Glutathione peroxidase-like protein that protects cells from phospholipid hydroperoxides and nonphospholipid peroxides during oxidative stress (PubMed:10480913, PubMed:11445588). Has peroxidase activity using thioredoxin or glutathione as a reducing power (PubMed:20572871, PubMed:22659048). Involved in peroxisome formation (PubMed:22659048). 2 glutathione + H2O2 = glutathione disulfide + 2 H2O [thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O Monomer. By glucose starvation. Impairs growth and peroxisome formation in oleic acid medium. The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this atypical 2-Cys peroxiredoxin, C(R) is present in the same subunit to form an intramolecular disulfide. Belongs to the glutathione peroxidase family. Was originally thought to be a glutathione peroxidase (PubMed:10480913) or a phospholipid hydroperoxide glutathione peroxidase (PubMed:11445588), but functions as an atypical 2-Cys peroxiredoxin using both glutathione and thioredoxin almost equally as reducing power instead (PubMed:20572871).