CATH Classification

Domain Context

CATH Clusters

Superfamily Malonyl-CoA ACP transacylase, ACP-binding
Functional Family Polyketide synthase type I

Enzyme Information
Beta-ketoacyl-[acyl-carrier-protein] synthase I.
based on mapping to UniProt O53579
Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl- [acyl-carrier-protein] + CO(2) + [acyl-carrier-protein].
-!- Responsible for the chain-elongation step of dissociated (type II) fatty-acid biosynthesis, i.e. the addition of two C atoms to the fatty-acid chain. -!- Escherichia coli mutants that lack this enzyme are deficient in unsaturated fatty acids. -!- Can use fatty acyl thioesters of ACP (C(2) to C(16)) as substrates, as well as fatty acyl thioesters of Co-A (C(4) to C(16)). -!- The substrate specificity is very similar to that of EC with the exception that the latter enzyme is far more active with palmitoleoyl-ACP (C(16)-Delta(9)) as substrate, allowing the organism to regulate its fatty-acid composition with changes in temperature.

UniProtKB Entries (1)

Mycobacterium tuberculosis CDC1551
Polyketide synthase

PDB Structure

External Links
Primary Citation
Biochemical and structural study of the atypical acyltransferase domain from the mycobacterial polyketide synthase pks13
Bergeret, F., Gavalda, S., Chalut, C., Malaga, W., Quemard, A., Pedelacq, J.D., Daffe, M., Guilhot, C., Mourey, L., Bon, C.