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P59423 (SYE_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 78. 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:bbp_065
OrganismBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]
Taxonomic identifier224915 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length472 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 – 472472Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119528

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif237 – 2415"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2401ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P59423 [UniParc].

Last modified March 28, 2003. Version 1.
Checksum: 39E1D9775632E2DD

FASTA47255,162
        10         20         30         40         50         60 
MIIKTRFAPS PTGPLHIGSV RTALYAWLFA KSMNGKFVLR IEDTDKRRST NAFTSEIINN 

        70         80         90        100        110        120 
LEWLGLNWDE GPYFQSDRLE YYRNIIKKMV EAGLAYKCYC TNDRLLKLRK FQISLGKKPK 

       130        140        150        160        170        180 
YDRKCRYLVK KDILSTDYVI RFCNPDFGCV TFCDKIRGKI SIENKELDDL VIQRADGIPT 

       190        200        210        220        230        240 
YNFCVVIDDR DMNITHVIRG EDHISNTPRQ INILRALNAN IPIYAHVSMV LSEDKQKLSK 

       250        260        270        280        290        300 
RNNTITSISE YRLCGYLPES LLNYIVRLGW SHGNQEIFSI SEMIKYFTLE SLNKSSSCLN 

       310        320        330        340        350        360 
KKKLLWLNRF YINNLPETVI KKHLQYQFNK NNIDYKNDSD LLKLVKLLGS RYYTLQEIVD 

       370        380        390        400        410        420 
YSRCFYNKSI CFNSNIMSKH LDNSSKLILK KIYDKFLDLE VWNVEVIRSL LNSSVCELQI 

       430        440        450        460        470 
SFKKVSMTIR IAVTGHVFSP NLCSVICFLG KNKFLLRIKE ALLYIKNMCF EV 

« Hide

References

[1]"Reductive genome evolution in Buchnera aphidicola."
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bp.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016826 Genomic DNA. Translation: AAO26802.1.
RefSeqNP_777697.1. NC_004545.1.

3D structure databases

ProteinModelPortalP59423.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224915.bbp065.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO26802; AAO26802; bbp_065.
GeneID1058176.
KEGGbab:bbp065.
PATRIC21244907. VBIBucAph80364_0062.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
KOK01885.
OMAHYIKELD.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycBAPH224915:GJ9D-65-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.
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.
ProtoNetSearch...

Entry information

Entry nameSYE_BUCBP
AccessionPrimary (citable) accession number: P59423
Entry history
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: March 28, 2003
Last modified: May 14, 2014
This is version 78 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