CATH Classification

Domain Context

CATH Clusters

Superfamily Malonyl-Coenzyme A Acyl Carrier Protein, domain 2
Functional Family Malonyl CoA-acyl carrier protein transacylase

Enzyme Information

2.3.1.39
[Acyl-carrier-protein] S-malonyltransferase.
based on mapping to UniProt P9WNG5
Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier- protein].
-!- Essential, along with EC 2.3.1.38, 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 2.7.8.7) is the preferred substrate. -!- This enzyme also forms part of the multienzyme complexes EC 4.1.1.88 and EC 4.1.1.89. -!- 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)

P9WNG5
FABD_MYCTU
Mycobacterium tuberculosis H37Rv
Malonyl CoA-acyl carrier protein transacylase

PDB Structure

PDB 2QC3
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
The Crystal Structure of MCAT from Mycobacterium tuberculosis Reveals Three New Catalytic Models.
Li, Z., Huang, Y., Ge, J., Fan, H., Zhou, X., Li, S., Bartlam, M., Wang, H., Rao, Z.
J.Mol.Biol.