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InterPro: IPR004391 Glutamate racemase

Protein matches Help

UniProtKB

Matches:

1725 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

IPR004391 Glu_race

Type

Family

Signatures Help

Database	ID	Name	Proteins
HAMAP	MF_00258	Glu_race	1373
TIGRFAMs	TIGR00067	glut_race	1708
Signatures in BioMart

InterPro Relationships Help

Parent

IPR001920 Asp/Glu racemase

Contains

IPR018187 Asp/Glu racemase, active site

GO Term annotation Help

Process

GO:0009252 peptidoglycan biosynthetic process

Function

GO:0008881 glutamate racemase activity

InterPro annotation

Entry Details in BioMart

Abstract

Glutamate racemase (EC:5.1.1.3) provides the (R)-glutamic acid required for cell wall biosynthesis. It converts L-glutamate to D-glutamate during peptidoglycan biosynthesis. The most closely related proteins differing in function are aspartate racemases.

Structural links Help

PDB - click here

SCOP: c.78.2.1

CATH: 3.40.50.1860

Database links Help

Enzyme: EC:5.1.1.3

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004391

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A2C175 Glutamate racemase

P22634 Glutamate racemase

P73737 Glutamate racemase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001920	Asp/Glu racemase
IPR018187	Asp/Glu racemase, active site
IPR004391	Glutamate racemase
IPR015942	Asp/Glu/hydantoin racemase
	SWISS-MODEL
	PDB Chain
	ModBase

Publications Help

Additional Reading Open in usermanual
	May M, Mehboob S, Mulhearn DC, Wang Z, Yu H, Thatcher GR, Santarsiero BD, Johnson ME, Mesecar AD. Structural and functional analysis of two glutamate racemase isozymes from Bacillus anthracis and implications for inhibitor design. J. Mol. Biol. 371 2007 1219-37 [PubMed: 17610893] http://dx.doi.org/10.1016/j.jmb.2007.05.093
	Ruzheinikov SN, Taal MA, Sedelnikova SE, Baker PJ, Rice DW. Substrate-induced conformational changes in Bacillus subtilis glutamate racemase and their implications for drug discovery. Structure 13 2005 1707-13 [PubMed: 16271894] http://dx.doi.org/10.1016/j.str.2005.07.024
	Kim KH, Bong YJ, Park JK, Shin KJ, Hwang KY, Kim EE. Structural basis for glutamate racemase inhibition. J. Mol. Biol. 372 2007 434-43 [PubMed: 17658548] http://dx.doi.org/10.1016/j.jmb.2007.05.003
	Lundqvist T, Fisher SL, Kern G, Folmer RH, Xue Y, Newton DT, Keating TA, Alm RA, de Jonge BL. Exploitation of structural and regulatory diversity in glutamate racemases. Nature 447 2007 817-22 [PubMed: 17568739] http://dx.doi.org/10.1038/nature05689
	Taal MA, Sedelnikova SE, Ruzheinikov SN, Baker PJ, Rice DW. Expression, purification and preliminary X-ray analysis of crystals of Bacillus subtilis glutamate racemase. Acta Crystallogr. D Biol. Crystallogr. 60 2004 2031-4 [PubMed: 15502318] http://dx.doi.org/10.1107/S0907444904021134

InterPro 23.1