Figure - available from: Frontiers in Microbiology
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Comparison of amino acid sequences of StKatG homologs. (A) Sequence alignment of StKatG1 and StKatG2. The sequences were aligned using the Clustal Omega and treated with ESPript 3 (https://espript.ibcp.fr/). The secondary structure elements presented on top were obtained from the predicted StKatG2 structure using Alphafold3 (α, α-helices; η, 3 10 helices; β, β-strands. TT, turns). Identical and similar residues are displayed in red and blue boxes, respectively. (B) Phylogenetic tree of KatG proteins from Salinicola tamaricis and other species. StKatG1 and StKatG2, Salinicola tamaricis KatGs; DkKatG, Drosophila kikkawai KatG; BpKatG, Burkholderia pseudomallei KatG; SeKatG, Salmonella enterica KatG; EcKatG, Escherichia coli KatG; SdKatG, Shigella dysenteriae KatG; RpKatG, Ralstonia pickettii KatG; BtKatG, Burkholderia thailandensis KatG; MpKatG, Methylibium petroleiphilum KatG; AvCP01, Azotobacter vinelandii KatG. The evolutionary analyses were conducted based on amino acid homology using the MEGA7. Bootstrap values are shown at branch points. (C) Predicted structures of StKatG1 and StKatG2 using AlphaFold3, with the manganese binding site in StKatG2 represented as a purple sphere.
Source publication
Manganese (Mn) oxidation processes have garnered significant attention recently due to their potential for degrading organic pollutants. These processes are primarily catalyzed by Mn(II) oxidases. Salinicola tamaricis F01, an endophytic bacterium derived from wetland plants, has demonstrated Mn(II)-oxidizing capacity. In this study, a catalase-pero...
