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B2I994 (SYE_XYLF2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 40. 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:XfasM23_1950
OrganismXylella fastidiosa (strain M23) [Complete proteome] [HAMAP]
Taxonomic identifier405441 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXylella

Protein attributes

Sequence length467 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 – 467467Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000090124

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif237 – 2415"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2401ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B2I994 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 01C2656E29E85802

FASTA46752,501
        10         20         30         40         50         60 
MTCRTRFAPS PTGYLHIGGA RTALYCWLEA RRRNGQFLLR IEDTDRERST QAAIDAILHA 

        70         80         90        100        110        120 
MDWLGLDYDE PPVYQTQRIE RYNQVAARLL AEGKAYYAYD SKDTLNAMRE AALRTGEKPR 

       130        140        150        160        170        180 
YNGAAREANL PYRDDPNRVI RFKNPHTGTV AFDDLIKGRI QISNSELDDM VILRPDGYPT 

       190        200        210        220        230        240 
YNFAVVVDDW DMNITEVIRG DDHINNTPRQ INLYHALGAP LPTFAHLPMI LDEQGAKLSK 

       250        260        270        280        290        300 
RTGAADVMQY RDSGYLPHAL INYLVRLGWS HGDQELFNRQ ALIDLFQIND VNSKAARLDM 

       310        320        330        340        350        360 
AKLGWVNQHY LKTDDPATLA PPLVWHLEQR GIDVSAGPAP TDVILALRER VQTLKEMAEK 

       370        380        390        400        410        420 
AEIWYCPLQR YDEIAVAKHL KPGAETALLH ARTLLAALPA WTVDNVDTAL RTTATTLEIG 

       430        440        450        460 
MGKVAQPLRV AITGTQVSPD IAYTVYLTGR NEALKRIDAA LIKISTA 

« Hide

References

[1]"Whole genome sequences of two Xylella fastidiosa strains (M12 and M23) causing almond leaf scorch disease in California."
Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.
J. Bacteriol. 192:4534-4534(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: M23.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001011 Genomic DNA. Translation: ACB93349.1.
RefSeqYP_001830623.1. NC_010577.1.

3D structure databases

ProteinModelPortalB2I994.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING405441.XfasM23_1950.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB93349; ACB93349; XfasM23_1950.
GeneID6202591.
KEGGxfn:XfasM23_1950.
PATRIC24146532. VBIXylFas85937_2427.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMADSHEHHA.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycXFAS405441:GJJI-1992-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_XYLF2
AccessionPrimary (citable) accession number: B2I994
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 10, 2008
Last modified: May 14, 2014
This is version 40 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