CATH Domain 3h4gA00

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

1.1.1.54	Allyl-alcohol dehydrogenase. based on mapping to UniProt P50578 Allyl alcohol + NADP(+) = acrolein + NADPH. -!- Also acts on saturated primary alcohols.
1.1.1.33	Mevaldate reductase (NADPH). based on mapping to UniProt P50578 (R)-mevalonate + NADP(+) = mevaldate + NADPH. -!- May be identical with EC 1.1.1.2.
1.1.1.19	Glucuronate reductase. based on mapping to UniProt P50578 L-gulonate + NADP(+) = D-glucuronate + NADPH. -!- Also reduces D-galacturonate. -!- May be identical with EC 1.1.1.2.
1.1.1.2	Alcohol dehydrogenase (NADP(+)). based on mapping to UniProt P50578 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.
1.1.1.20	Glucuronolactone reductase. based on mapping to UniProt P50578 L-gulono-1,4-lactone + NADP(+) = D-glucurono-3,6-lactone + NADPH.
1.1.1.372	D/L-glyceraldehyde reductase. based on mapping to UniProt P50578 (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.

UniProtKB Entries (1)

AK1A1_PIG

Sus scrofa

Aldo-keto reductase family 1 member A1

PDB Structure

PDB	3H4G
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Structure of aldehyde reductase holoenzyme in complex with the potent aldose reductase inhibitor fidarestat: implications for inhibitor binding and selectivity El-Kabbani, O., Carbone, V., Darmanin, C., Oka, M., Mitschler, A., Podjarny, A., Schulze-Briese, C., Chung, R.P. J.Med.Chem.