Iron-type alcohol dehydrogenase-like (IPR039697)

Short name: Alcohol_dehydrogenase_Fe

Overlapping homologous superfamilies


Family relationships


Alcohol dehydrogenase (EC: (ADH) catalyzes the reversible oxidation of ethanol to acetaldehyde with the concomitant reduction of NAD. 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) [PMID: 3584063], as well as in Zymomonas mobilis (gene adhB) [PMID: 2823079]. These two iron-containing ADH's are closely related to the following enzymes:

  • Escherichia coli lactaldehyde reductase (also known as propanediol oxidoreductase) (EC: (gene fucO) [PMID: 2661535], 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) [PMID: 1385386], an enzyme which has activity using butanol and ethanol as substrates.
  • E. coli aldehyde-alcohol dehydrogenase (AdhE) [PMID: 2015910], an iron-dependent enzyme which harbor three different activities: alcohol dehydrogenase, acetaldehyde dehydrogenase (acetylating) (EC: and pyruvate-formate-lyase deactivase.
  • 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: [PMID: 1644761].
  • E. coli and Salmonella typhimurium ethanolamine utilization protein eutG.
  • E. coli hypothetical protein yiaY.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.