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Conserved domains on  [gi|530397993|ref|XP_005271562|]
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isobutyryl-CoA dehydrogenase, mitochondrial isoform X5 [Homo sapiens]

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 ...
 41-236 3.91e-148

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: 418.39  E-value: 3.91e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993  41 LNEEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTT 120
Cdd:cd01162    1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993 121 AYISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESDI 200
Cdd:cd01162   81 AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDV 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 530397993 201 YVVMCRTGGPGPKGISCIVVEKGTPGLSFGKKEKKL 236
Cdd:cd01162  161 YVVMARTGGEGPKGISCFVVEKGTPGLSFGANEKKM 196
 
Name Accession Description Interval E-value
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 41-236 3.91e-148

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: 418.39  E-value: 3.91e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993  41 LNEEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTT 120
Cdd:cd01162    1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993 121 AYISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESDI 200
Cdd:cd01162   81 AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDV 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 530397993 201 YVVMCRTGGPGPKGISCIVVEKGTPGLSFGKKEKKL 236
Cdd:cd01162  161 YVVMARTGGEGPKGISCFVVEKGTPGLSFGANEKKM 196
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 41-236 4.91e-76

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: 235.12  E-value: 4.91e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993  41 LNEEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTT 120
Cdd:COG1960    5 LTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASLA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993 121 AYISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESDI 200
Cdd:COG1960   85 LPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVADV 164

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 530397993 201 YVVMCRTGG-PGPKGISCIVVEKGTPGLSFGKKEKKL 236
Cdd:COG1960  165 ILVLARTDPaAGHRGISLFLVPKDTPGVTVGRIEDKM 201
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 42-153 1.92e-41

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: 137.59  E-value: 1.92e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993   42 NEEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTTA 121
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 530397993  122 YISIHN-MCAWMIDSFGNEEQRHKFCPPLCTME 153
Cdd:pfam02771  81 ALSVHSsLGAPPILRFGTEEQKERYLPKLASGE 113
PLN02526 PLN02526
acyl-coenzyme A oxidase
 41-236 4.45e-27

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 107.63  E-value: 4.45e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993  41 LNEEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQtDVGGSGLSRLDTSVIFEALATGCTSTT 120
Cdd:PLN02526  29 LTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTIK-GYGCPGLSITASAIATAEVARVDASCS 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993 121 AYISIHN-MCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESD 199
Cdd:PLN02526 108 TFILVHSsLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFAD 187

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 530397993 200 IYVVMCRTggPGPKGISCIVVEKGTPGLSFGKKEKKL 236
Cdd:PLN02526 188 VLVIFARN--TTTNQINGFIVKKGAPGLKATKIENKI 222
 
Name Accession Description Interval E-value
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 41-236 3.91e-148

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: 418.39  E-value: 3.91e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993  41 LNEEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTT 120
Cdd:cd01162    1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993 121 AYISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESDI 200
Cdd:cd01162   81 AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDV 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 530397993 201 YVVMCRTGGPGPKGISCIVVEKGTPGLSFGKKEKKL 236
Cdd:cd01162  161 YVVMARTGGEGPKGISCFVVEKGTPGLSFGANEKKM 196
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 43-236 2.89e-76

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: 235.24  E-value: 2.89e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993  43 EEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTTAY 122
Cdd:cd01158    1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993 123 ISIHN-MCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESDIY 201
Cdd:cd01158   81 VSVHNsLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 530397993 202 VVMCRTGGP-GPKGISCIVVEKGTPGLSFGKKEKKL 236
Cdd:cd01158  161 IVFAVTDPSkGYRGITAFIVERDTPGLSVGKKEDKL 196
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 41-236 4.91e-76

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: 235.12  E-value: 4.91e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993  41 LNEEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTT 120
Cdd:COG1960    5 LTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASLA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993 121 AYISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESDI 200
Cdd:COG1960   85 LPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVADV 164

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 530397993 201 YVVMCRTGG-PGPKGISCIVVEKGTPGLSFGKKEKKL 236
Cdd:COG1960  165 ILVLARTDPaAGHRGISLFLVPKDTPGVTVGRIEDKM 201
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 40-236 2.02e-52

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: 174.14  E-value: 2.02e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993  40 GLNEEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTST 119
Cdd:cd01156    1 GLDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993 120 TAYISIH-NMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGES 198
Cdd:cd01156   81 ALSYGAHsNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDA 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 530397993 199 DIYVVMCRTGG-PGPKGISCIVVEKGTPGLSFGKKEKKL 236
Cdd:cd01156  161 DTLVVYAKTDPsAGAHGITAFIVEKGMPGFSRAQKLDKL 199
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 41-236 4.48e-47

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: 160.44  E-value: 4.48e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993  41 LNEEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTT 120
Cdd:cd01157    1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993 121 AYISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESDI 200
Cdd:cd01157   81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 530397993 201 YVVMCRTG----GPGPKGISCIVVEKGTPGLSFGKKEKKL 236
Cdd:cd01157  161 YFLLARSDpdpkCPASKAFTGFIVEADTPGIQPGRKELNM 200
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 43-236 4.93e-47

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: 159.97  E-value: 4.93e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993  43 EEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALA-TGCTSTTa 121
Cdd:cd01160    1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELArAGGSGPG- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993 122 yISIHN-MCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESDI 200
Cdd:cd01160   80 -LSLHTdIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADV 158

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 530397993 201 YVVMCRTGGP--GPKGISCIVVEKGTPGLSFGKKEKKL 236
Cdd:cd01160  159 VIVVARTGGEarGAGGISLFLVERGTPGFSRGRKLKKM 196
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 43-236 1.13e-46

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: 157.83  E-value: 1.13e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993  43 EEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLgfggvyiqtdvggsglsrldtsvifealatgctsttay 122
Cdd:cd00567    1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLL-------------------------------------- 42

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993 123 isihnMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESDIYV 202
Cdd:cd00567   43 -----LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFI 117

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 530397993 203 VMCRTGGPGP--KGISCIVVEKGTPGLSFGKKEKKL 236
Cdd:cd00567  118 VLARTDEEGPghRGISAFLVPADTPGVTVGRIWDKM 153
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 42-153 1.92e-41

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: 137.59  E-value: 1.92e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993   42 NEEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTTA 121
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 530397993  122 YISIHN-MCAWMIDSFGNEEQRHKFCPPLCTME 153
Cdd:pfam02771  81 ALSVHSsLGAPPILRFGTEEQKERYLPKLASGE 113
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 40-236 5.44e-35

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: 129.13  E-value: 5.44e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993  40 GLNEEQKEFQKVAFD----FAAREMAPnmAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFE--ALA 113
Cdd:cd01161   22 VLTEEQTEELNMLVGpvekFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEivGMD 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993 114 TGCTSTtayISIHNMCAWM-IDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQ--GDHYILNGSKA 190
Cdd:cd01161  100 LGFSVT---LGAHQSIGFKgILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSedGKHYVLNGSKI 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530397993 191 FISGAGESDIYVVMCRT-----GGPGPKGISCIVVEKGTPGLSFGKKEKKL 236
Cdd:cd01161  177 WITNGGIADIFTVFAKTevkdaTGSVKDKITAFIVERSFGGVTNGPPEKKM 227
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 41-236 4.02e-34

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: 126.32  E-value: 4.02e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993  41 LNEEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQtDVGGSGLSRLDTSVI---FEALATGCT 117
Cdd:cd01151   13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIK-GYGCAGLSSVAYGLIareVERVDSGYR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993 118 STtayISIH-NMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAG 196
Cdd:cd01151   92 SF---MSVQsSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSP 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 530397993 197 ESDIYVVMCRTGGPGpkGISCIVVEKGTPGLSFGKKEKKL 236
Cdd:cd01151  169 IADVFVVWARNDETG--KIRGFILERGMKGLSAPKIQGKF 206
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 157-236 1.43e-27

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: 101.20  E-value: 1.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993  157 SYCLTEPGSGSDAASLLTSA-KKQGDHYILNGSKAFISGAGESDIYVVMCRTGGPGPK-GISCIVVEKGTPGLSFGKKEK 234
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHgGISLFLVPKDAPGVSVRRIET 80


                  ..
gi 530397993  235 KL 236
Cdd:pfam02770  81 KL 82
PLN02526 PLN02526
acyl-coenzyme A oxidase
 41-236 4.45e-27

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 107.63  E-value: 4.45e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993  41 LNEEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQtDVGGSGLSRLDTSVIFEALATGCTSTT 120
Cdd:PLN02526  29 LTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTIK-GYGCPGLSITASAIATAEVARVDASCS 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993 121 AYISIHN-MCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESD 199
Cdd:PLN02526 108 TFILVHSsLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFAD 187

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 530397993 200 IYVVMCRTggPGPKGISCIVVEKGTPGLSFGKKEKKL 236
Cdd:PLN02526 188 VLVIFARN--TTTNQINGFIVKKGAPGLKATKIENKI 222
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 79-228 2.17e-25

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: 102.43  E-value: 2.17e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993  79 RKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASY 158
Cdd:cd01152   42 RALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQ 121

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530397993 159 CLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESDIYVVMCRTGGPGPK--GISCIVVEKGTPGLS 228
Cdd:cd01152  122 GFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDPEAPKhrGISILLVDMDSPGVT 193
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 37-236 3.38e-24

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 99.57  E-value: 3.38e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993  37 PSMGLNEEQKEFQKVAFDFAAREMAPNMAEWDQKELFP--VDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALAT 114
Cdd:PLN02519  22 SSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPkdVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISR 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993 115 GCTSTTAYISIH-NMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFIS 193
Cdd:PLN02519 102 ASGSVGLSYGAHsNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCT 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 530397993 194 GAGESDIYVVMCRTG-GPGPKGISCIVVEKGTPGLSFGKKEKKL 236
Cdd:PLN02519 182 NGPVAQTLVVYAKTDvAAGSKGITAFIIEKGMPGFSTAQKLDKL 225
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 44-235 3.25e-22

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 94.23  E-value: 3.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993  44 EQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATG----CTst 119
Cdd:PTZ00461  40 EHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYdpgfCL-- 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993 120 tAYISiHNMCawMIDSFGNE---EQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGD-HYILNGSKAFISGA 195
Cdd:PTZ00461 118 -AYLA-HSML--FVNNFYYSaspAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNG 193

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 530397993 196 GESDIYVVMCRTGGPgpkgISCIVVEKGTPGLSFGKKEKK 235
Cdd:PTZ00461 194 TVADVFLIYAKVDGK----ITAFVVERGTKGFTQGPKIDK 229
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 54-222 2.20e-19

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: 86.29  E-value: 2.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993  54 DFAAREMAPNMAEWDQKEL--------FP---VDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTsTTAY 122
Cdd:cd01153    7 RLAENVLAPLNADGDREGPvfddgrvvVPppfKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDA-PLMY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993 123 ISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGD-HYILNGSKAFISgAGESD-- 199
Cdd:cd01153   86 ASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFIS-AGEHDms 164

                        170       180
                 ....*....|....*....|....*...
gi 530397993 200 ---IYVVMCRTGGPGP--KGISCIVVEK 222
Cdd:cd01153  165 eniVHLVLARSEGAPPgvKGLSLFLVPK 192
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 56-228 3.15e-19

Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACAD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. ACAD's are generally homotetramers and have an active site glutamate at a conserved position.


Pssm-ID: 173844 [Multi-domain]  Cd Length: 394  Bit Score: 85.52  E-value: 3.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993  56 AAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEAL--------ATGCTSTtayiSIHN 127
Cdd:cd01155   25 FLEYYAEGGDRWWTPPPIIEKLKAKAKAEGLWNLFLPEVSGLSGLTNLEYAYLAEETgrsffapeVFNCQAP----DTGN 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993 128 McaWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPG-SGSDAASLLTSAKKQGDHYILNGSKAFISGAGESD--IYVVM 204
Cdd:cd01155  101 M--EVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGRKWWSSGAGDPRckIAIVM 178

                        170       180
                 ....*....|....*....|....*..
gi 530397993 205 CRTGGPGP---KGISCIVVEKGTPGLS 228
Cdd:cd01155  179 GRTDPDGAprhRQQSMILVPMDTPGVT 205
PRK12341 PRK12341
acyl-CoA dehydrogenase;
64-234 1.67e-17

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 80.54  E-value: 1.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993  64 MAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTstTAYISIHNMCAWMIDSFGNEEQRH 143
Cdd:PRK12341  29 FRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKCGA--PAFLITNGQCIHSMRRFGSAEQLR 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993 144 KfcpplcTMEKFA-----SYCL--TEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESDIYVVMCR-TGGPGP-KG 214
Cdd:PRK12341 107 K------TAESTLetgdpAYALalTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAKEYPYMLVLARdPQPKDPkKA 180

                        170       180
                 ....*....|....*....|
gi 530397993 215 ISCIVVEKGTPGLSFGKKEK 234
Cdd:PRK12341 181 FTLWWVDSSKPGIKINPLHK 200
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 41-234 3.88e-15

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 73.71  E-value: 3.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993  41 LNEEQKEFQKVAFDFAAREMAPN-MAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALatGCTST 119
Cdd:PRK03354   5 LNDEQELFVAGIRELMASENWEAyFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMEL--GRLGA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993 120 TAYISIHNMCAW-MIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGES 198
Cdd:PRK03354  83 PTYVLYQLPGGFnTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYT 162

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 530397993 199 DIYVVMCRTGGPGPKGI-SCIVVEKGTPGLSFGKKEK 234
Cdd:PRK03354 163 PYIVVMARDGASPDKPVyTEWFVDMSKPGIKVTKLEK 199
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 85-225 3.04e-13

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 68.74  E-value: 3.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993  85 GFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTTAY--ISIHNMCAWMidSFGNEEQRHKFCPPLCTMEKFASYCLTE 162
Cdd:PTZ00456 112 GWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYpgLSIGAANTLM--AWGSEEQKEQYLTKLVSGEWSGTMCLTE 189

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530397993 163 PGSGSDAASLLTSAKKQGD-HYILNGSKAFISgAGESD-----IYVVMCRTGG--PGPKGISCIVVEKGTP 225
Cdd:PTZ00456 190 PQCGTDLGQVKTKAEPSADgSYKITGTKIFIS-AGDHDlteniVHIVLARLPNslPTTKGLSLFLVPRHVV 259
PLN02876 PLN02876
acyl-CoA dehydrogenase
 136-228 1.06e-09

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 58.27  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993 136 FGNEEQRHKFCPPLCTMEKFASYCLTEPG-SGSDAASLLTSAKKQGDHYILNGSKAFISGAGES--DIYVVMCRT--GGP 210
Cdd:PLN02876 532 YGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPrcRVLIVMGKTdfNAP 611

                         90
                 ....*....|....*...
gi 530397993 211 GPKGISCIVVEKGTPGLS 228
Cdd:PLN02876 612 KHKQQSMILVDIQTPGVQ 629
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 123-224 2.10e-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: 53.91  E-value: 2.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993 123 ISIHNMCAWMIDSFGNEEQRHkFCPPLCTMEK----FASYCLTEPGSGSDAASLLTSAKKQ-GDHYILNGSKAFISGAgE 197
Cdd:cd01154  113 LTMTDAAVYALRKYGPEELKQ-YLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERSgGGVYRLNGHKWFASAP-L 190

                         90       100       110
                 ....*....|....*....|....*....|...
gi 530397993 198 SDIYVVMCRTGG--PGPKGISCIVV----EKGT 224
Cdd:cd01154  191 ADAALVLARPEGapAGARGLSLFLVprllEDGT 223
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 52-229 1.58e-06

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: 48.47  E-value: 1.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993  52 AFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIHNMCAW 131
Cdd:cd01163    2 RARPLAARIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGFVE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993 132 MIDSFGNEEQRhKFCPPLCTMEKFASYCLTEPGSgSDAASLLTSAKKQGDHYILNGSKAFISGAGESDiYVVMCRTGGPG 211
Cdd:cd01163   82 ALLLAGPEQFR-KRWFGRVLNGWIFGNAVSERGS-VRPGTFLTATVRDGGGYVLNGKKFYSTGALFSD-WVTVSALDEEG 158

                        170
                 ....*....|....*...
gi 530397993 212 PKGIscIVVEKGTPGLSF 229
Cdd:cd01163  159 KLVF--AAVPTDRPGITV 174
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
 116-185 1.42e-04

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 42.52  E-value: 1.42e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530397993 116 CTSTTAYISIH-NMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSA--KKQGDHYIL 185
Cdd:PTZ00460  88 CPQGTFISTVHfAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTAtyDKQTNEFVI 160
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
 56-220 3.21e-04

Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, which is active against Gram-positive bacteria. Polyketides are secondary metabolites, which have important biological functions such as antitumor, immunosupressive or antibiotic activities. NcnH is a hydroxylase involved in the biosynthesis of naphthocyclinone and possibly other polyketides.


Pssm-ID: 173848 [Multi-domain]  Cd Length: 370  Bit Score: 41.18  E-value: 3.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993  56 AAREMAP----NMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIHNMCAW 131
Cdd:cd01159    2 RAEDLAPlireRAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIVATHSR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993 132 MIDSFGNEEQRHKFcpplctmekfasycltepgsGSDAASLLTS-------AKKQGDHYILNGSKAFISGAGESDIYVVM 204
Cdd:cd01159   82 MLAAFPPEAQEEVW--------------------GDGPDTLLAGsyapggrAERVDGGYRVSGTWPFASGCDHADWILVG 141

                        170
                 ....*....|....*.
gi 530397993 205 CRTGGPGPKGISCIVV 220
Cdd:cd01159  142 AIVEDDDGGPLPRAFV 157
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 76-171 5.05e-03

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 38.01  E-value: 5.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993  76 DVMRKAaqlGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIHNMC--AWMIDSFGNEEQRHKFCPPLCTME 153
Cdd:PRK13026 115 DYLKKE---GFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPNSLgpGELLTHYGTQEQKDYWLPRLADGT 191

                         90
                 ....*....|....*...
gi 530397993 154 KFASYCLTEPGSGSDAAS 171
Cdd:PRK13026 192 EIPCFALTGPEAGSDAGA 209
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
 88-228 7.05e-03

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 37.17  E-value: 7.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993  88 GVYIQTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIH-NMCAWMIDSFGNEEQRHKFcppLCTME--KFASYCLTEPG 164
Cdd:PTZ00457  67 GARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHsGFCTYLLSTVGSKELKGKY---LTAMSdgTIMMGWATEEG 143

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530397993 165 SGSDAASLLTSAKKQGD-HYILNGSKAFISGAGESDiYVVMCRT-----GGPGPKGI---SCIVVEKGTPGLS 228
Cdd:PTZ00457 144 CGSDISMNTTKASLTDDgSYVLTGQKRCEFAASATH-FLVLAKTltqtaAEEGATEVsrnSFFICAKDAKGVS 215
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 103-203 9.25e-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: 36.92  E-value: 9.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397993 103 LDTSVIFEALATGCTSTTAYISIH-NMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAK--KQ 179
Cdd:cd01150   82 EKMLALTNSLGGYDLSLGAKLGLHlGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATydPL 161

                         90       100
                 ....*....|....*....|....*....
gi 530397993 180 GDHYILN-----GSKAFISGAGESDIYVV 203
Cdd:cd01150  162 TQEFVINtpdftATKWWPGNLGKTATHAV 190
 
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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