ADH5

Chr 4q23

alcohol dehydrogenase 5 (class III), chi polypeptide

Aliases:: ADH-3, ADHX, GSNOR
MANE:: ENST00000296412.14

OMIM: 103710 ↗NCBI: 128 ↗Ensembl ↗

Annotations refreshed 9 hours ago.

Predicted protein structure

AlphaFold predicted structure

ADH5 · P11766

v62025-08-01

Predicted Aligned Error matrix for ADH5 — diagonal shows residue index, colour shows pairwise prediction confidence (lower is better) — Predicted Aligned Error

Mean pLDDT

98.1/ 100

Very high

374 residues

Confidence breakdown

Very high(≥ 90)99%
Confident(70–90)1%
Low(50–70)0%
Very low(< 50)0%

Open interactive 3D viewer

AlphaFold (Jumper et al., 2021) · CC BY 4.0

Clinical relevance (Genomics England PanelApp)

Moderate Evidence (Amber)

Rare anaemia
BIALLELIC, autosomal or pseudoautosomal

Disease associations (Open Targets)

AMED syndrome, digenic
0.63
Alzheimer disease
0.28
gout
0.24
autoimmune disorder of central nervous system
0.22
aplastic anemia
0.19
microcephaly
0.19
Intellectual disability
0.19
ischemic stroke
0.13
coronary artery disorder
0.12
asthma
0.11

Score is the Open Targets composite evidence score (0-1). Higher = stronger gene-disease association.

Protein function (UniProt)

Alcohol dehydrogenase class-3

Catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione (PubMed:8460164). Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate (PubMed:16081420). Class-III ADH is remarkably ineffective in oxidizing ethanol (PubMed:8460164). Required for clearance of cellular formaldehyde, a cytotoxic and carcinogenic metabolite that induces DNA damage (PubMed:33355142). Also acts as a S-nitroso-glutathione reductase by catalyzing the NADH-dependent reduction of S-nitrosoglutathione, thereby regulating protein S-nitrosylation (By similarity)