Acyl-CoA dehydrogenase, C-terminal domain (IPR013107)

Short name: Acyl-CoA_DH_C_dom

Overlapping homologous superfamilies

Domain relationships


Acyl Co-A dehydrogenases (EC: are enzymes that catalyse the first step in each cycle of beta-oxidation in mitochondion. Acyl-CoA dehydrogenases [PMID: 3326738, PMID: 2777793, PMID: 8034667] catalyze the alpha,beta-dehydrogenation of acyl-CoA thioesters to the corresponding trans 2,3-enoyl CoA-products with concommitant reduction of enzyme-bound FAD. Reoxidation of the flavin involves transfer of electrons to ETF (electron transfering flavoprotein). These enzymes are homodimers containing one molecule of FAD.

The monomeric enzyme is folded into three domains of approximately equal size. The N-terminal and the C-terminal are mainly alpha-helices packed together, and the middle domain consists of two orthogonal beta-sheets. The flavin ring is buried in the crevise between two alpha-helical domains and the beta-sheet of one subunit, and the adenosine pyrophosphate moiety is stretched into the subunit junction with one formed by two C-terminal domains [PMID: 8356049]. The C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.

This entry represents the Acyl-CoA dehydrogenase C-terminal domain. The domain also appears to be found in other enzymes, including pigment production hydroxylases.

Contributing signatures

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