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Database: PROSITE(DOC)
Entry: PDOC00671
LinkDB: PDOC00671
Original site: PDOC00671 
{PDOC00671}
{PS00857; PREPHENATE_DEHYDR_1}
{PS00858; PREPHENATE_DEHYDR_2}
{PS51171; PREPHENATE_DEHYDR_3}
{BEGIN}
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* Prephenate dehydratase domain signatures and profile *
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Prephenate  dehydratase  (EC  4.2.1.51) (PDT) catalyzes the decarboxylation of
prephenate  into  phenylpyruvate.  In  microorganisms  PDT  is involved in the
terminal  pathway  of the biosynthesis of phenylalanine. In some bacteria such
as Escherichia coli PDT is part of a bifunctional enzyme (P-protein) that also
catalyzes the transformation of chorismate into prephenate (chorismate mutase,
see <PDOC51167>) while in other prokaryotes it is a monofunctional enzyme [1].
Fungal  and  plant  PDT  seem  to  be monofunctional enzymes as well. Most PDT
contain  a  C-terminal  regulatory  domain (R), which can be an ACT domain and
which allosterically regulates PDT by binding to aromatic amino acids [2,3].

Some proteins known to contain a prephenate dehydratase domain:

 - Bacterial  P-protein,  a  bifunctional  enzyme  composed  of  two catalytic
   domains, chorismate mutase and PDT for biosynthesis of phenylalanine (Phe).
   A C-terminal domain can be involved in feedback inhibition by Phe.
 - Mycobacterium tuberculosis PDT encoded by pheA, a monofunctional PDT that is
   allosterically activated by Phe, Tyr and Trp.
 - Yeast prephenate dehydratase.

As  signature  patterns  for  PDT we selected two conserved regions. The first
region  contains a conserved threonine which has been said to be essential for
the  activity of the enzyme in E. coli [4]. The second motif is located in the
regulatory  (Phe  binding)  region  in  the  part  C-terminal  to PDT and this
includes  a  conserved  glutamate. We also developed a profile that covers the
entire enzymatic domain of prephenate dehydratase.

-Consensus pattern: [FY]-x-[LIVM]-x(2)-[LIVM]-x(5)-[DN]-x(5)-T-R-F-[LIVMW]-x-
                    [LIVM]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Consensus pattern: [LIVM]-[ST]-[KR]-[LIVMF]-E-[ST]-R-P
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: December 2005 / Text revised; profile added.

[ 1] Fischer R.S., Zhao G., Jensen R.A.
     "Cloning, sequencing, and expression of the P-protein gene (pheA) of
     Pseudomonas stutzeri in Escherichia coli: implications for
     evolutionary relationships in phenylalanine biosynthesis."
     J. Gen. Microbiol. 137:1293-1301(1991).
     PubMed=1919506
[ 2] Zhang S., Pohnert G., Kongsaeree P., Wilson D.B., Clardy J., Ganem B.
     "Chorismate mutase-prephenate dehydratase from Escherichia coli. Study
     of catalytic and regulatory domains using genetically engineered
     proteins."
     J. Biol. Chem. 273:6248-6253(1998).
     PubMed=9497350
[ 3] Prakash P., Pathak N., Hasnain S.E.
     "pheA (Rv3838c) of Mycobacterium tuberculosis encodes an
     allosterically regulated monofunctional prephenate dehydratase that
     requires both catalytic and regulatory domains for optimum activity."
     J. Biol. Chem. 280:20666-20671(2005).
     PubMed=15753077; DOI=10.1074/jbc.M502107200
[ 4] Zhang S., Wilson D.B., Ganem B.
     "Probing the catalytic mechanism of prephenate dehydratase by
     site-directed mutagenesis of the Escherichia coli P-protein
     dehydratase domain."
     Biochemistry 39:4722-4728(2000).
     PubMed=10769128; DOI=10.1021/bi9926680
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