O82462 · SYEC_ARATH

Function

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).

Features

Showing features for binding site.

1719100200300400500600700
TypeIDPosition(s)Description
Binding site93ATP (UniProtKB | ChEBI)
Binding site217-219L-glutamate (UniProtKB | ChEBI)
Binding site227ATP (UniProtKB | ChEBI)
Binding site393-397L-glutamate (UniProtKB | ChEBI)
Binding site411L-glutamate (UniProtKB | ChEBI)
Binding site414ATP (UniProtKB | ChEBI)
Binding site448-452ATP (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytosol
Cellular Componentplastid
Molecular FunctionATP binding
Molecular Functionglutamate-tRNA ligase activity
Biological Processglutamyl-tRNA aminoacylation
Biological Processpost-embryonic development
Biological Processreproductive structure development

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glutamate--tRNA ligase, cytoplasmic
  • EC number
  • Alternative names
    • GluRSAt
    • Glutamyl-tRNA synthetase
      (GluRS
      )

Gene names

    • ORF names
      F21E10.12
    • Ordered locus names
      At5g26710

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    O82462
  • Secondary accessions
    • O65253

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004335431-719Glutamate--tRNA ligase, cytoplasmic

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Interacts with GLN2, COL4 and RPP13L4/ZAR1.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, motif.

TypeIDPosition(s)Description
Region176-205Disordered
Compositional bias191-205Basic and acidic residues
Motif220-230'HIGH' region
Motif448-452'KMSKS' region

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    719
  • Mass (Da)
    81,065
  • Last updated
    1998-11-01 v1
  • Checksum
    0778C243219DA24C
MDGMKLSFPPESPPLSVIVALSLSASPVTIDSSAAATTVPSFVFSDGRKLNGATVLLRYVGRSAKKLPDFYGNNAFDSSQIDEWVDYASVFSSGSEFENACGRVDKYLESSTFLVGHSLSIADVAIWSALAGTGQRWESLRKSKKYQSLVRWFNSILDEYSEVLNKVLATYVKKGSGKPVAAPKSKDSQQAVKGDGQDKGKPEVDLPEAEIGKVKLRFAPEPSGYLHIGHAKAALLNKYFAERYQGEVIVRFDDTNPAKESNEFVDNLVKDIGTLGIKYEKVTYTSDYFPELMDMAEKLMREGKAYVDDTPREQMQKERMDGIDSKCRNHSVEENLKLWKEMIAGSERGLQCCVRGKFNMQDPNKAMRDPVYYRCNPMSHHRIGDKYKIYPTYDFACPFVDSLEGITHALRSSEYHDRNAQYFKVLEDMGLRQVQLYEFSRLNLVFTLLSKRKLLWFVQTGLVDGWDDPRFPTVQGIVRRGLKIEALIQFILEQGASKNLNLMEWDKLWSINKRIIDPVCPRHTAVVAERRVLFTLTDGPDEPFVRMIPKHKKFEGAGEKATTFTKSIWLEEADASAISVGEEVTLMDWGNAIVKEITKDEEGRVTALSGVLNLQGSVKTTKLKLTWLPDTNELVNLTLTEFDYLITKKKLEDDDEVADFVNPNTKKETLALGDSNMRNLKCGDVIQLERKGYFRCDVPFVKSSKPIVLFSIPDGRAAK

Sequence caution

The sequence AAC13597.1 differs from that shown. Reason: Erroneous gene model prediction

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias191-205Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF067773
EMBL· GenBank· DDBJ
AAC36469.1
EMBL· GenBank· DDBJ
mRNA
AF058914
EMBL· GenBank· DDBJ
AAC13597.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
CP002688
EMBL· GenBank· DDBJ
AED93573.1
EMBL· GenBank· DDBJ
Genomic DNA
AY099592
EMBL· GenBank· DDBJ
AAM20443.1
EMBL· GenBank· DDBJ
mRNA
BT000248
EMBL· GenBank· DDBJ
AAN15567.1
EMBL· GenBank· DDBJ
mRNA
AK226448
EMBL· GenBank· DDBJ
BAE98590.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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