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CAZyme Information: MGYG000000437_01984

You are here: Home > Sequence: MGYG000000437_01984

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 sp001941065
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp001941065
CAZyme ID MGYG000000437_01984
CAZy Family GH18
CAZyme Description Endo-beta-N-acetylglucosaminidase F1
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
338 MGYG000000437_88|CGC1 37201.01 4.4911
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000437 3341375 MAG Sweden Europe
Gene Location Start: 11767;  End: 12783  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000437_01984.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06542 GH18_EndoS-like 8.50e-24 53 287 5 237
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 8.73e-07 116 194 59 138
Glycosyl hydrolases family 18.
smart00636 Glyco_18 2.05e-05 117 228 63 165
Glyco_18 domain.
cd02871 GH18_chitinase_D-like 3.33e-04 96 219 46 168
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 0.005 117 288 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BBL01829.1 3.97e-238 17 338 1 322
AFL77262.1 1.70e-79 3 338 33 358
CBK65022.1 1.46e-78 1 338 1 326
BBL12493.1 1.42e-77 17 338 1 310
BBL09699.1 1.42e-77 17 338 1 310

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2EBN_A 5.99e-35 54 323 15 289
CRYSTALSTRUCTURE OF ENDO-BETA-N-ACETYLGLUCOSAMINIDASE F1, AN ALPHA(SLASH)BETA-BARREL ENZYME ADAPTED FOR A COMPLEX SUBSTRATE [Elizabethkingia meningoseptica]
6T8I_A 3.73e-24 53 229 172 357
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 6.95e-24 53 229 172 357
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 5.24e-22 53 229 172 357
Crystalstructure of Bacteroides thetaiotamicron EndoBT-3987 in complex with Man9GlcNAc2Asn substrate [Bacteroides thetaiotaomicron VPI-5482]
1EDT_A 5.86e-22 49 307 9 265
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 2.47e-35 10 323 18 339
Endo-beta-N-acetylglucosaminidase F1 OS=Elizabethkingia meningoseptica OX=238 GN=endOF1 PE=1 SV=1
P80036 5.29e-23 49 314 55 313
Endo-beta-N-acetylglucosaminidase OS=Flavobacterium sp. (strain SK1022) OX=148444 PE=1 SV=2
P04067 6.32e-21 49 307 51 307
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 1.000061 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000437_01984.