CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.20 | Alpha-Beta Barrel |
|
3.20.20 | TIM Barrel |
|
3.20.20.100 | NADP-dependent oxidoreductase domain |
Domain Context
CATH Clusters
| Superfamily | NADP-dependent oxidoreductase domain |
| Functional Family | Aldo-keto reductase family 1 member A1 |
Enzyme Information
| 1.1.1.19 |
Glucuronate reductase.
based on mapping to UniProt Q9JII6
L-gulonate + NADP(+) = D-glucuronate + NADPH.
-!- Also reduces D-galacturonate. -!- May be identical with EC 1.1.1.2.
|
| 1.1.1.33 |
Mevaldate reductase (NADPH).
based on mapping to UniProt Q9JII6
(R)-mevalonate + NADP(+) = mevaldate + NADPH.
-!- May be identical with EC 1.1.1.2.
|
| 1.1.1.2 |
Alcohol dehydrogenase (NADP(+)).
based on mapping to UniProt Q9JII6
An alcohol + NADP(+) = an aldehyde + NADPH.
-!- Some members of this group oxidize only primary alcohols; others act also on secondary alcohols. -!- May be identical with EC 1.1.1.19, EC 1.1.1.33 and EC 1.1.1.55. -!- Re-specific with respect to NADPH.
|
| 1.1.1.372 |
D/L-glyceraldehyde reductase.
based on mapping to UniProt Q9JII6
(1) Glycerol + NADP(+) = L-glyceraldehyde + NADPH. (2) Glycerol + NADP(+) = D-glyceraldehyde + NADPH.
-!- The enzyme takes part in a D-galacturonate degradation pathway in the fungi Aspergillus niger and Trichoderma reesei (Hypocrea jecorina). -!- It has equal activity with D- and L-glyceraldehyde, and can also reduce glyoxal and methylglyoxal. -!- The reaction is only observed in the direction of glyceraldehyde reduction.
|
| 1.1.1.20 |
Glucuronolactone reductase.
based on mapping to UniProt Q9JII6
L-gulono-1,4-lactone + NADP(+) = D-glucurono-3,6-lactone + NADPH.
|
| 1.1.1.54 |
Allyl-alcohol dehydrogenase.
based on mapping to UniProt Q9JII6
Allyl alcohol + NADP(+) = acrolein + NADPH.
-!- Also acts on saturated primary alcohols.
|
UniProtKB Entries (1)
| Q9JII6 |
AK1A1_MOUSE
Mus musculus
Aldo-keto reductase family 1 member A1
|
PDB Structure
| PDB | 4GAC |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
High-resolution structure of AKR1a4 in the apo form and its interaction with ligands.
Acta Crystallogr.,Sect.F
|
