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InterPro: IPR013149 Alcohol dehydrogenase, zinc-binding

Protein matches Help

UniProtKB

Matches:

19661 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
Architectures
Accession List
Matches in BioMart

Accession

IPR013149 ADH_Zn-bd

Secondary

IPR002085

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00107	ADH_zinc_N	19661
Signatures in BioMart

InterPro Relationships Help

Parent

IPR016040 NAD(P)-binding domain

Found in

IPR004627 L-threonine 3-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
IPR020843 Polyketide synthase, enoylreductase

Contains

IPR002364 Quinone oxidoreductase/zeta-crystallin, conserved site

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 alcohols to their corresponding acetaldehyde or ketone with the concomitant reduction of NAD:

alcohol + NAD = aldehyde or ketone + 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 many species there is more than one isozyme (for example, humans 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.

Sorbitol dehydrogenase (EC:1.1.1.14)
L-threonine 3-dehydrogenase (EC:1.1.1.103)
Glutathione-dependent formaldehyde dehydrogenase (EC:1.1.1.284)
Mannitol dehydrogenase (EC:1.1.1.255)

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.

This entry represents the cofactor-binding domain of these enzymes, which is normally found towards the C terminus. Structural studies indicate that it forms a classical Rossman fold that reversibly binds NAD(H) [5, 6, 7].

Structural links Help

PDB - click here

SCOP: c.2.1.1

CATH: 3.40.50.720 , 3.90.180.10

Database links Help

Enzyme: EC:1

Pfam Clan: CL0063.21

AC	CL0063.21
ID	NADP_Rossmann
DE	FAD/NAD(P)-binding Rossmann fold Superfamily
PF00044	IPR020828	Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain
PF00056	IPR001236	Lactate/malate dehydrogenase
PF00070	IPR001327	Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
PF00106	IPR002198	Short-chain dehydrogenase/reductase SDR
PF00107	IPR013149	Alcohol dehydrogenase, zinc-binding
PF00208	IPR006096	Glutamate/phenylalanine/leucine/valine dehydrogenase, C-terminal
PF00479	IPR001282	Glucose-6-phosphate dehydrogenase
PF00670	IPR015878	S-adenosyl-L-homocysteine hydrolase, NAD binding
PF00732	IPR000172	Glucose-methanol-choline oxidoreductase, N-terminal
PF00743	IPR000960	Flavin-containing monooxygenase FMO
PF00890	IPR003953	Fumarate reductase/succinate dehydrogenase flavoprotein, N-terminal
PF00899	IPR000594	UBA/THIF-type NAD/FAD binding fold
PF00996	IPR018203	GDP dissociation inhibitor
PF01073	IPR002225	3-beta hydroxysteroid dehydrogenase/isomerase
PF01113	IPR000846	Dihydrodipicolinate reductase
PF01118	IPR000534	Semialdehyde dehydrogenase, NAD-binding
PF01134	IPR002218	Glucose-inhibited division protein A-related
PF01210	IPR011128	NAD-dependent glycerol-3-phosphate dehydrogenase, N-terminal
PF01225	IPR000713	Mur ligase, N-terminal
PF01232	IPR013131	Mannitol dehydrogenase, N-terminal
PF01262	IPR007698	Alanine dehydrogenase/PNT, C-terminal
PF01266	IPR006076	FAD dependent oxidoreductase
PF01370	IPR001509	NAD-dependent epimerase/dehydratase
PF01408	IPR000683	Oxidoreductase, N-terminal
PF01488	IPR006151	Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase
PF01494	IPR002938	Monooxygenase, FAD-binding
PF01593	IPR002937	Amine oxidase
PF01946	IPR002922	Thiamine biosynthesis Thi4 protein
PF02153	IPR003099	Prephenate dehydrogenase
PF02254	IPR003148	Regulator of K+ conductance, N-terminal
PF02423	IPR003462	Ornithine cyclodeaminase/mu-crystallin
PF02558	IPR013332	Ketopantoate reductase ApbA/PanE, N-terminal
PF02629	IPR003781	CoA-binding
PF02670	IPR013512	1-deoxy-D-xylulose 5-phosphate reductoisomerase, N-terminal
PF02719	IPR003869	Polysaccharide biosynthesis protein CapD-like
PF02737	IPR006176	3-hydroxyacyl-CoA dehydrogenase, NAD binding
PF02826	IPR006140	D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding
PF02882	IPR020631	Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain
PF03435	IPR005097	Saccharopine dehydrogenase
PF03446	IPR006115	6-phosphogluconate dehydrogenase, NAD-binding
PF03447	IPR005106	Aspartate/homoserine dehydrogenase, NAD-binding
PF03486	IPR004792	HI0933-like protein
PF03721	IPR001732	UDP-glucose/GDP-mannose dehydrogenase, N-terminal
PF03807	IPR004455	NADP oxidoreductase, coenzyme F420-dependent
PF03949	IPR012302	Malic enzyme, NAD-binding
PF04321	IPR005913	dTDP-4-dehydrorhamnose reductase
PF04723	IPR006812	Glycine reductase complex selenoprotein A
PF04820	IPR006905	Tryptophan halogenase
PF05368	IPR008030	NmrA-like
PF05834	IPR008671	Lycopene beta/epsilon cyclase
PF06039	IPR006231	Malate:quinone-oxidoreductase
PF07157	IPR009826	DNA circulation, N-terminal
PF07991	IPR013116	Acetohydroxy acid isomeroreductase, catalytic
PF07992	IPR013027	FAD-dependent pyridine nucleotide-disulphide oxidoreductase
PF07993	IPR013120	Male sterility, NAD-binding
PF07994	IPR002587	Myo-inositol-1-phosphate synthase
PF08491	IPR013698	Squalene epoxidase
PF08659	IPR013968	Polyketide synthase, KR
PF10727	IPR019665	Putative oxidoreductase/dehydrogenase, Rossmann-like domain

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR013149

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

Q8VDQ1 Prostaglandin reductase 2

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
4.	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
5.	Pauly TA, Ekstrom JL, Beebe DA, Chrunyk B, Cunningham D, Griffor M, Kamath A, Lee SE, Madura R, Mcguire D, Subashi T, Wasilko D, Watts P, Mylari BL, Oates PJ, Adams PD, Rath VL. X-ray crystallographic and kinetic studies of human sorbitol dehydrogenase. Structure 11 1071-85 2003 [PubMed: 12962626] http://dx.doi.org/10.1016/S0969-2126(03)00167-9
6.	Rubach JK, Plapp BV. Amino acid residues in the nicotinamide binding site contribute to catalysis by horse liver alcohol dehydrogenase. Biochemistry 42 2907-15 2003 [PubMed: 12627956] http://dx.doi.org/10.1021/bi0272656
7.	Thorn JM, Barton JD, Dixon NE, Ollis DL, Edwards KJ. Crystal structure of Escherichia coli QOR quinone oxidoreductase complexed with NADPH. J. Mol. Biol. 249 785-99 1995 [PubMed: 7602590] http://dx.doi.org/10.1006/jmbi.1995.0337

Additional Reading Open in usermanual
	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
	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