CATH Classification

Domain Context

CATH Clusters

Superfamily Malonyl-CoA ACP transacylase, ACP-binding
Functional Family Malonyl-CoA-acyl carrier protein transacylase, mitochondrial

Enzyme Information
[Acyl-carrier-protein] S-malonyltransferase.
based on mapping to UniProt Q8IVS2
Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier- protein].
-!- Essential, along with EC, for the initiation of fatty-acid biosynthesis in bacteria. -!- 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 is the preferred substrate. -!- This enzyme also forms part of the multienzyme complexes EC and EC -!- 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.

UniProtKB Entries (1)

Homo sapiens
Malonyl-CoA-acyl carrier protein transacylase, mitochondrial

PDB Structure

External Links
Primary Citation
Structural Basis for Different Specificities of Acyltransferases Associated with the Human Cytosolic and Mitochondrial Fatty Acid Synthases.
Bunkoczi, G., Misquitta, S., Wu, X., Lee, W.H., Rojkova, A., Kochan, G., Kavanagh, K.L., Oppermann, U., Smith, S.