LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Domain |
| Description | Acetyl-coenzyme A carboxylase ( ) (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 firstcarboxylated by bicarbonate and ATP and the carboxyl group temporarily bound to biotin is subsequently transferred to an acceptor substrate such asacetyl-CoA. The carboxyltransferase domain performs the second part of the reaction [, ].The N- and C-terminal regions of the carboxyltransferase domain share similar polypeptide backbone folds, with a central β-β-alpha superhelix [ ]. 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. |
| Short Name | COA_CT_C |
