Conserved Site

Short-chain dehydrogenase/reductase, conserved site (IPR020904)

Short name: Sc_DH/Rdtase_CS


The short-chain dehydrogenases/reductases family (SDR) [PMID: 7742302, PMID: 25526675] is a very large family of enzymes, most of which are known to be NAD- or NADP-dependent oxidoreductases. As the first member of this family to be characterised was Drosophila alcohol dehydrogenase, this family used to be called [PMID: 2707261, PMID: 1889416, PMID: 1740120] 'insect-type', or 'short-chain' alcohol dehydrogenases. Most members of this family are proteins of about 250 to 300 amino acid residues. Most dehydrogenases possess at least 2 domains [PMID: 6789320], the first binding the coenzyme, often NAD, and the second binding the substrate. This latter domain determines the substrate specificity and contains amino acids involved in catalysis. Little sequence similarity has been found in the coenzyme binding domain although there is a large degree of structural similarity, and it has therefore been suggested that the structure of dehydrogenases has arisen through gene fusion of a common ancestral coenzyme nucleotide sequence with various substrate specific domains [PMID: 6789320].

This entry contains a signature pattern for this family of proteins which covers one of the best conserved regions. It includes two perfectly conserved residues, a tyrosine and a lysine. The tyrosine residue participates in the catalytic mechanism.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0016491 oxidoreductase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns