PROSITE logo

PROSITE documentation PDOC00527

View entry in NiceDoc format
View entry in raw text format (no links)
{PDOC00527}
{PS00370; PEP_ENZYMES_PHOS_SITE}
{PS00742; PEP_ENZYMES_2}
{BEGIN}
************************************
* PEP-utilizing enzymes signatures *
************************************

A number of enzymes that catalyze  the  transfer  of  a  phosphoryl group from
phosphoenolpyruvate (PEP) via a phospho-histidine intermediate have been shown
to be structurally related [1,2,3,4]. These enzymes are:

 - Pyruvate,orthophosphate  dikinase (EC 2.7.9.1)  (PPDK).  PPDK catalyzes the
   reversible phosphorylation  of  pyruvate  and  phosphate  by ATP to PEP and
   diphosphate. In  plants PPDK function  in the direction of the formation of
   PEP, which is the primary acceptor of carbon dioxide in C4 and crassulacean
   acid metabolism plants.  In  some  bacteria, such as Bacteroides symbiosus,
   PPDK functions in the direction of ATP synthesis.
 - Phosphoenolpyruvate  synthase (EC 2.7.9.2) (pyruvate,water dikinase).  This
   enzyme catalyzes the reversible  phosphorylation of pyruvate by ATP to form
   PEP, AMP and phosphate, an essential step in gluconeogenesis when  pyruvate
   and lactate are used as a carbon source.
 - Phosphoenolpyruvate-protein  phosphatase  (EC 2.7.3.9).  This is  the first
   enzyme of the phosphoenolpyruvate-dependent sugar phosphotransferase system
   (PTS), a major carbohydrate transport system in bacteria. The PTS catalyzes
   the phosphorylation  of incoming  sugar substrates  concomitant with  their
   translocation across the cell membrane. The general mechanism of the PTS is
   the following: a phosphoryl group  from PEP is transferred to enzyme-I (EI)
   of PTS which in  turn transfers  it to a phosphoryl  carrier protein (HPr).
   Phospho-HPr  then  transfers  the  phosphoryl  group  to  a  sugar-specific
   permease.

All these enzymes share  the  same  catalytic  mechanism:  they  bind  PEP and
transfer the phosphoryl  group  from it  to a histidine residue.  The sequence
around that residue is highly conserved and can be used as a signature pattern
for  these enzymes.  As  a  second  signature  pattern we selected a conserved
region in the C-terminal part  of  the  PEP-utilizing enzymes.  The biological
significance of this region is not yet known.

-Consensus pattern: G-[GA]-x-[STN]-x-H-[STA]-[STAV]-[LIVM](2)-[STAV]-[RG]
                    [H is phosphorylated]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Consensus pattern: [DEQSKN]-x-[LIVMF]-[SA]-[LIVMF]-G-[ST]-N-D-[LIVM]-x-Q-
                    [LIVMFYGT]-[STALIV]-[LIVMFY]-[GAS]-x(2)-R
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

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

[ 1] Reizer J., Hoischen C., Reizer A., Pham T.N., Saier M.H. Jr.
     "Sequence analyses and evolutionary relationships among the
     energy-coupling proteins Enzyme I and HPr of the bacterial
     phosphoenolpyruvate: sugar phosphotransferase system."
     Protein Sci. 2:506-521(1993).
     PubMed=7686067
[ 2] Reizer J., Reizer A., Merrick M.J., Plunkett G. III, Rose D.J.,
     Saier M.H. Jr.
     "Novel phosphotransferase-encoding genes revealed by analysis of the
     Escherichia coli genome: a chimeric gene encoding an Enzyme I
     homologue that possesses a putative sensory transduction domain."
     Gene 181:103-108(1996).
     PubMed=8973315
[ 3] Pocalyko D.J., Carroll L.J., Martin B.M., Babbitt P.C.,
     Dunaway-Mariano D.
     "Analysis of sequence homologies in plant and bacterial pyruvate
     phosphate dikinase, enzyme I of the bacterial phosphoenolpyruvate:
     sugar phosphotransferase system and other PEP-utilizing enzymes.
     Identification of potential catalytic and regulatory motifs."
     Biochemistry 29:10757-10765(1990).
     PubMed=2176881
[ 4] Niersbach M., Kreuzaler F., Geerse R.H., Postma P.W., Hirsch H.J.
     "Cloning and nucleotide sequence of the Escherichia coli K-12 ppsA
     gene, encoding PEP synthase."
     Mol. Gen. Genet. 231:332-336(1992).
     PubMed=1310524

--------------------------------------------------------------------------------
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and
distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives
(CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html
--------------------------------------------------------------------------------

{END}