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 | Polyketide synthase type I |
Enzyme Information
2.3.1.41 |
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 2.3.1.179 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.
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UniProtKB Entries (1)
O53579 |
O53579_MYCTO
Mycobacterium tuberculosis CDC1551
Polyketide synthase
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PDB Structure
PDB | 3TZW |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Biochemical and structural study of the atypical acyltransferase domain from the mycobacterial polyketide synthase pks13
J.Biol.Chem.
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