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CAZyme Information: MGYG000000265_00979

You are here: Home > Sequence: MGYG000000265_00979

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 nordii
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides nordii
CAZyme ID MGYG000000265_00979
CAZy Family GH85
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1264 MGYG000000265_3|CGC1 140686.69 4.9781
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000265 5489209 Isolate China Asia
Gene Location Start: 62579;  End: 66373  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000265_00979.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH85 115 430 7.8e-60 0.946031746031746

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG4724 COG4724 1.79e-52 41 596 35 548
Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism].
cd06547 GH85_ENGase 6.76e-40 116 462 22 339
Endo-beta-N-acetylglucosaminidase (ENGase) hydrolyzes the N-N'-diacetylchitobiosyl core of N-glycosylproteins. The beta-1,4-glycosyl bond located between two N-acetylglucosamine residues is hydrolyzed such that N-acetylglucosamine 1 remains with the protein and N-acetylglucosamine 2 forms the reducing end of the released glycan. ENGase is a key enzyme in the processing of free oligosaccharides in the cytosol of eukaryotes. Oligosaccharides formed in the lumen of the endoplasmic reticulum are transported into the cytosol where they are catabolized by cytosolic ENGases and other enzymes, possibly to maximize the reutilization of the component sugars. ENGases have an eight-stranded alpha/beta barrel topology and are classified as a family 85 glycosyl hydrolase (GH85) domain. The GH85 ENGases are sequence-similar to the family 18 glycosyl hydrolases, also known as GH18 chitinases. An ENGase-like protein is also found in bacteria and is included in this alignment model.
pfam03644 Glyco_hydro_85 1.14e-39 115 427 4 291
Glycosyl hydrolase family 85. Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates.
pfam13385 Laminin_G_3 5.03e-18 951 1039 64 151
Concanavalin A-like lectin/glucanases superfamily. This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.
TIGR04183 Por_Secre_tail 3.85e-07 1190 1264 1 72
Por secretion system C-terminal sorting domain. Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUT77741.1 0.0 2 1264 1 1278
BCI64756.1 0.0 2 1264 1 1283
AHF12130.1 1.52e-287 2 1264 1 1287
EFC71170.1 1.81e-278 21 1264 19 1250
QUB76736.1 1.53e-269 2 1264 1 1259

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2W91_A 4.33e-43 43 665 18 582
Structureof a Streptococcus pneumoniae family 85 glycoside hydrolase, Endo-D. [Streptococcus pneumoniae TIGR4],2W92_A Structure of a Streptococcus pneumoniae family 85 glycoside hydrolase, Endo-D, in complex with NAG-thiazoline. [Streptococcus pneumoniae TIGR4]
3GDB_A 3.51e-42 43 665 169 733
Crystalstructure of Spr0440 glycoside hydrolase domain, Endo-D from Streptococcus pneumoniae R6 [Streptococcus pneumoniae R6]
2VTF_A 6.11e-40 43 525 19 462
X-raycrystal structure of the Endo-beta-N-acetylglucosaminidase from Arthrobacter protophormiae E173Q mutant reveals a TIM barrel catalytic domain and two ancillary domains [Glutamicibacter protophormiae],2VTF_B X-ray crystal structure of the Endo-beta-N-acetylglucosaminidase from Arthrobacter protophormiae E173Q mutant reveals a TIM barrel catalytic domain and two ancillary domains [Glutamicibacter protophormiae]
3FHA_A 2.47e-39 43 611 14 535
ChainA, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHA_B Chain B, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHA_C Chain C, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHA_D Chain D, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae]
3FHQ_A 1.06e-38 43 611 14 535
ChainA, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHQ_B Chain B, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHQ_D Chain D, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHQ_F Chain F, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae]

Swiss-Prot Hits      help

has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000613 0.998491 0.000290 0.000210 0.000199 0.000186

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000265_00979.