Functional analysis of α-1,3-glucanase domain structure from <i>Streptomyces thermodiastaticus</i> HF3-3

α-1,3-Glucanase from Streptomyces thermodiastaticus HF3-3 (Agl-ST) has been classified in the glycoside hydrolase (GH) family 87. Agl-ST is a multi-modular domain consisting of an N-terminal β-sandwich (β-SW), catalytic domain, uncharacterized (UC), and C-terminal discoidin (DS). Although did not hydrolyze α-1,4-glycosidic bonds, its amino acid sequence more similar to GH87 mycodextranase than α-1,3-glucanase. It might be categorized into new subfamily GH87. In this study, we investigated function domains. Several fusion proteins domains with green fluorescence protein (GFP) were constructed clarify each domain. The results showed that β-SW DS played role binding α-1,3-glucan enhancing hydrolysis α-1,3-glucan. domains, DS, also activity toward xylan, although it was lower for combination demonstrated high activities α-1,3-glucan, whereas only function. achieved effective cell wall complex Schizophyllum commune.