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Q8G0S1 (SYE1_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 1

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1
Gene names
Name:gltX1
Synonyms:gltX2
Ordered Locus Names:BR1016, BS1330_I1012
OrganismBrucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]
Taxonomic identifier204722 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length457 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 – 457457Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000119525

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif250 – 2545"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2531ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8G0S1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 4C98329D7800A0C1

FASTA45750,772
        10         20         30         40         50         60 
MTVTVRFAPS PTGYIHIGNT RTALSNWLYA SKNNGKFILR YDDTDVERSK DEYAQAIAVD 

        70         80         90        100        110        120 
LDWLGVRPDR VEYQSKRFDI YAKAVEKLKT AGLLYACYET ADELERRRKL RLARRLPPVY 

       130        140        150        160        170        180 
GREALKLTDA EKAALEAEGR KPHWRFLLPN FESDPFATQR TEVHWDDLVR GPQTVDLASM 

       190        200        210        220        230        240 
SDPILVREDG TYLYTLPSVV DDIDMGVTHI IRGDDHVTNT GVQISIFKAL GATPPVFGHH 

       250        260        270        280        290        300 
NLLTTISGEG LSKRTGALSV GSLREAGYEP MAVASLAILI GTSESVTAAP DMAALAEHFD 

       310        320        330        340        350        360 
LASISKSSAK FDPSELDALN RSLLHEMPFE KAKPRLEALG ICGAKAESFW LAVRGNLDRF 

       370        380        390        400        410        420 
SDVSDWWQVV SGDLPEAPDL SGEDRDFVRH AFDLLPPEPW NGQTWKSWTE AVKSATGRKG 

       430        440        450 
KNLFMPLRLA LTGQAHGPEL ADLLVLVGLE RTKSRRP 

« Hide

References

[1]"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts."
Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. expand/collapse author list , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1330.
[2]"Revised genome sequence of Brucella suis 1330."
Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.
J. Bacteriol. 193:6410-6410(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1330.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014291 Genomic DNA. Translation: AAN29938.1.
CP002997 Genomic DNA. Translation: AEM18356.1.
RefSeqNP_698023.1. NC_004310.3.
YP_005615848.1. NC_017251.1.

3D structure databases

ProteinModelPortalQ8G0S1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING204722.BR1016.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN29938; AAN29938; BR1016.
AEM18356; AEM18356; BS1330_I1012.
GeneID1166689.
12138042.
KEGGbms:BR1016.
bsi:BS1330_I1012.
PATRIC17790342. VBIBruSui107850_1027.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252721.
KOK01885.
OMAFFFANAV.
OrthoDBEOG6DRPF7.
ProtClustDBPRK12558.

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 nameSYE1_BRUSU
AccessionPrimary (citable) accession number: Q8G0S1
Secondary accession number(s): G0K9U0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 71 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

Brucella suis

Brucella suis (strain 1330): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries