Conserved Site

Glycoside hydrolase family 27/36, conserved site (IPR000111)

Short name: Glyco_hydro_27/36_CS


O-Glycosyl hydrolases (EC:3.2.1.) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [PMID: 7624375, PMID: 8535779]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site. Families 27 (GH27) and 36 (GH36) encompasses alpha-galactosidases and alpha-N-acetylgalactosaminidases.

Alpha-galactosidase (EC (melibiase) [PMID: 4561015] catalyses the hydrolysis of melibiose into galactose and glucose. In man, the deficiency of this enzyme is the cause of Fabry's disease (X-linked sphingolipidosis). Alpha-galactosidase is present in a variety of organisms. There is a considerable degree of similarity in the sequence of alpha-galactosidase from various eukaryotic species. Escherichia coli alpha-galactosidase (gene melA), which requires NAD and magnesium as cofactors, is not structurally related to the eukaryotic enzymes; by contrast, an Escherichia coli plasmid encoded alpha-galactosidase (gene rafA) [PMID: 2556373] contains a region of about 50 amino acids which is similar to a domain of the eukaryotic alpha-galactosidases.

Alpha-N-acetylgalactosaminidase (EC [PMID: 2174888] catalyses the hydrolysis of terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-alpha-D-galactosaminides. In man, the deficiency of this enzyme is the cause of Schindler and Kanzaki diseases. The sequence of this enzyme is highly related to that of the eukaryotic alpha-galactosidases.

This entry represents a conserved site in families 27 and 36. It contains two conserved aspartic acid residues which could be involved in the catalytic mechanism.

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 patterns