This enzyme, along with EC 22.214.171.124, [acyl-carrier-protein] S-acetyltransferase, is essential for the initiation of fatty-acid biosynthesis in bacteria. This enzyme also provides the malonyl groups for polyketide biosynthesis . The product of the reaction, malonyl-ACP, is an elongation substrate in fatty-acid biosynthesis. In Mycobacterium tuberculosis, holo-ACP (the product of EC 126.96.36.199, holo-[acyl-carrier-protein] synthase) is the preferred substrate . This enzyme also forms part of the multienzyme complexes EC 188.8.131.52 (biotin-independent malonate decarboxylase) and EC 184.108.40.206 (biotin-dependent malonate decarboxylase). Malonylation of ACP is immediately followed by decarboxylation within the malonate-decarboxylase complex to yield acetyl-ACP, the catalytically active species of the decarboxylase . In the enzyme from Klebsiella pneumoniae, methylmalonyl-CoA can also act as a substrate but acetyl-CoA cannot  whereas the enzyme from Pseudomonas putida can use both as substrates . The ACP subunit found in fatty-acid biosynthesis contains a pantetheine-4'-phosphate prosthetic group; that from malonate decarboxylase also contains pantetheine-4'-phosphate but in the form of a 2′-(5-triphosphoribosyl)-3′-dephospho-CoA prosthetic group.
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DNA and amino acid sequence determination and analysis, phylogenetic tree, expression as GFP-fusion protein containing the mitochondrial targeting sequence in mitochondria of HeLa cells, expression of truncated enzyme forms lacking the first 21 or 59 amino acid residues, respectively, in Escherichia coli strain BL21(DE3) as soluble enzymes, or in Spodoptera frugiperda Sf9 cells via baculovirus infection system