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Protein

Glutamate racemase

Gene

murI

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Provides the (R)-glutamate required for cell wall biosynthesis.UniRule annotation1 Publication2 Publications

Catalytic activityi

L-glutamate = D-glutamate.UniRule annotation2 Publications

Enzyme regulationi

The low basal catalytic activity in increased 1000-fold in the presence of UDP-MurNAc-Ala, the product of the preceding enzyme in the peptidoglycan biosynthesis.1 Publication

Pathwayi: peptidoglycan biosynthesis

This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.UniRule annotation1 Publication2 Publications
View all proteins of this organism that are known to be involved in the pathway peptidoglycan biosynthesis and in Cell wall biogenesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei92 – 921Proton donor/acceptorUniRule annotationBy similarity
Binding sitei104 – 1041UDP-MurNAc-L-AlaCombined sources1 Publication
Active sitei204 – 2041Proton donor/acceptorUniRule annotationBy similarity

GO - Molecular functioni

  • glutamate racemase activity Source: EcoCyc

GO - Biological processi

  • cell wall organization Source: UniProtKB-KW
  • peptidoglycan biosynthetic process Source: EcoCyc
  • regulation of cell shape Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Enzyme and pathway databases

BioCyciEcoCyc:GLUTRACE-MONOMER.
ECOL316407:JW5550-MONOMER.
MetaCyc:GLUTRACE-MONOMER.
SABIO-RKP22634.
UniPathwayiUPA00219.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate racemase1 PublicationUniRule annotation (EC:5.1.1.3UniRule annotation2 Publications)
Gene namesi
Name:murI2 PublicationsUniRule annotation
Synonyms:dga, glr, yijA
Ordered Locus Names:b3967, JW5550
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11204. murI.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 285285Glutamate racemasePRO_0000095470Add
BLAST

Proteomic databases

PaxDbiP22634.
PRIDEiP22634.

Interactioni

Subunit structurei

Monomer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
tufAP0CE471EBI-554903,EBI-301077

Protein-protein interaction databases

BioGridi4259606. 249 interactions.
DIPiDIP-10283N.
IntActiP22634. 13 interactions.
MINTiMINT-1222611.
STRINGi511145.b3967.

Structurei

Secondary structure

1
285
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi21 – 3111Combined sources
Helixi33 – 4311Combined sources
Beta strandi47 – 537Combined sources
Turni55 – 573Combined sources
Turni60 – 623Combined sources
Helixi65 – 8218Combined sources
Beta strandi86 – 905Combined sources
Helixi93 – 10614Combined sources
Helixi118 – 1247Combined sources
Beta strandi126 – 1349Combined sources
Helixi138 – 1403Combined sources
Helixi142 – 1509Combined sources
Beta strandi155 – 1617Combined sources
Helixi163 – 17311Combined sources
Helixi180 – 1867Combined sources
Helixi188 – 1914Combined sources
Beta strandi198 – 2025Combined sources
Helixi207 – 2104Combined sources
Helixi211 – 2177Combined sources
Beta strandi223 – 2253Combined sources
Helixi228 – 24114Combined sources
Beta strandi253 – 2586Combined sources
Helixi261 – 2644Combined sources
Helixi267 – 2726Combined sources
Beta strandi277 – 2804Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JFNX-ray1.90A1-285[»]
ProteinModelPortaliP22634.
SMRiP22634. Positions 20-285.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22634.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni28 – 292Substrate bindingUniRule annotationCombined sources1 Publication
Regioni60 – 612Substrate bindingUniRule annotationCombined sources1 Publication
Regioni93 – 942Substrate bindingUniRule annotationCombined sources1 Publication
Regioni113 – 1197UDP-MurNAc-Ala bindingCombined sources1 Publication
Regioni205 – 2062Substrate bindingUniRule annotationCombined sources1 Publication

Sequence similaritiesi

Belongs to the aspartate/glutamate racemases family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105F03. Bacteria.
COG0796. LUCA.
HOGENOMiHOG000262397.
InParanoidiP22634.
KOiK01776.
OMAiVYGCTHY.
OrthoDBiEOG6B6296.
PhylomeDBiP22634.

Family and domain databases

Gene3Di3.40.50.1860. 1 hit.
HAMAPiMF_00258. Glu_racemase.
InterProiIPR015942. Asp/Glu/hydantoin_racemase.
IPR001920. Asp/Glu_race.
IPR018187. Asp/Glu_racemase_AS_1.
IPR033134. Asp/Glu_racemase_AS_2.
IPR004391. Glu_race.
[Graphical view]
PfamiPF01177. Asp_Glu_race. 1 hit.
[Graphical view]
SUPFAMiSSF53681. SSF53681. 2 hits.
TIGRFAMsiTIGR00067. glut_race. 1 hit.
PROSITEiPS00923. ASP_GLU_RACEMASE_1. 1 hit.
PS00924. ASP_GLU_RACEMASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P22634-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATKLQDGNT PCLAATPSEP RPTVLVFDSG VGGLSVYDEI RHLLPDLHYI
60 70 80 90 100
YAFDNVAFPY GEKSEAFIVE RVVAIVTAVQ ERYPLALAVV ACNTASTVSL
110 120 130 140 150
PALREKFDFP VVGVVPAIKP AARLTANGIV GLLATRGTVK RSYTHELIAR
160 170 180 190 200
FANECQIEML GSAEMVELAE AKLHGEDVSL DALKRILRPW LRMKEPPDTV
210 220 230 240 250
VLGCTHFPLL QEELLQVLPE GTRLVDSGAA IARRTAWLLE HEAPDAKSAD
260 270 280
ANIAFCMAMT PGAEQLLPVL QRYGFETLEK LAVLG
Length:285
Mass (Da):31,002
Last modified:February 1, 1995 - v2
Checksum:iEC87281B577B8E93
GO

Sequence cautioni

The sequence AAA23677.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAC43073.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA23637.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA23638.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiI41187.
RefSeqiNP_418402.2. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC76949; AAC76949; b3967.
BAE77344; BAE77344; BAE77344.
GeneIDi948467.
KEGGiecj:JW5550.
eco:b3967.
PATRICi32123455. VBIEscCol129921_4088.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiI41187.
RefSeqiNP_418402.2. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JFNX-ray1.90A1-285[»]
ProteinModelPortaliP22634.
SMRiP22634. Positions 20-285.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259606. 249 interactions.
DIPiDIP-10283N.
IntActiP22634. 13 interactions.
MINTiMINT-1222611.
STRINGi511145.b3967.

Proteomic databases

PaxDbiP22634.
PRIDEiP22634.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76949; AAC76949; b3967.
BAE77344; BAE77344; BAE77344.
GeneIDi948467.
KEGGiecj:JW5550.
eco:b3967.
PATRICi32123455. VBIEscCol129921_4088.

Organism-specific databases

EchoBASEiEB1189.
EcoGeneiEG11204. murI.

Phylogenomic databases

eggNOGiENOG4105F03. Bacteria.
COG0796. LUCA.
HOGENOMiHOG000262397.
InParanoidiP22634.
KOiK01776.
OMAiVYGCTHY.
OrthoDBiEOG6B6296.
PhylomeDBiP22634.

Enzyme and pathway databases

UniPathwayiUPA00219.
BioCyciEcoCyc:GLUTRACE-MONOMER.
ECOL316407:JW5550-MONOMER.
MetaCyc:GLUTRACE-MONOMER.
SABIO-RKP22634.

Miscellaneous databases

EvolutionaryTraceiP22634.
PROiP22634.

Family and domain databases

Gene3Di3.40.50.1860. 1 hit.
HAMAPiMF_00258. Glu_racemase.
InterProiIPR015942. Asp/Glu/hydantoin_racemase.
IPR001920. Asp/Glu_race.
IPR018187. Asp/Glu_racemase_AS_1.
IPR033134. Asp/Glu_racemase_AS_2.
IPR004391. Glu_race.
[Graphical view]
PfamiPF01177. Asp_Glu_race. 1 hit.
[Graphical view]
SUPFAMiSSF53681. SSF53681. 2 hits.
TIGRFAMsiTIGR00067. glut_race. 1 hit.
PROSITEiPS00923. ASP_GLU_RACEMASE_1. 1 hit.
PS00924. ASP_GLU_RACEMASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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, PATHWAY, FUNCTION.
    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, PATHWAY, FUNCTION, CATALYTIC ACTIVITY.
  9. "Exploitation of structural and regulatory diversity in glutamate racemases."
    Lundqvist T., Fisher S.L., Kern G., Folmer R.H., Xue Y., Newton D.T., Keating T.A., Alm R.A., de Jonge B.L.
    Nature 447:817-822(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH GLUTAMATE AND UDP-N-ACETYL-ALPHA-D-MURAMOYL-L-ALANINE, FUNCTION, PATHWAY, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT.

Entry informationi

Entry nameiMURI_ECOLI
AccessioniPrimary (citable) accession number: P22634
Secondary accession number(s): P78133, Q2M8R2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: February 1, 1995
Last modified: March 16, 2016
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.