Species | Parabacteroides faecis | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides faecis | |||||||||||
CAZyme ID | MGYG000000174_00781 | |||||||||||
CAZy Family | GH101 | |||||||||||
CAZyme Description | Endo-alpha-N-acetylgalactosaminidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 924013; End: 927396 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH101 | 196 | 704 | 2.3e-111 | 0.7977369165487977 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam12905 | Glyco_hydro_101 | 7.59e-91 | 415 | 677 | 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 | 1.20e-84 | 428 | 700 | 2 | 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 | 4.43e-43 | 193 | 414 | 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. |
pfam17451 | Glyco_hyd_101C | 4.41e-21 | 685 | 780 | 3 | 110 | Glycosyl hydrolase 101 beta sandwich domain. 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 a S. pneumoniae protein, where Asp764 is the catalytic nucleophile-base and Glu796 the catalytic proton donor. This domain represents C-terminal the beta sandwich domain. |
pfam17974 | GalBD_like | 2.22e-15 | 965 | 1069 | 1 | 125 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ATP57185.1 | 0.0 | 53 | 1127 | 78 | 1136 |
AZN39795.1 | 3.74e-274 | 47 | 1125 | 48 | 1153 |
QHW33475.1 | 7.39e-262 | 58 | 1121 | 68 | 1207 |
AQT69519.1 | 1.19e-225 | 189 | 1069 | 47 | 927 |
ATD58436.1 | 3.71e-217 | 53 | 1118 | 547 | 1620 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6QEP_A | 1.76e-103 | 189 | 1068 | 8 | 1038 | EngBFDARPin Fusion 4b H14 [Bifidobacterium longum] |
2ZXQ_A | 2.23e-103 | 189 | 1068 | 23 | 1053 | Crystalstructure of endo-alpha-N-acetylgalactosaminidase from Bifidobacterium longum (EngBF) [Bifidobacterium longum] |
6QEV_B | 3.40e-103 | 193 | 1068 | 12 | 1038 | EngBFDARPin Fusion 4b B6 [Bifidobacterium longum] |
6SH9_B | 3.40e-103 | 193 | 1068 | 12 | 1038 | EngBFDARPin Fusion 4b D12 [Bifidobacterium longum subsp. longum JCM 1217] |
6QFK_A | 3.40e-103 | 193 | 1068 | 12 | 1038 | EngBFDARPin Fusion 4b G10 [Bifidobacterium longum] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
A9WNA0 | 2.30e-122 | 193 | 1066 | 52 | 971 | 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 |
Q8DR60 | 4.24e-96 | 20 | 1071 | 138 | 1334 | Endo-alpha-N-acetylgalactosaminidase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=spr0328 PE=1 SV=1 |
Q2MGH6 | 4.55e-95 | 20 | 1071 | 138 | 1334 | Endo-alpha-N-acetylgalactosaminidase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=SP_0368 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000221 | 0.999155 | 0.000154 | 0.000158 | 0.000147 | 0.000133 |
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