
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
16-502 |
8.98e-36 |
|
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: 138.94 E-value: 8.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 16 DRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVE 95
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 96 NCTPRAFIGGDGYTgyarttpgFAAVEAFVALGGPAagylgyeDLLARGGTSRPPHRAAAADAAVLhFSSGSTGRIKAAV 175
Cdd:cd12114 82 DAGARLVLTDGPDA--------QLDVAVFDVLILDL-------DALAAPAPPPPVDVAPDDLAYVI-FTSGSTGTPKGVM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 176 QSYGNRMASL----RKMLLGmdrqarPGDRLALIGPVTHAsgmlMQPF-----LYCGATLVLFD---RFEPAHFLAEVAR 243
Cdd:cd12114 146 ISHRAALNTIldinRRFAVG------PDDRVLALSSLSFD----LSVYdifgaLSAGATLVLPDearRRDPAHWAELIER 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 244 LRITHVFMVPAMIHMLLADPALEQADLSSLKT--LSYGAAPMA-PARIREAWERIGPIlsqgygaseSTSGVTRLSTADH 320
Cdd:cd12114 216 HGVTLWNSVPALLEMLLDVLEAAQALLPSLRLvlLSGDWIPLDlPARLRALAPDARLI---------SLGGATEASIWSI 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 321 AEAIAGRPGRLASC--GRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVD-----GWLRTGDL 393
Cdd:cd12114 287 YHPIDEVPPDWRSIpyGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVThpdgeRLYRTGDL 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 394 ARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCR 473
Cdd:cd12114 367 GRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIAPDALRAFLA 446
|
490 500
....*....|....*....|....*....
gi 1092251577 474 ERIADYKTPRSVEFVGELPKNPSGKVARK 502
Cdd:cd12114 447 QTLPAYMIPSRVIALEALPLTANGKVDRA 475
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
160-511 |
3.05e-35 |
|
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: 138.57 E-value: 3.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 160 VLHFSSGSTGRIKAAVQSYGNRMASLRKMllGMDRQARPGDRLALIGPVTHASGMLM-----------QpfLYCGATLVL 228
Cdd:cd05906 171 LLMLTSGSTGFPKAVPLTHRNILARSAGK--IQHNGLTPQDVFLNWVPLDHVGGLVElhlravylgcqQ--VHVPTEEIL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 229 FDrfePAHFLAEVARLRITHVFMvP----AMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIREAWERIGP------I 298
Cdd:cd05906 247 AD---PLRWLDLIDRYRVTITWA-PnfafALLNDLLEEIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPyglppdA 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 299 LSQGYGASESTSGVT---RLSTADHAEAIagrpgRLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGE 375
Cdd:cd05906 323 IRPAFGMTETCSGVIysrSFPTYDHSQAL-----EFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNN 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 376 PELTREVLV-DGWLRTGDLARVDeEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVME--ACVISVPDATWGESVK 452
Cdd:cd05906 398 PEANAEAFTeDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVRDPGAETEEL 476
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092251577 453 AVVAL----RPGRALEAAALIahcrERIADYKTPRSVEFV-----GELPKNPSGKVARKVVREPYWQG 511
Cdd:cd05906 477 AIFFVpeydLQDALSETLRAI----RSVVSREVGVSPAYLiplpkEEIPKTSLGKIQRSKLKAAFEAG 540
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
5-507 |
4.14e-35 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 140.86 E-value: 4.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 5 LFLQRAARYwGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPR 84
Cdd:PRK12316 516 LFEEQVERT-PEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPE 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 85 FTAAEASDVVENCTPRAFIggdGYTGYARTTPgFAAVEAFVALGGPAAGYLGYEDllarggtSRPPHRAAAADAAVLHFS 164
Cdd:PRK12316 595 YPAERLAYMLEDSGVQLLL---SQSHLGRKLP-LAAGVQVLDLDRPAAWLEGYSE-------ENPGTELNPENLAYVIYT 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 165 SGSTGRIKAAVQSYGNRMASLRKMLLGMDRQArpGDRLALIGPVTHASG--MLMQPfLYCGATLVLF---DRFEPAHFLA 239
Cdd:PRK12316 664 SGSTGKPKGAGNRHRALSNRLCWMQQAYGLGV--GDTVLQKTPFSFDVSvwEFFWP-LMSGARLVVAapgDHRDPAKLVE 740
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 240 EVARLRITHVFMVPAMIHMLLADPALeqADLSSLKTLSYGAAPMAPArireAWERIGPILSQG-----YGASESTSGVTR 314
Cdd:PRK12316 741 LINREGVDTLHFVPSMLQAFLQDEDV--ASCTSLRRIVCSGEALPAD----AQEQVFAKLPQAglynlYGPTEAAIDVTH 814
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 315 LSTADHAeaiagrpGRLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLV-----DG--W 387
Cdd:PRK12316 815 WTCVEEG-------GDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVpspfvAGerM 887
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 388 LRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPdatwGESVKAVVALRPGRALEAAA 467
Cdd:PRK12316 888 YRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVLESEGGDWREA 963
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1092251577 468 LIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVREP 507
Cdd:PRK12316 964 LKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAP 1003
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
6-506 |
5.89e-35 |
|
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: 137.18 E-value: 5.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 6 FLQRAARYWGDRpavMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRF 85
Cdd:cd05915 7 LFGRKEVVSRLH---TGEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 86 TAAEASDVVENCTPRAFIGGDGYTGYARTTpgFAAVEAFVALGGPAAGYLGYEDLLARGGTSRPPHRAAAADAAV-LHFS 164
Cdd:cd05915 84 SPKEIAYILNHAEDKVLLFDPNLLPLVEAI--RGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVRVPERAACgMAYT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 165 SGSTGRIKAAVqsYGNRMASLRKMLLGM--DRQARPGDRLALIGPVTHASG--MLMQPFLYCGATLVLFDRFEPAHFLAE 240
Cdd:cd05915 162 TGTTGLPKGVV--YSHRALVLHSLAASLvdGTALSEKDVVLPVVPMFHVNAwcLPYAATLVGAKQVLPGPRLDPASLVEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 241 VARLRITHVFMVPAMIHMLL-ADPALEQADLSSLKTLSYGAAPmapARIREAWERIGPI-LSQGYGASESTS-GVTRLST 317
Cdd:cd05915 240 FDGEGVTFTAGVPTVWLALAdYLESTGHRLKTLRRLVVGGSAA---PRSLIARFERMGVeVRQGYGLTETSPvVVQNFVK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 318 ADHAEAIAGRPGRL-ASCGRPHGETEVRVVDEQGREV--EGDAIGEIVIRGEDVFQGYWGEPELTR-EVLVDGWLRTGDL 393
Cdd:cd05915 317 SHLESLSEEEKLTLkAKTGLPIPLVRLRVADEEGRPVpkDGKALGEVQLKGPWITGGYYGNEEATRsALTPDGFFRTGDI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 394 ARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEaAALIAHCR 473
Cdd:cd05915 397 AVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTP-EELNEHLL 475
|
490 500 510
....*....|....*....|....*....|....
gi 1092251577 474 ERIADYKT-PRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:cd05915 476 KAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
8-507 |
7.85e-35 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 139.91 E-value: 7.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 8 QRAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTA 87
Cdd:PRK12467 519 EAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQ 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 88 AEASDVVENCTPRAFIGgdgYTGYARTTPGFAAVEAfVALGGPAagylgyeDLLARGGTSRPPHRAAAADAAVLHFSSGS 167
Cdd:PRK12467 599 DRLAYMLDDSGVRLLLT---QSHLLAQLPVPAGLRS-LCLDEPA-------DLLCGYSGHNPEVALDPDNLAYVIYTSGS 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 168 TGRIKAAvqsyGNRMASLRKMLLGMDRQAR--PGDRLALIGPVTHASGMLMQ-PFLYCGATLVLFDR---FEPAHFLAEV 241
Cdd:PRK12467 668 TGQPKGV----AISHGALANYVCVIAERLQlaADDSMLMVSTFAFDLGVTELfGALASGATLHLLPPdcaRDAEAFAALM 743
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 242 ARLRITHVFMVPAMIHMLLADPAleQADLSSLKTLSYGAAPMAPARIREaWERIGPILS--QGYGASESTSGVTRLSTAD 319
Cdd:PRK12467 744 ADQGVTVLKIVPSHLQALLQASR--VALPRPQRALVCGGEALQVDLLAR-VRALGPGARliNHYGPTETTVGVSTYELSD 820
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 320 HAEAIAGRPgrlasCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLV------DG--WLRTG 391
Cdd:PRK12467 821 EERDFGNVP-----IGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVpdpfgaDGgrLYRTG 895
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 392 DLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAA---- 467
Cdd:PRK12467 896 DLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVPAAVADGAEHQAtrde 975
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1092251577 468 LIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVREP 507
Cdd:PRK12467 976 LKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKP 1015
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
5-502 |
1.33e-34 |
|
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: 135.14 E-value: 1.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 5 LFLQRAARYwGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPR 84
Cdd:cd12115 4 LVEAQAART-PDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 85 FTAAEASDVVENCTPRafiggdgytgyarttpgfaaveafVALGGPAAgyLGYedllarggtsrpphraaaadaavLHFS 164
Cdd:cd12115 83 YPPERLRFILEDAQAR------------------------LVLTDPDD--LAY-----------------------VIYT 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 165 SGSTGRIKAAVQSYGNRMAslrkmLLGMDRQARPGDRLA----------------LIGPvthasgmlmqpfLYCGATLVL 228
Cdd:cd12115 114 SGSTGRPKGVAIEHRNAAA-----FLQWAAAAFSAEELAgvlastsicfdlsvfeLFGP------------LATGGKVVL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 229 FDrfEPAHFLAEVARLRITHVFMVPAMIHMLLADPALEQadlsSLKTLSYGAAPMAPARIREAWERI-GPILSQGYGASE 307
Cdd:cd12115 177 AD--NVLALPDLPAAAEVTLINTVPSAAAELLRHDALPA----SVRVVNLAGEPLPRDLVQRLYARLqVERVVNLYGPSE 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 308 ST--SGVTRLSTADHAEAiagrpgrlaSCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTRE-VLV 384
Cdd:cd12115 251 DTtySTVAPVPPGASGEV---------SIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAErFLP 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 385 DGWL------RTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALR 458
Cdd:cd12115 322 DPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAE 401
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1092251577 459 PGRALEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARK 502
Cdd:cd12115 402 PGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRS 445
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
24-491 |
1.04e-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: 132.86 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 24 ERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVENCTPRAFI 103
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 104 ggdgytgyarttpgfaaVEAfvalggpaagylgyedllarggtsrpphraaaadaAVLHFSSGSTGRIKAAVQSYGN--R 181
Cdd:cd05940 81 -----------------VDA-----------------------------------ALYIYTSGTTGLPKAAIISHRRawR 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 182 MASLRKMLLGMDRQarpgDRLALIGPVTHASGMLMQP--FLYCGATLVLFDRFEPAHFLAEVARLRITHVFMVPAMIHML 259
Cdd:cd05940 109 GGAFFAGSGGALPS----DVLYTCLPLYHSTALIVGWsaCLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGELCRYL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 260 LADPALEQADLSSLKTLSYGAapMAPARIREAWERIG-PILSQGYGASESTSGVTRLSTADHAeaiAGRPGRLASCGRPH 338
Cdd:cd05940 185 LNQPPKPTERKHKVRMIFGNG--LRPDIWEEFKERFGvPRIAEFYAATEGNSGFINFFGKPGA---IGRNPSLLRKVAPL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 339 G------ETEVRVVDEQGREVE------GDAIGEIVIRGEdvFQGYWG----EPELTREVLVDG--WLRTGDLARVDEEG 400
Cdd:cd05940 260 AlvkydlESGEPIRDAEGRCIKvprgepGLLISRINPLEP--FDGYTDpaatEKKILRDVFKKGdaWFNTGDLMRLDGEG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 401 FIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACV--ISVPDaTWGESVKAVVALRPGRALEAAALIAHCRERIAD 478
Cdd:cd05940 338 FWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPG-TDGRAGMAAIVLQPNEEFDLSALAAHLEKNLPG 416
|
490
....*....|...
gi 1092251577 479 YKTPRSVEFVGEL 491
Cdd:cd05940 417 YARPLFLRLQPEM 429
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
50-440 |
8.45e-33 |
|
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: 131.05 E-value: 8.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 50 PGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVENCTPRAFIGGDgYTGYARTTPGFAAVEAFVALGG 129
Cdd:cd05932 30 PGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGK-LDDWKAMAPGVPEGLISISLPP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 130 PAAG--YLGYEDLLARGGTSRPPHRAAAADAAVLHFSSGSTGRIKAAVQSYGNRMASLRKMLLGMDrqARPGDRLALIGP 207
Cdd:cd05932 109 PSAAncQYQWDDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIG--TEENDRMLSYLP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 208 VTH-ASGMLMQ-PFLYCGATLVLFDRFEPahFLAEVARLRITHVFMVP----------------AMIHMLLADP------ 263
Cdd:cd05932 187 LAHvTERVFVEgGSLYGGVLVAFAESLDT--FVEDVQRARPTLFFSVPrlwtkfqqgvqdkipqQKLNLLLKIPvvnslv 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 264 ---ALEQADLSSLKTLSYGAAPMAPARIrEAWERIGPILSQGYGASESTsgvtrlstadhAEAIAGRPGR--LASCGRPH 338
Cdd:cd05932 265 krkVLKGLGLDQCRLAGCGSAPVPPALL-EWYRSLGLNILEAYGMTENF-----------AYSHLNYPGRdkIGTVGNAG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 339 GETEVRVVDEqgrevegdaiGEIVIRGEDVFQGYWGEPELTREVLV-DGWLRTGDLARVDEEGFIYLVDRKKDMI-ISGG 416
Cdd:cd05932 333 PGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTaDGFLRTGDKGELDADGNLTITGRVKDIFkTSKG 402
|
410 420
....*....|....*....|....
gi 1092251577 417 FNVYPTEVEAVLYQHPDVMEACVI 440
Cdd:cd05932 403 KYVAPAPIENKLAEHDRVEMVCVI 426
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
251-501 |
1.67e-32 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 130.51 E-value: 1.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 251 MVPAMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIREAwERIGPILSQGYGASEStsGVTRLSTADHAEAIAGRPGr 330
Cdd:PRK05857 266 LVPTLLSKLVSELKSANATVPSLRLVGYGGSRAIAADVRFI-EATGVRTAQVYGLSET--GCTALCLPTDDGSIVKIEA- 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 331 lASCGRPHGETEVRVVDEQG------REVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDGWLRTGDLARVDEEGFIYL 404
Cdd:PRK05857 342 -GAVGRPYPGVDVYLAATDGigptapGAGPSASFGTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYI 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 405 VDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVK-AVVALRPGRALEAAAL----IAHCRERIADY 479
Cdd:PRK05857 421 KGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGlAVVASAELDESAARALkhtiAARFRRESEPM 500
|
250 260
....*....|....*....|..
gi 1092251577 480 KTPRSVEFVGELPKNPSGKVAR 501
Cdd:PRK05857 501 ARPSTIVIVTDIPRTQSGKVMR 522
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
163-505 |
1.74e-32 |
|
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: 131.28 E-value: 1.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 163 FSSGSTGRIKAAVQSYGNRMASLR---KMLLGMdrqaRPGDRL---ALIGPVTHASGMLMQPFLyCGATLVLF----DRF 232
Cdd:cd05967 237 YTSGTTGKPKGVVRDNGGHAVALNwsmRNIYGI----KPGDVWwaaSDVGWVVGHSYIVYGPLL-HGATTVLYegkpVGT 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 233 -EPAHFLAEVARLRITHVFMVPAMIHMLLADPA----LEQADLSSLKTLSYGAAPMAPARIREAWERIG-PILSQgYGAS 306
Cdd:cd05967 312 pDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPdgkyIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGvPVIDH-WWQT 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 307 ESTSGVTrlstaDHAEAIAGRPGRLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGE---DVFQGYWGEPELTREV- 382
Cdd:cd05967 391 ETGWPIT-----ANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPlppGCLLTLWKNDERFKKLy 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 383 --LVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPG 460
Cdd:cd05967 466 lsKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEG 545
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1092251577 461 RALEAA----ALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVR 505
Cdd:cd05967 546 VKITAEelekELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLR 594
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
4-507 |
5.30e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 131.62 E-value: 5.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 4 ALFLQRAARYwGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNP 83
Cdd:PRK12316 2007 QRIAEQAARA-PEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDP 2085
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 84 RFTAAEASDVVENCTPRAFIGGDGYTGYARTTPGFAAVEafvalggpaagyLGYEDLLARGGTSRPPHRAAAADAAVLHF 163
Cdd:PRK12316 2086 NYPAERLAYMLEDSGAALLLTQRHLLERLPLPAGVARLP------------LDRDAEWADYPDTAPAVQLAGENLAYVIY 2153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 164 SSGSTGRIKAAVQSYGNRMASLRKMllGMDRQARPGDRLALIGPVTH--ASGMLMQPFLYcGATLVLFD--RFEPAHFLA 239
Cdd:PRK12316 2154 TSGSTGLPKGVAVSHGALVAHCQAA--GERYELSPADCELQFMSFSFdgAHEQWFHPLLN-GARVLIRDdeLWDPEQLYD 2230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 240 EVARLRITHVFMVPAMIHmLLADPALEQADLSSLKTLSYGAAPMAPARIREAWERIGPI-LSQGYGASESTSGVTrLSTA 318
Cdd:PRK12316 2231 EMERHGVTILDFPPVYLQ-QLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVyLFNGYGPTEAVVTPL-LWKC 2308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 319 DHAEAIAgrpGRLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLV-------DGWL-RT 390
Cdd:PRK12316 2309 RPQDPCG---AAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVpdpfsasGERLyRT 2385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 391 GDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATwGESVKAVVALRPGRALEAAALIA 470
Cdd:PRK12316 2386 GDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGAS-GKQLVAYVVPDDAAEDLLAELRA 2464
|
490 500 510
....*....|....*....|....*....|....*..
gi 1092251577 471 HCRERIADYKTPRSVEFVGELPKNPSGKVARKVVREP 507
Cdd:PRK12316 2465 WLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKP 2501
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
7-506 |
9.71e-32 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 128.33 E-value: 9.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 7 LQRAARYWGDRPAV-------MHRErvlSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKA 79
Cdd:PRK06018 16 IDHAARIHGNREVVtrsvegpIVRT---TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 80 ALNPRFTAAEASDVVENCTPRAFIGGDGYTG-YARTTPGFAAVEAFVALGGPA-------AGYLGYEDLLARGGTSRPPH 151
Cdd:PRK06018 93 TVNPRLFPEQIAWIINHAEDRVVITDLTFVPiLEKIADKLPSVERYVVLTDAAhmpqttlKNAVAYEEWIAEADGDFAWK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 152 RAAAADAAVLHFSSGSTGRIKAAVQSY-GNRMASLRKML---LGMdrqaRPGDRLALIGPVTHAS--GMLMQ-PFLycGA 224
Cdd:PRK06018 173 TFDENTAAGMCYTSGTTGDPKGVLYSHrSNVLHALMANNgdaLGT----SAADTMLPVVPLFHANswGIAFSaPSM--GT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 225 TLVLfdrfePAHFL--AEVARL----RITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMaPARIREAWERIGPI 298
Cdd:PRK06018 247 KLVM-----PGAKLdgASVYELldteKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAM-PRSMIKAFEDMGVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 299 LSQGYGASEsTSGVTRLST-ADHAEAIAG--RPGRLASCGRPHGETEVRVVDEQGREV--EGDAIGEIVIRGEDVFQGYW 373
Cdd:PRK06018 321 VRHAWGMTE-MSPLGTLAAlKPPFSKLPGdaRLDVLQKQGYPPFGVEMKITDDAGKELpwDGKTFGRLKVRGPAVAAAYY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 374 GEPEltrEVL-VDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVK 452
Cdd:PRK06018 400 RVDG---EILdDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPL 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1092251577 453 AVVALRPGRALEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:PRK06018 477 LIVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1-479 |
9.92e-32 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 128.48 E-value: 9.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 1 MAFALFLQRAARYWGDRPAV----------MHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECA 70
Cdd:PRK09274 6 ANIARHLPRAAQERPDQLAVavpggrgadgKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 71 LYKSGLV---------KAALNPRFTAAEasdvvenctPRAFIGGDGYTgYARTT--PGFAAVEAFVALGGPAA-GYLGYE 138
Cdd:PRK09274 86 LFKAGAVpvlvdpgmgIKNLKQCLAEAQ---------PDAFIGIPKAH-LARRLfgWGKPSVRRLVTVGGRLLwGGTTLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 139 DLLARGGTSR-PPHRAAAADAAVLHFSSGSTGRIKAAVQSYGNRMASLRkmLLGMDRQARPGDR-------LALIGPVth 210
Cdd:PRK09274 156 TLLRDGAAAPfPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIE--ALREDYGIEPGEIdlptfplFALFGPA-- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 211 asgmlmqpflyCGATLVLFD-------RFEPAHFLAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPM 283
Cdd:PRK09274 232 -----------LGMTSVIPDmdptrpaTVDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 284 APArireAWERIGPILSQG------YGASE-----STSGVTRLS-TADHAEAIAGrpgrlaSC-GRPHGETEVRVVD--- 347
Cdd:PRK09274 301 PIA----VIERFRAMLPPDaeiltpYGATEalpisSIESREILFaTRAATDNGAG------ICvGRPVDGVEVRIIAisd 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 348 ------EQGREVEGDAIGEIVIRGEDVFQGYWGEPELTR-----EVLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGG 416
Cdd:PRK09274 371 apipewDDALRLATGEIGEIVVAGPMVTRSYYNRPEATRlakipDGQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAG 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092251577 417 FNVYPTEVEAVLYQHPDVMEACVISVPDAtwGESVKA-VVALRPGRALEAAALIAHCRERIADY 479
Cdd:PRK09274 451 GTLYTIPCERIFNTHPGVKRSALVGVGVP--GAQRPVlCVELEPGVACSKSALYQELRALAAAH 512
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
163-511 |
3.69e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 128.74 E-value: 3.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 163 FSSGSTGRIKAAvqsyGNRMASLRKMLLGMdRQAR---PGDRLALIGPVTHASGML-MQPFLYCGATLVLFD--RFEPAH 236
Cdd:PRK12467 3244 YTSGSTGKPKGV----GVRHGALANHLCWI-AEAYeldANDRVLLFMSFSFDGAQErFLWTLICGGCLVVRDndLWDPEE 3318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 237 FLAEVARLRITHVFMVPAMIHMLLADPalEQADLSSLKTLSYGAAPMAPARIREAWERIGPI-LSQGYGASESTSGVTRL 315
Cdd:PRK12467 3319 LWQAIHAHRISIACFPPAYLQQFAEDA--GGADCASLDIYVFGGEAVPPAAFEQVKRKLKPRgLTNGYGPTEAVVTVTLW 3396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 316 STADHAEAIAGrpgrLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLV-------DGWL 388
Cdd:PRK12467 3397 KCGGDAVCEAP----YAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVadpfsgsGGRL 3472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 389 -RTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALeAAA 467
Cdd:PRK12467 3473 yRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPADPQGDW-RET 3551
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1092251577 468 LIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVREPYWQG 511
Cdd:PRK12467 3552 LRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKG 3595
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
7-507 |
5.38e-31 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 127.85 E-value: 5.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 7 LQRAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFT 86
Cdd:PRK10252 464 VAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYP 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 87 AAEASDVVENCTPRAFIggdgytgyarTTPGFAAVEAfvalGGPAAGYLGYEDLLARGGtSRPPHRAAAADAAVLHFSSG 166
Cdd:PRK10252 544 DDRLKMMLEDARPSLLI----------TTADQLPRFA----DVPDLTSLCYNAPLAPQG-AAPLQLSQPHHTAYIIFTSG 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 167 STGRIKAAV---QSYGNRmaslrkmLLGMDRQ--ARPGDRLALIGPVTHASGM--LMQPFLyCGATLVLF------DRFE 233
Cdd:PRK10252 609 STGRPKGVMvgqTAIVNR-------LLWMQNHypLTADDVVLQKTPCSFDVSVweFFWPFI-AGAKLVMAepeahrDPLA 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 234 PAHFlaeVARLRITHVFMVPAMIHMLLADPALEQAD--LSSLK-TLSYGAApmAPARIREAWER-IGPILSQGYGASEST 309
Cdd:PRK10252 681 MQQF---FAEYGVTTTHFVPSMLAAFVASLTPEGARqsCASLRqVFCSGEA--LPADLCREWQQlTGAPLHNLYGPTEAA 755
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 310 SGVTRLSTAdhAEAIAGRPGRLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDG--- 386
Cdd:PRK10252 756 VDVSWYPAF--GEELAAVRGSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADpfa 833
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 387 ----WLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVME----ACVISVPDATWGES---VKAVV 455
Cdd:PRK10252 834 pgerMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQavthACVINQAAATGGDArqlVGYLV 913
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1092251577 456 AlRPGRALEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVREP 507
Cdd:PRK10252 914 S-QSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLP 964
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
160-499 |
2.62e-30 |
|
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: 123.60 E-value: 2.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 160 VLHFSSGSTGRIKAAVQSYGNRMASLRKMLLGMDrqARPGDRLALIGPVTHASGM---LMQPFLyCGATLVLFdrFEPah 236
Cdd:cd05909 151 VILFTSGSEGLPKGVVLSHKNLLANVEQITAIFD--PNPEDVVFGALPFFHSFGLtgcLWLPLL-SGIKVVFH--PNP-- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 237 flaevarlriTHVFMVPAMIH-----MLLADP--------ALEQADLSSLKTLSYGAAPMaPARIREAW-ERIGPILSQG 302
Cdd:cd05909 224 ----------LDYKKIPELIYdkkatILLGTPtflrgyarAAHPEDFSSLRLVVAGAEKL-KDTLRQEFqEKFGIRILEG 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 303 YGASEStSGVTRLSTADHAEaiagRPGrlaSCGRPHGETEVRVVDEQGREVEgdAIGE---IVIRGEDVFQGYWGEPELT 379
Cdd:cd05909 293 YGTTEC-SPVISVNTPQSPN----KEG---TVGRPLPGMEVKIVSVETHEEV--PIGEgglLLVRGPNVMLGYLNEPELT 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 380 REVLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQH-PDVMEACVISVPDATWGEsvkAVVALR 458
Cdd:cd05909 363 SFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGE---KIVLLT 439
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1092251577 459 PGRALEAAALIAHCRE-RIADYKTPRSVEFVGELPKNPSGKV 499
Cdd:cd05909 440 TTTDTDPSSLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKP 481
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
163-506 |
2.21e-29 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 123.11 E-value: 2.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 163 FSSGSTGRIKAAVQSYGNRMASLRK--MLLGMDRQarpgDRLALIGPVTHASGMLMQPFL-YCGATLVLF--DRFEPAHF 237
Cdd:PRK08633 789 FSSGSEGEPKGVMLSHHNILSNIEQisDVFNLRND----DVILSSLPFFHSFGLTVTLWLpLLEGIKVVYhpDPTDALGI 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 238 LAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAAPMaPARIREAW-ERIGPILSQGYGASEsTSGVTRLS 316
Cdd:PRK08633 865 AKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKL-KPEVADAFeEKFGIRILEGYGATE-TSPVASVN 942
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 317 TADHAEA-----IAGRPGrlaSCGRPHGETEVRVVD-EQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVD----G 386
Cdd:PRK08633 943 LPDVLAAdfkrqTGSKEG---SVGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIKDidgiG 1019
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 387 WLRTGDLARVDEEGFIYLVDRkkdmiIS-----GGFNVYPTEVE----AVLYQHPDVMeaCVISVPDATWGESVkaVVAL 457
Cdd:PRK08633 1020 WYVTGDKGHLDEDGFLTITDR-----YSrfakiGGEMVPLGAVEeelaKALGGEEVVF--AVTAVPDEKKGEKL--VVLH 1090
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1092251577 458 RPGraleaAALIAHCRERIADYK-----TPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:PRK08633 1091 TCG-----AEDVEELKRAIKESGlpnlwKPSRYFKVEALPLLGSGKLDLKGLKE 1139
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
163-506 |
3.00e-29 |
|
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: 120.34 E-value: 3.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 163 FSSGSTGRIKAAVQSYGNRMASLR--KMLLGMDRQARpgdrlaligpV----THASGMLMQPFLY---CGATLVL---FD 230
Cdd:cd05918 113 FTSGSTGKPKGVVIEHRALSTSALahGRALGLTSESR----------VlqfaSYTFDVSILEIFTtlaAGGCLCIpseED 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 231 RFEpahFLAEVA-RLRITHVFMVPAMIHMLlaDPAleqaDLSSLKTLSYGAAPMAPARIREAWERIGpiLSQGYGASEST 309
Cdd:cd05918 183 RLN---DLAGFInRLRVTWAFLTPSVARLL--DPE----DVPSLRTLVLGGEALTQSDVDTWADRVR--LINAYGPAECT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 310 SGVTRlstadhaeAIAGRPGRLASCGRPHGETeVRVVDEQ--GREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDG- 386
Cdd:cd05918 252 IAATV--------SPVVPSTDPRNIGRPLGAT-CWVVDPDnhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDp 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 387 -WL------------RTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQH-PDVMEACV--ISVPDATWGES 450
Cdd:cd05918 323 aWLkqegsgrgrrlyRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVevVKPKDGSSSPQ 402
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092251577 451 VKAVVALRPGR-----------------ALEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:cd05918 403 LVAFVVLDGSSsgsgdgdslflepsdefRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRE 475
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
51-506 |
3.13e-29 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 121.43 E-value: 3.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 51 GDRVAVQSRNCAELVEIecaLYKSGLVKAALNP----------RFTAAEASDVVENCTPR-------AFIGGDGYTGYAR 113
Cdd:PRK05620 64 DQRVGSMMYNCAEHLEV---LFAVACMGAVFNPlnkqlmndqiVHIINHAEDEVIVADPRlaeqlgeILKECPCVRAVVF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 114 TTPGFAAVEAFVALGGPAAgyLGYEDLLARGGTSRPPHRAAAADAAVLHFSSGSTGRIKAAVqsYGNRMASLRKMLLgmd 193
Cdd:PRK05620 141 IGPSDADSAAAHMPEGIKV--YSYEALLDGRSTVYDWPELDETTAAAICYSTGTTGAPKGVV--YSHRSLYLQSLSL--- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 194 rqaRPGDRLAligpVTHAsgmlmQPFLYC------------------GATLVLFDRFEPAHFLAEV---ARLRITHvfMV 252
Cdd:PRK05620 214 ---RTTDSLA----VTHG-----ESFLCCvpiyhvlswgvplaafmsGTPLVFPGPDLSAPTLAKIiatAMPRVAH--GV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 253 PA-----MIHMLLADPaleqaDLSSLKTLSYGAAPMAPARIReAWE-RIGPILSQGYGASESTSgvtrLSTADHAEAIAG 326
Cdd:PRK05620 280 PTlwiqlMVHYLKNPP-----ERMSLQEIYVGGSAVPPILIK-AWEeRYGVDVVHVWGMTETSP----VGTVARPPSGVS 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 327 RPGRLA---SCGRPHGETEVRVVDEqGREVEGD--AIGEIVIRGEDVFQGYWGEP-----------------ELTREVLV 384
Cdd:PRK05620 350 GEARWAyrvSQGRFPASLEYRIVND-GQVMESTdrNEGEIQVRGNWVTASYYHSPteegggaastfrgedveDANDRFTA 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 385 DGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPG--RA 462
Cdd:PRK05620 429 DGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGiePT 508
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1092251577 463 LEAAALIA-HCRERIADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:PRK05620 509 RETAERLRdQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
5-507 |
6.42e-29 |
|
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: 119.74 E-value: 6.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 5 LFLQRAARYwGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPR 84
Cdd:cd17655 2 LFEEQAEKT-PDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 85 FTAAEASdvvenctpraFIGGDGYTGYARTTPGFAAVEAFVALggpaAGYLGYEDLLARGGTSRPPHRAAAADAAVLhFS 164
Cdd:cd17655 81 YPEERIQ----------YILEDSGADILLTQSHLQPPIAFIGL----IDLLDEDTIYHEESENLEPVSKSDDLAYVI-YT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 165 SGSTGRIKAAV---QSYGNRMASLRKMLLgmdrQARpGDRLALIGPVT-HASGMLMQPFLYCGATLVLFDRFE--PAHFL 238
Cdd:cd17655 146 SGSTGKPKGVMiehRGVVNLVEWANKVIY----QGE-HLRVALFASISfDASVTEIFASLLSGNTLYIVRKETvlDGQAL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 239 AEVAR-LRITHVFMVPAMIHMLladPALEQADLSSLKTLSYGAAPMAPARIREAWERIG--PILSQGYGASESTSGVTrL 315
Cdd:cd17655 221 TQYIRqNRITIIDLTPAHLKLL---DAADDSEGLSLKHLIVGGEALSTELAKKIIELFGtnPTITNAYGPTETTVDAS-I 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 316 STADHAEAIAGRPgrlaSCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDG-------WL 388
Cdd:cd17655 297 YQYEPETDQQVSV----PIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDpfvpgerMY 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 389 RTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRpgRALEAAAL 468
Cdd:cd17655 373 RTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSE--KELPVAQL 450
|
490 500 510
....*....|....*....|....*....|....*....
gi 1092251577 469 IAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVREP 507
Cdd:cd17655 451 REFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPEP 489
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
116-501 |
2.05e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 118.56 E-value: 2.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 116 PGFAAVEAFVALGGpaaGYLGYEDLLARGGTSRPPhrAAAADAAVLHFSSGSTGRIKAAVQSYGNRMASLRKMLLGMdrQ 195
Cdd:PRK07768 117 PFLAAAPVLEEKGI---RVLTVADLLAADPIDPVE--TGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAA--E 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 196 ARPG-DRLALIGPVTHASGM---LMQPfLYCGATLVLFdrfEPAHFLAE-------VARLRIThVFMVPAMIHMLLADPA 264
Cdd:PRK07768 190 FDVEtDVMVSWLPLFHDMGMvgfLTVP-MYFGAELVKV---TPMDFLRDpllwaelISKYRGT-MTAAPNFAYALLARRL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 265 LEQA-----DLSSLKTLSYGAAPMAPARIR---EAWERIG---PILSQGYGASESTSGVT--------RLSTADhAEAIA 325
Cdd:PRK07768 265 RRQAkpgafDLSSLRFALNGAEPIDPADVEdllDAGARFGlrpEAILPAYGMAEATLAVSfspcgaglVVDEVD-ADLLA 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 326 ----------GRPGRLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYW---GEPELTREvlvDGWLRTGD 392
Cdd:PRK07768 344 alrravpatkGNTRRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGYLtmdGFIPAQDA---DGWLDTGD 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 393 LARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVP-DATWGESVKAVVAlrPGRALEAAALIAH 471
Cdd:PRK07768 421 LGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRlDAGHSREGFAVAV--ESNAFEDPAEVRR 498
|
410 420 430
....*....|....*....|....*....|....*...
gi 1092251577 472 CRERIADYKT------PRSVEFV--GELPKNPSGKVAR 501
Cdd:PRK07768 499 IRHQVAHEVVaevgvrPRNVVVLgpGSIPKTPSGKLRR 536
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
23-509 |
9.75e-28 |
|
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: 115.99 E-value: 9.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 23 RERVLSFRQLDERSTRLANA-LLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVENCTPRA 101
Cdd:cd05937 2 EGKTWTYSETYDLVLRYAHWlHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 102 FIGGDGYtgyarttpgfaaveafvalggPAAgylgyedllarggtsrpphraaaadaavLHFSSGSTGRIKAAVQSygNR 181
Cdd:cd05937 82 VIVDPDD---------------------PAI----------------------------LIYTSGTTGLPKAAAIS--WR 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 182 MASLRKMLLGMDRQARPGDRLALIGPVTHASGMLMQpFLYC---GATLVLFDRFEPAHFLAEVARLRITHVFMVPAMIHM 258
Cdd:cd05937 111 RTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLG-ACNClmsGGTLALSRKFSASQFWKDVRDSGATIIQYVGELCRY 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 259 LLADPAlEQADLSSLKTLSYGAApMAParirEAWERIG-----PILSQGYGASESTSGVTRLSTADHAEAIAGRPGRLAS 333
Cdd:cd05937 190 LLSTPP-SPYDRDHKVRVAWGNG-LRP----DIWERFRerfnvPEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 334 CGRPHGETEVRVVDEQG---------------REVEGDAIGEIVIRGEDVFQGYWGEPELTREVLV-------DGWLRTG 391
Cdd:cd05937 264 WKFENQVVLVKMDPETDdpirdpktgfcvrapVGEPGEMLGRVPFKNREAFQGYLHNEDATESKLVrdvfrkgDIYFRTG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 392 DLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACV--ISVPDATwGESVKAVVALRPGRALEA---- 465
Cdd:cd05937 344 DLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygVKVPGHD-GRAGCAAITLEESSAVPTeftk 422
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1092251577 466 AALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVREPYW 509
Cdd:cd05937 423 SLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGV 466
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
166-506 |
1.04e-27 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 115.48 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 166 GSTGRIKAAVQSYGNRMASLRkmllGMDR--QARPGDRLALIgPVTHASGmLMQ---PFLyCGATLVLFD--RFEPAhfl 238
Cdd:PRK07445 130 GSSGQIRFAIHTWETLTASVQ----GFQRyfQLQQVNSFCVL-PLYHVSG-LMQfmrSFL-TGGKLVILPykRLKSG--- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 239 aEVARLRITHVF--MVPAMIHMLLaDPALEQadLSSLKTLSYGAAPMAPARIREAWE---RIGPIlsqgYGASESTSGVT 313
Cdd:PRK07445 200 -QELPPNPSDFFlsLVPTQLQRLL-QLRPQW--LAQFRTILLGGAPAWPSLLEQARQlqlRLAPT----YGMTETASQIA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 314 RLSTADHaeaIAGRpgrlASCGR--PHgeteVRVvdeqgrEVEGDAIGEIVIRGEDVFQGYWgePELTREvlvDGWLRTG 391
Cdd:PRK07445 272 TLKPDDF---LAGN----NSSGQvlPH----AQI------TIPANQTGNITIQAQSLALGYY--PQILDS---QGIFETD 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 392 DLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGrALEAAALIAH 471
Cdd:PRK07445 330 DLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP-SISLEELKTA 408
|
330 340 350
....*....|....*....|....*....|....*
gi 1092251577 472 CRERIADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:PRK07445 409 IKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
163-517 |
1.23e-27 |
|
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: 115.53 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 163 FSSGSTGRIKAAVQSYGNRMASLRKMLLGMdrQARPGDRLALIGPVTHASGMLMQPFLY-CGATLVLFdrfEPAHFLAEV 241
Cdd:cd17640 95 YTSGTTGNPKGVMLTHANLLHQIRSLSDIV--PPQPGDRFLSILPIWHSYERSAEYFIFaCGCSQAYT---SIRTLKDDL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 242 ARLRITHVFMVP--------AMIHMLLADPALEQADLSSLKT-------LSyGAAPMAPaRIREAWERIGPILSQGYGAS 306
Cdd:cd17640 170 KRVKPHYIVSVPrlweslysGIQKQVSKSSPIKQFLFLFFLSggifkfgIS-GGGALPP-HVDTFFEAIGIEVLNGYGLT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 307 EsTSGVtrLSTADHAEAIAGrpgrlaSCGRPHGETEVRVVDEQGREVEGDAI-GEIVIRGEDVFQGYWGEPELTREVL-V 384
Cdd:cd17640 248 E-TSPV--VSARRLKCNVRG------SVGRPLPGTEIKIVDPEGNVVLPPGEkGIVWVRGPQVMKGYYKNPEATSKVLdS 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 385 DGWLRTGDLARVDEEGFIYLVDRKKDMII-SGGFNVYPTEVEAVLYQHPDVMEACVIsvpdatwGESVKAVvalrpgral 463
Cdd:cd17640 319 DGWFNTGDLGWLTCGGELVLTGRAKDTIVlSNGENVEPQPIEEALMRSPFIEQIMVV-------GQDQKRL--------- 382
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1092251577 464 eaAALIAHCRERIADYKTPRSVefvgELPKNPSGKVARKVVREPYWQGVARRVN 517
Cdd:cd17640 383 --GALIVPNFEELEKWAKESGV----KLANDRSQLLASKKVLKLYKNEIKDEIS 430
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
161-511 |
2.15e-27 |
|
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: 115.28 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 161 LHFSSGSTGRIKAAVQSYGNRMASLRKMLLGMDRQARpgDRLALIGPVTHASGML---MQPfLYCGAT-----LVLFDRf 232
Cdd:cd05908 111 IQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTK--DRILSWMPLTHDMGLIafhLAP-LIAGMNqylmpTRLFIR- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 233 EPAHFLAEVARLRITHV----FMVPAMIHMLlADPALEQADLSSLKTLSYGAAPMAPARIREAWERIGP-------ILSQ 301
Cdd:cd05908 187 RPILWLKKASEHKATIVsspnFGYKYFLKTL-KPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKyglkrnaILPV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 302 gYGASESTSGVT--------RLSTADHAEAIAGRPG-----------RLASCGRPHGETEVRVVDEQGREVEGDAIGEIV 362
Cdd:cd05908 266 -YGLAEASVGASlpkaqspfKTITLGRRHVTHGEPEpevdkkdseclTFVEVGKPIDETDIRICDEDNKILPDGYIGHIQ 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 363 IRGEDVFQGYWGEPELTREVLV-DGWLRTGDLARVdEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVM--EACV 439
Cdd:cd05908 345 IRGKNVTPGYYNNPEATAKVFTdDGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVElgRVVA 423
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092251577 440 ISVPDATWGESVKAVVALRPGRALEAAALIAHCRERIADYKTPRSVEFV--GELPKNPSGKVARKVVREPYWQG 511
Cdd:cd05908 424 CGVNNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHLNKRGGWQINEVLpiRRIPKTTSGKVKRYELAQRYQSG 497
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
27-485 |
2.54e-27 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 114.48 E-value: 2.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 27 LSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVENCTPRAFIGGd 106
Cdd:cd05910 3 LSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFIGI- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 107 gytgyarttpgFAAVEafvalggPAAgylgyedllarggtsrpphraaaadaavLHFSSGSTGRIKAAVQSYGNRMASLR 186
Cdd:cd05910 82 -----------PKADE-------PAA----------------------------ILFTSGSTGTPKGVVYRHGTFAAQID 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 187 kmLLGMDRQARPGDR-LALIGPVThasgmLMQPFLycGATLVLFD-------RFEPAHFLAEVARLRITHVFMVPAMIHM 258
Cdd:cd05910 116 --ALRQLYGIRPGEVdLATFPLFA-----LFGPAL--GLTSVIPDmdptrpaRADPQKLVGAIRQYGVSIVFGSPALLER 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 259 LLADPALEQADLSSLKTLSYGAAPMAPA---RIREAWERIGPILSQgYGASES---TSGVTRLSTADHAEAIAgrPGRLA 332
Cdd:cd05910 187 VARYCAQHGITLPSLRRVLSAGAPVPIAlaaRLRKMLSDEAEILTP-YGATEAlpvSSIGSRELLATTTAATS--GGAGT 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 333 SCGRPHGETEVRVVD---------EQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDG-----WLRTGDLARVDE 398
Cdd:cd05910 264 CVGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDnsegfWHRMGDLGYLDD 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 399 EGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVkAVVALRPGRALEAAALIAHCRERIAD 478
Cdd:cd05910 344 EGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPV-LCVEPLPGTITPRARLEQELRALAKD 422
|
....*..
gi 1092251577 479 YKTPRSV 485
Cdd:cd05910 423 YPHTQRI 429
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
163-502 |
5.17e-27 |
|
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: 113.68 E-value: 5.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 163 FSSGSTGRIKAAVQSYgnrmASLRKMLLGMDRQ--ARPGDRLALIGPVT-HASGMLMQPFLYCGATLVLFD---RFEPAH 236
Cdd:cd17644 113 YTSGSTGKPKGVMIEH----QSLVNLSHGLIKEygITSSDRVLQFASIAfDVAAEEIYVTLLSGATLVLRPeemRSSLED 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 237 FLAEVARLRITHVFMVPAMIHMLLADPALEQADL-SSLKTLSYGAAPMAPARIREAWERIG--PILSQGYGASESTSGVT 313
Cdd:cd17644 189 FVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLpSSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAAT 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 314 -RLSTADHAEAIAGRPgrlasCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLV-------- 384
Cdd:cd17644 269 vCRLTQLTERNITSVP-----IGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFIshpfnsse 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 385 -DGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRAL 463
Cdd:cd17644 344 sERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESP 423
|
330 340 350
....*....|....*....|....*....|....*....
gi 1092251577 464 EAAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARK 502
Cdd:cd17644 424 STVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRR 462
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
5-507 |
6.57e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 115.82 E-value: 6.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 5 LFLQRAARYwGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPR 84
Cdd:PRK12316 3062 LFEEQVERT-PDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPE 3140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 85 FTAAEASDVVENCTPRAFIggdgyTGYARTTPGFAAVEAFVALGGPaagylgyEDLlargGTSRPPHRAAAADAAVLHFS 164
Cdd:PRK12316 3141 YPEERLAYMLEDSGAQLLL-----SQSHLRLPLAQGVQVLDLDRGD-------ENY----AEANPAIRTMPENLAYVIYT 3204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 165 SGSTGRIKAAVQSYGNRMASLRKMLLGMDRQArpGDRLALIGPVT-HASGMLMQPFLYCGATLVLFDR---FEPAHFLAE 240
Cdd:PRK12316 3205 SGSTGKPKGVGIRHSALSNHLCWMQQAYGLGV--GDRVLQFTTFSfDVFVEELFWPLMSGARVVLAGPedwRDPALLVEL 3282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 241 VARLRITHVFMVPAMIHMLLADPalEQADLSSLKTLSYGAAPMaPARIREAWERIGPILSQgYGASESTSGVTRLSTADH 320
Cdd:PRK12316 3283 INSEGVDVLHAYPSMLQAFLEEE--DAHRCTSLKRIVCGGEAL-PADLQQQVFAGLPLYNL-YGPTEATITVTHWQCVEE 3358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 321 AEAiagrpgrLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLV-------DGWLRTGDL 393
Cdd:PRK12316 3359 GKD-------AVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVpdpfvpgERLYRTGDL 3431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 394 ARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPdatwGESVKAVVALRPGRALEAAALIAHCR 473
Cdd:PRK12316 3432 ARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVD----GRQLVAYVVPEDEAGDLREALKAHLK 3507
|
490 500 510
....*....|....*....|....*....|....
gi 1092251577 474 ERIADYKTPRSVEFVGELPKNPSGKVARKVVREP 507
Cdd:PRK12316 3508 ASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRP 3541
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
4-507 |
1.06e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 115.26 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 4 ALFLQRAARYWgDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNP 83
Cdd:PRK12467 1578 QLIEDQAAATP-EAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDP 1656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 84 RFTAAEASDVVENCTPRAFIGgdgytgYARTTPGFAAVEAFVALGGPAAGylgyeDLLARGGTSRPPHRAAAADAAVLHF 163
Cdd:PRK12467 1657 EYPRERLAYMIEDSGIELLLT------QSHLQARLPLPDGLRSLVLDQED-----DWLEGYSDSNPAVNLAPQNLAYVIY 1725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 164 SSGSTGRIKAAVQSYGNRMASLRKMllGMDRQARPGDRLALIGP----VTHASgmLMQPFLYcGATLVLFDRFE---PAH 236
Cdd:PRK12467 1726 TSGSTGRPKGAGNRHGALVNRLCAT--QEAYQLSAADVVLQFTSfafdVSVWE--LFWPLIN-GARLVIAPPGAhrdPEQ 1800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 237 FLAEVARLRITHVFMVPAMIHMLLADPALEQADLSsLKTLSYGAAPMAPARIREAWERIGPI-LSQGYGASESTSGVTrL 315
Cdd:PRK12467 1801 LIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLS-LRRVVCGGEALEVEALRPWLERLPDTgLFNLYGPTETAVDVT-H 1878
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 316 STADHAEAiagrPGRLAS-CGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLV-------DGW 387
Cdd:PRK12467 1879 WTCRRKDL----EGRDSVpIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVadpfgtvGSR 1954
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 388 L-RTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPG------ 460
Cdd:PRK12467 1955 LyRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGANGKQLVAYVVPTDPGlvddde 2034
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1092251577 461 -RALEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVREP 507
Cdd:PRK12467 2035 aQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAP 2082
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
161-505 |
3.72e-26 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 113.72 E-value: 3.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 161 LHFSSGSTGRIKAAVQSYGNRMASLRKMLLGMDRQARPGDRLALIGPVTHASGM---LMQPfLYCGATLVLFdrfEPAHF 237
Cdd:PRK05691 171 LQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPDDVIVSWLPLYHDMGLiggLLQP-IFSGVPCVLM---SPAYF 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 238 LAEVARL--RITH----VFMVPAMIHML----LADPALEQADLSSLKTLSYGAAPMAPARIREAWERIGPI------LSQ 301
Cdd:PRK05691 247 LERPLRWleAISEyggtISGGPDFAYRLcserVSESALERLDLSRWRVAYSGSEPIRQDSLERFAEKFAACgfdpdsFFA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 302 GYGASEST---------SGVTRLS------TADHAEAIAGRPgrLASCGRPHGETEVRVVDEQGREVEGD-AIGEIVIRG 365
Cdd:PRK05691 327 SYGLAEATlfvsggrrgQGIPALEldaealARNRAEPGTGSV--LMSCGRSQPGHAVLIVDPQSLEVLGDnRVGEIWASG 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 366 EDVFQGYWGEPELTREVLV--DG--WLRTGDLARVdEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVIS 441
Cdd:PRK05691 405 PSIAHGYWRNPEASAKTFVehDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVRKGRVA 483
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092251577 442 V----PDATWGESVKAVVALRPGRALEAAALIAHCRERIAD--YKTPRSVEFV--GELPKNPSGKVARKVVR 505
Cdd:PRK05691 484 AfavnHQGEEGIGIAAEISRSVQKILPPQALIKSIRQAVAEacQEAPSVVLLLnpGALPKTSSGKLQRSACR 555
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
16-502 |
4.53e-26 |
|
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: 110.63 E-value: 4.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 16 DRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEAsdvve 95
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 96 nctprAFIGGDGYTGYARTTPGFAAveafvalggpaagYLGYedllarggtsrpphraaaadaavlhfSSGSTGRIKAAV 175
Cdd:cd17650 77 -----QYMLEDSGAKLLLTQPEDLA-------------YVIY--------------------------TSGTTGKPKGVM 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 176 QSYGN--RMASLRKMLLGMDRQARPGDRLALIGPVTHASGMLMQpfLYCGATLVLFD---RFEPAHFLAEVARLRITHVF 250
Cdd:cd17650 113 VEHRNvaHAAHAWRREYELDSFPVRLLQMASFSFDVFAGDFARS--LLNGGTLVICPdevKLDPAALYDLILKSRITLME 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 251 MVPAMIHMLLADPALEQADLSSLKTLSYGAAPMAPARIREAWERIGP--ILSQGYGASEST--SGVTRLStADHAEAIAG 326
Cdd:cd17650 191 STPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQgmRIINSYGVTEATidSTYYEEG-RDPLGDSAN 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 327 RPgrlasCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDGWL-------RTGDLARVDEE 399
Cdd:cd17650 270 VP-----IGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermyRTGDLARWRAD 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 400 GFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVAlrPGRALEAAALIAHCRERIADY 479
Cdd:cd17650 345 GNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVV--AAATLNTAELRAFLAKELPSY 422
|
490 500
....*....|....*....|...
gi 1092251577 480 KTPRSVEFVGELPKNPSGKVARK 502
Cdd:cd17650 423 MIPSYYVQLDALPLTPNGKVDRR 445
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
423-498 |
1.01e-25 |
|
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: 100.31 E-value: 1.01e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092251577 423 EVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGK 498
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
5-506 |
4.19e-25 |
|
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: 107.78 E-value: 4.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 5 LFLQRAARyWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPR 84
Cdd:cd17653 2 AFERIAAA-HPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 85 FTAAEASDVVENCTPRAFIggdgYTGYARTTpgfaaveAFVAlggpaagylgyedllarggtsrpphraaaadaavlhFS 164
Cdd:cd17653 81 LPSARIQAILRTSGATLLL----TTDSPDDL-------AYII------------------------------------FT 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 165 SGSTGRIKAAVQSYGNRMASLRKMLLGMDrqARPGDRLALI-GPVTHAS-GMLMQPFLYcGATLVLFDrfePAHFLAEVA 242
Cdd:cd17653 114 SGSTGIPKGVMVPHRGVLNYVSQPPARLD--VGPGSRVAQVlSIAFDACiGEIFSTLCN-GGTLVLAD---PSDPFAHVA 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 243 RlrITHVFMV-PAMIHMLlaDPAleqaDLSSLKTLSYGAAPMAPARIREAWEriGPILSQGYGASESTSGVTRLSTadha 321
Cdd:cd17653 188 R--TVDALMStPSILSTL--SPQ----DFPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMTEL---- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 322 eaiagRPGRLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELT-REVLVDGW------LRTGDLA 394
Cdd:cd17653 254 -----LPGQPVTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTaSKFVPDPFwpgsrmYRTGDYG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 395 RVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQ-HPDVMEACVISVPDatwgesvkAVVALRPGRALEAAALIAHCR 473
Cdd:cd17653 329 RWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQsQPEVTQAAAIVVNG--------RLVAFVTPETVDVDGLRSELA 400
|
490 500 510
....*....|....*....|....*....|...
gi 1092251577 474 ERIADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:cd17653 401 KHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
164-506 |
3.60e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 100.89 E-value: 3.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 164 SSGSTGRIKAAVQSYGNRMASLRKMllgMDRQARPGDRLaLIGPVTHASGM--LMQPFLyCGATLVLFD---RFEPAHFL 238
Cdd:PRK07824 43 TSGTTGTPKGAMLTAAALTASADAT---HDRLGGPGQWL-LALPAHHIAGLqvLVRSVI-AGSEPVELDvsaGFDPTALP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 239 AEVARLRITHVF--MVPAMIHMLLADPALEQAdLSSLKTLSYGAAPMaPARIREAWERIGPILSQGYGASESTSGvtrls 316
Cdd:PRK07824 118 RAVAELGGGRRYtsLVPMQLAKALDDPAATAA-LAELDAVLVGGGPA-PAPVLDAAAAAGINVVRTYGMSETSGG----- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 317 tadhaeaiagrpgrlasC---GRPHGETEVRVVDeqgrevegdaiGEIVIRGEDVFQGYWGEPElTREVLVDGWLRTGDL 393
Cdd:PRK07824 191 -----------------CvydGVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPVD-PDPFAEPGWFRTDDL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 394 ARVDEeGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAAALIAHCR 473
Cdd:PRK07824 242 GALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLEALRAHVA 320
|
330 340 350
....*....|....*....|....*....|...
gi 1092251577 474 ERIADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:PRK07824 321 RTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
4-510 |
5.55e-23 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 102.80 E-value: 5.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 4 ALFLQRAARY-WGDRPAVMHRErVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALN 82
Cdd:PRK06060 8 GLLAEQASEAgWYDRPAFYAAD-VVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLAN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 83 P-----------RFTAA-------------EASDVVEnctprafiGGDGYTGYARTTPGfaaveAFVALGGPAAGYLGYe 138
Cdd:PRK06060 87 PelhrddhalaaRNTEPalvvtsdalrdrfQPSRVAE--------AAELMSEAARVAPG-----GYEPMGGDALAYATY- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 139 dllarggtsrpphraaaadaavlhfSSGSTGRIKAAVQSYGNRMASLRKMLLGMDRQArPGDRLALIGPVTHASGM---L 215
Cdd:PRK06060 153 -------------------------TSGTTGPPKAAIHRHADPLTFVDAMCRKALRLT-PEDTGLCSARMYFAYGLgnsV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 216 MQPFLYCGATLVlfdrfEPAHFLAEVA-----RLRITHVFMVPAMIHMLLAdpALEQADLSSLKTLSYGAAPMAPARIRE 290
Cdd:PRK06060 207 WFPLATGGSAVI-----NSAPVTPEAAailsaRFGPSVLYGVPNFFARVID--SCSPDSFRSLRCVVSAGEALELGLAER 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 291 AWERIG--PILSqGYGASEStsGVTRLS-TADHaeaiaGRPGRLASCGRPHgetEVRVVDEQGREVEGDAIGEIVIRGED 367
Cdd:PRK06060 280 LMEFFGgiPILD-GIGSTEV--GQTFVSnRVDE-----WRLGTLGRVLPPY---EIRVVAPDGTTAGPGVEGDLWVRGPA 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 368 VFQGYWGEPE--LTREvlvdGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDA 445
Cdd:PRK06060 349 IAKGYWNRPDspVANE----GWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRES 424
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092251577 446 TWGESVKAVVALRPGRALEAAALI-AHCR--ERIADYKTPRSVEFVGELPKNPSGKVARKVVR-----EPYWQ 510
Cdd:PRK06060 425 TGASTLQAFLVATSGATIDGSVMRdLHRGllNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRkqsptKPIWE 497
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
7-510 |
1.31e-22 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 102.55 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 7 LQRAARYWGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFT 86
Cdd:PRK05691 1137 LNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYP 1216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 87 AAEASDVVENCTPRAFIGGDGYTGYARTTPGFAAVeafvALggpaagylgyEDLLARGGTSRPP--HRAAAADAAVLHfS 164
Cdd:PRK05691 1217 AERLAYMLADSGVELLLTQSHLLERLPQAEGVSAI----AL----------DSLHLDSWPSQAPglHLHGDNLAYVIY-T 1281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 165 SGSTGRIKAAvqsyGNRMASLRKMLLGMDrqarpgDRLALigpvtHASGMLMQ--PF------------LYCGATLVLF- 229
Cdd:PRK05691 1282 SGSTGQPKGV----GNTHAALAERLQWMQ------ATYAL-----DDSDVLMQkaPIsfdvsvwecfwpLITGCRLVLAg 1346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 230 --DRFEPAHFLAEVARLRITHVFMVPAMIHMLLADPALeqADLSSLKTLSYGAAPMAPARIREAWERIGPI-LSQGYGAS 306
Cdd:PRK05691 1347 pgEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLA--AACTSLRRLFSGGEALPAELRNRVLQRLPQVqLHNRYGPT 1424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 307 ESTSGVT--RLSTADhaeaiagrpGRLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLV 384
Cdd:PRK05691 1425 ETAINVThwQCQAED---------GERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFV 1495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 385 ------DG--WLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVIsVPDATWGESVKAVVA 456
Cdd:PRK05691 1496 pdplgeDGarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-VREGAAGAQLVGYYT 1574
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1092251577 457 LRPGRALEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVREPYWQ 510
Cdd:PRK05691 1575 GEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQ 1628
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
161-504 |
1.79e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 99.73 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 161 LHFSSGSTG---RIKAAVQSYGNRMASLRKMLlgmdrqARPGDRLALIG-PVTHASGmlmqpfLYCGaTLVLFDRFEPAH 236
Cdd:PRK08308 106 LQYSSGTTGepkLIRRSWTEIDREIEAYNEAL------NCEQDETPIVAcPVTHSYG------LICG-VLAALTRGSKPV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 237 FLAE------VARLRITH---VFMVPAMIHMLladPALEQADLSSLKTLSYGAaPMAPARIREAWERiGPILSQGYGASE 307
Cdd:PRK08308 173 IITNknpkfaLNILRNTPqhiLYAVPLMLHIL---GRLLPGTFQFHAVMTSGT-PLPEAWFYKLRER-TTYMMQQYGCSE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 308 StsGVTRLS--TADHAEAiaGRPgrlascgRPHgeteVRVVDEQGRevegDAIGEIVIRGEDvfqgywgepeltREVlvd 385
Cdd:PRK08308 248 A--GCVSICpdMKSHLDL--GNP-------LPH----VSVSAGSDE----NAPEEIVVKMGD------------KEI--- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 386 gwlRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGraLEA 465
Cdd:PRK08308 294 ---FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEE--IDP 368
|
330 340 350
....*....|....*....|....*....|....*....
gi 1092251577 466 AALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVV 504
Cdd:PRK08308 369 VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
203-505 |
2.69e-22 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 100.60 E-value: 2.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 203 ALIGPVTHASGMLMQPfLYCGATLVLF----DRFEPAHFLAEVARLRITHVFMVPAMIHMLLA--DPALEQADLSSLKTL 276
Cdd:PRK00174 294 ADVGWVTGHSYIVYGP-LANGATTLMFegvpNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKegDEHPKKYDLSSLRLL 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 277 -SYGAaPMAParirEAWE----RIG----PILS---QgygaSEsTSG--VTRLstadhAEAIAGRPGrlaSCGRPHGETE 342
Cdd:PRK00174 373 gSVGE-PINP----EAWEwyykVVGgercPIVDtwwQ----TE-TGGimITPL-----PGATPLKPG---SATRPLPGIQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 343 VRVVDEQGREVEGDAIGEIVI--------RG-----EDVFQGYWGEpeltrevlVDGWLRTGDLARVDEEGFIYLVDRKK 409
Cdd:PRK00174 435 PAVVDEEGNPLEGGEGGNLVIkdpwpgmmRTiygdhERFVKTYFST--------FKGMYFTGDGARRDEDGYYWITGRVD 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 410 DMI-ISG---GfnvyPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRALEAA---ALIAHCRERIADYKTP 482
Cdd:PRK00174 507 DVLnVSGhrlG----TAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDElrkELRNWVRKEIGPIAKP 582
|
330 340
....*....|....*....|...
gi 1092251577 483 RSVEFVGELPKNPSGKVARKVVR 505
Cdd:PRK00174 583 DVIQFAPGLPKTRSGKIMRRILR 605
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
279-445 |
2.89e-21 |
|
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: 96.90 E-value: 2.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 279 GAAPMAPA---RIREAwerIGPILSQGYGASESTSGVTrlsTADHAEAIAGrpgrlaSCGRPHGETEVRVVD--EQGREV 353
Cdd:cd05927 282 GSAPLSPEvleFLRVA---LGCPVLEGYGQTECTAGAT---LTLPGDTSVG------HVGGPLPCAEVKLVDvpEMNYDA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 354 EG-DAIGEIVIRGEDVFQGYWGEPELTREVL-VDGWLRTGDLARVDEEGFIYLVDRKKDMI-ISGGFNVYPTEVEAVLYQ 430
Cdd:cd05927 350 KDpNPRGEVCIRGPNVFSGYYKDPEKTAEALdEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIENIYAR 429
|
170 180
....*....|....*....|....*.
gi 1092251577 431 HPDVMEACV-----------ISVPDA 445
Cdd:cd05927 430 SPFVAQIFVygdslksflvaIVVPDP 455
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
295-446 |
2.09e-20 |
|
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: 94.20 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 295 IGPILsQGYGASESTSGVTRLSTADHAEAIAGRPgrLASCgrphgetEVRVVD--EQGREVEGDAI-GEIVIRGEDVFQG 371
Cdd:cd17639 274 LCPVI-QGYGLTETCAGGTVQDPGDLETGRVGPP--LPCC-------EIKLVDweEGGYSTDKPPPrGEILIRGPNVFKG 343
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092251577 372 YWGEPELTREVLV-DGWLRTGDLARVDEEGFIYLVDRKKDMI-ISGGFNVYPTEVEAVLYQHPDVMEACVISVPDAT 446
Cdd:cd17639 344 YYKNPEKTKEAFDgDGWFHTGDIGEFHPDGTLKIIDRKKDLVkLQNGEYIALEKLESIYRSNPLVNNICVYADPDKS 420
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
5-502 |
7.16e-20 |
|
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: 92.23 E-value: 7.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 5 LFLQRAARYwGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPR 84
Cdd:cd17645 3 LFEEQVERT-PDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 85 FTAAEAsdvvenctprAFIGGDGytgyarttpgfaavEAFVALGGPaagylgyEDLlarggtsrpphraaaadaAVLHFS 164
Cdd:cd17645 82 YPGERI----------AYMLADS--------------SAKILLTNP-------DDL------------------AYVIYT 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 165 SGSTGRIKAAVQSYGN--RMASLRKMLLGMDrqarPGDRLALIGPVT-HASGMLMQPFLYCGATLvlfdrfepaHFLAEV 241
Cdd:cd17645 113 SGSTGLPKGVMIEHHNlvNLCEWHRPYFGVT----PADKSLVYASFSfDASAWEIFPHLTAGAAL---------HVVPSE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 242 ARL---RITHVFMVPAMIHMLLADPALEQ---ADLSSLKTLSYGAAPMAPArireawERIGPILSQGYGASESTSGVTRL 315
Cdd:cd17645 180 RRLdldALNDYFNQEGITISFLPTGAAEQfmqLDNQSLRVLLTGGDKLKKI------ERKGYKLVNNYGPTENTVVATSF 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 316 STADHAEAIagrpgrlaSCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLV-------DGWL 388
Cdd:cd17645 254 EIDKPYANI--------PIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIvhpfvpgERMY 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 389 RTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVAlrPGRALEAAAL 468
Cdd:cd17645 326 RTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT--APEEIPHEEL 403
|
490 500 510
....*....|....*....|....*....|....
gi 1092251577 469 IAHCRERIADYKTPRSVEFVGELPKNPSGKVARK 502
Cdd:cd17645 404 REWLKNDLPDYMIPTYFVHLKALPLTANGKVDRK 437
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
270-425 |
8.00e-20 |
|
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: 92.81 E-value: 8.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 270 LSSLKTLSYGAAPMaPARIREAWERIGPILSQGYGASEsTSGVTRLSTADHAeaiagrpgRLASCGRPHGETEVRVVDEq 349
Cdd:cd05933 319 LDRCQKFFTGAAPI-SRETLEFFLSLNIPIMELYGMSE-TSGPHTISNPQAY--------RLLSCGKALPGCKTKIHNP- 387
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092251577 350 grevEGDAIGEIVIRGEDVFQGYWGEPELTREVL-VDGWLRTGDLARVDEEGFIYLVDRKKDMII-SGGFNVYPTEVE 425
Cdd:cd05933 388 ----DADGIGEICFWGRHVFMGYLNMEDKTEEAIdEDGWLHSGDLGKLDEDGFLYITGRIKELIItAGGENVPPVPIE 461
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
16-499 |
3.30e-19 |
|
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: 90.15 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 16 DRPAVMHRERVLSFRQLDERSTRLANA-LLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVV 94
Cdd:cd17648 2 DRVAVVYGDKRLTYRELNERANRLAHYlLSVAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 95 ENCTPRAFIGGDGYTGYARttpgfaaveafvalggpaagylgyedllarggtsrpphraaaadaavlhFSSGSTGRIKAA 174
Cdd:cd17648 82 EDTGARVVITNSTDLAYAI-------------------------------------------------YTSGTTGKPKGV 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 175 VQSYG---NRMASLRKMLLGmdrqARPGDRLALIgpvthASGMLMQPF-------LYCGATLVLFD---RFEPAHFLAEV 241
Cdd:cd17648 113 LVEHGsvvNLRTSLSERYFG----RDNGDEAVLF-----FSNYVFDFFveqmtlaLLNGQKLVVPPdemRFDPDRFYAYI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 242 ARLRITHVFMVPAMIHMLladpalEQADLSSLKTLSYGAAPMAPARIREAWERI-GPILSqGYGASES--TSGVTRLSTA 318
Cdd:cd17648 184 NREKVTYLSGTPSVLQQY------DLARLPHLKRVDAAGEEFTAPVFEKLRSRFaGLIIN-AYGPTETtvTNHKRFFPGD 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 319 DHAEAiagrpgrlaSCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLV-----------DG- 386
Cdd:cd17648 257 QRFDK---------SLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLpnpfqteqeraRGr 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 387 ---WLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGES--VKAVVA---LR 458
Cdd:cd17648 328 narLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSriQKYLVGyylPE 407
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1092251577 459 PGrALEAAALIAHCRERIADYKTPRSVEFVGELPKNPSGKV 499
Cdd:cd17648 408 PG-HVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
23-483 |
4.24e-19 |
|
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: 90.43 E-value: 4.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 23 RERVLSFRQLDERSTRLANALLGLGL-RPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVENCTPRA 101
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLAHAGlRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 102 FI-GGDGYTGYARTTPGFAAVEAFVALGGPAAGYLGYEDLLAR--GGTSRPP---HRAAAADA--AVLHFSSGSTGRIKA 173
Cdd:cd05938 82 LVvAPELQEAVEEVLPALRADGVSVWYLSHTSNTEGVISLLDKvdAASDEPVpasLRAHVTIKspALYIYTSGTTGLPKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 174 AVQS-----YGNRMASLRKmllgmdrqARPGDRLALIGPVTHASGMLMQpFLYC---GATLVLFDRFEPAHFLAEVARLR 245
Cdd:cd05938 162 ARIShlrvlQCSGFLSLCG--------VTADDVIYITLPLYHSSGFLLG-IGGCielGATCVLKPKFSASQFWDDCRKHN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 246 ITHVFMVPAMIHMLLADPALEqADLSSLKTLSYGAApmaparIR-EAWE----RIGPI-LSQGYGASESTSGVtrLSTAD 319
Cdd:cd05938 233 VTVIQYIGELLRYLCNQPQSP-NDRDHKVRLAIGNG------LRaDVWReflrRFGPIrIREFYGSTEGNIGF--FNYTG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 320 HAEAIaGRPGRLASCGRPHG------ETEVRVVDEQGR--EVEGDAIGEIV--IRGEDVFQGYWGEPELTREVLV----- 384
Cdd:cd05938 304 KIGAV-GRVSYLYKLLFPFElikfdvEKEEPVRDAQGFciPVAKGEPGLLVakITQQSPFLGYAGDKEQTEKKLLrdvfk 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 385 --DGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACV--ISVPDATwGESVKAVVALRPG 460
Cdd:cd05938 383 kgDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVygVTVPGHE-GRIGMAAVKLKPG 461
|
490 500
....*....|....*....|...
gi 1092251577 461 RALEAAALIAHCRERIADYKTPR 483
Cdd:cd05938 462 HEFDGKKLYQHVREYLPAYARPR 484
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
9-506 |
5.53e-19 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 90.34 E-value: 5.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 9 RAARYW-GDRPAVmhrERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTA 87
Cdd:PLN02654 105 KIAIYWeGNEPGF---DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 88 AEASDVVENCTPRAFIGGDGYTGYARTTPGFAAVEAFV---ALGGPAAGY-LGYEDLLA--RGGTSRPPHRAAAADAAV- 160
Cdd:PLN02654 182 ESLAQRIVDCKPKVVITCNAVKRGPKTINLKDIVDAALdesAKNGVSVGIcLTYENQLAmkREDTKWQEGRDVWWQDVVp 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 161 ------------------LHFSSGSTGRIKAAVQSYGNRM---ASLRKMLLgmdrQARPGDRL---ALIGPVTHASGMLM 216
Cdd:PLN02654 262 nyptkcevewvdaedplfLLYTSGSTGKPKGVLHTTGGYMvytATTFKYAF----DYKPTDVYwctADCGWITGHSYVTY 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 217 QPFLYcGATLVLFDRF----EPAHFLAEVARLRITHVFMVPAMIHMLL--ADPALEQADLSSLKTLSYGAAPMAPARIRE 290
Cdd:PLN02654 338 GPMLN-GATVLVFEGApnypDSGRCWDIVDKYKVTIFYTAPTLVRSLMrdGDEYVTRHSRKSLRVLGSVGEPINPSAWRW 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 291 AWERIG----PIlSQGYGASEsTSG--VTRLSTAdhaeaiagRPGRLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIR 364
Cdd:PLN02654 417 FFNVVGdsrcPI-SDTWWQTE-TGGfmITPLPGA--------WPQKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVK 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 365 GE--DVFQGYWGEP---ELTREVLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACV 439
Cdd:PLN02654 487 KSwpGAFRTLYGDHeryETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAV 566
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 440 ISVPDATWGESVKAVVALRPGRALEA---AALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVRE 506
Cdd:PLN02654 567 VGIEHEVKGQGIYAFVTLVEGVPYSEelrKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 636
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
6-512 |
6.76e-19 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 89.80 E-value: 6.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 6 FLQRAARYWGDRPAVMH---------RERVLSFRQLDERsTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGL 76
Cdd:PRK12476 39 LIERNIANVGDTVAYRYldhshsaagCAVELTWTQLGVR-LRAVGARLQQVAGPGDRVAILAPQGIDYVAGFFAAIKAGT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 77 VKAAL-NPRFTA-AEASDVV-ENCTPRAFIggdgytgyaRTTPGFAAVEAFVAlGGPAAG---YLGYEDLLARGGTSRPP 150
Cdd:PRK12476 118 IAVPLfAPELPGhAERLDTAlRDAEPTVVL---------TTTAAAEAVEGFLR-NLPRLRrprVIAIDAIPDSAGESFVP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 151 HRAAAADAAVLHFSSGSTgRIKAAVQ-SYGNRMASLRKMLLGMDRQARPGDRLALIgPVTHASG--MLMQPFLYCG-ATL 226
Cdd:PRK12476 188 VELDTDDVSHLQYTSGST-RPPVGVEiTHRAVGTNLVQMILSIDLLDRNTHGVSWL-PLYHDMGlsMIGFPAVYGGhSTL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 227 VlfdrfEPAHF----------LAEVARLRIThVFMVPAMIHMLLAD----PALEQADLSSLkTLSYGAAPMAPARIREAW 292
Cdd:PRK12476 266 M-----SPTAFvrrpqrwikaLSEGSRTGRV-VTAAPNFAYEWAAQrglpAEGDDIDLSNV-VLIIGSEPVSIDAVTTFN 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 293 ERIGP------ILSQGYGASESTSGVTRLSTADHAEAI--------AGRPGRLA----------SCGRP-HGETEVRVVD 347
Cdd:PRK12476 339 KAFAPyglprtAFKPSYGIAEATLFVATIAPDAEPSVVyldreqlgAGRAVRVAadapnavahvSCGQVaRSQWAVIVDP 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 348 EQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREV--------LVDG-----------WLRTGDLArVDEEGFIYLVDRK 408
Cdd:PRK12476 419 DTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTfgaklqsrLAEGshadgaaddgtWLRTGDLG-VYLDGELYITGRI 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 409 KDMIISGGFNVYPTEVEA-VLYQHPDVMEACV--ISVPDATWGESVkaVVALR--------PGRALEA--AALIAHCRER 475
Cdd:PRK12476 498 ADLIVIDGRNHYPQDIEAtVAEASPMVRRGYVtaFTVPAEDNERLV--IVAERaagtsradPAPAIDAirAAVSRRHGLA 575
|
570 580 590
....*....|....*....|....*....|....*....
gi 1092251577 476 IADyktprsVEFV--GELPKNPSGKVARKVVREPYWQGV 512
Cdd:PRK12476 576 VAD------VRLVpaGAIPRTTSGKLARRACRAQYLDGR 608
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
138-505 |
4.24e-18 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 87.13 E-value: 4.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 138 EDLLARGGTSR------PPHraaaADAAVLHFSSGSTGRIKAAVQSYGNRMASLRKML--LGMDRqarPGDRLALIGPVT 209
Cdd:PRK05851 132 HDLATAAHTNRsasltpPDS----GGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNarVGLDA---ATDVGCSWLPLY 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 210 HASGM--LMQPFLyCGATLVL--FDRFEPAHF--LAEVARLRITHVfMVPAMIHMLLADPA--LEQADLSSLKTLSYGAA 281
Cdd:PRK05851 205 HDMGLafLLTAAL-AGAPLWLapTTAFSASPFrwLSWLSDSRATLT-AAPNFAYNLIGKYArrVSDVDLGALRVALNGGE 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 282 PM---APARIREAWERIG---PILSQGYGASESTSGVTR------LSTADHAEAIAGRPGRLASCGRPHGETEVRVV-DE 348
Cdd:PRK05851 283 PVdcdGFERFATAMAPFGfdaGAAAPSYGLAESTCAVTVpvpgigLRVDEVTTDDGSGARRHAVLGNPIPGMEVRISpGD 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 349 QGREVEGDAIGEIVIRGEDVFQGYWGEPELTRevlvDGWLRTGDLARVDEEGFIyLVDRKKDMIISGGFNVYPTEVEAVL 428
Cdd:PRK05851 363 GAAGVAGREIGEIEIRGASMMSGYLGQAPIDP----DDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVA 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 429 YQHPDVMEACVISVPDatwGESvkavvALRPGRALEA-------AALIAHCRERIADY--KTPRSVEFV--GELPKNPSG 497
Cdd:PRK05851 438 AQVRGVREGAVVAVGT---GEG-----SARPGLVIAAefrgpdeAGARSEVVQRVASEcgVVPSDVVFVapGSLPRTSSG 509
|
....*...
gi 1092251577 498 KVARKVVR 505
Cdd:PRK05851 510 KLRRLAVK 517
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
6-515 |
5.53e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 87.09 E-value: 5.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 6 FLQRAARYWGDRPAV----MHRER-----VLSFRQLDERStRLANALLGLGLRPGDRVAVQS-RNCAELVEIECALYkSG 75
Cdd:PRK07769 26 HVERWAKVRGDKLAYrfldFSTERdgvarDLTWSQFGARN-RAVGARLQQVTKPGDRVAILApQNLDYLIAFFGALY-AG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 76 LVKAalnPRFTAAEASD------VVENCTPRAFIggdgytgyaRTTPGFAAVEAFVAlGGPAAG---YLGYEDLLARGGT 146
Cdd:PRK07769 104 RIAV---PLFDPAEPGHvgrlhaVLDDCTPSAIL---------TTTDSAEGVRKFFR-ARPAKErprVIAVDAVPDEVGA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 147 SRPPHRAAAADAAVLHFSSGSTgRIKAAVQ-SYGNRMASLRKMLLGMDRQArpGDRLALIGPVTHASGMLMqpflycgat 225
Cdd:PRK07769 171 TWVPPEANEDTIAYLQYTSGST-RIPAGVQiTHLNLPTNVLQVIDALEGQE--GDRGVSWLPFFHDMGLIT--------- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 226 lVLfdrfepahfLAEVARLRIThvFMVPAM--------IHMLLADP-------------ALEQA-------------DLS 271
Cdd:PRK07769 239 -VL---------LPALLGHYIT--FMSPAAfvrrpgrwIRELARKPggtggtfsaapnfAFEHAaarglpkdgepplDLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 272 SLKTLSYGAAPMAPARIREAWERIGPI------LSQGYGASESTSGVTRLSTADHAEAI--------AGR--------PG 329
Cdd:PRK07769 307 NVKGLLNGSEPVSPASMRKFNEAFAPYglpptaIKPSYGMAEATLFVSTTPMDEEPTVIyvdrdelnAGRfvevpadaPN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 330 RLA--SCGRPHGETEVRVVD-EQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLV------------------DGWL 388
Cdd:PRK07769 387 AVAqvSAGKVGVSEWAVIVDpETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFQnilksrlseshaegapddALWV 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 389 RTGDLArVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVI---SVP----------DATWGESVKA-- 453
Cdd:PRK07769 467 RTGDYG-VYFDGELYITGRVKDLVIIDGRNHYPQDLEYTAQEATKALRTGYVaafSVPanqlpqvvfdDSHAGLKFDPed 545
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092251577 454 ------VVALR-PGRA-LEAAALIAHCRERIADYK--TPRSVEFV--GELPKNPSGKVARKVVREPYWQGVARR 515
Cdd:PRK07769 546 tseqlvIVAERaPGAHkLDPQPIADDIRAAIAVRHgvTVRDVLLVpaGSIPRTSSGKIARRACRAAYLDGSLRS 619
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
16-502 |
5.71e-18 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 86.37 E-value: 5.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 16 DRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEasdvve 95
Cdd:cd17656 3 DAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEER------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 96 nctpRAFIGGDGYTGYARTTpgfaaVEAFVALGGPAAGYLGYEDLLARGGTSRPPHRAAAADAAVLHFSSGSTGRIKAaV 175
Cdd:cd17656 77 ----RIYIMLDSGVRVVLTQ-----RHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKG-V 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 176 QSYGNRMASLRKMLLGMDRQARPGDRLALIGPVTHASGMLMQPFLYCGATLVLFD---RFEPAHFLAEVARLRITHVFMV 252
Cdd:cd17656 147 QLEHKNMVNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIReetKRDVEQLFDLVKRHNIEVVFLP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 253 PAMIHMLLADPALEQADLSSLKTL-SYGAAPMAPARIREAWERIGPILSQGYGASESTsgVTRLSTADHAEAIAGRPgrl 331
Cdd:cd17656 227 VAFLKFIFSEREFINRFPTCVKHIiTAGEQLVITNEFKEMLHEHNVHLHNHYGPSETH--VVTTYTINPEAEIPELP--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 332 aSCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDG-------WLRTGDLARVDEEGFIYL 404
Cdd:cd17656 302 -PIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDpfdpnerMYRTGDLARYLPDGNIEF 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 405 VDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVAlrPGRALEAAALIAHCRERIADYKTPRS 484
Cdd:cd17656 381 LGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV--MEQELNISQLREYLAKQLPEYMIPSF 458
|
490
....*....|....*...
gi 1092251577 485 VEFVGELPKNPSGKVARK 502
Cdd:cd17656 459 FVPLDQLPLTPNGKVDRK 476
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
317-511 |
1.54e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 85.76 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 317 TADHAEAIAGRPG-RLASCGRPHGETeVRVVD-EQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREV----LVDG---- 386
Cdd:PRK05850 355 SAGHAKRCETGGGtPLVSYGSPRSPT-VRIVDpDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTfgatLVDPspgt 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 387 ----WLRTGDLARVDeEGFIYLVDRKKDMIISGGFNVYPTEVEAVlyqhpdVME-----ACVISVPDATwGESVKAVVAL 457
Cdd:PRK05850 434 pegpWLRTGDLGFIS-EGELFIVGRIKDLLIVDGRNHYPDDIEAT------IQEitggrVAAISVPDDG-TEKLVAIIEL 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092251577 458 R-PGRALEAAA--LIAHCRERIADYKTPRSV---EFV----GELPKNPSGKVARKVVREPYWQG 511
Cdd:PRK05850 506 KkRGDSDEEAMdrLRTVKREVTSAISKSHGLsvaDLVlvapGSIPITTSGKIRRAACVEQYRQD 569
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
161-504 |
1.78e-17 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 85.56 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 161 LHFSSGSTGRIKAAVQSYGNRMASLRKMLLGMDRQARPGDRLAL--IGPVTHASGMLmqPFLYCGATLVLF--DRFEPAH 236
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHssIGWVSFHGFLY--GSLSLGNTFVMFegGIIKNKH 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 237 ----FLAEVARLRITHVFMVPAMIHMLL-ADPALEQA----DLSSLKTLSYGAAPMAPArIREAWE-RIGPILSQGYGAS 306
Cdd:PTZ00237 337 ieddLWNTIEKHKVTHTLTLPKTIRYLIkTDPEATIIrskyDLSNLKEIWCGGEVIEES-IPEYIEnKLKIKSSRGYGQT 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 307 EStsGVTRLSTADHAEAiagrpgRLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIR---GEDVFQGYWGEPELTREVL 383
Cdd:PTZ00237 416 EI--GITYLYCYGHINI------PYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmPPSFATTFYKNDEKFKQLF 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 384 VD--GWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGR 461
Cdd:PTZ00237 488 SKfpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQ 567
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1092251577 462 ALEAAALIAHCRE-------RIADYKTPRSVEFVGELPKNPSGKVARKVV 504
Cdd:PTZ00237 568 SNQSIDLNKLKNEinniitqDIESLAVLRKIIIVNQLPKTKTGKIPRQII 617
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
273-471 |
2.77e-17 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 84.87 E-value: 2.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 273 LKTLSYGAAPMAPARirEAWERIGP--ILSQGYGASEsTSGVTRLSTADHAeAIAGRPGRLASCgrphgeTEVRV--VDE 348
Cdd:PLN02430 385 LRLLISGGAPLSTEI--EEFLRVTScaFVVQGYGLTE-TLGPTTLGFPDEM-CMLGTVGAPAVY------NELRLeeVPE 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 349 QGREVEGD-AIGEIVIRGEDVFQGYWGEPELTREVLVDGWLRTGDLARVDEEGFIYLVDRKKDMI-ISGGFNVYPTEVEA 426
Cdd:PLN02430 455 MGYDPLGEpPRGEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEYLEN 534
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1092251577 427 VLYQHPDVMEACVisvpdatWGESVK----AVVALRPGRALEAAALIAH 471
Cdd:PLN02430 535 VYGQNPIVEDIWV-------YGDSFKsmlvAVVVPNEENTNKWAKDNGF 576
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
16-498 |
6.15e-17 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 83.86 E-value: 6.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 16 DRPAVMHRE----RVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEAS 91
Cdd:cd05943 84 DPAAIYAAEdgerTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 92 DVVENCTPRAFIGGDGYTGYARTTP----------GFAAVEAFVAL----------GGPAAGYLGYEDLLARgGTSRPPH 151
Cdd:cd05943 164 DRFGQIEPKVLFAVDAYTYNGKRHDvrekvaelvkGLPSLLAVVVVpytvaagqpdLSKIAKALTLEDFLAT-GAAGELE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 152 RAAAADAAVLH--FSSGSTGRIKAAVQSYGNR-MASLRKMLLGMDrqARPGDRLALigpVTHASGML---MQPFLYCGAT 225
Cdd:cd05943 243 FEPLPFDHPLYilYSSGTTGLPKCIVHGAGGTlLQHLKEHILHCD--LRPGDRLFY---YTTCGWMMwnwLVSGLAVGAT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 226 LVLFD----RFEPAHFLAEVARLRITHVFMVPAMIHMLL---ADPAlEQADLSSLKTLSYGAAPMAPARIREAWERIGP- 297
Cdd:cd05943 318 IVLYDgspfYPDTNALWDLADEEGITVFGTSAKYLDALEkagLKPA-ETHDLSSLRTILSTGSPLKPESFDYVYDHIKPd 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 298 -ILSqgygaseSTSGVTrlstaDHAEAIAG-------RPGRLaSCgrPHGETEVRVVDEQGREVEGDaIGEIVIR----G 365
Cdd:cd05943 397 vLLA-------SISGGT-----DIISCFVGgnpllpvYRGEI-QC--RGLGMAVEAFDEEGKPVWGE-KGELVCTkpfpS 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 366 EDVfqGYWGEPELTR------EVLVDGWlRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACV 439
Cdd:cd05943 461 MPV--GFWNDPDGSRyraayfAKYPGVW-AHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLV 537
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092251577 440 ISVPDATWGESVKAVVALRPGRALEaAALIAHCRERIADYKTPRSVE----FVGELPKNPSGK 498
Cdd:cd05943 538 VGQEWKDGDERVILFVKLREGVELD-DELRKRIRSTIRSALSPRHVPakiiAVPDIPRTLSGK 599
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
70-507 |
1.07e-16 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 83.48 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 70 ALYKSGLVKAALNprFTAAeASDVVENC---------TPRAFIGGdgytgyARTTPGFAAVEAFVALGgpaagYLgyEDL 140
Cdd:PRK06814 701 ALQSAGRVPAMIN--FSAG-IANILSACkaaqvktvlTSRAFIEK------ARLGPLIEALEFGIRII-----YL--EDV 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 141 LARGGT---------SRPPHRAAAADA----AVLHFSSGSTGRIKAAVQSYGNRMASLRKMLLGMDrqARPGDRLALIGP 207
Cdd:PRK06814 765 RAQIGLadkikgllaGRFPLVYFCNRDpddpAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARID--FSPEDKVFNALP 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 208 VTHA----SGMLM------QPFLY---------------CGATLVlfdrFEPAHFLAEVARLrithvfmvpamihmllAD 262
Cdd:PRK06814 843 VFHSfgltGGLVLpllsgvKVFLYpsplhyriipeliydTNATIL----FGTDTFLNGYARY----------------AH 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 263 PAleqaDLSSLKTLSYGAAPMApARIREAW-ERIGPILSQGYGASEsTSGVTRLSTADHaeaiaGRPGrlaSCGRPHGET 341
Cdd:PRK06814 903 PY----DFRSLRYVFAGAEKVK-EETRQTWmEKFGIRILEGYGVTE-TAPVIALNTPMH-----NKAG---TVGRLLPGI 968
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 342 EVRVVdeqgrEVEG-DAIGEIVIRGEDVFQGYW-GEPELTREVLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNV 419
Cdd:PRK06814 969 EYRLE-----PVPGiDEGGRLFVRGPNVMLGYLrAENPGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMI 1043
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 420 YPTEVEAVLYQ-HPDVMEAcVISVPDATWGESvkaVVALRPGRALEAAALIAHCRER-IADYKTPRSVEFVGELPKNPSG 497
Cdd:PRK06814 1044 SLAAVEELAAElWPDALHA-AVSIPDARKGER---IILLTTASDATRAAFLAHAKAAgASELMVPAEIITIDEIPLLGTG 1119
|
490
....*....|....
gi 1092251577 498 KV----ARKVVREP 507
Cdd:PRK06814 1120 KIdyvaVTKLAEEA 1133
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
279-411 |
3.76e-16 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 81.43 E-value: 3.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 279 GAAPMaPARIREaWERIGP--ILSQGYGASESTSGVTrlstadhaEAIAGRPGRLASCGRPHGETEVRV--VDEQGREVE 354
Cdd:PLN02861 391 GAAPL-PRHVEE-FLRVTScsVLSQGYGLTESCGGCF--------TSIANVFSMVGTVGVPMTTIEARLesVPEMGYDAL 460
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092251577 355 GDAI-GEIVIRGEDVFQGYWGEPELTREVLVDGWLRTGDLARVDEEGFIYLVDRKKDM 411
Cdd:PLN02861 461 SDVPrGEICLRGNTLFSGYHKRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNI 518
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
25-440 |
5.38e-16 |
|
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: 80.54 E-value: 5.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 25 RVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAEASDVVENCTPRAFIG 104
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 105 GD--------------------------GYTGYARttPGFAAVEAFVALGGPAAGYLG--YEDLLARGgtsRPphraaaA 156
Cdd:cd17641 90 EDeeqvdklleiadripsvryviycdprGMRKYDD--PRLISFEDVVALGRALDRRDPglYEREVAAG---KG------E 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 157 DAAVLHFSSGSTGRIKAAVQSYGNrMASLRKMLLGMDRQaRPGDR------LALIGPVTHASGMLMQpflyCGATlVLFD 230
Cdd:cd17641 159 DVAVLCTTSGTTGKPKLAMLSHGN-FLGHCAAYLAADPL-GPGDEyvsvlpLPWIGEQMYSVGQALV----CGFI-VNFP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 231 RfEPAHFLAEVARLRITHVFMVP---------AMIHMLLADP------------ALEQAD-------------------- 269
Cdd:cd17641 232 E-EPETMMEDLREIGPTFVLLPPrvwegiaadVRARMMDATPfkrfmfelgmklGLRALDrgkrgrpvslwlrlaswlad 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 270 ------------LSSLKTLSYGAAPMAPARIReAWERIGPILSQGYGASEsTSGVTRLSTADHAeaiagrpgRLASCGRP 337
Cdd:cd17641 311 allfrplrdrlgFSRLRSAATGGAALGPDTFR-FFHAIGVPLKQLYGQTE-LAGAYTVHRDGDV--------DPDTVGVP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 338 HGETEVRVvdeqgrevegDAIGEIVIRGEDVFQGYWGEPELTRE-VLVDGWLRTGDLARVDEEGFIYLVDRKKD-MIISG 415
Cdd:cd17641 381 FPGTEVRI----------DEVGEILVRSPGVFVGYYKNPEATAEdFDEDGWLHTGDAGYFKENGHLVVIDRAKDvGTTSD 450
|
490 500
....*....|....*....|....*
gi 1092251577 416 GFNVYPTEVEAVLYQHPDVMEACVI 440
Cdd:cd17641 451 GTRFSPQFIENKLKFSPYIAEAVVL 475
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
279-427 |
7.52e-16 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 80.45 E-value: 7.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 279 GAAPMAPARirEAWERIGPILS--QGYGASESTSGvTRLSTADHAeaiagrpGRLASCGRPHGETEVRVvdEQGREVEGD 356
Cdd:PLN02614 394 GAAPLASHV--ESFLRVVACCHvlQGYGLTESCAG-TFVSLPDEL-------DMLGTVGPPVPNVDIRL--ESVPEMEYD 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 357 AI-----GEIVIRGEDVFQGYWGEPELTREVLVDGWLRTGDLARVDEEGFIYLVDRKKDM--IISGGF-------NVYpT 422
Cdd:PLN02614 462 ALastprGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIfkLSQGEYvavenieNIY-G 540
|
....*
gi 1092251577 423 EVEAV 427
Cdd:PLN02614 541 EVQAV 545
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
25-493 |
1.36e-15 |
|
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: 79.01 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 25 RVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNP--RFTAAEASDVVENCtpRAF 102
Cdd:cd05939 2 RHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSnlRLESLLHCITVSKA--KAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 103 IggdgytgyartTPGFAAVEAFVALGGPAAGYLGYEDLLarggtsrpphraaaadaaVLHFSSGSTGRIKAAVQSYGN-- 180
Cdd:cd05939 80 I-----------FNLLDPLLTQSSTEPPSQDDVNFRDKL------------------FYIYTSGTTGLPKAAVIVHSRyy 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 181 RMASLRKMLLGMdrqaRPGDRLALIGPVTHASGMLM---QPFLYcGATLVLFDRFEPAHFLAEVARLRITHVFMVPAMIH 257
Cdd:cd05939 131 RIAAGAYYAFGM----RPEDVVYDCLPLYHSAGGIMgvgQALLH-GSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEICR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 258 MLLADPALEQADLSSLKtLSYGAApmaparIR-EAWE----RIG-PILSQGYGASESTSGV------------------- 312
Cdd:cd05939 206 YLLAQPPSEEEQKHNVR-LAVGNG------LRpQIWEqfvrRFGiPQIGEFYGATEGNSSLvnidnhvgacgfnsrilps 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 313 ---TRLSTADHA--EAIAGRPGRLASCgRPhGETEVRVvdeqGREVEGDAIGEivirgedvFQGYWGEPE----LTREVL 383
Cdd:cd05939 279 vypIRLIKVDEDtgELIRDSDGLCIPC-QP-GEPGLLV----GKIIQNDPLRR--------FDGYVNEGAtnkkIARDVF 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 384 VDG--WLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACV--ISVPDATWGESVKAVValRP 459
Cdd:cd05939 345 KKGdsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVPGVEGRAGMAAIV--DP 422
|
490 500 510
....*....|....*....|....*....|....
gi 1092251577 460 GRALEAAALIAHCRERIADYKTPRSVEFVGELPK 493
Cdd:cd05939 423 ERKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDK 456
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
6-399 |
1.86e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 79.32 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 6 FLQRAARYWGDRPAVMHRE------RVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKA 79
Cdd:PRK12582 54 LLAKWAAEAPDRPWLAQREpghgqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 80 ALNPRFTA-----AEASDVVENCTPRAFIGGDGYT-GYARTTPGFAAVEAFVALG-GPAAGYLGYEDLLArggtsRPPHR 152
Cdd:PRK12582 134 PVSPAYSLmshdhAKLKHLFDLVKPRVVFAQSGAPfARALAALDLLDVTVVHVTGpGEGIASIAFADLAA-----TPPTA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 153 AAAADAAVLH--------FSSGSTGRIKAAVQSYGnRMASLRKMLLGM---DRQARPGDRLALIgPVTHASG--MLMQPF 219
Cdd:PRK12582 209 AVAAAIAAITpdtvakylFTSGSTGMPKAVINTQR-MMCANIAMQEQLrprEPDPPPPVSLDWM-PWNHTMGgnANFNGL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 220 LYCGATLVLFD-RFEPAHFLAEVARLR-ITHVFM--VPAMIHMLLA----DPALEQADLSSLKTLSYGAAP--------M 283
Cdd:PRK12582 287 LWGGGTLYIDDgKPLPGMFEETIRNLReISPTVYgnVPAGYAMLAEamekDDALRRSFFKNLRLMAYGGATlsddlyerM 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 284 APARIREAWERIgPILSqGYGASEsTSGVTrLSTADHAEaiagRPGRLascGRPHGETEVRVVDeqgrevEGDAIgEIVI 363
Cdd:PRK12582 367 QALAVRTTGHRI-PFYT-GYGATE-TAPTT-TGTHWDTE----RVGLI---GLPLPGVELKLAP------VGDKY-EVRV 428
|
410 420 430
....*....|....*....|....*....|....*...
gi 1092251577 364 RGEDVFQGYWGEPELTREVL-VDGWLRTGDLAR-VDEE 399
Cdd:PRK12582 429 KGPNVTPGYHKDPELTAAAFdEEGFYRLGDAARfVDPD 466
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
7-395 |
7.50e-15 |
|
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: 77.09 E-value: 7.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 7 LQRAARYWGDRPAVMHRE-----RVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAAL 81
Cdd:cd05921 1 LAHWARQAPDRTWLAEREgnggwRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 82 NPRFTA-----AEASDVVENCTPRAFiggdgytgYARTTPGFA-AVEAFVALGGPAAGYLG---------YEDLLAR-GG 145
Cdd:cd05921 81 SPAYSLmsqdlAKLKHLFELLKPGLV--------FAQDAAPFArALAAIFPLGTPLVVSRNavagrgaisFAELAATpPT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 146 TSRPPHRAAAADAAV--LHFSSGSTGRIKAAVQSYGNrMASLRKMLlgMDRQARPGDRLALI---GPVTHASG--MLMQP 218
Cdd:cd05921 153 AAVDAAFAAVGPDTVakFLFTSGSTGLPKAVINTQRM-LCANQAML--EQTYPFFGEEPPVLvdwLPWNHTFGgnHNFNL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 219 FLYCGATLVLFD-RFEPAHFLAEVARLR---ITHVFMVPAMIHMLLA----DPALEQADLSSLKTLSYGAAPMAPA---- 286
Cdd:cd05921 230 VLYNGGTLYIDDgKPMPGGFEETLRNLReisPTVYFNVPAGWEMLVAalekDEALRRRFFKRLKLMFYAGAGLSQDvwdr 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 287 ----RIREAWERIgpILSQGYGASEsTSGVTRLSTADHAeaiagRPGRLascGRPHGETEVRVVDEQGREvegdaigEIV 362
Cdd:cd05921 310 lqalAVATVGERI--PMMAGLGATE-TAPTATFTHWPTE-----RSGLI---GLPAPGTELKLVPSGGKY-------EVR 371
|
410 420 430
....*....|....*....|....*....|....
gi 1092251577 363 IRGEDVFQGYWGEPELTREVL-VDGWLRTGDLAR 395
Cdd:cd05921 372 VKGPNVTPGYWRQPELTAQAFdEEGFYCLGDAAK 405
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
241-505 |
2.82e-14 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 75.37 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 241 VARLRITHVFMVPAMIHMLLA-DPA-LEQADLSSLKTLSYGAAPMAPARIREAWERIG-PILSQgYGASEstSGVTRLSt 317
Cdd:PRK10524 323 VEKYKVNRMFSAPTAIRVLKKqDPAlLRKHDLSSLRALFLAGEPLDEPTASWISEALGvPVIDN-YWQTE--TGWPILA- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 318 adHAEAIAGRPGRLASCGRPHGETEVRVVDEQ-GREVEGDAIGEIVIRG-------------EDVF-QGYWGepELTREV 382
Cdd:PRK10524 399 --IARGVEDRPTRLGSPGVPMYGYNVKLLNEVtGEPCGPNEKGVLVIEGplppgcmqtvwgdDDRFvKTYWS--LFGRQV 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 383 lvdgwLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRPGRA 462
Cdd:PRK10524 475 -----YSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDS 549
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1092251577 463 LE--------AAALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVR 505
Cdd:PRK10524 550 LAdrearlalEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQ 600
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
5-507 |
3.61e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 75.98 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 5 LFLQRAARYwGDRPAVMHRERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPR 84
Cdd:PRK05691 2193 LFAAQAART-PQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPE 2271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 85 FTAAEASDVVENCTPRAFIGgdgytgyarttpgFAAVeaFVALGGPAAGYLGY--ED---LLARGGTSRPPHRAAAADAA 159
Cdd:PRK05691 2272 YPLERLHYMIEDSGIGLLLS-------------DRAL--FEALGELPAGVARWclEDdaaALAAYSDAPLPFLSLPQHQA 2336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 160 VLHFSSGSTGRIKAAVQSYGNrmaslrkmlLGMDRQA-------RPGDRLALIGPVTH--ASGMLMQPFLyCGATLVLfd 230
Cdd:PRK05691 2337 YLIYTSGSTGKPKGVVVSHGE---------IAMHCQAvierfgmRADDCELHFYSINFdaASERLLVPLL-CGARVVL-- 2404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 231 RFEPAHFLAEVARL----RITHVFMVPAMIHMLLADPALEQADLSSLKTLSYGAA--PMAPARIREAWERigPILSQGYG 304
Cdd:PRK05691 2405 RAQGQWGAEEICQLireqQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGGEAltGEHLQRIRQAFAP--QLFFNAYG 2482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 305 ASESTSGVTRLSTADHAEAIAGRpgrlASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLV 384
Cdd:PRK05691 2483 PTETVVMPLACLAPEQLEEGAAS----VPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFV 2558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 385 ------DG--WLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVpDATWGESVKAVVA 456
Cdd:PRK05691 2559 adpfaaDGgrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYLV 2637
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1092251577 457 LRPGRALEAA------ALIAHCRERIADYKTPRSVEFVGELPKNPSGKVARKVVREP 507
Cdd:PRK05691 2638 SAVAGQDDEAqaalreALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAP 2694
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
212-502 |
4.34e-14 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 74.55 E-value: 4.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 212 SGMLMQPFLYCGATLVLFDRFEPAHF---LAEVARLRITHVFMVPAMIHMLLADPALEQADLSSLKT-------LSYGAA 281
Cdd:PRK04813 198 SVMDLYPTLASGGTLVALPKDMTANFkqlFETLPQLPINVWVSTPSFADMCLLDPSFNEEHLPNLTHflfcgeeLPHKTA 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 282 PMAPARIREAweRIgpilSQGYGASESTSGVTRLSTADhaEAIAGRPgRLAsCGRPHGETEVRVVDEQGREVEGDAIGEI 361
Cdd:PRK04813 278 KKLLERFPSA--TI----YNTYGPTEATVAVTSIEITD--EMLDQYK-RLP-IGYAKPDSPLLIIDEEGTKLPDGEQGEI 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 362 VIRGEDVFQGYWGEPELTREVL--VDGW--LRTGDLARVDEegfiylvdrkkDMIISGG-------FNVYPTE---VEAV 427
Cdd:PRK04813 348 VISGPSVSKGYLNNPEKTAEAFftFDGQpaYHTGDAGYLED-----------GLLFYQGridfqikLNGYRIEleeIEQN 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 428 LYQHPDVMEACVISVPDatwGESVK---AVVALRPGRALEAAALIAHCRE----RIADYKTPRSVEFVGELPKNPSGKVA 500
Cdd:PRK04813 417 LRQSSYVESAVVVPYNK---DHKVQyliAYVVPKEEDFEREFELTKAIKKelkeRLMEYMIPRKFIYRDSLPLTPNGKID 493
|
..
gi 1092251577 501 RK 502
Cdd:PRK04813 494 RK 495
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
233-507 |
7.16e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 74.82 E-value: 7.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 233 EPAHFLAEVARLRITHVFMVPAMIHMLLADpalEQADLSSLKTLSYGAAPMAPARIREAWERIGPI-LSQGYGASESTSG 311
Cdd:PRK05691 3948 DPQGLLAHVQAQGITVLESVPSLIQGMLAE---DRQALDGLRWMLPTGEAMPPELARQWLQRYPQIgLVNAYGPAECSDD 4024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 312 VT--RLSTADHAeaiagrpGRLASCGRPHGETEVRVVDEQGREVEGDAIGEIVIRGEDVFQGYWGEPELTREVLV----- 384
Cdd:PRK05691 4025 VAffRVDLASTR-------GSYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVphpfg 4097
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 385 ---DGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPdatwGESVKAVVA-LRPG 460
Cdd:PRK05691 4098 apgERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQE----GVNGKHLVGyLVPH 4173
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1092251577 461 R-ALEAAALIAHCRER----IADYKTPRSVEFVGELPKNPSGKVARKVVREP 507
Cdd:PRK05691 4174 QtVLAQGALLERIKQRlraeLPDYMVPLHWLWLDRLPLNANGKLDRKALPAL 4225
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
58-399 |
5.86e-13 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 71.06 E-value: 5.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 58 SRNCAELVEIeCALYKSGLVKAALNPRFTAAEASdVVENCTP----RAFIGGDGYTGYA---RTTPGFAAVEAFVALGGp 130
Cdd:PRK08180 132 SQDFGKLRHV-LELLTPGLVFADDGAAFARALAA-VVPADVEvvavRGAVPGRAATPFAallATPPTAAVDAAHAAVGP- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 131 aagylgyeDLLARggtsrpphraaaadaaVLhFSSGSTGRIKAAVQSYGNrMASLRKMLlgmdRQARPgdRLALIGPV-- 208
Cdd:PRK08180 209 --------DTIAK----------------FL-FTSGSTGLPKAVINTHRM-LCANQQML----AQTFP--FLAEEPPVlv 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 209 -----------THASGMLmqpfLYCGATLVLFD-RFEPAHFLAEVARLRI---THVFMVP----AMIHMLLADPALEQAD 269
Cdd:PRK08180 257 dwlpwnhtfggNHNLGIV----LYNGGTLYIDDgKPTPGGFDETLRNLREispTVYFNVPkgweMLVPALERDAALRRRF 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 270 LSSLKTLSYGAAPMAPArireAWERIG-----------PILSqGYGASEsTSGVTrLSTADHAEaiagRPGRLascGRPH 338
Cdd:PRK08180 333 FSRLKLLFYAGAALSQD----VWDRLDrvaeatcgeriRMMT-GLGMTE-TAPSA-TFTTGPLS----RAGNI---GLPA 398
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092251577 339 GETEVRVVDEQGREvegdaigEIVIRGEDVFQGYWGEPELTREVLVD-GWLRTGDLAR-VDEE 399
Cdd:PRK08180 399 PGCEVKLVPVGGKL-------EVRVKGPNVTPGYWRAPELTAEAFDEeGYYRSGDAVRfVDPA 454
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
15-504 |
2.22e-12 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 69.44 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 15 GDRPAVMHR-----ERVLSFRQLDERSTRLANALLGLGLRPGDRVAVQSRNCAELVEIECALYKSGLVKAALNPRFTAAE 89
Cdd:PRK03584 98 DDRPAIIFRgedgpRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 90 ASDVVENCTPRAFIGGDGYTgY-----------ARTTPGFAAVEAFV--------ALGGPAAGYLGYEDLLARGGTSRP- 149
Cdd:PRK03584 178 VLDRFGQIEPKVLIAVDGYR-YggkafdrrakvAELRAALPSLEHVVvvpylgpaAAAAALPGALLWEDFLAPAEAAELe 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 150 --------PhraaaadAAVLhFSSGSTGRIKAAVQSYG----NRMASLRkmlLGMDrqARPGDRL------------ALi 205
Cdd:PRK03584 257 fepvpfdhP-------LWIL-YSSGTTGLPKCIVHGHGgillEHLKELG---LHCD--LGPGDRFfwyttcgwmmwnWL- 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 206 gpvthASGMLmqpflyCGATLVLFD----RFEPAHFLAEVARLRITHVFMVPAMIHMLL---ADPAlEQADLSSLKTLSY 278
Cdd:PRK03584 323 -----VSGLL------VGATLVLYDgspfYPDPNVLWDLAAEEGVTVFGTSAKYLDACEkagLVPG-ETHDLSALRTIGS 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 279 GAAPMAPARIREAWERIGP--ILSqgygaseSTSGVTrlstaDHAEAIAG-------RPGRLAscGRPHGeTEVRVVDEQ 349
Cdd:PRK03584 391 TGSPLPPEGFDWVYEHVKAdvWLA-------SISGGT-----DICSCFVGgnpllpvYRGEIQ--CRGLG-MAVEAWDED 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 350 GREVEGDaIGEIVIRgedvfQ-------GYWGEPELTR------EVLVDGWlRTGDLARVDEEG--FIYlvDRKKDMIIS 414
Cdd:PRK03584 456 GRPVVGE-VGELVCT-----KpfpsmplGFWNDPDGSRyrdayfDTFPGVW-RHGDWIEITEHGgvVIY--GRSDATLNR 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 415 GGFNVYPTE----VEAVlyqhPDVMEACVISVPDATWGESVKAVVALRPGRALEaAALIAHCRERIADYKTPRSV----E 486
Cdd:PRK03584 527 GGVRIGTAEiyrqVEAL----PEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLD-DALRARIRTTIRTNLSPRHVpdkiI 601
|
570 580
....*....|....*....|..
gi 1092251577 487 FVGELPKNPSGK---VA-RKVV 504
Cdd:PRK03584 602 AVPDIPRTLSGKkveLPvKKLL 623
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
137-459 |
1.46e-11 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 67.05 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 137 YEDLLARGGTS-RPPHRAAAADAAVLHFSSGSTGRIKAAVQSYGNRMASLRKMLLGMDrqARPGDRLALIGPVTHA---S 212
Cdd:PLN02736 201 YSKLLAQGRSSpQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTK--FYPSDVHISYLPLAHIyerV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 213 GMLMQPFL------YCGATLVLFDRFE---PAHFlAEVARL--RI---------THVFMVPAMIHMLLA--DPALEQADL 270
Cdd:PLN02736 279 NQIVMLHYgvavgfYQGDNLKLMDDLAalrPTIF-CSVPRLynRIydgitnavkESGGLKERLFNAAYNakKQALENGKN 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 271 SS------------------LKTLSYGAAPMAParirEAWE--RI--GPILSQGYGASESTSGVTRLSTADHAEAIAGRP 328
Cdd:PLN02736 358 PSpmwdrlvfnkikaklggrVRFMSSGASPLSP----DVMEflRIcfGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSP 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 329 GrlASCgrphgetEVRVVD--EQGREVEGDAI--GEIVIRGEDVFQGYWGEPELTREVL-VDGWLRTGDLARVDEEGFIY 403
Cdd:PLN02736 434 N--PAC-------EVKLVDvpEMNYTSEDQPYprGEICVRGPIIFKGYYKDEVQTREVIdEDGWLHTGDIGLWLPGGRLK 504
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092251577 404 LVDRKKDMI-ISGGFNVYPTEVEAVlYQHPDVMEACVIsvpdatWGESVK----AVVALRP 459
Cdd:PLN02736 505 IIDRKKNIFkLAQGEYIAPEKIENV-YAKCKFVAQCFV------YGDSLNsslvAVVVVDP 558
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
279-409 |
1.15e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 64.23 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 279 GAAPMAPARirEAWERI--GPILsQGYGASEST--SGVTRlsTADHAEAIAGRPgrLASCgrphgetEVRVVD--EQGRE 352
Cdd:PTZ00216 436 GGGPLSAAT--QEFVNVvfGMVI-QGWGLTETVccGGIQR--TGDLEPNAVGQL--LKGV-------EMKLLDteEYKHT 501
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092251577 353 VEGDAIGEIVIRGEDVFQGYWGEPELTREVLV-DGWLRTGDLARVDEEGFIYLVDRKK 409
Cdd:PTZ00216 502 DTPEPRGEILLRGPFLFKGYYKQEELTREVLDeDGWFHTGDVGSIAANGTLRIIGRVK 559
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
163-502 |
3.58e-10 |
|
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: 62.10 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 163 FSSGSTGR---IKAAVQSYGNRMASLRKMLLGMDrqarpgDRLALIGPVTHASGMLMQPF--LYCGATLV---LFDRFEP 234
Cdd:cd17654 125 HTSGTTGTpkiVAVPHKCILPNIQHFRSLFNITS------EDILFLTSPLTFDPSVVEIFlsLSSGATLLivpTSVKVLP 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 235 AHF---LAEvaRLRITHVFMVPAMIHMLLADPALEQ--ADLSSLKTLSYGAAPMAPARIREAWERIGPILS--QGYGASE 307
Cdd:cd17654 199 SKLadiLFK--RHRITVLQATPTLFRRFGSQSIKSTvlSATSSLRVLALGGEPFPSLVILSSWRGKGNRTRifNIYGITE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 308 stsgVTRLSTADH-AEAIAGRPGrlascGRPHGETEVRVVDEQGREVEGDAIGEIVIRGeDVFQGYWGEPELTrevlvdg 386
Cdd:cd17654 277 ----VSCWALAYKvPEEDSPVQL-----GSPLLGTVIEVRDQNGSEGTGQVFLGGLNRV-CILDDEVTVPKGT------- 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 387 WLRTGDLARVdEEGFIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVisvpdaTWGESVKAVVALrpgRALEAA 466
Cdd:cd17654 340 MRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAV------TLSDQQRLIAFI---VGESSS 409
|
330 340 350
....*....|....*....|....*....|....*....
gi 1092251577 467 ALIaHCRERIAD---YKTPRSVEFVGELPKNPSGKVARK 502
Cdd:cd17654 410 SRI-HKELQLTLlssHAIPDTFVQIDKLPLTSHGKVDKS 447
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
279-434 |
2.94e-09 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 59.75 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 279 GAAPMAPARIREAWERIGPILSQGYGASESTSGVTrLSTADhaEAIAGRPGRLASCgrphgeTEVRVVD-EQGREVEGDA 357
Cdd:PLN02387 428 GGAPLSGDTQRFINICLGAPIGQGYGLTETCAGAT-FSEWD--DTSVGRVGPPLPC------CYVKLVSwEEGGYLISDK 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 358 I---GEIVIRGEDVFQGYWGEPELTREVL-VDG----WLRTGDLARVDEEGFIYLVDRKKDMI-ISGGFNVYPTEVEAVL 428
Cdd:PLN02387 499 PmprGEIVIGGPSVTLGYFKNQEKTDEVYkVDErgmrWFYTGDIGQFHPDGCLEIIDRKKDIVkLQHGEYVSLGKVEAAL 578
|
....*.
gi 1092251577 429 YQHPDV 434
Cdd:PLN02387 579 SVSPYV 584
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
163-498 |
5.60e-09 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 58.57 E-value: 5.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 163 FSSGSTGRIKAAVQSYGNRMASLRKMLLGMDRQARpgDRLALIGPVTHASGM---LMQPfLYCGATLVLF---------- 229
Cdd:PRK08043 372 FTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPN--DRFMSALPLFHSFGLtvgLFTP-LLTGAEVFLYpsplhyrivp 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 230 ----DR-----FEPAHFLAEVARLrithvfmvpamihmllADPAleqaDLSSLKTLSYGAAPMAPaRIREAW-ERIGPIL 299
Cdd:PRK08043 449 elvyDRnctvlFGTSTFLGNYARF----------------ANPY----DFARLRYVVAGAEKLQE-STKQLWqDKFGLRI 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 300 SQGYGASESTSGVtrlstadhaeAI----AGRPGrlaSCGRPHGETEVRVVDEQGREvEGdaiGEIVIRGEDVFQGYW-- 373
Cdd:PRK08043 508 LEGYGVTECAPVV----------SInvpmAAKPG---TVGRILPGMDARLLSVPGIE-QG---GRLQLKGPNIMNGYLrv 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 374 ---GEPEL-----TREVLVDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEAV-LYQHPDVMEACVIsVPD 444
Cdd:PRK08043 571 ekpGVLEVptaenARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLGVSPDKQHATAI-KSD 649
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1092251577 445 ATWGEsvkAVVALRPGRALEAAALIAHCRER-IADYKTPRSVEFVGELPKNPSGK 498
Cdd:PRK08043 650 ASKGE---ALVLFTTDSELTREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGK 701
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
389-506 |
1.29e-08 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 57.08 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 389 RTGDLARVDEEG---------FIYLVDRKKDMIISGGFNVYPTEVEAVLYQHPDVMEACVISVPDATWGESVKAVVALRP 459
Cdd:COG1541 298 RTGDLTRLLPEPcpcgrthprIGRILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVELAP 377
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1092251577 460 GRALEAAAliAHCRERIADY-KTPRSVEFV--GELPkNPSGKvARKVVRE 506
Cdd:COG1541 378 GASLEALA--EAIAAALKAVlGLRAEVELVepGSLP-RSEGK-AKRVIDR 423
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
14-485 |
1.74e-08 |
|
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: 57.08 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 14 WGDRPAVMHRER---------VLSFRQLDERST------------RLANALLGLGLRPGDRVAVQSRNCAELVEIECALY 72
Cdd:cd17632 35 YADRPALGQRATelvtdpatgRTTLRLLPRFETityaelwervgaVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 73 KSGLVKAALN----------------PRFTAAEASD-------VVENCTPRAFIGGDGYTGYARTTPGFAAveAFVALGG 129
Cdd:cd17632 115 RLGAVSVPLQagasaaqlapilaetePRLLAVSAEHldlaveaVLEGGTPPRLVVFDHRPEVDAHRAALES--ARERLAA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 130 PAAGYLGYEDLLARGGTSRPPHRAAAADAA----VLHFSSGSTGRIKAAVqsYGNRMASLRKMLLGMDRQARPGDRLAL- 204
Cdd:cd17632 193 VGIPVTTLTLIAVRGRDLPPAPLFRPEPDDdplaLLIYTSGSTGTPKGAM--YTERLVATFWLKVSSIQDIRPPASITLn 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 205 IGPVTHASG-MLMQPFLYCGATLVLFDRFEPAHFLAEVARLRITHVFMVPAMIHML-----------LADPALEQADLSS 272
Cdd:cd17632 271 FMPMSHIAGrISLYGTLARGGTAYFAAASDMSTLFDDLALVRPTELFLVPRVCDMLfqryqaeldrrSVAGADAETLAER 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 273 LKTL--------SYGAAPMAPARIRE---AW--ERIGPILSQGYGASESTS-----GVTRLSTADHAEAIAGRPGRLASc 334
Cdd:cd17632 351 VKAElrervlggRLLAAVCGSAPLSAemkAFmeSLLDLDLHDGYGSTEAGAvildgVIVRPPVLDYKLVDVPELGYFRT- 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 335 GRPHGEtevrvvdeqgrevegdaiGEIVIRGEDVFQGYWGEPELTREVL-VDGWLRTGD-LARVDEEGFIYlVDRKKDMI 412
Cdd:cd17632 430 DRPHPR------------------GELLVKTDTLFPGYYKRPEVTAEVFdEDGFYRTGDvMAELGPDRLVY-VDRRNNVL 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 413 -ISGGFNVYPTEVEAVLYQHPDVME-------------ACVISVPDATWGESVKavvALRPgRALEAAALIAHCRErIAD 478
Cdd:cd17632 491 kLSQGEFVTVARLEAVFAASPLVRQifvygnserayllAVVVPTQDALAGEDTA---RLRA-ALAESLQRIAREAG-LQS 565
|
....*..
gi 1092251577 479 YKTPRSV 485
Cdd:cd17632 566 YEIPRDF 572
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
266-452 |
4.09e-07 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 52.51 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 266 EQADLSSLKTLSYGAAPMAPArIREAWERIGP--ILSQGYGASEsTSGVTRLSTADHAeaiagrpgRLASC-GRPHGETE 342
Cdd:PRK06334 294 QESCLPSLRFVVIGGDAFKDS-LYQEALKTFPhiQLRQGYGTTE-CSPVITINTVNSP--------KHESCvGMPIRGMD 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 343 VRVVDEQGR-EVEGDAIGEIVIRGEDVFQGYWGEPELTREVLVDG--WLRTGDLARVDEEGFIYLVDRKKDMIISGGFNV 419
Cdd:PRK06334 364 VLIVSEETKvPVSSGETGLVLTRGTSLFSGYLGEDFGQGFVELGGetWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMV 443
|
170 180 190
....*....|....*....|....*....|....*....
gi 1092251577 420 YPTEVEAVLYQH------PDVMEACVISVPdatwGESVK 452
Cdd:PRK06334 444 SLEALESILMEGfgqnaaDHAGPLVVCGLP----GEKVR 478
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
195-469 |
7.28e-07 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 51.97 E-value: 7.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 195 QARPGDRLALIGPVTHASGMLMQPFL--YCGATLVLFDRFE----PAHFLAEVARLRITHVFMVPAMIHMLLADPALEQA 268
Cdd:cd05905 186 ELYESRPLVTVLDFKSGLGLWHGCLLsvYSGHHTILIPPELmktnPLLWLQTLSQYKVRDAYVKLRTLHWCLKDLSSTLA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 269 -------DLSSLKTLsygaapMAPA--RIR----EAW-ERIGPI-LS------------------QGYGASEST------ 309
Cdd:cd05905 266 slknrdvNLSSLRMC------MVPCenRPRisscDSFlKLFQTLgLSpravstefgtrvnpficwQGTSGPEPSrvyldm 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 310 ----SGVTRLSTADHAEAIAgrpgrLASCGRPHGETEVRVVDEQGREVEGDA-IGEIVIRGEDVFQGYW---GEPELTRE 381
Cdd:cd05905 340 ralrHGVVRLDERDKPNSLP-----LQDSGKVLPGAQVAIVNPETKGLCKDGeIGEIWVNSPANASGYFlldGETNDTFK 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 382 VLV----------DGWLRTGDL----------ARVDEEGFIYLVDRKKDMIISGGFNVYPTEVEA-VLYQHPDVMEACVi 440
Cdd:cd05905 415 VFPstrlstgitnNSYARTGLLgflrptkctdLNVEEHDLLFVVGSIDETLEVRGLRHHPSDIEAtVMRVHPYRGRCAV- 493
|
330 340
....*....|....*....|....*....
gi 1092251577 441 svpdATWGESVKAVVALRPGRALEAAALI 469
Cdd:cd05905 494 ----FSITGLVVVVAEQPPGSEEEALDLV 518
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
207-492 |
8.59e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 52.03 E-value: 8.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 207 PVTHASGML--MQPFLYCGATLVLFDRFEPAHFLAEVARLRITHVFMVPAMIHMLLADPALeQADLSSLKTLSYGAApmA 284
Cdd:PRK07868 654 PLHHESGLLvsLGGAVVGGSRIALSRGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAF-VLHGNHPVRLFIGSG--M 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 285 PArirEAWERIGPILsqgygasESTSGVTRLSTADHAEAIAGRPG-RLASCGRP-HGETEVRVV-----------DEQG- 350
Cdd:PRK07868 731 PT---GLWERVVEAF-------APAHVVEFFATTDGQAVLANVSGaKIGSKGRPlPGAGRVELAaydpehdlileDDRGf 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 351 -REVEGDAIGEIVIRGEdvfqgywGEPELTREVL------VDGWLRTGDLARVDEEGFIYLVDRKKDMIISGGFNVYPTE 423
Cdd:PRK07868 801 vRRAEVNEVGVLLARAR-------GPIDPTASVKrgvfapADTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEP 873
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092251577 424 VEAVLYQHPDVMEACVISVPDATWGESVKAvVALRPGRALEAAALIAHCRERIADYKtPRSVEFVGELP 492
Cdd:PRK07868 874 VTDALGRIGGVDLAVTYGVEVGGRQLAVAA-VTLRPGAAITAADLTEALASLPVGLG-PDIVHVVPEIP 940
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
301-412 |
8.10e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 48.56 E-value: 8.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 301 QGYGASESTSGVTRLSTAD-HAEAIAGRPGrlascgrPHGETEVRVVdEQGREVEGDAIGEIVIRGEDVFQGYWGEPELT 379
Cdd:PTZ00342 491 QGYGLTETTGPIFVQHADDnNTESIGGPIS-------PNTKYKVRTW-ETYKATDTLPKGELLIKSDSIFSGYFLEKEQT 562
|
90 100 110
....*....|....*....|....*....|....
gi 1092251577 380 REVLV-DGWLRTGDLARVDEEGFIYLVDRKKDMI 412
Cdd:PTZ00342 563 KNAFTeDGYFKTGDIVQINKNGSLTFLDRSKGLV 596
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
244-434 |
1.60e-04 |
|
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: 44.15 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 244 LRITHVFMVPAMiHMLLADPALEQ-ADL--SSLKTLSYGAAPMAPARIREAWERIGPILSQGYGASESTSGVTRLSTADH 320
Cdd:cd05913 169 FGPTVLCCTPSY-ALYLAEEAEEEgIDPreLSLKVGIFGAEPWTEEMRKRIERRLGIKAYDIYGLTEIIGPGVAFECEEK 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092251577 321 AEaiagrpgrlascgrPHGETE---VRVVD-EQGREVEGDAIGEIVIrgedvfqgywgePELTREVLVDGWLRTGDLAR- 395
Cdd:cd05913 248 DG--------------LHIWEDhfiPEIIDpETGEPVPPGEVGELVF------------TTLTKEAMPLIRYRTRDITRl 301
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1092251577 396 VDEEG----FIYLVD----RKKDMIISGGFNVYPTEVEAVLYQHPDV 434
Cdd:cd05913 302 LPGPCpcgrTHRRIDritgRSDDMLIIRGVNVFPSQIEDVLLKIPGL 348
|
|
| |
