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Q2KUY9 (SYE_BORA1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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:BAV2977
OrganismBordetella avium (strain 197N) [Complete proteome] [HAMAP]
Taxonomic identifier360910 [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_0000237342

Regions

Motif13 – 2311"HIGH" region HAMAP-Rule MF_00022
Motif245 – 2495"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2481ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2KUY9 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: CF0029900A23350D

FASTA46751,814
        10         20         30         40         50         60 
MTSPKPIRTR FAPSPTGFLH LGGARTALFS WAFARHHKGV FVLRIEDTDV ERSTDAAVQA 

        70         80         90        100        110        120 
ILDSMDWLGM QPDEGPFYQM KRLDRYSEVL QSMLAAGTAY HCYSSPEEVE AMREAARARG 

       130        140        150        160        170        180 
DKPRYDGTWR PEPGKTLPAI PEGRKPVIRF KNPQDGVTAW DDMVKGPVSF DNNELDDLII 

       190        200        210        220        230        240 
ARPDGTPTYN FCVVVDDWDM GMTHVIRGDD HVNNTPRQIN ILKALGADVP QYGHVPMILG 

       250        260        270        280        290        300 
PDGQKLSKRH GAVNVMEYDD QGYLPEAMVN YLARLGWSHG DAELFSREEF VRWFDTHHLS 

       310        320        330        340        350        360 
KSPSQWDPKK LNWVNAHYIK AMDNAELAQR VAPRIAKRGG DASRADLADI MGLFKDRAET 

       370        380        390        400        410        420 
LEQLADDAML FCAPFQAAPQ ELATQHLTPA AREALAGFAA AAAGTEWTRE AISALIKAQL 

       430        440        450        460 
AERGLKMPQL AIPLRVAVTG RAQTPAVDAV LVLLGKDVVL ERLKALL 

« Hide

References

[1]"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction."
Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M.
J. Bacteriol. 188:6002-6015(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 197N.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM167904 Genomic DNA. Translation: CAJ50587.1.
RefSeqYP_787472.1. NC_010645.1.

3D structure databases

ProteinModelPortalQ2KUY9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360910.BAV2977.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6266308.
KEGGbav:BAV2977.
PATRIC21132263. VBIBorAvi43433_3010.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMARANQGKF.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycBAVI360910:GCKI-3051-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_BORA1
AccessionPrimary (citable) accession number: Q2KUY9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: March 7, 2006
Last modified: February 19, 2014
This is version 54 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