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Q7VUU5 (SYE_BORPE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 66. 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:BP2978
OrganismBordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) [Reference proteome] [HAMAP]
Taxonomic identifier257313 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length460 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
Reference 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 – 460460Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119520

Regions

Motif7 – 1711"HIGH" region HAMAP-Rule MF_00022
Motif239 – 2435"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2421ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VUU5 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 3CB1BE13A27FFCBE

FASTA46051,082
        10         20         30         40         50         60 
MRTRFAPSPT GFLHLGGART ALFSWAFARH HQGVFVLRIE DTDVERSTPE AVQAILDSMD 

        70         80         90        100        110        120 
WLGMQPDEGP FYQMKRMDRY AEVLAGMLEA GTAYHCYCSP EEVDAMREAA RAKGLKPRYD 

       130        140        150        160        170        180 
GTWRPEPGKT LPPVPADRKP VIRFRNPIDG ATSWNDMVKG PISFDNGELD DLIIARPDGT 

       190        200        210        220        230        240 
PTYNFCVVVD DWDMGITHVL RGDDHVNNTP RQINILRALG ATLPEYGHVP MILGPDGEKL 

       250        260        270        280        290        300 
SKRHGAVNVM EYDAQGYLPE AMVNYLARLG WSHGDDELFT REQLVEWFDT RHLSKSASQW 

       310        320        330        340        350        360 
DPKKLNWVNA HYIKGMDDAE LAGRVAPRVE RRGGKPQAAD LPAIMGLLKD RAETLEQLAE 

       370        380        390        400        410        420 
DAMLFCGEYQ PAPAELAAQH LTETARAALA DFAARARDTE WNRAAISALI KAVLADRGLK 

       430        440        450        460 
MPQLGIPLRV AVTGRAQTPA VDAVLELLGK ETVLARLQAL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX640420 Genomic DNA. Translation: CAE43249.1.
RefSeqNP_881555.1. NC_002929.2.

3D structure databases

ProteinModelPortalQ7VUU5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257313.BP2978.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE43249; CAE43249; BP2978.
GeneID2666918.
KEGGbpe:BP2978.
PATRIC21159490. VBIBorPer7866_3222.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAHCLRASI.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycBPER257313:BP2978-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_BORPE
AccessionPrimary (citable) accession number: Q7VUU5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 66 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