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Reviewed, UniProtKB/Swiss-Prot P57173 (SYE_BUCAI)

Last modified December 15, 2009. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutamyl-tRNA synthetase
    EC=6.1.1.17
Alternative name(s):
    Glutamate--tRNA ligase
      Short name=GluRS
Gene names
Name: gltX
Ordered Locus Names: BU070
OrganismBuchnera aphidicola subsp. Acyrthosiphon pisum (Acyrthosiphon pisum symbiotic bacterium) [Complete proteome] [HAMAP]
Taxonomic identifier118099 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length467 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm HAMAP 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: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 467467Glutamyl-tRNA synthetase HAMAP MF_00022
PRO_0000119526

Regions

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

Sites

Binding site2401ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P57173-1 [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: 10993077] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tokyo 1998.

Cross-references

Sequence databases

BA000003 Genomic DNA. Translation: BAB12791.1.
RefSeqNP_239905.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1109475.
GenomeReviewsGene locus BU070 in contig BA000003_GR.
KEGGbuc:BU070.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628189.
OMADLVIQRS.

Enzyme and pathway databases

BioCycBSP107806:BU070-MON.

Family and domain databases

HAMAPMF_00022.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR004527. Glu-tRNA-synth_Ic_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ic.
IPR020061. Glu/Gln-tRNA-synth_Ic_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ic_cat-dom.
IPR020060. Glu/Gln-tRNA-synth_Ic_N.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
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: December 15, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Buchnera aphidicola (subsp. Acyrthosiphon pisum)

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents