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Conserved domains on  [gi|1958798438|ref|XP_038938217|]
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isobutyryl-CoA dehydrogenase, mitochondrial isoform X2 [Rattus norvegicus]

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 ...
 1-211 5.51e-147

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 cd01162:

Pssm-ID: 447864 [Multi-domain]  Cd Length: 375  Bit Score: 413.76  E-value: 5.51e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438   1 MCRTGGSGPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASC 80
Cdd:cd01162   164 MARTGGEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASC 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  81 SLGAAHASVVLTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDAVALCSMAKLFVTEECF 160
Cdd:cd01162   244 SLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATDECF 323

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958798438 161 TICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRSLLQ 211
Cdd:cd01162   324 DVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLT 374
 
Name Accession Description Interval E-value
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 1-211 5.51e-147

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: 413.76  E-value: 5.51e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438   1 MCRTGGSGPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASC 80
Cdd:cd01162   164 MARTGGEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASC 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  81 SLGAAHASVVLTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDAVALCSMAKLFVTEECF 160
Cdd:cd01162   244 SLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATDECF 323

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958798438 161 TICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRSLLQ 211
Cdd:cd01162   324 DVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLT 374
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 1-210 3.54e-83

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: 251.68  E-value: 3.54e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438   1 MCRTGGS-GPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVAS 79
Cdd:COG1960   168 LARTDPAaGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGRLGLAA 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  80 CSLGAAHASVVLTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEErEDAVALCSMAKLFVTEEC 159
Cdd:COG1960   248 QALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAG-EDAALEAAMAKLFATEAA 326

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958798438 160 FTICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRSLL 210
Cdd:COG1960   327 LEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLL 377
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 60-209 2.52e-51

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: 162.81  E-value: 2.52e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  60 GQGFLIAMKGLNGGRINVASCSLGAAHASVVLTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQE 139
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438 140 EREDAVAlCSMAKLFVTEECFTICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRSL 209
Cdd:pfam00441  81 GGPDGAE-ASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 7-212 7.30e-38

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 135.39  E-value: 7.30e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438   7 SGPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASCSLGAAH 86
Cdd:PLN02519  199 AGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQ 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  87 ASVVLTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDAVAlCSMAKLFVTEECFTICNQA 166
Cdd:PLN02519  279 ACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKD-CAGVILCAAERATQVALQA 357

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958798438 167 LQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRSLLQD 212
Cdd:PLN02519  358 IQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKE 403
 
Name Accession Description Interval E-value
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 1-211 5.51e-147

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: 413.76  E-value: 5.51e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438   1 MCRTGGSGPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASC 80
Cdd:cd01162   164 MARTGGEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASC 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  81 SLGAAHASVVLTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDAVALCSMAKLFVTEECF 160
Cdd:cd01162   244 SLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATDECF 323

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958798438 161 TICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRSLLQ 211
Cdd:cd01162   324 DVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLT 374
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 1-210 3.54e-83

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: 251.68  E-value: 3.54e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438   1 MCRTGGS-GPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVAS 79
Cdd:COG1960   168 LARTDPAaGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGRLGLAA 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  80 CSLGAAHASVVLTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEErEDAVALCSMAKLFVTEEC 159
Cdd:COG1960   248 QALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAG-EDAALEAAMAKLFATEAA 326

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958798438 160 FTICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRSLL 210
Cdd:COG1960   327 LEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLL 377
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 1-207 2.56e-81

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: 245.27  E-value: 2.56e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438   1 MCRTGGSGP--KGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVA 78
Cdd:cd00567   119 LARTDEEGPghRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLLA 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  79 SCSLGAAHASVVLTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDAVALCSMAKLFVTEE 158
Cdd:cd00567   199 AVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFATEA 278

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958798438 159 CFTICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISR 207
Cdd:cd00567   279 AREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 1-210 2.92e-79

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: 241.40  E-value: 2.92e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438   1 MCRTGGS-GPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVAS 79
Cdd:cd01158   163 FAVTDPSkGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGIAA 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  80 CSLGAAHASVVLTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAvALQEEREDAVALCSMAKLFVTEEC 159
Cdd:cd01158   243 QALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAA-RLKDNGEPFIKEAAMAKLFASEVA 321

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958798438 160 FTICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRSLL 210
Cdd:cd01158   322 MRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLL 372
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 3-210 5.78e-54

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: 176.54  E-value: 5.78e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438   3 RTGG--SGPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASC 80
Cdd:cd01160   164 RTGGeaRGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAAG 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  81 SLGAAHASVVLTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDaVALCSMAKLFVTEECF 160
Cdd:cd01160   244 ALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLD-VAEASMAKYWATELQN 322

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958798438 161 TICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRSLL 210
Cdd:cd01160   323 RVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 60-209 2.52e-51

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: 162.81  E-value: 2.52e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  60 GQGFLIAMKGLNGGRINVASCSLGAAHASVVLTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQE 139
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438 140 EREDAVAlCSMAKLFVTEECFTICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRSL 209
Cdd:pfam00441  81 GGPDGAE-ASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 6-212 5.69e-51

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: 169.57  E-value: 5.69e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438   6 GSGPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASCSLGAA 85
Cdd:cd01161   200 GSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTM 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  86 HASVVLTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMI-RTAAVALQEEREDAVALCSMAKLFVTEECFTICN 164
Cdd:cd01161   280 KRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAyMTSGNMDRGLKAEYQIEAAISKVFASEAAWLVVD 359

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958798438 165 QALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRSLLQD 212
Cdd:cd01161   360 EAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQH 407
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 3-211 1.97e-50

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: 167.59  E-value: 1.97e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438   3 RTGGS-GPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASCS 81
Cdd:cd01156   168 KTDPSaGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYERLVLAGGP 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  82 LGAAHASVVLTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDAVAlCSMAKLFVTEECFT 161
Cdd:cd01156   248 IGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKD-AAGVILYAAEKATQ 326

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958798438 162 ICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRSLLQ 211
Cdd:cd01156   327 VALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 10-210 4.79e-40

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: 140.41  E-value: 4.79e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  10 KGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASCSLGAAHASV 89
Cdd:cd01157   177 KAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKTRPPVAAGAVGLAQRAL 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  90 VLTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDAVaLCSMAKLFVTEECFTICNQALQM 169
Cdd:cd01157   257 DEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTY-YASIAKAFAADIANQLATDAVQI 335

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1958798438 170 HGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRSLL 210
Cdd:cd01157   336 FGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 7-212 7.30e-38

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 135.39  E-value: 7.30e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438   7 SGPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASCSLGAAH 86
Cdd:PLN02519  199 AGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQ 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  87 ASVVLTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDAVAlCSMAKLFVTEECFTICNQA 166
Cdd:PLN02519  279 ACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKD-CAGVILCAAERATQVALQA 357

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958798438 167 LQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRSLLQD 212
Cdd:PLN02519  358 IQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKE 403
PRK12341 PRK12341
acyl-CoA dehydrogenase;
10-212 1.14e-30

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 115.60  E-value: 1.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  10 KGISCIVVEKGTPGLSFGKKEKkVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASCSLGAAHASV 89
Cdd:PRK12341  179 KAFTLWWVDSSKPGIKINPLHK-IGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFEMERLINAARSLGFAECAF 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  90 VLTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAValqeEREDAVAL---CSMAKLFVTEECFTICNQA 166
Cdd:PRK12341  258 EDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAW----QADNGQSLrtsAALAKLYCARTAMEVIDDA 333

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958798438 167 LQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRSLLQD 212
Cdd:PRK12341  334 IQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKD 379
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 3-198 2.64e-25

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: 101.70  E-value: 2.64e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438   3 RTGGSGP--KGISCIVVEK----GTP-GLSFGKKEKKVGWNSQPTRAVIFEDCAVPVanrIGTEGQGFLIAMKGLNGGRI 75
Cdd:cd01153   174 RSEGAPPgvKGLSLFLVPKflddGERnGVTVARIEEKMGLHGSPTCELVFDNAKGEL---IGEEGMGLAQMFAMMNGARL 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  76 NVASCSLGAAHASVVLTQEHLKVRKQFGAPL--------ARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDAV-- 145
Cdd:cd01153   251 GVGTQGTGLAEAAYLNALAYAKERKQGGDLIkaapavtiIHHPDVRRSLMTQKAYAEGSRALDLYTATVQDLAERKATeg 330

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958798438 146 -----------ALCSMAKLFVTEECFTICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSN 198
Cdd:cd01153   331 edrkalsaladLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTT 394
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 11-207 5.65e-25

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: 100.51  E-value: 5.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  11 GISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIgTEGQGFLIAMKGLNGGRINVASCSLGAAHASVV 90
Cdd:cd01151   184 KIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL-PGAEGLRGPFKCLNNARYGIAWGALGAAEDCYH 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  91 LTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLM-IRTAavALQEEREDAVALCSMAKLFVTEECFTICNQALQM 169
Cdd:cd01151   263 TARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLAcLRVG--RLKDQGKATPEQISLLKRNNCGKALEIARTAREM 340

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958798438 170 HGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISR 207
Cdd:cd01151   341 LGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGR 378
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 1-212 2.62e-23

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 95.67  E-value: 2.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438   1 MCRTGGSGPKGI-SCIVVEKGTPGLSFGKKEKkVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVAS 79
Cdd:PRK03354  168 MARDGASPDKPVyTEWFVDMSKPGIKVTKLEK-LGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVAL 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  80 CSLGAAHASVVLTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVAlQEEREDAVALCSMAKLFVTEEC 159
Cdd:PRK03354  247 TNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWK-ADNGTITSGDAAMCKYFCANAA 325

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958798438 160 FTICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRSLLQD 212
Cdd:PRK03354  326 FEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQ 378
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 7-201 6.08e-23

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: 95.13  E-value: 6.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438   7 SGPKGISCIVV----EKGT-PGLSFGKKEKKVGWNSQPTRAVIFEDCavpVANRIGTEGQGFLIAMKGLNGGRINVASCS 81
Cdd:cd01154   205 AGARGLSLFLVprllEDGTrNGYRIRRLKDKLGTRSVATGEVEFDDA---EAYLIGDEGKGIYYILEMLNISRLDNAVAA 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  82 LGAAHASVVLTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDAVALCSMAKLFVTEECFT 161
Cdd:cd01154   282 LGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKPVEAHMARLATPVAKLI 361

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958798438 162 ICNQALQM-------HGGYGYLKDYAVQQYMRDSRVHQILEGSNEVM 201
Cdd:cd01154   362 ACKRAAPVtseamevFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQ 408
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 12-211 8.12e-22

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 91.92  E-value: 8.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  12 ISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASCSLGAAHASVVL 91
Cdd:PTZ00461  209 ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIAERSVEL 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  92 TQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDAVAlCSMAKLFVTEECFTICNQALQMHG 171
Cdd:PTZ00461  289 MTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLG-SDAAKLFATPIAKKVADSAIQVMG 367

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958798438 172 GYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRSLLQ 211
Cdd:PTZ00461  368 GMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLK 407
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
77-199 5.01e-19

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 79.31  E-value: 5.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  77 VASCSLGAAHASVVLTQEHL--KVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDA-------VAL 147
Cdd:pfam08028   2 IAAAALGAARAALAEFTERArgRVRAYFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAAAAGkpvtpalRAE 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958798438 148 CSMAKLFVTEECFTICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNE 199
Cdd:pfam08028  82 ARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 1-211 1.37e-17

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: 80.13  E-value: 1.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438   1 MCRTGGSGP---KGISCIVVEKGTPGLSFGKKEKKVGWNSQPT--RAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRI 75
Cdd:cd01155   178 MGRTDPDGAprhRQQSMILVPMDTPGVTIIRPLSVFGYDDAPHghAEITFDNVRVPASNLILGEGRGFEIAQGRLGPGRI 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  76 NVASCSLGAAHASVVLTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVAL-QEEREDAVALCSMAKLF 154
Cdd:cd01155   258 HHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIdTVGNKAARKEIAMIKVA 337

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958798438 155 VTEECFTICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRSLLQ 211
Cdd:cd01155   338 APRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARMELK 394
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 3-211 5.45e-14

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: 69.68  E-value: 5.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438   3 RTGGSGPK--GISCIVVEKGTPGLSFGKKEKKVGwnSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGR---INV 77
Cdd:cd01152   169 RTDPEAPKhrGISILLVDMDSPGVTVRPIRSING--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERvsiGGS 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  78 ASCSLGAAhasvvltQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEReDAVALCSMAKLFVTE 157
Cdd:cd01152   247 AATFFELL-------LARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGK-PPGAEASIAKLFGSE 318

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798438 158 ECFTICNQALQMHGGYGYLKDYA--------VQQYMRDSRVHQILEGSNEVMRMLISRSLLQ 211
Cdd:cd01152   319 LAQELAELALELLGTAALLRDPApgaelagrWEADYLRSRATTIYGGTSEIQRNIIAERLLG 380
PLN02876 PLN02876
acyl-CoA dehydrogenase
 1-211 8.37e-12

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 63.66  E-value: 8.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438   1 MCRTGGSGP--KGISCIVVEKGTPGLSFGKKEKKVGWNSQPT--RAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRIN 76
Cdd:PLN02876  603 MGKTDFNAPkhKQQSMILVDIQTPGVQIKRPLLVFGFDDAPHghAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLH 682

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  77 VASCSLGAAHASVVLTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEE-REDAVALCSMAKLFV 155
Cdd:PLN02876  683 HCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDRLgNKKARGIIAMAKVAA 762

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958798438 156 TEECFTICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRSLLQ 211
Cdd:PLN02876  763 PNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAKLELQ 818
PLN02526 PLN02526
acyl-coenzyme A oxidase
 12-209 1.83e-11

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 62.18  E-value: 1.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  12 ISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIgTEGQGFLIAMKGLNGGRINVASCSLGAAHASVVL 91
Cdd:PLN02526  201 INGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRL-PGVNSFQDTNKVLAVSRVMVAWQPIGISMGVYDM 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  92 TQEHLKVRKQFGAPLARSQYLQFQLADM-----ATKLVASRLmirtaaVALQEEREDAVALCSMAKLFVTEECFTICNQA 166
Cdd:PLN02526  280 CHRYLKERKQFGAPLAAFQINQEKLVRMlgniqAMFLVGWRL------CKLYESGKMTPGHASLGKAWITKKARETVALG 353

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958798438 167 LQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRSL 209
Cdd:PLN02526  354 RELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREI 396
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 11-174 6.64e-11

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 60.99  E-value: 6.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  11 GISCIVVEKGTPGLSFGKKEKKVGWNSQ--PTRAvifEDCAVPVANRIGTE---GQGFLIAMKGLNGGR-INVASCSLGA 84
Cdd:PRK09463  268 GITCALIPTDTPGVEIGRRHFPLNVPFQngPTRG---KDVFIPLDYIIGGPkmaGQGWRMLMECLSVGRgISLPSNSTGG 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  85 AHASVVLTQEHLKVRKQFGAPLARSQYLQFQLADMATK---LVASRLMIrTAAVALQEerEDAVaLCSMAKLFVTEECFT 161
Cdd:PRK09463  345 AKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNaylMDAARTLT-TAAVDLGE--KPSV-LSAIAKYHLTERGRQ 420

                         170
                  ....*....|...
gi 1958798438 162 ICNQALQMHGGYG 174
Cdd:PRK09463  421 VINDAMDIHGGKG 433
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 5-174 1.81e-10

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 59.59  E-value: 1.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438   5 GGSGPKGISCIVVEKGTPGLSFGKKEKKVGWNSQ--PTRAvifEDCAVPVANRIGTE---GQGFLIAMKGLNGGR-INVA 78
Cdd:PRK13026  261 GDKKELGITCALIPTDHPGVEIGRRHNPLGMAFMngTTRG---KDVFIPLDWIIGGPdyaGRGWRMLVECLSAGRgISLP 337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  79 SCSLGAAHASVVLTQEHLKVRKQFGAPLARSQYLQFQLADMATK---LVASRLMIrTAAVALQEEREDAVAlcsMAKLFV 155
Cdd:PRK13026  338 ALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGNtylLEAARRLT-TTGLDLGVKPSVVTA---IAKYHM 413

                         170
                  ....*....|....*....
gi 1958798438 156 TEECFTICNQALQMHGGYG 174
Cdd:PRK13026  414 TELARDVVNDAMDIHAGKG 432
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 150-210 9.31e-07

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 48.71  E-value: 9.31e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798438 150 MAKLFVTEECFTICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRM-LISRSLL 210
Cdd:PTZ00456  418 IAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALdFIGRKVL 479
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 1-46 2.78e-06

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: 44.19  E-value: 2.78e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1958798438   1 MCRTGG-SGPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFE 46
Cdd:pfam02770  49 LARTGGdDRHGGISLFLVPKDAPGVSVRRIETKLGVRGLPTGELVFD 95
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
 11-209 4.48e-06

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 46.67  E-value: 4.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  11 GISCIVVEKGTP-----GLSFGKKEKKVGWNSQPTRAVIFEDCavpVANRIGTEGQGF--LIAMKGLNggRINvasCSLG 83
Cdd:PRK11561  234 GLSCFFVPRFLPdgqrnAIRLERLKDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIrlILKMGGMT--RFD---CALG 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  84 AaHA------SVVLTQEHLkvRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDAVALcsMAKLFVTE 157
Cdd:PRK11561  306 S-HGlmrrafSVAIYHAHQ--RQVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDRRADAKEAL--WARLFTPA 380

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798438 158 ECFTICNQ-------ALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRSL 209
Cdd:PRK11561  381 AKFVICKRgipfvaeAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVL 439
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 22-210 3.97e-05

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: 43.86  E-value: 3.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  22 PGLSFGKKEKKVGWNSQPTRAVIFEDCAVP---VANRIG-------------TEGQGFLIAMKGLNGGRINVASCSLGAA 85
Cdd:cd01150   221 PGVTVGDIGPKMGLNGVDNGFLQFRNVRIPrenLLNRFGdvspdgtyvspfkDPNKRYGAMLGTRSGGRVGLIYDAAMSL 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  86 HASVVLTQEHLKVRKQFGAPLARS----------QYLQF-QLA-----DMATKLVASRL--MIRTAAVALQEEREDAVAL 147
Cdd:cd01150   301 KKAATIAIRYSAVRRQFGPKPSDPevqildyqlqQYRLFpQLAaayafHFAAKSLVEMYheIIKELLQGNSELLAELHAL 380

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958798438 148 CSMAKLFVTEECFTICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRSLL 210
Cdd:cd01150   381 SAGLKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLL 443
PLN02636 PLN02636
acyl-coenzyme A oxidase
 22-211 6.40e-04

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 40.23  E-value: 6.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  22 PGLSFGKKEKKVGWNSQPTRAVIFEDCAVP---VANRIG-------------TEGQGFLIAMKGLNGGRINVASCSLGAA 85
Cdd:PLN02636  266 PGVEIRDCGHKVGLNGVDNGALRFRSVRIPrdnLLNRFGdvsrdgkytsslpTINKRFAATLGELVGGRVGLAYGSVGVL 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798438  86 HASVVLTQEHLKVRKQFGAP------LARSQYLQFQLADM-----ATKLVASRLMIRTAAVALQEERE---DAVALCSMA 151
Cdd:PLN02636  346 KASNTIAIRYSLLRQQFGPPkqpeisILDYQSQQHKLMPMlastyAFHFATEYLVERYSEMKKTHDDQlvaDVHALSAGL 425

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958798438 152 KLFVTE---ECFTICNQALqmhGGYGYLkdyAVQQY--MR-DSRVHQILEGSNEVMRMLISRSLLQ 211
Cdd:PLN02636  426 KAYITSytaKALSTCREAC---GGHGYA---AVNRFgsLRnDHDIFQTFEGDNTVLLQQVAADLLK 485
 
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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