Species | Paenibacillus odorifer | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus odorifer | |||||||||||
CAZyme ID | MGYG000002414_03041 | |||||||||||
CAZy Family | GH42 | |||||||||||
CAZyme Description | Beta-galactosidase bgaB | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 3433614; End: 3435794 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH42 | 18 | 384 | 8.1e-65 | 0.9730458221024259 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam02449 | Glyco_hydro_42 | 6.95e-36 | 22 | 382 | 9 | 369 | 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 | 6.26e-22 | 12 | 490 | 22 | 489 | Beta-galactosidase GanA [Carbohydrate transport and metabolism]. |
cd03143 | A4_beta-galactosidase_middle_domain | 2.19e-08 | 404 | 489 | 2 | 84 | 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. |
cd01653 | GATase1 | 0.006 | 423 | 492 | 8 | 86 | Type 1 glutamine amidotransferase (GATase1)-like domain. Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AWV33842.1 | 0.0 | 1 | 726 | 1 | 726 |
AIQ24059.1 | 0.0 | 6 | 726 | 5 | 725 |
BBH22140.1 | 0.0 | 6 | 725 | 5 | 712 |
BBH22309.1 | 0.0 | 40 | 725 | 1 | 685 |
QTH41499.1 | 0.0 | 1 | 726 | 1 | 716 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5E9A_A | 2.98e-20 | 46 | 352 | 79 | 380 | 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 | 5.95e-19 | 23 | 668 | 18 | 634 | 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] |
5XB7_A | 5.37e-17 | 8 | 617 | 9 | 601 | GH42alpha-L-arabinopyranosidase from Bifidobacterium animalis subsp. lactis Bl-04 [Bifidobacterium animalis subsp. lactis],5XB7_B GH42 alpha-L-arabinopyranosidase from Bifidobacterium animalis subsp. lactis Bl-04 [Bifidobacterium animalis subsp. lactis],5XB7_C GH42 alpha-L-arabinopyranosidase from Bifidobacterium animalis subsp. lactis Bl-04 [Bifidobacterium animalis subsp. lactis],5XB7_D GH42 alpha-L-arabinopyranosidase from Bifidobacterium animalis subsp. lactis Bl-04 [Bifidobacterium animalis subsp. lactis],5XB7_E GH42 alpha-L-arabinopyranosidase from Bifidobacterium animalis subsp. lactis Bl-04 [Bifidobacterium animalis subsp. lactis],5XB7_F GH42 alpha-L-arabinopyranosidase from Bifidobacterium animalis subsp. lactis Bl-04 [Bifidobacterium animalis subsp. lactis] |
4UCF_A | 3.64e-13 | 25 | 414 | 36 | 424 | Crystalstructure of Bifidobacterium bifidum beta-galactosidase in complex with alpha-galactose [Bifidobacterium bifidum S17],4UCF_B Crystal structure of Bifidobacterium bifidum beta-galactosidase in complex with alpha-galactose [Bifidobacterium bifidum S17],4UCF_C Crystal structure of Bifidobacterium bifidum beta-galactosidase in complex with alpha-galactose [Bifidobacterium bifidum S17],4UZS_A Crystal structure of Bifidobacterium bifidum beta-galactosidase [Bifidobacterium bifidum S17],4UZS_B Crystal structure of Bifidobacterium bifidum beta-galactosidase [Bifidobacterium bifidum S17],4UZS_C Crystal structure of Bifidobacterium bifidum beta-galactosidase [Bifidobacterium bifidum S17] |
6Y2K_A | 2.92e-11 | 11 | 215 | 4 | 196 | ChainA, beta-galactosidase [Marinomonas sp. ef1] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
D5JGG0 | 1.77e-29 | 25 | 671 | 24 | 626 | Beta-galactosidase LacZ OS=Weizmannia coagulans OX=1398 GN=lacZ PE=3 SV=1 |
P19668 | 2.38e-28 | 25 | 703 | 23 | 660 | Beta-galactosidase bgaB OS=Geobacillus kaustophilus OX=1462 GN=bgaB PE=1 SV=1 |
C9S0R2 | 7.42e-28 | 25 | 703 | 23 | 660 | Beta-galactosidase BgaB OS=Geobacillus sp. (strain Y412MC61) OX=544556 GN=bgaB PE=3 SV=1 |
Q9KI47 | 1.86e-22 | 22 | 675 | 23 | 645 | Beta-galactosidase BgaA OS=Planococcus sp. (strain 'SOS Orange') OX=128803 GN=bgaA PE=1 SV=1 |
D9SM34 | 2.34e-22 | 22 | 671 | 14 | 621 | Beta-galactosidase BgaA OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=bgaA PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000078 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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