CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.720 | NAD(P)-binding Rossmann-like Domain |
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.
Plos One
|