Species | ||||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-552; UBA10677; | |||||||||||
CAZyme ID | MGYG000000640_01069 | |||||||||||
CAZy Family | GH2 | |||||||||||
CAZyme Description | Beta-galactosidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 43149; End: 45650 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH2 | 51 | 698 | 4.6e-86 | 0.6090425531914894 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3250 | LacZ | 4.23e-53 | 7 | 654 | 18 | 631 | Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]. |
PRK10340 | ebgA | 1.08e-14 | 58 | 450 | 113 | 456 | cryptic beta-D-galactosidase subunit alpha; Reviewed |
pfam17753 | Ig_mannosidase | 2.18e-12 | 753 | 827 | 1 | 74 | Ig-fold domain. This Ig-like fold domain is found in mannosidase enzymes. |
pfam00703 | Glyco_hydro_2 | 5.95e-07 | 183 | 308 | 2 | 106 | Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities. |
pfam02837 | Glyco_hydro_2_N | 7.55e-07 | 58 | 122 | 69 | 131 | Glycosyl hydrolases family 2, sugar binding domain. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities and has a jelly-roll fold. The domain binds the sugar moiety during the sugar-hydrolysis reaction. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QHI68839.1 | 1.13e-169 | 17 | 803 | 27 | 804 |
AQQ71581.1 | 3.21e-156 | 13 | 807 | 33 | 812 |
AKJ63700.1 | 9.35e-130 | 16 | 813 | 26 | 827 |
ACK43074.1 | 7.09e-103 | 8 | 734 | 10 | 714 |
ADL68205.1 | 3.21e-102 | 8 | 814 | 11 | 807 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5N6U_A | 3.29e-101 | 8 | 737 | 33 | 739 | Crystalstructure of Beta-D-Mannosidase from Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12],5N6U_B Crystal structure of Beta-D-Mannosidase from Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12],5N6U_C Crystal structure of Beta-D-Mannosidase from Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12],5N6U_D Crystal structure of Beta-D-Mannosidase from Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12] |
2VJX_A | 2.94e-74 | 8 | 827 | 15 | 832 | 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] |
2JE8_A | 3.03e-74 | 8 | 827 | 17 | 834 | Structureof a beta-mannosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],2JE8_B Structure of a beta-mannosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482] |
7OP6_A | 3.08e-74 | 8 | 827 | 17 | 834 | ChainA, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP6_B Chain B, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP7_A Chain A, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP7_B Chain B, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482] |
2WBK_A | 4.10e-74 | 8 | 827 | 15 | 832 | Structureof the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis [Bacteroides thetaiotaomicron VPI-5482],2WBK_B Structure of the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis [Bacteroides thetaiotaomicron VPI-5482] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
I2C092 | 6.30e-77 | 6 | 827 | 11 | 850 | Beta-mannosidase B OS=Thermothelomyces thermophilus OX=78579 GN=man9 PE=1 SV=1 |
Q8K2I4 | 3.60e-73 | 7 | 797 | 28 | 844 | Beta-mannosidase OS=Mus musculus OX=10090 GN=Manba PE=1 SV=1 |
Q95327 | 3.30e-72 | 7 | 674 | 28 | 709 | Beta-mannosidase OS=Capra hircus OX=9925 GN=MANBA PE=1 SV=1 |
Q29444 | 2.74e-70 | 7 | 670 | 28 | 703 | Beta-mannosidase OS=Bos taurus OX=9913 GN=MANBA PE=1 SV=1 |
Q4FZV0 | 3.49e-69 | 18 | 782 | 40 | 830 | Beta-mannosidase OS=Rattus norvegicus OX=10116 GN=Manba PE=2 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000041 | 0.000002 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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