CATH Classification

Domain Context

CATH Clusters

Superfamily 3.40.47.10
Functional Family 3-oxoacyl-[acyl-carrier-protein] synthase 2

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.

UniProtKB Entries (1)

P9WQD9
FAB1_MYCTU
Mycobacterium tuberculosis H37Rv
3-oxoacyl-[acyl-carrier-protein] synthase 1

PDB Structure

PDB 5LD8
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Identification of KasA as the cellular target of an anti-tubercular scaffold.
Abrahams, K.A., Chung, C.W., Ghidelli-Disse, S., Rullas, J., Rebollo-Lopez, M.J., Gurcha, S.S., Cox, J.A., Mendoza, A., Jimenez-Navarro, E., Martinez-Martinez, M.S., Neu, M., Shillings, A., Homes, P., Argyrou, A., Casanueva, R., Loman, N.J., Moynihan, P.J., Lelievre, J., Selenski, C., Axtman, M., Kremer, L., Bantscheff, M., Angulo-Barturen, I., Izquierdo, M.C., Cammack, N.C., Drewes, G., Ballell, L., Barros, D., Besra, G.S., Bates, R.H.
Nat Commun