Alcohol dehydrogenase, iron-type (IPR001670)
Short name: ADH_Fe
Alcohol dehydrogenase (EC:126.96.36.199) (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 propanediol oxidoreductase (EC:188.8.131.52) (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 adhE [PMID: 2015910], an iron-dependent enzyme which harbor three different activities: alcohol dehydrogenase, acetaldehyde dehydrogenase (acetylating) (EC:184.108.40.206) and pyruvate-formate-lyase deactivase.
- Bacterial glycerol dehydrogenase (EC:220.127.116.11) (gene gldA or dhaD) [PMID: 8132480].
- Clostridium kluyveri NAD-dependent 4-hydroxybutyrate dehydrogenase (4hbd) (EC:18.104.22.168).
- Citrobacter freundii and Klebsiella pneumoniae 1,3-propanediol dehydrogenase (EC:22.214.171.124) (gene dhaT).
- Bacillus methanolicus NAD-dependent methanol dehydrogenase (EC:126.96.36.199) [PMID: 1644761].
- E. coli and Salmonella typhimurium ethanolamine utilization protein eutG.
- E. coli hypothetical protein yiaY.
- PF00465 (Fe-ADH)