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 Q81GI3 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. | 
UniProtKB Entries (1)
| Q81GI3 | FABI_BACCR Bacillus cereus ATCC 14579 Enoyl-[acyl-carrier-protein] reductase [NADH] FabI | 
PDB Structure
| PDB | 5YCR | 
| External Links | |
| Method | X-RAY DIFFRACTION | 
| Organism | |
| Primary Citation | Structural insights into the dimer-tetramer transition of FabI from Bacillus anthracis Biochem. Biophys. Res. Commun. | 
