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Literature summary for 2.3.1.234 extracted from

  • Thiaville, P.C.; El Yacoubi, B.; Perrochia, L.; Hecker, A.; Prigent, M.; Thiaville, J.J.; Forterre, P.; Namy, O.; Basta, T.; de Crecy-Lagard, V.
    Cross kingdom functional conservation of the core universally conserved threonylcarbamoyladenosine tRNA synthesis enzymes (2014), Eukaryot. Cell, 13, 1222-1231.
    View publication on PubMedView publication on EuropePMC
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Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion Sua5 catalyzes the first step leading to the threonyl-carbamoyl-AMP intermediate. Proteins Qri7 and Sua5 together constitute the mitochondrial pathway for the biosynthesis of N6-threonylcarbamoyladenosine. The import of cytoplasmic Sua5 into the mitochondria is required for this organelle to be functional Saccharomyces cerevisiae 5739
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Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P43122
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Synonyms

Synonyms Comment Organism
Qri7
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 Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function threonylcarbamoyl-AMP synthase Sua5 catalyzes the first step leading to the threonyl-carbamoyl-AMP intermediate. Proteins Qri7 and Sua5 together constitute the mitochondrial pathway for the biosynthesis of N6-threonylcarbamoyladenosine. The import of cytoplasmic Sua5 into the mitochondria is required for this organelle to be functional. In vitro, yeast Qri7 can function with either Sua5 or Escherichia coli TsaC. In vivo, Qri7 requires Sua5 Saccharomyces cerevisiae