Home  |  Contact
PROSITE documentation PDOC00527 [for PROSITE entry PS00370]

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 (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 (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 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.

Last update:

December 2004 / Pattern and text revised.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

PEP_ENZYMES_PHOS_SITE, PS00370; PEP-utilizing enzymes phosphorylation site signature  (PATTERN)

PEP_ENZYMES_2, PS00742; PEP-utilizing enzymes signature 2  (PATTERN)


1AuthorsReizer J. Hoischen C. Reizer A. Pham T.N. Saier M.H. Jr.
TitleSequence analyses and evolutionary relationships among the energy-coupling proteins Enzyme I and HPr of the bacterial phosphoenolpyruvate: sugar phosphotransferase system.
SourceProtein Sci. 2:506-521(1993).
PubMed ID7686067

2AuthorsReizer J. Reizer A. Merrick M.J. Plunkett G. III Rose D.J. Saier M.H. Jr.
TitleNovel 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.
SourceGene 181:103-108(1996).
PubMed ID8973315

3AuthorsPocalyko D.J. Carroll L.J. Martin B.M. Babbitt P.C. Dunaway-Mariano D.
TitleAnalysis 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.
SourceBiochemistry 29:10757-10765(1990).
PubMed ID2176881

4AuthorsNiersbach M. Kreuzaler F. Geerse R.H. Postma P.W. Hirsch H.J.
TitleCloning and nucleotide sequence of the Escherichia coli K-12 ppsA gene, encoding PEP synthase.
SourceMol. Gen. Genet. 231:332-336(1992).
PubMed ID1310524

PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.


View entry in original PROSITE document format
View entry in raw text format (no links)