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CAZyme Information: MGYG000004658_01842

You are here: Home > Sequence: MGYG000004658_01842

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 Alistipes finegoldii
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes finegoldii
CAZyme ID MGYG000004658_01842
CAZy Family GH18
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
333 MGYG000004658_68|CGC1 36230.45 4.4586
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004658 3509081 Isolate United States North America
Gene Location Start: 2521;  End: 3522  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004658_01842.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06542 GH18_EndoS-like 1.45e-19 52 282 6 239
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 2.84e-05 118 201 57 142
Glycosyl hydrolases family 18.
cd00598 GH18_chitinase-like 3.66e-04 121 281 61 207
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.
cd02871 GH18_chitinase_D-like 6.88e-04 117 192 66 139
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 7.27e-04 149 201 93 154
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
CBK64285.1 2.47e-234 17 333 1 317
BBL12727.1 3.76e-217 29 333 1 305
BBL09934.1 3.76e-217 29 333 1 305
BBL01454.1 6.87e-216 1 333 1 336
CBK65022.1 2.63e-119 1 329 1 324

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1EDT_A 5.94e-29 47 293 9 258
ChainA, ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H, ENDO H [Streptomyces plicatus]
6VE1_A 7.33e-29 47 293 13 262
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 1.41e-28 47 293 4 253
ChainA, ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H [Streptomyces plicatus],1C90_B Chain B, ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H [Streptomyces plicatus]
1C91_A 1.41e-28 47 293 4 253
ChainA, ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H [Streptomyces plicatus]
1C8X_A 1.96e-28 47 293 4 253
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 7.54e-28 47 293 51 300
Endo-beta-N-acetylglucosaminidase H OS=Streptomyces plicatus OX=1922 PE=1 SV=1
P80036 2.66e-24 47 299 55 308
Endo-beta-N-acetylglucosaminidase OS=Flavobacterium sp. (strain SK1022) OX=148444 PE=1 SV=2
P36911 6.03e-18 35 316 44 339
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 1.000047 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004658_01842.