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Q7W3X9 (SYE_BORPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 69. 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:BPP3898
OrganismBordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253) [Complete proteome] [HAMAP]
Taxonomic identifier257311 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length481 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 – 481481Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119519

Regions

Motif28 – 3811"HIGH" region HAMAP-Rule MF_00022
Motif260 – 2645"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2631ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7W3X9 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 6D8554F74E16DC7C

FASTA48153,413
        10         20         30         40         50         60 
MAQSAERPRP YAFMTANATR PVRTRFAPSP TGFLHLGGAR TALFSWAFAR HHQGVFVLRI 

        70         80         90        100        110        120 
EDTDVERSTP EAVQAILDSM DWLGMQPDEG PFYQMKRMDR YAEVLAGMLE AGTAYHCYCS 

       130        140        150        160        170        180 
PEEVDAMREA ARAKGLKPRY DGTWRPEPGK TLPPVPADRK PVIRFRNPID GATSWNDMVK 

       190        200        210        220        230        240 
GPISFDNGEL DDLIIARPDG TPTYNFCVVV DDWDMGITHV LRGDDHVNNT PRQINILRAL 

       250        260        270        280        290        300 
GATLPEYGHV PMILGPDGEK LSKRHGAVNV MEYDAQGYLP EAMINYLARL GWSHGDDELF 

       310        320        330        340        350        360 
TREQLVEWFD TRHLSKSASQ WDPKKLNWVN AHYIKGMDDA ELAGRVAPRV ERRGGKPQAA 

       370        380        390        400        410        420 
DLPAIMGLLK DRAETLEQLA EDAMLFCGEY QPAPAELAAQ HLTETARAAL ADFAARARDT 

       430        440        450        460        470        480 
EWNRAAISAL IKAVLADRGL KMPQLGIPLR VAVTGRAQTP AVDAVLELLG KETVLARLQA 


L 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX640435 Genomic DNA. Translation: CAE39181.1.
RefSeqNP_886048.1. NC_002928.3.

3D structure databases

ProteinModelPortalQ7W3X9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257311.BPP3898.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE39181; CAE39181; BPP3898.
GeneID1666861.
KEGGbpa:BPP3898.
PATRIC21151868. VBIBorPar43418_4092.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAHCLRASI.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycBPAR257311:BPP3898-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_BORPA
AccessionPrimary (citable) accession number: Q7W3X9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 69 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