EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR006318 Phosphoenolpyruvate-protein phosphotransferase

Protein matches Help

UniProtKB

Matches:

2314 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR006318 PEP_P_trans

Type

Domain

Signatures Help

Database	ID	Name	Proteins
PRINTS	PR01736	PHPHTRNFRASE	2307
TIGRFAMs	TIGR01417	PTS_I_fam	2058
Signatures in BioMart

InterPro Relationships Help

Found in

IPR000121 PEP-utilising enzyme
IPR006319 Phosphoenolpyruvate synthase
IPR015813 Pyruvate/Phosphoenolpyruvate kinase, catalytic core

Contains

IPR008279 PEP-utilising enzyme, mobile domain
IPR008731 Phosphotransferase system, PEP-utilising enzyme, N-terminal
IPR018274 PEP-utilising enzyme, mobile region, conserved site

GO Term annotation Help

Function

GO:0016772 transferase activity, transferring phosphorus-containing groups

InterPro annotation

Entry Details in BioMart

Abstract

These sequences are a distinct clade of phophoenolpyruvate (PEP)-dependent enzymes. Most members are known or deduced to function as the phosphoenolpyruvate-protein phosphotransferase (or enzyme I) of PTS sugar transport systems. However, some species with both a member of this family and a homologue of the phosphocarrier protein HPr lack a IIC component able to serve as a permease. An HPr homologue designated NPr has been implicated in the regulation of nitrogen assimilation, which demonstrates that not all phosphotransferase system components are associated directly with PTS transport.

Structural links Help

PDB - click here

SCOP: a.60.10.1 , c.8.1.2

CATH: 1.10.274.10 , 3.20.20.60 , 3.50.30.10

Database links Help

Enzyme: EC:2.7.3.9

Blocks: IPB006318

PRIAM: PRI001401

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006318

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O29548 Probable phosphoenolpyruvate synthase

P08839 Phosphoenolpyruvate-protein phosphotransferase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR008731	Phosphotransferase system, PEP-utilising enzyme, N-terminal
IPR013815	ATP-grasp fold, subdomain 1
IPR000121	PEP-utilising enzyme
IPR002192	Pyruvate phosphate dikinase, PEP/pyruvate-binding
IPR006318	Phosphoenolpyruvate-protein phosphotransferase
IPR008279	PEP-utilising enzyme, mobile domain
IPR018274	PEP-utilising enzyme, mobile region, conserved site
IPR006319	Phosphoenolpyruvate synthase
IPR015813	Pyruvate/Phosphoenolpyruvate kinase, catalytic core
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Help

Additional Reading Open in usermanual
	Garrett DS, Seok YJ, Peterkofsky A, Gronenborn AM, Clore GM. Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr. Nat. Struct. Biol. 6 1999 166-73 [PubMed: 10048929] http://dx.doi.org/10.1038/5854
	Liao DI, Silverton E, Seok YJ, Lee BR, Peterkofsky A, Davies DR. The first step in sugar transport: crystal structure of the amino terminal domain of enzyme I of the E. coli PEP: sugar phosphotransferase system and a model of the phosphotransfer complex with HPr. Structure 4 1996 861-72 [PubMed: 8805571] http://dx.doi.org/10.1016/S0969-2126(96)00092-5
	Tjandra N, Garrett DS, Gronenborn AM, Bax A, Clore GM. Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy. Nat. Struct. Biol. 4 1997 443-9 [PubMed: 9187651] http://dx.doi.org/10.1038/nsb0697-443
	Garrett DS, Seok YJ, Liao DI, Peterkofsky A, Gronenborn AM, Clore GM. Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR. Biochemistry 36 1997 2517-30 [PubMed: 9054557] http://dx.doi.org/10.1021/bi962924y
	Saffen DW, Presper KA, Doering TL, Roseman S. Sugar transport by the bacterial phosphotransferase system. Molecular cloning and structural analysis of the Escherichia coli ptsH, ptsI, and crr genes. J. Biol. Chem. 262 1987 16241-53 [PubMed: 2960675] http://intl.jbc.org/cgi/content/abstract/262/33/16241
	Oberholzer AE, Bumann M, Schneider P, Bachler C, Siebold C, Baumann U, Erni B. Crystal structure of the phosphoenolpyruvate-binding enzyme I-domain from the Thermoanaerobacter tengcongensis PEP: sugar phosphotransferase system (PTS). J. Mol. Biol. 346 2005 521-32 [PubMed: 15670601] http://dx.doi.org/10.1016/j.jmb.2004.11.077
	Ginsburg A, Peterkofsky A. Enzyme I: the gateway to the bacterial phosphoenolpyruvate:sugar phosphotransferase system. Arch. Biochem. Biophys. 397 2002 273-8 [PubMed: 11795882] http://dx.doi.org/10.1006/abbi.2001.2603
	Higa F, Edelstein PH. Potential virulence role of the Legionella pneumophila ptsP ortholog. Infect. Immun. 69 2001 4782-9 [PubMed: 11447151] http://dx.doi.org/10.1128/IAI.69.8.4782-4789.2001

InterPro 24.0