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P27000 (SYE_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. 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:TTHA0438
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length468 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). Ref.4 Ref.6

Catalytic activity

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

Enzyme regulation

In the absence of bound tRNA, ATP is bound in a non-productive mode, and the enzyme cannot activate amino acids. Ref.6

Subunit structure

Monomer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00022_B.

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=4.7 µM for tRNA-Glu Ref.4

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 – 468468Glutamate--tRNA ligase HAMAP-Rule MF_00022_B
PRO_0000119683

Regions

Nucleotide binding243 – 2475ATP HAMAP-Rule MF_00022_B
Region5 – 73Glutamate binding HAMAP-Rule MF_00022_B
Region187 – 1915Glutamate binding HAMAP-Rule MF_00022_B
Region432 – 44716Interaction with tRNA HAMAP-Rule MF_00022_B
Motif8 – 1811"HIGH" region HAMAP-Rule MF_00022_B
Motif243 – 2475"KMSKS" region HAMAP-Rule MF_00022_B

Sites

Binding site151ATP
Binding site411Glutamate
Binding site2051Glutamate
Binding site2081ATP
Binding site2361ATP; via amide nitrogen and carbonyl oxygen
Site3541Interaction with tRNA; via carbonyl oxygen
Site3581Essential for discrimination between tRNA(Glu) and tRNA(Gln)

Experimental info

Mutagenesis3581R → Q: Reduces affinity for tRNA and abolishes the ability to discriminate between tRNA(Glu) and tRNA(Gln). Ref.4
Sequence conflict74 – 774GGPH → AAPT in CAA45854. Ref.1

Secondary structure

................................................................................ 468
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27000 [UniParc].

Last modified March 29, 2005. Version 2.
Checksum: 920E7F3363AF19E9

FASTA46853,910
        10         20         30         40         50         60 
MVVTRIAPSP TGDPHVGTAY IALFNYAWAR RNGGRFIVRI EDTDRARYVP GAEERILAAL 

        70         80         90        100        110        120 
KWLGLSYDEG PDVGGPHGPY RQSERLPLYQ KYAEELLKRG WAYRAFETPE ELEQIRKEKG 

       130        140        150        160        170        180 
GYDGRARNIP PEEAEERARR GEPHVIRLKV PRPGTTEVKD ELRGVVVYDN QEIPDVVLLK 

       190        200        210        220        230        240 
SDGYPTYHLA NVVDDHLMGV TDVIRAEEWL VSTPIHVLLY RAFGWEAPRF YHMPLLRNPD 

       250        260        270        280        290        300 
KTKISKRKSH TSLDWYKAEG FLPEALRNYL CLMGFSMPDG REIFTLEEFI QAFTWERVSL 

       310        320        330        340        350        360 
GGPVFDLEKL RWMNGKYIRE VLSLEEVAER VKPFLREAGL SWESEAYLRR AVELMRPRFD 

       370        380        390        400        410        420 
TLKEFPEKAR YLFTEDYPVS EKAQRKLEEG LPLLKELYPR LRAQEEWTEA ALEALLRGFA 

       430        440        450        460 
AEKGVKLGQV AQPLRAALTG SLETPGLFEI LALLGKERAL RRLERALA 

« Hide

References

« Hide 'large scale' references
[1]"Glutamyl-tRNA synthetase from Thermus thermophilus HB8. Molecular cloning of the gltX gene and crystallization of the overproduced protein."
Nureki O., Suzuki K., Hara-Yokoyama M., Kohno T., Matsuzawa H., Ohta T., Shimizu T., Morikawa K., Miyazawa T., Yokoyama S.
Eur. J. Biochem. 204:465-472(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genome sequence of Thermus thermophilus HB8."
Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HB8 / ATCC 27634 / DSM 579.
[3]"Architectures of class-defining and specific domains of glutamyl-tRNA synthetase."
Nureki O., Vassylyev D.G., Katayanagi K., Shimizu T., Sekine S., Kigawa T., Miyazawa T., Yokoyama S., Morikawa K.
Science 267:1958-1965(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[4]"Structural basis for anticodon recognition by discriminating glutamyl-tRNA synthetase."
Sekine S., Nureki O., Shimada A., Vassylyev D.G., Yokoyama S.
Nat. Struct. Biol. 8:203-206(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH TRNA-GLU, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-358.
[5]"ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding."
Sekine S., Nureki O., Dubois D.Y., Bernier S., Chenevert R., Lapointe J., Vassylyev D.G., Yokoyama S.
EMBO J. 22:676-688(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH ATP; GLUTAMATE AND TRNA.
[6]"Structural bases of transfer RNA-dependent amino acid recognition and activation by glutamyl-tRNA synthetase."
Sekine S., Shichiri M., Bernier S., Chenevert R., Lapointe J., Yokoyama S.
Structure 14:1791-1799(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH ATP; GLUTAMATE AND TRNA, FUNCTION, ENZYME REGULATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X64557 Genomic DNA. Translation: CAA45854.1.
AP008226 Genomic DNA. Translation: BAD70261.1.
RefSeqYP_143704.1. NC_006461.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G59X-ray2.40A/C1-468[»]
1GLNX-ray2.50A1-468[»]
1J09X-ray1.80A1-468[»]
1N75X-ray1.90A1-468[»]
1N77X-ray2.40A/B1-468[»]
1N78X-ray2.10A/B1-468[»]
2CUZX-ray1.98A1-468[»]
2CV0X-ray2.40A/B1-468[»]
2CV1X-ray2.41A/B1-468[»]
2CV2X-ray2.69A/B1-468[»]
2DXIX-ray2.20A/B1-468[»]
ProteinModelPortalP27000.
SMRP27000. Positions 1-468.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29168N.
STRING300852.TTHA0438.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD70261; BAD70261; BAD70261.
GeneID3168748.
KEGGttj:TTHA0438.
PATRIC23955847. VBITheThe93045_0438.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAVTGQTHG.
OrthoDBEOG6DRPF7.
PhylomeDBP27000.

Enzyme and pathway databases

BioCycTTHE300852:GH8R-459-MONOMER.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
1.10.8.70. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020752. aa-tRNA-synth_I_codon-bd_sub1.
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

EvolutionaryTraceP27000.

Entry information

Entry nameSYE_THET8
AccessionPrimary (citable) accession number: P27000
Secondary accession number(s): Q5SL55
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: March 29, 2005
Last modified: July 9, 2014
This is version 109 of the entry and version 2 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