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"accession": "PS00061",
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"name": {
"name": "Short-chain dehydrogenases/reductases family signature",
"short": "ADH_SHORT"
},
"description": [
{
"text": "<p>The short-chain dehydrogenases/reductases family (SDR) [1] is a very large\nfamily of enzymes, most of which are known to be NAD- or NADP-dependent\noxidoreductases. As the first member of this family to be characterized was\nDrosophila alcohol dehydrogenase, this family used to be called [[cite:PUB00001371]][[cite:PUB00001399]][[cite:PUB00001408]]\n'insect-type', or 'short-chain' alcohol dehydrogenases. Most member of this\nfamily are proteins of about 250 to 300 amino acid residues. The proteins\ncurrently known to belong to this family are listed below.\n\n - Alcohol dehydrogenase (EC 1.1.1.1) from insects such as Drosophila.\n - Acetoin dehydrogenase (EC 1.1.1.5) from Klebsiella terrigena (gene budC).\n - D-beta-hydroxybutyrate dehydrogenase (BDH) (EC 1.1.1.30) from mammals.\n - Acetoacetyl-CoA reductase (EC 1.1.1.36) from various bacterial species\n (gene phbB or phaB).\n - Glucose 1-dehydrogenase (EC 1.1.1.47) from Bacillus.\n - 3-beta-hydroxysteroid dehydrogenase (EC 1.1.1.51) from Comomonas\n testosteroni.\n - 20-beta-hydroxysteroid dehydrogenase (EC 1.1.1.53) from Streptomyces\n hydrogenans.\n - Ribitol 2-dehydrogenase (EC 1.1.1.56) (RDH) from Klebsiella aerogenes.\n - Estradiol 17-beta-dehydrogenase (EC 1.1.1.62) from human.\n - Gluconate 5-dehydrogenase (EC 1.1.1.69) from Gluconobacter oxydans (gene\n gno).\n - 3-oxoacyl-[acyl-carrier protein] reductase (EC 1.1.1.100) from Escherichia\n coli (gene fabG) and from plants.\n - Retinol dehydrogenase (EC 1.1.1.105) from mammals.\n - 2-deoxy-d-gluconate 3-dehydrogenase (EC 1.1.1.125) from Escherichia coli\n and Erwinia chrysanthemi (gene kduD).\n - Sorbitol-6-phosphate 2-dehydrogenase (EC 1.1.1.140) from Escherichia coli\n (gene gutD) and from Klebsiella pneumoniae (gene sorD).\n - 15-hydroxyprostaglandin dehydrogenase (NAD+) (EC 1.1.1.141) from human.\n - Corticosteroid 11-beta-dehydrogenase (EC 1.1.1.146) (11-DH) from mammals.\n - 7-alpha-hydroxysteroid dehydrogenase (EC 1.1.1.159) from Escherichia coli\n (gene hdhA), Eubacterium strain VPI 12708 (gene baiA) and from Clostridium\n sordellii.\n - NADPH-dependent carbonyl reductase (EC 1.1.1.184) from mammals.\n - Tropinone reductase-I (EC 1.1.1.206) and -II (EC 1.1.1.236) from plants.\n - N-acylmannosamine 1-dehydrogenase (EC 1.1.1.233) from Flavobacterium strain\n 141-8.\n - D-arabinitol 2-dehydrogenase (ribulose forming) (EC 1.1.1.250) from fungi.\n - Tetrahydroxynaphthalene reductase (EC 1.1.1.252) from Magnaporthe grisea.\n - Pteridine reductase 1 (EC 1.5.1.33) (gene PTR1) from Leishmania.\n - 2,5-dichloro-2,5-cyclohexadiene-1,4-diol dehydrogenase (EC 1.1.-.-) from\n Pseudomonas paucimobilis.\n - Cis-1,2-dihydroxy-3,4-cyclohexadiene-1-carboxylate dehydrogenase (EC 1.3.1.\n -) from Acinetobacter calcoaceticus (gene benD) and Pseudomonas putida\n (gene xylL).\n - Biphenyl-2,3-dihydro-2,3-diol dehydrogenase (EC 1.3.1.-) (gene bphB) from\n various Pseudomonaceae.\n - Cis-toluene dihydrodiol dehydrogenase (EC 1.3.1.-) from Pseudomonas putida\n (gene todD).\n - Cis-benzene glycol dehydrogenase (EC 1.3.1.19) from Pseudomonas putida\n (gene bnzE).\n - 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (EC 1.3.1.28) from\n Escherichia coli (gene entA) and Bacillus subtilis (gene dhbA).\n - Dihydropteridine reductase (EC 1.5.1.34) (HDHPR) from mammals.\n - Lignin degradation enzyme ligD from Pseudomonas paucimobilis.\n - Agropine synthesis reductase from Agrobacterium plasmids (gene mas1).\n - Versicolorin reductase from Aspergillus parasiticus (gene VER1).\n - Putative keto-acyl reductases from Streptomyces polyketide biosynthesis\n operons.\n\n - A trifunctional hydratase-dehydrogenase-epimerase from the peroxisomal\n beta-oxidation system of Candida tropicalis. This protein contains two\n tandemly repeated 'short-chain dehydrogenase-type' domain in its N-terminal\n extremity.\n\n - Nodulation protein nodG from species of Azospirillum and Rhizobium which is\n probably involved in the modification of the nodulation Nod factor fatty\n acyl chain.\n - Nitrogen fixation protein fixR from Bradyrhizobium japonicum.\n - Bacillus subtilis protein dltE which is involved in the biosynthesis of D-\n alanyl-lipoteichoic acid.\n - Human follicular variant translocation protein 1 (FVT1).\n - Mouse adipocyte protein p27.\n - Mouse protein Ke 6.\n - Maize sex determination protein TASSELSEED 2.\n - Sarcophaga peregrina 25 Kd development specific protein.\n - Drosophila fat body protein P6.\n - A Listeria monocytogenes hypothetical protein encoded in the internalins\n gene region.\n - Escherichia coli hypothetical protein yciK.\n - Escherichia coli hypothetical protein ydfG.\n - Escherichia coli hypothetical protein yjgI.\n - Escherichia coli hypothetical protein yjgU.\n - Escherichia coli hypothetical protein yohF.\n - Bacillus subtilis hypothetical protein yoxD.\n - Bacillus subtilis hypothetical protein ywfD.\n - Bacillus subtilis hypothetical protein ywfH.\n - Yeast hypothetical protein YIL124w.\n - Yeast hypothetical protein YIR035c.\n - Yeast hypothetical protein YIR036c.\n - Yeast hypothetical protein YKL055c.\n - Fission yeast hypothetical protein SpAC23D3.11.\n\nWe use as a signature pattern for this family of proteins one of the best\nconserved regions which includes two perfectly conserved residues, a tyrosine\nand a lysine. The tyrosine residue participates in the catalytic mechanism.</p>",
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],
"wikipedia": null,
"literature": {
"PUB00001408": {
"PMID": 1740120,
"ISBN": null,
"volume": "204",
"issue": "1",
"year": 1992,
"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.",
"URL": null,
"raw_pages": "113-20",
"medline_journal": "Eur J Biochem",
"ISO_journal": "Eur. J. Biochem.",
"authors": [
"Neidle E",
"Hartnett C",
"Ornston LN",
"Bairoch A",
"Rekik M",
"Harayama S."
],
"DOI_URL": "http://dx.doi.org/10.1111/j.1432-1033.1992.tb16612.x"
},
"PUB00001371": {
"PMID": 2707261,
"ISBN": null,
"volume": "180",
"issue": "1",
"year": 1989,
"title": "The primary structure of alcohol dehydrogenase from Drosophila lebanonensis. Extensive variation within insect 'short-chain' alcohol dehydrogenase lacking zinc.",
"URL": null,
"raw_pages": "191-7",
"medline_journal": "Eur J Biochem",
"ISO_journal": "Eur. J. Biochem.",
"authors": [
"Villarroya A",
"Juan E",
"Egestad B",
"Jornvall H."
],
"DOI_URL": "http://dx.doi.org/10.1111/j.1432-1033.1989.tb14632.x"
},
"PUB00001399": {
"PMID": 1889416,
"ISBN": null,
"volume": "200",
"issue": "2",
"year": 1991,
"title": "Characteristics of short-chain alcohol dehydrogenases and related enzymes.",
"URL": null,
"raw_pages": "537-43",
"medline_journal": "Eur J Biochem",
"ISO_journal": "Eur. J. Biochem.",
"authors": [
"Persson B",
"Krook M",
"Jornvall H."
],
"DOI_URL": "http://dx.doi.org/10.1111/j.1432-1033.1991.tb16215.x"
}
},
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"matches": 621067,
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"proteins": 619284,
"proteomes": 21044,
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"structural_models": {
"alphafold": 470776,
"bfvd": 3
},
"structures": 818,
"taxa": 40848
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
