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Q2SX36 (SYE_BURTA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 58. 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

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Ordered Locus Names:BTH_I1984
OrganismBurkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP]
Taxonomic identifier271848 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length469 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 term3D-structure
Complete 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 – 469469Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000237349

Regions

Motif11 – 2111"HIGH" region HAMAP-Rule MF_00022
Motif243 – 2475"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2461ATP By similarity

Secondary structure

................................................................. 469
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q2SX36 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: EEE0D68248D730E0

FASTA46952,046
        10         20         30         40         50         60 
MTRPVRTRFA PSPTGFIHLG NIRSALYPWA FARKMKGTFV LRIEDTDVER SSQEAVDAIL 

        70         80         90        100        110        120 
EGMAWLGLDY DEGPYYQMQR MDRYREVLAQ MQEKGLVYPC YMSTEELDAL RERQRAAGEK 

       130        140        150        160        170        180 
PRYDGTWRPE PGKVLPEPPA GVAPVLRFRN PLTGTVAWDD AVKGRVEISN EELDDLVVAR 

       190        200        210        220        230        240 
PDGTPMYNFC VVVDDLDMGI THVIRGDDHV NNTPRQINIL RALGGEVPVY AHLPTVLNEQ 

       250        260        270        280        290        300 
GEKMSKRHGA MSVMGYRDAG YLPEAVLNYL ARLGWSHGDA EIFTREQFVE WFDLEHLGKS 

       310        320        330        340        350        360 
PAQYDHNKLN WLNNHYIKEA DDARLAGLAK PFFAALGIDA GAIEQGPDLV SVMGLMKDRA 

       370        380        390        400        410        420 
STVKEIAENS AMFYRAPAPG ADALAQHVTD AVRPALVEFA AALKTVEWTK EAIAAALKAV 

       430        440        450        460 
LGAHKLKMPQ LAMPVRLLVA GTTHTPSIDA VLLLFGRDVV VSRIEAALA 

« Hide

References

[1]"Bacterial genome adaptation to niches: divergence of the potential virulence genes in three Burkholderia species of different survival strategies."
Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., DeShazer D.
BMC Genomics 6:174-174(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E264 / ATCC 700388 / DSM 13276 / CIP 106301.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000086 Genomic DNA. Translation: ABC37833.1.
RefSeqYP_442513.1. NC_007651.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4G6ZX-ray2.05A1-469[»]
ProteinModelPortalQ2SX36.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING271848.BTH_I1984.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC37833; ABC37833; BTH_I1984.
GeneID3850087.
KEGGbte:BTH_I1984.
PATRIC19307002. VBIBurTha36512_4795.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMADSHEHHA.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycBTHA271848:GJMY-1985-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_BURTA
AccessionPrimary (citable) accession number: Q2SX36
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: January 24, 2006
Last modified: May 14, 2014
This is version 58 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries