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Q9X172 (SYE1_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 98. 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 1

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1
Gene names
Name:gltX1
Ordered Locus Names:TM_1351
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

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_B

Catalytic activity

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

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00022_B

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00022_B.

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
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 – 469469Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022_B
PRO_0000119680

Regions

Motif8 – 1811"HIGH" region HAMAP-Rule MF_00022_B
Motif250 – 2545"KMSKS" region HAMAP-Rule MF_00022_B

Sites

Binding site2531ATP By similarity

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9X172 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: F27D3AB4FE070BD8

FASTA46954,607
        10         20         30         40         50         60 
MVRVRFAPSP TGFLHVGGAR TALFNFLFAR KEKGKFILRI EDTDLERSER EYEEKLMESL 

        70         80         90        100        110        120 
RWLGLLWDEG PDVGGDHGPY RQSERVEIYR EHAERLVKEG KAYYVYAYPE EIEEMREKLL 

       130        140        150        160        170        180 
SEGKAPHYSQ EMFEKFDTPE RRREYEEKGL RPAVFFKMPR KDYVLNDVVK GEVVFKTGAI 

       190        200        210        220        230        240 
GDFVIMRSNG LPTYNFACVV DDMLMEITHV IRGDDHLSNT LRQLALYEAF EKAPPVFAHV 

       250        260        270        280        290        300 
STILGPDGKK LSKRHGATSV EAFRDMGYLP EALVNYLALL GWSHPEGKEL LTLEELISSF 

       310        320        330        340        350        360 
SLDRLSPNPA IFDPQKLKWM NGYYLRNMPI EKLAELAKPF FEKAGIKIID EEYFKKVLEI 

       370        380        390        400        410        420 
TKERVEVLSE FPEESRFFFE DPAPVEIPEE MKEVFSQLKE ELQNVRWTME EITPVFKKVL 

       430        440        450        460 
KQHGVKPKEF YMTLRRVLTG REEGPELVNI IPLLGKEIFL RRIERSLGG 

« Hide

References

« Hide 'large scale' references
[1]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"Crystal structure of glutamyl-tRNA synthetase 1 (EC 6.1.1.17) (glutamate-tRNA ligase 1) (glurS 1) (TM1351) from Thermotoga maritima at 2.5 A resolution."
Joint center for structural genomics (JCSG)
Submitted (DEC-2006) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000512 Genomic DNA. Translation: AAD36422.1.
PIRG72264.
RefSeqNP_229152.1. NC_000853.1.
YP_007977707.1. NC_021214.1.
YP_008991558.1. NC_023151.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2O5RX-ray2.34A1-469[»]
ProteinModelPortalQ9X172.
SMRQ9X172. Positions 1-468.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243274.TM1351.

Proteomic databases

PRIDEQ9X172.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD36422; AAD36422; TM_1351.
GeneID15494960.
18093363.
898129.
KEGGtma:TM1351.
tmm:Tmari_1358.
PATRIC23937640. VBITheMar51294_1363.

Phylogenomic databases

eggNOGCOG0008.
KOK09698.
OMACDCTREA.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

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

EvolutionaryTraceQ9X172.

Entry information

Entry nameSYE1_THEMA
AccessionPrimary (citable) accession number: Q9X172
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: March 19, 2014
This is version 98 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