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B5Z6J9 (SYE1_HELPG) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 27. 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:HPG27_434
OrganismHelicobacter pylori (strain G27) [Complete proteome] [HAMAP]
Taxonomic identifier563041 [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_B

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022_B

Subunit structure

Monomer By similarity. HAMAP MF_00022_B

Subcellular location

Cytoplasm By similarity HAMAP MF_00022_B.

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: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 463463Glutamate--tRNA ligase 1 HAMAP MF_00022_B
PRO_0000367681

Regions

Motif10 – 2011"HIGH" region HAMAP MF_00022_B
Motif238 – 2425"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2411ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B5Z6J9 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: 4698E5559F338919

FASTA46353,318
        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 IGFNDGVKGE VKVNTNELDD FIIARSDGTP 

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

       250        260        270        280        290        300 
KRHGATNVMD YQEMGYLKEA LVNFLVRLGW SYQDKEIFSM QELLECFDPK DLNSSPSCFS 

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

       370        380        390        400        410        420 
IDEVLIAPVE YEEKVFKKLN QALIMPLLEK FKLELKEANF NDESALENAM HKIIEEEKIK 

       430        440        450        460 
AGSFMQPLRL ALLGKGGGIG LKEALFILGK TESVKRIENF LKN 

« Hide

References

[1]"The complete genome sequence of Helicobacter pylori strain G27."
Baltrus D.A., Amieva M.R., Covacci A., Lowe T.M., Merrell D.S., Ottemann K.M., Stein M., Salama N.R., Guillemin K.
J. Bacteriol. 191:447-448(2009) [PubMed: 18952803] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: G27.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001173 Genomic DNA. Translation: ACI27198.1.
RefSeqYP_002266064.1. NC_011333.1.

3D structure databases

ProteinModelPortalB5Z6J9.
ModBaseSearch...

Protein-protein interaction databases

STRINGB5Z6J9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6963323.
GenomeReviewsGene locus HPG27_434 in contig CP001173_GR.
KEGGhpg:HPG27_434.
PATRIC20598833. VBIHelPyl113476_0472.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628189.
OMAANFNDES.
ProtClustDBPRK01406.

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_Ib_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ib.
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]
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. 2 hits.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
KOK01885.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PTHR10119:SF1. PTHR10119:SF1. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMsTIGR00464. GltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE1_HELPG
AccessionPrimary (citable) accession number: B5Z6J9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 25, 2008
Last modified: January 25, 2012
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families