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Q7VIM2 (SYE2_HELHP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 72. 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 2

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 2
Short name=GluRS 2
Gene names
Name:gltX2
Ordered Locus Names:HH_0582
OrganismHelicobacter hepaticus (strain ATCC 51449 / 3B1) [Complete proteome] [HAMAP]
Taxonomic identifier235279 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length441 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 – 441441Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000119575

Regions

Motif6 – 1611"HIGH" region HAMAP-Rule MF_00022
Motif231 – 2355"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2341ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VIM2 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: D46963489B27BFFA

FASTA44151,047
        10         20         30         40         50         60 
MLRFAPSPTG DMHIGNLRAA IFNYIIAKQQ NQKFLIRIED TDIARNIVDK DKEILNLLNL 

        70         80         90        100        110        120 
FGLLWDNLVY QSSNFERHRQ LAQHLISKDL AFYCYCSKEF LESKRLEAKE QKKPFRYDPS 

       130        140        150        160        170        180 
WAEIEKSSNT KPVVRIRGAS EAISFEDAIK GTLRFEAHEI DSFVILKEDG IPTYNFACAI 

       190        200        210        220        230        240 
DDMLYDISFI VRGEDHVSNT PRQILIHRAL GYDKVLGYAH LPIILGESGS KMSKRDNASS 

       250        260        270        280        290        300 
VAWLLEEGFL PQAIMNYLIS MGNHTPTEVF KLQDAYNWFD IKNIAKSPVK FDIKRLRFLN 

       310        320        330        340        350        360 
REHLKMLNEQ EFALLLDSKD SSIGALGKLH LQEASTLNEI RSKIERIFSP KCIAQNEEGE 

       370        380        390        400        410        420 
NFENECKILY DILHQMIESY DESLNDYDTF KNALMAKSSL KGKKFFKPLR ILLTGQTQGL 

       430        440 
ELSEIYPYLR FFLRDIVRLS K 

« Hide

References

[1]"The complete genome sequence of the carcinogenic bacterium Helicobacter hepaticus."
Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M., Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R., Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B. expand/collapse author list , Shen Z., Weber J., Frosch M., Fox J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51449 / 3B1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017125 Genomic DNA. Translation: AAP77179.1.
RefSeqNP_860113.1. NC_004917.1.

3D structure databases

ProteinModelPortalQ7VIM2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING235279.HH0582.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP77179; AAP77179; HH_0582.
GeneID1493636.
KEGGhhe:HH0582.
PATRIC20588618. VBIHelHep90276_0586.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
KOK01885.
OMAIHGPELS.
OrthoDBEOG6DRPF7.
ProtClustDBPRK12410.

Enzyme and pathway databases

BioCycHHEP235279:GHUA-600-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 nameSYE2_HELHP
AccessionPrimary (citable) accession number: Q7VIM2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: October 1, 2003
Last modified: February 19, 2014
This is version 72 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