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InterPro: IPR002085 Alcohol dehydrogenase superfamily, zinc-containing
Protein matches
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UniProtKB Matches: 19974 proteins |
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Accession
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IPR002085 ADH_SF_Zn |
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Type
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Family |
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Signatures
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InterPro Relationships
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Children
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IPR004627 L-threonine 3-dehydrogenase
IPR005903 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide a dehydrogenase
IPR010085 Crotonyl-CoA reductase
IPR014182 Alcohol dehydrogenase, zinc-binding type 1
IPR014183 Alcohol dehydrogenase class III/S-(hydroxymethyl)glutathione dehydrogenase
IPR014184 Formaldehyde dehydrogenase, glutathione-independent
IPR014187 Alcohol dehydrogenase, zinc-binding type 2
IPR014188 Quinone oxidoreductase putative, YhdH/YhfP
IPR014189 Quinone oxidoreductase putative, PIG3
IPR014190 Leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase
IPR017614 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase
IPR017743 Alcohol dehydrogenase, phosphonate catabolism-associated, putative
IPR017816 Formaldehyde dehydrogenase, mycothiol-dependent
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Contains
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IPR002328 Alcohol dehydrogenase, zinc-containing, conserved site
IPR002364 Quinone oxidoreductase/zeta-crystallin, conserved site
IPR013154 Alcohol dehydrogenase GroES-like
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GO Term annotation
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Process
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GO:0055114 oxidation reduction
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Function
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GO:0008270 zinc ion binding
GO:0016491 oxidoreductase activity
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InterPro annotation
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 Entry Details in BioMart
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Abstract
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Alcohol dehydrogenase (EC:1.1.1.1) (ADH) catalyzes the reversible oxidation of
ethanol to acetaldehyde with the concomitant reduction of NAD:
Ethanol + NAD = Acetaldehyde + NADH
Currently three structurally and catalytically different types of alcohol
dehydrogenases are known:
- Zinc-containing 'long-chain' alcohol dehydrogenases.
- Insect-type, or 'short-chain' alcohol dehydrogenases.
- Iron-containing alcohol dehydrogenases.
Zinc-containing ADH's [1, 2] are dimeric or tetrameric enzymes that bind two
atoms of zinc per subunit. One of the zinc atom is essential for catalytic
activity while the other is not. Both zinc atoms are coordinated by either
cysteine or histidine residues; the catalytic zinc is coordinated by two
cysteines and one histidine. Zinc-containing ADH's are found in bacteria,
mammals, plants, and in fungi. In most species there are more than one isozyme
(for example, human have at least six isozymes, yeast have three, etc.). A
number of other zinc-dependent dehydrogenases are closely related to zinc
ADH [3] and are included in this family.
In addition, this family includes NADP-dependent quinone oxidoreductase (EC:1.6.5.5),
an enzyme found in bacteria (gene qor), in yeast and in mammals where, in some
species such as rodents, it has been recruited as an eye lens protein and is
known as zeta-crystallin [4]. The sequence of quinone oxidoreductase is
distantly related to that other zinc-containing alcohol dehydrogenases and it
lacks the zinc-ligand residues. The torpedo fish and mammalian synaptic vesicle
membrane protein vat-1 is related to qor.
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Structural links
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Database links
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Publications
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1.
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Jornvall H, Persson B, Jeffery J.
Characteristics of alcohol/polyol dehydrogenases. The zinc-containing long-chain alcohol dehydrogenases.
Eur. J. Biochem. 167 195-201 1987
[PubMed: 3622514]
http://dx.doi.org/10.1111/j.1432-1033.1987.tb13323.x
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2.
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Sun HW, Plapp BV.
Progressive sequence alignment and molecular evolution of the Zn-containing alcohol dehydrogenase family.
J. Mol. Evol. 34 522-35 1992
[PubMed: 1593644]
http://dx.doi.org/10.1007/BF00160465
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3.
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Persson B, Hallborn J, Walfridsson M, Hahn-Hagerdal B, Keranen S, Penttila M, Jornvall H.
Dual relationships of xylitol and alcohol dehydrogenases in families of two protein types.
FEBS Lett. 324 9-14 1993
[PubMed: 8504864]
http://dx.doi.org/10.1016/0014-5793(93)81522-2
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4.
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Jornvall H, Persson B, Du Bois GC, Lavers GC, Chen JH, Gonzalez P, Rao PV, Zigler JS Jr.
Zeta-crystallin versus other members of the alcohol dehydrogenase super-family. Variability as a functional characteristic.
FEBS Lett. 322 240-4 1993
[PubMed: 8486156]
http://dx.doi.org/10.1016/0014-5793(93)81578-N
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Additional Reading
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Goihberg E, Dym O, Tel-Or S, Shimon L, Frolow F, Peretz M, Burstein Y.
Thermal stabilization of the protozoan Entamoeba histolytica alcohol dehydrogenase by a single proline substitution.
Proteins 72 2008 711-9
[PubMed: 18260103]
http://dx.doi.org/10.1002/prot.21946
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Youn B, Camacho R, Moinuddin SG, Lee C, Davin LB, Lewis NG, Kang C.
Crystal structures and catalytic mechanism of the Arabidopsis cinnamyl alcohol dehydrogenases AtCAD5 and AtCAD4.
Org. Biomol. Chem. 4 2006 1687-97
[PubMed: 16633561]
http://dx.doi.org/10.1039/b601672c
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Brouns SJ, Turnbull AP, Willemen HL, Akerboom J, van der Oost J.
Crystal structure and biochemical properties of the D-arabinose dehydrogenase from Sulfolobus solfataricus.
J. Mol. Biol. 371 2007 1249-60
[PubMed: 17610898]
http://dx.doi.org/10.1016/j.jmb.2007.05.097
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Meijers R, Adolph HW, Dauter Z, Wilson KS, Lamzin VS, Cedergren-Zeppezauer ES.
Structural evidence for a ligand coordination switch in liver alcohol dehydrogenase.
Biochemistry 46 2007 5446-54
[PubMed: 17429946]
http://dx.doi.org/10.1021/bi6023594
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Goihberg E, Dym O, Tel-Or S, Levin I, Peretz M, Burstein Y.
A single proline substitution is critical for the thermostabilization of Clostridium beijerinckii alcohol dehydrogenase.
Proteins 66 2007 196-204
[PubMed: 17063493]
http://dx.doi.org/10.1002/prot.21170
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InterPro 23.1
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