Species | COE1 sp900753305 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; COE1; COE1 sp900753305 | |||||||||||
CAZyme ID | MGYG000001814_02521 | |||||||||||
CAZy Family | GH42 | |||||||||||
CAZyme Description | Beta-galactosidase BgaA | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 12799; End: 14790 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH42 | 8 | 379 | 2.3e-149 | 0.9919137466307277 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam02449 | Glyco_hydro_42 | 2.07e-164 | 8 | 376 | 1 | 370 | 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 | 2.49e-130 | 6 | 659 | 19 | 673 | Beta-galactosidase GanA [Carbohydrate transport and metabolism]. |
pfam08532 | Glyco_hydro_42M | 5.09e-61 | 394 | 588 | 2 | 198 | 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 | 1.50e-21 | 395 | 516 | 1 | 123 | 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. |
pfam08533 | Glyco_hydro_42C | 6.75e-07 | 605 | 658 | 1 | 58 | Beta-galactosidase C-terminal domain. This domain is found at the C-terminus of beta-galactosidase enzymes that belong to the glycosyl hydrolase 42 family. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BCJ94071.1 | 1.72e-296 | 3 | 656 | 4 | 661 |
QFR24549.1 | 1.71e-259 | 3 | 658 | 5 | 661 |
QEU47466.1 | 6.67e-259 | 3 | 658 | 5 | 661 |
QFR62998.1 | 2.52e-256 | 3 | 658 | 5 | 661 |
AGB41273.1 | 1.04e-200 | 3 | 652 | 1 | 651 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6LVW_A | 2.71e-140 | 3 | 619 | 1 | 634 | PolyextremophilicBeta-galactosidase from the Antarctic haloarchaeon Halorubrum lacusprofundi [Halorubrum lacusprofundi ATCC 49239] |
3TTS_A | 1.27e-119 | 3 | 631 | 9 | 642 | 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] |
1KWG_A | 2.16e-119 | 6 | 656 | 3 | 642 | 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] |
6Y2K_A | 4.82e-111 | 6 | 516 | 4 | 529 | ChainA, beta-galactosidase [Marinomonas sp. ef1] |
5E9A_A | 1.83e-99 | 2 | 637 | 38 | 683 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
D9SM34 | 2.40e-158 | 3 | 631 | 1 | 626 | Beta-galactosidase BgaA OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=bgaA PE=1 SV=1 |
P94804 | 4.71e-147 | 6 | 643 | 4 | 640 | Beta-galactosidase BgaH OS=Haloferax lucentense (strain DSM 14919 / JCM 9276 / NCIMB 13854 / Aa 2.2) OX=1230452 GN=bgaH PE=1 SV=2 |
B9LW38 | 1.49e-139 | 3 | 619 | 1 | 634 | Beta-galactosidase Bga OS=Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34) OX=416348 GN=Hlac_2868 PE=1 SV=1 |
P19668 | 1.28e-129 | 3 | 642 | 7 | 645 | Beta-galactosidase bgaB OS=Geobacillus kaustophilus OX=1462 GN=bgaB PE=1 SV=1 |
C9S0R2 | 1.98e-128 | 3 | 642 | 7 | 645 | Beta-galactosidase BgaB OS=Geobacillus sp. (strain Y412MC61) OX=544556 GN=bgaB PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000048 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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