Species | Eubacterium_R sp900766895 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Eubacterium_R; Eubacterium_R sp900766895 | |||||||||||
CAZyme ID | MGYG000003430_00614 | |||||||||||
CAZy Family | GH2 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 10515; End: 13037 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH2 | 2 | 746 | 1.6e-98 | 0.7752659574468085 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3250 | LacZ | 3.66e-93 | 1 | 767 | 11 | 773 | Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]. |
pfam17753 | Ig_mannosidase | 3.97e-16 | 724 | 801 | 1 | 78 | Ig-fold domain. This Ig-like fold domain is found in mannosidase enzymes. |
pfam00703 | Glyco_hydro_2 | 1.82e-10 | 189 | 285 | 5 | 106 | Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities. |
PRK10150 | PRK10150 | 3.39e-10 | 3 | 417 | 13 | 417 | beta-D-glucuronidase; Provisional |
pfam02837 | Glyco_hydro_2_N | 3.15e-05 | 3 | 138 | 2 | 148 | 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 |
---|---|---|---|---|---|
BCJ98156.1 | 2.98e-210 | 1 | 825 | 2 | 847 |
BAJ62595.1 | 1.25e-183 | 9 | 799 | 14 | 825 |
AUG59052.1 | 1.50e-182 | 5 | 801 | 5 | 816 |
CUS03525.2 | 1.48e-180 | 3 | 801 | 4 | 817 |
QEH70285.1 | 1.51e-179 | 5 | 802 | 6 | 821 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2VJX_A | 3.20e-147 | 5 | 777 | 11 | 814 | 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 | 3.37e-147 | 5 | 777 | 13 | 816 | 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 | 3.47e-147 | 5 | 777 | 13 | 816 | 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 | 9.12e-147 | 5 | 777 | 11 | 814 | 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] |
2VQU_A | 3.75e-145 | 5 | 777 | 11 | 814 | Structuraland biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron],2VQU_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q95327 | 4.16e-111 | 4 | 801 | 24 | 877 | Beta-mannosidase OS=Capra hircus OX=9925 GN=MANBA PE=1 SV=1 |
Q29444 | 1.17e-109 | 4 | 801 | 24 | 877 | Beta-mannosidase OS=Bos taurus OX=9913 GN=MANBA PE=1 SV=1 |
O00462 | 2.66e-101 | 4 | 802 | 24 | 878 | Beta-mannosidase OS=Homo sapiens OX=9606 GN=MANBA PE=1 SV=3 |
I2C092 | 1.67e-98 | 5 | 784 | 9 | 841 | Beta-mannosidase B OS=Thermothelomyces thermophilus OX=78579 GN=man9 PE=1 SV=1 |
Q4FZV0 | 2.04e-98 | 4 | 802 | 24 | 880 | 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 |
---|---|---|---|---|---|
1.000065 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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