{PDOC00471}
{PS00545; ALDOSE_1_EPIMERASE}
{BEGIN}
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* Aldose 1-epimerase putative active site *
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Aldose 1-epimerase (EC 5.1.3.3) (mutarotase)  is  the  enzyme  responsible for
the anomeric interconversion of  D-glucose  and  other  aldoses  between their
alpha- and beta-forms.

The sequence of mutarotase from two bacteria,  Acinetobacter calcoaceticus and
Streptococcus thermophilus is available [1].  It has also been  shown that, on
the basis of  extensive sequence similarities, a  mutarotase domain seem to be
present in the C-terminal half of the fungal GAL10  protein  which encodes, in
the N-terminal part, for UDP-glucose 4-epimerase.

The best conserved region in  the  sequence of mutarotase is centered around a
conserved histidine residue which may be involved in the catalytic mechanism.

-Consensus pattern: [NS]-x-T-N-H-x-Y-[FW]-N-[LI]
                    [The H may be an active site residue]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: May 2004 / Text revised.

[ 1] Poolman B., Royer T.J., Mainzer S.E., Schmidt B.F.
     "Carbohydrate utilization in Streptococcus thermophilus:
     characterization of the genes for aldose 1-epimerase (mutarotase) and
     UDPglucose 4-epimerase."
     J. Bacteriol. 172:4037-4047(1990).
     PubMed=1694527

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