TreeGrafter-generated GO annotations
Combined Automated Annotation using Multiple IEA Methods
The role of UbiX in Escherichia coli coenzyme Q biosynthesis.
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UbiX and UbiD are both required for decarboxylation of the UbiA product in E. coli.
"Our results suggest that both UbiX and UbiD are required for the decarboxylation of 4-hydroxy-3-octaprenyl-benzoate in E. coli coenzyme Q biosynthesis, especially during logarithmic growth."
Isofunctional enzymes PAD1 and UbiX catalyze formation of a novel cofactor required by ferulic acid decarboxylase and 4-hydroxy-3-polyprenylbenzoic acid decarboxylase.
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UbiX and UbiD form a two-component decarboxylase system sharing the flavin-derived cofactor used by Pad1/Fdc1.
"Our results suggest that UbiX and UbiD constitute a similar two-component decarboxylase system and that the same flavin-based cofactor is necessary for the biosynthesis of ubiquinone."
A Soluble Metabolon Synthesizes the Isoprenoid Lipid Ubiquinone.
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The seven-protein E. coli Ubi complex (UbiE, F, G, H, I, J, K) catalyses the last six reactions; UbiD is not a member.
"Here, we demonstrate that seven Ubi proteins form the Ubi complex, a stable metabolon that catalyzes the last six reactions of the UQ biosynthetic pathway in Escherichia coli."
Membrane-associated reactions in ubiquinone biosynthesis in Escherichia coli. 3-Octaprenyl-4-hydroxybenzoate carboxy-lyase.
UniProt entry Q88CG8 for ubiD
UniProt entry Q88C65 for ubiA
OpenScientist functional review of PSEPK ubiD