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B1VA59 (SYE_PHYAS) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 43. 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

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Ordered Locus Names:PA0498
OrganismPhytoplasma australiense [Complete proteome] [HAMAP]
Taxonomic identifier59748 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesAcholeplasmatalesAcholeplasmataceaeCandidatus Phytoplasma16SrXII (Stolbur group)

Protein attributes

Sequence length448 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 – 448448Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367736

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif214 – 2185"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2171ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B1VA59 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: CE15060913FEDAC3

FASTA44852,517
        10         20         30         40         50         60 
MNKIRVRYAP SPTGFLHIGN ARTALFNYLF AKHHQGDFIL RIEDTDLLRN VADGEASQLK 

        70         80         90        100        110        120 
NLRWLGIDWK EGPDINGPFG PYRQSERLTI YQKYAFELLE KNLAYRDFEK DKKNFAIRFK 

       130        140        150        160        170        180 
VPPNQTFTFC DLIRGKLTFL SKEIEDWVII KSNGYPSYNF AASIDDHLMQ ISHIFRGEEH 

       190        200        210        220        230        240 
ITNTPKQIMI YQSFNWSIPK FAHMTLILNQ ERKKLSKRDV NVCQFIQDYA DLGYLPQSLF 

       250        260        270        280        290        300 
NFLSLLGFSP SSCKEILTPQ EIISLFDVNR LNKSPAIFDK TKLDFFNNHY LRKTPIDDIV 

       310        320        330        340        350        360 
SFIKTKLDFF EVLPINNQKW LTKFILLFQE RINYIKQLKD LYHHFFDKNT SLSEEVEQFL 

       370        380        390        400        410        420 
KKHDCALSVL TLFYHKLNLV VFEKEAINPI IAEIAQNMKI NKKNLFVILR IGATHKMQGP 

       430        440 
SLALFLELLG KKQVLNNLSK IVELLKNQ 

« Hide

References

[1]"Comparative genome analysis of 'Candidatus Phytoplasma australiense' (subgroup tuf-Australia I; rp-A) and 'Ca. Phytoplasma asteris' strains OY-M and AY-WB."
Tran-Nguyen L.T., Kube M., Schneider B., Reinhardt R., Gibb K.S.
J. Bacteriol. 190:3979-3991(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM422018 Genomic DNA. Translation: CAM11832.1.
RefSeqYP_001799084.1. NC_010544.1.

3D structure databases

ProteinModelPortalB1VA59.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING59748.PAa_0498.

Proteomic databases

PRIDEB1VA59.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM11832; CAM11832; EBG00000298791.
GeneID6799630.
KEGGpal:PAa_0498.
PATRIC31993357. VBICanPhy111091_0543.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
KOK01885.
OMAGPELIDI.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycPAUS59748:GJ8P-506-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 nameSYE_PHYAS
AccessionPrimary (citable) accession number: B1VA59
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: June 11, 2014
This is version 43 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