{PDOC00058}
{PS00059; ADH_ZINC}
{PS01162; QOR_ZETA_CRYSTAL}
{BEGIN}
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* Zinc-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.

Zinc-containing ADH's [2,3] are  dimeric or  tetrameric enzymes  that bind two
atoms of zinc per subunit.  One  of  the  zinc atom is essential for catalytic
activity while the other is not.   Both  zinc atoms  are coordinated by either
cysteine or histidine residues;  the  catalytic zinc  is  coordinated  by  two
cysteines  and one histidine.   Zinc-containing ADH's  are  found in bacteria,
mammals, plants, and in fungi. In most species there are more than one isozyme
(for example,  human  have  at  least six isozymes, yeast have three, etc.). A
number of  other   zinc-dependent dehydrogenases  are  closely related to zinc
ADH [4], these are:

 - Xylitol dehydrogenase (EC 1.1.1.9) (D-xylulose reductase).
 - Sorbitol dehydrogenase (EC 1.1.1.14).
 - Aryl-alcohol dehydrogenase (EC 1.1.1.90) (benzyl alcohol dehydrogenase).
 - L-threonine 3-dehydrogenase (EC 1.1.1.103).
 - Cinnamyl-alcohol  dehydrogenase  (EC  1.1.1.195)  (CAD) [5]. CAD is a plant
   enzyme involved in the biosynthesis of lignin.
 - Galactitol-1-phosphate 5-dehydrogenase (EC 1.1.1.251).
 - Escherichia coli L-idonate 5-dehydrogenase (EC 1.1.1.264).
 - Pseudomonas putida 5-exo-alcohol dehydrogenase (EC 1.1.1.-) [6].
 - Escherichia coli starvation sensing protein rspB.
 - Escherichia coli hypothetical protein yjgB.
 - Escherichia coli hypothetical protein yjgV.
 - Escherichia coli hypothetical protein yjjN.
 - Yeast hypothetical protein YAL060w (FUN49).
 - Yeast hypothetical protein YAL061w (FUN50).
 - Yeast hypothetical protein YCR105w.

The pattern that  we developed to  detect this  class of enzymes is based on a
conserved region that includes a histidine  residue which is the second ligand
of the catalytic zinc atom.

This family also includes NADP-dependent quinone  oxidoreductase (EC 1.6.5.5),
an enzyme found in bacteria (gene qor), in yeast and in mammals where, in some
species such as rodents, it has  been  recruited as an eye lens protein and is
known as  zeta-crystallin  [7].  The  sequence  of  quinone  oxidoreductase is
distantly related to that other zinc-containing alcohol  dehydrogenases and it
lacks the zinc-ligand residues. The torpedo fish and mammlian synaptic vesicle
membrane protein vat-1 is realted to qor. We have developed a specific pattern
for this subfamily.

-Consensus pattern: G-H-E-x-{EL}-G-{AP}-x(4)-[GA]-x(2)-[IVSAC]
                    [H is a zinc ligand]
-Sequences known to belong to this class detected by the pattern: ALL,  except
 for quinone oxidoreductases.
-Other sequence(s) detected in Swiss-Prot: 10.

-Consensus pattern: [GSDN]-[DEQHKM]-x(2)-L-x(3)-[SAG](2)-G(2)-x-G-x(4)-Q-x(2)-
                    [KRS]
-Sequences known to belong to this class detected by the pattern: ALL  quinone
 oxidoreductases.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Expert(s) to contact by email:
           Joernvall H.; hans.jornvall@ki.se
           Persson B.; bengt.persson@icm.uu.se

-Last update: April 2006 / Patterns revised.

[ 1] Branden C.-I., Joernvall H., Eklund H., Furugren B.
     (In) The Enzymes (3rd edition) 11:104-190(1975).
[ 2] Joernvall H., Persson B., Jeffery J.
     Eur. J. Biochem. 167:195-201(1987).
[ 3] Sun H.-W., Plapp B.V.
     "Progressive sequence alignment and molecular evolution of the
     Zn-containing alcohol dehydrogenase family."
     J. Mol. Evol. 34:522-535(1992).
     PubMed=1593644
[ 4] Persson B., Hallborn J., Walfridsson M., Hahn-Hagerdal B., Keranen S.,
     Penttila M., Jornvall H.
     "Dual relationships of xylitol and alcohol dehydrogenases in families
     of two protein types."
     FEBS Lett. 324:9-14(1993).
     PubMed=8504864
[ 5] Knight M.E., Halpin C., Schuch W.
     "Identification and characterisation of cDNA clones encoding cinnamyl
     alcohol dehydrogenase from tobacco."
     Plant Mol. Biol. 19:793-801(1992).
     PubMed=1643282
[ 6] Koga H., Aramaki H., Yamaguchi E., Takeuchi K., Horiuchi T.,
     Gunsalus I.C.
     "camR, a negative regulator locus of the cytochrome P-450cam
     hydroxylase operon."
     J. Bacteriol. 166:1089-1095(1986).
     PubMed=3011733
[ 7] Joernvall H., Persson B., Du Bois G., Lavers G.C., Chen J.H.,
     Gonzalez P., Rao P.V., Zigler J.S. Jr.
     FEBS Lett. 322:240-244(1993).

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