Acetyl-coenzyme A carboxyltransferase, C-terminal (IPR011763)

Short name: COA_CT_C

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.

The acetyl-coenzyme A carboxyltransferase domain is also found in the following enzymes:

  • Methylcrotonyl-CoA carboxylase beta chain, mitochondrial precursor.
  • Glutaconyl-CoA decarboxylase alpha subunit.
  • Propionyl-CoA carboxylase beta chain (PCCase).

This domain is the C subdomain and recognizes also the alpha-subunit of bacterial ACC.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0016874 ligase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

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