logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000003922_00995

You are here: Home > Sequence: MGYG000003922_00995

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 Bacteroides sp014385165
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp014385165
CAZyme ID MGYG000003922_00995
CAZy Family GH18
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
644 MGYG000003922_8|CGC3 71791.97 4.4692
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003922 4876803 MAG China Asia
Gene Location Start: 89798;  End: 91732  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.96

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06542 GH18_EndoS-like 1.11e-60 189 457 1 255
Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of various asparagine (N)-linked glycans and glycoproteins. The endo-beta-N-acetylglucosaminidases have a glycosyl hydrolase family 18 (GH18) catalytic domain. Some members also have an additional C-terminal glycosyl hydrolase family 20 (GH20) domain while others have an N-terminal domain of unknown function (pfam08522). Members of this family include endo-beta-N-acetylglucosaminidase S (EndoS) from Streptococcus pyogenes, EndoF1, EndoF2, EndoF3, and EndoH from Flavobacterium meningosepticum, and EndoE from Enterococcus faecalis. EndoS is a secreted endoglycosidase from Streptococcus pyogenes that specifically hydrolyzes the glycan on human IgG between two core N-acetylglucosamine residues. EndoE is a secreted endoglycosidase, encoded by the ndoE gene in Enterococcus faecalis, that hydrolyzes the glycan on human RNase B.
pfam08522 DUF1735 1.93e-16 45 161 2 118
Domain of unknown function (DUF1735). This domain of unknown function is found in a number of bacterial proteins including acylhydrolases. The structure of this domain has a beta-sandwich fold.
pfam00704 Glyco_hydro_18 1.65e-09 223 381 26 176
Glycosyl hydrolases family 18.
cd02871 GH18_chitinase_D-like 8.24e-06 218 321 28 129
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins. The domain architecture of ChiD includes a catalytic glycosyl hydrolase family 18 (GH18) domain, a chitin-binding domain, and a fibronectin type III domain. The chitin-binding and fibronectin type III domains are located either N-terminal or C-terminal to the catalytic domain. This family includes exochitinase Chi36 from Bacillus cereus.
cd02878 GH18_zymocin_alpha 2.19e-05 247 380 45 185
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle progression. The zymocin alpha subunit has a chitinase activity that is essential for holoenzyme action from the cell exterior while the gamma subunit contains the intracellular toxin responsible for G1 phase cell cycle arrest. The zymocin alpha and beta subunits are thought to act from the cell's exterior by docking to the cell wall-associated chitin, thus mediating gamma-toxin translocation. The alpha subunit has an eight-stranded TIM barrel fold similar to that of family 18 glycosyl hydrolases such as hevamine, chitolectin, and chitobiase.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QDO69363.1 0.0 1 644 4 660
QUT92946.1 0.0 1 643 4 657
QPH59421.1 4.57e-268 1 643 1 658
QMI80605.1 6.48e-268 1 643 1 658
QBJ19120.1 6.48e-268 1 643 1 658

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6T8I_A 3.71e-58 78 466 52 429
Crystalstructure of wild type EndoBT-3987 from Bacteroides thetaiotamicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482],6T8K_A Crystal structure of Bacteroides thetaiotamicron EndoBT-3987 in complex with Man9GlcNAc product in P1 [Bacteroides thetaiotaomicron VPI-5482],6T8K_B Crystal structure of Bacteroides thetaiotamicron EndoBT-3987 in complex with Man9GlcNAc product in P1 [Bacteroides thetaiotaomicron VPI-5482],6T8L_A Crystal structure of Bacteroides thetaiotamicron EndoBT-3987 with Man9GlcNAc product in P212121 [Bacteroides thetaiotaomicron VPI-5482],6TCW_A Crystal structure of Bacteroides thetaiotamicron EndoBT-3987 with Man5GlcNAc product [Bacteroides thetaiotaomicron VPI-5482],7NWF_A Chain A, Endo-beta-N-acetylglucosaminidase F1 [Bacteroides thetaiotaomicron VPI-5482]
3POH_A 2.63e-56 78 466 52 429
Crystalstructure of an endo-beta-N-acetylglucosaminidase (BT_3987) from BACTEROIDES THETAIOTAOMICRON VPI-5482 at 1.55 A resolution [Bacteroides thetaiotaomicron VPI-5482]
6TCV_B 7.01e-56 78 466 52 429
Crystalstructure of Bacteroides thetaiotamicron EndoBT-3987 in complex with Man9GlcNAc2Asn substrate [Bacteroides thetaiotaomicron VPI-5482]
2EBN_A 1.05e-49 180 471 1 288
CRYSTALSTRUCTURE OF ENDO-BETA-N-ACETYLGLUCOSAMINIDASE F1, AN ALPHA(SLASH)BETA-BARREL ENZYME ADAPTED FOR A COMPLEX SUBSTRATE [Elizabethkingia meningoseptica]
1EDT_A 2.64e-42 182 437 2 245
ChainA, ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H, ENDO H [Streptomyces plicatus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P36911 2.19e-48 180 471 51 338
Endo-beta-N-acetylglucosaminidase F1 OS=Elizabethkingia meningoseptica OX=238 GN=endOF1 PE=1 SV=1
P04067 8.11e-41 191 437 53 287
Endo-beta-N-acetylglucosaminidase H OS=Streptomyces plicatus OX=1922 PE=1 SV=1
P80036 4.47e-37 186 457 52 307
Endo-beta-N-acetylglucosaminidase OS=Flavobacterium sp. (strain SK1022) OX=148444 PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000077 0.999947 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003922_00995.