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Literature summary extracted from

  • Cheng, W.; Li, W.
    Structural insights into ubiquinone biosynthesis in membranes (2014), Science, 343, 878-881.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.5.1.39 crystal structures of the enzyme in its apo and substrate-bound states at 3.3 and 3.6 A resolution, respectively Aeropyrum pernix

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.5.1.39 membrane the enzyme has nine transmembrane helices and an extramembrane cap domain that surround a large central cavity containing the active site. To facilitate the catalysis inside membranes, UbiA has an unusual active site that opens laterally to the lipid bilayer Aeropyrum pernix 16020
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Organism

EC Number Organism UniProt Comment Textmining
2.5.1.39 Aeropyrum pernix Q9YBM8
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2.5.1.39 Aeropyrum pernix DSM 11879 Q9YBM8
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Synonyms

EC Number Synonyms Comment Organism
2.5.1.39 ubiA
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 Aeropyrum pernix