Glycosyl hydrolase family 76. Family of alpha-1,6-mannanases.

Predicted alpha-1,6-mannanase, GH76 family [Carbohydrate transport and metabolism].

Carbohydrate Binding Module 6 (CBM6); many are appended to glycoside hydrolase (GH) family 11 and GH43 xylanase domains. This family includes carbohydrate binding module 6 (CBM6) domains that are appended mainly to glycoside hydrolase (GH) family domains, including GH3, GH11, and GH43 domains. These CBM6s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. Examples of proteins having CMB6s belonging to this family are Microbispora bispora GghA, a 1,4-beta-D-glucan glucohydrolase (GH3); Clostridium thermocellum xylanase U (GH11), and Penicillium purpurogenum ABF3, a bifunctional alpha-L-arabinofuranosidase/xylobiohydrolase (GH43). GH3 comprises enzymes with activities including beta-glucosidase (hydrolyzes beta-galactosidase) and beta-xylosidase (hydrolyzes 1,4-beta-D-xylosidase). GH11 family comprises enzymes with xylanase (endo-1,4-beta-xylanase) activity which catalyze the hydrolysis of beta-1,4 bonds of xylan, the major component of hemicelluloses, to generate xylooligosaccharides and xylose. GH43 includes beta-xylosidases and beta-xylanases, using aryl-glycosides as substrates. 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.

Ricin-type beta-trefoil lectin domain-like.

Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins. LanM-like proteins. LanM is a bifunctional enzyme, involved in the synthesis of class II lantibiotics. It is responsible for both the dehydration and the cyclization of the precursor-peptide during lantibiotic synthesis. The C-terminal domain shows similarity to LanC, the cyclase component of the lan operon, but the N terminus seems to be unrelated to the dehydratase, LanB.

ChainA, Alpha-1,6-mannanase [Niallia circulans]

ChainA, Alpha-1,6-mannanase [Niallia circulans],4BOJ_B Chain B, Alpha-1,6-mannanase [Niallia circulans],4BOJ_C Chain C, Alpha-1,6-mannanase [Niallia circulans]

ChainA, Alpha-1,6-mannanase [Niallia circulans],4D4A_B Chain B, Alpha-1,6-mannanase [Niallia circulans],4D4B_A Chain A, Alpha-1,6-mannanase [Niallia circulans],4D4B_B Chain B, Alpha-1,6-mannanase [Niallia circulans],4D4C_A Chain A, Alpha-1,6-mannanase [Niallia circulans],4D4C_B Chain B, Alpha-1,6-mannanase [Niallia circulans],4D4D_A Chain A, Alpha-1,6-mannanase [Niallia circulans],4D4D_B Chain B, Alpha-1,6-mannanase [Niallia circulans],5N0F_A Chain A, Alpha-1,6-mannanase [Niallia circulans],5N0F_B Chain B, Alpha-1,6-mannanase [Niallia circulans],6ZBX_A Chain A, Alpha-1,6-mannanase [Niallia circulans],6ZBX_B Chain B, Alpha-1,6-mannanase [Niallia circulans],7NL5_A Chain A, Alpha-1,6-mannanase [Niallia circulans]

ChainA, Alpha-1,6-mannanase [Niallia circulans],5M77_B Chain B, Alpha-1,6-mannanase [Niallia circulans]

ChainA, Alpha-1,6-mannanase [Niallia circulans],5AGD_B Chain B, Alpha-1,6-mannanase [Niallia circulans],6ZBM_A Chain A, Alpha-1,6-mannanase [Niallia circulans],6ZBW_A Chain A, Alpha-1,6-mannanase [Niallia circulans],6ZBW_B Chain B, Alpha-1,6-mannanase [Niallia circulans]