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B0CGG7 (SYE1_BRUSI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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 1

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1
Gene names
Name:gltX1
Ordered Locus Names:BSUIS_A1059
OrganismBrucella suis (strain ATCC 23445 / NCTC 10510) [Complete proteome] [HAMAP]
Taxonomic identifier470137 [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_0000367627

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
B0CGG7 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: F3D3CDDD74CCAC01

FASTA45750,794
        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 
SDVSHWWQVV SGDLPEAPDL SGEDRDFVRH AFDLLPPEPW NGQTWKSWTE AVKSATGRKG 

       430        440        450 
KNLFMPLRLA LTGQAHGPEL ADLLVLVGLE RTKSRRP 

« Hide

References

[1]"Brucella suis ATCC 23445 whole genome shotgun sequencing project."
Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C., Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S., Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M., Snyder E.E. expand/collapse author list , Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Bruce D., Detter C., Munk C., Brettin T.S.
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 23445 / NCTC 10510.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000911 Genomic DNA. Translation: ABY38118.1.
RefSeqYP_001627688.1. NC_010169.1.

3D structure databases

ProteinModelPortalB0CGG7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING470137.BSUIS_A1059.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY38118; ABY38118; BSUIS_A1059.
GeneID5838260.
KEGGbmt:BSUIS_A1059.
PATRIC17869665. VBIBruSui83806_2631.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBSUI470137:GJIC-1050-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 nameSYE1_BRUSI
AccessionPrimary (citable) accession number: B0CGG7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 26, 2008
Last modified: February 19, 2014
This is version 45 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