CATH Classification

Domain Context

CATH Clusters

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

Enzyme Information
[Acyl-carrier-protein] S-malonyltransferase.
based on mapping to UniProt Q99UN8
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)

Staphylococcus aureus subsp. aureus Mu50
Malonyl CoA-acyl carrier protein transacylase

PDB Structure

External Links
Primary Citation
New design platform for malonyl-CoA-acyl carrier protein transacylase
Hong, S.K., Kim, K.H., Park, J.K., Jeong, K.-W., Kim, Y.M., Kim, E.E.
Febs Lett.