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CAZyme Information: MGYG000001597_00448

You are here: Home > Sequence: MGYG000001597_00448

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 UBA866 sp900543295
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; UBA866; UBA866 sp900543295
CAZyme ID MGYG000001597_00448
CAZy Family GH85
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1457 159659.77 4.096
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001597 2473217 MAG China Asia
Gene Location Start: 19525;  End: 23898  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001597_00448.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH85 103 454 9.1e-51 0.9841269841269841

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG4724 COG4724 1.89e-62 57 640 41 551
Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism].
pfam03644 Glyco_hydro_85 3.51e-50 116 451 3 291
Glycosyl hydrolase family 85. Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates.
cd06547 GH85_ENGase 3.94e-37 99 483 1 336
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.
pfam00754 F5_F8_type_C 7.39e-07 1130 1208 38 120
F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
sd00031 LRR_1 3.72e-05 969 1058 4 107
leucine-rich repeats. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AQP47875.1 4.96e-224 15 941 10 924
SMF77083.1 4.16e-221 1 923 1 916
AVM41738.1 1.91e-212 44 1076 72 1088
QQM67248.1 8.99e-212 16 934 17 944
VEG55861.1 2.48e-211 11 952 12 963

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2W91_A 3.68e-46 41 735 5 634
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 1.88e-45 30 735 145 785
Crystalstructure of Spr0440 glycoside hydrolase domain, Endo-D from Streptococcus pneumoniae R6 [Streptococcus pneumoniae R6]
2VTF_A 4.60e-34 54 721 20 609
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 5.85e-34 54 721 15 604
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 7.80e-34 54 721 15 604
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
0.001028 0.997629 0.000538 0.000338 0.000232 0.000200

TMHMM  Annotations      download full data without filtering help

start end
5 27
1428 1450