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Q1GHK0 (SYE1_RUEST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. 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 1

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1
Gene names
Name:gltX1
Ordered Locus Names:TM1040_1133
OrganismRuegeria sp. (strain TM1040) (Silicibacter sp.) [Complete proteome] [HAMAP]
Taxonomic identifier292414 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRuegeria

Protein attributes

Sequence length466 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 – 466466Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_1000001966

Regions

Motif11 – 2111"HIGH" region HAMAP-Rule MF_00022
Motif239 – 2435"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2421ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1GHK0 [UniParc].

Last modified June 27, 2006. Version 1.
Checksum: 6887661B81F5B4AF

FASTA46651,359
        10         20         30         40         50         60 
MSQPVVTRFA PSPTGFLHIG GARTALFNWL FARGRGGKFL LRIEDTDRAR STPEATAAIL 

        70         80         90        100        110        120 
QGMAWLGLDH DGEVVSQFEG AERHAEVAHQ LLAEGKAYKC FSTQEEIAAF REAAKAEGKS 

       130        140        150        160        170        180 
TLFHSPWRDT PESEHPDAPF AIRIKAPKDG ETVIRDQVQG DVTIKNAQLD DMILLRSDGT 

       190        200        210        220        230        240 
PVYMLAVVVD DHDMGVTHVI RGDDHLMNAA RQMMIYEAMG WDVPVYAHIP LIHGSDGKKL 

       250        260        270        280        290        300 
SKRHGALGAQ EYQAMGYPAA GMRNYLARLG WSHGDDEFFT DEQAKDWFDL DGIGKSPARF 

       310        320        330        340        350        360 
DTKKLENLCG QHIAIADDAA LRQEIEAYLD AAGQPALNDV QSQGLERAMY CLKDRAKTFP 

       370        380        390        400        410        420 
ELLEKAHFVL TSRPLERDAK AEKALDPVSI GILNELTPHL QNASWSRDEL EAALNEFAAA 

       430        440        450        460 
KDTKFGKLAG PLRAVLAGRA VTPSVFDMMI CLGREETLAR LKDVTG 

« Hide

References

[1]"Complete sequence of chromosome of Silicibacter sp. TM1040."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Goodwin L., Thompson L.S., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Belas R., Moran M.A., Buchan A., Gonzalez J.M., Schell M.A., Sun F., Richardson P.
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TM1040.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000377 Genomic DNA. Translation: ABF63866.1.
RefSeqYP_613128.1. NC_008044.1.

3D structure databases

ProteinModelPortalQ1GHK0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING292414.TM1040_1133.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF63866; ABF63866; TM1040_1133.
GeneID4077254.
KEGGsit:TM1040_1133.
PATRIC23386396. VBIRueSp69653_2023.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycRSP292414:GHCT-1151-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 nameSYE1_RUEST
AccessionPrimary (citable) accession number: Q1GHK0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 27, 2006
Last modified: May 14, 2014
This is version 62 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