Superoxide dismutases serve to convert damaging superoxide radicals, a key form of ROS, to less damaging hydrogen peroxide that can be converted into water by catalase action (By similarity). Degrades host-derived reactive oxygen species to escape innate immune surveillance (By similarity). Involved in the occurrence of miconazole-tolerant persisters in biofilms (By similarity). Persisters are cells that survive high doses of an antimicrobial agent. The unusual attributes of SOD5-like fungal proteins, including the absence of zinc and an open active site that readily captures extracellular copper, make these SODs well suited to meet challenges in zinc and copper availability at the host-pathogen interface (By similarity). 2 H(+) + 2 superoxide = H2O2 + O2 Binds 1 copper ion per subunit. Monomer. Covalently-linked GPI-modified cell wall protein (GPI-CWP). Expression is down-regulated in presence of human keratinocytes. The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer. Belongs to the Cu-Zn superoxide dismutase family. Although the beta-barrel of Cu/Zn SODs is largely preserved, SOD5 is a monomeric copper protein that lacks a zinc-binding site and is missing the electrostatic loop element proposed to promote catalysis through superoxide guidance. Without an electrostatic loop, the copper site of SOD5 is not recessed and is readily accessible to bulk solvent.