Annotation inferences using phylogenetic trees
Electronic Gene Ontology annotations created by ARBA machine learning models
Pseudomonas aeruginosa MdaB and WrbA are water-soluble two-electron quinone oxidoreductases with the potential to defend against oxidative stress.
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Purified P. aeruginosa orthologs of MdaB, ChrR, WrbA, NfsB and NQO1 reduce quinones by a two-electron route in vitro.
"In in vitro assays, each enzyme was shown to reduce quinone substrates with only minimal semiquinone formation."
Identification of NAD(P)H quinone oxidoreductase activity in azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone oxidoreductases belong to the same FMN-dependent superfamily of enzymes.
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PA4975 is noted as unusually similar to human NQO2, and its quinone reductase activity is cited from the Ackerley group's work.
"PA4975 is unusual in bacteria in that it shows significant sequence similarity to the human enzyme NQO2 (61% similarity)."
Functional genomics enables identification of genes of the arginine transaminase pathway in Pseudomonas aeruginosa.
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PA4975 is the last gene of the arginine-induced PA4981-PA4975 cluster; a knockout was made, but no PA4975-specific role in arginine catabolism is reported.
"As shown in Table 2 , the contiguous PA4981-to-PA4975 genes were coordinately induced to a high level by l -arginine in the argR mutant."