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A5EK39 (SYE_BRASB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 47. 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:BBta_4501
OrganismBradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182) [Complete proteome] [HAMAP]
Taxonomic identifier288000 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length474 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

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
Nucleotide-binding
   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

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 474474Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000001876

Regions

Motif11 – 2111"HIGH" region HAMAP-Rule MF_00022
Motif240 – 2445"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2431ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A5EK39 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: B83AD3D87BC1F459

FASTA47452,284
        10         20         30         40         50         60 
MTSPIVTRFA PSPTGFLHIG GARTALFNWL YARGRCGKML LRIEDTDRER STTAAIDAIL 

        70         80         90        100        110        120 
DGLKWLELDW DGEVIYQYSR AARHREVAEQ LLASGMAYRC YATAEELAAM REKARAEGRT 

       130        140        150        160        170        180 
RLYDGMWRDR DPKDAPGDVK PTIRLRAPLT GETVIEDQVQ GRVVWQNENL DDLVLLRGDG 

       190        200        210        220        230        240 
NPTYMLAVVV DDHDMGVTHV IRGDDHLINA ARQKQIYDAL GWTVPSMSHI PLIHGPDGSK 

       250        260        270        280        290        300 
LSKRHGALGV DAYRAMGYLP SALRNYLVRL GWSHGDQEIF STEEMIKAFD LPAIGRSAAR 

       310        320        330        340        350        360 
FDFAKLENLN GHYIRHSDDA ALVRQFEDVL NYVPNGATLK AKLNDATRAQ LTQAMPSLKE 

       370        380        390        400        410        420 
RAKTLLELID GAAFLFADRP LPIDAKAAAL LTPDSRALIG RLHDALAAVE PWSGPATEAA 

       430        440        450        460        470 
LRAFAETNNL KLGAVAQPLR AALTGRTTSP GIFDVLAILG RDESLGRLKD QTTS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000494 Genomic DNA. Translation: ABQ36533.1.
RefSeqYP_001240439.1. NC_009485.1.

3D structure databases

ProteinModelPortalA5EK39.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING288000.BBta_4501.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ36533; ABQ36533; BBta_4501.
GeneID5154831.
KEGGbbt:BBta_4501.
PATRIC21209747. VBIBraSp29847_4541.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMARANQGKF.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycBSP288000:GJBR-4295-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_BRASB
AccessionPrimary (citable) accession number: A5EK39
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 12, 2007
Last modified: February 19, 2014
This is version 47 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