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InterPro: IPR018274 PEP-utilising enzyme, mobile region, conserved site

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2778 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession List
Matches in BioMart

Accession

IPR018274 PEP_mobile_CS

Type

Conserved_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS00370	PEP_ENZYMES_PHOS_SITE	2778
Signatures in BioMart

InterPro Relationships Help

Found in

IPR006318 Phosphoenolpyruvate-protein phosphotransferase
IPR006319 Phosphoenolpyruvate synthase
IPR008279 PEP-utilising enzyme, mobile domain
IPR010121 Pyruvate, phosphate dikinase

GO Term annotation Help

Process

GO:0016310 phosphorylation

Function

GO:0016772 transferase activity, transferring phosphorus-containing groups

InterPro annotation

Entry Details in BioMart

Abstract

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]. All these enzymes share the same catalytic mechanism: they bind PEP and transfer the phosphoryl group from it to a histidine residue. This domain is a "swivelling" beta/beta/alpha domain which is thought to be mobile in all proteins known to contain it [5]. It is often found associated with the pyruvate phosphate dikinase, PEP/pyruvate-binding domain (IPR002192) at its N terminus.

This entry represents a conserved site of the PEP-utilising enzyme.

Structural links Help

PDB - click here

SCOP: c.8.1.1 , c.8.1.2

CATH: 3.50.30.10

Database links Help

Enzyme: EC:2.7

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR018274

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O23404 Pyruvate, phosphate dikinase 1, chloroplastic

O27190 Probable phosphoenolpyruvate synthase

P08839 Phosphoenolpyruvate-protein phosphotransferase

Q55905 Phosphoenolpyruvate synthase

Q6AVA8 Pyruvate, phosphate dikinase 1, chloroplastic

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
IPR013816	ATP-grasp fold, subdomain 2
IPR000121	PEP-utilising enzyme
IPR002192	Pyruvate phosphate dikinase, PEP/pyruvate-binding
IPR006318	Phosphoenolpyruvate-protein phosphotransferase
IPR010121	Pyruvate, phosphate dikinase
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 Open in usermanual
1.	Reizer J, Hoischen C, Reizer A, Pham TN, Saier MH Jr. Sequence analyses and evolutionary relationships among the energy-coupling proteins Enzyme I and HPr of the bacterial phosphoenolpyruvate: sugar phosphotransferase system. Protein Sci. 2 506-21 1993 [PubMed: 7686067] http://www.proteinscience.org/cgi/content/abstract/2/4/506
2.	Reizer J, Reizer A, Merrick MJ, Plunkett G 3rd, Rose DJ, Saier MH 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 181 103-8 1996 [PubMed: 8973315] http://dx.doi.org/10.1016/S0378-1119(96)00481-7
3.	Pocalyko DJ, Carroll LJ, Martin BM, Babbitt PC, 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 10757-65 1990 [PubMed: 2176881] http://dx.doi.org/10.1021/bi00500a006
4.	Unternahrer S, Hinnen A. Temperature sensitivity of the cdc9-1 allele of Saccharomyces cerevisiae DNA ligase is dependent on specific combinations of amino acids in the primary structure of the expressed protein. Mol. Gen. Genet. 232 332-4 1992 [PubMed: 1557039]
5.	Cosenza LW, Bringaud F, Baltz T, Vellieux FM. The 3.0 A resolution crystal structure of glycosomal pyruvate phosphate dikinase from Trypanosoma brucei. J. Mol. Biol. 318 1417-32 2002 [PubMed: 12083528] http://dx.doi.org/10.1016/S0022-2836(02)00113-4

Additional Reading Open in usermanual
	Lin Y, Lusin JD, Ye D, Dunaway-Mariano D, Ames JB. Examination of the structure, stability, and catalytic potential in the engineered phosphoryl carrier domain of pyruvate phosphate dikinase. Biochemistry 45 2006 1702-11 [PubMed: 16460017] http://dx.doi.org/10.1021/bi051816l
	Niersbach M, Kreuzaler F, Geerse RH, Postma PW, Hirsch HJ. Cloning and nucleotide sequence of the Escherichia coli K-12 ppsA gene, encoding PEP synthase. Mol. Gen. Genet. 231 1992 332-6 [PubMed: 1310524]
	Lim K, Read RJ, Chen CC, Tempczyk A, Wei M, Ye D, Wu C, Dunaway-Mariano D, Herzberg O. Swiveling domain mechanism in pyruvate phosphate dikinase. Biochemistry 46 2007 14845-53 [PubMed: 18052212] http://dx.doi.org/10.1021/bi701848w
	Nakanishi T, Nakatsu T, Matsuoka M, Sakata K, Kato H. Crystal structures of pyruvate phosphate dikinase from maize revealed an alternative conformation in the swiveling-domain motion. Biochemistry 44 2005 1136-44 [PubMed: 15667207] http://dx.doi.org/10.1021/bi0484522
	Nakanishi T, Ohki Y, Oda J, Matsuoka M, Sakata K, Kato H. Purification, crystallization and preliminary X-ray diffraction studies on pyruvate phosphate dikinase from maize. Acta Crystallogr. D Biol. Crystallogr. 60 2004 193-4 [PubMed: 14684927]

InterPro 23.1