Acetyl-coenzyme A carboxyltransferase, N-terminal (IPR011762)

Short name: COA_CT_N

Overlapping homologous superfamilies

Domain relationships



Acetyl-coenzyme A carboxylase (EC: (ACC), a member of the biotin-dependent enzyme family, catalyses the formation of malonyl-coenzyme A (CoA) and regulates fatty acid biosynthesis and oxidation. Biotin-dependent carboxylase enzymes perform a two step reaction: enzyme-bound biotin is first carboxylated by bicarbonate and ATP and the carboxyl group temporarily bound to biotin is subsequently transferred to an acceptor substrate such as acetyl-CoA. The carboxyltransferase domain performs the second part of the reaction [PMID: 2673009, PMID: 11851389].

The N- and C-terminal regions of the carboxyltransferase domain share similar polypeptide backbone folds, with a central beta-beta-alpha superhelix [PMID: 12663926]. The CoA molecule is mostly associated with the N subdomain. In bacterial acetyl coenzyme A carboxylase the N and C subdomains are encoded by two different polypeptides.

This entry represents the N-terminal subdomain and contains the bacterial ACC beta-subunit.

Contributing signatures

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