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A9I219 (SYE_BORPD) 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

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Ordered Locus Names:Bpet0588
OrganismBordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448) [Complete proteome] [HAMAP]
Taxonomic identifier340100 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

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_0000367618

Regions

Motif14 – 2411"HIGH" region HAMAP-Rule MF_00022
Motif246 – 2505"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2491ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A9I219 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 8CDD6311E0BF68DF

FASTA46751,765
        10         20         30         40         50         60 
MTSTPATIRT RFAPSPTGFL HLGGARTALF SWAFARHHQG VFVLRIEDTD LERSTPEAVQ 

        70         80         90        100        110        120 
AILDSMDWLG MQPDEGPFYQ MQRMDRYREV IAQMLQAGTA YHCYSSPEEV EAMREAARAR 

       130        140        150        160        170        180 
GLKPRYDGTW RPEPGKTLPP VPAGRKPVVR FKNPQDGATG WNDMVKGPIS FDNTELDDLI 

       190        200        210        220        230        240 
IARPDGTPTY NFCVVVDDWD MGITHVLRGD DHVNNTPRQI NILRALGATL PEYGHVPMIL 

       250        260        270        280        290        300 
GPDGEKLSKR HGAVNVMEYD AQGYLPEAMV NYLARLGWSH GDDELFTREQ LVQWFDTRHL 

       310        320        330        340        350        360 
SKSASQWDPK KLNWVNAHYI KQMDNAELAA RVAPRIERRG GNPAAVDLAA AMGLLKDRAE 

       370        380        390        400        410        420 
TLEQLAESAL LFCKPYQPAP AELAEQHLTP AAREALADFA QRAQGADWTR EAIAALIKAV 

       430        440        450        460 
LADRGLKMPQ LAIPLRVAVV GQTQTPAVDA VLALVGKDAV LQRLAAL 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM902716 Genomic DNA. Translation: CAP40920.1.
RefSeqYP_001629191.1. NC_010170.1.

3D structure databases

ProteinModelPortalA9I219.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING340100.Bpet0588.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAP40920; CAP40920; Bpet0588.
GeneID5818533.
KEGGbpt:Bpet0588.
PATRIC21162633. VBIBorPet31633_0596.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMADSHEHHA.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycBPET340100:GJBO-591-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_BORPD
AccessionPrimary (citable) accession number: A9I219
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