Species | Paenibacillus_B thiaminolyticus | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_B; Paenibacillus_B thiaminolyticus | |||||||||||
CAZyme ID | MGYG000002490_00381 | |||||||||||
CAZy Family | GH2 | |||||||||||
CAZyme Description | Beta-galactosidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 118157; End: 120640 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH2 | 4 | 733 | 3.9e-109 | 0.738031914893617 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3250 | LacZ | 7.91e-111 | 5 | 773 | 14 | 763 | Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]. |
pfam17753 | Ig_mannosidase | 3.60e-22 | 742 | 822 | 1 | 78 | Ig-fold domain. This Ig-like fold domain is found in mannosidase enzymes. |
pfam17786 | Mannosidase_ig | 2.46e-16 | 647 | 737 | 1 | 91 | Mannosidase Ig/CBM-like domain. This domain corresponds to domain 4 in the structure of Bacteroides thetaiotaomicron beta-mannosidase, BtMan2A. This domain has an Ig-like fold. |
PRK10340 | ebgA | 3.78e-13 | 176 | 426 | 195 | 449 | cryptic beta-D-galactosidase subunit alpha; Reviewed |
pfam00703 | Glyco_hydro_2 | 4.85e-11 | 191 | 295 | 2 | 106 | Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QDM44823.1 | 0.0 | 1 | 827 | 1 | 827 |
AJY74274.1 | 0.0 | 1 | 824 | 1 | 828 |
QUH28340.1 | 0.0 | 1 | 822 | 1 | 817 |
AUG59052.1 | 0.0 | 4 | 823 | 3 | 817 |
AWB45455.1 | 0.0 | 1 | 822 | 1 | 816 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6BYE_A | 2.40e-173 | 1 | 820 | 3 | 850 | Crystalstructure of the GH2 exo-beta-mannanase from Xanthomonas axonopodis pv. citri in complex with mannose [Xanthomonas citri pv. citri str. 306],6BYE_B Crystal structure of the GH2 exo-beta-mannanase from Xanthomonas axonopodis pv. citri in complex with mannose [Xanthomonas citri pv. citri str. 306] |
6BYC_A | 2.47e-173 | 1 | 820 | 3 | 850 | Crystalstructure of the GH2 exo-beta-mannanase from Xanthomonas axonopodis pv. citri [Xanthomonas citri pv. citri str. 306] |
6BYI_A | 1.78e-172 | 1 | 820 | 1 | 848 | Crystalstructure of the acid-base mutant (E477A) of the GH2 exo-beta-mannanase from Xanthomonas axonopodis pv. citri [Xanthomonas citri pv. citri str. 306],6BYI_B Crystal structure of the acid-base mutant (E477A) of the GH2 exo-beta-mannanase from Xanthomonas axonopodis pv. citri [Xanthomonas citri pv. citri str. 306] |
6BYG_A | 1.83e-172 | 1 | 820 | 3 | 850 | Crystalstructure of the nucleophile mutant (E575A) of the GH2 exo-beta-mannanase from Xanthomonas axonopodis pv. citri [Xanthomonas citri pv. citri str. 306],6BYG_B Crystal structure of the nucleophile mutant (E575A) of the GH2 exo-beta-mannanase from Xanthomonas axonopodis pv. citri [Xanthomonas citri pv. citri str. 306] |
2VJX_A | 5.82e-163 | 6 | 808 | 11 | 827 | Structuraland biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VJX_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VL4_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VL4_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VMF_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VMF_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VO5_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VO5_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VOT_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VOT_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VQT_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron],2VQT_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron],2VR4_A Transition-state mimicry in mannoside hydrolysis: characterisation of twenty six inhibitors and insight into binding from linear free energy relationships and 3-D structure [Bacteroides thetaiotaomicron VPI-5482],2VR4_B Transition-state mimicry in mannoside hydrolysis: characterisation of twenty six inhibitors and insight into binding from linear free energy relationships and 3-D structure [Bacteroides thetaiotaomicron VPI-5482] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q95327 | 5.51e-113 | 1 | 824 | 20 | 879 | Beta-mannosidase OS=Capra hircus OX=9925 GN=MANBA PE=1 SV=1 |
Q29444 | 1.15e-110 | 1 | 824 | 20 | 879 | Beta-mannosidase OS=Bos taurus OX=9913 GN=MANBA PE=1 SV=1 |
O00462 | 4.50e-109 | 2 | 824 | 21 | 879 | Beta-mannosidase OS=Homo sapiens OX=9606 GN=MANBA PE=1 SV=3 |
Q0CCA0 | 4.19e-107 | 10 | 726 | 13 | 755 | Beta-mannosidase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=mndB PE=3 SV=2 |
A1CGA8 | 2.44e-104 | 3 | 695 | 6 | 751 | Beta-mannosidase B OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=mndB PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000063 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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