Abstract
Laccases (EC 1.10.3.2), a group of multi-copper oxidases (MCOs), play multiple biological functions and widely exist in many species. Fungal laccases have been extensively studied for their industrial applications, however, there was no database specially focused on fungal laccases. To provide a comparative genomics platform for fungal laccases, we have developed a comparative genomics platform for laccases and MCOs (http://laccase.riceblast.snu.ac.kr/). Based on protein domain profiles of characterized sequences, 3,571 laccases were predicted from 690 genomes including 253 fungi. The number of putative laccases and their properties exhibited dynamic distribution across the taxonomy. A total of 505 laccases from 68 genomes were selected and subjected to phylogenetic analysis. As a result, four clades comprised of nine subclades were phylogenetically grouped by their putative functions and analyzed at the sequence level. Our work would provide a workbench for putative laccases mainly focused on the fungal kingdom as well as a new perspective in the identification and classification of putative laccases and MCOs.
Highlights
Laccases (EC 1.10.3.2), the biggest subgroup of multi-copper oxidases (MCOs), are known to catalyze the oxidation of a broad range of substrates such as phenolic compounds and aromatic amines [1]
We present the Fungal Laccase Database which would serve as a database mainly focused on fungal species based on protein domain profiles
Laccases account for the largest family of multi-copper oxidase superfamily, accurate definition of laccases still remains elusive [26,67]
Summary
Laccases (EC 1.10.3.2), the biggest subgroup of multi-copper oxidases (MCOs), are known to catalyze the oxidation of a broad range of substrates such as phenolic compounds and aromatic amines [1]. Laccases have been actively investigated for their ability in the degradation of a variety of compounds, such as phenols, ascorbates, amines, lignin, and phosphates. CotA, a laccase in Bacillus subtilis, for example, played additional roles as bilirubin oxidase activity and in brown pigmentation in spore coat [9,10]. Laccases were known to be involved in ectopic lignin polymerization and seed coat browning in Arabidopsis thaliana [11,12]. In other plant species Liriodendron tulipifera, laccases were reported to have putative roles in iron uptake or weak electron acceptor in cytokinin degradation [13,14]
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