|
Name |
Accession |
Description |
Interval |
E-value |
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
6-386 |
2.11e-113 |
|
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism]; Acyl-CoA dehydrogenase related to the alkylation response protein AidB is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 441563 [Multi-domain] Cd Length: 381 Bit Score: 336.04 E-value: 2.11e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 6 FIESEERQALRKAVASWVANYGHEYYLDKARKHEHTSELWAEAGKLGFLGVNLPEEYGGGGAGMYELSLVMEEMAAAGSA 85
Cdd:COG1960 3 FELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 86 LLLMVVSPAINGTIIAKFGTDDQKKRWLPGIADGSLTMAFAITEPDAGSNSHKITTTARRDGSDWIIKGQKVFISGIDQA 165
Cdd:COG1960 83 LALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 166 QAVLVVGRSEEAKtGKLRPALFVVPTDAPGFSYTPIE--MELvSPERQFQVFLDDVRLPADALVGAEDAAIAQLFAGLNP 243
Cdd:COG1960 163 DVILVLARTDPAA-GHRGISLFLVPKDTPGVTVGRIEdkMGL-RGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 244 ERIMGAASAVGMGRFALGRAVDYVKTRKVWSTPIGAHQGLAHPLAQCHIEVELAKLMTQKAATLYDHGDDFGAAeaANMA 323
Cdd:COG1960 241 GRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALE--AAMA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489995628 324 KYAAAEASSRAVDQAVQSMGGNGLTKEYGVAAMMTSARLARIAPISREMVLNFVAQTSLGLPR 386
Cdd:COG1960 319 KLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
10-379 |
2.79e-91 |
|
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal acyl-CoA oxidases (AXO) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. In contrast, AXO catalyzes a different oxidative half-reaction, in which the reduced FAD is reoxidized by molecular oxygen. The ACAD family includes the eukaryotic beta-oxidation enzymes, short (SCAD), medium (MCAD), long (LCAD) and very-long (VLCAD) chain acyl-CoA dehydrogenases. These enzymes all share high sequence similarity, but differ in their substrate specificities. The ACAD family also includes amino acid catabolism enzymes such as Isovaleryl-CoA dehydrogenase (IVD), short/branched chain acyl-CoA dehydrogenases(SBCAD), Isobutyryl-CoA dehydrogenase (IBDH), glutaryl-CoA deydrogenase (GCD) and Crotonobetainyl-CoA dehydrogenase. The mitochondrial ACAD's are generally homotetramers, except for VLCAD, which is a homodimer. Related enzymes include the SOS adaptive reponse proten aidB, Naphthocyclinone hydroxylase (NcnH), and and Dibenzothiophene (DBT) desulfurization enzyme C (DszC)
Pssm-ID: 173838 [Multi-domain] Cd Length: 327 Bit Score: 277.63 E-value: 2.79e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 10 EERQALRKAVASWVANYGHEYYLDKARKHEHTSELWAEAGKLGflgvnlpeeyggggagmyelslvmeemaaagsalllm 89
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLL------------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 90 vvspaiNGTIIAKFGTDDQKKRWLPGIADGSLTMAFAITEPDAGSNSHKITTTARRDGSDWIIKGQKVFISGIDQAQAVL 169
Cdd:cd00567 44 ------GAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 170 VVGRSEEAKTGKLRPALFVVPTDAPGFSYTPIEMEL-VSPERQFQVFLDDVRLPADALVGAEDAAIAQLFAGLNPERIMG 248
Cdd:cd00567 118 VLARTDEEGPGHRGISAFLVPADTPGVTVGRIWDKMgMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 249 AASAVGMGRFALGRAVDYVKTRKVWSTPIGAHQGLAHPLAQCHIEVELAKLMTQKAATLYDHGDDfGAAEAANMAKYAAA 328
Cdd:cd00567 198 AAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPD-EARLEAAMAKLFAT 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 489995628 329 EASSRAVDQAVQSMGGNGLTKEYGVAAMMTSARLARIAPISREMVLNFVAQ 379
Cdd:cd00567 277 EAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
10-383 |
4.57e-70 |
|
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases; Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.
Pssm-ID: 173847 [Multi-domain] Cd Length: 373 Bit Score: 224.45 E-value: 4.57e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 10 EERQALRKAVASWVAN--YGHEYYLDKarKHEHTSELWAEAGKLGFLGVNLPEEYGGGGAGMYELSLVMEEMAAA-GSAL 86
Cdd:cd01158 1 EEHQMIRKTVRDFAEKeiAPLAAEMDE--KGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVdASVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 87 LLMVVSPAINGTIIAKFGTDDQKKRWLPGIADGSLTMAFAITEPDAGSNSHKITTTARRDGSDWIIKGQKVFISGIDQAQ 166
Cdd:cd01158 79 VIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 167 AVLVVGRSEEAKTGKLRPAlFVVPTDAPGFSYTPIEMEL---VSPerQFQVFLDDVRLPADALVGAEDAAIAQLFAGLNP 243
Cdd:cd01158 159 FYIVFAVTDPSKGYRGITA-FIVERDTPGLSVGKKEDKLgirGSS--TTELIFEDVRVPKENILGEEGEGFKIAMQTLDG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 244 ERIMGAASAVGMGRFALGRAVDYVKTRKVWSTPIGAHQGLAHPLAQCHIEVELAKLMTQKAATLYDHGDDFgaAEAANMA 323
Cdd:cd01158 236 GRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPF--IKEAAMA 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 324 KYAAAEASSRAVDQAVQSMGGNGLTKEYGVAAMMTSARLARIAPISREMVLNFVAQTSLG 383
Cdd:cd01158 314 KLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
12-379 |
3.46e-62 |
|
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found in the mitochondria of eukaryotes and in some prokaryotes. It catalyzes the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of LCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. LCAD acts as a homodimer.
Pssm-ID: 173849 [Multi-domain] Cd Length: 372 Bit Score: 204.27 E-value: 3.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 12 RQALRKAVASWVANYGHEYylDKArkHEHTSELWAEAGKLGFLGVNLPEEYGGGGAGMYELSLVMEEMAAAGSALLLMVV 91
Cdd:cd01160 7 RDVVRRFFAKEVAPFHHEW--EKA--GEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGSGPGLSL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 92 SPAINGTIIAKFGTDDQKKRWLPGIADGSLTMAFAITEPDAGSNSHKITTTARRDGSDWIIKGQKVFISGIDQAQAVLVV 171
Cdd:cd01160 83 HTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVIVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 172 GRSEEAKTGKLRPALFVVPTDAPGFSYT-PIEMELVSPERQFQVFLDDVRLPADALVGAEDAAIAQLFAGLNPERIMGAA 250
Cdd:cd01160 163 ARTGGEARGAGGISLFLVERGTPGFSRGrKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 251 SAVGMGRFALGRAVDYVKTRKVWSTPIGAHQGLAHPLAQCHIEVELAKLMTQKAATLYDHGDDFGAaeAANMAKYAAAEA 330
Cdd:cd01160 243 GALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVA--EASMAKYWATEL 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 489995628 331 SSRAVDQAVQSMGGNGLTKEYGVAAMMTSARLARIAPISREMVLNFVAQ 379
Cdd:cd01160 321 QNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISR 369
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
9-383 |
1.47e-49 |
|
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- dehydrogenation of short branched chain acyl-CoA intermediates in valine catabolism. It is predicted to be a homotetramer.
Pssm-ID: 173851 [Multi-domain] Cd Length: 375 Bit Score: 171.09 E-value: 1.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 9 SEERQALRKAVASWVANYGHEYYLDKARKHEHTSELWAEAGKLGFLGVNLPEEYGGGGAGMYELSLVMEEMAAAGSALLL 88
Cdd:cd01162 2 NEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 89 MVVSPAINGTIIAKFGTDDQKKRWLPGIADGSLTMAFAITEPDAGSNSHKITTTARRDGSDWIIKGQKVFISGIDQAQAV 168
Cdd:cd01162 82 YISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDVY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 169 LVVGRSEEAktGKLRPALFVVPTDAPGFSYTPIEMEL---VSPERqfQVFLDDVRLPADALVGAEDAAIAQLFAGLNPER 245
Cdd:cd01162 162 VVMARTGGE--GPKGISCFVVEKGTPGLSFGANEKKMgwnAQPTR--AVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 246 IMGAASAVGMGRFALGRAVDYVKTRKVWSTPIGAHQGLAHPLAQCHIEVELAKLMTQKAATLYDHGDDfGAAEAANMAKY 325
Cdd:cd01162 238 LNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDP-DAVKLCAMAKR 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 489995628 326 AAAEASSRAVDQAVQSMGGNGLTKEYGVAAMMTSARLARIAPISREMVLNFVAQTSLG 383
Cdd:cd01162 317 FATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLT 374
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
9-357 |
1.66e-47 |
|
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. It uses electron transfer flavoprotein (ETF) as an electron acceptor. GCD is a homotetramer. GCD deficiency leads to a severe neurological disorder in humans.
Pssm-ID: 173840 [Multi-domain] Cd Length: 386 Bit Score: 165.99 E-value: 1.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 9 SEERQALRKAVASW----VANYGHEYYLDKARKHEHTSELwaeaGKLGFLGVNlPEEYGGGGAGMYELSLVMEEMAAAGS 84
Cdd:cd01151 14 TEEERAIRDTAREFcqeeLAPRVLEAYREEKFDRKIIEEM----GELGLLGAT-IKGYGCAGLSSVAYGLIAREVERVDS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 85 AL-LLMVVSPAINGTIIAKFGTDDQKKRWLPGIADGSLTMAFAITEPDAGSNSHKITTTARRDGSDWIIKGQKVFISGID 163
Cdd:cd01151 89 GYrSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 164 QAQAVLVVGRSEEakTGKLRPalFVVPTDAPGFSYTPIEMELVSPERQF-QVFLDDVRLPADALVGAEDAAIAQlFAGLN 242
Cdd:cd01151 169 IADVFVVWARNDE--TGKIRG--FILERGMKGLSAPKIQGKFSLRASITgEIVMDNVFVPEENLLPGAEGLRGP-FKCLN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 243 PERIMGAASAVGMGRFALGRAVDYVKTRKVWSTPIGAHQGLAHPLAQCHIEVELAKLMTQKAATLYDHGddfGAAeaANM 322
Cdd:cd01151 244 NARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQG---KAT--PEQ 318
|
330 340 350
....*....|....*....|....*....|....*...
gi 489995628 323 AKYAAAEASSRAVD---QAVQSMGGNGLTKEYGVAAMM 357
Cdd:cd01151 319 ISLLKRNNCGKALEiarTAREMLGGNGISDEYHIIRHM 356
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
10-383 |
1.99e-44 |
|
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173841 [Multi-domain] Cd Length: 380 Bit Score: 157.89 E-value: 1.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 10 EERQALRKAVASWVANY----GHEYYLDKARKHEHTSELWAEA-GKLGFLGVNLPEEYGGGGAGMYELSLVMEEMAAAG- 83
Cdd:cd01152 1 PSEEAFRAEVRAWLAAHlppeLREESALGYREGREDRRRWQRAlAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 84 -----SALLLMVvspainGTIIAKFGTDDQKKRWLPGIADGSLTMAFAITEPDAGSNSHKITTTARRDGSDWIIKGQKVF 158
Cdd:cd01152 81 pvpfnQIGIDLA------GPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 159 ISGIDQAQAVLVVGRS--EEAKTGKLrpALFVVPTDAPGFSYTPIEmELVSPERQFQVFLDDVRLPADALVGAEDAAIAQ 236
Cdd:cd01152 155 TSGAHYADWAWLLVRTdpEAPKHRGI--SILLVDMDSPGVTVRPIR-SINGGEFFNEVFLDDVRVPDANRVGEVNDGWKV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 237 LFAGLNPERIMGAASAVgMGRFALGRAVDYVKTRkvwSTPIGAHQGLAHPLAQCHIEVELAKLMTQKAATLYDHGDDFGA 316
Cdd:cd01152 232 AMTTLNFERVSIGGSAA-TFFELLLARLLLLTRD---GRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGA 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489995628 317 AeaANMAKYAAAEASSRAVDQAVQSMGGNGLTKEYG--------VAAMMTSARLARIAPISREMVLNFVAQTSLG 383
Cdd:cd01152 308 E--ASIAKLFGSELAQELAELALELLGTAALLRDPApgaelagrWEADYLRSRATTIYGGTSEIQRNIIAERLLG 380
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
6-366 |
6.98e-44 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 156.43 E-value: 6.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 6 FIESEERQALRKAVASWVANYGHEYYLDKA-RKHEHTSELW---AEAGkLGFLGVnlPEEYGGGGAGMYELSLVMEEMAA 81
Cdd:PRK12341 3 FSLTEEQELLLASIRELITRNFPEEYFRTCdENGTYPREFMralADNG-ISMLGV--PEEFGGTPADYVTQMLVLEEVSK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 82 AGSALLLMVVSPAINGtiIAKFGTDDQKKR-WLPGIADGSLTMAFAITEPDAGSNSHKITTTA-RRDGSdWIIKGQKVFI 159
Cdd:PRK12341 80 CGAPAFLITNGQCIHS--MRRFGSAEQLRKtAESTLETGDPAYALALTEPGAGSDNNSATTTYtRKNGK-VYLNGQKTFI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 160 SGIDQAQAVLVVGRSEEAKTGKLRPALFVVPTDAPGFSYTPIEMELVSPERQFQVFLDDVRLPADALVGAEDAAIAQLFA 239
Cdd:PRK12341 157 TGAKEYPYMLVLARDPQPKDPKKAFTLWWVDSSKPGIKINPLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 240 GLNPERIMGAASAVGMGRFALGRAVDYVKTRKVWSTPIGAHQGLAHPLAQCHIEVELAKLMTQKAATLYDHGddFGAAEA 319
Cdd:PRK12341 237 NFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNG--QSLRTS 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 489995628 320 ANMAKYAAAEASSRAVDQAVQSMGGNGLTKEYGVAAMMTSARLARIA 366
Cdd:PRK12341 315 AALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIG 361
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
28-366 |
2.20e-43 |
|
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACAD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. ACAD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173844 [Multi-domain] Cd Length: 394 Bit Score: 155.24 E-value: 2.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 28 HEYY-LDKARKHEHT---SELWAEAGKLGFLGVNLPEEYGGGGAGMYELSLVMEEMAAAgsalllmVVSPAI-------- 95
Cdd:cd01155 26 LEYYaEGGDRWWTPPpiiEKLKAKAKAEGLWNLFLPEVSGLSGLTNLEYAYLAEETGRS-------FFAPEVfncqapdt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 96 -NGTIIAKFGTDDQKKRWLPGIADGSLTMAFAITEPD-AGSNSHKITTTARRDGSDWIIKGQKVFISGI-DQAQAVLVV- 171
Cdd:cd01155 99 gNMEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGRKWWSSGAgDPRCKIAIVm 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 172 GRSEEAKTGK-LRPALFVVPTDAPGfsytpiemelVSPERQFQVF-------------LDDVRLPADALVGAEDA--AIA 235
Cdd:cd01155 179 GRTDPDGAPRhRQQSMILVPMDTPG----------VTIIRPLSVFgyddaphghaeitFDNVRVPASNLILGEGRgfEIA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 236 QlfAGLNPERIMGAASAVGMGRFALGRAVDYVKTRKVWSTPIGAHQGLAHPLAQCHIEVELAKLMTQKAATLYDHGDDFG 315
Cdd:cd01155 249 Q--GRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTVGNKA 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 489995628 316 AAEAANMAKYAAAEASSRAVDQAVQSMGGNGLTKEYGVAAMMTSARLARIA 366
Cdd:cd01155 327 ARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIA 377
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
36-373 |
4.01e-43 |
|
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which catalyze the alpha,beta dehydrogenation of the corresponding medium chain acyl-CoA by FAD, which becomes reduced. The reduced form of MCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. MCAD is a homotetramer.
Pssm-ID: 173846 [Multi-domain] Cd Length: 378 Bit Score: 154.28 E-value: 4.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 36 RKHEHTSELWAEAGKLGFLGVNLPEEYGGGGAGMYELSLVMEEMAAAGSALLLMVVSPAINGTIIAKFGTDDQKKRWLPG 115
Cdd:cd01157 29 KSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQTAIEANSLGQMPVIISGNDEQKKKYLGR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 116 IADGSLTMAFAITEPDAGSNSHKITTTARRDGSDWIIKGQKVFISGIDQAQAVLVVGRSE---EAKTGKLRPAlFVVPTD 192
Cdd:cd01157 109 MTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDpdpKCPASKAFTG-FIVEAD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 193 APGFsyTPIEMELVSPERQFQ---VFLDDVRLPADALVGAEDAAIAQLFAGLNPERIMGAASAVGMGRFALGRAVDYVKT 269
Cdd:cd01157 188 TPGI--QPGRKELNMGQRCSDtrgITFEDVRVPKENVLIGEGAGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 270 RKVWSTPIGAHQGLAHPLAQCHIEVELAKLMTQKAATLYDHG--DDFGAAeaanMAKYAAAEASSRAVDQAVQSMGGNGL 347
Cdd:cd01157 266 RKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGrrNTYYAS----IAKAFAADIANQLATDAVQIFGGNGF 341
|
330 340 350
....*....|....*....|....*....|....*
gi 489995628 348 TKEYGVAAMMTSARLARIAP---------ISREMV 373
Cdd:cd01157 342 NSEYPVEKLMRDAKIYQIYEgtsqiqrliISREHL 376
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
9-365 |
3.64e-41 |
|
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA dehydrogenase, which catalyzes the third step in leucine catabolism, the conversion of isovaleryl-CoA (3-methylbutyryl-CoA) into 3-methylcrotonyl-CoA. IVD is a homotetramer and has the greatest affinity for small branched chain substrates.
Pssm-ID: 173845 [Multi-domain] Cd Length: 376 Bit Score: 149.10 E-value: 3.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 9 SEERQALRKAVASWVANYGHEYYLDKARKHEHTSELWAEAGKLGFLGVNLPEEYGGGGAGMYELSLVMEEMAAAGSALLL 88
Cdd:cd01156 3 DDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 89 MVVSPA---INGtiIAKFGTDDQKKRWLPGIADGSLTMAFAITEPDAGSNSHKITTTARRDGSDWIIKGQKVFISGIDQA 165
Cdd:cd01156 83 SYGAHSnlcINQ--IYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 166 QAVLVVGRSEEAKTGKLRPAlFVVPTDAPGFSYTPiEMELV----SPerQFQVFLDDVRLPADALVGAEDAAIAQLFAGL 241
Cdd:cd01156 161 DTLVVYAKTDPSAGAHGITA-FIVEKGMPGFSRAQ-KLDKLgmrgSN--TCELVFEDCEVPEENILGGENKGVYVLMSGL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 242 NPERIMGAASAVGMGRFALGRAVDYVKTRKVWSTPIGAHQGLAHPLAQCHIEVELAK--LMTQKAATLYDHGDDFGAAea 319
Cdd:cd01156 237 DYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRsyLYTVAKACDRGNMDPKDAA-- 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 489995628 320 anMAKYAAAEASSRAVDQAVQSMGGNGLTKEYGVAAMMTSARLARI 365
Cdd:cd01156 315 --GVILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEI 358
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
8-382 |
5.88e-40 |
|
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is found in the mitochondria of eukaryotes and in some bacteria. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. VLCAD acts as a homodimer.
Pssm-ID: 173850 [Multi-domain] Cd Length: 409 Bit Score: 146.46 E-value: 5.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 8 ESEERQALRKAVASWVANYGHEYYLDKARKH-EHTSElwaEAGKLGFLGVNLPEEYGGGGAGMYELSLVMEEMAAAGSAL 86
Cdd:cd01161 27 QTEELNMLVGPVEKFFEEVNDPAKNDQLEKIpRKTLT---QLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMDLGFS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 87 LLMVVSPAINGTIIAKFGTDDQKKRWLPGIADGSLTMAFAITEPDAGSNSHKITTTARR--DGSDWIIKGQKVFISGIDQ 164
Cdd:cd01161 104 VTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLseDGKHYVLNGSKIWITNGGI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 165 AQAVLVVGRSEEAK-TGKLRPAL--FVVPTDAPGFSYTPIEMEL-VSPERQFQVFLDDVRLPADALVGAEDAAIAQLFAG 240
Cdd:cd01161 184 ADIFTVFAKTEVKDaTGSVKDKItaFIVERSFGGVTNGPPEKKMgIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMNI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 241 LNPERIMGAASAVGMGRFALGRAVDYVKTRKVWSTPIGAHQGLAHPLAQCHIEVELAKLMTQKAATLYDHGDDFGAAEAA 320
Cdd:cd01161 264 LNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLKAEYQIEA 343
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489995628 321 NMAKYAAAEASSRAVDQAVQSMGGNGLTKEYGVAAMMTSARLARIAPISREMVLNFVAQTSL 382
Cdd:cd01161 344 AISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGL 405
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
9-119 |
6.83e-33 |
|
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain.
Pssm-ID: 460686 [Multi-domain] Cd Length: 113 Bit Score: 119.10 E-value: 6.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 9 SEERQALRKAVASWVANYGHEYYLDKARKHEHTSELWAEAGKLGFLGVNLPEEYGGGGAGMYELSLVMEEMAAAGSAL-L 87
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVaL 80
|
90 100 110
....*....|....*....|....*....|..
gi 489995628 88 LMVVSPAINGTIIAKFGTDDQKKRWLPGIADG 119
Cdd:pfam02771 81 ALSVHSSLGAPPILRFGTEEQKERYLPKLASG 112
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
52-365 |
5.96e-32 |
|
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173842 [Multi-domain] Cd Length: 407 Bit Score: 124.81 E-value: 5.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 52 GFLGVNLPEEYGGGGagmyeLSLVMEEMAA----AGSALLLMVVSPAINGTIIAKFGTDDQKKRWLPGIADGSLTMAFAI 127
Cdd:cd01153 49 GWMALGVPEEYGGQG-----LPITVYSALAeifsRGDAPLMYASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 128 TEPDAGSNSHKITTTA--RRDGSdWIIKGQKVFISGIDQAQAV----LVVGRSEEAKTGKLRPALFVVP-----TDAPGF 196
Cdd:cd01153 124 TEPDAGSDLGALRTKAvyQADGS-WRINGVKRFISAGEHDMSEnivhLVLARSEGAPPGVKGLSLFLVPkflddGERNGV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 197 SYTPIEMEL---VSPerQFQVFLDDVRLPadaLVGAEDAAIAQLFAGLNPERIMGAASAVGMGRFALGRAVDYVKTRKVW 273
Cdd:cd01153 203 TVARIEEKMglhGSP--TCELVFDNAKGE---LIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 274 STPIGAhqglAHPLAQCHIEVELAKLMTQKA-------ATLY------------DHGDDFGAAEAANM-----AKYAAAE 329
Cdd:cd01153 278 GDLIKA----APAVTIIHHPDVRRSLMTQKAyaegsraLDLYtatvqdlaerkaTEGEDRKALSALADlltpvVKGFGSE 353
|
330 340 350
....*....|....*....|....*....|....*.
gi 489995628 330 ASSRAVDQAVQSMGGNGLTKEYGVAAMMTSARLARI 365
Cdd:cd01153 354 AALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTI 389
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
11-365 |
4.40e-27 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 111.18 E-value: 4.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 11 ERQALRKAVASWVAnyghEYYLDKARKHE----HTSELWAEAGKLGFLGVNLPEEYGGGGAGMYELSLVMEEMAAAGSAL 86
Cdd:PTZ00461 40 EHAALRETVAKFSR----EVVDKHAREDDinmhFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 87 LLMVVSPAIngTIIAKF---GTDDQKKRWLPGIADGSLTMAFAITEPDAGSNSHKITTTARRDGS-DWIIKGQKVFISGI 162
Cdd:PTZ00461 116 CLAYLAHSM--LFVNNFyysASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 163 DQAQAVLVVGRSEeaktGKLrpALFVVPTDAPGFSYTP-IEMELVSPERQFQVFLDDVRLPADALVGAEDAAIAQLFAGL 241
Cdd:PTZ00461 194 TVADVFLIYAKVD----GKI--TAFVVERGTKGFTQGPkIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 242 NPERIMGAASAVGMGRFALGRAVDYVKTRKVWSTPIGAHQGLAHPLAQCHIEVELAKLMTQKAATLYDHGDD--FGAaea 319
Cdd:PTZ00461 268 ELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKnrLGS--- 344
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 489995628 320 aNMAKYAAAEASSRAVDQAVQSMGGNGLTKEYGVAAMMTSARLARI 365
Cdd:PTZ00461 345 -DAAKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEI 389
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
30-372 |
6.24e-27 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 110.31 E-value: 6.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 30 YYLDKARKHEHTSELWAEAGKLGFLGVNLPEEYGGGGAGMYELSLVMEEMAAAGSALLLMVVSPAINGTIIaKFGTDDQK 109
Cdd:PRK03354 28 YFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAPTYVLYQLPGGFNTFL-REGTQEQI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 110 KRWLPGIADGSLTMAFAITEPDAGSNSHKITTTARRDGSDWIIKGQKVFISGIDQAQAVLVVGRSEEAKTGKLRPALFVv 189
Cdd:PRK03354 107 DKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTPYIVVMARDGASPDKPVYTEWFV- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 190 PTDAPGFSYTPIEMELVSPERQFQVFLDDVRLPADALVGAEDAAIAQLFAGLNPERIMGAASAVGMGRFALGRAVDYVKT 269
Cdd:PRK03354 186 DMSKPGIKVTKLEKLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQ 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 270 RKVWSTPIGAHQGLAHPLAQCHIEVELAKLMTQKAATLYDHGDdFGAAEAANMAKYAAaEASSRAVDQAVQSMGGNGLTK 349
Cdd:PRK03354 266 RVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGT-ITSGDAAMCKYFCA-NAAFEVVDSAMQVLGGVGIAG 343
|
330 340
....*....|....*....|...
gi 489995628 350 EYGVAAMMTSARLARIAPISREM 372
Cdd:PRK03354 344 NHRISRFWRDLRVDRVSGGSDEM 366
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
28-372 |
1.94e-26 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 109.20 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 28 HEYYLDKARKHEHTSELWAEAGKLGFLGVNLPEEYGGGGAGMYELSLVMEEMA-AAGSALLLMVVSPAINGTIIAKFGTD 106
Cdd:PLN02519 48 HAAAIDATNSFPKDVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISrASGSVGLSYGAHSNLCINQLVRNGTP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 107 DQKKRWLPGIADGSLTMAFAITEPDAGSNSHKITTTARRDGSDWIIKGQKVFISGIDQAQAVLVVGRSEEAKTGKLRPAl 186
Cdd:PLN02519 128 AQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTDVAAGSKGITA- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 187 FVVPTDAPGFSYTPIEMEL-VSPERQFQVFLDDVRLPADALVGAEDAAIAQLFAGLNPERIMGAASAVGMGRFALGRAVD 265
Cdd:PLN02519 207 FIIEKGMPGFSTAQKLDKLgMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLP 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 266 YVKTRKVWSTPIGAHQGLAHPLAQCHIEVELAKLMTQKAATLYDHG--DDFGAAeaanMAKYAAAEASSRAVDQAVQSMG 343
Cdd:PLN02519 287 YVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGkvDRKDCA----GVILCAAERATQVALQAIQCLG 362
|
330 340
....*....|....*....|....*....
gi 489995628 344 GNGLTKEYGVAAMMTSARLARIAPISREM 372
Cdd:PLN02519 363 GNGYINEYPTGRLLRDAKLYEIGAGTSEI 391
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
240-379 |
1.45e-24 |
|
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.
Pssm-ID: 395354 [Multi-domain] Cd Length: 149 Bit Score: 98.10 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 240 GLNPERIMGAASAVGMGRFALGRAVDYVKTRKVWSTPIGAHQGLAHPLAQCHIEVELAKLMTQKAATLYDHGDDFGAAea 319
Cdd:pfam00441 10 TLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAGGPDGAE-- 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 320 ANMAKYAAAEASSRAVDQAVQSMGGNGLTKEYGVAAMMTSARLARIAPISREMVLNFVAQ 379
Cdd:pfam00441 88 ASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIAR 147
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
96-382 |
2.63e-18 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 86.77 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 96 NGTIIAKFGTDDQKKRWLPGIADGSLTMAFAITEPD-AGSNSHKITTTARRDGSDWIIKGQKVFISG-ID-QAQAVLVVG 172
Cdd:PLN02876 525 NMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGaMDpRCRVLIVMG 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 173 RSEEAKTGKLRPALFVVPTDAPGFSytpIEMELV------SPERQFQVFLDDVRLPADALVGAEDAA--IAQlfAGLNPE 244
Cdd:PLN02876 605 KTDFNAPKHKQQSMILVDIQTPGVQ---IKRPLLvfgfddAPHGHAEISFENVRVPAKNILLGEGRGfeIAQ--GRLGPG 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 245 RIMGAASAVGMGRFALGRAVDYVKTRKVWSTPIGAHQGLAHPLAQCHIEVELAKLMTQKAAtlyDHGDDFGAAEAANMAK 324
Cdd:PLN02876 680 RLHHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAA---DQLDRLGNKKARGIIA 756
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489995628 325 YAAAEASS---RAVDQAVQSMGGNGLTKEYGVAAMMTSARLARIAPISREMVLNFVAQTSL 382
Cdd:PLN02876 757 MAKVAAPNmalKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAKLEL 817
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
9-311 |
2.75e-18 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 85.67 E-value: 2.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 9 SEERQALRKAVASW----VANYGHEYYldkaRKHEHTSELWAEAGKLGFLGVNLpEEYGGGGAGMYELSLVMEEMA---A 81
Cdd:PLN02526 30 TPEEQALRKRVRECmekeVAPIMTEYW----EKAEFPFHIIPKLGSLGIAGGTI-KGYGCPGLSITASAIATAEVArvdA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 82 AGSALLLMVVSPAIngTIIAKFGTDDQKKRWLPGIADGSLTMAFAITEPDAGSNSHKITTTARRDGSDWIIKGQKVFISG 161
Cdd:PLN02526 105 SCSTFILVHSSLAM--LTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 162 IDQAQAVLVVGRSeeAKTGKLRPalFVVPTDAPGFSYTPIE----MELVspeRQFQVFLDDVRLP-ADALVGAEdaAIAQ 236
Cdd:PLN02526 183 STFADVLVIFARN--TTTNQING--FIVKKGAPGLKATKIEnkigLRMV---QNGDIVLKDVFVPdEDRLPGVN--SFQD 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489995628 237 LFAGLNPERIMGAASAVG--MGRFALGRAvdYVKTRKVWSTPIGAHQGLAHPLAQCHIEVELAKLMTQKAATLYDHG 311
Cdd:PLN02526 254 TNKVLAVSRVMVAWQPIGisMGVYDMCHR--YLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESG 328
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
106-368 |
2.88e-18 |
|
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of several genes involved in the SOS adaptive response to DNA alkylation damage, whose expression is activated by the Ada protein. Its function has not been entirely elucidated; however, it is similar in sequence and function to acyl-CoA dehydrogenases. It has been proposed that aidB directly destroys DNA alkylating agents such as nitrosoguanidines (nitrosated amides) or their reaction intermediates.
Pssm-ID: 173843 [Multi-domain] Cd Length: 418 Bit Score: 85.89 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 106 DDQKKRWLPGIA----DGSLTMAFAITEPDAGSNSHKITTTARRDGSD-WIIKGQKVFISGIDqAQAVLVVGRSEEAKTG 180
Cdd:cd01154 128 PEELKQYLPGLLsdryKTGLLGGTWMTEKQGGSDLGANETTAERSGGGvYRLNGHKWFASAPL-ADAALVLARPEGAPAG 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 181 KLRPALFVVPTDAPGFSYTPIEME----------LVSPERQFQvflddvrlpaDA---LVGAEDAAIAQLFAGLNPERIM 247
Cdd:cd01154 207 ARGLSLFLVPRLLEDGTRNGYRIRrlkdklgtrsVATGEVEFD----------DAeayLIGDEGKGIYYILEMLNISRLD 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 248 GAASAVGMGRFALGRAVDYVKTRKVWSTPIGAHQGLAHPLAQCHIEVELAKLMTQKAATLYDH--GDDFGAAEAA----N 321
Cdd:cd01154 277 NAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRaaADKPVEAHMArlatP 356
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 489995628 322 MAKYAAAEASSRAVDQAVQSMGGNGLTKEYGVaammtsARLARIAPI 368
Cdd:cd01154 357 VAKLIACKRAAPVTSEAMEVFGGNGYLEEWPV------ARLHREAQV 397
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
124-202 |
6.79e-18 |
|
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a beta-barrel fold.
Pssm-ID: 460685 [Multi-domain] Cd Length: 95 Bit Score: 78.09 E-value: 6.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 124 AFAITEPDAGSNSHKI-TTTARRDGSDWIIKGQKVFISGIDQAQAVLVVGRSEEAKtGKLRPALFVVPTDAPGFSYTPIE 202
Cdd:pfam02770 1 AFALTEPGAGSDVASLkTTAADGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDD-RHGGISLFLVPKDAPGVSVRRIE 79
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
33-309 |
2.36e-15 |
|
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, which catalyzes the first two steps of DBT desulfurization in mesophilic bacteria. DszC converts DBT to DBT-sulfoxide, which is then converted to DBT-sulfone. Bacteria with this enzyme are candidates for the removal of organic sulfur compounds from fossil fuels, which pollute the environment. An equivalent enzyme tdsC, is found in thermophilic bacteria. This alignment also contains a closely related uncharacterized subgroup.
Pssm-ID: 173852 [Multi-domain] Cd Length: 377 Bit Score: 76.59 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 33 DKARKHEHTS-ELWAEAGklgFLGVNLPEEYGGGGAGMYELSLVMEEMAAAGSAL-------LLMVVSpaingtiIAKFG 104
Cdd:cd01163 18 DRQRGLPYEEvALLRQSG---LGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIaqalrahFGFVEA-------LLLAG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 105 TDDQKKRWLPGIADGSLTMAfAITEPDaGSNSHKITTTARRDGSDWIIKGQKVFISGIDQAQAVLVVGRSEEAKtgklrP 184
Cdd:cd01163 88 PEQFRKRWFGRVLNGWIFGN-AVSERG-SVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGK-----L 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 185 ALFVVPTDAPGFS----YTPIEMELV-SPERQF---QVFLDDVRL-PADALVGAEDAAIAQLFAglnperimgAASAVGM 255
Cdd:cd01163 161 VFAAVPTDRPGITvvddWDGFGQRLTaSGTVTFdnvRVEPDEVLPrPNAPDRGTLLTAIYQLVL---------AAVLAGI 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 256 GRFALGRAVDYVKTR-KVWSTPiGAHQGLAHPLAQCHI-----EVELAKLMTQKAATLYD 309
Cdd:cd01163 232 ARAALDDAVAYVRSRtRPWIHS-GAESARDDPYVQQVVgdlaaRLHAAEALVLQAARALD 290
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
52-365 |
5.54e-13 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 70.28 E-value: 5.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 52 GFLGVNLPEEYGGGGAGmYELSLVMEEMAAAGSALLLMVVSPAING--TIIAkFGTDDQKKRWLPGIADGSLTMAFAITE 129
Cdd:PTZ00456 112 GWTGISEPEEYGGQALP-LSVGFITRELMATANWGFSMYPGLSIGAanTLMA-WGSEEQKEQYLTKLVSGEWSGTMCLTE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 130 PDAGSNSHKITTTARR--DGSdWIIKGQKVFISGIDQ---AQAV-LVVGRSEEAKTGKLRPALFVVPTDAP---GFSYTP 200
Cdd:PTZ00456 190 PQCGTDLGQVKTKAEPsaDGS-YKITGTKIFISAGDHdltENIVhIVLARLPNSLPTTKGLSLFLVPRHVVkpdGSLETA 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 201 IEMELVSPERQF--------QVFLDDvrlPADALVGAEDAAIAQLFAGLNPERIMGAASAVGMGRFALGRAVDYVKTRKV 272
Cdd:PTZ00456 269 KNVKCIGLEKKMgikgsstcQLSFEN---SVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERRS 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 273 WSTPIGAH--QGLAHPLAqCHIEVELaKLMTQKA------ATLYDHG---DDFGAAEAANMAKYAAAEA----------- 330
Cdd:PTZ00456 346 MRALSGTKepEKPADRII-CHANVRQ-NILFAKAvaeggrALLLDVGrllDIHAAAKDAATREALDHEIgfytpiakgcl 423
|
330 340 350
....*....|....*....|....*....|....*...
gi 489995628 331 ---SSRAVDQAVQSMGGNGLTKEYGVAAMMTSARLARI 365
Cdd:PTZ00456 424 tewGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTL 461
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
43-143 |
7.85e-13 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 69.99 E-value: 7.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 43 ELWAEAGKLGFLGVNLPEEYGGGGAGMYELSLVMEEMAAAGS--ALLLMVVSPAINGTIIAKFGTDDQKKRWLPGIADGS 120
Cdd:PRK13026 112 EVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVSKIATRSVsaAVTVMVPNSLGPGELLTHYGTQEQKDYWLPRLADGT 191
|
90 100
....*....|....*....|...
gi 489995628 121 LTMAFAITEPDAGSNSHKITTTA 143
Cdd:PRK13026 192 EIPCFALTGPEAGSDAGAIPDTG 214
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
43-134 |
5.57e-11 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 64.07 E-value: 5.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 43 ELWAEAGKLGFLGVNLPEEYGGGGAGMYELSLVMEEMAAAGSALLLMVVSPaiN----GTIIAKFGTDDQKKRWLPGIAD 118
Cdd:PRK09463 113 EVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTVMVP--NslgpGELLLHYGTDEQKDHYLPRLAR 190
|
90
....*....|....*.
gi 489995628 119 GSLTMAFAITEPDAGS 134
Cdd:PRK09463 191 GEEIPCFALTSPEAGS 206
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
55-197 |
2.89e-08 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 55.27 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 55 GVNLPEEYGGGGAGMYELSLVMEEMAAAGSALLLMVVSPAINGT-IIAKFGTDDQKKRWLPGIADGSLTMAFAITEPDAG 133
Cdd:PTZ00457 67 GARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHSGFCTyLLSTVGSKELKGKYLTAMSDGTIMMGWATEEGCGS 146
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489995628 134 SNSHKITTTARRDGSDWIIKGQK--VFISGidqAQAVLVVGR------SEEAKTGKLRPALFVVPTDAPGFS 197
Cdd:PTZ00457 147 DISMNTTKASLTDDGSYVLTGQKrcEFAAS---ATHFLVLAKtltqtaAEEGATEVSRNSFFICAKDAKGVS 215
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
6-146 |
2.01e-06 |
|
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in the peroxisomal fatty acid beta-oxidation, the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. In a second oxidative half-reaction, the reduced FAD is reoxidized by molecular oxygen. AXO is generally a homodimer, but it has been reported to form a different type of oligomer in yeast. There are several subtypes of AXO's, based on substrate specificity. Palmitoyl-CoA oxidase acts on straight-chain fatty acids and prostanoids; whereas, the closely related Trihydroxycoprostanoly-CoA oxidase has the greatest activity for 2-methyl branched side chains of bile precursors. Pristanoyl-CoA oxidase, acts on 2-methyl branched fatty acids. AXO has an additional domain, C-terminal to the region with similarity to acyl-CoA dehydrogenases, which is included in this alignment.
Pssm-ID: 173839 [Multi-domain] Cd Length: 610 Bit Score: 49.63 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 6 FIESEERQALRKAVASWVAN---YGHE---YYLDKARKHEHTSELWAEAGKL-GFLGVNLPEEYggggAGMYELSLVMEE 78
Cdd:cd01150 21 LEGGEENLRRKREVERELESdplFQRElpsKHLSREELYEELKRKAKTDVERmGELMADDPEKM----LALTNSLGGYDL 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489995628 79 MAAAGSALLLMVVSPAINGTiiakfGTDDQKKRWLPGIADGSLTMAFAITEPDAGSNSHKITTTARRD 146
Cdd:cd01150 97 SLGAKLGLHLGLFGNAIKNL-----GTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYD 159
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
52-350 |
8.17e-03 |
|
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, which is active against Gram-positive bacteria. Polyketides are secondary metabolites, which have important biological functions such as antitumor, immunosupressive or antibiotic activities. NcnH is a hydroxylase involved in the biosynthesis of naphthocyclinone and possibly other polyketides.
Pssm-ID: 173848 [Multi-domain] Cd Length: 370 Bit Score: 38.10 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 52 GFLGVNLPEEYGGGGAGMYELSLVMEEMAAAGSALLLMVVSPAINGTIIAKFGTDDQKKRWlpgiADGSLTMAfaitepd 131
Cdd:cd01159 35 GFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIVATHSRMLAAFPPEAQEEVW----GDGPDTLL------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 132 agSNSHKITTTARRDGSDWIIKGQKVFISGIDQAQAVLVVGRSEEAKTGKLrPALFVVPT---------DAPGF----SY 198
Cdd:cd01159 104 --AGSYAPGGRAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDDGGPL-PRAFVVPRaeyeivdtwHVVGLrgtgSN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 199 TPIEMELVSPERQFQVFLDDVRLPADalvGAEDAAIAQLFAGLNPERImgAASAVGMGRFALGRAVDYVKTRkVWSTPIG 278
Cdd:cd01159 181 TVVVDDVFVPEHRTLTAGDMMAGDGP---GGSTPVYRMPLRQVFPLSF--AAVSLGAAEGALAEFLELAGKR-VRQYGAA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995628 279 AHQGLA----HPLAQCHIEVELAKLMTQKAAT-LYDHGDDFGAA-----EAANMAKYAAAEASSRAVDQAVQSMGGNGLT 348
Cdd:cd01159 255 VKMAEApitqLRLAEAAAELDAARAFLERATRdLWAHALAGGPIdveerARIRRDAAYAAKLSAEAVDRLFHAAGGSALY 334
|
..
gi 489995628 349 KE 350
Cdd:cd01159 335 TA 336
|
|
| |
