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Q8DLI5 (SYE_THEEB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 72. 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:tll0506
OrganismThermosynechococcus elongatus (strain BP-1) [Reference proteome] [HAMAP]
Taxonomic identifier197221 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus

Protein attributes

Sequence length485 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Non-discriminating glutamyl-tRNA synthetase. 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). Acylates both tRNA(Glu) and tRNA(Gln) with glutamate, but has 13-fold higher efficiency with tRNA(Glu). Ref.2

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022_B

Cofactor

Does not require zinc. Ref.2

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00022_B

Subcellular location

Cytoplasm HAMAP-Rule MF_00022_B.

Miscellaneous

This organism lacks a tRNA synthetase for tRNA(Gln). Instead, tRNA(Gln) is first charged with Glu, and then the bound glutamate is converted to glutamine by GatCAB.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.79 µM for tRNA-Glu Ref.2

KM=3.7 µM for tRNA-Gln

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical term3D-structure
Complete proteome
Reference 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 – 485485Glutamate--tRNA ligase HAMAP-Rule MF_00022_B
PRO_0000119674

Regions

Region210 – 2145Glutamate binding HAMAP-Rule MF_00022_B
Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022_B
Motif248 – 2525"KMSKS" region HAMAP-Rule MF_00022_B

Sites

Binding site61Glutamate
Binding site1921Glutamate
Binding site2511ATP By similarity

Secondary structure

.............................................................................. 485
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8DLI5 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: C3547C6415FDDCBA

FASTA48554,362
        10         20         30         40         50         60 
MTVRVRLAPS PTGNLHIGTA RTAVFNWLYA RHRGGKFILR IEDTDRERSR PEYTENILEG 

        70         80         90        100        110        120 
LQWLGLTWDE GPYFQSDRLD LYRQAIQTLL DKGLAYYCYC TPEELEALRA EQKAKGQAPR 

       130        140        150        160        170        180 
YDNRHRHLTP EEQAAFEAAG RTPVIRFKIE DDRQIEWQDL VRGRVSWQGA DLGGDMVIAR 

       190        200        210        220        230        240 
AAPRGEIGYP LYNLVVVVDD IAMGITDVIR GEDHIGNTPK QILLYEALGA TPPNFAHTPL 

       250        260        270        280        290        300 
ILNSTGQKLS KRDGVTSISD FRAMGYLAPA LANYMTLLGW SPPEGVGELF TLDLAAKHFS 

       310        320        330        340        350        360 
FERINKAGAR FDWDKLNWLN RQYIQQLEPE EFLAELIPLW QGAGYAFDEE RDRPWLFDLA 

       370        380        390        400        410        420 
QLLQPGLNTL REAIDQGAVF FIPSVTFDSE AMAQLGQPQS ATILAYLLEH LPAEPALTVA 

       430        440        450        460        470        480 
MGQQLIQQAA KAAGVKKGAT MRTLRAALTG AVHGPDLMAA WQILHQRGWD EPRLAAALKQ 


AQTTS 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1."
Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takeuchi C., Yamada M., Tabata S.
DNA Res. 9:123-130(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BP-1.
[2]"Crystal structure of a non-discriminating glutamyl-tRNA synthetase."
Schulze J.O., Masoumi A., Nickel D., Jahn M., Jahn D., Schubert W.-D., Heinz D.W.
J. Mol. Biol. 361:888-897(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEX WITH GLUTAMATE, FUNCTION, ABSENCE OF COFACTOR REQUIREMENT, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000039 Genomic DNA. Translation: BAC08058.1.
RefSeqNP_681296.1. NC_004113.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CFOX-ray2.45A/B2-485[»]
ProteinModelPortalQ8DLI5.
SMRQ8DLI5. Positions 2-485.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING197221.tll0506.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC08058; BAC08058; BAC08058.
GeneID1012165.
KEGGtel:tll0506.
PATRIC23926260. VBITheElo119873_0533.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMARANQGKF.
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.
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...

Other

EvolutionaryTraceQ8DLI5.

Entry information

Entry nameSYE_THEEB
AccessionPrimary (citable) accession number: Q8DLI5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 72 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