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A5EV06 (SYE_DICNV) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. 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:DNO_0734
OrganismDichelobacter nodosus (strain VCS1703A) [Complete proteome] [HAMAP]
Taxonomic identifier246195 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaCardiobacterialesCardiobacteriaceaeDichelobacter

Protein attributes

Sequence length465 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 – 465465Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000330968

Regions

Motif8 – 1811"HIGH" region HAMAP-Rule MF_00022
Motif235 – 2395"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2381ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A5EV06 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: AACF8137D22A3E1B

FASTA46552,634
        10         20         30         40         50         60 
MLITRFAPSP TGDLHIGGVR TALFSWLVAK QKGGEFRLRI EDTDLERSTE ASTQVILKGM 

        70         80         90        100        110        120 
EWLGLDYQGE VIYQSRRTDI YNAVIDDMIA QGLAYYCWCT PEELEEMRAA QKARGEKPRY 

       130        140        150        160        170        180 
NGKYRNGGEP VDGVTPVVRF KNPLEGTVSW HDHVRGVVTI DNSELDDFII RRSDGMPTYN 

       190        200        210        220        230        240 
FCVVIDDHAQ DIGLVIRGDD HVSNTPRQIN LYRALGYQVP EFAHVPMILG DDGKRLSKRH 

       250        260        270        280        290        300 
GATNVLDYQK EGYLPEAIIN YLVRLGWAYG DQEIFSIEEL LTHFSIDDVH SAPSTFNTEK 

       310        320        330        340        350        360 
LRWLNQQYLM HTDIKELARL LPDFCAAQGY QLTQEQLLTV VPHYQERAKT LREMAEMMRW 

       370        380        390        400        410        420 
VACAPETFPE AAAKKAFKND TAQIMQLLIT KLQALQDFDE KTVHDALAAV VSELNIGFGK 

       430        440        450        460 
MGQPARLAIT GGLPSPDLAL CFALIGKENA LQRLQYAIKF MTQNQ 

« Hide

References

[1]"Genome sequence and identification of candidate vaccine antigens from the animal pathogen Dichelobacter nodosus."
Myers G.S.A., Parker D., Al-Hasani K., Kennan R.M., Seemann T., Ren Q., Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., Boyce J.D., McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., Holley T., Fedorova N. expand/collapse author list , Khouri H., Bottomley S.P., Whittington R.J., Adler B., Songer J.G., Rood J.I., Paulsen I.T.
Nat. Biotechnol. 25:569-575(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VCS1703A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000513 Genomic DNA. Translation: ABQ13746.1.
RefSeqYP_001209639.1. NC_009446.1.

3D structure databases

ProteinModelPortalA5EV06.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING246195.DNO_0734.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ13746; ABQ13746; DNO_0734.
GeneID5122161.
KEGGdno:DNO_0734.
PATRIC21785792. VBIDicNod48475_0736.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMARANQGKF.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycDNOD246195:GHHS-734-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_DICNV
AccessionPrimary (citable) accession number: A5EV06
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: June 12, 2007
Last modified: February 19, 2014
This is version 51 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