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 O85140
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)

O85140
FABD_SALTY
Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Malonyl CoA-acyl carrier protein transacylase

PDB Structure

PDB 3H0P
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
2.0 Angstrom Crystal Structure of an Acyl Carrier Protein S-malonyltransferase from Salmonella typhimurium.
Minasov, G., Wawrzak, Z., Skarina, T., Onopriyenko, O., Peterson, S.N., Savchenko, A., Anderson, W.F., Center for Structural Genomics of Infectious Diseases (CSGID)
TO BE PUBLISHED