uncharacterized members of the carbohydrate binding module 6 (CBM6) and CBM35_like superfamily. Carbohydrate binding module family 6 (CBM6, family 6 CBM), also known as cellulose binding domain family VI (CBD VI), and related CBMs (CBM35 and CBM36). These are non-catalytic carbohydrate binding domains found in a range of enzymes that display activities against a diverse range of carbohydrate targets, including mannan, xylan, beta-glucans, cellulose, agarose, and arabinans. These domains facilitate the strong binding of the appended catalytic modules to their dedicated, insoluble substrates. Many of these CBMs are associated with glycoside hydrolase (GH) domains. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. CBM36s are calcium-dependent xylan binding domains. CBM35s display conserved specificity through extensive sequence similarity, but divergent function through their appended catalytic modules.

Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases.

Pectate lyase superfamily protein. This family of proteins possesses a beta helical structure like Pectate lyase. This family is most closely related to glycosyl hydrolase family 28.

Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases.

Polysaccharide Lyase Family 6. Polysaccharide Lyase Family 6 is a family of beta-helical polysaccharide lyases. Members include alginate lyase (EC 4.2.2.3) and chondroitinase B (EC 4.2.2.19). Chondroitinase B is an enzyme that only cleaves the beta-(1,4)-linkage of dermatan sulfate (DS), leading to 4,5-unsaturated dermatan sulfate disaccharides as the product. DS is a highly sulfated, unbranched polysaccharide belonging to a family of glycosaminoglycans (GAGs) composed of alternating hexosamine (gluco- or galactosamine) and uronic acid (D-glucuronic or L-iduronic acid) moieties. DS contains alternating 1,4-beta-D-galactosamine (GalNac) and 1,3-alpha-L-iduronic acid units. The related chondroitin sulfate (CS) contains alternating GalNac and 1,3-beta-D-glucuronic acid units. Alginate lyases (known as either mannuronate (EC 4.2.2.3) or guluronate lyases (EC 4.2.2.11) catalyze the degradation of alginate, a copolymer of alpha-L-guluronate and its C5 epimer beta-D-mannuronate.

ChainA, Alpha-1,3-glucanase [Niallia circulans],5ZRU_C Chain C, Alpha-1,3-glucanase [Niallia circulans]

Crystalstructure of the catalytic unit of thermostable GH87 alpha-1,3-glucanase from Streptomyces thermodiastaticus strain HF3-3 [Streptomyces thermodiastaticus],7C7D_B Crystal structure of the catalytic unit of thermostable GH87 alpha-1,3-glucanase from Streptomyces thermodiastaticus strain HF3-3 [Streptomyces thermodiastaticus]

Catalyticdomain of GH87 alpha-1,3-glucanase from Paenibacillus glycanilyticus FH11 [Paenibacillus glycanilyticus],6K0N_A Catalytic domain of GH87 alpha-1,3-glucanase in complex with nigerose [Paenibacillus glycanilyticus]

Catalyticdomain of GH87 alpha-1,3-glucanase D1069A in complex with nigerose [Paenibacillus glycanilyticus],6K0V_A Catalytic domain of GH87 alpha-1,3-glucanase D1069A in complex with tetrasaccharides [Paenibacillus glycanilyticus],6K0V_B Catalytic domain of GH87 alpha-1,3-glucanase D1069A in complex with tetrasaccharides [Paenibacillus glycanilyticus],6K0V_C Catalytic domain of GH87 alpha-1,3-glucanase D1069A in complex with tetrasaccharides [Paenibacillus glycanilyticus],6K0V_D Catalytic domain of GH87 alpha-1,3-glucanase D1069A in complex with tetrasaccharides [Paenibacillus glycanilyticus]