Gene Ontology annotation through association of InterPro records with GO terms
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Evolution of Ubiquinone Biosynthesis: Multiple Proteobacterial Enzymes with Various Regioselectivities To Catalyze Three Contiguous Aromatic Hydroxylation Reactions.
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Pseudomonas aeruginosa uses UbiH, UbiI and Coq7 instead of the E. coli UbiH, UbiI and UbiF set; UbiH and UbiI regioselectivities (C-1 and C-5) are expected to be conserved in beta- and gammaproteobacteria.
"Interestingly, the two gammaproteobacteria Pseudomonas aeruginosa and Thiobacillus ferrooxidans (also called Acidithiobacillus ferrooxidans) lack ubiF but possess instead a Coq7 homolog, which has been shown to complement the C-6 hydroxylation defect of an E. coli strain in which ubiF is deleted (16)."
ubiI, a new gene in Escherichia coli coenzyme Q biosynthesis, is involved in aerobic C5-hydroxylation.
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The crystal structure of E. coli UbiI shows the FAD-dependent PHBH fold of the UbiH/UbiI/UbiF family.
"This structure shares many features with the canonical FAD-dependent para-hydroxybenzoate hydroxylase and represents the first structural characterization of a monooxygenase involved in Q biosynthesis."
UniProt entry Q88CI2 for ubiH
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Unreviewed entry; its FAD cofactor, pathway and family comments are ARBA-only and are not used as support. Family signatures (NCBIfam TIGR01984 UbiH, InterPro IPR011295, PANTHER PTHR43876:SF8) are used.
Pairwise identity of P. putida KT2440 ring hydroxylases to E. coli UbiI, UbiH and UbiF
OpenScientist functional review of PSEPK ubiH