CATH Classification

Domain Context

CATH Clusters

Superfamily NAD(P)-binding Rossmann-like Domain
Functional Family Photoreceptor dehydrogenase, isoform C

Enzyme Information

1.1.1.105
All-trans-retinol dehydrogenase (NAD(+)).
based on mapping to UniProt Q9VV42
All-trans-retinol-[cellular-retinol-binding-protein] + NAD(+) = all- trans-retinal-[cellular-retinol-binding-protein] + NADH.
-!- The enzyme recognizes all-trans-retinol and all-trans-retinal as substrates and exhibits a strong preference for NAD(+)/NADH as cofactors. -!- Recognizes the substrate both in free form and when bound to cellular-retinol-binding-protein (CRBP1), but has higher affinity for the bound form. -!- No activity with 11-cis-retinol or 11-cis-retinal (cf. EC 1.1.1.315). -!- Also active with 3-alpha-hydroxysteroids.
1.1.1.1
Alcohol dehydrogenase.
based on mapping to UniProt Q9VV42
(1) An alcohol + NAD(+) = an aldehyde or ketone + NADH. (2) A secondary alcohol + NAD(+) = a ketone + NADH.
-!- Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. -!- The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.

UniProtKB Entries (1)

Q9VV42
Q9VV42_DROME
Drosophila melanogaster
HL08057p

PDB Structure

PDB 5ILG
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural Insights into the Drosophila melanogaster Retinol Dehydrogenase, a Member of the Short-Chain Dehydrogenase/Reductase Family.
Hofmann, L., Tsybovsky, Y., Alexander, N.S., Babino, D., Leung, N.Y., Montell, C., Banerjee, S., von Lintig, J., Palczewski, K.
Biochemistry