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 WrbA (and four other quinone reductases) reduce quinone substrates in vitro with minimal semiquinone formation.
"In in vitro assays, each enzyme was shown to reduce quinone substrates with only minimal semiquinone formation."
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Over-expression gives no H2O2-protective phenotype in wild-type P. aeruginosa; protection is seen only in a katA mutant.
"in a katA mutant, H2O2 challenged strains over-expressing the WrbA and MdaB orthologs grew significantly better than the empty plasmid control."
WrbA from Escherichia coli and Archaeoglobus fulgidus is an NAD(P)H:quinone oxidoreductase.
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E. coli and A. fulgidus WrbA are FMN-containing NAD(P)H:quinone oxidoreductases; the paper defines WrbA as type IV NQO.
"Biochemical characterization of the prototypic WrbA protein from E. coli and WrbA from Archaeoglobus fulgidus, a hyperthermophilic species from the Archaea domain, shows that these enzymes have NQO activity"
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The only mention of P. aeruginosa is its published crystal structure; no P. aeruginosa protein was assayed.
"The presence of this fold has recently been confirmed in the published crystal structures of the Deinococcus radiodurans and Pseudomonas aeruginosa WrbA homologues"
Crystal structures of the tryptophan repressor binding protein WrbA and complexes with flavin mononucleotide.
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Crystal structures of P. aeruginosa WrbA show one FMN per protomer in a homotetramer.
"each WrbA protein forms a homotetramer with 222 symmetry, unique among flavodoxin-like proteins, in which each protomer binds one flavin mononucleotide cofactor molecule."
Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Automatic Gene Ontology annotation based on Rhea mapping
Combined Automated Annotation using Multiple IEA Methods