|PROSITE documentation PDOC00060
Short-chain dehydrogenases/reductases family signature
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 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 188.8.131.52) from insects such as Drosophila.
- Acetoin dehydrogenase (EC 184.108.40.206) from Klebsiella terrigena (gene budC).
- D-β-hydroxybutyrate dehydrogenase (BDH) (EC 220.127.116.11) from mammals.
- Acetoacetyl-CoA reductase (EC 18.104.22.168) from various bacterial species
(gene phbB or phaB).
- Glucose 1-dehydrogenase (EC 22.214.171.124) from Bacillus.
- 3-β-hydroxysteroid dehydrogenase (EC 126.96.36.199) from Comomonas
- 20-β-hydroxysteroid dehydrogenase (EC 188.8.131.52) from Streptomyces
- Ribitol 2-dehydrogenase (EC 184.108.40.206) (RDH) from Klebsiella aerogenes.
- Estradiol 17-β-dehydrogenase (EC 220.127.116.11) from human.
- Gluconate 5-dehydrogenase (EC 18.104.22.168) from Gluconobacter oxydans (gene
- 3-oxoacyl-[acyl-carrier protein] reductase (EC 22.214.171.124) from Escherichia
coli (gene fabG) and from plants.
- Retinol dehydrogenase (EC 126.96.36.199) from mammals.
- 2-deoxy-d-gluconate 3-dehydrogenase (EC 188.8.131.52) from Escherichia coli
and Erwinia chrysanthemi (gene kduD).
- Sorbitol-6-phosphate 2-dehydrogenase (EC 184.108.40.206) from Escherichia coli
(gene gutD) and from Klebsiella pneumoniae (gene sorD).
- 15-hydroxyprostaglandin dehydrogenase (NAD+) (EC 220.127.116.11) from human.
- Corticosteroid 11-β-dehydrogenase (EC 18.104.22.168) (11-DH) from mammals.
- 7-α-hydroxysteroid dehydrogenase (EC 22.214.171.124) from Escherichia coli
(gene hdhA), Eubacterium strain VPI 12708 (gene baiA) and from Clostridium
- NADPH-dependent carbonyl reductase (EC 126.96.36.199) from mammals.
- Tropinone reductase-I (EC 188.8.131.52) and -II (EC 184.108.40.206) from plants.
- N-acylmannosamine 1-dehydrogenase (EC 220.127.116.11) from Flavobacterium strain
- D-arabinitol 2-dehydrogenase (ribulose forming) (EC 18.104.22.168) from fungi.
- Tetrahydroxynaphthalene reductase (EC 22.214.171.124) from Magnaporthe grisea.
- Pteridine reductase 1 (EC 126.96.36.199) (gene PTR1) from Leishmania.
- 2,5-dichloro-2,5-cyclohexadiene-1,4-diol dehydrogenase (EC 1.1.-.-) from
- Cis-1,2-dihydroxy-3,4-cyclohexadiene-1-carboxylate dehydrogenase (EC 1.3.1.
-) from Acinetobacter calcoaceticus (gene benD) and Pseudomonas putida
- Biphenyl-2,3-dihydro-2,3-diol dehydrogenase (EC 1.3.1.-) (gene bphB) from
- Cis-toluene dihydrodiol dehydrogenase (EC 1.3.1.-) from Pseudomonas putida
- Cis-benzene glycol dehydrogenase (EC 188.8.131.52) from Pseudomonas putida
- 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (EC 184.108.40.206) from
Escherichia coli (gene entA) and Bacillus subtilis (gene dhbA).
- Dihydropteridine reductase (EC 220.127.116.11) (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
- 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
- Nodulation protein nodG from species of Azospirillum and Rhizobium which is
probably involved in the modification of the nodulation Nod factor fatty
- Nitrogen fixation protein fixR from Bradyrhizobium japonicum.
- Bacillus subtilis protein dltE which is involved in the biosynthesis of D-
- 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
- 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.
April 2006 / Pattern revised.
PROSITE method (with tools and information) covered by this documentation:
|ADH_SHORT, PS00061; Short-chain dehydrogenases/reductases family signature (PATTERN)
Y is an active site residue
|Sequences known to belong to this class detected by the pattern:
||ALL, except for 18 sequences
|Other sequence(s) detected in Swiss-Prot:
|Matching PDB structures:
1A27 1A4U 1AE1 1AHH ... [ALL]
||Joernvall H., Persson B., Krook M., Atrian S., Gonzalez-Duarte R., Jeffery J., Ghosh D.
||Villarroya A., Juan E., Egestad B., Joernvall H.
||The primary structure of alcohol dehydrogenase from Drosophila lebanonensis. Extensive variation within insect 'short-chain' alcohol dehydrogenase lacking zinc.
||Eur. J. Biochem. 180:191-197(1989).
||Persson B., Krook M., Jorenvall H.
||Characteristics of short-chain alcohol dehydrogenases and related enzymes.
||Eur. J. Biochem. 200:537-543(1991).
||Neidle E.L., Hartnett C., Ornston L.N., Bairoch A., Rekik M., Harayama S.
||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.
||Eur. J. Biochem. 204:113-120(1992).
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