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Protein

Glutamate racemase

Gene

murI

Organism
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
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 annotation

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 sitei72 – 721Proton donor/acceptorUniRule annotationBy similarity
Active sitei183 – 1831Proton 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

BioCyciLMON169963:LMO1237-MONOMER.
UniPathwayiUPA00219.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate racemaseUniRule annotation (EC:5.1.1.3UniRule annotation)
Gene namesi
Name:murIUniRule annotation
Synonyms:racE
Ordered Locus Names:lmo1237
OrganismiListeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Taxonomic identifieri169963 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
Proteomesi
  • UP000000817 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 266266Glutamate racemasePRO_0000095487Add
BLAST

Proteomic databases

PaxDbiQ8Y7N7.

Interactioni

Protein-protein interaction databases

STRINGi169963.lmo1237.

Structurei

Secondary structure

1
266
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 128Combined sources
Helixi15 – 2410Combined sources
Beta strandi30 – 345Combined sources
Helixi36 – 383Combined sources
Helixi46 – 6217Combined sources
Beta strandi66 – 705Combined sources
Helixi73 – 8614Combined sources
Beta strandi91 – 944Combined sources
Helixi95 – 10511Combined sources
Beta strandi107 – 1159Combined sources
Helixi117 – 1226Combined sources
Helixi124 – 1329Combined sources
Beta strandi137 – 1426Combined sources
Helixi145 – 1517Combined sources
Helixi158 – 16811Combined sources
Helixi169 – 1735Combined sources
Beta strandi178 – 1814Combined sources
Helixi186 – 1894Combined sources
Helixi190 – 1978Combined sources
Beta strandi201 – 2044Combined sources
Helixi207 – 22014Combined sources
Beta strandi234 – 2396Combined sources
Helixi241 – 25212Combined sources
Beta strandi259 – 2613Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HFRX-ray2.30A/B1-266[»]
3ISTX-ray1.65A/B1-266[»]
3ISVX-ray1.85A/B1-266[»]
ProteinModelPortaliQ8Y7N7.
SMRiQ8Y7N7. Positions 3-265.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8Y7N7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni9 – 102Substrate bindingUniRule annotationBy similarity
Regioni41 – 422Substrate bindingUniRule annotationCombined sourcesBy similarity
Regioni73 – 742Substrate bindingUniRule annotationBy similarity
Regioni184 – 1852Substrate bindingUniRule annotationBy similarity

Sequence similaritiesi

Belongs to the aspartate/glutamate racemases family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105F03. Bacteria.
COG0796. LUCA.
HOGENOMiHOG000262396.
KOiK01776.
OMAiVYGCTHY.
OrthoDBiEOG6CZQQP.
PhylomeDBiQ8Y7N7.

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.

Q8Y7N7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKQAIGFIDS GVGGLTVVRE VLKQLPHEQV YYLGDTARCP YGPRDKEEVA
60 70 80 90 100
KFTWEMTNFL VDRGIKMLVI ACNTATAAAL YDIREKLDIP VIGVIQPGSR
110 120 130 140 150
AALKATRNNK IGVLGTLGTV ESMAYPTALK GLNRRVEVDS LACPKFVSVV
160 170 180 190 200
ESGEYKSAIA KKVVAESLLP LKSTKIDTVI LGCTHYPLLK PIIENFMGDG
210 220 230 240 250
VAVINSGEET ASEVSALLDY HNLLDATDEE IEHRFFTTGS TQIFKDIAKD
260
WLNMPDMTVE HIKLGK
Length:266
Mass (Da):29,160
Last modified:March 1, 2002 - v1
Checksum:i912A19482409991B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL591978 Genomic DNA. Translation: CAC99315.1.
PIRiAE1229.
RefSeqiNP_464762.1. NC_003210.1.
WP_003723856.1. NC_003210.1.

Genome annotation databases

EnsemblBacteriaiCAC99315; CAC99315; CAC99315.
GeneIDi986027.
KEGGilmo:lmo1237.
PATRICi20311583. VBILisMon69206_1269.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL591978 Genomic DNA. Translation: CAC99315.1.
PIRiAE1229.
RefSeqiNP_464762.1. NC_003210.1.
WP_003723856.1. NC_003210.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HFRX-ray2.30A/B1-266[»]
3ISTX-ray1.65A/B1-266[»]
3ISVX-ray1.85A/B1-266[»]
ProteinModelPortaliQ8Y7N7.
SMRiQ8Y7N7. Positions 3-265.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi169963.lmo1237.

Proteomic databases

PaxDbiQ8Y7N7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC99315; CAC99315; CAC99315.
GeneIDi986027.
KEGGilmo:lmo1237.
PATRICi20311583. VBILisMon69206_1269.

Phylogenomic databases

eggNOGiENOG4105F03. Bacteria.
COG0796. LUCA.
HOGENOMiHOG000262396.
KOiK01776.
OMAiVYGCTHY.
OrthoDBiEOG6CZQQP.
PhylomeDBiQ8Y7N7.

Enzyme and pathway databases

UniPathwayiUPA00219.
BioCyciLMON169963:LMO1237-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ8Y7N7.

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 BAA-679 / EGD-e.
  2. "Crystal structure of glutamate racemase from Listeria monocytogenes in complex with succinic acid."
    Majorek K.A., Chruszcz M., Skarina T., Onopriyenko O., Stam J., Anderson W.F., Savchenko A., Bujnicki J.M., Minor W.
    Submitted (AUG-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH SUCCINATE.

Entry informationi

Entry nameiMURI_LISMO
AccessioniPrimary (citable) accession number: Q8Y7N7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: March 1, 2002
Last modified: March 16, 2016
This is version 93 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.