Glycoside hydrolase, family 33, N-terminal (IPR004124)

Short name: Glyco_hydro_33_N

Overlapping homologous superfamilies

Domain relationships



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.

Sialidases (GH33) hydrolyse alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)-glycosidic linkages of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates. Sialidases may act as pathogenic factors in microbial infections [PMID: 2034213].

The 1.8 A structure of trans-sialidase from leech (Macrobdella decora, Q27701) in complex with 2-deoxy-2, 3-didehydro-NeuAc was solved. The refined model comprising residues 81-769 has a catalytic beta-propeller domain, a N-terminal lectin-like domain and an irregular beta-stranded domain inserted into the catalytic domain [PMID: 9562562].

GO terms

Biological Process

GO:0005975 carbohydrate metabolic process

Molecular Function

GO:0004308 exo-alpha-sialidase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

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