Species | Niallia sp900199695 | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; Bacillales_B; DSM-18226; Niallia; Niallia sp900199695 | |||||||||||
CAZyme ID | MGYG000003133_00815 | |||||||||||
CAZy Family | GH42 | |||||||||||
CAZyme Description | Beta-galactosidase YesZ | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 73690; End: 75675 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH42 | 10 | 369 | 1.4e-117 | 0.9811320754716981 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG1874 | GanA | 1.28e-162 | 1 | 660 | 13 | 673 | Beta-galactosidase GanA [Carbohydrate transport and metabolism]. |
pfam02449 | Glyco_hydro_42 | 4.02e-152 | 10 | 375 | 2 | 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. |
pfam08532 | Glyco_hydro_42M | 5.70e-40 | 387 | 592 | 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 | 7.13e-18 | 389 | 492 | 1 | 105 | 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. |
pfam01373 | Glyco_hydro_14 | 0.001 | 152 | 213 | 180 | 237 | Glycosyl hydrolase family 14. This family are beta amylases. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AYV73940.1 | 0.0 | 1 | 658 | 22 | 679 |
QKH62810.1 | 0.0 | 1 | 657 | 1 | 657 |
QJX63641.1 | 0.0 | 1 | 658 | 1 | 658 |
AYV67717.1 | 0.0 | 1 | 658 | 22 | 679 |
AOR97116.1 | 0.0 | 1 | 660 | 1 | 660 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1KWG_A | 1.32e-74 | 7 | 656 | 3 | 641 | Crystalstructure of Thermus thermophilus A4 beta-galactosidase [Thermus thermophilus],1KWK_A Crystal structure of Thermus thermophilus A4 beta-galactosidase in complex with galactose [Thermus thermophilus] |
6LVW_A | 5.50e-73 | 7 | 497 | 4 | 509 | PolyextremophilicBeta-galactosidase from the Antarctic haloarchaeon Halorubrum lacusprofundi [Halorubrum lacusprofundi ATCC 49239] |
5E9A_A | 8.41e-67 | 4 | 472 | 39 | 516 | Crystalstructure analysis of the cold-adamped beta-galactosidase from Rahnella sp. R3 [Rahnella sp. R3],5E9A_B Crystal structure analysis of the cold-adamped beta-galactosidase from Rahnella sp. R3 [Rahnella sp. R3],5E9A_C Crystal structure analysis of the cold-adamped beta-galactosidase from Rahnella sp. R3 [Rahnella sp. R3],5E9A_D Crystal structure analysis of the cold-adamped beta-galactosidase from Rahnella sp. R3 [Rahnella sp. R3],5E9A_E Crystal structure analysis of the cold-adamped beta-galactosidase from Rahnella sp. R3 [Rahnella sp. R3],5E9A_F Crystal structure analysis of the cold-adamped beta-galactosidase from Rahnella sp. R3 [Rahnella sp. R3] |
3TTS_A | 4.12e-58 | 3 | 650 | 8 | 665 | 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] |
4OIF_A | 2.40e-57 | 4 | 567 | 15 | 595 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
O31529 | 0.0 | 1 | 660 | 1 | 660 | Beta-galactosidase YesZ OS=Bacillus subtilis (strain 168) OX=224308 GN=yesZ PE=1 SV=1 |
Q65KX8 | 1.89e-302 | 3 | 657 | 4 | 657 | Beta-galactosidase YesZ OS=Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46) OX=279010 GN=yesZ PE=3 SV=2 |
P94804 | 3.33e-82 | 7 | 632 | 4 | 633 | Beta-galactosidase BgaH OS=Haloferax lucentense (strain DSM 14919 / JCM 9276 / NCIMB 13854 / Aa 2.2) OX=1230452 GN=bgaH PE=1 SV=2 |
Q9RFN0 | 1.57e-76 | 2 | 658 | 5 | 665 | Beta-galactosidase BgaB OS=Carnobacterium maltaromaticum OX=2751 GN=bgaB PE=1 SV=1 |
D5JGG0 | 1.07e-75 | 3 | 607 | 7 | 611 | Beta-galactosidase LacZ OS=Weizmannia coagulans OX=1398 GN=lacZ PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000076 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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