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InterPro: IPR005952 Phosphoglycerate mutase 1

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UniProtKB

Matches:

1477 proteins

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

Accession

IPR005952 Phosphogly_mut1

Type

Family

Signatures Help

Database	ID	Name	Proteins
HAMAP	MF_01039	Phosphogly_mut1	1064
PANTHER	PTHR11931	Phosphogly_mut1	1461
TIGRFAMs	TIGR01258	pgm_1	1404
Signatures in BioMart

InterPro Relationships Help

Contains

IPR001345 Phosphoglycerate/bisphosphoglycerate mutase, active site
IPR013078 Phosphoglycerate mutase

GO Term annotation Help

Process

GO:0006096 glycolysis

Function

GO:0016868 intramolecular transferase activity, phosphotransferases

InterPro annotation

Entry Details in BioMart

Abstract

Most members of this family are phosphoglycerate mutase (EC:5.4.2.1). This enzyme interconverts 2-phosphoglycerate and 3-phosphoglycerate.

2-phospho-D-glycerate + 2,3-diphosphoglycerate = 3-phospho-D-glycerate + 2,3-diphosphoglycerate.

The enzyme is transiently phosphorylated on an active site histidine by 2,3-diphosphoglyerate, which is both substrate and product. Some members of this family have are phosphoglycerate mutase as a minor activity and act primarily as a bisphoglycerate mutase, interconverting 2,3-diphosphoglycerate and 1,3-diphosphoglycerate (EC:5.4.2.4).

Structural links Help

PDB - click here

SCOP: c.60.1.1

CATH: 3.40.50.1240

Database links Help

Enzyme: EC:5.4.2.1

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR005952

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O70250 Phosphoglycerate mutase 2

P00950 Phosphoglycerate mutase 1

P07738 Bisphosphoglycerate mutase

P07952 Bisphosphoglycerate mutase

P0A5R6 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013078	Phosphoglycerate mutase
IPR001345	Phosphoglycerate/bisphosphoglycerate mutase, active site
IPR005952	Phosphoglycerate mutase 1
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Help

Additional Reading Open in usermanual
	Wang Y, Liu L, Wei Z, Cheng Z, Lin Y, Gong W. Seeing the process of histidine phosphorylation in human bisphosphoglycerate mutase. J. Biol. Chem. 281 2006 39642-8 [PubMed: 17052986] http://dx.doi.org/10.1074/jbc.M606421200
	Wang Y, Wei Z, Liu L, Cheng Z, Lin Y, Ji F, Gong W. Crystal structure of human B-type phosphoglycerate mutase bound with citrate. Biochem. Biophys. Res. Commun. 331 2005 1207-15 [PubMed: 15883004] http://dx.doi.org/10.1016/j.bbrc.2005.03.243
	Bond CS, White MF, Hunter WN. Mechanistic implications for Escherichia coli cofactor-dependent phosphoglycerate mutase based on the high-resolution crystal structure of a vanadate complex. J. Mol. Biol. 316 2002 1071-81 [PubMed: 11884145] http://dx.doi.org/10.1006/jmbi.2002.5418
	Wang Y, Wei Z, Bian Q, Cheng Z, Wan M, Liu L, Gong W. Crystal structure of human bisphosphoglycerate mutase. J. Biol. Chem. 279 2004 39132-8 [PubMed: 15258155] http://dx.doi.org/10.1074/jbc.M405982200
	Muller P, Sawaya MR, Pashkov I, Chan S, Nguyen C, Wu Y, Perry LJ, Eisenberg D. The 1.70 angstroms X-ray crystal structure of Mycobacterium tuberculosis phosphoglycerate mutase. Acta Crystallogr. D Biol. Crystallogr. 61 2005 309-15 [PubMed: 15735341] http://dx.doi.org/10.1107/S0907444904033190
	Heinisch JJ, Muller S, Schluter E, Jacoby J, Rodicio R. Investigation of two yeast genes encoding putative isoenzymes of phosphoglycerate mutase. Yeast 14 1998 203-13 [PubMed: 9544241] http://dx.doi.org/10.1002/(SICI)1097-0061(199802)14:3<203::AID-YEA205>3.3.CO;2-#

InterPro 23.1