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Fig. S1. Multiple-sequence alignment of SHMTs from bacteria and archaea obtained using clustalw program on UniProt server. Asterisks denote identical residues. Colons and periods correspond to highly and weakly conserved residues. White letters on black ground and dark-shaded letters indicate amino acids expected to form hydrogen bonds and hydrophobic interactions with l-allo-threonine–PLP aldimine, respectively, based on sequence similarity with bsSHMT, whose crystal structure is determined in complex with l-allo-threonine.

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