Species | RUG420 sp900542575 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; RUG420; RUG420 sp900542575 | |||||||||||
CAZyme ID | MGYG000003153_00907 | |||||||||||
CAZy Family | GH2 | |||||||||||
CAZyme Description | Beta-galactosidase BoGH2A | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 65903; End: 68275 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH2 | 4 | 539 | 1.9e-79 | 0.589095744680851 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3250 | LacZ | 6.16e-46 | 54 | 401 | 67 | 432 | Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]. |
PRK10150 | PRK10150 | 4.69e-32 | 50 | 399 | 65 | 446 | beta-D-glucuronidase; Provisional |
pfam18565 | Glyco_hydro2_C5 | 4.16e-16 | 684 | 786 | 1 | 103 | Glycoside hydrolase family 2 C-terminal domain 5. Domain 5 is found in dimeric beta-D-galactosidase from Paracoccus sp. 32d, which contributes to stabilization of the functional dimer. It is suggested that the location of this domain 5, may be one of the factors responsible for the creation of a functional dimer and cold-adaptation of this enzyme. |
PRK10340 | ebgA | 2.95e-15 | 54 | 396 | 113 | 470 | cryptic beta-D-galactosidase subunit alpha; Reviewed |
PRK09525 | lacZ | 6.76e-15 | 54 | 369 | 124 | 464 | beta-galactosidase. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AFN84582.1 | 8.00e-179 | 22 | 789 | 17 | 769 |
AEE97750.1 | 2.11e-171 | 1 | 787 | 1 | 784 |
QTL78998.1 | 1.75e-163 | 1 | 788 | 1 | 800 |
AHF23998.1 | 3.04e-144 | 1 | 781 | 23 | 823 |
QHC60608.1 | 4.00e-144 | 10 | 781 | 16 | 792 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6B6L_A | 9.98e-80 | 15 | 764 | 30 | 753 | Thecrystal structure of glycosyl hydrolase family 2 (GH2) member from Bacteroides cellulosilyticus DSM 14838 [Bacteroides cellulosilyticus DSM 14838],6B6L_B The crystal structure of glycosyl hydrolase family 2 (GH2) member from Bacteroides cellulosilyticus DSM 14838 [Bacteroides cellulosilyticus DSM 14838] |
7RSK_A | 3.87e-79 | 15 | 764 | 30 | 753 | ChainA, Glycosyl hydrolase family 2, sugar binding domain protein [Bacteroides cellulosilyticus DSM 14838],7RSK_B Chain B, Glycosyl hydrolase family 2, sugar binding domain protein [Bacteroides cellulosilyticus DSM 14838] |
5T98_A | 1.48e-53 | 2 | 762 | 55 | 793 | Crystalstructure of BuGH2Awt [Bacteroides uniformis],5T98_B Crystal structure of BuGH2Awt [Bacteroides uniformis],5T99_A Crystal structure of BuGH2Awt in complex with Galactoisofagomine [Bacteroides uniformis],5T99_B Crystal structure of BuGH2Awt in complex with Galactoisofagomine [Bacteroides uniformis] |
4YPJ_A | 1.10e-52 | 15 | 787 | 35 | 805 | ChainA, Beta galactosidase [Niallia circulans],4YPJ_B Chain B, Beta galactosidase [Niallia circulans] |
7CWD_A | 2.85e-49 | 20 | 787 | 34 | 799 | ChainA, beta-glalactosidase [Niallia circulans],7CWI_A Chain A, beta-galactosidase [Niallia circulans] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
A7LXS9 | 3.04e-46 | 16 | 781 | 68 | 842 | Beta-galactosidase BoGH2A OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02645 PE=1 SV=1 |
A7MN76 | 6.28e-19 | 54 | 398 | 134 | 494 | Beta-galactosidase OS=Cronobacter sakazakii (strain ATCC BAA-894) OX=290339 GN=lacZ PE=3 SV=1 |
P12265 | 2.55e-17 | 15 | 403 | 70 | 480 | Beta-glucuronidase OS=Mus musculus OX=10090 GN=Gusb PE=1 SV=2 |
O18835 | 1.36e-16 | 50 | 403 | 97 | 483 | Beta-glucuronidase OS=Canis lupus familiaris OX=9615 GN=GUSB PE=1 SV=1 |
P06760 | 4.09e-16 | 15 | 403 | 70 | 480 | Beta-glucuronidase OS=Rattus norvegicus OX=10116 GN=Gusb PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.998263 | 0.001755 | 0.000018 | 0.000003 | 0.000002 | 0.000004 |
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