CATH Classification

Domain Context

CATH Clusters

Superfamily 3.40.47.10
Functional Family

Enzyme Information

2.3.1.180
Beta-ketoacyl-[acyl-carrier-protein] synthase III.
based on mapping to UniProt Q9KLJ3
Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier- protein] + CoA + CO(2).
-!- Involved in the dissociated (or type II) fatty-acid biosynthesis system that occurs in plants and bacteria. -!- In contrast to EC 2.3.1.41 and EC 2.3.1.179, this enzyme specifically uses CoA thioesters rather than acyl-ACP as the primer. -!- In addition to the above reaction, the enzyme can also catalyze the reaction of EC 2.3.1.38, but to a much lesser extent. -!- Responsible for initiating both straight- and branched-chain fatty- acid biosynthesis, with the substrate specificity in an organism reflecting the fatty-acid composition found in that organism. -!- For example, Streptococcus pneumoniae, a Gram-positive bacterium, is able to use both straight- and branched-chain (C4--C6) acyl-CoA primers whereas Escherichia coli, a Gram-negative organism, uses primarily short straight-chain acyl CoAs, with a preference for acetyl-CoA.

UniProtKB Entries (1)

Q9KLJ3
FABH2_VIBCH
Vibrio cholerae O1 biovar El Tor str. N16961
3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 2

PDB Structure

PDB 4X9O
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural and enzymatic studies of beta-ketoacyl-(acyl carrier protein) synthase III (FabH) from Vibrio cholerae
Hou, J., Zheng, H., Cooper, D.R., Chruszcz, M., Chordia, M.D., Grabowski, M., Minor, W., Center for Structural Genomics of Infectious Diseases (CSGID)
to be published