P48525 · SYEM_YEAST

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).

Miscellaneous

Present with 2940 molecules/cell in log phase SD medium.

Features

Showing features for binding site.

153650100150200250300350400450500
TypeIDPosition(s)Description
Binding site48-50L-glutamate (UniProtKB | ChEBI)
Binding site58ATP (UniProtKB | ChEBI)
Binding site84L-glutamate (UniProtKB | ChEBI)
Binding site235-239L-glutamate (UniProtKB | ChEBI)
Binding site253L-glutamate (UniProtKB | ChEBI)
Binding site256ATP (UniProtKB | ChEBI)
Binding site291-295ATP (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentmitochondrial matrix
Cellular Componentmitochondrion
Molecular FunctionATP binding
Molecular Functionglutamate-tRNA ligase activity
Molecular FunctiontRNA binding
Molecular Functionzinc ion binding
Biological Processglutamyl-tRNA aminoacylation
Biological Processmitochondrial glutamyl-tRNA aminoacylation
Biological Processmitochondrial translation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

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

Gene names

    • Name
      MSE1
    • Ordered locus names
      YOL033W

Organism names

Accessions

  • Primary accession
    P48525
  • Secondary accessions
    • D6W232
    • Q08203

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001197401-536Glutamate--tRNA ligase, mitochondrial

Proteomic databases

PTM databases

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for motif.

TypeIDPosition(s)Description
Motif53-61'HIGH' region
Motif291-295'KMSKS' region

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    536
  • Mass (Da)
    61,603
  • Last updated
    1997-11-01 v2
  • Checksum
    5CF36FBAD0E8C58C
MIMLRIPTRSYCSPSKLIKGVGLSPLKKSLLSKKIKEDIHPSLPVRTRFAPSPTGFLHLGSLRTALYNYLLARNTNGQFLLRLEDTDQKRLIEGAEENIYEILKWCNINYDETPIKQSERKLIYDKYVKILLSSGKAYRCFCSKERLNDLRHSAMELKPPSMASYDRCCAHLGEEEIKSKLAQGIPFTVRFKSPERYPTFTDLLHGQINLQPQVNFNDKRYDDLILVKSDKLPTYHLANVVDDHLMGITHVIRGEEWLPSTPKHIALYNAFGWACPKFIHIPLLTTVGDKKLSKRKGDMSISDLKRQGVLPEALINFCALFGWSPPRDLASKKHECFSMEELETIFNLNGLTKGNAKVDDKKLWFFNKHFLQKRILNPSTLRELVDDIMPSLESIYNTSTISREKVAKILLNCGGSLSRINDFHDEFYYFFEKPKYNDNDAVTKFLSKNESRHIAHLLKKLGQFQEGTDAQEVESMVETMYYENGFSRKVTYQAMRFALAGCHPGAKIAAMIDILGIKESNKRLSEGLQFLQREKK

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict464in Ref. 1; AAA61403

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L39015
EMBL· GenBank· DDBJ
AAA61403.1
EMBL· GenBank· DDBJ
Genomic DNA
Z74775
EMBL· GenBank· DDBJ
CAA99033.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006948
EMBL· GenBank· DDBJ
DAA10748.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp