Protein Domain : Coenzyme A transferase family I IPR004165

Type	Family
Description	Coenzyme A (CoA) transferases belong to an evolutionary conserved [ , ] family of enzymes catalyzing the reversible transfer of CoA from one carboxylic acid to another. They have been identified in many prokaryotes and in mammalian tissues. The bacterial enzymes are heterodimer of two subunits (A and B) of about 25 Kd each while eukaryotic SCOT consist of a single chain which is colinear with the two bacterial subunits.CoA-transferases are found in organisms from all kingdoms of life. They catalyse reversible transfer reactions of coenzyme A groups from CoA-thioesters to free acids. There are at least three families of CoA-transferases, which differ in sequence and reaction mechanism:Family I consists of CoA-transferases for 3-oxoacids ( , ), short-chain fatty acids ( , ) and glutaconate ( ). Most use succinyl-CoA or acetyl-CoA as CoA donors. Family II consists of the homodimeric alpha-subunits of citrate lyase and citramalate lyase ( , ). These enzymes catalyse the transfer of acyl carrier protein (ACP) with a covalently bound CoA derivative, but can accept free CoA thioesters as well. Family III consists of formyl-CoA:oxalate CoA-transferase [ ], succinyl-CoA:(R)-benzylsuccinate CoA-transferase [], (E)-cinnamoyl-CoA:(R)-phenyllactate CoA-transferase [], succinyl-CoA:mesaconate CoA-transferase [] and butyrobetainyl-CoA:(R)-carnitine CoA-transferase []. These CoA-transferases occur in prokaryotes and eukaryotes, and catalyse CoA-transfer reactions in a highly substrate- and stereo-specific manner [].This family consists of 3-oxoacid CoA-transferases and related CoA-transferases from family I.
Short Name	CoA_trans_fam_I