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InterPro: IPR001670 Alcohol dehydrogenase, iron-type

Protein matches Help

UniProtKB

Matches:

5111 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

IPR001670 ADH_Fe

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00465	Fe-ADH	5111
Signatures in BioMart

InterPro Relationships Help

Found in

IPR012079 Bifunctional aldehyde/alcohol dehydrogenase
IPR013460 Lactaldehyde reductase
IPR016205 Glycerol dehydrogenase
IPR017775 Iron-containing alcohol dehydrogenase, phosphonate metabolism-associated

Contains

IPR018211 Alcohol dehydrogenase, iron-type, conserved site

GO Term annotation Help

Process

GO:0055114 oxidation reduction

Function

GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding

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 [1]. 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.

Iron-containing ADH's have been found in yeast (gene ADH4) [2], as well as in Zymomonas mobilis (gene adhB) [3]. These two iron-containing ADH's are closely related to the following enzymes:

Escherichia coli propanediol oxidoreductase (EC:1.1.1.77) (gene fucO) [4], an enzyme involved in the metabolism of fucose and which also seems to contain ferrous ion(s).
Clostridium acetobutylicum NADPH- and NADH-dependent butanol dehydrogenases (EC:1.1.1) (genes adh1, bdhA and bdhB) [5], an enzyme which has activity using butanol and ethanol as substrates.
E. coli adhE [6], an iron-dependent enzyme which harbor three different activities: alcohol dehydrogenase, acetaldehyde dehydrogenase (acetylating) (EC:1.2.1.10) and pyruvate-formate-lyase deactivase.
Bacterial glycerol dehydrogenase (EC:1.1.1.6) (gene gldA or dhaD) [7].
Clostridium kluyveri NAD-dependent 4-hydroxybutyrate dehydrogenase (4hbd) (EC:1.1.1.61).
Citrobacter freundii and Klebsiella pneumoniae 1,3-propanediol dehydrogenase (EC:1.1.1.202) (gene dhaT).
Bacillus methanolicus NAD-dependent methanol dehydrogenase (EC:1.1.1.244) [8].
E. coli and Salmonella typhimurium ethanolamine utilization protein eutG.
E. coli hypothetical protein yiaY.

Structural links Help

PDB - click here

SCOP: e.22.1.2

CATH: 1.20.1090.10 , 3.40.50.1970

Database links Help

PDBe-motif: PS00060 , PS00913

Enzyme: EC:1.1

PROSITE doc: PDOC00059

PANDIT: PF00465

Blocks: IPB001670

COMe: PRX001203

Pfam Clan: CL0224.4

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001670

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A6ZTT5 Alcohol dehydrogenase 4

Q8IWW8 Hydroxyacid-oxoacid transhydrogenase, mitochondrial

Q8R0N6 Hydroxyacid-oxoacid transhydrogenase, mitochondrial

Q9U2M4 Probable hydroxyacid-oxoacid transhydrogenase, mitochondrial

Q9W265 Probable hydroxyacid-oxoacid transhydrogenase, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001670	Alcohol dehydrogenase, iron-type
IPR018211	Alcohol dehydrogenase, iron-type, conserved site
	SWISS-MODEL
	ModBase

Publications Open in usermanual
1.	Joernvall H, Branden C-I, Eklund H, Furugren B. 11 104-90 1975
2.	Conway T, Sewell GW, Osman YA, Ingram LO. Cloning and sequencing of the alcohol dehydrogenase II gene from Zymomonas mobilis. J. Bacteriol. 169 2591-7 1987 [PubMed: 3584063] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=3584063&action=stream&blobtype=pdf
3.	Williamson VM, Paquin CE. Homology of Saccharomyces cerevisiae ADH4 to an iron-activated alcohol dehydrogenase from Zymomonas mobilis. Mol. Gen. Genet. 209 374-81 1987 [PubMed: 2823079] http://dx.doi.org/10.1007/BF00329668
4.	Conway T, Ingram LO. Similarity of Escherichia coli propanediol oxidoreductase (fucO product) and an unusual alcohol dehydrogenase from Zymomonas mobilis and Saccharomyces cerevisiae. J. Bacteriol. 171 3754-9 1989 [PubMed: 2661535] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=2661535
5.	Walter KA, Bennett GN, Papoutsakis ET. Molecular characterization of two Clostridium acetobutylicum ATCC 824 butanol dehydrogenase isozyme genes. J. Bacteriol. 174 7149-58 1992 [PubMed: 1385386] http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=1385386&action=stream&blobtype=pdf
6.	Kessler D, Leibrecht I, Knappe J. Pyruvate-formate-lyase-deactivase and acetyl-CoA reductase activities of Escherichia coli reside on a polymeric protein particle encoded by adhE. FEBS Lett. 281 59-63 1991 [PubMed: 2015910] http://dx.doi.org/10.1016/0014-5793(91)80358-A
7.	Truniger V, Boos W. Mapping and cloning of gldA, the structural gene of the Escherichia coli glycerol dehydrogenase. J. Bacteriol. 176 1796-800 1994 [PubMed: 8132480] http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=8132480&action=stream&blobtype=pdf
8.	de Vries GE, Arfman N, Terpstra P, Dijkhuizen L. Cloning, expression, and sequence analysis of the Bacillus methanolicus C1 methanol dehydrogenase gene. J. Bacteriol. 174 5346-53 1992 [PubMed: 1644761] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=1644761&action=stream&blobtype=pdf

Additional Reading Open in usermanual
	Sulzenbacher G, Alvarez K, Van Den Heuvel RH, Versluis C, Spinelli S, Campanacci V, Valencia C, Cambillau C, Eklund H, Tegoni M. Crystal structure of E.coli alcohol dehydrogenase YqhD: evidence of a covalently modified NADP coenzyme. J. Mol. Biol. 342 2004 489-502 [PubMed: 15327949] http://dx.doi.org/10.1016/j.jmb.2004.07.034
	Montella C, Bellsolell L, Perez-Luque R, Badia J, Baldoma L, Coll M, Aguilar J. Crystal structure of an iron-dependent group III dehydrogenase that interconverts L-lactaldehyde and L-1,2-propanediol in Escherichia coli. J. Bacteriol. 187 2005 4957-66 [PubMed: 15995211] http://dx.doi.org/10.1128/JB.187.14.4957-4966.2005
	Lesley SA, Kuhn P, Godzik A, Deacon AM, Mathews I, Kreusch A, Spraggon G, Klock HE, McMullan D, Shin T, Vincent J, Robb A, Brinen LS, Miller MD, McPhillips TM, Miller MA, Scheibe D, Canaves JM, Guda C, Jaroszewski L, Selby TL, Elsliger MA, Wooley J, Taylor SS, Hodgson KO, Wilson IA, Schultz PG, Stevens RC. Structural genomics of the Thermotoga maritima proteome implemented in a high-throughput structure determination pipeline. Proc. Natl. Acad. Sci. U.S.A. 99 2002 11664-9 [PubMed: 12193646] http://dx.doi.org/10.1073/pnas.142413399
	Schwarzenbacher R, von Delft F, Canaves JM, Brinen LS, Dai X, Deacon AM, Elsliger MA, Eshaghi S, Floyd R, Godzik A, Grittini C, Grzechnik SK, Guda C, Jaroszewski L, Karlak C, Klock HE, Koesema E, Kovarik JS, Kreusch A, Kuhn P, Lesley SA, McMullan D, McPhillips TM, Miller MA, Miller MD, Morse A, Moy K, Ouyang J, Page R, Robb A, Rodrigues K, Selby TL, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, Wang X, West B, Wolf G, Hodgson KO, Wooley J, Wilson IA. Crystal structure of an iron-containing 1,3-propanediol dehydrogenase (TM0920) from Thermotoga maritima at 1.3 A resolution. Proteins 54 2004 174-7 [PubMed: 14705036] http://dx.doi.org/10.1002/prot.10594
	Badger J, Sauder JM, Adams JM, Antonysamy S, Bain K, Bergseid MG, Buchanan SG, Buchanan MD, Batiyenko Y, Christopher JA, Emtage S, Eroshkina A, Feil I, Furlong EB, Gajiwala KS, Gao X, He D, Hendle J, Huber A, Hoda K, Kearins P, Kissinger C, Laubert B, Lewis HA, Lin J, Loomis K, Lorimer D, Louie G, Maletic M, Marsh CD, Miller I, Molinari J, Muller-Dieckmann HJ, Newman JM, Noland BW, Pagarigan B, Park F, Peat TS, Post KW, Radojicic S, Ramos A, Romero R, Rutter ME, Sanderson WE, Schwinn KD, Tresser J, Winhoven J, Wright TA, Wu L, Xu J, Harris TJ. Structural analysis of a set of proteins resulting from a bacterial genomics project. Proteins 60 2005 787-96 [PubMed: 16021622] http://dx.doi.org/10.1002/prot.20541

InterPro 23.1