Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A0Q4G6 (SYE_FRATN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. 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:FTN_0221
OrganismFrancisella tularensis subsp. novicida (strain U112) [Complete proteome] [HAMAP]
Taxonomic identifier401614 [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_1000001903

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
A0Q4G6 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 5609708B77FF8884

FASTA46852,925
        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 
DGKCRDANYV 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 EVEYHFAKTG LDISNGPDLK ELVAVMAEKV DTLVELAEKS 

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

       430        440        450        460 
VGMGKVGMPL RVAITGSGQS PDIGITLKLL GKNKVVARLT KALEELCK 

« Hide

References

[1]"Comparison of Francisella tularensis genomes reveals evolutionary events associated with the emergence of human pathogenic strains."
Rohmer L., Fong C., Abmayr S., Wasnick M., Larson Freeman T.J., Radey M., Guina T., Svensson K., Hayden H.S., Jacobs M., Gallagher L.A., Manoil C., Ernst R.K., Drees B., Buckley D., Haugen E., Bovee D., Zhou Y. expand/collapse author list , Chang J., Levy R., Lim R., Gillett W., Guenthener D., Kang A., Shaffer S.A., Taylor G., Chen J., Gallis B., D'Argenio D.A., Forsman M., Olson M.V., Goodlett D.R., Kaul R., Miller S.I., Brittnacher M.J.
Genome Biol. 8:R102.1-R102.16(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: U112.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000439 Genomic DNA. Translation: ABK89131.1.
RefSeqYP_897885.1. NC_008601.1.

3D structure databases

ProteinModelPortalA0Q4G6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING401614.FTN_0221.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK89131; ABK89131; FTN_0221.
GeneID4547821.
KEGGftn:FTN_0221.
PATRIC17933499. VBIFraNov128299_0232.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAHYIKELD.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycFNOV401614:GC4M-221-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_FRATN
AccessionPrimary (citable) accession number: A0Q4G6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 9, 2007
Last modified: May 14, 2014
This is version 59 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