PROSITE documentation PDOC00059
Iron-containing alcohol dehydrogenases signatures


Alcohol dehydrogenase (EC (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 (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.
  • Escherichia coli adhE [6], an iron-dependent enzyme which harbor three different activities: alcohol dehydrogenase, acetaldehyde dehydrogenase (acetylating) (EC and pyruvate-formate-lyase deactivase.
  • Bacterial glycerol dehydrogenase (EC (gene gldA or dhaD) [7].
  • Clostridium kluyveri NAD-dependent 4-hydroxybutyrate dehydrogenase (4hbd) (EC
  • Citrobacter freundii and Klebsiella pneumoniae 1,3-propanediol dehydrogenase (EC (gene dhaT).
  • Bacillus methanolicus NAD-dependent methanol dehydrogenase (EC [8].
  • Escherichia coli and Salmonella typhimurium ethanolamine utilization protein eutG.
  • Escherichia coli hypothetical protein yiaY.
  • Escherichia coli hypothetical protein ybdH.
  • Escherichia coli hypothetical protein yqhD.
  • Methanococcus jannaschii hypothetical protein MJ0712.

The patterns that we developed to detect this class of enzymes are based on two conserved regions.

Last update:

July 1998 / Patterns and text revised.


Technical section

PROSITE methods (with tools and information) covered by this documentation:

ADH_IRON_1, PS00913; Iron-containing alcohol dehydrogenases signature 1  (PATTERN)

ADH_IRON_2, PS00060; Iron-containing alcohol dehydrogenases signature 2  (PATTERN)


1AuthorsBranden C.-I. Joernvall H. Eklund H. Furugren B.
Source(In) The Enzymes (3rd edition) 11:104-190(1975).

2AuthorsConway T. Sewell G.W. Osman Y.A. Ingram L.O.
TitleCloning and sequencing of the alcohol dehydrogenase II gene from Zymomonas mobilis.
SourceJ. Bacteriol. 169:2591-2597(1987).
PubMed ID3584063

3AuthorsWilliamson V.M. Paquin C.E.
TitleHomology of Saccharomyces cerevisiae ADH4 to an iron-activated alcohol dehydrogenase from Zymomonas mobilis.
SourceMol. Gen. Genet. 209:374-381(1987).
PubMed ID2823079

4AuthorsConway T. Ingram L.O.
TitleSimilarity of Escherichia coli propanediol oxidoreductase (fucO product) and an unusual alcohol dehydrogenase from Zymomonas mobilis and Saccharomyces cerevisiae.
SourceJ. Bacteriol. 171:3754-3759(1989).
PubMed ID2661535

5AuthorsWalter K.A. Bennett G.N. Papoutsakis E.T.
TitleMolecular characterization of two Clostridium acetobutylicum ATCC 824 butanol dehydrogenase isozyme genes.
SourceJ. Bacteriol. 174:7149-7158(1992).
PubMed ID1385386

6AuthorsKessler D. Leibrecht I. Knappe J.
TitlePyruvate-formate-lyase-deactivase and acetyl-CoA reductase activities of Escherichia coli reside on a polymeric protein particle encoded by adhE.
SourceFEBS Lett. 281:59-63(1991).
PubMed ID2015910

7AuthorsTruniger V. Boos W.
TitleMapping and cloning of gldA, the structural gene of the Escherichia coli glycerol dehydrogenase.
SourceJ. Bacteriol. 176:1796-1800(1994).
PubMed ID8132480

8Authorsde Vries G.E. Arfman N. Terpstra P. Dijkhuizen L.
SourceJ. Bacteriol. 174:5346-5353(1992).

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