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.

CARDB. Cell adhesion related domain found in bacteria.

CARDB. Cell adhesion related domain found in bacteria.

Carbohydrate Binding Module 35 (CBM35) domains similar to Lmo2446. This family includes carbohydrate binding module 35 (CBM35) domains that are appended to several carbohydrate binding enzymes. Some CBM35 domains belonging to this family are appended to glycoside hydrolase (GH) family domains, including glycoside hydrolase family 31 (GH31), for example the CBM35 domain of Lmo2446, an uncharacterized protein from Listeria monocytogenes EGD-e. These CBM35s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. GH31 has a wide range of hydrolytic activities such as alpha-glucosidase, alpha-xylosidase, 6-alpha-glucosyltransferase, or alpha-1,4-glucan lyase, cleaving a terminal carbohydrate moiety from a substrate that may be a starch or a glycoprotein. Most characterized GH31 enzymes are alpha-glucosidases.

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 D1045A 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]