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Q0BNU3 (SYE_FRATO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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:FTH_0213
OrganismFrancisella tularensis subsp. holarctica (strain OSU18) [Complete proteome] [HAMAP]
Taxonomic identifier393011 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella

Protein attributes

Sequence length468 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 – 468468Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000001904

Regions

Motif8 – 1811"HIGH" region HAMAP-Rule MF_00022
Motif236 – 2405"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding971Zinc By similarity
Metal binding991Zinc By similarity
Metal binding1241Zinc By similarity
Metal binding1261Zinc By similarity
Binding site2391ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0BNU3 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: E9DBBA29EE3BF93F

FASTA46853,007
        10         20         30         40         50         60 
MITTRFAPSP TGFLHVGGVR TALFSWLYAK NNNGKFILRI EDTDLERSTQ EAVDAILDGM 

        70         80         90        100        110        120 
SWLGLKNDGE IYYQTKRFDR YKEVIQELIA DGKAYYCSCS KERLEELREY QQANNLKTGY 

       130        140        150        160        170        180 
DGKCRDANYI PQQGESYVVR FKNPQDGVVS WDDAVKGRIS ISNHELDDMI IQRADGSPTY 

       190        200        210        220        230        240 
NFCVVVDDID MAITHIIRGD DHVNNTPKQI NIYKALNANV PVFAHVPMIL GPDGAKLSKR 

       250        260        270        280        290        300 
HGAVNVMQYR EDGYLPQAIL NYLVRLGWSH GDQEIFSIEE MIKAFNLEHI NASPSRFDFE 

       310        320        330        340        350        360 
KLKWLNKHYI KESKFDDIQT EVEYHFAKIG LDISNGPDLK ELVAVMAEKV DTLVELAEKS 

       370        380        390        400        410        420 
SYFYSDDISY DENAVKKHIK ASTGEIFVKL LENFEALDAQ QWQDPDVLYN IVSTTAEQCQ 

       430        440        450        460 
VGMGKVGMPL RVAITSSGQS PDIGITLKLL GKNKVVARLT KALEELCK 

« Hide

References

[1]"Chromosome rearrangement and diversification of Francisella tularensis revealed by the type B (OSU18) genome sequence."
Petrosino J.F., Xiang Q., Karpathy S.E., Jiang H., Yerrapragada S., Liu Y., Gioia J., Hemphill L., Gonzalez A., Raghavan T.M., Uzman A., Fox G.E., Highlander S., Reichard M., Morton R.J., Clinkenbeard K.D., Weinstock G.M.
J. Bacteriol. 188:6977-6985(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OSU18.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000437 Genomic DNA. Translation: ABI82241.1.
RefSeqYP_762878.1. NC_008369.1.

3D structure databases

ProteinModelPortalQ0BNU3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING393011.FTH_0213.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI82241; ABI82241; FTH_0213.
GeneID4308036.
KEGGfth:FTH_0213.
PATRIC17950159. VBIFraTul3936_0247.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMACDCTREA.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycFTUL393011:GHFN-220-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_FRATO
AccessionPrimary (citable) accession number: Q0BNU3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 17, 2006
Last modified: February 19, 2014
This is version 57 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