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. 2022 Aug 24;88(17):e00806-22. doi: 10.1128/aem.00806-22

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Copyright © 2022 Wang et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license.

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FIG 4 — In silico analysis of the FAD-dependent halogenase (FDH) OrfA. (A) The ML tree for FDHs in different clades. Each clade is given by bootstrap percentage values, and each terminal branch corresponds to a given enzyme in FDHs. Color stands for a specific substrate for one type of FDH; blue, peptides; yellow, free Trp; green, phenyl, alkenyl, and alkyl groups of substrates tethered to a carrier protein (tethered substrates). (B) Multisequence alignment of OrfA with selected FDHs, MibH, PyrH, PrnA, RebH, ThaI, PltA, CndH, XanH, and LlpH. The red frames highlight two conserved motifs, GXGXXG and WXWXIP, in FDHs, which are also presented in sequence logos. The numbering for two logos does not reflect the correct individual sequence number. The multisequence alignment was generated by ClustalW version 2.0, and the sequence logos were generated by WebLogo version 2.8.2.