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B5RRI1 (SYE_BORRA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 43. 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:BRE_371
OrganismBorrelia recurrentis (strain A1) [Complete proteome] [HAMAP]
Taxonomic identifier412418 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorrelia

Protein attributes

Sequence length506 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 – 506506Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367620

Regions

Motif24 – 3411"HIGH" region HAMAP-Rule MF_00022
Motif266 – 2705"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1211Zinc By similarity
Metal binding1231Zinc By similarity
Metal binding1481Zinc By similarity
Metal binding1501Zinc By similarity
Binding site2691ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B5RRI1 [UniParc].

Last modified November 4, 2008. Version 1.
Checksum: C76EB3D9597B2950

FASTA50658,487
        10         20         30         40         50         60 
MIFQKRTFFI KRGCVLNIRV RYAPSPTGLQ HIGGIRTALF NYFFAKSFNG KFLLRIEDTD 

        70         80         90        100        110        120 
QTRYYKEAEE DLYQSLAWLG IDFDEGPTCG GSYSPYIQSQ RTEIYRKYAK ELIESGNAYY 

       130        140        150        160        170        180 
CYCSPDRLER IRKIQTINKM VPGYDRHCRH LNKDEIKDAL SLGISPVIRF KIPFDGETSF 

       190        200        210        220        230        240 
NDILLGKITW ANKDISPDPV ILKSDGFPTY HLANVVDDHL MEISHVLRAQ EWISSGSLHV 

       250        260        270        280        290        300 
LLYNAFGWNP PIYCHLPMVM GSDGQKLSKR HGATALKQFI DDGYLPEAII NYVTLLGWSY 

       310        320        330        340        350        360 
DGKSEFFTKN ELQKLFSIDK ISKSPAVFDY NKLDFFNSHY IRTKEDHELA ELLLPFLQKA 

       370        380        390        400        410        420 
GYIKKDSNSC DKEKLLLLVP LIKPRIRKLG DAVGMLRFFY TNISTWNVNE FLGKKKTVRD 

       430        440        450        460        470        480 
IYLLLEKIKP VLEGFETRIL SENEQIFYNF AKENNLKIGE VLIPIRIAVL GSKVSPPLFD 

       490        500 
SLQLLGKVKV FDRINKAQDF LKKYEL 

« Hide

References

[1]"The genome of Borrelia recurrentis, the agent of deadly louse-borne relapsing fever, is a degraded subset of tick-borne Borrelia duttonii."
Lescot M., Audic S., Robert C., Nguyen T.T., Blanc G., Cutler S.J., Wincker P., Couloux A., Claverie J.-M., Raoult D., Drancourt M.
PLoS Genet. 4:E1000185-E1000185(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: A1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000993 Genomic DNA. Translation: ACH94615.1.
RefSeqYP_002222836.1. NC_011244.1.

3D structure databases

ProteinModelPortalB5RRI1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING412418.BRE_371.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACH94615; ACH94615; BRE_371.
GeneID6918913.
KEGGbre:BRE_371.
PATRIC20569899. VBIBorRec40566_0397.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAWLPEEMG.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycBREC412418:GJIA-371-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.
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.
ProtoNetSearch...

Entry information

Entry nameSYE_BORRA
AccessionPrimary (citable) accession number: B5RRI1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 4, 2008
Last modified: May 14, 2014
This is version 43 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