IPR013222
Glycosyl hydrolase family 98, putative carbohydrate-binding module
InterPro entry
Short name | Glyco_hyd_98_carb-bd |
Overlapping homologous superfamilies |
Description
This entry represents a putative carbohydrate binding module (NPCBM) domain found at the N terminus of glycosyl hydrolase family 98 proteins
[2].
Proteins containing this domain include CpGH98 from C. perfringens. It specifically hydrolyses fucose-containing trisaccharides from the glycotopes of blood groups A and B and is implicated for the infectivity and virulence of this pathogen
[1]. CpGH98 has a central TIM barrel catalytic domain, in which putative catalytic residues may be tentatively identified, and an N-terminal novel putative carbohydrate binding module (NPCBM)
[1].
NPCBM domains found in bacterial conflict systems are predicted to interact with invasive molecules and recruit downstream effectors
[3].
References
1.A clostridial endo-beta-galactosidase that cleaves both blood group A and B glycotopes: the first member of a new glycoside hydrolase family, GH98. Anderson KM, Ashida H, Maskos K, Dell A, Li SC, Li YT. J. Biol. Chem. 280, 7720-8, (2005). View articlePMID: 15618227
2.Analysis of glycoside hydrolase family 98: catalytic machinery, mechanism and a novel putative carbohydrate binding module. Rigden DJ. FEBS Lett. 579, 5466-72, (2005). View articlePMID: 16212961
Cross References
Representative structure
2vmh: The structure of CBM51 from Clostridium perfringens GH95