Species | Eubacterium_R sp000434995 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Eubacterium_R; Eubacterium_R sp000434995 | |||||||||||
CAZyme ID | MGYG000001737_00746 | |||||||||||
CAZy Family | GH2 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 218490; End: 221039 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH2 | 3 | 748 | 2.3e-100 | 0.7659574468085106 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3250 | LacZ | 1.24e-77 | 1 | 630 | 11 | 635 | Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]. |
pfam17753 | Ig_mannosidase | 6.59e-21 | 730 | 807 | 1 | 78 | Ig-fold domain. This Ig-like fold domain is found in mannosidase enzymes. |
PRK10340 | ebgA | 7.04e-13 | 3 | 416 | 42 | 449 | cryptic beta-D-galactosidase subunit alpha; Reviewed |
pfam00703 | Glyco_hydro_2 | 3.49e-10 | 186 | 284 | 1 | 106 | Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities. |
pfam17786 | Mannosidase_ig | 1.91e-09 | 638 | 724 | 3 | 90 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BCJ98156.1 | 5.64e-201 | 3 | 822 | 4 | 839 |
AUG59052.1 | 7.53e-198 | 1 | 807 | 1 | 816 |
AVQ95585.1 | 4.29e-185 | 5 | 799 | 6 | 808 |
ADU26456.1 | 4.29e-185 | 5 | 799 | 6 | 808 |
AYF38249.1 | 4.29e-185 | 5 | 799 | 6 | 808 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2VJX_A | 9.01e-154 | 2 | 785 | 8 | 816 | 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 | 9.52e-154 | 2 | 785 | 10 | 818 | 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 | 9.79e-154 | 2 | 785 | 10 | 818 | 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 | 2.58e-153 | 2 | 785 | 8 | 816 | 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 | 1.07e-151 | 2 | 785 | 8 | 816 | 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 |
---|---|---|---|---|---|---|
Q29444 | 1.52e-107 | 4 | 807 | 24 | 877 | Beta-mannosidase OS=Bos taurus OX=9913 GN=MANBA PE=1 SV=1 |
Q5B7W2 | 5.06e-107 | 5 | 785 | 9 | 826 | Beta-mannosidase B OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=mndB PE=1 SV=2 |
Q95327 | 3.14e-104 | 4 | 807 | 24 | 877 | Beta-mannosidase OS=Capra hircus OX=9925 GN=MANBA PE=1 SV=1 |
A2QYN2 | 2.10e-103 | 4 | 785 | 8 | 828 | Beta-mannosidase B OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=mndB PE=3 SV=1 |
Q0CCA0 | 7.74e-103 | 3 | 785 | 7 | 826 | Beta-mannosidase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=mndB PE=3 SV=2 |
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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