| Type: | Domain | Name: | 3-oxoacid CoA-transferase, subunit A |
| Description: | CoA-transferases catalyse the reversible transfer of of coenzyme A from CoA-thioesters to free acids, and can be divided into three families []. Family I includes transferases for 3-oxoacids (, ), short-chain fatty acids (, ) and glutaconate (). 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 [].This entry represents the CoA-binding A subunit of family I CoA-transferases. This domain forms a three-layer alpha-beta-alpha sandwich where the central layer is an all parallel beta-sheet, against which helices pack from both sides [, ]. The active site is thought to be located at the interface of the A and B subunits and formed by loops from both subunits. | Short Name: | 3-oxoacid_CoA-transf_A |
