Glutamate racemase - Escherichia coli (strain K12)

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P22634 (MURI_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 125. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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) [Reference 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-Rule MF_00258
Catalytic activity	L-glutamate = D-glutamate. HAMAP-Rule MF_00258
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP-Rule MF_00258
Sequence similarities	Belongs to the aspartate/glutamate racemases family.
Sequence caution	The sequence AAA23677.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence AAC43073.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAA23637.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAA23638.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Molecular function	Isomerase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
tufA	P0CE47	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-Rule MF_00258

PRO_0000095470

Secondary structure

285

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P22634 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: EC87281B577B8E93
Show »

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

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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: AAC76949.2.
AP009048 Genomic DNA. Translation: BAE77344.1.

PIR

I41187.

RefSeq

NP_418402.2. NC_000913.2.
YP_491485.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

P22634.

SMR

P22634. Positions 20-285.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10283N.

IntAct

P22634. 5 interactions.

MINT

MINT-1222611.

STRING

511145.b3967.

Proteomic databases

PaxDb

P22634.

PRIDE

P22634.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76949; AAC76949; b3967.
BAE77344; BAE77344; BAE77344.

GeneID

12930612.
948467.

KEGG

ecj:Y75_p3221.
eco:b3967.

PATRIC

32123455. VBIEscCol129921_4088.

Organism-specific databases

EchoBASE

EB1189.

EcoGene

EG11204. murI.

Phylogenomic databases

eggNOG

COG0796.

HOGENOM

HOG000262397.

K01776.

OMA

VIMACNT.

ProtClustDB

PRK00865.

Enzyme and pathway databases

BioCyc

EcoCyc:GLUTRACE-MONOMER.
ECOL316407:JW5550-MONOMER.
MetaCyc:GLUTRACE-MONOMER.

SABIO-RK

P22634.

UniPathway

UPA00219.

Gene expression databases

Genevestigator

P22634.

Family and domain databases

Gene3D

3.40.50.1860. 1 hit.

HAMAP

MF_00258. Glu_racemase.

InterPro

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

PANTHER

PTHR21198. PTHR21198. 1 hit.

Pfam

PF01177. Asp_Glu_race. 1 hit.
[Graphical view]

SUPFAM

SSF53681. Asp/Glu_race. 2 hits.

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...

Other

EvolutionaryTrace

P22634.

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:	May 1, 2013
This is version 125 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents