Endo-alpha-N-acetylgalactosaminidase. Virulence of pathogenic organisms such as the Gram-positive Streptococcus pneumoniae is largely determined by the ability to degrade host glycoproteins and to metabolize the resultant carbohydrates. This family is the enzymatic region, EC:3.2.1.97, of the cell surface proteins that specifically cleave Gal-beta-1,3-GalNAc-alpha-Ser/Thr (T-antigen, galacto-N-biose), the core 1 type O-linked glycan common to mucin glycoproteins. This reaction is exemplified by the S. pneumoniae protein Endo-alpha-N-acetylgalactosaminidase, where Asp764 is the catalytic nucleophile-base and Glu796 the catalytic proton donor.

Endo-a-N-acetylgalactosaminidase and related glcyosyl hydrolases. This family contains the enzymatically active domain of cell surface proteins that specifically cleave Gal-beta-1,3-GalNAc-alpha-Ser/Thr (T-antigen, galacto-N-biose), the core 1 type O-linked glycan common to mucin glycoproteins (EC:3.2.1.97). It has been classified as glycosyl hydrolase family 101 in the Cazy resource. Virulence of pathogenic organisms such as the Gram-positive Streptococcus pneumoniae and other commensal human bacteria is largely determined by their ability to degrade host glycoproteins and to metabolize the resultant carbohydrates.

NPCBM/NEW2 domain. This novel putative carbohydrate binding module (NPCBM) domain is found at the N-terminus of glycosyl hydrolase family 98 proteins. This domain has also been called the NEW2 domain (Naumoff DG. Phylogenetic analysis of alpha-galactosidases of the GH27 family. Molecular Biology (Engl Transl). (2004)38:388-399.)

Galactose mutarotase-like fold domain. This domain is found in endo-alpha-N-acetylgalactosaminidase present in Streptococcus pneumoniae. Endo-alpha-N-acetylgalactosaminidase is a cell surface-anchored glycoside hydrolase involved in the breakdown of mucin type O-linked glycans. The domain, known as domain 2, exhibits strong structural similarlity to the galactose mutarotase-like fold but lacks the active site residues. Domains, found in a number of glycoside hydrolases, structurally similar to domain 2 confer stability to the multidomain architectures.

This novel putative carbohydrate binding module (NPCBM) domain is found at the N-terminus of glycosyl hydrolase family 98 proteins.

Crystalstructure of endo-alpha-N-acetylgalactosaminidase from Bifidobacterium longum (EngBF) [Bifidobacterium longum]

EngBFDARPin Fusion 9b 3G124 [Bifidobacterium longum]

EngBFDARPin Fusion 4b H14 [Bifidobacterium longum]

EngBFDARPin Fusion 4b G10 [Bifidobacterium longum]

EngBFDARPin Fusion 4b B6 [Bifidobacterium longum]

Putative endo-alpha-N-acetylgalactosaminidase OS=Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235) OX=288705 GN=RSal33209_1326 PE=3 SV=2

Endo-alpha-N-acetylgalactosaminidase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=SP_0368 PE=1 SV=1

Endo-alpha-N-acetylgalactosaminidase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=spr0328 PE=1 SV=1

Serine-rich adhesin for platelets OS=Staphylococcus aureus (strain MRSA252) OX=282458 GN=sasA PE=3 SV=1

Serine-rich adhesin for platelets OS=Staphylococcus aureus (strain MSSA476) OX=282459 GN=sraP PE=3 SV=1