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CAZyme Information: MGYG000000924_00522

You are here: Home > Sequence: MGYG000000924_00522

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_00522
CAZy Family GH101
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1035 MGYG000000924_5|CGC1 115425.58 4.2431
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000924 2081481 MAG China Asia
Gene Location Start: 23369;  End: 26476  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000924_00522.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH101 300 835 1.8e-87 0.8076379066478077

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd14244 GH_101_like 5.10e-74 544 823 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 2.56e-62 522 770 1 245
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 8.86e-43 296 521 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 3.26e-23 808 905 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.
pfam03442 CBM_X2 0.004 48 88 45 83
Carbohydrate binding domain X2. This domain binds to cellulose and to bacterial cell walls. It is found in glycosyl hydrolases and in scaffolding proteins of cellulosomes (multiprotein glycosyl hydrolase complexes). In the cellulosome it may aid cellulose degradation by anchoring the cellulosome to the bacterial cell wall and by binding it to its substrate. This domain has an Ig-like fold.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ATD58436.1 9.55e-254 47 1015 447 1392
ATD54117.1 9.55e-254 47 1015 447 1392
QBJ76357.1 9.55e-254 47 1015 447 1392
SLK22612.1 9.55e-254 47 1015 447 1392
BBK62189.1 1.65e-240 47 1022 270 1239

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6QEP_A 3.28e-70 291 955 7 776
EngBFDARPin Fusion 4b H14 [Bifidobacterium longum]
2ZXQ_A 3.46e-70 291 955 22 791
Crystalstructure of endo-alpha-N-acetylgalactosaminidase from Bifidobacterium longum (EngBF) [Bifidobacterium longum]
6QEV_B 5.91e-70 295 955 11 776
EngBFDARPin Fusion 4b B6 [Bifidobacterium longum]
6SH9_B 5.91e-70 295 955 11 776
EngBFDARPin Fusion 4b D12 [Bifidobacterium longum subsp. longum JCM 1217]
6QFK_A 5.91e-70 295 955 11 776
EngBFDARPin Fusion 4b G10 [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 4.26e-79 295 1020 51 797
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 2.86e-66 284 1015 322 1125
Endo-alpha-N-acetylgalactosaminidase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=SP_0368 PE=1 SV=1
Q8DR60 6.77e-66 284 1015 322 1125
Endo-alpha-N-acetylgalactosaminidase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=spr0328 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000013 0.000013 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000924_00522.