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InterPro: IPR002328 Alcohol dehydrogenase, zinc-containing, conserved site

Protein matches Help

UniProtKB

Matches:

8506 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
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Accession List
Matches in BioMart

Accession

IPR002328 ADH_Zn_CS

Type

Conserved_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS00059	ADH_ZINC	8506
Signatures in BioMart

InterPro Relationships Help

Found in

IPR002085 Alcohol dehydrogenase superfamily, zinc-containing
IPR004627 L-threonine 3-dehydrogenase
IPR011032 GroES-like
IPR013154 Alcohol dehydrogenase GroES-like
IPR014183 Alcohol dehydrogenase class III/S-(hydroxymethyl)glutathione dehydrogenase
IPR014184 Formaldehyde dehydrogenase, glutathione-independent
IPR014187 Alcohol dehydrogenase, zinc-binding type 2
IPR017816 Formaldehyde dehydrogenase, mycothiol-dependent

GO Term annotation Help

Process

GO:0055114 oxidation reduction

Function

GO:0008270 zinc ion binding
GO:0016491 oxidoreductase activity

InterPro annotation

Entry Details in BioMart

Abstract

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, including xylitol dehydrogenase (EC:1.1.1.9); sorbitol dehydrogenase (EC:1.1.1.14); aryl-alcohol dehydrogenase (EC:1.1.1.90); threonine 3-dehydrogenase (EC:1.1.1.103); cinnamyl-alcohol dehydrogenase (EC:1.1.1.195) (CAD); galactitol-1-phosphate dehydrogenase (EC:1.1.1.251); and Pseudomonas putida 5-exo-alcohol dehydrogenase (EC:1.1.1).

Structural links Help

PDB - click here

SCOP: b.35.1.2

CATH: 3.90.180.10

Database links Help

PDBe-motif: PS00059

Enzyme: EC:1.1.1

PROSITE doc: PDOC00058

Blocks: IPB002328

COMe: PRX000511

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR002328

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O45687 Alcohol dehydrogenase 2

P00325 Alcohol dehydrogenase 1B

P00330 Alcohol dehydrogenase 1

P46415 Alcohol dehydrogenase class-3

Q9QYY9 Alcohol dehydrogenase 4

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR002328	Alcohol dehydrogenase, zinc-containing, conserved site
IPR013149	Alcohol dehydrogenase, zinc-binding
IPR013154	Alcohol dehydrogenase GroES-like
IPR011032	GroES-like
IPR016040	NAD(P)-binding domain
IPR002085	Alcohol dehydrogenase superfamily, zinc-containing
IPR014183	Alcohol dehydrogenase class III/S-(hydroxymethyl)glutathione dehydrogenase
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	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
2.	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
3.	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

Additional Reading Open in usermanual
	Koga H, Aramaki H, Yamaguchi E, Takeuchi K, Horiuchi T, Gunsalus IC. camR, a negative regulator locus of the cytochrome P-450cam hydroxylase operon. J. Bacteriol. 166 1986 1089-95 [PubMed: 3011733] http://jb.asm.org/cgi/content/abstract/166/3/1089
	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
	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
	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
	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
	Knight ME, Halpin C, Schuch W. Identification and characterisation of cDNA clones encoding cinnamyl alcohol dehydrogenase from tobacco. Plant Mol. Biol. 19 1992 793-801 [PubMed: 1643282] http://dx.doi.org/10.1007/BF00027075
	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

InterPro 23.1