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A9ISQ6 (SYE1_BART1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 44. 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:BT_0931
OrganismBartonella tribocorum (strain CIP 105476 / IBS 506) [Complete proteome] [HAMAP]
Taxonomic identifier382640 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length476 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 – 476476Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000367612

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif238 – 2425"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2411ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A9ISQ6 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: A806BBF8BAAA9777

FASTA47653,830
        10         20         30         40         50         60 
MSVITRFAPS PTGFLHIGGA RTALFNWLYA KHTGGKMLLR IEDTDRERST EAAVRAIIDG 

        70         80         90        100        110        120 
LHWMGLSYDG SPISQFERAE RHRQIAEQLV ENGKAYYCYA SPEELAEMRE KARAEGRPPR 

       130        140        150        160        170        180 
YDGRWRNRDH SEAPQGIKPV IRIKAPEDGE TIVHDRVQGD VRFPNKDLDD FIILRSDGSP 

       190        200        210        220        230        240 
TYMHAVVVDD HDMGVTHIIR GDDHLTNAAR QTIIFKAMGW DIPVMAHIPL IHGENGAKLS 

       250        260        270        280        290        300 
KRHGALGVDA YRTMGYLPAA LRNYLVRLGW SHGDDELMSL QDMISWFDIE DINKGAARFD 

       310        320        330        340        350        360 
LKKLDSINGH YMRMSNDQEL FDAALDILPE TDGGTEIIER LDEQRRVQFL KAIPHLKERS 

       370        380        390        400        410        420 
KTLCELIDNA SFIFTQRPLQ LNEKAQMLLD KNGRTILNDL YLALKACPSW DTKALDETLR 

       430        440        450        460        470 
SYIQTQNLKF GSIAQPLRAA LTGCTTSPGV LDVLILLGRD ESLYRINDQL ITTVGL 

« Hide

References

[1]"Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors."
Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.
Nat. Genet. 39:1469-1476(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CIP 105476 / IBS 506.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM260525 Genomic DNA. Translation: CAK01328.1.
RefSeqYP_001609323.1. NC_010161.1.

3D structure databases

ProteinModelPortalA9ISQ6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING382640.Btr_0931.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5829124.
KEGGbtr:Btr_0931.
PATRIC20549618. VBIBarTri113218_0963.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
KOK01885.
OMAAMGWEVP.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycBTRI382640:GJEK-830-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_BART1
AccessionPrimary (citable) accession number: A9ISQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 5, 2008
Last modified: May 14, 2014
This is version 44 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