Species | Acetatifactor sp003447295 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Acetatifactor; Acetatifactor sp003447295 | |||||||||||
CAZyme ID | MGYG000004250_02441 | |||||||||||
CAZy Family | GH2 | |||||||||||
CAZyme Description | Beta-galactosidase large subunit | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 62; End: 1981 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH2 | 28 | 632 | 7.4e-145 | 0.6263297872340425 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
PRK10340 | ebgA | 3.01e-159 | 6 | 629 | 3 | 596 | cryptic beta-D-galactosidase subunit alpha; Reviewed |
PRK09525 | lacZ | 6.31e-142 | 11 | 630 | 20 | 623 | beta-galactosidase. |
pfam02836 | Glyco_hydro_2_C | 2.60e-130 | 346 | 633 | 5 | 298 | Glycosyl hydrolases family 2, TIM barrel domain. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities. |
COG3250 | LacZ | 2.62e-123 | 33 | 638 | 3 | 557 | Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]. |
pfam02837 | Glyco_hydro_2_N | 1.94e-30 | 42 | 226 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QNM02889.1 | 0.0 | 1 | 639 | 1 | 639 |
ABX42393.1 | 8.21e-313 | 1 | 633 | 1 | 636 |
AQP40966.1 | 4.16e-304 | 1 | 633 | 1 | 630 |
CBK94938.1 | 4.98e-298 | 1 | 633 | 1 | 630 |
CBK90745.1 | 4.07e-297 | 1 | 633 | 1 | 630 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6S6Z_A | 2.41e-117 | 9 | 632 | 5 | 593 | Structureof beta-Galactosidase from Thermotoga maritima [Thermotoga maritima MSB8],6S6Z_B Structure of beta-Galactosidase from Thermotoga maritima [Thermotoga maritima MSB8],6S6Z_C Structure of beta-Galactosidase from Thermotoga maritima [Thermotoga maritima MSB8],6S6Z_D Structure of beta-Galactosidase from Thermotoga maritima [Thermotoga maritima MSB8],6S6Z_E Structure of beta-Galactosidase from Thermotoga maritima [Thermotoga maritima MSB8],6S6Z_F Structure of beta-Galactosidase from Thermotoga maritima [Thermotoga maritima MSB8],6S6Z_G Structure of beta-Galactosidase from Thermotoga maritima [Thermotoga maritima MSB8],6S6Z_H Structure of beta-Galactosidase from Thermotoga maritima [Thermotoga maritima MSB8] |
6SD0_A | 2.45e-117 | 9 | 632 | 6 | 594 | Structureof beta-galactosidase from Thermotoga maritima. [Thermotoga maritima MSB8],6SD0_B Structure of beta-galactosidase from Thermotoga maritima. [Thermotoga maritima MSB8],6SD0_C Structure of beta-galactosidase from Thermotoga maritima. [Thermotoga maritima MSB8],6SD0_D Structure of beta-galactosidase from Thermotoga maritima. [Thermotoga maritima MSB8] |
1F4A_A | 8.34e-101 | 9 | 630 | 15 | 620 | E.COLI (LACZ) BETA-GALACTOSIDASE (NCS CONSTRAINED MONOMER-ORTHORHOMBIC) [Escherichia coli],1F4A_B E. COLI (LACZ) BETA-GALACTOSIDASE (NCS CONSTRAINED MONOMER-ORTHORHOMBIC) [Escherichia coli],1F4A_C E. COLI (LACZ) BETA-GALACTOSIDASE (NCS CONSTRAINED MONOMER-ORTHORHOMBIC) [Escherichia coli],1F4A_D E. COLI (LACZ) BETA-GALACTOSIDASE (NCS CONSTRAINED MONOMER-ORTHORHOMBIC) [Escherichia coli],1F4H_A E. COLI (LACZ) BETA-GALACTOSIDASE (ORTHORHOMBIC) [Escherichia coli],1F4H_B E. COLI (LACZ) BETA-GALACTOSIDASE (ORTHORHOMBIC) [Escherichia coli],1F4H_C E. COLI (LACZ) BETA-GALACTOSIDASE (ORTHORHOMBIC) [Escherichia coli],1F4H_D E. COLI (LACZ) BETA-GALACTOSIDASE (ORTHORHOMBIC) [Escherichia coli] |
6CVM_A | 8.34e-101 | 9 | 630 | 16 | 621 | Atomicresolution cryo-EM structure of beta-galactosidase [Escherichia coli K-12],6CVM_B Atomic resolution cryo-EM structure of beta-galactosidase [Escherichia coli K-12],6CVM_C Atomic resolution cryo-EM structure of beta-galactosidase [Escherichia coli K-12],6CVM_D Atomic resolution cryo-EM structure of beta-galactosidase [Escherichia coli K-12],6X1Q_A 1.8 Angstrom resolution structure of b-galactosidase with a 200 kV cryoARM electron microscope [Escherichia coli K-12],6X1Q_B 1.8 Angstrom resolution structure of b-galactosidase with a 200 kV cryoARM electron microscope [Escherichia coli K-12],6X1Q_C 1.8 Angstrom resolution structure of b-galactosidase with a 200 kV cryoARM electron microscope [Escherichia coli K-12],6X1Q_D 1.8 Angstrom resolution structure of b-galactosidase with a 200 kV cryoARM electron microscope [Escherichia coli K-12] |
5A1A_A | 8.48e-101 | 9 | 630 | 16 | 621 | 2.2A resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor [Escherichia coli K-12],5A1A_B 2.2 A resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor [Escherichia coli K-12],5A1A_C 2.2 A resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor [Escherichia coli K-12],5A1A_D 2.2 A resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor [Escherichia coli K-12] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q48846 | 9.19e-288 | 1 | 633 | 1 | 622 | Beta-galactosidase large subunit OS=Latilactobacillus sakei OX=1599 GN=lacL PE=3 SV=1 |
Q02603 | 1.75e-278 | 1 | 633 | 1 | 623 | Beta-galactosidase large subunit OS=Leuconostoc lactis OX=1246 GN=lacL PE=1 SV=1 |
Q7WTB4 | 1.08e-277 | 1 | 633 | 1 | 625 | Beta-galactosidase large subunit OS=Lactobacillus helveticus OX=1587 GN=lacL PE=2 SV=1 |
O07684 | 1.36e-273 | 1 | 633 | 1 | 625 | Beta-galactosidase large subunit OS=Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) OX=272621 GN=lacL PE=3 SV=2 |
Q9K9C6 | 1.16e-213 | 3 | 632 | 5 | 614 | Beta-galactosidase OS=Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) OX=272558 GN=lacZ PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000052 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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