PROSITE documentation PDOC00060
Short-chain dehydrogenases/reductases family signature


The short-chain dehydrogenases/reductases family (SDR) [1] 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 characterized was Drosophila alcohol dehydrogenase, this family used to be called [2,3,4] 'insect-type', or 'short-chain' alcohol dehydrogenases. Most member of this family are proteins of about 250 to 300 amino acid residues. The proteins currently known to belong to this family are listed below.

  • Alcohol dehydrogenase (EC from insects such as Drosophila.
  • Acetoin dehydrogenase (EC from Klebsiella terrigena (gene budC).
  • D-β-hydroxybutyrate dehydrogenase (BDH) (EC from mammals.
  • Acetoacetyl-CoA reductase (EC from various bacterial species (gene phbB or phaB).
  • Glucose 1-dehydrogenase (EC from Bacillus.
  • 3-β-hydroxysteroid dehydrogenase (EC from Comomonas testosteroni.
  • 20-β-hydroxysteroid dehydrogenase (EC from Streptomyces hydrogenans.
  • Ribitol 2-dehydrogenase (EC (RDH) from Klebsiella aerogenes.
  • Estradiol 17-β-dehydrogenase (EC from human.
  • Gluconate 5-dehydrogenase (EC from Gluconobacter oxydans (gene gno).
  • 3-oxoacyl-[acyl-carrier protein] reductase (EC from Escherichia coli (gene fabG) and from plants.
  • Retinol dehydrogenase (EC from mammals.
  • 2-deoxy-d-gluconate 3-dehydrogenase (EC from Escherichia coli and Erwinia chrysanthemi (gene kduD).
  • Sorbitol-6-phosphate 2-dehydrogenase (EC from Escherichia coli (gene gutD) and from Klebsiella pneumoniae (gene sorD).
  • 15-hydroxyprostaglandin dehydrogenase (NAD+) (EC from human.
  • Corticosteroid 11-β-dehydrogenase (EC (11-DH) from mammals.
  • 7-α-hydroxysteroid dehydrogenase (EC from Escherichia coli (gene hdhA), Eubacterium strain VPI 12708 (gene baiA) and from Clostridium sordellii.
  • NADPH-dependent carbonyl reductase (EC from mammals.
  • Tropinone reductase-I (EC and -II (EC from plants.
  • N-acylmannosamine 1-dehydrogenase (EC from Flavobacterium strain 141-8.
  • D-arabinitol 2-dehydrogenase (ribulose forming) (EC from fungi.
  • Tetrahydroxynaphthalene reductase (EC from Magnaporthe grisea.
  • Pteridine reductase 1 (EC (gene PTR1) from Leishmania.
  • 2,5-dichloro-2,5-cyclohexadiene-1,4-diol dehydrogenase (EC 1.1.-.-) from Pseudomonas paucimobilis.
  • Cis-1,2-dihydroxy-3,4-cyclohexadiene-1-carboxylate dehydrogenase (EC 1.3.1. -) from Acinetobacter calcoaceticus (gene benD) and Pseudomonas putida (gene xylL).
  • Biphenyl-2,3-dihydro-2,3-diol dehydrogenase (EC 1.3.1.-) (gene bphB) from various Pseudomonaceae.
  • Cis-toluene dihydrodiol dehydrogenase (EC 1.3.1.-) from Pseudomonas putida (gene todD).
  • Cis-benzene glycol dehydrogenase (EC from Pseudomonas putida (gene bnzE).
  • 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (EC from Escherichia coli (gene entA) and Bacillus subtilis (gene dhbA).
  • Dihydropteridine reductase (EC (HDHPR) from mammals.
  • Lignin degradation enzyme ligD from Pseudomonas paucimobilis.
  • Agropine synthesis reductase from Agrobacterium plasmids (gene mas1).
  • Versicolorin reductase from Aspergillus parasiticus (gene VER1).
  • Putative keto-acyl reductases from Streptomyces polyketide biosynthesis operons.
  • A trifunctional hydratase-dehydrogenase-epimerase from the peroxisomal β-oxidation system of Candida tropicalis. This protein contains two tandemly repeated 'short-chain dehydrogenase-type' domain in its N-terminal extremity.
  • Nodulation protein nodG from species of Azospirillum and Rhizobium which is probably involved in the modification of the nodulation Nod factor fatty acyl chain.
  • Nitrogen fixation protein fixR from Bradyrhizobium japonicum.
  • Bacillus subtilis protein dltE which is involved in the biosynthesis of D- alanyl-lipoteichoic acid.
  • Human follicular variant translocation protein 1 (FVT1).
  • Mouse adipocyte protein p27.
  • Mouse protein Ke 6.
  • Maize sex determination protein TASSELSEED 2.
  • Sarcophaga peregrina 25 Kd development specific protein.
  • Drosophila fat body protein P6.
  • A Listeria monocytogenes hypothetical protein encoded in the internalins gene region.
  • Escherichia coli hypothetical protein yciK.
  • Escherichia coli hypothetical protein ydfG.
  • Escherichia coli hypothetical protein yjgI.
  • Escherichia coli hypothetical protein yjgU.
  • Escherichia coli hypothetical protein yohF.
  • Bacillus subtilis hypothetical protein yoxD.
  • Bacillus subtilis hypothetical protein ywfD.
  • Bacillus subtilis hypothetical protein ywfH.
  • Yeast hypothetical protein YIL124w.
  • Yeast hypothetical protein YIR035c.
  • Yeast hypothetical protein YIR036c.
  • Yeast hypothetical protein YKL055c.
  • Fission yeast hypothetical protein SpAC23D3.11.

We use as a signature pattern for this family of proteins one of the best conserved regions which includes two perfectly conserved residues, a tyrosine and a lysine. The tyrosine residue participates in the catalytic mechanism.

Expert(s) to contact by email:

Joernvall H.
Persson B.

Last update:

April 2006 / Pattern revised.


Technical section

PROSITE method (with tools and information) covered by this documentation:

ADH_SHORT, PS00061; Short-chain dehydrogenases/reductases family signature  (PATTERN)


1AuthorsJoernvall H. Persson B. Krook M. Atrian S. Gonzalez-Duarte R. Jeffery J. Ghosh D.
SourceBiochemistry 34:6003-6013(1995).

2AuthorsVillarroya A. Juan E. Egestad B. Joernvall H.
TitleThe primary structure of alcohol dehydrogenase from Drosophila lebanonensis. Extensive variation within insect 'short-chain' alcohol dehydrogenase lacking zinc.
SourceEur. J. Biochem. 180:191-197(1989).
PubMed ID2707261

3AuthorsPersson B. Krook M. Jorenvall H.
TitleCharacteristics of short-chain alcohol dehydrogenases and related enzymes.
SourceEur. J. Biochem. 200:537-543(1991).
PubMed ID1889416

4AuthorsNeidle E.L. Hartnett C. Ornston L.N. Bairoch A. Rekik M. Harayama S.
Titlecis-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.
SourceEur. J. Biochem. 204:113-120(1992).
PubMed ID1740120

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