Figure 1

Structure-based multiple sequence alignment of the catalytic (NodB-like) domains of CE4 family enzymes. The alignment comprises four enzymes with known deacetylase activity and three putative chitin deacetylases from Aspergillus nidulans FGSC A4, AnCDA (EAA66447, this study), EAA65017 and ACF22099. The other enzymes are: SlCE4, acetyl xylan deacetylase from Streptomyces lividans, AAC06115.2¹⁷; SpPgdA, peptidoglycan deacetylase from Streptococcus pneumoniae, NP_358926¹⁵; ClCDA, CDA from Colletotrichum lindemuthianum, AAT68493⁹; VcCDA, CDA from Vibrio cholerae, AAF94439.1¹⁸. Fully conserved residues in the five sequence motifs that are important for activity (see text)¹⁵ are shown with yellow background. The purple background indicates aromatic surface residues in AnCDA that are discussed in the text. Blue asterisks indicate residues in the metal binding triad, while pink dots indicate the catalytic acid and base^{15, 17}. The alignment was prepared with PyMod 2.0 (plugin in PyMol)⁵¹ by doing a structure based sequence alignment of AnCDA, SlCE4, SpPgdA, ClCDA, and VcCDA, before adding EAA65017 and ACF22099 to the alignment.