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CAZyme Information: MGYG000000675_02496

You are here: Home > Sequence: MGYG000000675_02496

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 congonensis
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides congonensis
CAZyme ID MGYG000000675_02496
CAZy Family GH18
CAZyme Description Endo-beta-N-acetylglucosaminidase H
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
322 MGYG000000675_56|CGC1 35163.31 5.5744
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000675 5782172 MAG Kazakhstan Asia
Gene Location Start: 14243;  End: 15211  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000675_02496.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 73 278 1.3e-16 0.5878378378378378

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06542 GH18_EndoS-like 2.01e-36 49 290 1 240
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.
pfam00704 Glyco_hydro_18 6.88e-13 67 261 10 202
Glycosyl hydrolases family 18.
cd00598 GH18_chitinase-like 5.39e-10 73 225 17 157
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model.
cd06548 GH18_chitinase 9.13e-06 146 238 102 203
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant polymer of N-acetylglucosamine and have been identified in bacteria, fungi, insects, plants, viruses, and protozoan parasites. The structure of this domain is an eight-stranded alpha/beta barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel.
cd02878 GH18_zymocin_alpha 9.89e-05 157 209 95 150
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
QDM12014.1 2.53e-138 1 322 1 315
BCA50677.1 1.00e-135 33 322 6 286
BCA50675.1 1.56e-120 29 322 1 286
ALJ41501.1 3.96e-66 4 322 1 306
QUT39058.1 7.90e-66 4 322 1 306

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1EDT_A 2.97e-39 49 307 9 265
ChainA, ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H, ENDO H [Streptomyces plicatus]
6VE1_A 3.81e-39 49 307 13 269
ChainA, Endo-beta-N-acetylglucosaminidase H [Streptomyces plicatus],6VE1_B Chain B, Endo-beta-N-acetylglucosaminidase H [Streptomyces plicatus],6VE1_C Chain C, Endo-beta-N-acetylglucosaminidase H [Streptomyces plicatus],6VE1_D Chain D, Endo-beta-N-acetylglucosaminidase H [Streptomyces plicatus]
1C90_A 7.05e-39 49 307 4 260
ChainA, ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H [Streptomyces plicatus],1C90_B Chain B, ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H [Streptomyces plicatus]
1C91_A 7.05e-39 49 307 4 260
ChainA, ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H [Streptomyces plicatus]
1C8X_A 9.89e-39 49 307 4 260
ChainA, ENDO-BETA-N-ACETYLGLUCOSAMINIDASE 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
P04067 4.46e-38 49 307 51 307
Endo-beta-N-acetylglucosaminidase H OS=Streptomyces plicatus OX=1922 PE=1 SV=1
P80036 6.73e-37 49 310 55 312
Endo-beta-N-acetylglucosaminidase OS=Flavobacterium sp. (strain SK1022) OX=148444 PE=1 SV=2
P36911 6.95e-30 10 286 16 299
Endo-beta-N-acetylglucosaminidase F1 OS=Elizabethkingia meningoseptica OX=238 GN=endOF1 PE=1 SV=1

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 0.000003 1.000024 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000675_02496.