Species | Gracilibacillus massiliensis | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Bacillales_D; Amphibacillaceae; Gracilibacillus; Gracilibacillus massiliensis | |||||||||||
CAZyme ID | MGYG000001523_01026 | |||||||||||
CAZy Family | GH2 | |||||||||||
CAZyme Description | Beta-glucuronidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 256348; End: 257466 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH2 | 9 | 355 | 2.5e-83 | 0.4029255319148936 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
PRK10150 | PRK10150 | 0.0 | 1 | 371 | 1 | 374 | beta-D-glucuronidase; Provisional |
COG3250 | LacZ | 5.63e-84 | 1 | 357 | 1 | 368 | Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]. |
PRK10340 | ebgA | 3.63e-36 | 9 | 353 | 38 | 398 | cryptic beta-D-galactosidase subunit alpha; Reviewed |
pfam02837 | Glyco_hydro_2_N | 1.25e-35 | 15 | 182 | 4 | 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. |
pfam02836 | Glyco_hydro_2_C | 1.11e-34 | 275 | 357 | 1 | 83 | Glycosyl hydrolases family 2, TIM barrel domain. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ARK29794.1 | 6.75e-198 | 1 | 365 | 1 | 368 |
QNU27070.1 | 6.82e-195 | 1 | 372 | 1 | 373 |
QGQ44950.1 | 1.52e-194 | 1 | 365 | 1 | 368 |
AAR75615.1 | 8.70e-194 | 1 | 365 | 1 | 368 |
AAR75621.1 | 8.70e-194 | 1 | 365 | 1 | 368 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4JKM_A | 9.84e-182 | 1 | 365 | 4 | 369 | CrystalStructure of Clostridium perfringens beta-glucuronidase [Clostridium perfringens str. 13],4JKM_B Crystal Structure of Clostridium perfringens beta-glucuronidase [Clostridium perfringens str. 13],6CXS_A Crystal Structure of Clostridium perfringens beta-glucuronidase bound with a novel, potent inhibitor 4-(8-(piperazin-1-yl)-1,2,3,4-tetrahydro-[1,2,3]triazino[4',5':4,5]thieno[2,3-c]isoquinolin-5-yl)morpholine [Clostridium perfringens str. 13],6CXS_B Crystal Structure of Clostridium perfringens beta-glucuronidase bound with a novel, potent inhibitor 4-(8-(piperazin-1-yl)-1,2,3,4-tetrahydro-[1,2,3]triazino[4',5':4,5]thieno[2,3-c]isoquinolin-5-yl)morpholine [Clostridium perfringens str. 13] |
6D4O_A | 6.02e-139 | 1 | 362 | 4 | 377 | Eubacteriumeligens beta-glucuronidase bound to an amoxapine-glucuronide conjugate [Lachnospira eligens] |
6BO6_A | 3.12e-138 | 1 | 362 | 1 | 374 | Eubacteriumeligens beta-glucuronidase bound to UNC4917 glucuronic acid conjugate [[Eubacterium] eligens ATCC 27750] |
6BJQ_A | 6.18e-138 | 1 | 362 | 25 | 398 | ChainA, Glycoside Hydrolase Family 2 candidate b-glucuronidase [[Eubacterium] eligens ATCC 27750] |
6BJW_A | 6.37e-138 | 1 | 362 | 25 | 398 | ChainA, Glycoside Hydrolase Family 2 candidate b-glucuronidase [[Eubacterium] eligens ATCC 27750] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
O97524 | 1.81e-114 | 1 | 360 | 27 | 413 | Beta-glucuronidase OS=Felis catus OX=9685 GN=GUSB PE=1 SV=1 |
O18835 | 7.17e-114 | 1 | 360 | 27 | 413 | Beta-glucuronidase OS=Canis lupus familiaris OX=9615 GN=GUSB PE=1 SV=1 |
Q4FAT7 | 2.07e-113 | 1 | 370 | 28 | 421 | Beta-glucuronidase OS=Sus scrofa OX=9823 GN=GUSB PE=3 SV=1 |
P06760 | 9.13e-111 | 1 | 360 | 27 | 410 | Beta-glucuronidase OS=Rattus norvegicus OX=10116 GN=Gusb PE=1 SV=1 |
P05804 | 1.89e-108 | 1 | 361 | 1 | 360 | Beta-glucuronidase OS=Escherichia coli (strain K12) OX=83333 GN=uidA PE=1 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.999911 | 0.000140 | 0.000001 | 0.000000 | 0.000000 | 0.000000 |
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