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A8F597 (SYE1_THELT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 47. 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:Tlet_0765
OrganismThermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / TMO) [Complete proteome] [HAMAP]
Taxonomic identifier416591 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length470 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 – 470470Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000367788

Regions

Motif8 – 1811"HIGH" region HAMAP-Rule MF_00022
Motif250 – 2545"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2531ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A8F597 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 9C0343F255E6FF11

FASTA47054,007
        10         20         30         40         50         60 
MVRVRFAPSP TGYLHVGGAR TALFNYLFAK HHGGKFILRI EDTDIARSEG IFEENLMKTL 

        70         80         90        100        110        120 
QWLGLNWDEG PDIGGSFGPY RQSERLNIYE EYAKKLIALD KAYEVFAYPE EIEEIREKLL 

       130        140        150        160        170        180 
SKGLTPHYDR TIFEPFATKE RKREYEEKGL KPAIYFSMPR KAFIHNDLVK GTVQFSEGSV 

       190        200        210        220        230        240 
GDFAILRSNG IPTYNFACVV DDMLMQITHV IRGDDHLPNT VKQLALYEAF SARPPEIGHV 

       250        260        270        280        290        300 
STILGPDGKK LSKRHGATSI EELRERGYLP QAVVNYLALL GWSSPDAKEI MSMQEMIERF 

       310        320        330        340        350        360 
SIDRLSKNPA IFDPAKLSWM NGQYIRSTNE EELEQLLKPL LEKWNFIPRN QDWLRRVIIA 

       370        380        390        400        410        420 
VKDRLHTLED FQHVADFFFV KPEIKTETEY QIKCAMLECA DKLESLDRSD KNSIVEVFRS 

       430        440        450        460        470 
TIKKQKVSAK EFYSTLRYVL TGKHEGPELV DIVFLLGPNE VAARIKSILG 

« Hide

References

[1]"Complete sequence of Thermotoga lettingae TMO."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Foster B., Bruce D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.
Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-301 / DSM 14385 / TMO.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000812 Genomic DNA. Translation: ABV33331.1.
RefSeqYP_001470395.1. NC_009828.1.

3D structure databases

ProteinModelPortalA8F597.
SMRA8F597. Positions 1-470.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING416591.Tlet_0765.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV33331; ABV33331; Tlet_0765.
GeneID5607932.
KEGGtle:Tlet_0765.
PATRIC23932073. VBITheLet125395_0797.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMANDYNQLE.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycTLET416591:GI64-781-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...

Entry information

Entry nameSYE1_THELT
AccessionPrimary (citable) accession number: A8F597
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 13, 2007
Last modified: May 14, 2014
This is version 47 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