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B6JH82 (SYE_OLICO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 35. 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:OCAR_5972, OCA5_c20520
OrganismOligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5) [Complete proteome] [HAMAP]
Taxonomic identifier504832 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeOligotropha

Protein attributes

Sequence length473 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 – 473473Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000090094

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
B6JH82 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: 0641DCF01364B4C4

FASTA47352,213
        10         20         30         40         50         60 
MTEPVVTRFA PSPTGFLHIG GARTALFNWL YARKQGGKML LRIEDTDRER STDAAIKAIL 

        70         80         90        100        110        120 
DGLNWLGIEW DGEVIYQFSR AARHREVAEQ LLAEGKAYRC YATPEELTKM REAARAEGRA 

       130        140        150        160        170        180 
VRYDGRWRDR DPSEAPADVK PVIRLKAPQT GETVIEDQVQ GRVVWQNENL DDLVLLRSDG 

       190        200        210        220        230        240 
TPTYMLAVVV DDHDMGVTHV IRGDDHLINA ARQKHIYDAL GWTVPTMAHI PLIHGPDGSK 

       250        260        270        280        290        300 
LSKRHGALGV EAYRTMGYLP AALRNYLVRL GWSHGDQEIF STSEMIEAFE LSGIGRSAAR 

       310        320        330        340        350        360 
FDFAKLENLN GHYMRASGDA ELVKAFEDIL QFLPQGPALQ AKLNDTTRAQ LLQAMPGLKE 

       370        380        390        400        410        420 
RAKTLLELID SAAYIFADRP LALDAKASAV LTPQVRALLG ELRSSLANVT DWNAANTEAA 

       430        440        450        460        470 
MRAYAEKNNL KLGAVAQPLR AALTGRTTSP GIFDVLAVLG RDDALARLQD QAA 

« Hide

References

[1]"Genome sequence of the chemolithoautotrophic bacterium Oligotropha carboxidovorans OM5T."
Paul D., Bridges S., Burgess S.C., Dandass Y., Lawrence M.L.
J. Bacteriol. 190:5531-5532(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49405 / DSM 1227 / OM5.
[2]"Complete genome sequences of the chemolithoautotrophic Oligotropha carboxidovorans strains OM4 and OM5."
Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G., Meyer O.
J. Bacteriol. 193:5043-5043(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49405 / DSM 1227 / OM5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001196 Genomic DNA. Translation: ACI93092.1.
CP002826 Genomic DNA. Translation: AEI06759.1.
RefSeqYP_002288957.1. NC_011386.1.
YP_004633000.1. NC_015684.1.

3D structure databases

ProteinModelPortalB6JH82.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING504832.OCAR_5972.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACI93092; ACI93092; OCAR_5972.
AEI06759; AEI06759; OCA5_c20520.
GeneID10847184.
6992110.
KEGGoca:OCAR_5972.
ocg:OCA5_c20520.
PATRIC22805825. VBIOliCar134280_1870.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycOCAR504832:GJPZ-2052-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_OLICO
AccessionPrimary (citable) accession number: B6JH82
Secondary accession number(s): F8BW48
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: December 16, 2008
Last modified: February 19, 2014
This is version 35 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