Dyp-type peroxidase sequences can be detected in fungi, mycetozoa, bacteria and archaea. A distinct branch of this family has a typical twin-arginine dependent signal sequence (TAT domain) characteristic of exported proteins with bound redox cofactors. DyP from fungus show no homology to other fungal peroxidases such as LiP and MnP, and lacks the typical heme-binding region conserved among plant peroxidase superfamily (Sugano et al. 1999). DyP differs from MnP because of its ability to oxidize phenolic compounds, such as 2,6-dimethoxyphenol and guaiacol, in the absence of Mn2+. Moreover, DyP does not degrade non-phenolic compounds, thus differing from LiP.
Another singular characteristic of DyP is its ability to degrade several synthetic dyes (Kim and Shoda 1999), mainly anthraquinone dyes, which are not oxidized by most of the other peroxidases. As a fact LiP, versatile peroxidase (Ruiz-Duenas et al. 2001) and manganese-independent peroxidase (Ruiz-Duenas et al. 1999) have been reported to mainly degrade azo dyes.
Bacterial DyP sequences are not detected neither in Archeaebacteria nor in Chlamydiae/Verrucomicrobia nor in Cyanobacteria; they are poorly represented in Bacteroidetes/Chlorobi. Together with chlorite dismutases and EfeB known also as Heme Q they constitute a large CDE superfamily (Goblirsch et al. 2011) known also as the peroxidase-chlorite dismutase superfamily.
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