logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000000211_01988

You are here: Home > Sequence: MGYG000000211_01988

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 Bacteroides sp900556215
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp900556215
CAZyme ID MGYG000000211_01988
CAZy Family GH2
CAZyme Description Beta-galactosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
960 MGYG000000211_4|CGC3 110526.21 7.3022
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000211 6486320 Isolate China Asia
Gene Location Start: 311575;  End: 314457  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.23

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH2 21 665 3.6e-68 0.6422872340425532

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK10150 PRK10150 2.21e-21 26 348 14 296
beta-D-glucuronidase; Provisional
COG3250 LacZ 3.04e-18 27 482 15 433
Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
PRK10340 ebgA 5.78e-13 23 384 40 373
cryptic beta-D-galactosidase subunit alpha; Reviewed
pfam02837 Glyco_hydro_2_N 6.34e-13 24 220 1 169
Glycosyl hydrolases family 2, sugar binding domain. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities and has a jelly-roll fold. The domain binds the sugar moiety during the sugar-hydrolysis reaction.
pfam00703 Glyco_hydro_2 6.99e-10 222 328 1 106
Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QDO67494.1 0.0 5 960 4 959
QIU94545.1 0.0 1 960 1 958
CBK68224.1 0.0 1 960 1 958
QDH54516.1 0.0 1 960 1 958
QRM98514.1 0.0 1 960 1 958

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7VQM_A 1.10e-18 27 410 16 368
ChainA, GH2 beta-galacturonate AqGalA [Aquimarina sp.],7VQM_B Chain B, GH2 beta-galacturonate AqGalA [Aquimarina sp.],7VQM_C Chain C, GH2 beta-galacturonate AqGalA [Aquimarina sp.],7VQM_D Chain D, GH2 beta-galacturonate AqGalA [Aquimarina sp.]
3K4A_A 1.35e-17 27 359 17 305
Crystalstructure of selenomethionine substituted E. coli beta-glucuronidase [Escherichia coli K-12],3K4A_B Crystal structure of selenomethionine substituted E. coli beta-glucuronidase [Escherichia coli K-12]
4JHZ_A 4.07e-17 27 359 17 305
Structureof E. coli beta-Glucuronidase bound with a novel, potent inhibitor 2-[4-(1,3-benzodioxol-5-ylmethyl)piperazin-1-yl]-N-[(1S,2S,5S)-2,5-dimethoxycyclohexyl]acetamide [Escherichia coli K-12],4JHZ_B Structure of E. coli beta-Glucuronidase bound with a novel, potent inhibitor 2-[4-(1,3-benzodioxol-5-ylmethyl)piperazin-1-yl]-N-[(1S,2S,5S)-2,5-dimethoxycyclohexyl]acetamide [Escherichia coli K-12]
3LPF_A 4.09e-17 27 359 17 305
Structureof E. coli beta-Glucuronidase bound with a novel, potent inhibitor 1-((6,7-dimethyl-2-oxo-1,2-dihydroquinolin-3-yl)methyl)-1-(2-hydroxyethyl)-3-(3-methoxyphenyl)thiourea [Escherichia coli K-12],3LPF_B Structure of E. coli beta-Glucuronidase bound with a novel, potent inhibitor 1-((6,7-dimethyl-2-oxo-1,2-dihydroquinolin-3-yl)methyl)-1-(2-hydroxyethyl)-3-(3-methoxyphenyl)thiourea [Escherichia coli K-12],3LPG_A Structure of E. coli beta-Glucuronidase bound with a novel, potent inhibitor 3-(2-fluorophenyl)-1-(2-hydroxyethyl)-1-((6-methyl-2-oxo-1,2-dihydroquinolin-3-yl)methyl)urea [Escherichia coli K-12],3LPG_B Structure of E. coli beta-Glucuronidase bound with a novel, potent inhibitor 3-(2-fluorophenyl)-1-(2-hydroxyethyl)-1-((6-methyl-2-oxo-1,2-dihydroquinolin-3-yl)methyl)urea [Escherichia coli K-12],5CZK_A Structure of E. coli beta-glucuronidase bound with a novel, potent inhibitor 1-((6,8-dimethyl-2-oxo-1,2-dihydroquinolin-3-yl)methyl)-1-(2-hydroxyethyl)-3-(4-hydroxyphenyl)thiourea [Escherichia coli K-12],5CZK_B Structure of E. coli beta-glucuronidase bound with a novel, potent inhibitor 1-((6,8-dimethyl-2-oxo-1,2-dihydroquinolin-3-yl)methyl)-1-(2-hydroxyethyl)-3-(4-hydroxyphenyl)thiourea [Escherichia coli K-12]
6JZ1_A 5.37e-17 26 411 19 359
Apostructure of b-glucuronidase from Ruminococcus gnavus at 1.7 Angstrom resolution [[Ruminococcus] gnavus],6JZ1_B Apo structure of b-glucuronidase from Ruminococcus gnavus at 1.7 Angstrom resolution [[Ruminococcus] gnavus],6JZ5_A b-glucuronidase from Ruminococcus gnavus in complex with D-glucuronic acid [[Ruminococcus] gnavus],6JZ5_B b-glucuronidase from Ruminococcus gnavus in complex with D-glucuronic acid [[Ruminococcus] gnavus],6JZ6_A b-glucuronidase from Ruminococcus gnavus in complex with C6-substituted uronic isofagomine [[Ruminococcus] gnavus],6JZ6_B b-glucuronidase from Ruminococcus gnavus in complex with C6-substituted uronic isofagomine [[Ruminococcus] gnavus],6JZ7_A b-glucuronidase from Ruminococcus gnavus in complex with N1-substituted uronic isofagomine [[Ruminococcus] gnavus],6JZ7_B b-glucuronidase from Ruminococcus gnavus in complex with N1-substituted uronic isofagomine [[Ruminococcus] gnavus],6JZ8_A b-glucuronidase from Ruminococcus gnavus in complex with D-glucaro 1,5-lactone [[Ruminococcus] gnavus],6JZ8_B b-glucuronidase from Ruminococcus gnavus in complex with D-glucaro 1,5-lactone [[Ruminococcus] gnavus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P05804 6.77e-16 27 359 15 303
Beta-glucuronidase OS=Escherichia coli (strain K12) OX=83333 GN=uidA PE=1 SV=2
P08236 6.71e-12 27 483 41 483
Beta-glucuronidase OS=Homo sapiens OX=9606 GN=GUSB PE=1 SV=2
Q5R5N6 1.16e-11 27 483 41 483
Beta-glucuronidase OS=Pongo abelii OX=9601 GN=GUSB PE=2 SV=2
O77695 4.58e-11 27 480 38 477
Beta-glucuronidase (Fragment) OS=Chlorocebus aethiops OX=9534 GN=GUSB PE=2 SV=1
P0C1Y0 3.14e-06 19 478 47 487
Beta-galactosidase OS=Lactobacillus delbrueckii subsp. bulgaricus OX=1585 GN=lacZ 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
0.000202 0.999238 0.000142 0.000144 0.000133 0.000129

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000211_01988.