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Q83HJ1 (SYE_TROW8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 68. 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:TW563
OrganismTropheryma whipplei (strain TW08/27) (Whipple's bacillus) [Complete proteome] [HAMAP]
Taxonomic identifier218496 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeTropheryma

Protein attributes

Sequence length480 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 – 480480Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119688

Regions

Motif12 – 2211"HIGH" region HAMAP-Rule MF_00022
Motif255 – 2595"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2581ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q83HJ1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 798470EDC1A71F42

FASTA48054,801
        10         20         30         40         50         60 
MRDPRVRVRF CPSPTGAPHL GLVRTALFNW VFARKHGGGF IFRIEDTDAT RNREESCSQL 

        70         80         90        100        110        120 
IDTLKWLGLD WDEGPDKGGQ FGPYYQSQRG DIYQEVLDKL LAADLAYESF STKEEIEKRN 

       130        140        150        160        170        180 
LEAGRPIQLG YDNYDRTLSE QTKAAMREAG RTPIIRLRMD DENIAFEDLV KGEVVFTDPI 

       190        200        210        220        230        240 
PDFALTRASG EPLYTLVNPV DDAFMKITHV LRGEDLLSST PRQIALYKAL ITIGITDYVP 

       250        260        270        280        290        300 
FFGHLPIVMG EGNRKLSKRN PESDFYFYKA RGFIREGLLN YLSLLGWSIS NSRDTFSLSE 

       310        320        330        340        350        360 
MIHAFDVRDV RGNPARFDYK KCLAINAYHL RELNVEDFFL RLVPFVEEML GIPLSFEQKN 

       370        380        390        400        410        420 
SLRAICPFVQ GRVQLLTEAA EMVRFLLVDN ISVDFAVTDK EIDVLRHCLA LLNLLDTWES 

       430        440        450        460        470        480 
AQIASCIKQA IEQFDLQPKR IFSILRLAIT GRRVSPPLFE SMQILGRSAS LNRVETFVTN 

« Hide

References

[1]"Sequencing and analysis of the genome of the Whipple's disease bacterium Tropheryma whipplei."
Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G., Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A., Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J., Relman D.A.
Lancet 361:637-644(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TW08/27.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX251411 Genomic DNA. Translation: CAD67229.1.
RefSeqNP_789491.1. NC_004551.1.

3D structure databases

ProteinModelPortalQ83HJ1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING218496.TW563.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD67229; CAD67229; TW563.
GeneID1064766.
KEGGtws:TW563.
PATRIC23999629. VBITroWhi42739_0635.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

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.
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.
ProtoNetSearch...

Entry information

Entry nameSYE_TROW8
AccessionPrimary (citable) accession number: Q83HJ1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: February 19, 2014
This is version 68 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