CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.40 | 3-Layer(aba) Sandwich | |
3.40.47 | Peroxisomal Thiolase; Chain A, domain 1 | |
3.40.47.10 | Thiolase/Chalcone synthase |
Domain Context
CATH Clusters
Superfamily | 3.40.47.10 |
Functional Family | 3-oxoacyl-[acyl-carrier-protein] synthase 1 |
Enzyme Information
2.3.1.41 |
Beta-ketoacyl-[acyl-carrier-protein] synthase I.
based on mapping to UniProt P9WQD9
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)
P9WQD9 |
FAB1_MYCTU
Mycobacterium tuberculosis H37Rv
3-oxoacyl-[acyl-carrier-protein] synthase 1
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PDB Structure
PDB | 2WGF |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Crystal Structures of Mycobacterium Tuberculosis Kasa Show Mode of Action within Cell Wall Biosynthesis and its Inhibition by Thiolactomycin
Structure
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