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CAZyme Information: MGYG000001633_01397

You are here: Home > Sequence: MGYG000001633_01397

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 RC9 sp000435075
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; UBA932; RC9; RC9 sp000435075
CAZyme ID MGYG000001633_01397
CAZy Family GH18
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
513 MGYG000001633_21|CGC1 58574.8 4.7772
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001633 2721018 MAG China Asia
Gene Location Start: 29551;  End: 31092  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001633_01397.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06542 GH18_EndoS-like 1.92e-14 247 386 44 175
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 5.24e-06 264 355 60 146
Glycosyl hydrolases family 18.
cd02871 GH18_chitinase_D-like 6.24e-05 264 353 70 152
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.
cd00598 GH18_chitinase-like 1.76e-04 264 355 61 147
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.
pfam08522 DUF1735 2.31e-04 41 154 10 115
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BBL12726.1 1.83e-115 12 513 23 538
BBL09933.1 1.83e-115 12 513 23 538
BBL01455.1 1.05e-109 12 513 23 532
CBK64286.1 1.05e-109 12 513 23 532
BBL09700.1 2.05e-109 12 513 20 544

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2EBN_A 3.72e-17 196 386 16 199
CRYSTALSTRUCTURE OF ENDO-BETA-N-ACETYLGLUCOSAMINIDASE F1, AN ALPHA(SLASH)BETA-BARREL ENZYME ADAPTED FOR A COMPLEX SUBSTRATE [Elizabethkingia meningoseptica]
1C90_A 3.90e-16 230 409 41 213
ChainA, ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H [Streptomyces plicatus],1C90_B Chain B, ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H [Streptomyces plicatus]
1C93_A 3.90e-16 230 409 41 213
ChainA, ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H [Streptomyces plicatus]
1C8Y_A 3.90e-16 230 409 41 213
ChainA, ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H [Streptomyces plicatus]
1C8X_A 3.90e-16 230 409 41 213
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
P36911 3.81e-16 196 386 66 249
Endo-beta-N-acetylglucosaminidase F1 OS=Elizabethkingia meningoseptica OX=238 GN=endOF1 PE=1 SV=1
P04067 5.51e-15 230 409 88 260
Endo-beta-N-acetylglucosaminidase H OS=Streptomyces plicatus OX=1922 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 0.000000 1.000056 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001633_01397.