|
Name |
Accession |
Description |
Interval |
E-value |
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
7-380 |
2.89e-117 |
|
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: 345.87 E-value: 2.89e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 7 PEQRQLQAEIRQYFSNLISPDERTEMEKDRHGP--AYRAVIRRMGRDGRLGVGWPKEFGGLGFGPIEQQIFVNEAHRADV 84
Cdd:cd01152 1 PSEEAFRAEVRAWLAAHLPPELREESALGYREGreDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 85 PLPA--VTLQTVGPTLQAHGSELQKKKFLPAILAGEAHFAIGYTEPEAGTDLASLRTTAVRDGDHYIVNGQKVFTTGAHD 162
Cdd:cd01152 81 PVPFnqIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 163 ADYIWLACRTDPNAAKHKGISILIVDTKDPGYSWTPIILADGAHHTNATYYNDVRVPVDMLVGKENDGWRLITTQLNNER 242
Cdd:cd01152 161 ADWAWLLVRTDPEAPKHRGISILLVDMDSPGVTVRPIRSINGGEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 243 VMLG--PAGRFASIYDRVHAWASVPGGNGVTPIDHDDVKRALGEIRAIWrineLLNWQVAS--AGEDINMADAAATKVFG 318
Cdd:cd01152 241 VSIGgsAATFFELLLARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALR----LLVFRLASalAAGKPPGAEASIAKLFG 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15610679 319 TERVQRAGRLAEEIVGKYGNPAEP-DTAELLRWLDAQTKRNLVITFGGGVNEVMREMIAASGL 380
Cdd:cd01152 317 SELAQELAELALELLGTAALLRDPaPGAELAGRWEADYLRSRATTIYGGTSEIQRNIIAERLL 379
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
1-384 |
6.68e-102 |
|
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: 306.38 E-value: 6.68e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 1 MFIDLTPEQRQLQAEIRQYFSNLISPDERtemEKDRHGPAYRAVIRRMGRDGRLGVGWPKEFGGLGFGPIEQQIFVNEAH 80
Cdd:COG1960 1 MDFELTEEQRALRDEVREFAEEEIAPEAR---EWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 81 RADVPLP-AVTLQT-VGPTLQAHGSELQKKKFLPAILAGEAHFAIGYTEPEAGTDLASLRTTAVRDGDHYIVNGQKVFTT 158
Cdd:COG1960 78 RADASLAlPVGVHNgAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFIT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 159 GAHDADYIWLACRTDPnAAKHKGISILIVDTKDPGYSWTPIILADG--AHHTNATYYNDVRVPVDMLVGKENDGWRLITT 236
Cdd:COG1960 158 NAPVADVILVLARTDP-AAGHRGISLFLVPKDTPGVTVGRIEDKMGlrGSDTGELFFDDVRVPAENLLGEEGKGFKIAMS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 237 QLNNERVMLGP--AGRFASIYDRVHAWASVPGGNGVTPIDHDDVKRALGEIRAIWRINELLNWQVAS---AGEDInMADA 311
Cdd:COG1960 237 TLNAGRLGLAAqaLGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWlldAGEDA-ALEA 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15610679 312 AATKVFGTERVQRAGRLAEEIVGKYGNPAEPDTAELLRwlDAQtkrnlVITFGGGVNEVMREMIAASGLKVPR 384
Cdd:COG1960 316 AMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYR--DAR-----ILTIYEGTNEIQRLIIARRLLGRPG 381
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
7-376 |
1.75e-57 |
|
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: 191.94 E-value: 1.75e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 7 PEQRQLQAEIRQYFSNLISPDERtemEKDRHGPAYRAVIRRMGRDGRLGVGWPKEFGGLGFGPIEQQIFVNEAHRADVPL 86
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHH---EWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGSG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 87 PAVTLQT--VGPTLQAHGSELQKKKFLPAILAGEAHFAIGYTEPEAGTDLASLRTTAVRDGDHYIVNGQKVFTTGAHDAD 164
Cdd:cd01160 78 PGLSLHTdiVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 165 YIWLACRTDPNAAKHKGISILIVDTKDPGYSWTPIILADG--AHHTNATYYNDVRVPVDMLVGKENDGWRLITTQLNNER 242
Cdd:cd01160 158 VVIVVARTGGEARGAGGISLFLVERGTPGFSRGRKLKKMGwkAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQER 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 243 VMLGpAGRFAS---IYDRVHAWASVPGGNGVTPIDHDDVKRALGE----IRAIWRINELLNWQVASAGEDInmADAAATK 315
Cdd:cd01160 238 LLIA-AGALAAaefMLEETRNYVKQRKAFGKTLAQLQVVRHKIAElatkVAVTRAFLDNCAWRHEQGRLDV--AEASMAK 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15610679 316 VFGTERVQRAGRLAEEIVGKYGNPAEPDTAELLRwlDAQtkrnlVITFGGGVNEVMREMIA 376
Cdd:cd01160 315 YWATELQNRVAYECVQLHGGWGYMREYPIARAYR--DAR-----VQPIYGGTTEIMKELIS 368
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
7-376 |
2.41e-57 |
|
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: 190.19 E-value: 2.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 7 PEQRQLQAEIRQYFSNLISPDERtemEKDRHGPAYRAVIRRMGrdgrlgvgwpkefgglgfgpieqqifvneahradvpl 86
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYAR---ERRETPEEPWELLAELG------------------------------------- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 87 pavtLQTVGPTLQAHGSELQKKKFLPAILAGEAHFAIGYTEPEAGTDLASLRTTAVRDGDHYIVNGQKVFTTGAHDADYI 166
Cdd:cd00567 41 ----LLLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLF 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 167 WLACRTDPNAAKHKGISILIVDTKDPGYSWTPIILADGAHHTNA--TYYNDVRVPVDMLVGKENDGWRLITTQLNNERVM 244
Cdd:cd00567 117 IVLARTDEEGPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTgeLVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 245 LGPA--GRFASIYDRVHAWASVPGGNGVTPIDHDDVKRALGEIRAIWRINELLNWQVA---SAGEDINMADAAATKVFGT 319
Cdd:cd00567 197 LAAValGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAwllDQGPDEARLEAAMAKLFAT 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 15610679 320 ERVQRAGRLAEEIVGKYGNPAEPDTAELLRwlDAqtkrnLVITFGGGVNEVMREMIA 376
Cdd:cd00567 277 EAAREVADLAMQIHGGRGYSREYPVERYLR--DA-----RAARIAEGTAEIQRLIIA 326
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
4-376 |
1.98e-49 |
|
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: 170.67 E-value: 1.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 4 DLTPEQRQLQAEIRQYFSNLISPdERTEMEKDRHGPayRAVIRRMGRDGRLGVGWPKEFGGLGFGPIEQQIFVNEAHRAD 83
Cdd:cd01156 1 GLDDEIEMLRQSVREFAQKEIAP-LAAKIDRDNEFP--RDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRAS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 84 vplPAVTLqTVGP-------TLQAHGSELQKKKFLPAILAGEAHFAIGYTEPEAGTDLASLRTTAVRDGDHYIVNGQKVF 156
Cdd:cd01156 78 ---GSVAL-SYGAhsnlcinQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 157 TTGAHDADYIWLACRTDPNAAKHkGISILIVDTKDPGYSWTPII--LADGAHHTNATYYNDVRVPVDMLVGKENDGWRLI 234
Cdd:cd01156 154 ITNGPDADTLVVYAKTDPSAGAH-GITAFIVEKGMPGFSRAQKLdkLGMRGSNTCELVFEDCEVPEENILGGENKGVYVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 235 TTQLNNERVML--GPAGRFASIYDRVHAWASVPGGNGvTPIDHDD-VKRALGEIRAIWRINELLNWQVASAGEDINMA-- 309
Cdd:cd01156 233 MSGLDYERLVLagGPIGIMQAALDVAIPYAHQRKQFG-QPIGEFQlVQGKLADMYTRLNASRSYLYTVAKACDRGNMDpk 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15610679 310 DAAATKVFGTERVQRAGRLAEEIVGKYGNPAEPDTAELLRwlDAQtkrnlVITFGGGVNEVMREMIA 376
Cdd:cd01156 312 DAAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRLLR--DAK-----LYEIGAGTSEIRRMVIG 371
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
7-381 |
2.98e-45 |
|
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: 159.74 E-value: 2.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 7 PEQRQLQAEIRQYFSNLISPDERtemEKDRHGPAYRAVIRRMGRDGRLGVGWPKEFGGLGFGPIEQQIFVNEAHRADVPL 86
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAA---EMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 87 ---PAVTLQTVGPTLQAHGSELQKKKFLPAILAGEAHFAIGYTEPEAGTDLASLRTTAVRDGDHYIVNGQKVFTTGAHDA 163
Cdd:cd01158 78 aviVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 164 DYIWLACRTDPnAAKHKGISILIVDTKDPGYSWTPII--LADGAHHTNATYYNDVRVPVDMLVGKENDGWRLITTQLNNE 241
Cdd:cd01158 158 DFYIVFAVTDP-SKGYRGITAFIVERDTPGLSVGKKEdkLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 242 RV-----MLGPAgRFASIYDRVHAWASVPGGngvTPI-DHDDVKRALGEIRAIWRINELLNWQVA---SAGEDINMaDAA 312
Cdd:cd01158 237 RIgiaaqALGIA-QAALDAAVDYAKERKQFG---KPIaDFQGIQFKLADMATEIEAARLLTYKAArlkDNGEPFIK-EAA 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15610679 313 ATKVFGTERVQRAGRLAEEIVGKYGNPAEPDTAELLRwlDAQtkrnlVITFGGGVNEVMREMIAASGLK 381
Cdd:cd01158 312 MAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYR--DAK-----ITEIYEGTSEIQRLVIAKHLLK 373
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
1-381 |
2.00e-31 |
|
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: 123.35 E-value: 2.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 1 MFIDLTPEQRQLQAEIRQYFSNLISPDERTEMEKDRhgpayRAVIRRMGRDGRLGVGWPKEFGGLGFGPIEQQIFVNEAH 80
Cdd:cd01161 23 LTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEKIP-----RKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 81 RAdvplpavtlQTVGPTLQAH-----------GSELQKKKFLPAILAGEAHFAIGYTEPEAGTDLASLRTTAVR--DGDH 147
Cdd:cd01161 98 MD---------LGFSVTLGAHqsigfkgillfGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLseDGKH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 148 YIVNGQKVFTTGAHDADYIWLACRT---DPNAAKHKGISILIVDTKDPGYSWTPIILADG--AHHTNATYYNDVRVPVDM 222
Cdd:cd01161 169 YVLNGSKIWITNGGIADIFTVFAKTevkDATGSVKDKITAFIVERSFGGVTNGPPEKKMGikGSNTAEVYFEDVKIPVEN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 223 LVGKENDGWRLITTQLNNERVMLGPA--GRFASIYDRV--HAWASVPGGNGVTPIDHDDVKRALGEIRA------IWRIN 292
Cdd:cd01161 249 VLGEVGDGFKVAMNILNNGRFGMGAAliGTMKRCIEKAvdYANNRKQFGKKIHEFGLIQEKLANMAILQyatesmAYMTS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 293 ELLNwqvASAGEDINMaDAAATKVFGTERVQRAGRLAEEIVGKYGNPAEPDTAELLRwldaQTKRNLVITfggGVNEVMR 372
Cdd:cd01161 329 GNMD---RGLKAEYQI-EAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLR----DLRIFRIFE---GTNEILR 397
|
....*....
gi 15610679 373 EMIAASGLK 381
Cdd:cd01161 398 LFIALTGLQ 406
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
5-378 |
5.18e-31 |
|
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: 121.40 E-value: 5.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 5 LTPEQRQLQAEIRQYFSNLISPdERTEMEKDRHGPAyrAVIRRMGRDGRLGVGWPKEFGGLGFGPIEQQIFVNEAHRADV 84
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAP-HAADWDQKKHFPV--DVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 85 PLPA-VTLQT-VGPTLQAHGSELQKKKFLPAILAGEAHFAIGYTEPEAGTDLASLRTTAVRDGDHYIVNGQKVFTTGAHD 162
Cdd:cd01162 78 STAAyISIHNmCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 163 ADYIWLACRTDPNAAkhKGISILIVDTKDPGYS---------WTpiiladgAHHTNATYYNDVRVPVDMLVGKENDGWRL 233
Cdd:cd01162 158 SDVYVVMARTGGEGP--KGISCFVVEKGTPGLSfganekkmgWN-------AQPTRAVIFEDCRVPVENRLGGEGQGFGI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 234 ITTQLNNERVMLGPA--GRFASIYDRVHAWASVPGGNGVTPIDHDDVKRALGEIRAIWRINELLNWQVASAGEDiNMADA 311
Cdd:cd01162 229 AMAGLNGGRLNIASCslGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDR-GDPDA 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15610679 312 ----AATKVFGTERVQRAGRLAEEIVGKYGNPAEPDTAELLRwlDAQTKRNLvitfgGGVNEVMREMIAAS 378
Cdd:cd01162 308 vklcAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVR--DLRVHQIL-----EGTNEIMRLIIARA 371
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
228-378 |
3.04e-27 |
|
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: 105.41 E-value: 3.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 228 NDGWRLITTQLNNERVMLG--PAGRFASIYDRVHAWASVPGGNGVTPIDHDDVKRALGEIRAIWRINELLNWQVASAGED 305
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAamALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15610679 306 INM--ADAAATKVFGTERVQRAGRLAEEIVGKYGNPAEPDTAELLRWldaqtkrNLVITFGGGVNEVMREMIAAS 378
Cdd:pfam00441 81 GGPdgAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRD-------ARVLRIGEGTSEIQRNIIARR 148
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
9-375 |
3.38e-26 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 108.43 E-value: 3.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 9 QRQLQAEIRQYFSNLISPDERTeMEKDRHGPAYRAVIRRMGRDGRLGVGWPKEFGGLGFGPIEQQIFVNEAHRADvplpa 88
Cdd:PLN02519 30 QLQFKESVQQFAQENIAPHAAA-IDATNSFPKDVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRAS----- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 89 vtlQTVGPTLQAH-----------GSELQKKKFLPAILAGEAHFAIGYTEPEAGTDLASLRTTAVRDGDHYIVNGQKVFT 157
Cdd:PLN02519 104 ---GSVGLSYGAHsnlcinqlvrnGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWC 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 158 TGAHDADYIWLACRTDPnAAKHKGISILIVDTKDPGYSWTPII--LADGAHHTNATYYNDVRVPVDMLVGKENDGWRLIT 235
Cdd:PLN02519 181 TNGPVAQTLVVYAKTDV-AAGSKGITAFIIEKGMPGFSTAQKLdkLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMM 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 236 TQLNNERVML--GPAGRFASIYDRVHAWASvpggngvtpiDHDDVKRALGEIRAI----------WRINELLNWQVASAG 303
Cdd:PLN02519 260 SGLDLERLVLaaGPLGLMQACLDVVLPYVR----------QREQFGRPIGEFQFIqgkladmytsLQSSRSYVYSVARDC 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15610679 304 ED--INMADAAATKVFGTERVQRAGRLAEEIVGKYGNPAEPDTAELLRwlDAQtkrnlVITFGGGVNEVMREMI 375
Cdd:PLN02519 330 DNgkVDRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLR--DAK-----LYEIGAGTSEIRRMLI 396
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
6-118 |
9.05e-26 |
|
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: 100.23 E-value: 9.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 6 TPEQRQLQAEIRQYFSNLISPDERtEMEKDRHGPayRAVIRRMGRDGRLGVGWPKEFGGLGFGPIEQQIFVNEAHRADVP 85
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAA-EWDEEGEFP--RELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADAS 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 15610679 86 L---PAVTLQTVGPTLQAHGSELQKKKFLPAILAGE 118
Cdd:pfam02771 78 ValaLSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
5-349 |
1.31e-23 |
|
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: 100.74 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 5 LTPEQRQLQAEIRQYFSNLISPderTEMEKDRHGPAYRAVIRRMGRDGRLGVGWPKEFGGLGFGPIEQQIFVNE-AHRAD 83
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIP---VAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEElAYGCT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 84 VPLPAVTLQTVGPT-LQAHGSELQKKKFLPAILAGEAHFAIGYTEPEAGTDLASLRTTAVRDGDHYIVNGQKVFTTGAHD 162
Cdd:cd01157 78 GVQTAIEANSLGQMpVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 163 ADYIWLACRTDPN--AAKHKGISILIVDTKDPGYS--WTPIILADGAHHTNATYYNDVRVPVDMLVGKENDGWRLITTQL 238
Cdd:cd01157 158 ANWYFLLARSDPDpkCPASKAFTGFIVEADTPGIQpgRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 239 NNER--VMLGPAGRFASIYDRVHAWASVPGGNGVTPIDHDDVKRALGEI-------RAIWRineLLNWQVASAGEdiNMA 309
Cdd:cd01157 238 DKTRppVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMamkvelaRLAYQ---RAAWEVDSGRR--NTY 312
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15610679 310 DAAATKVFGTERVQRAGRLAEEIVGKYGNPAEPDTAELLR 349
Cdd:cd01157 313 YASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMR 352
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
39-287 |
1.39e-23 |
|
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: 101.31 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 39 PAYRAVIRRMGRDGRLGVGWPKEFGGLGFgPIEQQIFVNE-AHRADVPLP-AVTLQTVGPTLQAHGSELQKKKFLPAILA 116
Cdd:cd01153 36 PPFKEALDAFAEAGWMALGVPEEYGGQGL-PITVYSALAEiFSRGDAPLMyASGTQGAAATLLAHGTEAQREKWIPRLAE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 117 GEAHFAIGYTEPEAGTDLASLRTTAVRDGD-HYIVNGQKVF-TTGAHDAD----YIWLAcRTDPNAAKHKGISILIVDTK 190
Cdd:cd01153 115 GEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFiSAGEHDMSenivHLVLA-RSEGAPPGVKGLSLFLVPKF 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 191 DPGYSWTPIILADGAH----HTNAT---YYNDVRVPvdmLVGKENDGWRLITTQLNNERVMLGPAG-RFASI-YDRVHAW 261
Cdd:cd01153 194 LDDGERNGVTVARIEEkmglHGSPTcelVFDNAKGE---LIGEEGMGLAQMFAMMNGARLGVGTQGtGLAEAaYLNALAY 270
|
250 260 270
....*....|....*....|....*....|....
gi 15610679 262 AS--VPGGNG------VTPIDHDDVKRALGEIRA 287
Cdd:cd01153 271 AKerKQGGDLikaapaVTIIHHPDVRRSLMTQKA 304
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
2-381 |
1.42e-22 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 98.47 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 2 FIDL---TPEQRQLQAEIRQYFSNLISPDERtemEKDRHGPAYRAVIRRMGRDGRLGVGWPKEFGGLGFGPIEQQIFVNE 78
Cdd:PTZ00461 31 FMDLynpTPEHAALRETVAKFSREVVDKHAR---EDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 79 AHRADvplPAVTLQTVGPTL------QAHGSELQKKKFLPAILAGEAHFAIGYTEPEAGTDLASLRTTAVRDGD-HYIVN 151
Cdd:PTZ00461 108 LSKYD---PGFCLAYLAHSMlfvnnfYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 152 GQKVFTTGAHDADYIWLACRTDPNaakhkgISILIVDTKDPGYSWTPIILADG--AHHTNATYYNDVRVPVDMLVGKEND 229
Cdd:PTZ00461 185 GSKIWITNGTVADVFLIYAKVDGK------ITAFVVERGTKGFTQGPKIDKCGmrASHMCQLFFEDVVVPAENLLGEEGK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 230 GWRLITTQLNNERVMLgpAGRFASIYDR----VHAWASVPGGNGVTPIDHDDVKRALGEIRAIWRINELLNWQVAS--AG 303
Cdd:PTZ00461 259 GMVGMMRNLELERVTL--AAMAVGIAERsvelMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHnvHP 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15610679 304 EDINMADAAATKVFGTERVQRAGRLAEEIVGKYGNPAEPDTAELlrWLDAQtkrnlVITFGGGVNEVMREMIAASGLK 381
Cdd:PTZ00461 337 GNKNRLGSDAAKLFATPIAKKVADSAIQVMGGMGYSRDMPVERL--WRDAK-----LLEIGGGTIEAHHKNITKDLLK 407
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
5-262 |
2.15e-22 |
|
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: 97.43 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 5 LTPEQRQLQAEIRQYFSNLISPdeRTEMEKdRHGPAYRAVIRRMGRDGRLGvGWPKEFGGLGFGPIEQQIFVNEAHRADV 84
Cdd:cd01151 13 LTEEERAIRDTAREFCQEELAP--RVLEAY-REEKFDRKIIEEMGELGLLG-ATIKGYGCAGLSSVAYGLIAREVERVDS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 85 PL-PAVTLQT--VGPTLQAHGSELQKKKFLPAILAGEAHFAIGYTEPEAGTDLASLRTTAVRDGDHYIVNGQKVFTTGAH 161
Cdd:cd01151 89 GYrSFMSVQSslVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 162 DADY--IWLACRTDpnaakhKGISILIVDTKDPGYSwTPII---LADGAHHTNATYYNDVRVPVDMLVgKENDGWRLITT 236
Cdd:cd01151 169 IADVfvVWARNDET------GKIRGFILERGMKGLS-APKIqgkFSLRASITGEIVMDNVFVPEENLL-PGAEGLRGPFK 240
|
250 260
....*....|....*....|....*...
gi 15610679 237 QLNNERVML--GPAGRFASIYDRVHAWA 262
Cdd:cd01151 241 CLNNARYGIawGALGAAEDCYHTARQYV 268
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
1-371 |
4.84e-22 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 96.34 E-value: 4.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 1 MFIDLTPEQRQLQAEIRQYFSNLISPDE-RTEMEKDRHGPAYRAVIRRMGRdGRLGVgwPKEFGGLGFGPIEQQIFVNEA 79
Cdd:PRK12341 1 MDFSLTEEQELLLASIRELITRNFPEEYfRTCDENGTYPREFMRALADNGI-SMLGV--PEEFGGTPADYVTQMLVLEEV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 80 HRADVPLPAVTLQTVGPTLQAHGSELQKKK-FLPAILAGEAHFAIGYTEPEAGTDLASLRTTAVR-DGDHYIvNGQKVFT 157
Cdd:PRK12341 78 SKCGAPAFLITNGQCIHSMRRFGSAEQLRKtAESTLETGDPAYALALTEPGAGSDNNSATTTYTRkNGKVYL-NGQKTFI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 158 TGAHDADYIWLACRTDPNAAKHKGISILIVDTKDPGYSWTPiiLADGAHHTNAT---YYNDVRVPVDMLVGKENDGWRLI 234
Cdd:PRK12341 157 TGAKEYPYMLVLARDPQPKDPKKAFTLWWVDSSKPGIKINP--LHKIGWHMLSTcevYLDNVEVEESDLVGEEGMGFLNV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 235 TTQLNNERVM-----LGPAGrfASIYDRVH-AWASVPGGNgvtPIDHDDV---KRALGEIraiwRINELLNWQVASAGED 305
Cdd:PRK12341 235 MYNFEMERLInaarsLGFAE--CAFEDAARyANQRIQFGK---PIGHNQLiqeKLTLMAI----KIENMRNMVYKVAWQA 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 306 IN----MADAAATKVFGTERVQRAGRLAEEIVGKYGNPAEPDTAELlrWLDAQTKRnlvitFGGGVNEVM 371
Cdd:PRK12341 306 DNgqslRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRF--WRDVRCER-----IGGGTDEIM 368
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
122-199 |
4.72e-21 |
|
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: 86.95 E-value: 4.72e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15610679 122 AIGYTEPEAGTDLASLRTTAV-RDGDHYIVNGQKVFTTGAHDADYIWLACRTDPnAAKHKGISILIVDTKDPGYSWTPI 199
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAAdGDGGGWVLNGTKWWITNAGIADLFLVLARTGG-DDRHGGISLFLVPKDAPGVSVRRI 78
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
98-243 |
2.60e-19 |
|
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: 88.60 E-value: 2.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 98 LQAHGSELQKKKFLPAILAGEAHFAIGYTEPE-AGTDLASLRTTAVRDGDHYIVNGQKVFTTGAHDAD---YIWLaCRTD 173
Cdd:cd01155 104 LHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGRKWWSSGAGDPRckiAIVM-GRTD 182
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15610679 174 PN-AAKHKGISILIVDTKDPGYSW---TPIILADGAHHTNA--TYYNdVRVPVDMLVGKENDGWRLITTQLNNERV 243
Cdd:cd01155 183 PDgAPRHRQQSMILVPMDTPGVTIirpLSVFGYDDAPHGHAeiTFDN-VRVPASNLILGEGRGFEIAQGRLGPGRI 257
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
39-187 |
6.17e-14 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 73.36 E-value: 6.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 39 PAYRAVIRRMGRDGRLGVGWPKEFGG----LGFGPIEQQIFVNeahrADVPLPAVTLQTVGP--TLQAHGSELQKKKFLP 112
Cdd:PTZ00456 99 KGFKEAYQALKAGGWTGISEPEEYGGqalpLSVGFITRELMAT----ANWGFSMYPGLSIGAanTLMAWGSEEQKEQYLT 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 113 AILAGEAHFAIGYTEPEAGTDLASLRTTAVRDGD-HYIVNGQKVF-TTGAHDAD----YIWLAcRTDPNAAKHKGISILI 186
Cdd:PTZ00456 175 KLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFiSAGDHDLTenivHIVLA-RLPNSLPTTKGLSLFL 253
|
.
gi 15610679 187 V 187
Cdd:PTZ00456 254 V 254
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
101-226 |
2.01e-13 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 71.75 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 101 HGSELQKKKFLPAILAGEAHFAIGYTEPE-AGTDLASLRTTAVRDGDHYIVNGQKVFTTGAHD--ADYIWLACRTDPNAA 177
Cdd:PLN02876 532 YGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAMDprCRVLIVMGKTDFNAP 611
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 15610679 178 KHKGISILIVDTKDPGYSWTPIILA---DGAHHTNATY-YNDVRVPV-DMLVGK 226
Cdd:PLN02876 612 KHKQQSMILVDIQTPGVQIKRPLLVfgfDDAPHGHAEIsFENVRVPAkNILLGE 665
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
5-337 |
3.42e-13 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 70.27 E-value: 3.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 5 LTPEQRQLQAEIRQYFSNLISPDERTEMEKDRHgPAYraVIRRMGRDGRLGvGWPKEFGGLGFGPIEQQIFVNEAHRADV 84
Cdd:PLN02526 29 LTPEEQALRKRVRECMEKEVAPIMTEYWEKAEF-PFH--IIPKLGSLGIAG-GTIKGYGCPGLSITASAIATAEVARVDA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 85 PLPAVTL---QTVGPTLQAHGSELQKKKFLPAILAGEAHFAIGYTEPEAGTDLASLRTTAVRDGDHYIVNGQKVFTTGAH 161
Cdd:PLN02526 105 SCSTFILvhsSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNST 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 162 DADY-IWLACRTDPNAakhkgISILIVDTKDPGYSWTPI-------ILADGahhtnATYYNDVRVP-VDMLVGKenDGWR 232
Cdd:PLN02526 185 FADVlVIFARNTTTNQ-----INGFIVKKGAPGLKATKIenkiglrMVQNG-----DIVLKDVFVPdEDRLPGV--NSFQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 233 LITTQLNNERVMLG--PAGRFASIYDRVHAWASVPGGNGVT----PIDHDDVKRALGEIRAIWrineLLNWQVASAGEDI 306
Cdd:PLN02526 253 DTNKVLAVSRVMVAwqPIGISMGVYDMCHRYLKERKQFGAPlaafQINQEKLVRMLGNIQAMF----LVGWRLCKLYESG 328
|
330 340 350
....*....|....*....|....*....|...
gi 15610679 307 NMADAAAT--KVFGTERVQRAGRLAEEIVGKYG 337
Cdd:PLN02526 329 KMTPGHASlgKAWITKKARETVALGRELLGGNG 361
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
1-246 |
1.57e-10 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 62.16 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 1 MFIDLTPEQRQLQAEIRQYFSNLISPDERTEMEKDRHGPA-YRAVIRRMGRDGRLgvgWPKEFGGLGFGPIEQQIFVNEA 79
Cdd:PRK03354 1 MDFNLNDEQELFVAGIRELMASENWEAYFAECDRDSVYPErFVKALADMGIDSLL---IPEEHGGLDAGFVTLAAVWMEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 80 HRADVPlPAVTLQTVG--PTLQAHGSELQKKKFLPAILAGEAHFAIGYTEPEAGTDLASLRTTAVRDGDHYIVNGQKVFT 157
Cdd:PRK03354 78 GRLGAP-TYVLYQLPGgfNTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 158 TGAHDADYIWLACRtDPNAAKHKGISILIVDTKDPGYSWTPII-LADGAHHTNATYYNDVRVPVDMLVGKENDGWRLITT 236
Cdd:PRK03354 157 TSSAYTPYIVVMAR-DGASPDKPVYTEWFVDMSKPGIKVTKLEkLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKE 235
|
250
....*....|
gi 15610679 237 QLNNERVMLG 246
Cdd:PRK03354 236 EFDHERFLVA 245
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
33-332 |
8.88e-10 |
|
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: 59.64 E-value: 8.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 33 EKDRHGPAYRAVIRRMGRDGRLGVGWPKEFGGLGfGPIEQQI-FVNEAHRADvplpavtlQTVGPTLQAH---------- 101
Cdd:cd01163 16 ERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLG-ASLPDLYeVVRELAAAD--------SNIAQALRAHfgfveallla 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 102 GSELQKKKFLPAILAGeaHFaIGYTEPEAGTDLASLRTTA-VRDGDHYIVNGQKVFTTGAHDADYIWLACrTDPNAAkhk 180
Cdd:cd01163 87 GPEQFRKRWFGRVLNG--WI-FGNAVSERGSVRPGTFLTAtVRDGGGYVLNGKKFYSTGALFSDWVTVSA-LDEEGK--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 181 gISILIVDTKDPGYS----WTPIiladGAHHTNA--TYYNDVRVPVDMLVGKENDGWR-----------LITTQLNNERV 243
Cdd:cd01163 160 -LVFAAVPTDRPGITvvddWDGF----GQRLTASgtVTFDNVRVEPDEVLPRPNAPDRgtlltaiyqlvLAAVLAGIARA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 244 MLGPAGRFASIYDRVHAWASVPggngvTPIDHDDVKRALGEIRA-IWRINELlnwqVASAGEDInmaDAAATKVFGTERV 322
Cdd:cd01163 235 ALDDAVAYVRSRTRPWIHSGAE-----SARDDPYVQQVVGDLAArLHAAEAL----VLQAARAL---DAAAAAGTALTAE 302
|
330
....*....|
gi 15610679 323 QRaGRLAEEI 332
Cdd:cd01163 303 AR-GEAALAV 311
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
35-193 |
3.27e-08 |
|
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: 55.07 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 35 DRHG---------PAYRAVIRRMGRDGRLGVGWpkefGGLGFGPIEQQ---IFVNEAHRADVPLP-AVTLQTVgPTLQAH 101
Cdd:cd01154 52 DRWGrrvdrvwvhPAWHALMRRLIEEGVINIED----GPAGEGRRHVHfaaGYLLSDAAAGLLCPlTMTDAAV-YALRKY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 102 GSELQKKkFLPAILAGEAH----FAIGYTEPEAGTDLASLRTTAVRD-GDHYIVNGQKVFTTGAhDADYIWLACRTDPNA 176
Cdd:cd01154 127 GPEELKQ-YLPGLLSDRYKtgllGGTWMTEKQGGSDLGANETTAERSgGGVYRLNGHKWFASAP-LADAALVLARPEGAP 204
|
170
....*....|....*..
gi 15610679 177 AKHKGISILIVDTKDPG 193
Cdd:cd01154 205 AGARGLSLFLVPRLLED 221
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
59-233 |
7.20e-06 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 48.03 E-value: 7.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 59 PKEFGGLGFGPIEQ-QIFVNEAHRADVPlpAVTL---QTVGP--TLQAHGSELQKKKFLPAILAGEAHFAIGYTEPEAGT 132
Cdd:PRK13026 128 PKEYGGKGFSAYANsTIVSKIATRSVSA--AVTVmvpNSLGPgeLLTHYGTQEQKDYWLPRLADGTEIPCFALTGPEAGS 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 133 DLASLRTTAV-----RDGDHYI---VNGQKVFTTGAHDADYIWLACRT-DPNA----AKHKGISILIVDTKDPGyswtpi 199
Cdd:PRK13026 206 DAGAIPDTGIvcrgeFEGEEVLglrLTWDKRYITLAPVATVLGLAFKLrDPDGllgdKKELGITCALIPTDHPG------ 279
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15610679 200 iLADGAHH--TNATYYN------DVRVPVDMLVG---KENDGWRL 233
Cdd:PRK13026 280 -VEIGRRHnpLGMAFMNgttrgkDVFIPLDWIIGgpdYAGRGWRM 323
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
59-232 |
1.03e-03 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 41.34 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 59 PKEFGGLGFGPIEQ-QIFVNEAHRADVplPAVTL---QTVGPT--LQAHGSELQKKKFLPAILAGEAHFAIGYTEPEAGT 132
Cdd:PRK09463 129 PKEYGGLEFSAYAHsRVLQKLASRSGT--LAVTVmvpNSLGPGelLLHYGTDEQKDHYLPRLARGEEIPCFALTSPEAGS 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610679 133 DLASLRTTAV-----RDGDHYI---VNGQKVFTTGAHDADYIWLACRT-DPNAakhkgisiLIVDTKDPGyswtpIILA- 202
Cdd:PRK09463 207 DAGSIPDTGVvckgeWQGEEVLgmrLTWNKRYITLAPIATVLGLAFKLyDPDG--------LLGDKEDLG-----ITCAl 273
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15610679 203 ---------DGAHH--TNATYYN------DVRVPVDMLVG-KEN--DGWR 232
Cdd:PRK09463 274 iptdtpgveIGRRHfpLNVPFQNgptrgkDVFIPLDYIIGgPKMagQGWR 323
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
95-144 |
2.96e-03 |
|
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: 39.62 E-value: 2.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 15610679 95 GPTLQAHGSELQKKKFLPAILAGEAHFAIGYTEPEAGTDLASLRTTAVRD 144
Cdd:cd01150 110 GNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYD 159
|
|
| |
