Domain

Acyl-CoA dehydrogenase/oxidase C-terminal (IPR009075)

Short name: AcylCo_DH/oxidase_C

Domain relationships

Description

Acyl-CoA dehydrogenases (EC:1.3.99.3) are a family of flavoproteins that catalyse the alpha,beta-dehydrogenation of acyl-CoA thioesters to the corresponding trans 2,3-enoyl CoA-products with the concomitant reduction of enzyme-bound FAD. Different family members share a high sequence identity, catalytic mechanisms, and structural properties, but differ in the position of their catalytic bases and in their substrate binding specificity. Butyryl-CoA dehydrogenase [PMID: 11812788] prefers short chain substrates, medium chain- and long-chain acyl-CoA dehydrogenases prefer medium and long chain substrates, respectively, and Isovaleryl-CoA dehydrogenase [PMID: 9214289] prefers branched-chain substrates.

The monomeric enzyme is folded into three domains of approximately equal size, where the N-terminal domain is all-alpha, the middle domain is an open [PMID: 14728676, PMID: 14728675] barrel, and the C-terminal domain is a four-helical bundle. This entry represents the C-terminal domain found in medium chain acyl-CoA dehydrogenases, as well as in the related peroxisomal acyl-CoA oxidase-II enzymes, where this domain occurs as a tandem duplication. Acyl-CoA oxidase (ACO; EC:1.3.3.6) catalyzes the first and rate-determining step of the peroxisomal beta-oxidation of fatty acids [PMID: 11872165].

GO terms

Biological Process

GO:0055114 oxidation-reduction process

Molecular Function

GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
Pfam
SUPERFAMILY