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B0SKQ2 (SYE_LEPBP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate--tRNA ligase

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Ordered Locus Names:LEPBI_I0677
OrganismLeptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris) [Complete proteome] [HAMAP]
Taxonomic identifier456481 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length517 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) By similarity. HAMAP-Rule MF_00022

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00022

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00022

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00022.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglutamyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 517517Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367700

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif250 – 2545"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1071Zinc By similarity
Metal binding1091Zinc By similarity
Metal binding1341Zinc By similarity
Metal binding1361Zinc By similarity
Binding site2531ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B0SKQ2 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 01F51E9F307E26D0

FASTA51758,314
        10         20         30         40         50         60 
MTEVRTRFAP SPSGFLHVGG ARTALFNYLY AKAKKGKFLL RIEDTDQDRS TEASFKIILE 

        70         80         90        100        110        120 
SLKWLGMEWD EGPGVGGPNG PYTQSERIHI YKEYTDKLIQ EKKAYRCFCT AEELEGKKKQ 

       130        140        150        160        170        180 
ADAMGIPYIY DGKCSDLSDA EIGSQLEKKI PFTVRFKTPH KIVIVDDMIQ GKVKFESKLI 

       190        200        210        220        230        240 
GDFIIVKSDG FPSYNYAVVI DDALMKITHV IRGVGHLSNT PRQILIFEAF GFPLPRFAHA 

       250        260        270        280        290        300 
SEIVGTDGKK LSKRAGATSV LAFRDLGYSS ETMRNYMALL GWTSPDGKEY MSDEELCSVF 

       310        320        330        340        350        360 
DVERCSKSPA TFDVFKKLKE EEKESVDFNK LTILGLAEYL NPKSKLNWMS NKYIRDTKIE 

       370        380        390        400        410        420 
TLGKALEPFL KDCQIPEAFK SGENPQLLSI LDSVRVYLDR LIQAPPYIEE FFLENLSFEN 

       430        440        450        460        470        480 
DEAKQLVLEG KGKEVVAEFY RIVKESSLTT PDAYKESMAK VGEITGEKGR TLFMPIRAIT 

       490        500        510 
TGKSHGLELP ILFSLLGQEK MVKRMEQLAG ILGISLR 

« Hide

References

[1]"Genome sequence of the saprophyte Leptospira biflexa provides insights into the evolution of Leptospira and the pathogenesis of leptospirosis."
Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N., Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A., Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L., Rood J.I., Lajus A. expand/collapse author list , Davies J.K., Medigue C., Adler B.
PLoS ONE 3:E1607-E1607(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Patoc 1 / ATCC 23582 / Paris.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000786 Genomic DNA. Translation: ABZ96809.1.
RefSeqYP_001838085.1. NC_010602.1.

3D structure databases

ProteinModelPortalB0SKQ2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING456481.LEPBI_I0677.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABZ96809; ABZ96809; LEPBI_I0677.
GeneID6224229.
KEGGlbi:LEPBI_I0677.
PATRIC22348068. VBILepBif123590_0682.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMAHHAPVVR.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycLBIF456481:GCM0-672-MONOMER.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-ligase_bac/mito.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. SSF48163. 1 hit.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_LEPBP
AccessionPrimary (citable) accession number: B0SKQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
Last modified: February 19, 2014
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries