Species | Streptococcus oralis_E | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Streptococcus; Streptococcus oralis_E | |||||||||||
CAZyme ID | MGYG000003739_00314 | |||||||||||
CAZy Family | GH101 | |||||||||||
CAZyme Description | Endo-alpha-N-acetylgalactosaminidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 44911; End: 51210 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH101 | 595 | 1303 | 0 | 0.9985855728429985 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam12905 | Glyco_hydro_101 | 3.86e-161 | 846 | 1136 | 1 | 273 | 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. |
cd14244 | GH_101_like | 2.44e-131 | 859 | 1159 | 1 | 298 | 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. |
pfam18080 | Gal_mutarotas_3 | 1.64e-114 | 593 | 845 | 1 | 243 | 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. |
pfam17974 | GalBD_like | 3.32e-104 | 1466 | 1663 | 1 | 190 | Galactose-binding domain-like. Proteins containing a galactose-binding domain-like fold can be found in several different protein families, in both eukaryotes and prokaryotes. The common function of these domains is to bind to specific ligands, such as cell-surface-attached carbohydrate substrates for galactose oxidase and sialidase, phospholipids on the outer side of the mammalian cell membrane for coagulation factor Va, membrane-anchored ephrin for the Eph family of receptor tyrosine kinases, and a complex of broken single-stranded DNA and DNA polymerase beta for XRCC1. The structure of the galactose-binding domain-like members consists of a beta-sandwich, in which the strands making up the sheets exhibit a jellyroll fold. |
pfam17995 | GH101_N | 1.43e-91 | 384 | 565 | 1 | 180 | Endo-alpha-N-acetylgalactosaminidase N-terminal. This is the N-terminal domain found in Streptococcus pneumoniae endo-alpha-N-acetylgalactosaminidase (EC:3.2.1.97), a cell surface-anchored glycoside hydrolase from family GH101 involved in the breakdown of mucin type O-linked glycans. This is a twisted beta-sandwich domain composed of two sheets of six and seven antiparallel beta-strands. The domain appears to be missing the extended metal and carbohydrate-binding loops. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QXW61151.1 | 0.0 | 1 | 2099 | 1 | 2121 |
QLL96372.1 | 0.0 | 1 | 2099 | 1 | 2121 |
AQA07482.1 | 0.0 | 1 | 2099 | 1 | 2121 |
QLL98145.1 | 0.0 | 1 | 2099 | 1 | 2122 |
CBZ01294.1 | 0.0 | 1 | 2099 | 1 | 2122 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6QFK_A | 0.0 | 586 | 1677 | 5 | 1116 | EngBFDARPin Fusion 4b G10 [Bifidobacterium longum] |
5A59_A | 0.0 | 576 | 1685 | 2 | 1111 | Thestructure of GH101 E796Q mutant from Streptococcus pneumoniae TIGR4 in complex with T-antigen [Streptococcus pneumoniae TIGR4],5A5A_A The structure of GH101 E796Q mutant from Streptococcus pneumoniae TIGR4 in complex with PNP-T-antigen [Streptococcus pneumoniae TIGR4] |
6QEP_A | 0.0 | 586 | 1677 | 5 | 1116 | EngBFDARPin Fusion 4b H14 [Bifidobacterium longum] |
6QEV_B | 0.0 | 586 | 1677 | 5 | 1116 | EngBFDARPin Fusion 4b B6 [Bifidobacterium longum] |
2ZXQ_A | 0.0 | 588 | 1884 | 22 | 1372 | Crystalstructure of endo-alpha-N-acetylgalactosaminidase from Bifidobacterium longum (EngBF) [Bifidobacterium longum] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q2MGH6 | 0.0 | 383 | 2099 | 124 | 1767 | Endo-alpha-N-acetylgalactosaminidase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=SP_0368 PE=1 SV=1 |
Q8DR60 | 0.0 | 384 | 2099 | 125 | 1767 | Endo-alpha-N-acetylgalactosaminidase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=spr0328 PE=1 SV=1 |
A9WNA0 | 8.35e-116 | 592 | 1677 | 51 | 1037 | 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 |
P29767 | 3.59e-10 | 1761 | 1897 | 63 | 195 | Sialidase OS=Clostridium septicum OX=1504 PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000392 | 0.998841 | 0.000183 | 0.000201 | 0.000182 | 0.000149 |
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