Species | Paraprevotella sp003477995 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Paraprevotella; Paraprevotella sp003477995 | |||||||||||
CAZyme ID | MGYG000002275_02647 | |||||||||||
CAZy Family | GH2 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 37361; End: 40120 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH2 | 26 | 517 | 8.6e-71 | 0.5093085106382979 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3250 | LacZ | 2.23e-21 | 25 | 446 | 11 | 426 | Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]. |
PRK10150 | PRK10150 | 1.21e-17 | 27 | 322 | 13 | 296 | beta-D-glucuronidase; Provisional |
pfam02837 | Glyco_hydro_2_N | 1.32e-11 | 29 | 170 | 4 | 155 | 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 | 9.63e-11 | 196 | 302 | 1 | 106 | Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities. |
PRK10340 | ebgA | 6.40e-10 | 12 | 425 | 21 | 449 | cryptic beta-D-galactosidase subunit alpha; Reviewed |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BAD47686.1 | 0.0 | 19 | 918 | 25 | 922 |
AUI45420.1 | 0.0 | 28 | 918 | 36 | 922 |
QRP91141.1 | 0.0 | 19 | 918 | 25 | 922 |
CBW21485.1 | 0.0 | 19 | 918 | 25 | 922 |
QTO27419.1 | 0.0 | 28 | 918 | 36 | 922 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6XXW_A | 2.83e-08 | 87 | 425 | 69 | 416 | Structureof beta-D-Glucuronidase for Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12] |
4CU6_A | 5.81e-08 | 90 | 425 | 74 | 428 | Unravellingthe multiple functions of the architecturally intricate Streptococcus pneumoniae beta-galactosidase, BgaA [Streptococcus pneumoniae TIGR4],4CU7_A Unravelling the multiple functions of the architecturally intricate Streptococcus pneumoniae beta-galactosidase, BgaA [Streptococcus pneumoniae TIGR4],4CU8_A Unravelling the multiple functions of the architecturally intricate Streptococcus pneumoniae beta-galactosidase, BgaA [Streptococcus pneumoniae TIGR4] |
4CUC_A | 5.81e-08 | 90 | 425 | 74 | 428 | Unravellingthe multiple functions of the architecturally intricate Streptococcus pneumoniae beta-galactosidase, BgaA. [Streptococcus pneumoniae TIGR4] |
4JHZ_A | 2.56e-07 | 29 | 164 | 17 | 142 | 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] |
6LEG_A | 2.56e-07 | 29 | 164 | 16 | 141 | ChainA, Beta-D-glucuronidase [Escherichia coli],6LEG_B Chain B, Beta-D-glucuronidase [Escherichia coli],6LEG_C Chain C, Beta-D-glucuronidase [Escherichia coli],6LEG_D Chain D, Beta-D-glucuronidase [Escherichia coli],6LEL_A Chain A, Beta-D-glucuronidase [Escherichia coli],6LEL_B Chain B, Beta-D-glucuronidase [Escherichia coli] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P05804 | 1.40e-06 | 29 | 164 | 15 | 140 | 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 |
---|---|---|---|---|---|
0.000463 | 0.998617 | 0.000267 | 0.000215 | 0.000197 | 0.000197 |
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