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CAZyme Information: MGYG000002115_00121

You are here: Home > Sequence: MGYG000002115_00121

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
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; CAG-110;
CAZyme ID MGYG000002115_00121
CAZy Family GH85
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
2183 MGYG000002115_2|CGC1 235048.34 4.7328
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002115 2270238 MAG Mongolia Asia
Gene Location Start: 3759;  End: 10310  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002115_00121.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH85 113 414 1.8e-55 0.9968253968253968

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG4724 COG4724 1.04e-117 58 579 28 552
Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism].
pfam03644 Glyco_hydro_85 4.88e-67 125 410 1 291
Glycosyl hydrolase family 85. Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates.
cd06547 GH85_ENGase 2.51e-64 108 447 1 339
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.
PTZ00121 PTZ00121 6.21e-09 1859 2142 1275 1529
MAEBL; Provisional
PRK12472 PRK12472 2.78e-07 1810 2010 152 330
hypothetical protein; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ASM70437.1 0.0 31 1210 30 1212
SQI03683.1 1.98e-177 42 1070 31 1028
ASY50962.1 5.19e-177 42 1070 31 1028
BAB80524.1 5.19e-177 42 1070 31 1028
AXH51875.1 5.19e-177 42 1070 31 1028

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3GDB_A 1.11e-100 55 841 156 937
Crystalstructure of Spr0440 glycoside hydrolase domain, Endo-D from Streptococcus pneumoniae R6 [Streptococcus pneumoniae R6]
2W91_A 2.46e-84 55 686 5 644
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]
2VTF_A 2.20e-82 59 674 11 621
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]
3FHQ_A 1.20e-81 59 674 6 616
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]
3FHA_A 1.63e-81 59 674 6 616
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A1L251 5.22e-25 42 512 44 489
Cytosolic endo-beta-N-acetylglucosaminidase OS=Danio rerio OX=7955 GN=engase PE=2 SV=1
Q8NFI3 1.10e-17 36 516 62 517
Cytosolic endo-beta-N-acetylglucosaminidase OS=Homo sapiens OX=9606 GN=ENGASE PE=1 SV=1
Q8BX80 2.89e-16 36 516 54 509
Cytosolic endo-beta-N-acetylglucosaminidase OS=Mus musculus OX=10090 GN=Engase PE=1 SV=1
P0C7A1 1.00e-14 51 498 72 488
Cytosolic endo-beta-N-acetylglucosaminidase OS=Gallus gallus OX=9031 GN=ENGASE PE=1 SV=1
E8MGH9 3.62e-14 1877 2069 1667 1871
Beta-L-arabinobiosidase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=hypBA2 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.505131 0.183726 0.302916 0.001160 0.000652 0.006414

TMHMM  Annotations      download full data without filtering help

start end
12 34
2155 2177