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Conserved domains on  [gi|2006156588|ref|WP_207240342|]
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acyl-CoA dehydrogenase family protein, partial [Pseudomonas sp. GW456-E6]

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 ...
10-43 4.77e-13

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 cd01160:

Pssm-ID: 447864 [Multi-domain]  Cd Length: 372  Bit Score: 60.21  E-value: 4.77e-13
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2006156588  10 EHELFRDSVRTFLEKEAVPFHGQWEKQGYIDRKL 43
Cdd:cd01160     2 EHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREV 35
 
Name Accession Description Interval E-value
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
10-43 4.77e-13

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: 60.21  E-value: 4.77e-13
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2006156588  10 EHELFRDSVRTFLEKEAVPFHGQWEKQGYIDRKL 43
Cdd:cd01160     2 EHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREV 35
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
8-43 8.38e-09

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: 46.30  E-value: 8.38e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2006156588   8 SSEHELFRDSVRTFLEKEAVPFHGQWEKQGYIDRKL 43
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPREL 36
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
7-43 4.82e-06

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: 40.21  E-value: 4.82e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2006156588   7 FSSEHELFRDSVRTFLEKEAVPFHGQWEKQGYIDRKL 43
Cdd:COG1960     5 LTEEQRALRDEVREFAEEEIAPEAREWDREGEFPREL 41
 
Name Accession Description Interval E-value
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
10-43 4.77e-13

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: 60.21  E-value: 4.77e-13
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2006156588  10 EHELFRDSVRTFLEKEAVPFHGQWEKQGYIDRKL 43
Cdd:cd01160     2 EHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREV 35
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
8-43 8.38e-09

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: 46.30  E-value: 8.38e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2006156588   8 SSEHELFRDSVRTFLEKEAVPFHGQWEKQGYIDRKL 43
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPREL 36
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
7-43 4.82e-06

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: 40.21  E-value: 4.82e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2006156588   7 FSSEHELFRDSVRTFLEKEAVPFHGQWEKQGYIDRKL 43
Cdd:COG1960     5 LTEEQRALRDEVREFAEEEIAPEAREWDREGEFPREL 41
 
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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