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CAZyme Information: MGYG000002407_00746

You are here: Home > Sequence: MGYG000002407_00746

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 Cohnella sp900169535
Lineage Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Cohnella; Cohnella sp900169535
CAZyme ID MGYG000002407_00746
CAZy Family GH85
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
931 MGYG000002407_15|CGC2 103182.11 4.4639
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002407 6325359 Isolate not provided not provided
Gene Location Start: 97925;  End: 100720  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002407_00746.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH85 113 477 1.6e-65 0.9777777777777777

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG4724 COG4724 1.42e-79 48 655 27 551
Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism].
pfam03644 Glyco_hydro_85 2.92e-52 120 473 2 291
Glycosyl hydrolase family 85. Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates.
cd06547 GH85_ENGase 1.76e-46 105 508 2 339
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AWV31864.1 0.0 1 928 59 987
AIQ69045.1 0.0 8 928 8 929
QUL53214.1 0.0 18 928 18 931
QQZ59873.1 0.0 8 928 8 929
CQR56044.1 0.0 8 928 8 929

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2W91_A 1.22e-53 122 754 79 643
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 1.64e-52 122 774 230 819
Crystalstructure of Spr0440 glycoside hydrolase domain, Endo-D from Streptococcus pneumoniae R6 [Streptococcus pneumoniae R6]
3FHA_A 3.33e-48 60 698 16 563
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 4.50e-48 60 698 16 563
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]
2VTF_A 6.52e-48 60 698 21 568
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9SRL4 1.96e-16 165 602 108 491
Cytosolic endo-beta-N-acetylglucosaminidase 2 OS=Arabidopsis thaliana OX=3702 GN=ENGASE2 PE=1 SV=1
F4JZC2 6.65e-12 165 701 103 597
Cytosolic endo-beta-N-acetylglucosaminidase 1 OS=Arabidopsis thaliana OX=3702 GN=ENGASE1 PE=1 SV=1
Q8BX80 4.29e-10 79 334 102 311
Cytosolic endo-beta-N-acetylglucosaminidase OS=Mus musculus OX=10090 GN=Engase PE=1 SV=1
A1L251 5.54e-10 76 325 85 294
Cytosolic endo-beta-N-acetylglucosaminidase OS=Danio rerio OX=7955 GN=engase PE=2 SV=1
Q8NFI3 2.62e-08 165 312 163 304
Cytosolic endo-beta-N-acetylglucosaminidase OS=Homo sapiens OX=9606 GN=ENGASE PE=1 SV=1

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
0.001159 0.997076 0.000944 0.000358 0.000227 0.000186

TMHMM  Annotations      download full data without filtering help

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