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biotin-independent malonate decarboxylase subunit gamma
This family consists of several bacterial malonate decarboxylase gamma subunit proteins. Malonate decarboxylase of Klebsiella pneumoniae consists of four different subunits and catalyses the conversion of malonate plus H+ to acetate and CO2. The catalysis proceeds via acetyl and malonyl thioester residues with the phosphribosyl-dephospho-CoA prosthetic group of the acyl carrier protein (ACP) subunit. MdcD and E together probably function as malonyl-S-ACP decarboxylase [1]. [1]. 9208947. Sequence of a gene cluster from Klebsiella pneumoniae encoding malonate decarboxylase and expression of the enzyme in Escherichia coli. Hoenke S, Schmid M, Dimroth P;. Eur J Biochem 1997;246:530-538. (from Pfam)
biotin-independent malonate decarboxylase subunit gamma is part of the enzyme that converts malonate to acetate, and is required for the transfer of the malonate carboxy group from the acyl-carrier protein (ACP) to the prosthetic group of the biotin carrier MADF; also required for the regeneration of ACP
Members of this protein family are the gamma subunit of malonate decarboxylase. Malonate decarboxylase may be a soluble enzyme, or linked to membrane subunits and active as a sodium pump. In the malonate decarboxylase complex, the beta subunit appears to act as a malonyl-CoA decarboxylase, while the gamma subunit appears either to mediate subunit interaction or to act as a co-decarboxylase with the beta subunit. The beta and gamma subunits exhibit some local sequence similarity.
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