CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.30 | 2-Layer Sandwich | |
3.30.70 | Alpha-Beta Plaits | |
3.30.70.250 | Malonyl-CoA ACP transacylase, ACP-binding |
Domain Context
CATH Clusters
Superfamily | Malonyl-CoA ACP transacylase, ACP-binding |
Functional Family | Malonyl CoA-ACP 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.
J.Mol.Biol.
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