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Protein

Glutamate racemase

Gene

murI

Organism
Enterococcus faecalis (strain ATCC 700802 / V583)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Provides the (R)-glutamate required for cell wall biosynthesis.UniRule annotation

Catalytic activityi

L-glutamate = D-glutamate.UniRule annotation2 Publications

Pathwayi: peptidoglycan biosynthesis

This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.UniRule annotation
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 sitei74 – 741Proton donor/acceptorUniRule annotationBy similarity
Active sitei185 – 1851Proton donor/acceptorUniRule annotationBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Enzyme and pathway databases

BioCyciEFAE226185:GHI1-1111-MONOMER.
BRENDAi5.1.1.3. 2095.
SABIO-RKQ836J0.
UniPathwayiUPA00219.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate racemaseUniRule annotation (EC:5.1.1.3UniRule annotation2 Publications)
Gene namesi
Name:murIUniRule annotation
Ordered Locus Names:EF_1121
OrganismiEnterococcus faecalis (strain ATCC 700802 / V583)
Taxonomic identifieri226185 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus
Proteomesi
  • UP000001415 Componenti: Chromosome

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5298.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 273273Glutamate racemasePRO_1000047564Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

DIPiDIP-60301N.
STRINGi226185.EF1121.

Chemistry

BindingDBiQ836J0.

Structurei

Secondary structure

1
273
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 43Combined sources
Beta strandi7 – 148Combined sources
Helixi17 – 2610Combined sources
Beta strandi32 – 365Combined sources
Turni38 – 403Combined sources
Helixi48 – 6316Combined sources
Turni64 – 663Combined sources
Beta strandi68 – 725Combined sources
Helixi75 – 8814Combined sources
Beta strandi93 – 975Combined sources
Helixi98 – 10710Combined sources
Beta strandi109 – 1179Combined sources
Helixi119 – 1235Combined sources
Helixi126 – 1327Combined sources
Beta strandi138 – 1447Combined sources
Helixi148 – 1536Combined sources
Helixi160 – 17011Combined sources
Helixi171 – 1733Combined sources
Turni174 – 1763Combined sources
Beta strandi179 – 1835Combined sources
Helixi188 – 1914Combined sources
Helixi192 – 1998Combined sources
Beta strandi204 – 2074Combined sources
Helixi208 – 22215Combined sources
Beta strandi237 – 2426Combined sources
Helixi244 – 25512Combined sources
Beta strandi262 – 2643Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JFOX-ray2.50A/B1-273[»]
2JFPX-ray1.98A/B1-273[»]
2VVTX-ray1.65A/B1-270[»]
ProteinModelPortaliQ836J0.
SMRiQ836J0. Positions 2-268.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ836J0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 122Substrate bindingUniRule annotationCombined sources2 Publications
Regioni43 – 442Substrate bindingUniRule annotationCombined sources2 Publications
Regioni75 – 762Substrate bindingUniRule annotationCombined sources2 Publications
Regioni186 – 1872Substrate bindingUniRule annotationCombined sources2 Publications

Sequence similaritiesi

Belongs to the aspartate/glutamate racemases family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105F03. Bacteria.
COG0796. LUCA.
KOiK01776.
OMAiVYGCTHY.
OrthoDBiEOG6CZQQP.

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.

Q836J0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNQEAIGLI DSGVGGLTVL KEALKQLPNE RLIYLGDTAR CPYGPRPAEQ
60 70 80 90 100
VVQFTWEMAD FLLKKRIKML VIACNTATAV ALEEIKAALP IPVVGVILPG
110 120 130 140 150
ARAAVKVTKN NKIGVIGTLG TIKSASYEIA IKSKAPTIEV TSLDCPKFVP
160 170 180 190 200
IVESNQYRSS VAKKIVAETL QALQLKGLDT LILGCTHYPL LRPVIQNVMG
210 220 230 240 250
SHVTLIDSGA ETVGEVSMLL DYFDIAHTPE APTQPHEFYT TGSAKMFEEI
260 270
ASSWLGIENL KAQQIHLGGN END
Length:273
Mass (Da):29,479
Last modified:June 1, 2003 - v1
Checksum:i1F2ADF4D0B93991D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016830 Genomic DNA. Translation: AAO80921.1.
RefSeqiNP_814851.1. NC_004668.1.
WP_010706575.1. NZ_KE136528.1.

Genome annotation databases

EnsemblBacteriaiAAO80921; AAO80921; EF_1121.
GeneIDi1200023.
KEGGiefa:EF1121.
PATRICi21852632. VBIEntFae7065_1047.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016830 Genomic DNA. Translation: AAO80921.1.
RefSeqiNP_814851.1. NC_004668.1.
WP_010706575.1. NZ_KE136528.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JFOX-ray2.50A/B1-273[»]
2JFPX-ray1.98A/B1-273[»]
2VVTX-ray1.65A/B1-270[»]
ProteinModelPortaliQ836J0.
SMRiQ836J0. Positions 2-268.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60301N.
STRINGi226185.EF1121.

Chemistry

BindingDBiQ836J0.
ChEMBLiCHEMBL5298.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO80921; AAO80921; EF_1121.
GeneIDi1200023.
KEGGiefa:EF1121.
PATRICi21852632. VBIEntFae7065_1047.

Phylogenomic databases

eggNOGiENOG4105F03. Bacteria.
COG0796. LUCA.
KOiK01776.
OMAiVYGCTHY.
OrthoDBiEOG6CZQQP.

Enzyme and pathway databases

UniPathwayiUPA00219.
BioCyciEFAE226185:GHI1-1111-MONOMER.
BRENDAi5.1.1.3. 2095.
SABIO-RKQ836J0.

Miscellaneous databases

EvolutionaryTraceiQ836J0.
PROiQ836J0.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700802 / V583.
  2. "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 (1.98 ANGSTROMS) IN COMPLEX WITH GLUTAMATE, CATALYTIC ACTIVITY, SUBUNIT.
  3. "Exploring 9-benzyl purines as inhibitors of glutamate racemase (MurI) in Gram-positive bacteria."
    Geng B., Breault G., Comita-Prevoir J., Petrichko R., Eyermann C., Lundqvist T., Doig P., Gorseth E., Noonan B.
    Bioorg. Med. Chem. Lett. 18:4368-4372(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-270 IN COMPLEX WITH D-GLUTAMATE, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiMURI_ENTFA
AccessioniPrimary (citable) accession number: Q836J0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 1, 2003
Last modified: June 8, 2016
This is version 88 of the entry and version 1 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.