|
Name |
Accession |
Description |
Interval |
E-value |
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
13-371 |
3.99e-65 |
|
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: 211.62 E-value: 3.99e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 13 VAAEHAERVDTDCAFPAEAVDALRKTGLLGLVLPREIGGMGSGPVEFTEVVAQLSAACGSTAMIYLMHMAAAVTVAASPP 92
Cdd:COG1960 23 EIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASLALPVGVHNGAAEALLRFGT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 93 PGLPD-LLADMASGKQLGTLAFSEPGSRSHFWAPVSTASADGDGIAVRADKSWVTSAGFADVYVVSV--GSADGAAGdVD 169
Cdd:COG1960 103 EEQKErYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVADVILVLArtDPAAGHRG-IS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 170 LYAVPADTPGLRVAGTFTGMGLRGNASAPMA-VDIRIPDSYRLGEAGGGFGIMMQTvLPWFNLGNAAVSLGLATAATGAA 248
Cdd:COG1960 182 LFLVPKDTPGVTVGRIEDKMGLRGSDTGELFfDDVRVPAENLLGEEGKGFKIAMST-LNAGRLGLAAQALGIAEAALELA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 249 VKHVGTARleHLGGSLAELPTIRAQIARMGTTLAAQKAYLEVAANSVSSPDDTTLtHVLGVKASVNDAALTITESAMRVC 328
Cdd:COG1960 261 VAYARERE--QFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAAL-EAAMAKLFATEAALEVADEALQIH 337
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 15608817 329 GGAAFSKHLPIERAFRDARAGSVMAPTADALYDFYGRAVTGLP 371
Cdd:COG1960 338 GGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRP 380
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
97-348 |
1.64e-40 |
|
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: 145.50 E-value: 1.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 97 DLLADMASGKQLGTLAFSEPGSRSHFWAPVSTASADGDGIAVRADKSWVTSAGFADVYVVSVGSADGAAGD--VDLYAVP 174
Cdd:cd00567 59 RYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLARTDEEGPGHrgISAFLVP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 175 ADTPGLRVAGTFTGMGLRGnaSAPMAV---DIRIPDSYRLGEAGGGFGIMMQTVLPWFnLGNAAVSLGLATAATGAAVKH 251
Cdd:cd00567 139 ADTPGVTVGRIWDKMGMRG--SGTGELvfdDVRVPEDNLLGEEGGGFELAMKGLNVGR-LLLAAVALGAARAALDEAVEY 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 252 VGTARLehLGGSLAELPTIRAQIARMGTTLAAQKAYLEVAANSVSSPDDTTLTHVLGVKASVNDAALTITESAMRVCGGA 331
Cdd:cd00567 216 AKQRKQ--FGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFATEAAREVADLAMQIHGGR 293
|
250
....*....|....*..
gi 15608817 332 AFSKHLPIERAFRDARA 348
Cdd:cd00567 294 GYSREYPVERYLRDARA 310
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
15-365 |
3.55e-19 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 88.01 E-value: 3.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 15 AEHAERVDTDCAFPAEaVDALRKTG---LLGLVLPREIGGMGSGPVEFTEVVAQLSAACGSTAMIYLMHMAAAVT--VAA 89
Cdd:PLN02519 46 APHAAAIDATNSFPKD-VNLWKLMGdfnLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCINqlVRN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 90 SPPPGLPDLLADMASGKQLGTLAFSEPGSRSHFWAPVSTASADGDGIAVRADKSWVTSAGFADVYVVSVGSaDGAAGD-- 167
Cdd:PLN02519 125 GTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYAKT-DVAAGSkg 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 168 VDLYAVPADTPGLRVAGTFTGMGLRGNASAPMAV-DIRIPDSYRLGEAGGGFGIMMQTvLPWFNLGNAAVSLGLATAATG 246
Cdd:PLN02519 204 ITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFeNCFVPEENVLGQEGKGVYVMMSG-LDLERLVLAAGPLGLMQACLD 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 247 AAVKHVgtARLEHLGGSLAELPTIRAQIARMGTTLAAQKAYLEVAA----NSVSSPDDTTlthvlGVKASVNDAALTITE 322
Cdd:PLN02519 283 VVLPYV--RQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVArdcdNGKVDRKDCA-----GVILCAAERATQVAL 355
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 15608817 323 SAMRVCGGAAFSKHLPIERAFRDARAGSVMAPTADALYDFYGR 365
Cdd:PLN02519 356 QAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGR 398
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
110-199 |
2.48e-13 |
|
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: 65.38 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 110 TLAFSEPGSRSHFWAPVSTA-SADGDGIAVRADKSWVTSAGFADVYVVSVGSA-DGAAGDVDLYAVPADTPGLRVAGTFT 187
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGgDDRHGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|..
gi 15608817 188 GMGLRGNASAPM 199
Cdd:pfam02770 81 KLGVRGLPTGEL 92
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
13-371 |
3.99e-65 |
|
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: 211.62 E-value: 3.99e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 13 VAAEHAERVDTDCAFPAEAVDALRKTGLLGLVLPREIGGMGSGPVEFTEVVAQLSAACGSTAMIYLMHMAAAVTVAASPP 92
Cdd:COG1960 23 EIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASLALPVGVHNGAAEALLRFGT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 93 PGLPD-LLADMASGKQLGTLAFSEPGSRSHFWAPVSTASADGDGIAVRADKSWVTSAGFADVYVVSV--GSADGAAGdVD 169
Cdd:COG1960 103 EEQKErYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVADVILVLArtDPAAGHRG-IS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 170 LYAVPADTPGLRVAGTFTGMGLRGNASAPMA-VDIRIPDSYRLGEAGGGFGIMMQTvLPWFNLGNAAVSLGLATAATGAA 248
Cdd:COG1960 182 LFLVPKDTPGVTVGRIEDKMGLRGSDTGELFfDDVRVPAENLLGEEGKGFKIAMST-LNAGRLGLAAQALGIAEAALELA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 249 VKHVGTARleHLGGSLAELPTIRAQIARMGTTLAAQKAYLEVAANSVSSPDDTTLtHVLGVKASVNDAALTITESAMRVC 328
Cdd:COG1960 261 VAYARERE--QFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAAL-EAAMAKLFATEAALEVADEALQIH 337
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 15608817 329 GGAAFSKHLPIERAFRDARAGSVMAPTADALYDFYGRAVTGLP 371
Cdd:COG1960 338 GGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRP 380
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
97-348 |
1.64e-40 |
|
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: 145.50 E-value: 1.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 97 DLLADMASGKQLGTLAFSEPGSRSHFWAPVSTASADGDGIAVRADKSWVTSAGFADVYVVSVGSADGAAGD--VDLYAVP 174
Cdd:cd00567 59 RYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLARTDEEGPGHrgISAFLVP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 175 ADTPGLRVAGTFTGMGLRGnaSAPMAV---DIRIPDSYRLGEAGGGFGIMMQTVLPWFnLGNAAVSLGLATAATGAAVKH 251
Cdd:cd00567 139 ADTPGVTVGRIWDKMGMRG--SGTGELvfdDVRVPEDNLLGEEGGGFELAMKGLNVGR-LLLAAVALGAARAALDEAVEY 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 252 VGTARLehLGGSLAELPTIRAQIARMGTTLAAQKAYLEVAANSVSSPDDTTLTHVLGVKASVNDAALTITESAMRVCGGA 331
Cdd:cd00567 216 AKQRKQ--FGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFATEAAREVADLAMQIHGGR 293
|
250
....*....|....*..
gi 15608817 332 AFSKHLPIERAFRDARA 348
Cdd:cd00567 294 GYSREYPVERYLRDARA 310
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
15-347 |
1.34e-39 |
|
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: 144.33 E-value: 1.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 15 AEHAERVDTDCAFPAEAVDALRKTGLLGLVLPREIGGMGSGPVEFTEVVAQLSAACGSTAMIylmhMAAAVTVAASP--P 92
Cdd:cd01158 19 APLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI----VSVHNSLGANPiiK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 93 PGLPDL----LADMASGKQLGTLAFSEPGSRSHFWAPVSTASADGDGIAVRADKSWVTSAGFADVYVV--SVGSADGAAG 166
Cdd:cd01158 95 FGTEEQkkkyLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFYIVfaVTDPSKGYRG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 167 dVDLYAVPADTPGLRVAGTFTGMGLRGNASAPMAV-DIRIPDSYRLGEAGGGFGIMMQTvLPWFNLGNAAVSLGLATAAT 245
Cdd:cd01158 175 -ITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFeDVRVPKENILGEEGEGFKIAMQT-LDGGRIGIAAQALGIAQAAL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 246 GAAVKHVgTARlEHLGGSLAELPTIRAQIARMGTTLAAQKAYLEVAANSVSSPDDTTLTHVLGvKASVNDAALTITESAM 325
Cdd:cd01158 253 DAAVDYA-KER-KQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMA-KLFASEVAMRVTTDAV 329
|
330 340
....*....|....*....|..
gi 15608817 326 RVCGGAAFSKHLPIERAFRDAR 347
Cdd:cd01158 330 QIFGGYGYTKDYPVERYYRDAK 351
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
15-365 |
3.44e-33 |
|
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: 127.23 E-value: 3.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 15 AEHAERVDTDCAFPAEAVDALRKTGLLGLVLPREIGGMGsGPVEFTEVVAQLSAACGSTAMIYLMH--MAAAVTVAASPP 92
Cdd:cd01160 19 APFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIG-GDLLSAAVLWEELARAGGSGPGLSLHtdIVSPYITRAGSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 93 PGLPDLLADMASGKQLGTLAFSEPGSRSHFWAPVSTASADGDGIAVRADKSWVTSAGFADVYVVSV--GSADGAAGDVDL 170
Cdd:cd01160 98 EQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVIVVArtGGEARGAGGISL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 171 YAVPADTPGLRVAGTFTGMGLRGNASAPMAV-DIRIPDSYRLGEAGGGFGIMMQTvLPWFNLGNAAVSLGLATAATGAAV 249
Cdd:cd01160 178 FLVERGTPGFSRGRKLKKMGWKAQDTAELFFdDCRVPAENLLGEENKGFYYLMQN-LPQERLLIAAGALAAAEFMLEETR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 250 KHVgTARlEHLGGSLAELPTIRAQIARMGTTLAAQKAYLEVAANSVSSpDDTTLTHVLGVKASVNDAALTITESAMRVCG 329
Cdd:cd01160 257 NYV-KQR-KAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQ-GRLDVAEASMAKYWATELQNRVAYECVQLHG 333
|
330 340 350
....*....|....*....|....*....|....*.
gi 15608817 330 GAAFSKHLPIERAFRDARAGSVMAPTADALYDFYGR 365
Cdd:cd01160 334 GWGYMREYPIARAYRDARVQPIYGGTTEIMKELISR 369
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
15-347 |
2.45e-27 |
|
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: 111.00 E-value: 2.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 15 AEHAERVDTDCAFPaeaVDALRKT---GLLGLVLPREIGGMGSGPVEFTEVVAQLSAACGSTAMIYLMH-MAAAVTVAAS 90
Cdd:cd01162 21 APHAADWDQKKHFP---VDVLRKAaelGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAAYISIHnMCAWMIDSFG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 91 PPPGLPDLLADMASGKQLGTLAFSEPGSRSHFWAPVSTASADGDGIAVRADKSWVTSAGFADVYVVSVGS-ADGAAGdVD 169
Cdd:cd01162 98 NDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDVYVVMARTgGEGPKG-IS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 170 LYAVPADTPGLRVAGTFTGMGLRGNASAPMAV-DIRIPDSYRLGEAGGGFGIMMQTvLPWFNLGNAAVSLGLATAATGAA 248
Cdd:cd01162 177 CFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFeDCRVPVENRLGGEGQGFGIAMAG-LNGGRLNIASCSLGAAQAALDLA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 249 VKHVGTARleHLGGSLAELPTIRAQIARMGTTLAAQKAYLEVAANSVSS--PDDTTLTHVlgVKASVNDAALTITESAMR 326
Cdd:cd01162 256 RAYLEERK--QFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRgdPDAVKLCAM--AKRFATDECFDVANQALQ 331
|
330 340
....*....|....*....|.
gi 15608817 327 VCGGAAFSKHLPIERAFRDAR 347
Cdd:cd01162 332 LHGGYGYLKDYPVEQYVRDLR 352
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
15-357 |
1.90e-26 |
|
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: 108.65 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 15 AEHAERVDTDCAFPAEAVDALRKTGLLGLVLPREIGGMGSGPVEFTEVVAQLSAACGSTAMIYLMHMAAAVT------VA 88
Cdd:cd01156 22 APLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVALSYGAHSNLCINqiyrngSA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 89 ASPPPGLPDLladmASGKQLGTLAFSEPGSRSHFWAPVSTASADGDGIAVRADKSWVTSAGFADVYVV--SVGSADGAAG 166
Cdd:cd01156 102 AQKEKYLPKL----ISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDADTLVVyaKTDPSAGAHG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 167 dVDLYAVPADTPGLRVAGTFTGMGLRGNASAPMAV-DIRIPDSYRLGEAGGGFGIMM------QTVLPWFNLGNAAVSLG 239
Cdd:cd01156 178 -ITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFeDCEVPEENILGGENKGVYVLMsgldyeRLVLAGGPIGIMQAALD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 240 LAtaatgaavkhVGTARL-EHLGGSLAELPTIRAQIARMGTTLAAQKAYLEVAANSVSSpDDTTLTHVLGVKASVNDAAL 318
Cdd:cd01156 257 VA----------IPYAHQrKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDR-GNMDPKDAAGVILYAAEKAT 325
|
330 340 350
....*....|....*....|....*....|....*....
gi 15608817 319 TITESAMRVCGGAAFSKHLPIERAFRDARAGSVMAPTAD 357
Cdd:cd01156 326 QVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSE 364
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
6-370 |
1.10e-24 |
|
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: 104.09 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 6 VVQEVVSVAAEHAERVdtdcafPAEAVDALRKTGLLGLVLPREIGGMGSGPVEFTEVVAQLSAACGSTamiylMHMAAAV 85
Cdd:cd01161 42 FEEVNDPAKNDQLEKI------PRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMDLGFS-----VTLGAHQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 86 TVAASPP--PGLPD----LLADMASGKQLGTLAFSEPGSRSHFWAPVSTA--SADGDGIAVRADKSWVTSAGFADVYVV- 156
Cdd:cd01161 111 SIGFKGIllFGTEAqkekYLPKLASGEWIAAFALTEPSSGSDAASIRTTAvlSEDGKHYVLNGSKIWITNGGIADIFTVf 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 157 ---SVGSADGAAGD-VDLYAVPADTPGLRVAGTFTGMGLRGNASAPMAV-DIRIPDSYRLGEAGGGFGIMMQtVLPWFNL 231
Cdd:cd01161 191 aktEVKDATGSVKDkITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFeDVKIPVENVLGEVGDGFKVAMN-ILNNGRF 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 232 GNAAVSLGLATAATGAAVKHvGTARLEhLGGSLAELPTIRAQIARMgttlaAQKAYL-EVAANSVSSPDDTTLTHVLGVK 310
Cdd:cd01161 270 GMGAALIGTMKRCIEKAVDY-ANNRKQ-FGKKIHEFGLIQEKLANM-----AILQYAtESMAYMTSGNMDRGLKAEYQIE 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15608817 311 ASVN-----DAALTITESAMRVCGGAAFSKHLPIERAFRDARAGSVMAPTADALYDFYgrAVTGL 370
Cdd:cd01161 343 AAISkvfasEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFI--ALTGL 405
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
6-369 |
2.37e-20 |
|
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: 91.26 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 6 VVQEVVSVAAEHAERVDTDCAFPAEAVDALRKTGLLGLVLPREIGGMGSGPVEFTEVVAQLSAACGSTAMIYLMHMAAAV 85
Cdd:cd01159 2 RAEDLAPLIRERAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIVATHSR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 86 TVAASPPPGLPDLLADMASGKQLGTLafsepgsrshfwAPVSTASADGDGIAVRADKSWVTSAGFAD-VYVVSVGSADGA 164
Cdd:cd01159 82 MLAAFPPEAQEEVWGDGPDTLLAGSY------------APGGRAERVDGGYRVSGTWPFASGCDHADwILVGAIVEDDDG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 165 AGDVDLYAVPADtpGLRVAGTFTGMGLRGNASAPMAVD---------IRIPDSYRLGEAGGGFGIMMQTVLPWFNLGNAA 235
Cdd:cd01159 150 GPLPRAFVVPRA--EYEIVDTWHVVGLRGTGSNTVVVDdvfvpehrtLTAGDMMAGDGPGGSTPVYRMPLRQVFPLSFAA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 236 VSLGLATAATGAAVKHVGTaRLEHLGGS--LAELPTIRAQIARMGTTLAAQKAYLEVAANSV-------SSPDDTTLTHV 306
Cdd:cd01159 228 VSLGAAEGALAEFLELAGK-RVRQYGAAvkMAEAPITQLRLAEAAAELDAARAFLERATRDLwahalagGPIDVEERARI 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15608817 307 LGVKASVNDAALTITESAMRVCGGAAFSKHLPIERAFRDARAGSVMAPT-ADALYDFYGRAVTG 369
Cdd:cd01159 307 RRDAAYAAKLSAEAVDRLFHAAGGSALYTASPLQRIWRDIHAAAQHAALnPETAAEAYGRALLG 370
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
15-365 |
3.55e-19 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 88.01 E-value: 3.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 15 AEHAERVDTDCAFPAEaVDALRKTG---LLGLVLPREIGGMGSGPVEFTEVVAQLSAACGSTAMIYLMHMAAAVT--VAA 89
Cdd:PLN02519 46 APHAAAIDATNSFPKD-VNLWKLMGdfnLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCINqlVRN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 90 SPPPGLPDLLADMASGKQLGTLAFSEPGSRSHFWAPVSTASADGDGIAVRADKSWVTSAGFADVYVVSVGSaDGAAGD-- 167
Cdd:PLN02519 125 GTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYAKT-DVAAGSkg 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 168 VDLYAVPADTPGLRVAGTFTGMGLRGNASAPMAV-DIRIPDSYRLGEAGGGFGIMMQTvLPWFNLGNAAVSLGLATAATG 246
Cdd:PLN02519 204 ITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFeNCFVPEENVLGQEGKGVYVMMSG-LDLERLVLAAGPLGLMQACLD 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 247 AAVKHVgtARLEHLGGSLAELPTIRAQIARMGTTLAAQKAYLEVAA----NSVSSPDDTTlthvlGVKASVNDAALTITE 322
Cdd:PLN02519 283 VVLPYV--RQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVArdcdNGKVDRKDCA-----GVILCAAERATQVAL 355
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 15608817 323 SAMRVCGGAAFSKHLPIERAFRDARAGSVMAPTADALYDFYGR 365
Cdd:PLN02519 356 QAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGR 398
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
17-347 |
7.25e-16 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 78.44 E-value: 7.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 17 HAERVDTDCAFPAEAVDALRKTGLLGLVLPREIGGMGSGPVEFTEVVAQLSAACGSTAMIYLMHMAAAVT--VAASPPPG 94
Cdd:PTZ00461 59 HAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLAYLAHSMLFVNnfYYSASPAQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 95 LPDLLADMASGKQLGTLAFSEPGSRSHFWAPVSTASADGDGIAV-RADKSWVTSAGFADVYVVSVGsadgAAGDVDLYAV 173
Cdd:PTZ00461 139 RARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGNYVlNGSKIWITNGTVADVFLIYAK----VDGKITAFVV 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 174 PADTPGLRVAGTFTGMGLRGNASAPMAVD-IRIPDSYRLGEAGGGFGIMMQTV-LPWFNLGNAAVSLGLATAATGAAVkh 251
Cdd:PTZ00461 215 ERGTKGFTQGPKIDKCGMRASHMCQLFFEdVVVPAENLLGEEGKGMVGMMRNLeLERVTLAAMAVGIAERSVELMTSY-- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 252 vgTARLEHLGGSLAELPTIRAQIARMGTTLAAQKAYLEVAANSVSsPDDTTLTHVLGVKASVNDAALTITESAMRVCGGA 331
Cdd:PTZ00461 293 --ASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVH-PGNKNRLGSDAAKLFATPIAKKVADSAIQVMGGM 369
|
330
....*....|....*.
gi 15608817 332 AFSKHLPIERAFRDAR 347
Cdd:PTZ00461 370 GYSRDMPVERLWRDAK 385
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
8-348 |
3.07e-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: 76.21 E-value: 3.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 8 QEVVSVAAEHAERVDTDCAFPAEAVDALRKTGLLGLVLPREIGGMGSGPVEFTEVVAQLSAACGSTAMIYLMHMAAAVTV 87
Cdd:cd01163 4 RPLAARIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGFVEAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 88 AASPPPGLPDLLADMASGKQLGTLAFSEPGSRSHFWAPVSTASaDGDGIAVRADKSWVTSAGFADVYVVSVGSADGAAGD 167
Cdd:cd01163 84 LLAGPEQFRKRWFGRVLNGWIFGNAVSERGSVRPGTFLTATVR-DGGGYVLNGKKFYSTGALFSDWVTVSALDEEGKLVF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 168 VdlyAVPADTPGLRVAGTFTGMGLRGNASAPMAVD-IRIPD-----SYRLGEAGGGFGIMMQTVLPWFNLG---NAAVSL 238
Cdd:cd01163 163 A---AVPTDRPGITVVDDWDGFGQRLTASGTVTFDnVRVEPdevlpRPNAPDRGTLLTAIYQLVLAAVLAGiarAALDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 239 GLATAATGAAVKHVGTAR-------LEHLGGSLAELPTIRAQIARMGTTLaaQKAYLEVAANSvsspdDTTLTH----VL 307
Cdd:cd01163 240 VAYVRSRTRPWIHSGAESarddpyvQQVVGDLAARLHAAEALVLQAARAL--DAAAAAGTALT-----AEARGEaalaVA 312
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 15608817 308 GVKASVNDAALTITESAMRVCGGAAFSKHLPIERAFRDARA 348
Cdd:cd01163 313 AAKVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNART 353
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
8-347 |
8.17e-14 |
|
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: 71.85 E-value: 8.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 8 QEVVSVAAEHaervDTDCAFPAEAVDALRKTGLLGLVLPREIGGMGSGPVEFTEVVAQLSAAC-GSTAMIYLMHMAAAVT 86
Cdd:cd01157 18 EEIIPVAAEY----DKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCtGVQTAIEANSLGQMPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 87 VAASPPPGLPDLLADMASGKQLGTLAFSEPGSRSHFWAPVSTASADGDGIAVRADKSWVTSAGFADVYVVSVGSADG--- 163
Cdd:cd01157 94 IISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDpkc 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 164 -AAGDVDLYAVPADTPGLRVAGTFTGMGLRGNASAPMAV-DIRIPDSYRLGEAGGGFGIMMQTvlpwFNLGNAAVSLGLA 241
Cdd:cd01157 174 pASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFeDVRVPKENVLIGEGAGFKIAMGA----FDKTRPPVAAGAV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 242 TAATGAAVKHVGTArLEH--LGGSLAELPTIRAQIARMGTTLAAQKAYLEVAANSVSSPDDTTLTHVLGvKASVNDAALT 319
Cdd:cd01157 250 GLAQRALDEATKYA-LERktFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIA-KAFAADIANQ 327
|
330 340
....*....|....*....|....*...
gi 15608817 320 ITESAMRVCGGAAFSKHLPIERAFRDAR 347
Cdd:cd01157 328 LATDAVQIFGGNGFNSEYPVEKLMRDAK 355
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
20-347 |
2.02e-13 |
|
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: 70.88 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 20 RVDTDCAFPA---EAVDALRKTGLLGLVLPREIGGMGSGPVEFTEVVAQLSAACGSTAMIYLMHMAAAVTVAASPPPGLP 96
Cdd:cd01153 27 FDDGRVVVPPpfkEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPLMYASGTQGAAATLLAHGTEAQRE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 97 DLLADMASGKQLGTLAFSEPGSRSHFWAPVSTASADGDGI-AVRADKSWVTsAGFAD--------VYVVSVGSADGAAGd 167
Cdd:cd01153 107 KWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGSwRINGVKRFIS-AGEHDmsenivhlVLARSEGAPPGVKG- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 168 VDLYAVP-----ADTPGLRVAGTFTGMGLRGNASAPMAVDIRIPdsYRLGEAGGGFGIMMqTVLPWFNLGNAAVSLGLAT 242
Cdd:cd01153 185 LSLFLVPkflddGERNGVTVARIEEKMGLHGSPTCELVFDNAKG--ELIGEEGMGLAQMF-AMMNGARLGVGTQGTGLAE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 243 AATGAAVKHvgtARLEHLGGSL-AELPTIR----AQIARMgttLAAQKAYLE--------------VAANSVSSPDDTTL 303
Cdd:cd01153 262 AAYLNALAY---AKERKQGGDLiKAAPAVTiihhPDVRRS---LMTQKAYAEgsraldlytatvqdLAERKATEGEDRKA 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15608817 304 THVLG------VKASVNDAALTITESAMRVCGGAAFSKHLPIERAFRDAR 347
Cdd:cd01153 336 LSALAdlltpvVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDAR 385
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
110-199 |
2.48e-13 |
|
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: 65.38 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 110 TLAFSEPGSRSHFWAPVSTA-SADGDGIAVRADKSWVTSAGFADVYVVSVGSA-DGAAGDVDLYAVPADTPGLRVAGTFT 187
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGgDDRHGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|..
gi 15608817 188 GMGLRGNASAPM 199
Cdd:pfam02770 81 KLGVRGLPTGEL 92
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
22-367 |
3.22e-13 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 70.25 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 22 DTDCAFPAEAVDALRKTGLLGLVLPREIGGMGSGPVEFTEVVAQLSAACGSTAMIYLMHMAAAVTVAASPPPGLPDLLAD 101
Cdd:PRK03354 33 DRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAPTYVLYQLPGGFNTFLREGTQEQIDKIMAF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 102 MASGKQLGTLAFSEPGSRSHFWAPVSTASADGDGIAVRADKSWVTSAGFADvYVVsVGSADGAAGDVDLYA---VPADTP 178
Cdd:PRK03354 113 RGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTP-YIV-VMARDGASPDKPVYTewfVDMSKP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 179 GLRVaGTFTGMGLRGNASAPMAVD-IRIPDSYRLGEAGGGFgimmQTVLPWFNLGN---AAVSLGLATAATGAAVKHvGT 254
Cdd:PRK03354 191 GIKV-TKLEKLGLRMDSCCEITFDdVELDEKDMFGREGNGF----NRVKEEFDHERflvALTNYGTAMCAFEDAARY-AN 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 255 ARLEhLGGSLAELPTIRAQIARMGTTLAAQKAYLEVAA----NSVSSPDDTTLThvlgvKASVNDAALTITESAMRVCGG 330
Cdd:PRK03354 265 QRVQ-FGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAwkadNGTITSGDAAMC-----KYFCANAAFEVVDSAMQVLGG 338
|
330 340 350
....*....|....*....|....*....|....*..
gi 15608817 331 AAFSKHLPIERAFRDARAGSVMAPTADALYDFYGRAV 367
Cdd:PRK03354 339 VGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAV 375
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
34-224 |
3.73e-12 |
|
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: 66.99 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 34 ALRKTGLLGLVLPREIGGMGSGPVEFTEVVAQLSAACGSTAMIYL-MHMAAAVTVAASPPPGLPDLLADMASGKQLGTLA 112
Cdd:cd01152 43 ALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPFNQIgIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 113 FSEPGSRSHFWAPVSTASADGDGIAVRADKSWVTSAGFADVYVVSV---GSADGAAGdVDLYAVPADTPGLRVAGTFTGM 189
Cdd:cd01152 123 FSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVrtdPEAPKHRG-ISILLVDMDSPGVTVRPIRSIN 201
|
170 180 190
....*....|....*....|....*....|....*
gi 15608817 190 GlRGNASAPMAVDIRIPDSYRLGEAGGGFGIMMQT 224
Cdd:cd01152 202 G-GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTT 235
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
7-85 |
9.11e-11 |
|
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: 58.63 E-value: 9.11e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15608817 7 VQEVVsvaAEHAERVDTDCAFPAEAVDALRKTGLLGLVLPREIGGMGSGPVEFTEVVAQLSAACGSTAMIYLMHMAAAV 85
Cdd:pfam02771 15 AEEEI---APHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVALALSVHSSLGA 90
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
26-373 |
3.75e-10 |
|
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: 60.83 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 26 AFPAEAVDALRKTGLLGlVLPREIGGMGSGPVEF---TEVVAQLSAACGSTAMIYL---MHMAAAVTVAASPPPGLPDll 99
Cdd:cd01151 44 KFDRKIIEEMGELGLLG-ATIKGYGCAGLSSVAYgliAREVERVDSGYRSFMSVQSslvMLPIYDFGSEEQKQKYLPK-- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 100 adMASGKQLGTLAFSEPGSRSHFWAPVSTASADGDGIAVRADKSWVTSAGFADVYVvsVGSADGAAGDVDLYAVPADTPG 179
Cdd:cd01151 121 --LASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIADVFV--VWARNDETGKIRGFILERGMKG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 180 LRvAGTFTG-MGLRGNASAPMAVD-IRIPDSYRLGEA---GGGFGIMMQT--VLPWFNLGnAAVSLglataatgaavkhV 252
Cdd:cd01151 197 LS-APKIQGkFSLRASITGEIVMDnVFVPEENLLPGAeglRGPFKCLNNAryGIAWGALG-AAEDC-------------Y 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 253 GTAR---LE--HLGGSLAELPTIRAQIARMGTTLAA-QKAYLEVAA---NSVSSPDDTTLthvlgVKASVNDAALTITES 323
Cdd:cd01151 262 HTARqyvLDrkQFGRPLAAFQLVQKKLADMLTEIALgLLACLRVGRlkdQGKATPEQISL-----LKRNNCGKALEIART 336
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15608817 324 AMRVCGGAAFSKHLPIERAFRDARAGSVMAPTADALYDFYGRAVTGLPLF 373
Cdd:cd01151 337 AREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAITGIQAF 386
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
66-351 |
1.86e-07 |
|
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: 52.76 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 66 LSAACGSTAMIYLMHMAAAVTVAASPPPGLPDLLADMAS--GKQLGTLA--FSEPGSRSHFWAPVSTASADGDGIAVRAD 141
Cdd:cd01154 102 LSDAAAGLLCPLTMTDAAVYALRKYGPEELKQYLPGLLSdrYKTGLLGGtwMTEKQGGSDLGANETTAERSGGGVYRLNG 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 142 KSWVTSAGFADVYVVS---VGSADGAAGdVDLYAVPADTP-----GLRVAGTFTGMGLRGNASAPMAVDIRIpdSYRLGE 213
Cdd:cd01154 182 HKWFASAPLADAALVLarpEGAPAGARG-LSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDDAE--AYLIGD 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 214 AGGGFGIMMQtVLPWFNLGNAAVSLGLATAATGAAVKHVGTARLehLGGSLAELPTIRAQIARMGTTLAAQKAYLEVAAN 293
Cdd:cd01154 259 EGKGIYYILE-MLNISRLDNAVAALGIMRRALSEAYHYARHRRA--FGKPLIDHPLMRRDLAEMEVDVEAATALTFRAAR 335
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15608817 294 SV--SSPDDTT-------LTHVLGVKASvnDAALTITESAMRVCGGAAFSKHLPIERAFRDARAGSV 351
Cdd:cd01154 336 AFdrAAADKPVeahmarlATPVAKLIAC--KRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPI 400
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
215-353 |
2.61e-07 |
|
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: 49.56 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 215 GGGFGIMMQTvLPWFNLGNAAVSLGLATAATGAAVKHVGTARLehLGGSLAELPTIRAQIARMGTTLAAQKAYLEVAANS 294
Cdd:pfam00441 1 GRGFRVAMET-LNHERLAIAAMALGLARRALDEALAYARRRKA--FGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEA 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 15608817 295 VSSpDDTTLTHVLGVKASVNDAALTITESAMRVCGGAAFSKHLPIERAFRDARAGSVMA 353
Cdd:pfam00441 78 LDA-GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGE 135
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
16-367 |
3.74e-07 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 51.65 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 16 EHAERVDTDCAFPAEAVDALRKTGLLGLVLPREIGGMgsgPVEFTE---VVAQLSAACGSTAMIYLMHMAAAVTVAASPP 92
Cdd:PRK12341 27 EYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGT---PADYVTqmlVLEEVSKCGAPAFLITNGQCIHSMRRFGSAE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 93 PGLPDLLADMASGKQLGTLAFSEPGSRSHFWAPVSTASADGDGIAVRADKSWVTSAGFADVYVVSV--GSADGAAGDVDL 170
Cdd:PRK12341 104 QLRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAKEYPYMLVLArdPQPKDPKKAFTL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 171 YAVPADTPGLRVAgTFTGMGLRGNASAPMAVD-IRIPDSYRLGEAGGGFGIMMQTvlpwFN---LGNAAVSLGLATAATG 246
Cdd:PRK12341 184 WWVDSSKPGIKIN-PLHKIGWHMLSTCEVYLDnVEVEESDLVGEEGMGFLNVMYN----FEmerLINAARSLGFAECAFE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 247 AAVKHVGTaRLEhLGGSLAELPTIRAQIARMGTTLAAQKAYLEVAA----NSVSSPDDTTLThvlgvKASVNDAALTITE 322
Cdd:PRK12341 259 DAARYANQ-RIQ-FGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAwqadNGQSLRTSAALA-----KLYCARTAMEVID 331
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 15608817 323 SAMRVCGGAAFSKHLPIERAFRDARAGSVMAPTADALYDFYGRAV 367
Cdd:PRK12341 332 DAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQI 376
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
8-211 |
9.30e-04 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 40.99 E-value: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 8 QEVVSVAAEHAERVDtdcaFPAEAVDALRKTGLLGLVlpreIGGMGSGPVEFTEV------VAQLSAACGStamIYLMHM 81
Cdd:PLN02526 46 KEVAPIMTEYWEKAE----FPFHIIPKLGSLGIAGGT----IKGYGCPGLSITASaiataeVARVDASCST---FILVHS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608817 82 A-AAVTVA-----ASPPPGLPDLladmASGKQLGTLAFSEPGSRSHFWAPVSTASADGDGIAVRADKSWVTSAGFADVYV 155
Cdd:PLN02526 115 SlAMLTIAlcgseAQKQKYLPSL----AQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFADVLV 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15608817 156 VSVGSADgaAGDVDLYAVPADTPGLRVAGTFTGMGLR--GNASAPMAvDIRIPDSYRL 211
Cdd:PLN02526 191 IFARNTT--TNQINGFIVKKGAPGLKATKIENKIGLRmvQNGDIVLK-DVFVPDEDRL 245
|
|
| |
