Species | Eubacterium_R sp900539325 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Eubacterium_R; Eubacterium_R sp900539325 | |||||||||||
CAZyme ID | MGYG000004392_00627 | |||||||||||
CAZy Family | GH2 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 255749; End: 258274 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH2 | 2 | 751 | 1.5e-104 | 0.7805851063829787 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3250 | LacZ | 1.39e-90 | 1 | 629 | 11 | 635 | Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]. |
pfam17753 | Ig_mannosidase | 1.14e-16 | 725 | 802 | 1 | 78 | Ig-fold domain. This Ig-like fold domain is found in mannosidase enzymes. |
PRK10340 | ebgA | 2.62e-13 | 3 | 416 | 42 | 449 | cryptic beta-D-galactosidase subunit alpha; Reviewed |
pfam00703 | Glyco_hydro_2 | 1.41e-11 | 196 | 284 | 26 | 106 | Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities. |
pfam17786 | Mannosidase_ig | 6.64e-09 | 637 | 720 | 3 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BCJ98156.1 | 4.37e-204 | 1 | 826 | 2 | 847 |
AUG59052.1 | 6.97e-184 | 5 | 802 | 5 | 816 |
ADL52891.1 | 3.59e-180 | 5 | 802 | 6 | 817 |
BAV13124.1 | 4.70e-180 | 5 | 802 | 15 | 826 |
BBI32724.1 | 1.44e-177 | 4 | 802 | 5 | 821 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2VJX_A | 4.26e-156 | 9 | 778 | 15 | 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 | 4.51e-156 | 9 | 778 | 17 | 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 | 4.63e-156 | 9 | 778 | 17 | 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 | 1.22e-155 | 9 | 778 | 15 | 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 | 5.08e-154 | 9 | 778 | 15 | 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 | 1.23e-108 | 4 | 653 | 24 | 718 | Beta-mannosidase OS=Capra hircus OX=9925 GN=MANBA PE=1 SV=1 |
Q29444 | 1.71e-108 | 4 | 653 | 24 | 718 | Beta-mannosidase OS=Bos taurus OX=9913 GN=MANBA PE=1 SV=1 |
Q4FZV0 | 2.86e-100 | 4 | 632 | 24 | 698 | Beta-mannosidase OS=Rattus norvegicus OX=10116 GN=Manba PE=2 SV=1 |
O00462 | 7.40e-100 | 4 | 636 | 24 | 702 | Beta-mannosidase OS=Homo sapiens OX=9606 GN=MANBA PE=1 SV=3 |
Q0CCA0 | 9.54e-99 | 9 | 780 | 13 | 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 |
---|---|---|---|---|---|
1.000052 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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