logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000000924_01862

You are here: Home > Sequence: MGYG000000924_01862

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species An172 sp002160515
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; An172; An172 sp002160515
CAZyme ID MGYG000000924_01862
CAZy Family GH101
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
2077 229969.56 4.2517
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000924 2081481 MAG China Asia
Gene Location Start: 231;  End: 6464  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000924_01862.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH101 513 1027 1.2e-85 0.801980198019802

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd14244 GH_101_like 4.09e-63 750 1019 4 298
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.
pfam12905 Glyco_hydro_101 2.40e-60 734 993 1 270
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.
pfam18080 Gal_mutarotas_3 1.89e-41 509 733 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 1.22e-24 1004 1107 3 111
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.
pfam13385 Laminin_G_3 3.04e-22 1677 1838 1 150
Concanavalin A-like lectin/glucanases superfamily. This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ATD58436.1 4.99e-203 36 1452 235 1634
ATD54117.1 4.99e-203 36 1452 235 1634
QBJ76357.1 4.99e-203 36 1452 235 1634
SLK22612.1 4.99e-203 36 1452 235 1634
AZN39795.1 2.30e-179 319 1392 18 1093

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6QEP_A 4.53e-81 507 1378 10 1026
EngBFDARPin Fusion 4b H14 [Bifidobacterium longum]
6SH9_B 4.62e-81 507 1378 10 1026
EngBFDARPin Fusion 4b D12 [Bifidobacterium longum subsp. longum JCM 1217]
6QFK_A 4.62e-81 507 1378 10 1026
EngBFDARPin Fusion 4b G10 [Bifidobacterium longum]
6QEV_B 4.62e-81 507 1378 10 1026
EngBFDARPin Fusion 4b B6 [Bifidobacterium longum]
2ZXQ_A 5.23e-81 507 1378 25 1041
Crystalstructure of endo-alpha-N-acetylgalactosaminidase from Bifidobacterium longum (EngBF) [Bifidobacterium longum]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A9WNA0 4.16e-76 508 1378 51 961
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
Q2MGH6 6.20e-74 368 1389 177 1330
Endo-alpha-N-acetylgalactosaminidase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=SP_0368 PE=1 SV=1
Q8DR60 5.51e-73 368 1389 177 1330
Endo-alpha-N-acetylgalactosaminidase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=spr0328 PE=1 SV=1
P20533 1.28e-10 1445 1632 460 642
Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
A0P8X0 1.71e-10 1427 1543 794 907
Alpha-amylase OS=Niallia circulans OX=1397 GN=igtZ PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000238 0.999071 0.000193 0.000162 0.000154 0.000145

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000924_01862.