Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q1CU52 (SYE1_HELPH)

Last modified February 9, 2010. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutamyl-tRNA synthetase 1
    EC=6.1.1.17
Alternative name(s):
    Glutamate--tRNA ligase 1
      Short name=GluRS 1
Gene names
Name: gltX1
Ordered Locus Names: HPAG1_0453
OrganismHelicobacter pylori (strain HPAG1) [Complete proteome] [HAMAP]
Taxonomic identifier357544 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length463 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 MF_00022

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022

Subunit structure

Monomer By similarity. HAMAP MF_00022

Subcellular location

Cytoplasm By similarity HAMAP 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: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 463463Glutamyl-tRNA synthetase 1 HAMAP MF_00022
PRO_0000367683

Regions

Motif10 – 2011"HIGH" region HAMAP MF_00022
Motif238 – 2425"KMSKS" region HAMAP MF_00022

Sites

Binding site2411ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1CU52-1 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: 864E471A756A5AA6

FASTA46353,414
        10         20         30         40         50         60 
MSLIVTRFAP SPTGYLHIGG LRTAIFNYLF ARANQGKFFL RIEDTDLSRN SIEAANAIIE 

        70         80         90        100        110        120 
AFKWVGLEYD GEILYQSKRF EIYKEYIQKL LDEDKAYYCY MSKDELDALR EEQKARKETP 

       130        140        150        160        170        180 
RYDNRYRDFK GTPPKGIEPV VRIKVPQNEV IVFNDGVKGE VKVNTNELDD FIIARSDGTP 

       190        200        210        220        230        240 
TYNFVVIVDD ALMGITDVIR GDDHLSNTPK QIVLYKALNF KIPNFFHVPM ILNEEGQKLS 

       250        260        270        280        290        300 
KRHGATNVMD YQERGYLKEA LVNFLARLGW SYQDKEIFSM QELLECFDPK DLNSSPSCFS 

       310        320        330        340        350        360 
WHKLNWLNAH YLKNQSAQEL LELLKPFSFS DLSHLNPAQL DRLLDALKER SQTLKELALK 

       370        380        390        400        410        420 
IDEVLTAPIE YEKKVFKKLN QALVMPLLEK FKLELNKVNF NDENALENAM HKIIEEEKIK 

       430        440        450        460 
AGSFMQPLRL ALLGKGGGIG LKEALFILGK TESLKRIEKF LKN 

« Hide

References

[1]"The complete genome sequence of a chronic atrophic gastritis Helicobacter pylori strain: evolution during disease progression."
Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A., Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006) [PubMed: 16788065] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000241 Genomic DNA. Translation: ABF84520.1.
RefSeqYP_627194.1.

3D structure databases

SMRQ1CU52. Positions 3-461.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1CU52.

Genome annotation databases

GeneID4099369.
GenomeReviewsGene locus HPAG1_0453 in contig CP000241_GR.
KEGGhpa:HPAG1_0453.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHBG628189.
OMAKVNTNEL.

Enzyme and pathway databases

BioCycHPYL357544:HPAG1_0453-MONOMER.

Family and domain databases

HAMAPMF_00022_B. Glu_tRNA_synth_B.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-synth_Ic_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ic.
IPR020061. Glu/Gln-tRNA-synth_Ic_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ic_cat-dom.
IPR020060. Glu/Gln-tRNA-synth_Ic_N.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE1_HELPH
AccessionPrimary (citable) accession number: Q1CU52
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 11, 2006
Last modified: February 9, 2010
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents