Pathways & interactions
Alcohol dehydrogenase, C-terminal (IPR013149)
Short name: ADH_C
Alcohol dehydrogenase (EC:126.96.36.199) (ADH) catalyzes the reversible oxidation of
alcohols to their corresponding acetaldehyde or ketone with the concomitant reduction of NAD:
- Zinc-containing 'long-chain' alcohol dehydrogenases.
- Insect-type, or 'short-chain' alcohol dehydrogenases.
- Iron-containing alcohol dehydrogenases.
- Sorbitol dehydrogenase (EC:188.8.131.52)
- L-threonine 3-dehydrogenase (EC:184.108.40.206)
- Glutathione-dependent formaldehyde dehydrogenase (EC:220.127.116.114)
- Mannitol dehydrogenase (EC:18.104.22.168)
In addition, this family includes NADP-dependent quinone oxidoreductase (EC:22.214.171.124), an enzyme found in bacteria (gene qor), in yeast and in mammals where, in some species such as rodents, it has been recruited as an eye lens protein and is known as zeta-crystallin [PMID: 8486156]. The sequence of quinone oxidoreductase is distantly related to that other zinc-containing alcohol dehydrogenases and it lacks the zinc-ligand residues. The torpedo fish and mammalian synaptic vesicle membrane protein vat-1 is related to qor.
This entry represents the cofactor-binding domain of these enzymes, which is normally found towards the C terminus. Structural studies indicate that it forms a classical Rossman fold that reversibly binds NAD(H) [PMID: 12962626, PMID: 12627956, PMID: 7602590].
- PF00107 (ADH_zinc_N)