Glycoside hydrolase family 16 (IPR000757)

Short name: GH16

Overlapping homologous superfamilies

Domain relationships


The glycosyl hydrolases family 16 (GH16) [PMID: 1747104] contains functionally heterogeneous members, including lichenase (EC:; xyloglucan xyloglucosyltransferase (EC:; agarase (EC:; kappa-carrageenase (EC:; endo-beta-1,3-glucanase (EC:; endo-beta-1,3-1,4-glucanase (EC:; endo-beta-galactosidase (EC: These enzymes share a common ancestor and have diverged significantly in their primary sequence.

The GH16 catalytic domain has a classical sandwich-like beta-jelly roll fold, formed by two main, closely packed and curved antiparallel beta 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 [PMID: 12970344, PMID: 11435116].

Two closely clustered conserved glutamates have been shown [PMID: 8182059] to be involved in the catalytic activity of Bacillus licheniformis lichenase. This domain contains these residues.

GO terms

Biological Process

GO:0005975 carbohydrate metabolic process

Molecular Function

GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles