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CAZyme Information: MGYG000004371_02019

You are here: Home > Sequence: MGYG000004371_02019

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 Prevotella sp002251385
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp002251385
CAZyme ID MGYG000004371_02019
CAZy Family GH18
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
453 MGYG000004371_76|CGC1 50071.47 4.7541
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004371 2690194 MAG Israel Asia
Gene Location Start: 9119;  End: 10480  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004371_02019.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06542 GH18_EndoS-like 2.79e-38 214 435 28 251
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 2.89e-18 44 154 5 117
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.
cd00598 GH18_chitinase-like 5.18e-04 214 422 24 208
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AEA20837.1 5.75e-197 1 453 1 452
QUB88025.1 5.75e-197 1 453 1 452
QUI93726.1 1.64e-196 1 453 1 452
QUB92922.1 1.64e-196 1 453 1 452
QUB87240.1 6.65e-196 1 453 1 452

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2EBN_A 1.92e-80 189 453 14 289
CRYSTALSTRUCTURE OF ENDO-BETA-N-ACETYLGLUCOSAMINIDASE F1, AN ALPHA(SLASH)BETA-BARREL ENZYME ADAPTED FOR A COMPLEX SUBSTRATE [Elizabethkingia meningoseptica]
6T8I_A 5.30e-56 29 423 8 408
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]
6TCV_B 1.11e-53 29 423 8 408
Crystalstructure of Bacteroides thetaiotamicron EndoBT-3987 in complex with Man9GlcNAc2Asn substrate [Bacteroides thetaiotaomicron VPI-5482]
3POH_A 1.60e-52 29 423 8 408
Crystalstructure of an endo-beta-N-acetylglucosaminidase (BT_3987) from BACTEROIDES THETAIOTAOMICRON VPI-5482 at 1.55 A resolution [Bacteroides thetaiotaomicron VPI-5482]
6VE1_A 2.76e-29 178 446 6 274
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P36911 4.99e-79 189 453 64 339
Endo-beta-N-acetylglucosaminidase F1 OS=Elizabethkingia meningoseptica OX=238 GN=endOF1 PE=1 SV=1
P04067 2.71e-27 188 446 54 312
Endo-beta-N-acetylglucosaminidase H OS=Streptomyces plicatus OX=1922 PE=1 SV=1
P80036 1.49e-19 173 441 43 309
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
0.000002 0.001585 0.998456 0.000001 0.000001 0.000001

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004371_02019.