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 | 1,5-anhydro-D-fructose reductase |
Enzyme Information
| 1.1.1.292 |
1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming).
based on mapping to UniProt Q92KZ3
1,5-anhydro-D-mannitol + NADP(+) = 1,5-anhydro-D-fructose + NADPH.
-!- Present in some but not all Rhizobium species. -!- Differs from hepatic 1,5-anhydro-D-fructose reductase, which yields 1,5-anhydro-D-glucitol as the product (see EC 1.1.1.263). -!- In Sinorhizobium morelense, the product of the reaction, 1,5-anhydro- D-mannitol, can be further metabolized to D-mannose. -!- Also reduces 1,5-anhydro-D-erythro-hexo-2,3-diulose and 2-ketoaldoses (called osones), such as D-glucosone (D-arabino-hexos-2-ulose) and 6-deoxy-D-glucosone. -!- Does not reduce common aldoses and ketoses, or non-sugar aldehydes and ketones.
|
| 1.1.1.- |
With NAD(+) or NADP(+) as acceptor.
based on mapping to UniProt Q92KZ3
|
UniProtKB Entries (1)
| Q92KZ3 |
AFR_RHIME
Sinorhizobium meliloti 1021
1,5-anhydro-D-fructose reductase
|
PDB Structure
| PDB | 4KOA |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The structure of substrate-free 1,5-anhydro-D-fructose reductase from Sinorhizobium meliloti 1021 reveals an open enzyme conformation.
Acta Crystallogr.,Sect.F
|
