Species | ||||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Fusicatenibacter; | |||||||||||
CAZyme ID | MGYG000004233_00246 | |||||||||||
CAZy Family | GH42 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 78606; End: 80690 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH42 | 22 | 383 | 8.2e-48 | 0.9703504043126685 |
GH164 | 301 | 594 | 6e-16 | 0.44029850746268656 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG1874 | GanA | 1.00e-20 | 113 | 669 | 119 | 661 | Beta-galactosidase GanA [Carbohydrate transport and metabolism]. |
pfam02449 | Glyco_hydro_42 | 3.75e-18 | 101 | 385 | 86 | 375 | 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 | 3.40e-12 | 399 | 586 | 3 | 186 | 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 | 4.67e-06 | 399 | 521 | 1 | 112 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QGQ98429.1 | 1.26e-190 | 8 | 644 | 4 | 653 |
QDS99940.1 | 6.57e-75 | 11 | 682 | 7 | 686 |
QOY85233.1 | 1.79e-57 | 15 | 665 | 44 | 721 |
QYY35048.1 | 1.08e-56 | 11 | 623 | 16 | 631 |
AHF91909.1 | 3.72e-54 | 8 | 614 | 11 | 632 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4OIF_A | 2.50e-16 | 22 | 644 | 34 | 649 | 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 | 2.51e-16 | 22 | 644 | 35 | 650 | 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 | 4.36e-16 | 22 | 644 | 34 | 649 | 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] |
5E9A_A | 1.37e-15 | 24 | 659 | 60 | 687 | 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] |
1KWG_A | 1.83e-13 | 101 | 644 | 90 | 615 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
D5JGG0 | 2.44e-25 | 29 | 586 | 28 | 576 | Beta-galactosidase LacZ OS=Weizmannia coagulans OX=1398 GN=lacZ PE=3 SV=1 |
Q9RFN0 | 9.23e-23 | 125 | 642 | 120 | 629 | Beta-galactosidase BgaB OS=Carnobacterium maltaromaticum OX=2751 GN=bgaB PE=1 SV=1 |
C8WV58 | 9.57e-15 | 119 | 588 | 123 | 596 | Beta-galactosidase BglY OS=Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-IA) OX=521098 GN=bglY PE=1 SV=1 |
Q0TUR6 | 2.90e-14 | 119 | 655 | 123 | 662 | 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 |
Q65CX4 | 8.61e-14 | 120 | 684 | 107 | 660 | Beta-galactosidase GalA 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=lacA PE=1 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000058 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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