In this research, 63 complete amino acid sequences of laccase enzymes from fungi (40), bacteria (5), insects (8), and plants (10) were used for a phylogenetic analysis. A common ancestor that diverged in the laccases in prokaryote and eukaryote was observed. Additionally, it was determined that there was a difference in the type of amino acids bound to the histidines linked to the copper atoms of the active site, and that a fungal laccase of approximately 279 Ma was an ancestor of the laccases in the basidiomycetes considered in this study. In contrast, Lacc 6 of Pleurotus ostreatus was used as a template to generate mutants. Through modeling, the changes in the secondary and tertiary structures of this enzyme were observed with the substitution of amino acids adjacent to histidines in the conserved region of the active site, via the presence of amino acids in a similar place in the laccases of bacteria.