PROSITE documentation PDOC00060

Short-chain dehydrogenases/reductases family signature

Description

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 1.1.1.1) from insects such as Drosophila.
  • Acetoin dehydrogenase (EC 1.1.1.5) from Klebsiella terrigena (gene budC).
  • D-β-hydroxybutyrate dehydrogenase (BDH) (EC 1.1.1.30) from mammals.
  • Acetoacetyl-CoA reductase (EC 1.1.1.36) from various bacterial species (gene phbB or phaB).
  • Glucose 1-dehydrogenase (EC 1.1.1.47) from Bacillus.
  • 3-β-hydroxysteroid dehydrogenase (EC 1.1.1.51) from Comomonas testosteroni.
  • 20-β-hydroxysteroid dehydrogenase (EC 1.1.1.53) from Streptomyces hydrogenans.
  • Ribitol 2-dehydrogenase (EC 1.1.1.56) (RDH) from Klebsiella aerogenes.
  • Estradiol 17-β-dehydrogenase (EC 1.1.1.62) from human.
  • Gluconate 5-dehydrogenase (EC 1.1.1.69) from Gluconobacter oxydans (gene gno).
  • 3-oxoacyl-[acyl-carrier protein] reductase (EC 1.1.1.100) from Escherichia coli (gene fabG) and from plants.
  • Retinol dehydrogenase (EC 1.1.1.105) from mammals.
  • 2-deoxy-d-gluconate 3-dehydrogenase (EC 1.1.1.125) from Escherichia coli and Erwinia chrysanthemi (gene kduD).
  • Sorbitol-6-phosphate 2-dehydrogenase (EC 1.1.1.140) from Escherichia coli (gene gutD) and from Klebsiella pneumoniae (gene sorD).
  • 15-hydroxyprostaglandin dehydrogenase (NAD+) (EC 1.1.1.141) from human.
  • Corticosteroid 11-β-dehydrogenase (EC 1.1.1.146) (11-DH) from mammals.
  • 7-α-hydroxysteroid dehydrogenase (EC 1.1.1.159) from Escherichia coli (gene hdhA), Eubacterium strain VPI 12708 (gene baiA) and from Clostridium sordellii.
  • NADPH-dependent carbonyl reductase (EC 1.1.1.184) from mammals.
  • Tropinone reductase-I (EC 1.1.1.206) and -II (EC 1.1.1.236) from plants.
  • N-acylmannosamine 1-dehydrogenase (EC 1.1.1.233) from Flavobacterium strain 141-8.
  • D-arabinitol 2-dehydrogenase (ribulose forming) (EC 1.1.1.250) from fungi.
  • Tetrahydroxynaphthalene reductase (EC 1.1.1.252) from Magnaporthe grisea.
  • Pteridine reductase 1 (EC 1.5.1.33) (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 1.3.1.19) from Pseudomonas putida (gene bnzE).
  • 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (EC 1.3.1.28) from Escherichia coli (gene entA) and Bacillus subtilis (gene dhbA).
  • Dihydropteridine reductase (EC 1.5.1.34) (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)
Consensus pattern: [LIVSPADNK]-x(9)-{P}-x(2)-Y-[PSTAGNCV]-[STAGNQCIVM]-[STAGC]-K-{PC}-[SAGFYR]-[LIVMSTAGD]-x-{K}-[LIVMFYW]-{D}-x-{YR}-[LIVMFYWGAPTHQ]-[GSACQRHM]
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: 35.
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00061
• Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00061
• Scan Swiss-Prot/TrEMBL entries against PS00061
• view ligand binding statistics
Matching PDB structures: 1A27 1A4U 1AE1 1AHH ... [ALL]

References

1 Authors Joernvall H., Persson B., Krook M., Atrian S., Gonzalez-Duarte R., Jeffery J., Ghosh D.
Source Biochemistry 34:6003-6013(1995).
2 Authors Villarroya A., Juan E., Egestad B., Joernvall H.
Title The primary structure of alcohol dehydrogenase from Drosophila lebanonensis. Extensive variation within insect 'short-chain' alcohol dehydrogenase lacking zinc.
Source Eur. J. Biochem. 180:191-197(1989).
PubMed ID 2707261
3 Authors Persson B., Krook M., Jorenvall H.
Title Characteristics of short-chain alcohol dehydrogenases and related enzymes.
Source Eur. J. Biochem. 200:537-543(1991).
PubMed ID 1889416
4 Authors Neidle E.L., Hartnett C., Ornston L.N., Bairoch A., Rekik M., Harayama S.
Title 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.
Source Eur. J. Biochem. 204:113-120(1992).
PubMed ID 1740120

Copyright

PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)