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Fig. 5.

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Fig. 5. Comparison of xylanases in S. viridodiastaticus and S. lividans. (A) Comparison of primary structures in xylanase C (XynCliv) obtained from S. lividans and its orthologue (XynCvir) obtained from S. viridodiastaticus. The signal peptide cleavage sites predicted by SignalP 6.0 are indicated by arrows, and the amino-terminal amino acid sequence confirmed in mature form of XynCvir is indicated by a box. (B) Phylogenetic relationship between three xylanases reported in S. lividans and S. viridodiastaticus. An evolutionary tree was constructed using the neighbor-joining method in the MEGA 6 program. The subjects used to construct the phylogenetic tree included three xylanases from S. lividans—xylanase A (XynAliv), xylanase B (XynBliv), and xylanase C (XynCliv)—and three xylanases from S. viridodiastaticus—xylanase A (XynAvir), xylanase B (XynBvir), and xylanase C (XynCvir). An evolutionarily distant xylanase (AAB84458.1) from Bacillus subtilis was also included in the tree. The evolutionary distance was calculated using the Poisson correction method. Sequence IDs of proteins are indicated in parentheses.
J. Microbiol. Biotechnol. 2024;34:176~184
© J. Microbiol. Biotechnol.