Fig. 1

Alignment of the MtCh509 amino acid sequence with other bacterial chitinases. Similar sequences are marked by boxes and identical sequences are highlighted in red. The chitin-binding domain and the SXGG and DXXDXDXE motifs are marked with black, red, and blue lines under the sequences, respectively. The conserved catalytic proton donor is marked with a black inverted triangle. The conserved α + β insertion domain is marked with a gray line. Secondary structural elements (i.e., alpha helix [α], beta sheet [β], random coil [ƞ], and beta turn [T]) are marked on the MtCh509 sequence. MtCh509: chitinase from M. thermotolerance DAU221 (WP_06714446); S. aga: glycosyl hydrolase from Simiduia agarivorans (WP_015046629); C. jap: glycosyl hydrolase from Cellvibrio japonicus (WP_012488573); C. mix: glycosyl hydrolase from Cellvibrio mixtus (WP_039915554); G. aga: glycosyl hydrolase from Gilvimarinus agarilyticus (WP_041522559); and S. deg: glycosyl hydrolase from Saccharophagus degradans (WP_011468184)