{PDOC00720}
{PS00934; GLYOXALASE_I_1}
{PS00935; GLYOXALASE_I_2}
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* Glyoxalase I signatures *
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Glyoxalase I  (EC 4.4.1.5) (lactoylglutathione lyase) catalyzes the first step
of the  glyoxal  pathway,  the transformation of methylglyoxal and glutathione
into S-lactoylglutathione  which  is then converted by glyoxalase II to lactic
acid [1].  Glyoxalase I is  an  ubiquitous enzyme which binds one mole of zinc
per subunit. The bacterial and yeast enzymes are monomeric while the mammalian
one is homodimeric.

The sequence  of  glyoxalase I is well conserved. In bacteria and mammals, the
enzyme is  a  protein  of about 130 to 180 residues while in fungi it is about
twice longer. In these  organisms the enzyme is built out of the tandem repeat
of an homologous domain.

We have   derived  two  signature  patterns  for this family. The first one is
located in  the  N-terminal  region  while  the  second  one is located in the
central section  of  the protein and contains a conserved histidine that could
be implicated in the binding of the zinc atom.

-Consensus pattern: [HQ]-[IVT]-x-[LIVFY]-x-[IV]-x(4)-{E}-[STA]-x(2)-F-[YM]-
                    x(2,3)-[LMF]-G-[LMF]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: 2.

-Consensus pattern: G-[NTKQ]-x(0,5)-[GA]-[LVFY]-[GH]-H-[IVF]-[CGA]-x-[STAGLE]-
                    x(2)-[DNC]
-Sequences known to belong to this class detected by the pattern: ALL,  except
 B.subtilis ywbC.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: December 2004 / Pattern and text revised.

[ 1] Kim N.-S., Umezawa Y., Ohmura S., Kato S.
     "Human glyoxalase I. cDNA cloning, expression, and sequence similarity
     to glyoxalase I from Pseudomonas putida."
     J. Biol. Chem. 268:11217-11221(1993).
     PubMed=7684374;

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