Displays both high peroxidase and manganese peroxidase activity. Is likely involved in lignin degradation. Also has a Mn-dependent oxidase mode of action that expands its substrate scope in vitro; is thus able to catalyze the O(2)- and Mn-dependent oxidative decarboxylation of 4-methoxymandelate to anisaldehyde. 1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = glycolaldehyde + guaiacol + H2O + vanillin 2 H(+) + H2O2 + 2 Mn(2+) = 2 H2O + 2 Mn(3+) 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O 2 H2O2 + Reactive Blue 5 = 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H(+) + 2 H2O + phthalate Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. kcat is 87 sec(-1) for peroxidase activity with ABTS as substrate. kcat is 34 sec(-1) for peroxidase activity with Reactive Blue 5 as substrate. kcat is 0.38 sec(-1) for peroxidase activity with Reactive Black 5 as substrate. kcat is 68 sec(-1) for peroxidase activity with 2,4-dichlorophenol as substrate. kcat is 24 sec(-1) for manganese peroxidase activity. Optimum pH is 4.5 for the H(2)O(2)-dependent oxidation of Reactive Blue 5, and 5.0 for the O(2)-dependent oxidation of 4-methoxymandelate. Exists both as a monomeric and oligomeric species in solution; the monomeric form contains no bound heme cofactor and is inactive. Although no signal sequence is found, the secretory machinery for actinomycetes is not fully characterized, and the low pH optimum for DyP2 along with the observation that many DyPs have been isolated from the secreted protein fraction imply that DyP2 could be secreted and still possibly play a role in extracellular oxidation chemistry (PubMed:23054399). Belongs to the DyP-type peroxidase family.