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CAZyme Information: MGYG000004266_00188

You are here: Home > Sequence: MGYG000004266_00188

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 Streptococcus sp900550895
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Streptococcus; Streptococcus sp900550895
CAZyme ID MGYG000004266_00188
CAZy Family GH85
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1485 MGYG000004266_6|CGC1 164502.52 4.864
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004266 1795280 MAG China Asia
Gene Location Start: 13435;  End: 17892  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.96

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH85 208 517 1.5e-110 0.9904761904761905

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG4724 COG4724 0.0 160 679 37 553
Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism].
pfam03644 Glyco_hydro_85 1.88e-104 218 513 1 291
Glycosyl hydrolase family 85. Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates.
cd06547 GH85_ENGase 1.66e-92 213 548 13 339
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.
pfam07523 Big_3 9.57e-11 1134 1200 3 67
Bacterial Ig-like domain (group 3). This family consists of bacterial domains with an Ig-like fold. Members of this family are found in a variety of bacterial surface proteins.
TIGR01168 YSIRK_signal 4.25e-10 2 40 1 39
Gram-positive signal peptide, YSIRK family. Many surface proteins found in Streptococcus, Staphylococcus, and related lineages share apparently homologous signal sequences. A motif resembling [YF]SIRKxxxGxxS[VIA] appears at the start of the transmembrane domain. The GxxS motif appears perfectly conserved, suggesting a specific function and not just homology. There is a strong correlation between proteins carrying this region at the N-terminus and those carrying the Gram-positive anchor domain with the LPXTG sortase processing site at the C-terminus.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QLL96936.1 0.0 1 1485 1 1574
CBZ00044.1 0.0 1 1485 1 1563
QLL97472.1 0.0 1 1485 1 1485
VEF79601.1 0.0 1 1485 1 1574
AQA08589.1 0.0 1 1485 1 1574

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2W91_A 0.0 147 795 5 653
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 0.0 78 928 104 937
Crystalstructure of Spr0440 glycoside hydrolase domain, Endo-D from Streptococcus pneumoniae R6 [Streptococcus pneumoniae R6]
2VTF_A 1.00e-86 160 739 19 588
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 2.24e-86 160 739 14 583
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 2.24e-86 160 739 14 583
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      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8BX80 4.73e-20 218 615 135 506
Cytosolic endo-beta-N-acetylglucosaminidase OS=Mus musculus OX=10090 GN=Engase PE=1 SV=1
P0C7A1 1.27e-18 160 573 89 463
Cytosolic endo-beta-N-acetylglucosaminidase OS=Gallus gallus OX=9031 GN=ENGASE PE=1 SV=1
Q8NFI3 1.81e-16 148 601 79 500
Cytosolic endo-beta-N-acetylglucosaminidase OS=Homo sapiens OX=9606 GN=ENGASE PE=1 SV=1
P49610 8.61e-07 1339 1467 1047 1179
Beta-N-acetylhexosaminidase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=strH PE=1 SV=2

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
0.001643 0.995447 0.002256 0.000251 0.000203 0.000174

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004266_00188.