Reviewed all 13 annotations. Accepted valid broad peroxidase, oxidoreductase, antioxidant, stress-response and redox-homeostasis annotations, plus bacterial cytosol and direct hydrogen peroxide catabolism. Additional organic hydroperoxide substrates do not exclude H2O2 catabolism. PMID:12483614 identifies a soluble AhpC and cotranscribed ahpF in KT2442; PMID:17107553 supports OxyR regulation of P. putida peroxide-degrading enzymes. Existing OpenScientist and Falcon findings are incorporated without blindly adopting their exact locus/accession claims.
QuickGO GO:0008379 was checked on 2026-09-20 and explicitly reports isObsolete=true. The source identifier is retained; the existing peroxiredoxin replacement is appropriate. The AhpCF system is NADH-dependent, while AhpC receives electrons from AhpF; the donor-independent single-subunit refinement is retained with that scope distinction explicit. A curation second opinion may address use of the system-level NADH-dependent term on AhpC, but the existing report already discusses this mechanism and no duplicate thioredoxin hypothesis was requested.
Remove a duplicate evidence entry and retain localization-specific evidence on localization rows. Source GOA assertions are unchanged.