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{PDOC00097}
{PS00104; EPSP_SYNTHASE_1}
{PS00885; EPSP_SYNTHASE_2}
{BEGIN}
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* EPSP synthase signatures *
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EPSP   synthase (3-phosphoshikimate  1-carboxyvinyltransferase)  (EC 2.5.1.19)
catalyzes the sixth step  in the biosynthesis from  chorismate of the aromatic
amino acids (the shikimate pathway)  in bacteria (gene aroA), plants and fungi
(where it is part of a multifunctional enzyme which catalyzes five consecutive
steps in  this  pathway) [1]. EPSP synthase has been extensively studied as it
is the target of the potent herbicide glyphosate which inhibits the enzyme.

The sequence  of EPSP from various biological sources shows that the structure
of the  enzyme  has  been well conserved throughout evolution. We selected two
conserved regions  as  signature  patterns. The first pattern corresponds to a
region that  is  part  of  the active site and which is also important for the
resistance to  glyphosate [2]. The second pattern is located in the C-terminal
part of  the  protein  and  contains  a  conserved  lysine  which  seems to be
important for the activity of the enzyme.

-Consensus pattern: [LIVF]-{LV}-x-[GANQK]-[NLG]-[SA]-[GA]-[TAI]-[STAGV]-{N}-R-
                    x-[LIVMFYAT]-x-[GSTAP]
-Sequences known to belong to this class detected by the pattern: ALL,  except
 for Mycobacterium tuberculosis aroA.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Consensus pattern: [KR]-x-[KH]-E-[CSTVI]-[DNE]-R-[LIVMY]-x-[GSTAVLD]-
                    [LIVMCTF]-x(3)-[LIVMFA]-x(2)-[LIVMFCGANY]-G
-Sequences known to belong to this class detected by the pattern: ALL,  except
 for Lactococcus lactis and Staphylococcus aureus aroA.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: April 2006 / Pattern revised.

[ 1] Stallings W.C., Abdel-Meguid S.S., Lim L.W., Shieh H.-S., Dayringer H.E.,
     Leimgruber N.K., Stegeman R.A., Anderson K.S., Sikorski J.A.,
     Padgette S.R., Kishore G.M.
     "Structure and topological symmetry of the glyphosate target
     5-enolpyruvylshikimate-3-phosphate synthase: a distinctive protein
     fold."
     Proc. Natl. Acad. Sci. U.S.A. 88:5046-5050(1991).
     PubMed=11607190;
[ 2] Padgette S.R., Re D.B., Gaser C.S., Eicholtz D.A., Frazier R.B.,
     Hironaka C.M., Levine E.B., Shah D.M., Fraley R.T., Kishore G.M.
     "Site-directed mutagenesis of a conserved region of the
     5-enolpyruvylshikimate-3-phosphate synthase active site."
     J. Biol. Chem. 266:22364-22369(1991).
     PubMed=1939260;

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