Non-specific peroxidase that can use thioredoxin or glutathione as a reducing agent. In vitro, utilizes preferentially thioredoxin A to decompose hydrogen peroxide as well as cumene-, tert-butyl-, and linoleic acid hydroperoxides, suggesting that it may have one or more organic hydroperoxide as its physiological substrate. 2 glutathione + H2O2 = glutathione disulfide + 2 H2O [thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O Appears to have a periplasmic location. It has the mean hydropathy of a soluble protein but lacks an obvious signal sequence. Induced by oxidative stress conditions. Deletion has no significant effect on the binding, transport or utilization of vitamin B12 or other cobalamins. Belongs to the glutathione peroxidase family. BtuE subfamily. Part of the btuCED operon, and was originally thought to participate in the transport of vitamin B12, but it was shown later that it plays no essential role in vitamin B12 transport.