Species | Eubacterium_R coprostanoligenes | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Eubacterium_R; Eubacterium_R coprostanoligenes | |||||||||||
CAZyme ID | MGYG000001569_00835 | |||||||||||
CAZy Family | GH2 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 325673; End: 328198 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH2 | 3 | 747 | 1.6e-104 | 0.773936170212766 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3250 | LacZ | 1.23e-88 | 1 | 692 | 11 | 696 | Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]. |
pfam17753 | Ig_mannosidase | 5.28e-17 | 725 | 802 | 1 | 78 | Ig-fold domain. This Ig-like fold domain is found in mannosidase enzymes. |
PRK10150 | PRK10150 | 2.53e-16 | 3 | 416 | 13 | 417 | beta-D-glucuronidase; Provisional |
PRK10340 | ebgA | 4.85e-12 | 3 | 416 | 42 | 449 | cryptic beta-D-galactosidase subunit alpha; Reviewed |
pfam00703 | Glyco_hydro_2 | 2.84e-11 | 187 | 284 | 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 |
---|---|---|---|---|---|
BCJ98156.1 | 1.22e-212 | 1 | 826 | 2 | 847 |
AUG59052.1 | 1.39e-183 | 5 | 802 | 5 | 816 |
ADL52891.1 | 7.14e-180 | 1 | 802 | 1 | 817 |
BAV13124.1 | 9.36e-180 | 1 | 802 | 10 | 826 |
BBI32724.1 | 3.29e-179 | 5 | 802 | 6 | 821 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2VJX_A | 3.94e-153 | 4 | 778 | 10 | 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 | 4.16e-153 | 4 | 778 | 12 | 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 | 4.28e-153 | 4 | 778 | 12 | 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 | 1.13e-152 | 4 | 778 | 10 | 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] |
5N6U_A | 3.54e-151 | 5 | 791 | 29 | 819 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q29444 | 1.32e-105 | 5 | 634 | 25 | 700 | Beta-mannosidase OS=Bos taurus OX=9913 GN=MANBA PE=1 SV=1 |
Q95327 | 3.57e-105 | 5 | 634 | 25 | 700 | Beta-mannosidase OS=Capra hircus OX=9925 GN=MANBA PE=1 SV=1 |
Q4FZV0 | 5.43e-102 | 5 | 695 | 25 | 765 | Beta-mannosidase OS=Rattus norvegicus OX=10116 GN=Manba PE=2 SV=1 |
O00462 | 7.33e-101 | 5 | 803 | 25 | 878 | Beta-mannosidase OS=Homo sapiens OX=9606 GN=MANBA PE=1 SV=3 |
Q8K2I4 | 2.00e-98 | 5 | 687 | 25 | 757 | Beta-mannosidase OS=Mus musculus OX=10090 GN=Manba PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000062 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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