Protein Domain : Glycoside hydrolase family 16 IPR000757

Type	Domain
Description	The glycosyl hydrolases family 16 (GH16) [ ] contains functionally heterogeneous members, including lichenase (); xyloglucan xyloglucosyltransferase ( ); agarase ( ); kappa-carrageenase ( ); endo-beta-1,3-glucanase ( ); endo-beta-1,3-1,4-glucanase ( ); endo-beta-galactosidase ( ). These enzymes share a common ancestor and have diverged significantly in their primary sequence. The GH16 catalytic domain has a classical sandwich-like β-jelly roll fold, formed by two main, closely packed and curved antiparallel β-sheets, creating a deep channel harboring the catalytic machinery. Even though the GH16 domains have now diverged significantly in their primary sequences, they all feature a common catalytic motif, E-[ILV]-D-[IVAF]-[VILMF](0,1)-E. The two glutamic acid residues in the conserved motif are the nucleophile and the general base involved in catalysis, whereas the aspartic acid residue is important in maintaining the relative position of these catalytic amino acids [, ].Two closely clustered conserved glutamates have been shown [ ] to be involved in the catalytic activity of Bacillus licheniformis lichenase. This domain contains these residues.
Short Name	GH16