Gene Ontology annotation based on Enzyme Commission mapping

Annotation inferences using phylogenetic trees

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

GO_REF:0000117

Electronic Gene Ontology annotations created by ARBA machine learning models

PMID:25085734

Pseudomonas aeruginosa MdaB and WrbA are water-soluble two-electron quinone oxidoreductases with the potential to defend against oxidative stress.

Purified PA2580 reduces quinones by two-electron transfer; overexpression protects a katA mutant, but not wild type, against H2O2.

"in a katA mutant, H2O2 challenged strains over-expressing the WrbA and MdaB orthologs grew significantly better than the empty plasmid control."

PMID:14977943

An NADPH quinone reductase of Helicobacter pylori plays an important role in oxidative stress resistance and host colonization.

H. pylori mdaB mutant is sensitive to oxygen, peroxides and paraquat; the enzyme is an NADPH-preferring two-electron quinone reductase.

"The mdaB mutant is also more sensitive to H(2)O(2), organic hydroperoxides, and the superoxide-generating agent paraquat."

PMID:17923370

The NADPH quinone reductase MdaB confers oxidative stress resistance to Helicobacter hepaticus.

H. hepaticus mdaB mutant is sensitive to oxygen and peroxides.

"the mdaB strain was clearly inhibited at this oxygen level"

PMID:16630630

Modulator of drug activity B from Escherichia coli: crystal structure of a prokaryotic homologue of DT-diaphorase.

E. coli MdaB is an FAD flavoprotein; the null mutant is not menadione-sensitive.

"We have shown by mass spectrometry that the endogenously associated cofactor is flavin adenine dinucleotide"

file:PSEAE/PA2580/PA2580-uniprot.txt

UniProt entry Q9I0Q6 (unreviewed)