{PDOC00059}
{PS00913; ADH_IRON_1}
{PS00060; ADH_IRON_2}
{BEGIN}
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* Iron-containing alcohol dehydrogenases signatures *
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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.
 - Escherichia 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].
 - 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.

-Consensus pattern: [STALIV]-[LIVF]-x-[DE]-x(6,7)-P-x(4)-[ALIV]-x-[GST]-x(2)-
                    D-[TAIVM]-[LIVMF]-x(4)-E
-Sequences known to belong to this class detected by the pattern: ALL,  except
 for a few.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Consensus pattern: [GSW]-x-[LIVTSACD]-[GH]-x(2)-[GSAE]-[GSHYQ]-x-[LIVTP]-
                    [GAST]-[GAS]-x(3)-[LIVMT]-x-[HNS]-[GA]-x-[GTAC]
-Sequences known to belong to this class detected by the pattern: ALL,  except
 for a few.
-Other sequence(s) detected in Swiss-Prot: 1.

-Last update: July 1998 / Patterns and text revised.

[ 1] Branden C.-I., Joernvall H., Eklund H., Furugren B.
     (In) The Enzymes (3rd edition) 11:104-190(1975).
[ 2] Conway T., Sewell G.W., Osman Y.A., Ingram L.O.
     "Cloning and sequencing of the alcohol dehydrogenase II gene from
     Zymomonas mobilis."
     J. Bacteriol. 169:2591-2597(1987).
     PubMed=3584063
[ 3] Williamson V.M., Paquin C.E.
     "Homology of Saccharomyces cerevisiae ADH4 to an iron-activated
     alcohol dehydrogenase from Zymomonas mobilis."
     Mol. Gen. Genet. 209:374-381(1987).
     PubMed=2823079
[ 4] Conway T., Ingram L.O.
     "Similarity of Escherichia coli propanediol oxidoreductase (fucO
     product) and an unusual alcohol dehydrogenase from Zymomonas mobilis
     and Saccharomyces cerevisiae."
     J. Bacteriol. 171:3754-3759(1989).
     PubMed=2661535
[ 5] Walter K.A., Bennett G.N., Papoutsakis E.T.
     "Molecular characterization of two Clostridium acetobutylicum ATCC 824
     butanol dehydrogenase isozyme genes."
     J. Bacteriol. 174:7149-7158(1992).
     PubMed=1385386
[ 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
[ 7] Truniger V., Boos W.
     "Mapping and cloning of gldA, the structural gene of the Escherichia
     coli glycerol dehydrogenase."
     J. Bacteriol. 176:1796-1800(1994).
     PubMed=8132480
[ 8] de Vries G.E., Arfman N., Terpstra P., Dijkhuizen L.
     J. Bacteriol. 174:5346-5353(1992).

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