InterPro : IPR002427

Name  Alcohol dehydrogenase-related Short Name  ADH-rel
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 members of this family are proteins of about 250 to 300 amino acid residues. Most dehydrogenases possess at least two 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 [].Insect ADH is very different from yeast and mammalian ADHs. The enzyme from Drosophila lebanonensis(Fruit fly) has been characterised by protein analysis and wasfound to have a 254-residue protein chain with an acetyl-blocked N-terminalMet []. Comparisons with the enzyme from other species reveals that theyhave diverged considerably. The structural variation within Drosophila is about as large as that for mammalian zinc-containing alcohol dehydrogenase.The crystal structure of the apo form of D. lebanonensis ADH has been solved to1.9A resolution []. Three structural features characterise the active site architecture: (i) a deep cavity, covered by aflexible 33-residue loop and an 11-residue C-terminal tail of the neighbouring subunit, whose hydrophobic surface is likely to increase thespecificity of the enzyme for secondary aliphatic alcohols; (ii) the Ser-Tyr-Lys residues of the catalytic triad are known to be involved inenzymatic catalysis; and (iii) three well-ordered water molecules in hydrogen bonding distance of side-chains of the catalytic triad may be significantfor the proton release steps in the catalysis.A number of proteins within the SDR family share a strong phylogeneticrelationship with insect ADH. Amongst these are Drosophila ADH-relatedprotein (duplicate of Adh or Adh-dup) []; drosophila fat body protein; and development-specific 25Kd protein from Sarcophaga peregrina(Flesh fly).

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

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
IPR002424 Alcohol dehydrogenase, insect-type ADH_insect Family

6 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
Benach J The refined crystal structure of Drosophila lebanonensis alcohol dehydrogenase at 1.9 A resolution. 1998 J Mol Biol 282 383-99

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)