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P57173 (SYE_BUCAI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BU070
OrganismBuchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium) [Reference proteome] [HAMAP]
Taxonomic identifier107806 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

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
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 – 467467Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119526

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
P57173 [UniParc].

Last modified December 1, 2000. Version 1.
Checksum: 1C35E3DA15A27593

FASTA46754,703
        10         20         30         40         50         60 
MKVKTRFAPS PTGNLHIGSI RTALYSWLFA RHHNGKFVLR IEDTDLVRSE LISIDSIFNG 

        70         80         90        100        110        120 
LKWLGLNWDE GPYFQTKRLD RYKEVINVML EKEDAYICVC SCQELEEIRK KQIEKGNKPR 

       130        140        150        160        170        180 
YPGTCRNLNI KNISNQNHVI RFKNPLFGKV KFQDKIRGEI VFDNAELDDL VIQRSNGMPT 

       190        200        210        220        230        240 
YNFCVVVDDM DMKITHVIRG EDHISNTPRQ INILNSLKVK IPVYAHLSMI LDEKGNKISK 

       250        260        270        280        290        300 
RKNAINIIEY YENGFLPEAL LNYIIRLGWS YGDKEIFNLS EMKELFNLKS ITKSSSTVNF 

       310        320        330        340        350        360 
KKLLWMNKYY INNSPLDYVS DCLKNYMEKK NINVEKGPDL ELLVKLFRSR HHTLKEITES 

       370        380        390        400        410        420 
CRYFYEEINF FNHTVIEKYF TRKNCFILQT CYKKIEKLSI WDNKNISKII NDVSELIKVT 

       430        440        450        460 
KKEISMILRI SMTGDICSPS ISTVILLIGK EKALLRINNV VNYIKNL 

« Hide

References

[1]"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS."
Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.
Nature 407:81-86(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: APS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000003 Genomic DNA. Translation: BAB12791.1.
RefSeqNP_239905.1. NC_002528.1.

3D structure databases

ProteinModelPortalP57173.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP57173.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB12791; BAB12791; BAB12791.
GeneID1109475.
KEGGbuc:BU070.
PATRIC21243646. VBIBucAph127364_0077.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAITESCRY.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycBAPH107806:GBZJ-70-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_BUCAI
AccessionPrimary (citable) accession number: P57173
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: February 19, 2014
This is version 84 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

Buchnera aphidicola (subsp. Acyrthosiphon pisum)

Buchnera aphidicola (subsp. Acyrthosiphon pisum): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries