Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Comparison of the genomes of two Xanthomonas pathogens with differing host specificities
The Escherichia coli btuE gene, encodes a glutathione peroxidase that is induced under oxidative stress conditions.
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Purified E. coli BtuE (P06610), which is in the same PANTHER subfamily and PAINT clade (PTN000173904) as Q8P365, reduces H2O2 and cumene, tert-butyl and linoleic acid hydroperoxides. It prefers thioredoxins A or C to glutathione as the reductant.
"Figure 2 shows that BtuE uses preferentially thioredoxins A or C as reducing agents irrespective of the peroxide substrate."
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E. coli btuE expression is induced by oxidative-stress elicitors.
"The btuE gene was induced when cells were exposed to oxidative stress elicitors that included potassium tellurite, menadione and hydrogen peroxide"
UniProt record for Q8P365 (btuE)
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UniProt classifies Q8P365 as a glutathione peroxidase belonging to the glutathione peroxidase family, with an active site at position 37 and conserved GSHPx, thioredoxin-like fold, and GPX active site domains.
Falcon deep research for btuE (Q8P365)
Q8P365 re-review bioinformatics (PANTHER tree placement and alignment to E. coli BtuE)
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In the PANTHER 19 tree, Q8P365 descends from PTN000173904 (Gammaproteobacteria, SF40) together with E. coli BtuE. The Xanthomonas paralog Q8PAI2 arises from a lineage-specific duplication. Q8P365 is 49% identical to P06610, with conserved C37, C83, Q71, W143 and N144.