InterPro : IPR002198

Name  Short-chain dehydrogenase/reductase SDR Short Name  DH_sc/Rdtase_SDR
Type  Family Description  The short-chain dehydrogenases/reductases family (SDR) []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 [, , ]'insect-type', or 'short-chain' alcohol dehydrogenases. Most member of this family are proteins of about 250 to 300 amino acid residues. Most dehydrogenases possess at least 2 domains [], 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 [].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



3 Child Features

Id Name Short Name Type
IPR002424 Alcohol dehydrogenase, insect-type ADH_insect Family
IPR027052 Dehydrogenase/reductase SDR member 2 DHRS2 Family
IPR027533 Very-long-chain 3-oxoacyl-CoA reductase, fungal 3_ketoreductase_fungal Family

2 Contains

Id Name Short Name Type
IPR016040 NAD(P)-binding domain NAD(P)-bd_dom Domain
IPR020904 Short-chain dehydrogenase/reductase, conserved site Sc_DH/Rdtase_CS Conserved_site

0 Found In

1 Parent Features

Id Name Short Name Type
IPR002347 Glucose/ribitol dehydrogenase Glc/ribitol_DH Family

5 Publications

First Author Title Year Journal Volume Pages
Jörnvall H Short-chain dehydrogenases/reductases (SDR). 1995 Biochemistry 34 6003-13
Villarroya A The primary structure of alcohol dehydrogenase from Drosophila lebanonensis. Extensive variation within insect 'short-chain' alcohol dehydrogenase lacking zinc. 1989 Eur J Biochem 180 191-7
Persson B Characteristics of short-chain alcohol dehydrogenases and related enzymes. 1991 Eur J Biochem 200 537-43
Neidle E cis-diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and the Acinetobacter calcoaceticus chromosomal benD gene are members of the short-chain alcohol dehydrogenase superfamily. 1992 Eur J Biochem 204 113-20
Benyajati C Alcohol dehydrogenase gene of Drosophila melanogaster: relationship of intervening sequences to functional domains in the protein. 1981 Proc Natl Acad Sci U S A 78 2717-21

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)