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Conserved domains on  [gi|919110950|ref|WP_052666593|]
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acyl-CoA dehydrogenase family protein [Nitriliruptor alkaliphilus]

Protein Classification

acyl-CoA dehydrogenase family protein( domain architecture ID 550)

acyl-CoA dehydrogenase (ACAD) family protein similar to acyl-CoA dehydrogenase that catalyzes the alpha,beta dehydrogenation of an acyl-CoA to form 2,3-dehydroacyl-CoA; requires an acceptor such as FAD, which becomes reduced

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ACAD super family cl09933
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 7-392 7.38e-124

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)


The actual alignment was detected with superfamily member cd01152:

Pssm-ID: 447864 [Multi-domain]  Cd Length: 380  Bit Score: 363.21  E-value: 7.38e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950   7 DDQQQLRDELRVYFEGLVTPELQEELAVTE-GGGPLAKQAIRRMAQDGWLGIGWPTEYGGRGFGAVEQFLFYDEAQRAGA 85
Cdd:cd01152    1 PSEEAFRAEVRAWLAAHLPPELREESALGYrEGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  86 PVPF--LTINTVGPSIANFGSEEMKRELLPKVLAGELFFSIGYTEPSAGTDLASLTTRAERDGDDLVINGQKIYTSLVDH 163
Cdd:cd01152   81 PVPFnqIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 164 ADYVWLACRTTPWPPehegtpvpeggsKHEGISIVLVPTDAEGFSYTPI-DTVGDARTFATYYDDVRVPVSNVVGGLDNG 242
Cdd:cd01152  161 ADWAWLLVRTDPEAP------------KHRGISILLVDMDSPGVTVRPIrSINGGEFFNEVFLDDVRVPDANRVGEVNDG 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 243 WKVIVGQLNHERVSLCSSGLLERKYIEVRRWAQQtklADSRRVVDQEWVQVHLARVHAKLEALRLMNYKVAWGTSVGKVS 322
Cdd:cd01152  229 WKVAMTTLNFERVSIGGSAATFFELLLARLLLLT---RDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPP 305

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 323 VADSSATKVYGTELYCEAYGLLLEILGAHGLLRRGSPDALLKSSLERAYRGTLILTFGGGTNEVQRDLIA 392
Cdd:cd01152  306 GAEASIAKLFGSELAQELAELALELLGTAALLRDPAPGAELAGRWEADYLRSRATTIYGGTSEIQRNIIA 375
 
Name Accession Description Interval E-value
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 7-392 7.38e-124

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: 363.21  E-value: 7.38e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950   7 DDQQQLRDELRVYFEGLVTPELQEELAVTE-GGGPLAKQAIRRMAQDGWLGIGWPTEYGGRGFGAVEQFLFYDEAQRAGA 85
Cdd:cd01152    1 PSEEAFRAEVRAWLAAHLPPELREESALGYrEGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  86 PVPF--LTINTVGPSIANFGSEEMKRELLPKVLAGELFFSIGYTEPSAGTDLASLTTRAERDGDDLVINGQKIYTSLVDH 163
Cdd:cd01152   81 PVPFnqIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 164 ADYVWLACRTTPWPPehegtpvpeggsKHEGISIVLVPTDAEGFSYTPI-DTVGDARTFATYYDDVRVPVSNVVGGLDNG 242
Cdd:cd01152  161 ADWAWLLVRTDPEAP------------KHRGISILLVDMDSPGVTVRPIrSINGGEFFNEVFLDDVRVPDANRVGEVNDG 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 243 WKVIVGQLNHERVSLCSSGLLERKYIEVRRWAQQtklADSRRVVDQEWVQVHLARVHAKLEALRLMNYKVAWGTSVGKVS 322
Cdd:cd01152  229 WKVAMTTLNFERVSIGGSAATFFELLLARLLLLT---RDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPP 305

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 323 VADSSATKVYGTELYCEAYGLLLEILGAHGLLRRGSPDALLKSSLERAYRGTLILTFGGGTNEVQRDLIA 392
Cdd:cd01152  306 GAEASIAKLFGSELAQELAELALELLGTAALLRDPAPGAELAGRWEADYLRSRATTIYGGTSEIQRNIIA 375
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 1-400 9.33e-109

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: 324.49  E-value: 9.33e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950   1 MHLALSDDQQQLRDELRVYFEGLVTPELQEelavTEGGGPLAKQAIRRMAQDGWLGIGWPTEYGGRGFGAVEQFLFYDEA 80
Cdd:COG1960    1 MDFELTEEQRALRDEVREFAEEEIAPEARE----WDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEEL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  81 QRAGAPV--PFLTINTVGPSIANFGSEEMKRELLPKVLAGELFFSIGYTEPSAGTDLASLTTRAERDGDDLVINGQKIYT 158
Cdd:COG1960   77 ARADASLalPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 159 SLVDHADYVWLACRTtpwppehegtpvpEGGSKHEGISIVLVPTDAEGFSYTPIDTVGDARTFAT---YYDDVRVPVSNV 235
Cdd:COG1960  157 TNAPVADVILVLART-------------DPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTgelFFDDVRVPAENL 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 236 VGGLDNGWKVIVGQLNHERVSLCSS--GLLERKYIEVRRWAQQTKlADSRRVVDQEWVQVHLARVHAKLEALRLMNYKVA 313
Cdd:COG1960  224 LGEEGKGFKIAMSTLNAGRLGLAAQalGIAEAALELAVAYARERE-QFGRPIADFQAVQHRLADMAAELEAARALVYRAA 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 314 WGTSVGKVSVADSSATKVYGTELYCEAYGLLLEILGAHGLLrRGSPdallkssLERAYRGTLILTFGGGTNEVQRDLIAV 393
Cdd:COG1960  303 WLLDAGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYT-REYP-------LERLYRDARILTIYEGTNEIQRLIIAR 374


                 ....*..
gi 919110950 394 FGLEMPR 400
Cdd:COG1960  375 RLLGRPG 381
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 240-392 2.61e-37

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: 132.38  E-value: 2.61e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  240 DNGWKVIVGQLNHERVSLCSS--GLLERKYIEVRRWAQQTKlADSRRVVDQEWVQVHLARVHAKLEALRLMNYKVAWGTS 317
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMalGLARRALDEALAYARRRK-AFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALD 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919110950  318 VGKVSVADSSATKVYGTELYCEAYGLLLEILGAHGLLRRGspdallksSLERAYRGTLILTFGGGTNEVQRDLIA 392
Cdd:pfam00441  80 AGGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREY--------PVERLYRDARVLRIGEGTSEIQRNIIA 146
PRK12341 PRK12341
acyl-CoA dehydrogenase;
1-386 2.94e-33

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 127.92  E-value: 2.94e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950   1 MHLALSDDQQQLRDELRvyfeGLVTPELQEE-LAVTEGGGPLAKQAIRRMAQDGWLGIGWPTEYGGRGFGAVEQFLFYDE 79
Cdd:PRK12341   1 MDFSLTEEQELLLASIR----ELITRNFPEEyFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  80 AQRAGAPVPFLTINTVGPSIANFGSEEMKRELLPKVL-AGELFFSIGYTEPSAGTDLASLTTRAERDGDDLVINGQKIYT 158
Cdd:PRK12341  77 VSKCGAPAFLITNGQCIHSMRRFGSAEQLRKTAESTLeTGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 159 SLVDHADYVWLACRTtpwppehegtpvPEGGSKHEGISIVLVPTDAEGFSYTPIDTVG--DARTFATYYDDVRVPVSNVV 236
Cdd:PRK12341 157 TGAKEYPYMLVLARD------------PQPKDPKKAFTLWWVDSSKPGIKINPLHKIGwhMLSTCEVYLDNVEVEESDLV 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 237 GGLDNGWKVIVGQLNHERVSLCSS--GLLERKYIEVRRWAQQtKLADSRRVVDQEWVQVHLARVHAKLEALRLMNYKVAW 314
Cdd:PRK12341 225 GEEGMGFLNVMYNFEMERLINAARslGFAECAFEDAARYANQ-RIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAW 303

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919110950 315 GTSVGKVSVADSSATKVYGTELYCEAYGLLLEILGAHGLLRrgspdallKSSLERAYRGTLILTFGGGTNEV 386
Cdd:PRK12341 304 QADNGQSLRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTD--------EARVSRFWRDVRCERIGGGTDEI 367
 
Name Accession Description Interval E-value
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 7-392 7.38e-124

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: 363.21  E-value: 7.38e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950   7 DDQQQLRDELRVYFEGLVTPELQEELAVTE-GGGPLAKQAIRRMAQDGWLGIGWPTEYGGRGFGAVEQFLFYDEAQRAGA 85
Cdd:cd01152    1 PSEEAFRAEVRAWLAAHLPPELREESALGYrEGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  86 PVPF--LTINTVGPSIANFGSEEMKRELLPKVLAGELFFSIGYTEPSAGTDLASLTTRAERDGDDLVINGQKIYTSLVDH 163
Cdd:cd01152   81 PVPFnqIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 164 ADYVWLACRTTPWPPehegtpvpeggsKHEGISIVLVPTDAEGFSYTPI-DTVGDARTFATYYDDVRVPVSNVVGGLDNG 242
Cdd:cd01152  161 ADWAWLLVRTDPEAP------------KHRGISILLVDMDSPGVTVRPIrSINGGEFFNEVFLDDVRVPDANRVGEVNDG 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 243 WKVIVGQLNHERVSLCSSGLLERKYIEVRRWAQQtklADSRRVVDQEWVQVHLARVHAKLEALRLMNYKVAWGTSVGKVS 322
Cdd:cd01152  229 WKVAMTTLNFERVSIGGSAATFFELLLARLLLLT---RDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPP 305

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 323 VADSSATKVYGTELYCEAYGLLLEILGAHGLLRRGSPDALLKSSLERAYRGTLILTFGGGTNEVQRDLIA 392
Cdd:cd01152  306 GAEASIAKLFGSELAQELAELALELLGTAALLRDPAPGAELAGRWEADYLRSRATTIYGGTSEIQRNIIA 375
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 1-400 9.33e-109

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: 324.49  E-value: 9.33e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950   1 MHLALSDDQQQLRDELRVYFEGLVTPELQEelavTEGGGPLAKQAIRRMAQDGWLGIGWPTEYGGRGFGAVEQFLFYDEA 80
Cdd:COG1960    1 MDFELTEEQRALRDEVREFAEEEIAPEARE----WDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEEL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  81 QRAGAPV--PFLTINTVGPSIANFGSEEMKRELLPKVLAGELFFSIGYTEPSAGTDLASLTTRAERDGDDLVINGQKIYT 158
Cdd:COG1960   77 ARADASLalPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 159 SLVDHADYVWLACRTtpwppehegtpvpEGGSKHEGISIVLVPTDAEGFSYTPIDTVGDARTFAT---YYDDVRVPVSNV 235
Cdd:COG1960  157 TNAPVADVILVLART-------------DPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTgelFFDDVRVPAENL 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 236 VGGLDNGWKVIVGQLNHERVSLCSS--GLLERKYIEVRRWAQQTKlADSRRVVDQEWVQVHLARVHAKLEALRLMNYKVA 313
Cdd:COG1960  224 LGEEGKGFKIAMSTLNAGRLGLAAQalGIAEAALELAVAYARERE-QFGRPIADFQAVQHRLADMAAELEAARALVYRAA 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 314 WGTSVGKVSVADSSATKVYGTELYCEAYGLLLEILGAHGLLrRGSPdallkssLERAYRGTLILTFGGGTNEVQRDLIAV 393
Cdd:COG1960  303 WLLDAGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYT-REYP-------LERLYRDARILTIYEGTNEIQRLIIAR 374


                 ....*..
gi 919110950 394 FGLEMPR 400
Cdd:COG1960  375 RLLGRPG 381
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 70-392 1.21e-65

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: 212.14  E-value: 1.21e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  70 AVEQFLFYDEAQRAGAPVPFLTINTVG-----PSIANFGSEEMKRELLPKVLAGELFFSIGYTEPSAGTDLASLTTRAER 144
Cdd:cd00567   14 AAEELEPYARERRETPEEPWELLAELGlllgaALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARK 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 145 DGDDLVINGQKIYTSLVDHADYVWLACRTtpwppehegtpvPEGGSKHEGISIVLVPTDAEGFSYTPIDTVGDAR---TF 221
Cdd:cd00567   94 DGDGYVLNGRKIFISNGGDADLFIVLART------------DEEGPGHRGISAFLVPADTPGVTVGRIWDKMGMRgsgTG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 222 ATYYDDVRVPVSNVVGGLDNGWKVIVGQLNHERVSLCSS--GLLERKYIEVRRWAQQTKLADsRRVVDQEWVQVHLARVH 299
Cdd:cd00567  162 ELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLLAAValGAARAALDEAVEYAKQRKQFG-KPLAEFQAVQFKLADMA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 300 AKLEALRLMNYKVAWGTSVGKVSVA-DSSATKVYGTELYCEAYGLLLEILGAHGLLRRgspdallkSSLERAYRGTLILT 378
Cdd:cd00567  241 AELEAARLLLYRAAWLLDQGPDEARlEAAMAKLFATEAAREVADLAMQIHGGRGYSRE--------YPVERYLRDARAAR 312

                        330
                 ....*....|....
gi 919110950 379 FGGGTNEVQRDLIA 392
Cdd:cd00567  313 IAEGTAEIQRLIIA 326
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 8-392 1.27e-61

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: 203.12  E-value: 1.27e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950   8 DQQQLRDELRVYFEGLVTPELQEelavTEGGGPLAKQAIRRMAQDGWLGIGWPTEYGGRGFGAVEQFLFYDEAQRAGAPV 87
Cdd:cd01160    2 EHDAFRDVVRRFFAKEVAPFHHE----WEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGSG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  88 PFLTINT--VGPSIANFGSEEMKRELLPKVLAGELFFSIGYTEPSAGTDLASLTTRAERDGDDLVINGQKIYTSLVDHAD 165
Cdd:cd01160   78 PGLSLHTdiVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLAD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 166 YVWLACRTTpwppehegtpvPEGGSKHeGISIVLVPTDAEGFSYT-PIDTVG--DARTFATYYDDVRVPVSNVVGGLDNG 242
Cdd:cd01160  158 VVIVVARTG-----------GEARGAG-GISLFLVERGTPGFSRGrKLKKMGwkAQDTAELFFDDCRVPAENLLGEENKG 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 243 WKVIVGQLNHERVSLCSSGLLERKYI--EVRRWAQQTKlADSRRVVDQEWVQVHLARVHAKLEALRLMNYKVAWGTSVGK 320
Cdd:cd01160  226 FYYLMQNLPQERLLIAAGALAAAEFMleETRNYVKQRK-AFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGR 304

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919110950 321 VSVADSSATKVYGTELYCEAYGLLLEILGAHGLLRrgspdallKSSLERAYRGTLILTFGGGTNEVQRDLIA 392
Cdd:cd01160  305 LDVAEASMAKYWATELQNRVAYECVQLHGGWGYMR--------EYPIARAYRDARVQPIYGGTTEIMKELIS 368
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 7-392 2.47e-53

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: 181.31  E-value: 2.47e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950   7 DDQQQLRDELRVYfeglvtpeLQEELAvtegggPLAKQ----------AIRRMAQDGWLGIGWPTEYGGRGFGAVEQFLF 76
Cdd:cd01158    1 EEHQMIRKTVRDF--------AEKEIA------PLAAEmdekgefpreVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIA 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  77 YDEAQRAGAPVP-FLTINT--VGPSIANFGSEEMKRELLPKVLAGELFFSIGYTEPSAGTDLASLTTRAERDGDDLVING 153
Cdd:cd01158   67 IEELAKVDASVAvIVSVHNslGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNG 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 154 QKIYTSLVDHADYVWLACRTTPwppehegtpvpegGSKHEGISIVLVPTDAEGFSY-TPIDTVGD--ARTFATYYDDVRV 230
Cdd:cd01158  147 SKMWITNGGEADFYIVFAVTDP-------------SKGYRGITAFIVERDTPGLSVgKKEDKLGIrgSSTTELIFEDVRV 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 231 PVSNVVGGLDNGWKVIVGQLNHERVSL--CSSGLLERKYIEVRRWAQQTKlADSRRVVDQEWVQVHLARVHAKLEALRLM 308
Cdd:cd01158  214 PKENILGEEGEGFKIAMQTLDGGRIGIaaQALGIAQAALDAAVDYAKERK-QFGKPIADFQGIQFKLADMATEIEAARLL 292

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 309 NYKVAWGTSVGKVSVADSSATKVYGTELYCEAYGLLLEILGAHGLLRRGspdallksSLERAYRGTLILTFGGGTNEVQR 388
Cdd:cd01158  293 TYKAARLKDNGEPFIKEAAMAKLFASEVAMRVTTDAVQIFGGYGYTKDY--------PVERYYRDAKITEIYEGTSEIQR 364


                 ....
gi 919110950 389 DLIA 392
Cdd:cd01158  365 LVIA 368
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 4-392 1.22e-46

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: 164.12  E-value: 1.22e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950   4 ALSDDQQQLRDELRVYFeglvtpelQEELAvtegggPLAKQ----------AIRRMAQDGWLGIGWPTEYGGRGFGAVEQ 73
Cdd:cd01156    1 GLDDEIEMLRQSVREFA--------QKEIA------PLAAKidrdnefprdLWRKMGKLGLLGITAPEEYGGSGMGYLAH 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  74 FLFYDEAQRAGAPVPF-------LTINtvgpSIANFGSEEMKRELLPKVLAGELFFSIGYTEPSAGTDLASLTTRAERDG 146
Cdd:cd01156   67 VIIMEEISRASGSVALsygahsnLCIN----QIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKG 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 147 DDLVINGQKIYTSLVDHADYVWLACRTTPWPPEHegtpvpeggskheGISIVLVPTDAEGFSYTP-IDTVG--DARTFAT 223
Cdd:cd01156  143 DRYVLNGSKMWITNGPDADTLVVYAKTDPSAGAH-------------GITAFIVEKGMPGFSRAQkLDKLGmrGSNTCEL 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 224 YYDDVRVPVSNVVGGLDNGWKVIVGQLNHERVSLCSS--GLLERKYIEVRRWAQQTKlADSRRVVDQEWVQVHLARVHAK 301
Cdd:cd01156  210 VFEDCEVPEENILGGENKGVYVLMSGLDYERLVLAGGpiGIMQAALDVAIPYAHQRK-QFGQPIGEFQLVQGKLADMYTR 288

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 302 LEALRLMNYKVAWGTSVGKVSVADSSATKVYGTELYCEAYGLLLEILGAHGLLRrgspdallKSSLERAYRGTLILTFGG 381
Cdd:cd01156  289 LNASRSYLYTVAKACDRGNMDPKDAAGVILYAAEKATQVALDAIQILGGNGYIN--------DYPTGRLLRDAKLYEIGA 360

                        410
                 ....*....|.
gi 919110950 382 GTNEVQRDLIA 392
Cdd:cd01156  361 GTSEIRRMVIG 371
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 240-392 2.61e-37

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: 132.38  E-value: 2.61e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  240 DNGWKVIVGQLNHERVSLCSS--GLLERKYIEVRRWAQQTKlADSRRVVDQEWVQVHLARVHAKLEALRLMNYKVAWGTS 317
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMalGLARRALDEALAYARRRK-AFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALD 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919110950  318 VGKVSVADSSATKVYGTELYCEAYGLLLEILGAHGLLRRGspdallksSLERAYRGTLILTFGGGTNEVQRDLIA 392
Cdd:pfam00441  80 AGGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREY--------PVERLYRDARVLRIGEGTSEIQRNIIA 146
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 5-392 3.20e-37

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: 138.73  E-value: 3.20e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950   5 LSDDQQQLRDELRVYFEGLVTPEL-----QEELAVtegggplakQAIRRMAQDGWLGIGWPTEYGGRGFGAVEQFLFYdE 79
Cdd:cd01162    1 LNEEQRAIQEVARAFAAKEMAPHAadwdqKKHFPV---------DVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIF-E 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  80 AQRAGAPV--PFLTI-NTVGPSIANFGSEEMKRELLPKVLAGELFFSIGYTEPSAGTDLASLTTRAERDGDDLVINGQKI 156
Cdd:cd01162   71 ALSTGCVStaAYISIhNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 157 YTSLVDHADYVWLACRTtpwppehegtpvpeGGSKHEGISIVLVPTDAEGFSY-TPIDTVG--DARTFATYYDDVRVPVS 233
Cdd:cd01162  151 FISGAGDSDVYVVMART--------------GGEGPKGISCFVVEKGTPGLSFgANEKKMGwnAQPTRAVIFEDCRVPVE 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 234 NVVGGLDNGWKVIVGQLNHERVSL--CSSG------LLERKYIEVRRwaqqtklADSRRVVDQEWVQVHLARVHAKLEAL 305
Cdd:cd01162  217 NRLGGEGQGFGIAMAGLNGGRLNIasCSLGaaqaalDLARAYLEERK-------QFGKPLADFQALQFKLADMATELVAS 289

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 306 RLMNYKVAWGTSVG-KVSVADSSATKVYGTELYCEAYGLLLEILGAHGLLRrgspdallKSSLERAYRGTLILTFGGGTN 384
Cdd:cd01162  290 RLMVRRAASALDRGdPDAVKLCAMAKRFATDECFDVANQALQLHGGYGYLK--------DYPVEQYVRDLRVHQILEGTN 361


                 ....*...
gi 919110950 385 EVQRDLIA 392
Cdd:cd01162  362 EIMRLIIA 369
PRK12341 PRK12341
acyl-CoA dehydrogenase;
1-386 2.94e-33

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 127.92  E-value: 2.94e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950   1 MHLALSDDQQQLRDELRvyfeGLVTPELQEE-LAVTEGGGPLAKQAIRRMAQDGWLGIGWPTEYGGRGFGAVEQFLFYDE 79
Cdd:PRK12341   1 MDFSLTEEQELLLASIR----ELITRNFPEEyFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  80 AQRAGAPVPFLTINTVGPSIANFGSEEMKRELLPKVL-AGELFFSIGYTEPSAGTDLASLTTRAERDGDDLVINGQKIYT 158
Cdd:PRK12341  77 VSKCGAPAFLITNGQCIHSMRRFGSAEQLRKTAESTLeTGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 159 SLVDHADYVWLACRTtpwppehegtpvPEGGSKHEGISIVLVPTDAEGFSYTPIDTVG--DARTFATYYDDVRVPVSNVV 236
Cdd:PRK12341 157 TGAKEYPYMLVLARD------------PQPKDPKKAFTLWWVDSSKPGIKINPLHKIGwhMLSTCEVYLDNVEVEESDLV 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 237 GGLDNGWKVIVGQLNHERVSLCSS--GLLERKYIEVRRWAQQtKLADSRRVVDQEWVQVHLARVHAKLEALRLMNYKVAW 314
Cdd:PRK12341 225 GEEGMGFLNVMYNFEMERLINAARslGFAECAFEDAARYANQ-RIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAW 303

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919110950 315 GTSVGKVSVADSSATKVYGTELYCEAYGLLLEILGAHGLLRrgspdallKSSLERAYRGTLILTFGGGTNEV 386
Cdd:PRK12341 304 QADNGQSLRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTD--------EARVSRFWRDVRCERIGGGTDEI 367
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 1-397 8.82e-27

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: 110.64  E-value: 8.82e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950   1 MHLALSDDQQQLRDELRVYFEGLVTPELQEELavteggGPLAKQAIRRMAQDGWLGIGWPTEYGGRGF-----GAVEQFL 75
Cdd:cd01161   23 LTEEQTEELNMLVGPVEKFFEEVNDPAKNDQL------EKIPRKTLTQLKELGLFGLQVPEEYGGLGLnntqyARLAEIV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  76 FYDeaqrAGAPVPFLTINTVG-PSIANFGSEEMKRELLPKVLAGELFFSIGYTEPSAGTDLASLTTRAER--DGDDLVIN 152
Cdd:cd01161   97 GMD----LGFSVTLGAHQSIGfKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLseDGKHYVLN 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 153 GQKIYTSLVDHADyVWLACRTTPwppehegtPVPEGGSKHEGISIVLVPTDAEGFSYTPIDT---VGDARTFATYYDDVR 229
Cdd:cd01161  173 GSKIWITNGGIAD-IFTVFAKTE--------VKDATGSVKDKITAFIVERSFGGVTNGPPEKkmgIKGSNTAEVYFEDVK 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 230 VPVSNVVGGLDNGWKVIVGQLNHERVSLCS--SGLLER------KYIEVRrwaQQTKladsRRVVDQEWVQVHLARVHAK 301
Cdd:cd01161  244 IPVENVLGEVGDGFKVAMNILNNGRFGMGAalIGTMKRciekavDYANNR---KQFG----KKIHEFGLIQEKLANMAIL 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 302 LEALRLMNYKVAWGTSVGKVS--VADSSATKVYGTE---LYC-EAygllLEILGAHGLLRrgspdallKSSLERAYRGTL 375
Cdd:cd01161  317 QYATESMAYMTSGNMDRGLKAeyQIEAAISKVFASEaawLVVdEA----IQIHGGMGFMR--------EYGVERVLRDLR 384

                        410       420
                 ....*....|....*....|..
gi 919110950 376 ILTFGGGTNEVQRDLIAVFGLE 397
Cdd:cd01161  385 IFRIFEGTNEILRLFIALTGLQ 406
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 5-392 2.21e-26

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: 108.83  E-value: 2.21e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950   5 LSDDQQQLRDELRVYFEGLVTPELQEELAVTEGGGPLakqaIRRMAQDGWLGIGWPTEYGGRGFGAVEQFLFYDEAQRAG 84
Cdd:cd01157    1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPL----IKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGC 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  85 APVPF-LTINTVG--PSIANfGSEEMKRELLPKVLAGELFFSIGYTEPSAGTDLASLTTRAERDGDDLVINGQKIYTSLV 161
Cdd:cd01157   77 TGVQTaIEANSLGqmPVIIS-GNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 162 DHADYVWLACRTTPWPpehegtPVPEGgskhEGISIVLVPTDAEGFSYTPIDTVGDAR---TFATYYDDVRVPVSNVVGG 238
Cdd:cd01157  156 GKANWYFLLARSDPDP------KCPAS----KAFTGFIVEADTPGIQPGRKELNMGQRcsdTRGITFEDVRVPKENVLIG 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 239 LDNGWKVIVGQLNHER--VSLCSSGLLERKYIEVRRWAQQTKlADSRRVVDQEWVQVHLARVHAKLEALRLMNYKVAWGT 316
Cdd:cd01157  226 EGAGFKIAMGAFDKTRppVAAGAVGLAQRALDEATKYALERK-TFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEV 304

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919110950 317 SVGKVSVADSSATKVYGTELYCEAYGLLLEILGAHGLLRrgspdallKSSLERAYRGTLILTFGGGTNEVQRDLIA 392
Cdd:cd01157  305 DSGRRNTYYASIAKAFAADIANQLATDAVQIFGGNGFNS--------EYPVEKLMRDAKIYQIYEGTSQIQRLIIS 372
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 6-119 3.09e-24

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: 96.38  E-value: 3.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950    6 SDDQQQLRDELRVYFEGLVTPELQEelAVTEGGGPlaKQAIRRMAQDGWLGIGWPTEYGGRGFGAVEQFLFYDEAQRAGA 85
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAE--WDEEGEFP--RELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADA 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 919110950   86 PV---PFLTINTVGPSIANFGSEEMKRELLPKVLAGE 119
Cdd:pfam02771  77 SValaLSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 5-354 2.94e-23

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: 100.13  E-value: 2.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950   5 LSDDQQQLRDELRVYFEGLVTPELQEELAVTEgggpLAKQAIRRMAQDGWLGiGWPTEYGGRGFGAVEQFLFYDEAQRAG 84
Cdd:cd01151   13 LTEEERAIRDTAREFCQEELAPRVLEAYREEK----FDRKIIEEMGELGLLG-ATIKGYGCAGLSSVAYGLIAREVERVD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  85 APV-PFLTIN---TVGPsIANFGSEEMKRELLPKVLAGELFFSIGYTEPSAGTDLASLTTRAERDGDDLVINGQKIYTSL 160
Cdd:cd01151   88 SGYrSFMSVQsslVMLP-IYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITN 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 161 VDHADY--VWLACRTTpwppehegtpvpeggskhEGISIVLVPTDAEGFSYTPIDTVGDARTFAT---YYDDVRVPVSNV 235
Cdd:cd01151  167 SPIADVfvVWARNDET------------------GKIRGFILERGMKGLSAPKIQGKFSLRASITgeiVMDNVFVPEENL 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 236 VGGLdNGWKVIVGQLNHER--VSLCSSGLLERKYIEVRRWAQQTK-----LADSrrvvdqEWVQVHLARVHAKLEALRLM 308
Cdd:cd01151  229 LPGA-EGLRGPFKCLNNARygIAWGALGAAEDCYHTARQYVLDRKqfgrpLAAF------QLVQKKLADMLTEIALGLLA 301

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 919110950 309 NYKVAWGTSVGKVSVADSSATKVYGTELYCEAYGLLLEILGAHGLL 354
Cdd:cd01151  302 CLRVGRLKDQGKATPEQISLLKRNNCGKALEIARTAREMLGGNGIS 347
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 3-391 1.93e-22

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 98.03  E-value: 1.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950   3 LALSDDQQQLRDELRVYFEGLVTPelQEELAVTEGGGPLAKQAIRRMAQDGWLGIGWPTEYGGRGFGAVEQFLFYDEAQR 82
Cdd:PLN02519  24 LLFDDTQLQFKESVQQFAQENIAP--HAAAIDATNSFPKDVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISR 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  83 AGAPVPF-------LTINtvgpSIANFGSEEMKRELLPKVLAGELFFSIGYTEPSAGTDLASLTTRAERDGDDLVINGQK 155
Cdd:PLN02519 102 ASGSVGLsygahsnLCIN----QLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNK 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 156 IYTSLVDHADYVWLACRTTpwppehegtpvPEGGSKheGISIVLVPTDAEGFSYT-PIDTVG--DARTFATYYDDVRVPV 232
Cdd:PLN02519 178 MWCTNGPVAQTLVVYAKTD-----------VAAGSK--GITAFIIEKGMPGFSTAqKLDKLGmrGSDTCELVFENCFVPE 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 233 SNVVGGLDNGWKVIVGQLNHERVSLCSS--GLLERKYIEVRRWAQQTKlADSRRVVDQEWVQVHLARVHAKLEALRLMNY 310
Cdd:PLN02519 245 ENVLGQEGKGVYVMMSGLDLERLVLAAGplGLMQACLDVVLPYVRQRE-QFGRPIGEFQFIQGKLADMYTSLQSSRSYVY 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 311 KVAWGTSVGKVSVADSSATKVYGTELYCEAYGLLLEILGAHGLLRRGSPDALLksslerayRGTLILTFGGGTNEVQRDL 390
Cdd:PLN02519 324 SVARDCDNGKVDRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLL--------RDAKLYEIGAGTSEIRRML 395


                 .
gi 919110950 391 I 391
Cdd:PLN02519 396 I 396
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 10-314 2.03e-22

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: 97.85  E-value: 2.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  10 QQLRDELRVYFEGLVTPELQEELAVTEGGG------PLAKQAIRRMAQDgwLGIgW----PTEYGGRGFGAVEQFLFYDE 79
Cdd:cd01155    4 QELRARVKAFMEEHVYPAEQEFLEYYAEGGdrwwtpPPIIEKLKAKAKA--EGL-WnlflPEVSGLSGLTNLEYAYLAEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  80 AQRAG-APVPFltiNTVGPSIAN------FGSEEMKRELLPKVLAGELFFSIGYTEPS-AGTDLASLTTRAERDGDDLVI 151
Cdd:cd01155   81 TGRSFfAPEVF---NCQAPDTGNmevlhrYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVI 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 152 NGQKIYTSLVDHAD---YVWLaCRTTpwppehegtpvPEGGSKHEGISIVLVPTDAEGFSYT-PIDTVG--DART--FAT 223
Cdd:cd01155  158 NGRKWWSSGAGDPRckiAIVM-GRTD-----------PDGAPRHRQQSMILVPMDTPGVTIIrPLSVFGydDAPHghAEI 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 224 YYDDVRVPVSNVVGGLDNGWKVIVGQLNHERVSLC--SSGLLERKyIEV--RRWAQQTklADSRRVVDQEWVQVHLARVH 299
Cdd:cd01155  226 TFDNVRVPASNLILGEGRGFEIAQGRLGPGRIHHCmrLIGAAERA-LELmcQRAVSRE--AFGKKLAQHGVVAHWIAKSR 302

                        330
                 ....*....|....*
gi 919110950 300 AKLEALRLMNYKVAW 314
Cdd:cd01155  303 IEIEQARLLVLKAAH 317
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 43-387 7.08e-22

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: 96.30  E-value: 7.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  43 KQAIRRMAQDGWLGIGWPTEYGGRGFG-AVEQFLF-YDEAQRAGAPVPFLTINTVGpSIANFGSEEMKRELLPKVLAGEL 120
Cdd:cd01153   39 KEALDAFAEAGWMALGVPEEYGGQGLPiTVYSALAeIFSRGDAPLMYASGTQGAAA-TLLAHGTEAQREKWIPRLAEGEW 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 121 FFSIGYTEPSAGTDLASLTTRAERDGD-DLVINGQKIYTSLVDHAD-----YVWLAcRTtpwppehegtpvPEGGSKHEG 194
Cdd:cd01153  118 TGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGEHDMsenivHLVLA-RS------------EGAPPGVKG 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 195 ISIVLVPTDAEGFSYTPIDTVG--------DARTFATYYDDVRVPvsnVVGGLDNGWKVIVGQLNHER--VSLCSSGLLE 264
Cdd:cd01153  185 LSLFLVPKFLDDGERNGVTVARieekmglhGSPTCELVFDNAKGE---LIGEEGMGLAQMFAMMNGARlgVGTQGTGLAE 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 265 RKYIEVRRWAQQTK-----LADSRRV--VDQEWVQVHLARVHAKLEALRLMN-YKV-----AWGTSVGKVSVADSSA--- 328
Cdd:cd01153  262 AAYLNALAYAKERKqggdlIKAAPAVtiIHHPDVRRSLMTQKAYAEGSRALDlYTAtvqdlAERKATEGEDRKALSAlad 341

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919110950 329 -----TKVYGTELYCEAYGLLLEILGAHGLLRrgspdallKSSLERAYRGTLILTFGGGTNEVQ 387
Cdd:cd01153  342 lltpvVKGFGSEAALEAVSDAIQVHGGSGYTR--------EYPIEQYYRDARITTIYEGTTGIQ 397
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 46-391 2.88e-20

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 91.92  E-value: 2.88e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  46 IRRMAQDGWLGIGWPTEYGGRGFGAVEQFLFYDEAQR--AGAPVPFLTINTVgpSIANF---GSEEMKRELLPKVLAGEL 120
Cdd:PTZ00461  74 FKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKydPGFCLAYLAHSML--FVNNFyysASPAQRARWLPKVLTGEH 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 121 FFSIGYTEPSAGTDLASLTTRAERDGD-DLVINGQKIYTSLVDHADYVWLAcrttpwppehegtpvpeggSKHEG-ISIV 198
Cdd:PTZ00461 152 VGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGTVADVFLIY-------------------AKVDGkITAF 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 199 LVPTDAEGFSYTP-IDTVG--DARTFATYYDDVRVPVSNVVGGLDNGWKVIVGQLNHERVSLCSS--GLLERKYIEVRRW 273
Cdd:PTZ00461 213 VVERGTKGFTQGPkIDKCGmrASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMavGIAERSVELMTSY 292

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 274 AQQTKlADSRRVVDQEWVQVHLARVHAKLEALRLMNYKVAWGTSVGKVSVADSSATKVYGTELYCEAYGLLLEILGAHGl 353
Cdd:PTZ00461 293 ASERK-AFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAKLFATPIAKKVADSAIQVMGGMG- 370

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 919110950 354 LRRGSPdallkssLERAYRGTLILTFGGGTNE-----VQRDLI 391
Cdd:PTZ00461 371 YSRDMP-------VERLWRDAKLLEIGGGTIEahhknITKDLL 406
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 123-215 6.51e-20

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: 83.87  E-value: 6.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  123 SIGYTEPSAGTDLASLTTRA-ERDGDDLVINGQKIYTSLVDHADYVWLACRTtpwppehegtpvpEGGSKHEGISIVLVP 201
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLART-------------GGDDRHGGISLFLVP 67

                          90
                  ....*....|....
gi 919110950  202 TDAEGFSYTPIDTV 215
Cdd:pfam02770  68 KDAPGVSVRRIETK 81
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 1-387 7.09e-16

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 78.33  E-value: 7.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950   1 MHLALSDDQQQLRDELRvyfEGLVTPELQEELAVTEGGGPLAKQAIRRMAQDGWLGIGWPTEYGGRGFGAVEQFLFYDEA 80
Cdd:PRK03354   1 MDFNLNDEQELFVAGIR---ELMASENWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMEL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  81 QRAGAPVPFL-----TINTVgpsiANFGSEEMKRELLPKVLAGELFFSIGYTEPSAGTDLASLTTRAERDGDDLVINGQK 155
Cdd:PRK03354  78 GRLGAPTYVLyqlpgGFNTF----LREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 156 IYTSLVDHADYVWLACRttpwppehegtpvpEGGSKHEGI-SIVLVPTDAEGFSYTPIDTVG---DArTFATYYDDVRVP 231
Cdd:PRK03354 154 CFITSSAYTPYIVVMAR--------------DGASPDKPVyTEWFVDMSKPGIKVTKLEKLGlrmDS-CCEITFDDVELD 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 232 VSNVVGGLDNGWKVIVGQLNHER--VSLCSSGLLERKYIEVRRWAQQtKLADSRRVVDQEWVQVHLARVHAKLEALRLMN 309
Cdd:PRK03354 219 EKDMFGREGNGFNRVKEEFDHERflVALTNYGTAMCAFEDAARYANQ-RVQFGEAIGRFQLIQEKFAHMAIKLNSMKNML 297

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919110950 310 YKVAWGTSVGKVSVADSSATKVYGTELYCEAYGLLLEILGAHGLLRrgspdallKSSLERAYRGTLILTFGGGTNEVQ 387
Cdd:PRK03354 298 YEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAG--------NHRISRFWRDLRVDRVSGGSDEMQ 367
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 43-201 8.01e-13

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 69.90  E-value: 8.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  43 KQAIRRMAQDGWLGIGWPTEYGGRGF----GAVEQFLFydeaqrAGAPVPFLTINTVGPSIAN----FGSEEMKRELLPK 114
Cdd:PTZ00456 102 KEAYQALKAGGWTGISEPEEYGGQALplsvGFITRELM------ATANWGFSMYPGLSIGAANtlmaWGSEEQKEQYLTK 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 115 VLAGELFFSIGYTEPSAGTDLASLTTRAERDGD-DLVINGQKIYTSLVDH-----ADYVWLAcRTTPWPPehegtpvpeg 188
Cdd:PTZ00456 176 LVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISAGDHdltenIVHIVLA-RLPNSLP---------- 244

                        170
                 ....*....|...
gi 919110950 189 GSKheGISIVLVP 201
Cdd:PTZ00456 245 TTK--GLSLFLVP 255
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 44-387 1.06e-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: 56.61  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  44 QAIRRMAQDGWLGIGW-PTEYGGRGFGAVEQFLFYDEAQRAGAPVPfLTINTVgPSIANFGSEEMKRELLPKVLAGE--- 119
Cdd:cd01154   69 ALMRRLIEEGVINIEDgPAGEGRRHVHFAAGYLLSDAAAGLLCPLT-MTDAAV-YALRKYGPEELKQYLPGLLSDRYktg 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 120 LFFSIGYTEPSAGTDLASLTTRAERDGDDL-VINGQKIYTSLVDhADYVWLACRTtpwppehEGTPvpeggSKHEGISIV 198
Cdd:cd01154  147 LLGGTWMTEKQGGSDLGANETTAERSGGGVyRLNGHKWFASAPL-ADAALVLARP-------EGAP-----AGARGLSLF 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 199 LVPTDAEGFSYTPI------DTVGDaRTFAT---YYDDVrvpVSNVVGGLDNGWKVIVGQLNHERVS--LCSSGLLERKY 267
Cdd:cd01154  214 LVPRLLEDGTRNGYrirrlkDKLGT-RSVATgevEFDDA---EAYLIGDEGKGIYYILEMLNISRLDnaVAALGIMRRAL 289

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 268 IEVRRWAQQTKlADSRRVVDQEWVQVHLARVHAKLEALRLMNYKVA--WG----------------TSVGKVSVADSSAT 329
Cdd:cd01154  290 SEAYHYARHRR-AFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAAraFDraaadkpveahmarlaTPVAKLIACKRAAP 368

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 919110950 330 KVYgtelycEAygllLEILGAHGLLRrgspdallKSSLERAYRGTLILTFGGGTNEVQ 387
Cdd:cd01154  369 VTS------EA----MEVFGGNGYLE--------EWPVARLHREAQVTPIWEGTGNIQ 408
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 24-355 2.18e-08

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: 55.41  E-value: 2.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  24 VTPELQEELAVTEGGGPLAKQAIRRMAQDGWLGIGWPTEYGGRGfGAVEQFL-FYDEAQRAGAPVPFLTINTVG--PSIA 100
Cdd:cd01163    6 LAARIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLG-ASLPDLYeVVRELAAADSNIAQALRAHFGfvEALL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 101 NFGSEEMKRELLPKVLAGELFFsiGYTEPSAGTDLASLTTRAERDGDDLVINGQKIYTSLVDHADYVWLACRttpwppEH 180
Cdd:cd01163   85 LAGPEQFRKRWFGRVLNGWIFG--NAVSERGSVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSAL------DE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 181 EGTPVpeggskhegisIVLVPTDAEGfsytpIDTVGDARTF--------ATYYDDVRVPVSNVVGGlDNGWKVI-----V 247
Cdd:cd01163  157 EGKLV-----------FAAVPTDRPG-----ITVVDDWDGFgqrltasgTVTFDNVRVEPDEVLPR-PNAPDRGtlltaI 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 248 GQLNHERVSLCSS-GLLERKYIEVRRWAQQTKLADSRRVVDQEWVQVHLARVHAKLEALRLMNYKVAW------------ 314
Cdd:cd01163  220 YQLVLAAVLAGIArAALDDAVAYVRSRTRPWIHSGAESARDDPYVQQVVGDLAARLHAAEALVLQAARaldaaaaagtal 299

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 919110950 315 -GTSVGKVSVAdSSATKVYGTELYCEAYGLLLEILGAHGLLR 355
Cdd:cd01163  300 tAEARGEAALA-VAAAKVVVTRLALDATSRLFEVGGASATAR 340
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 53-308 2.62e-08

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 56.12  E-value: 2.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  53 GWLGIGWPTEYGGRGFGA------VEQFlfydeAQRAG-APVPFLTINTVGPS--IANFGSEEMKRELLPKVLAGELFFS 123
Cdd:PRK13026 121 GFFALIIPKEYGGKGFSAyanstiVSKI-----ATRSVsAAVTVMVPNSLGPGelLTHYGTQEQKDYWLPRLADGTEIPC 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 124 IGYTEPSAGTDLASLT-----TRAERDGDD---LVINGQKIYTSLVDHADYVWLACRTTPwppehegtpvPE---GGSKH 192
Cdd:PRK13026 196 FALTGPEAGSDAGAIPdtgivCRGEFEGEEvlgLRLTWDKRYITLAPVATVLGLAFKLRD----------PDgllGDKKE 265

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 193 EGISIVLVPTDAEGFS----YTPIDTVgdartF---ATYYDDVRVPVSNVVGGLDN---GWKVIVGQLNHER-VSLCS-- 259
Cdd:PRK13026 266 LGITCALIPTDHPGVEigrrHNPLGMA-----FmngTTRGKDVFIPLDWIIGGPDYagrGWRMLVECLSAGRgISLPAlg 340

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 919110950 260 --SGLLERK----YIEVRRwaqQTKLAdsrrvVDQ-EWVQVHLARVHAK---LEALRLM 308
Cdd:PRK13026 341 taSGHMATRttgaYAYVRR---QFGMP-----IGQfEGVQEALARIAGNtylLEAARRL 391
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 49-261 5.55e-06

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 48.66  E-value: 5.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  49 MAQDGWLGIGWPTEYGGRGFGA-----VEQFLfydeAQRAGAP-----VPfltiNTVGPS--IANFGSEEMKRELLPKVL 116
Cdd:PRK09463 118 IKEHGFFGMIIPKEYGGLEFSAyahsrVLQKL----ASRSGTLavtvmVP----NSLGPGelLLHYGTDEQKDHYLPRLA 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 117 AGELFFSIGYTEPSAGTDLASLT-----TRAERDGDDLV---INGQKIYTSLVDHADYVWLACRTtpWPPEHEgtpvpEG 188
Cdd:PRK09463 190 RGEEIPCFALTSPEAGSDAGSIPdtgvvCKGEWQGEEVLgmrLTWNKRYITLAPIATVLGLAFKL--YDPDGL-----LG 262

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 189 GSKHEGISIVLVPTDAEGFS----YTPIDTVgdartF---ATYYDDVRVPVSNVVGGLDN---GWKVIVGQLNHER-VSL 257
Cdd:PRK09463 263 DKEDLGITCALIPTDTPGVEigrrHFPLNVP-----FqngPTRGKDVFIPLDYIIGGPKMagqGWRMLMECLSVGRgISL 337


                 ....
gi 919110950 258 CSSG 261
Cdd:PRK09463 338 PSNS 341
PLN02876 PLN02876
acyl-CoA dehydrogenase
 102-258 7.20e-05

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 45.17  E-value: 7.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 102 FGSEEMKRELLPKVLAGELFFSIGYTEPS-AGTDLASLTTRAERDGDDLVINGQKIYTS--LVDHADYVWLACRTTPWPP 178
Cdd:PLN02876 532 YGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSgaMDPRCRVLIVMGKTDFNAP 611

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 179 EHEGTPVPEGGSKHEGISIVLvPTDAEGFSYTPidtVGDARtfaTYYDDVRVPVSNVVGGLDNGWKVIVGQLNHERVSLC 258
Cdd:PLN02876 612 KHKQQSMILVDIQTPGVQIKR-PLLVFGFDDAP---HGHAE---ISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHC 684
PLN02526 PLN02526
acyl-coenzyme A oxidase
 5-354 7.41e-05

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 44.46  E-value: 7.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950   5 LSDDQQQLRDELRVYFEGLVTPELQEELAVTEgggpLAKQAIRRMAQDGWLGiGWPTEYGGRGFGAVEQFLFYDEAQRAG 84
Cdd:PLN02526  29 LTPEEQALRKRVRECMEKEVAPIMTEYWEKAE----FPFHIIPKLGSLGIAG-GTIKGYGCPGLSITASAIATAEVARVD 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  85 APVP-FLTINT--VGPSIANFGSEEMKRELLPKVLAGELFFSIGYTEPSAGTDLASLTTRAERDGDDLVINGQKIYTSLV 161
Cdd:PLN02526 104 ASCStFILVHSslAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNS 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 162 DHADYVWLACRTTpwppehegtpvpeggsKHEGISIVLVPTDAEGFSYTPIDTVGDARTFAT---YYDDVRVPVSNVVGG 238
Cdd:PLN02526 184 TFADVLVIFARNT----------------TTNQINGFIVKKGAPGLKATKIENKIGLRMVQNgdiVLKDVFVPDEDRLPG 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 239 LdNGWKVIVGQLNHERV--------------SLCSSGLLERKYIEVRRWAQQtkladsrrvVDQEwvqvHLARVHAKLEA 304
Cdd:PLN02526 248 V-NSFQDTNKVLAVSRVmvawqpigismgvyDMCHRYLKERKQFGAPLAAFQ---------INQE----KLVRMLGNIQA 313

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 919110950 305 LRLMNYKVAWGTSVGKVSVADSSATKVYGTELYCEAYGLLLEILGAHGLL 354
Cdd:PLN02526 314 MFLVGWRLCKLYESGKMTPGHASLGKAWITKKARETVALGRELLGGNGIL 363
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
 61-244 2.09e-04

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 43.33  E-value: 2.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  61 TEYGGRGFGAVEQFLFYDEAQRAGAPVPFLTINTVGPS---IANFGSEEMKRELLPKVLAGELFfsIGY-TEPSAGTDLA 136
Cdd:PTZ00457  72 TEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHSGFCtylLSTVGSKELKGKYLTAMSDGTIM--MGWaTEEGCGSDIS 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950 137 SLTTRAE-RDGDDLVINGQKIYTSLVDHADYVWLACRTTPWPPEhegtpvpEGGSKHEGISIVLVPTDAEGFSytpidTV 215
Cdd:PTZ00457 150 MNTTKASlTDDGSYVLTGQKRCEFAASATHFLVLAKTLTQTAAE-------EGATEVSRNSFFICAKDAKGVS-----VN 217

                        170       180
                 ....*....|....*....|....*....
gi 919110950 216 GDARTFATyyddvrVPVSNVVGGLDNGWK 244
Cdd:PTZ00457 218 GDSVVFEN------TPAADVVGVVGEGFK 240
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 75-152 2.68e-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: 40.00  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919110950  75 LFYDeaQRAGAPVpFLTINTVGPSIANFGSEEMKRELLPKVLAGELFFSIGYTEPSAGTDLASLTTRAERD--GDDLVIN 152
Cdd:cd01150   92 GGYD--LSLGAKL-GLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDplTQEFVIN 168
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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