Reviewed, UniProtKB/Swiss-Prot P22634 (MURI_ECOLI)

Names and origin

Protein names

Recommended name:
    Glutamate racemase
    EC=5.1.1.3

Gene names

Name:	murI
Synonyms:	dga, glr, yijA
Ordered Locus Names:	b3967, JW5550

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	285 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Provides the (R)-glutamate required for cell wall biosynthesis. HAMAP MF_00258
Catalytic activity	L-glutamate = D-glutamate. HAMAP MF_00258
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00258
Sequence similarities	Belongs to the aspartate/glutamate racemases family.

Ontologies

Keywords
Biological process	Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Molecular function	Isomerase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: HAMAP regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	glutamate racemase activity Inferred from electronic annotation. Source: HAMAP protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
tufA	P0A6N1	1	EBI-554903,EBI-301077

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 285

285

Glutamate racemase HAMAP MF_00258

PRO_0000095470

Secondary structure

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285

Helix Strand Turn

Details...

Beta strand

21 – 28

8

Helix

35 – 43

9

Beta strand

47 – 53

7

Turn

55 – 57

3

Helix

65 – 82

18

Beta strand

86 – 90

5

Helix

93 – 106

14

Helix

118 – 124

7

Helix

142 – 150

9

Beta strand

157 – 160

4

Helix

163 – 173

11

Helix

180 – 186

7

Helix

188 – 191

4

Beta strand

198 – 201

4

Helix

207 – 210

4

Helix

211 – 217

7

Beta strand

223 – 225

3

Helix

230 – 241

12

Beta strand

253 – 258

6

Helix

264 – 266

3

Helix

267 – 272

6

Beta strand

277 – 280

4

Sequences

	Sequence		Length	Mass (Da)
	P22634-1 [UniParc]. Last modified February 1, 1995. Version 2. Checksum: EC87281B577B8E93	FASTA	285	31,002
	10 20 30 40 50 60 MATKLQDGNT PCLAATPSEP RPTVLVFDSG VGGLSVYDEI RHLLPDLHYI YAFDNVAFPY 70 80 90 100 110 120 GEKSEAFIVE RVVAIVTAVQ ERYPLALAVV ACNTASTVSL PALREKFDFP VVGVVPAIKP 130 140 150 160 170 180 AARLTANGIV GLLATRGTVK RSYTHELIAR FANECQIEML GSAEMVELAE AKLHGEDVSL 190 200 210 220 230 240 DALKRILRPW LRMKEPPDTV VLGCTHFPLL QEELLQVLPE GTRLVDSGAA IARRTAWLLE 250 260 270 280 HEAPDAKSAD ANIAFCMAMT PGAEQLLPVL QRYGFETLEK LAVLG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Gene organization and primary structure of a ribosomal RNA operon from Escherichia coli." Brosius J., Dull T.J., Sleeter D.D., Noller H.F. J. Mol. Biol. 148:107-127(1981) [PubMed: 7028991] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Identification of two new promoters probably involved in the transcription of a ribosomal RNA gene of Escherichia coli." Boros I., Csordas-Toth E., Kiss A., Kiss I., Toeroek I., Udvardy A., Udvardy K., Venetianer P. Biochim. Biophys. Acta 739:173-180(1983) [PubMed: 6297582] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The Escherichia coli mutant requiring D-glutamic acid is the result of mutations in two distinct genetic loci." Dougherty T.J., Thanassi J.A., Pucci M.J. J. Bacteriol. 175:111-116(1993) [PubMed: 8093236] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: B.
[4]	"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L. Nucleic Acids Res. 21:5408-5417(1993) [PubMed: 8265357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[6]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"Identification of the Escherichia coli murI gene, which is required for the biosynthesis of D-glutamic acid, a specific component of bacterial peptidoglycan." Doublet P., van Heijenoort J., Mengin-Lecreulx D. J. Bacteriol. 174:5772-5779(1992) [PubMed: 1355768] [Abstract] Cited for: CHARACTERIZATION. Strain: K12.
[8]	"The murI gene of Escherichia coli is an essential gene that encodes a glutamate racemase activity." Doublet P., van Heijenoort J., Bohin J.-P., Mengin-Lecreulx D. J. Bacteriol. 175:2970-2979(1993) [PubMed: 8098327] [Abstract] Cited for: CHARACTERIZATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V00348 Genomic DNA. Translation: CAA23638.1. Different initiation.
V00347 Genomic DNA. Translation: CAA23637.1. Different initiation.
L14556 Genomic DNA. Translation: AAA23677.1. Different initiation.
U00006 Genomic DNA. Translation: AAC43073.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76949.1. Different initiation.
AP009048 Genomic DNA. Translation: BAE77344.1.

PIR

I41187.

RefSeq

AP_003843.1.
NP_418402.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JFN	X-ray	1.90	A	1-285	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10283N.

IntAct

P22634. 5 interactions.

STRING

P22634.

Genome annotation databases

GeneID

948467.

GenomeReviews

Gene locus JW5550 in contig AP009048_GR.
Gene locus b3967 in contig U00096_GR.

KEGG

ecj:JW5550.
eco:b3967.

Organism-specific databases

EchoBASE

EB1189.

EcoGene

EG11204. murI.

CMR

Search...

Phylogenomic databases

eggNOG

COG0796.

HOGENOM

HBG645102.

OMA

VITQPCP.

Enzyme and pathway databases

BioCyc

EcoCyc:GLUTRACE-MONOMER.
ECOL168927:B3967-MONOMER.
MetaCyc:GLUTRACE-MONOMER.

Gene expression databases

Genevestigator

P22634.

Family and domain databases

HAMAP

MF_00258. Glu_racemase.
[Tree]

InterPro

IPR015942. Asp/Glu/hydantoin_racemase.
IPR001920. Asp/Glu_race.
IPR018187. Asp/Glu_racemase_AS.
IPR004391. Glu_race.
[Graphical view]

Gene3D

G3DSA:3.40.50.1860. Asp/Glu_race. 1 hit.

Pfam

PF01177. Asp_Glu_race. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00067. glut_race. 1 hit.

PROSITE

PS00923. ASP_GLU_RACEMASE_1. 1 hit.
PS00924. ASP_GLU_RACEMASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

MURI_ECOLI

Accession

Primary (citable) accession number: P22634
Secondary accession number(s): P78133, Q2M8R2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	February 1, 1995
Last modified:	February 9, 2010
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)