CATH Classification

Domain Context

CATH Clusters

Superfamily Malonyl-CoA ACP transacylase, ACP-binding
Functional Family Fatty acid synthase subunit beta

Enzyme Information

2.3.1.39
[Acyl-carrier-protein] S-malonyltransferase.
based on mapping to UniProt Q3JF88
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)

Q3JF88
Q3JF88_BURP1
Burkholderia pseudomallei 1710b
Malonyl CoA-acyl carrier protein transacylase

PDB Structure

PDB 3G87
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Crystal structure of malonyl CoA-acyl carrier protein transacylase from Burkholderia pseudomallei using dried seaweed as nucleant or protease
Edwards, T.E., Staker, B.L., Christensen, J., Seattle Structural Genomics Center for Infectious Disease
To be Published