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B6JL62 (SYE1_HELP2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 34. 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:HPP12_0486
OrganismHelicobacter pylori (strain P12) [Complete proteome] [HAMAP]
Taxonomic identifier570508 [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-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 – 463463Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000367685

Regions

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

Sites

Binding site2411ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B6JL62 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: F15DBFF3C85C6F5D

FASTA46353,377
        10         20         30         40         50         60 
MSLIVTRFAP SPTGYLHIGG LRTAIFNYLF ARANQGKFFL RIEDTDLSRN SIEAANAIIE 

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

       130        140        150        160        170        180 
RYDNRYRDFK GTPPKGIEPV VRIKVPQNEV IGFNDGVKGE VRVNTNELDD FIIARSDGVP 

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

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

       310        320        330        340        350        360 
WHKLNWLNAH YLKNQSTQEL LKLLKPFSFS DLSHLNPAQL DRLLDALKER SQTLKELALK 

       370        380        390        400        410        420 
IDEVLTAPIE YEEKVLKKLN QALVMPLLEK FKLELNTTNF NDESALENAM HQIIEEEKIK 

       430        440        450        460 
AGSFMQPLRL ALLGKGGGIG LKEALFILGK TESVKRIEKF LKN 

« Hide

References

[1]"The complete genome sequence of Helicobacter pylori strain P12."
Fischer W., Windhager L., Karnholz A., Zeiller M., Zimmer R., Haas R.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: P12.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001217 Genomic DNA. Translation: ACJ07640.1.
RefSeqYP_002301120.1. NC_011498.1.

3D structure databases

ProteinModelPortalB6JL62.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING570508.HPP12_0486.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ07640; ACJ07640; HPP12_0486.
GeneID7010861.
KEGGhpp:HPP12_0486.
PATRIC20608944. VBIHelPyl2824_0512.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMARANQGKF.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycHPYL570508:GJ8D-500-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_HELP2
AccessionPrimary (citable) accession number: B6JL62
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: December 16, 2008
Last modified: February 19, 2014
This is version 34 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