3-oxoacid CoA-transferase, subunit B (IPR012791)

Short name: 3-oxoacid_CoA-transf_B

Overlapping homologous superfamilies

Domain relationships



CoA-transferases catalyse the reversible transfer of of coenzyme A from CoA-thioesters to free acids, and can be divided into three families [PMID: 11749953]. Family I includes transferases for 3-oxoacids (EC:, EC:, short-chain fatty acids (EC:, EC: and glutaconate (EC: Most of the family I enzymes use acetyl-CoA or succinyl-CoA as CoA donors, and are composed of two separate polypeptides, subunits A and B, which generally aggregate as heterodimers or heterotetramers. The eukaryotic enzymes, however, are generally composed of a single two-domain polypetide representing a fusion of the A and B subunits. The transfer of CoA from one substrate to another occurs via a ping pong mechanism which involves the formation of thioester bond between CoA and a conserved glutamate residue at the active site of the enzyme [PMID: 10409616].

This entry represents the B subunit of family I CoA-transferases, which contains the conserved active-site glutamate residue. This domain forms a three-layer alpha-beta-alpha sandwich where the central layer is a mixed beta-sheet, against which helices pack from both sides [PMID: 12463743, PMID: 15388917]. The active site is thought to be located at the interface of the A and B subunits and formed by loops from both subunits.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0008410 CoA-transferase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

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