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CAZyme Information: MGYG000001391_02377

You are here: Home > Sequence: MGYG000001391_02377

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 Coprobacter fastidiosus
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Coprobacteraceae; Coprobacter; Coprobacter fastidiosus
CAZyme ID MGYG000001391_02377
CAZy Family GH85
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1002 MGYG000001391_4|CGC6 111071.54 4.5573
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001391 3843461 Isolate not provided not provided
Gene Location Start: 363682;  End: 366690  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001391_02377.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH85 121 430 5.8e-44 0.9587301587301588

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG4724 COG4724 1.34e-32 111 596 84 552
Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism].
cd06547 GH85_ENGase 2.64e-25 121 458 17 336
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 5.87e-13 122 427 1 291
Glycosyl hydrolase family 85. Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates.
TIGR04183 Por_Secre_tail 0.010 946 1002 13 71
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
BCI64641.1 0.0 1 1002 1 1006
AGB28382.1 0.0 28 1001 199 1188
QUT74553.1 0.0 1 1002 1 1019
QUB47476.1 0.0 20 999 20 1002
EFC71166.1 0.0 1 1001 1 1004

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2W91_A 8.34e-14 130 596 84 536
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 1.08e-13 130 596 235 687
Crystalstructure of Spr0440 glycoside hydrolase domain, Endo-D from Streptococcus pneumoniae R6 [Streptococcus pneumoniae R6]

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
0.001113 0.896150 0.101558 0.000535 0.000343 0.000278

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001391_02377.