{PDOC00788}
{PS01028; DEHYDROQUINASE_I}
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* Dehydroquinase class I active site *
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3-dehydroquinate dehydratase  (EC 4.2.1.10), or  dehydroquinase, catalyzes the
conversion of  3-dehydroquinate  into 3-dehydroshikimate. It is the third step
in the  shikimate  pathway  for  the biosynthesis of aromatic amino acids from
chorismate. Two classes of dehydroquinases exist, known as types I and II. The
best studied  type  I  enzyme is from Escherichia coli (gene aroD) and related
bacteria where  it is a homodimeric protein of a chain of about 250  residues.
In fungi,  dehydroquinase  is part of a multifunctional enzyme which catalyzes
five consecutive  steps  in  the shikimate pathway. In aroD, it has been shown
[1] that  a  histidine  is  involved  in  the catalytic mechanism; we used the
region around this residue as a signature pattern.

-Consensus pattern: D-[LIVM]-[DE]-[LIVMN]-x(18,20)-[LIVM](2)-x-[SC]-[NHY]-H-
                    [DN]
                    [H is the 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: December 2001 / Pattern and text revised.

[ 1] Deka R.K., Kleanthous C., Coggins J.R.
     "Identification of the essential histidine residue at the active site
     of Escherichia coli dehydroquinase."
     J. Biol. Chem. 267:22237-22242(1992).
     PubMed=1429576

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