Species | Blautia stercoris | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia; Blautia stercoris | |||||||||||
CAZyme ID | MGYG000002286_01448 | |||||||||||
CAZy Family | GH42 | |||||||||||
CAZyme Description | Beta-galactosidase BgaA | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 114280; End: 116229 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH42 | 6 | 379 | 2.1e-127 | 0.9919137466307277 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam02449 | Glyco_hydro_42 | 4.27e-136 | 6 | 382 | 1 | 376 | Beta-galactosidase. This group of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. The enzyme catalyzes the hydrolysis of terminal, non-reducing terminal beta-D-galactosidase residues. |
COG1874 | GanA | 1.20e-121 | 1 | 647 | 16 | 670 | Beta-galactosidase GanA [Carbohydrate transport and metabolism]. |
pfam08532 | Glyco_hydro_42M | 3.26e-48 | 392 | 600 | 1 | 206 | Beta-galactosidase trimerisation domain. This is non catalytic domain B of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. This domain is related to glutamine amidotransferase enzymes, but the catalytic residues are replaced by non functional amino acids. This domain is involved in trimerisation. |
cd03143 | A4_beta-galactosidase_middle_domain | 1.04e-25 | 394 | 520 | 1 | 125 | A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain. A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to beta-galactosidase from Thermus thermophilus. Beta-Galactosidase hydrolyzes the beta-1,4-D-galactosidic linkage of lactose, as well as those of related chromogens, o-nitrophenyl-beta-D-galactopyranoside (ONP-Gal) and 5-bromo-4-chloro-3-indolyl-beta-D-galactoside (X-gal). This A4 beta-galactosidase middle domain lacks the catalytic triad of typical GATase1 domains. The reactive Cys residue found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow in typical GATase1 domains is not conserved in this group. |
pfam01301 | Glyco_hydro_35 | 3.26e-05 | 9 | 152 | 23 | 159 | Glycosyl hydrolases family 35. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QQQ99503.1 | 0.0 | 1 | 646 | 1 | 646 |
ANU45745.1 | 0.0 | 1 | 646 | 1 | 646 |
QIX93296.1 | 0.0 | 1 | 646 | 1 | 646 |
AVQ18862.1 | 0.0 | 1 | 647 | 1 | 647 |
QNM14994.1 | 4.20e-310 | 1 | 646 | 1 | 644 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3TTS_A | 8.10e-108 | 1 | 632 | 9 | 640 | ChainA, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTS_B Chain B, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTS_C Chain C, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTS_D Chain D, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTS_E Chain E, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTS_F Chain F, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTY_A Chain A, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTY_B Chain B, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTY_C Chain C, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTY_D Chain D, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTY_E Chain E, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTY_F Chain F, Beta-galactosidase [Niallia circulans subsp. alkalophilus] |
6LVW_A | 2.08e-97 | 1 | 618 | 1 | 632 | PolyextremophilicBeta-galactosidase from the Antarctic haloarchaeon Halorubrum lacusprofundi [Halorubrum lacusprofundi ATCC 49239] |
4OIF_A | 4.73e-87 | 4 | 614 | 18 | 633 | 3Dstructure of Gan42B, a GH42 beta-galactosidase from G. [Geobacillus stearothermophilus],4OIF_B 3D structure of Gan42B, a GH42 beta-galactosidase from G. [Geobacillus stearothermophilus],4OIF_C 3D structure of Gan42B, a GH42 beta-galactosidase from G. [Geobacillus stearothermophilus] |
4OJY_A | 4.84e-87 | 4 | 614 | 19 | 634 | 3Dstructure of the E323A catalytic mutant of Gan42B, a GH42 beta-galactosidase from G. stearothermophilus [Geobacillus stearothermophilus],4OJY_B 3D structure of the E323A catalytic mutant of Gan42B, a GH42 beta-galactosidase from G. stearothermophilus [Geobacillus stearothermophilus],4OJY_C 3D structure of the E323A catalytic mutant of Gan42B, a GH42 beta-galactosidase from G. stearothermophilus [Geobacillus stearothermophilus] |
5DFA_A | 3.51e-86 | 4 | 614 | 18 | 633 | 3Dstructure of the E323A catalytic mutant of Gan42B, a GH42 beta-galactosidase from G. stearothermophilus [Geobacillus stearothermophilus],5DFA_B 3D structure of the E323A catalytic mutant of Gan42B, a GH42 beta-galactosidase from G. stearothermophilus [Geobacillus stearothermophilus],5DFA_C 3D structure of the E323A catalytic mutant of Gan42B, a GH42 beta-galactosidase from G. stearothermophilus [Geobacillus stearothermophilus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
D9SM34 | 2.46e-121 | 1 | 633 | 1 | 624 | Beta-galactosidase BgaA OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=bgaA PE=1 SV=1 |
D5JGG0 | 3.76e-101 | 4 | 627 | 11 | 624 | Beta-galactosidase LacZ OS=Weizmannia coagulans OX=1398 GN=lacZ PE=3 SV=1 |
Q5FJ41 | 2.45e-98 | 4 | 631 | 10 | 633 | Beta-galactosidase LacZ OS=Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) OX=272621 GN=lacZ PE=1 SV=1 |
Q0TUR6 | 4.46e-97 | 4 | 631 | 17 | 653 | Beta-galactosidase Pbg OS=Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A) OX=195103 GN=pbg PE=3 SV=1 |
B9LW38 | 1.14e-96 | 1 | 618 | 1 | 632 | Beta-galactosidase Bga OS=Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34) OX=416348 GN=Hlac_2868 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000051 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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