CATH Classification

Domain Context

CATH Clusters

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

Enzyme Information

2.3.1.39
[Acyl-carrier-protein] S-malonyltransferase.
based on mapping to UniProt P0AAI9
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)

P0AAI9
FABD_ECOLI
Escherichia coli K-12
Malonyl CoA-acyl carrier protein transacylase

PDB Structure

PDB 1MLA
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
The Escherichia coli malonyl-CoA:acyl carrier protein transacylase at 1.5-A resolution. Crystal structure of a fatty acid synthase component.
Serre, L., Verbree, E.C., Dauter, Z., Stuitje, A.R., Derewenda, Z.S.
J.Biol.Chem.
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