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Q17WZ1 (SYE1_HELAH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 55. 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:Hac_1071
OrganismHelicobacter acinonychis (strain Sheeba) [Complete proteome] [HAMAP]
Taxonomic identifier382638 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length439 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 – 439439Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000367680

Regions

Motif6 – 1611"HIGH" region HAMAP-Rule MF_00022
Motif232 – 2365"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2351ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q17WZ1 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: CCE83AF43A82F840

FASTA43951,278
        10         20         30         40         50         60 
MLRFAPSPTG DMHIGNLRAA IFNYIVAKQQ HKPFLIRIED TDKERNIEGK DQEILEILKL 

        70         80         90        100        110        120 
MGMNWDKLVY QSHNIDYHRE MAEKLLKENK AFYCYASVGF LEQEKEKAKN EKRPFRYLDE 

       130        140        150        160        170        180 
WAALEKNQHN TPVVRLKAPN HAVSFNDAIK KEVKFEPYEL DSFVLLRKDK SPTYNFACAC 

       190        200        210        220        230        240 
DDLLYEISLI IRGEDHVSNT PKQILIQQAL GSNNPIIYAH LPIILDEASG KKMSKRDEAS 

       250        260        270        280        290        300 
SVKWLLNQGF LPVAIVNYLI TIGNKVPKEV FSLDEALEWF SLENLSNSPA HFNLKYLKHL 

       310        320        330        340        350        360 
NHQHLKRLDD EKLLELSQIK DRNLLGLLRL FIEECDTLLE LKEKISLFLE PKDIVKTYEN 

       370        380        390        400        410        420 
EDFKERCSIL FNALKSMDFQ AYKDFESFKK EAMRLSQLKG KDFFKPLRIL LIGDSHGVEL 

       430 
PLIFPYIQSH YQEILRLKA 

« Hide

References

[1]"Who ate whom? Adaptive Helicobacter genomic changes that accompanied a host jump from early humans to large felines."
Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G., Gressmann H., Achtman M., Schuster S.C.
PLoS Genet. 2:1097-1110(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sheeba.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM260522 Genomic DNA. Translation: CAJ99835.1.
RefSeqYP_664834.1. NC_008229.1.

3D structure databases

ProteinModelPortalQ17WZ1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING382638.Hac_1071.

Proteomic databases

PRIDEQ17WZ1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ99835; CAJ99835; Hac_1071.
GeneID4177262.
KEGGhac:Hac_1071.
PATRIC20585984. VBIHelAci71660_1006.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAIFNYICS.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycHACI382638:GJAU-990-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_HELAH
AccessionPrimary (citable) accession number: Q17WZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 25, 2006
Last modified: May 14, 2014
This is version 55 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