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Conserved domains on  [gi|1972243728|ref|NP_001379683|]
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Acyl-CoA dehydrogenase/oxidase N-terminal domain-containing protein [Caenorhabditis elegans]

Protein Classification

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 ...
38-90 2.92e-07

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 cd01158:

Pssm-ID: 447864 [Multi-domain]  Cd Length: 373  Bit Score: 49.19  E-value: 2.92e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1972243728  38 ENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKL 90
Cdd:cd01158     1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEY 53
 
Name Accession Description Interval E-value
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
38-90 2.92e-07

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: 49.19  E-value: 2.92e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1972243728  38 ENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKL 90
Cdd:cd01158     1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEY 53
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
37-84 1.93e-06

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: 44.76  E-value: 1.93e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1972243728  37 NENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGL 84
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGI 48
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
35-90 2.31e-05

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: 43.68  E-value: 2.31e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1972243728  35 HLNENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKL 90
Cdd:COG1960     4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEY 59
 
Name Accession Description Interval E-value
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
38-90 2.92e-07

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: 49.19  E-value: 2.92e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1972243728  38 ENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKL 90
Cdd:cd01158     1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEY 53
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
37-84 1.93e-06

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: 44.76  E-value: 1.93e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1972243728  37 NENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGL 84
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGI 48
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
35-90 2.31e-05

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: 43.68  E-value: 2.31e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1972243728  35 HLNENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKL 90
Cdd:COG1960     4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEY 59
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
35-88 2.49e-04

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: 40.47  E-value: 2.49e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1972243728  35 HLNENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDP 88
Cdd:cd01156     1 GLDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPE 54
 
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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