Species | ||||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Tissierellales; Peptoniphilaceae; Anaerococcus; | |||||||||||
CAZyme ID | MGYG000003760_00084 | |||||||||||
CAZy Family | GH101 | |||||||||||
CAZyme Description | Endo-alpha-N-acetylgalactosaminidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 88931; End: 94786 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH101 | 377 | 1099 | 0 | 0.9957567185289957 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam12905 | Glyco_hydro_101 | 1.12e-141 | 643 | 934 | 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 | 6.82e-120 | 656 | 957 | 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. |
pfam17974 | GalBD_like | 1.22e-92 | 1269 | 1459 | 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. |
pfam18080 | Gal_mutarotas_3 | 5.27e-82 | 374 | 642 | 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. |
pfam17995 | GH101_N | 1.00e-63 | 169 | 348 | 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 |
---|---|---|---|---|---|
ACV29694.1 | 0.0 | 1 | 1951 | 1 | 1968 |
QQB61808.1 | 0.0 | 162 | 1949 | 119 | 1814 |
AYQ24117.1 | 0.0 | 186 | 1774 | 235 | 1804 |
QQA36326.1 | 0.0 | 168 | 1737 | 157 | 1697 |
QQQ35090.1 | 0.0 | 186 | 1749 | 419 | 1966 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3ECQ_A | 0.0 | 184 | 1623 | 106 | 1530 | Endo-alpha-N-acetylgalactosaminidasefrom Streptococcus pneumoniae: SeMet structure [Streptococcus pneumoniae R6],3ECQ_B Endo-alpha-N-acetylgalactosaminidase from Streptococcus pneumoniae: SeMet structure [Streptococcus pneumoniae R6] |
6QEP_A | 0.0 | 367 | 1582 | 5 | 1230 | EngBFDARPin Fusion 4b H14 [Bifidobacterium longum] |
5A59_A | 0.0 | 361 | 1480 | 6 | 1110 | 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] |
5A58_A | 0.0 | 361 | 1480 | 6 | 1110 | Thestructure of GH101 D764N mutant from Streptococcus pneumoniae TIGR4 in complex with serinyl T-antigen [Streptococcus pneumoniae TIGR4] |
5A55_A | 0.0 | 361 | 1480 | 8 | 1112 | Thenative structure of GH101 from Streptococcus pneumoniae TIGR4 [Streptococcus pneumoniae TIGR4] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q2MGH6 | 0.0 | 184 | 1735 | 142 | 1677 | 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 | 184 | 1735 | 142 | 1677 | Endo-alpha-N-acetylgalactosaminidase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=spr0328 PE=1 SV=1 |
A9WNA0 | 3.73e-109 | 369 | 1478 | 47 | 1042 | 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 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.273761 | 0.713867 | 0.009673 | 0.001320 | 0.000635 | 0.000739 |
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