CATH Classification

Domain Context

CATH Clusters

Superfamily NAD(P)-binding Rossmann-like Domain
Functional Family Enoyl-[acyl-carrier-protein] reductase [NADH]

Enzyme Information

1.3.1.9
Enoyl-[acyl-carrier-protein] reductase (NADH).
based on mapping to UniProt Q2P9J6
An acyl-[acyl-carrier protein] + NAD(+) = a trans-2,3-dehydroacyl-[acyl- carrier protein] + NADH.
-!- The enzyme catalyzes an essential step in fatty acid biosynthesis, the reduction of the 2,3-double bond in enoyl-acyl-[acyl-carrier- protein] derivatives of the elongating fatty acid moiety. -!- The enzyme from the bacterium Escherichia coli accepts substrates with carbon chain length from 4 to 18. -!- The FAS-I enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12 to 24 carbons.
1.3.1.44
Trans-2-enoyl-CoA reductase (NAD(+)).
based on mapping to UniProt Q2P9J6
Acyl-CoA + NAD(+) = trans-didehydroacyl-CoA + NADH.
-!- The enzyme from Euglena gracilis acts on crotonoyl-CoA and, more slowly, on trans-hex-2-enoyl-CoA and trans-oct-2-enoyl-CoA.

UniProtKB Entries (1)

Q2P9J6
FABV_XANOM
Xanthomonas oryzae pv. oryzae MAFF 311018
Enoyl-[acyl-carrier-protein] reductase [NADH]

PDB Structure

PDB 3S8M
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Determination of the Crystal Structure and Active Residues of FabV, the Enoyl-ACP Reductase from Xanthomonas oryzae.
Li, H., Zhang, X., Bi, L., He, J., Jiang, T.
Plos One
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