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P57173 (SYE_BUCAI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 70. 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)
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 MF_00022_B

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022_B

Subunit structure

Monomer By similarity. HAMAP MF_00022_B

Subcellular location

Cytoplasm HAMAP MF_00022_B.

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: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 467467Glutamate--tRNA ligase HAMAP MF_00022_B
PRO_0000119526

Regions

Motif9 – 1911"HIGH" region HAMAP MF_00022_B
Motif237 – 2415"KMSKS" region HAMAP MF_00022_B

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: 10993077] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: APS.
+Additional computationally mapped references.

Cross-references

Sequence databases

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

3D structure databases

ProteinModelPortalP57173.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBUCT00000002787; EBBUCP00000002563; EBBUCG00000002787.
GeneID1109475.
GenomeReviewsGene locus BU070 in contig BA000003_GR.
KEGGbuc:BU070.
PATRIC21243646. VBIBucAph127364_0077.

Phylogenomic databases

GeneTreeEBGT00050000008076.
HOGENOMHBG628189.
OMADLVIQRS.
PhylomeDBP57173.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycBSP107806:BU070-MONOMER.

Family and domain databases

HAMAPMF_00022_B. Glu_tRNA_synth_B.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR004527. Glu-tRNA-synth_Ib_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ib.
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]
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. 2 hits.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
KOK01885.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PTHR10119:SF1. PTHR10119:SF1. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMsTIGR00464. GltX_bact. 1 hit.
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: January 25, 2012
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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