The domain within your query sequence starts at position 203 and ends at position 334; the E-value for the ADH_zinc_N domain shown below is 2.4e-20.

GVGSAIVMGCKASGASRIIGVDINEEKFPRARALGVTDCLNPNKLEKPVQEVVMEMTGVG
VDFAFEAIGLVDTMVAAWNSCNNSYGVCLIAGLAPSDAQLSLEAPKILSGKTLKGVCLGD
YKTRDCIPQIVT

ADH_zinc_N

 ADH_zinc_N
PFAM accession number:PF00107
Interpro abstract (IPR013149):

Alcohol dehydrogenase ( EC 1.1.1.1 ) (ADH) catalyzes the reversible oxidation of alcohols to their corresponding acetaldehyde or ketone with the concomitant reduction of NAD: alcohol + NAD = aldehyde or ketone + NADH Currently three structurally and catalytically different types of alcohol dehydrogenases are known:

  1. Zinc-containing 'long-chain' alcohol dehydrogenases.
  2. Insect-type, or 'short-chain' alcohol dehydrogenases.
  3. Iron-containing alcohol dehydrogenases.
Zinc-containing ADH's [ (PUBMED:3622514) (PUBMED:1593644) ] are dimeric or tetrameric enzymes that bind two atoms of zinc per subunit. One of the zinc atom is essential for catalytic activity while the other is not. Both zinc atoms are coordinated by either cysteine or histidine residues; the catalytic zinc is coordinated by two cysteines and one histidine. Zinc-containing ADH's are found in bacteria, mammals, plants, and in fungi. In many species there is more than one isozyme (for example, humans have at least six isozymes, yeast have three, etc.). A number of other zinc-dependent dehydrogenases are closely related to zinc ADH [ (PUBMED:8504864) ] and are included in this family.

In addition, this family includes NADP-dependent quinone oxidoreductase ( EC 1.6.5.5 ), 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 [ (PUBMED: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) [ (PUBMED:12962626) (PUBMED:12627956) (PUBMED:7602590) ].

GO process:oxidation-reduction process (GO:0055114)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry ADH_zinc_N