Species | ||||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; ; | |||||||||||
CAZyme ID | MGYG000000574_03503 | |||||||||||
CAZy Family | GH2 | |||||||||||
CAZyme Description | Exo-beta-D-glucosaminidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 1; End: 2364 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH2 | 16 | 646 | 2.1e-75 | 0.6303191489361702 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3250 | LacZ | 8.62e-41 | 20 | 609 | 29 | 631 | Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]. |
PRK10340 | ebgA | 4.73e-21 | 55 | 439 | 112 | 473 | cryptic beta-D-galactosidase subunit alpha; Reviewed |
PRK10150 | PRK10150 | 1.65e-10 | 41 | 287 | 53 | 281 | beta-D-glucuronidase; Provisional |
pfam02837 | Glyco_hydro_2_N | 3.35e-06 | 58 | 174 | 66 | 169 | 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. |
pfam00703 | Glyco_hydro_2 | 2.02e-05 | 177 | 282 | 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 |
---|---|---|---|---|---|
QUR45526.1 | 4.88e-178 | 17 | 787 | 84 | 852 |
QUT31548.1 | 9.71e-178 | 17 | 787 | 84 | 852 |
QDH53450.1 | 2.72e-177 | 17 | 787 | 84 | 852 |
SCV07058.1 | 5.42e-177 | 17 | 787 | 84 | 852 |
QRQ54566.1 | 5.42e-177 | 17 | 787 | 84 | 852 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5N6U_A | 3.13e-55 | 23 | 620 | 46 | 673 | 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 | 8.50e-55 | 8 | 775 | 13 | 817 | 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 | 8.65e-55 | 8 | 775 | 15 | 819 | 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 | 8.73e-55 | 8 | 775 | 15 | 819 | 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 | 2.13e-54 | 8 | 775 | 13 | 817 | 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 |
---|---|---|---|---|---|---|
Q29444 | 1.11e-45 | 23 | 610 | 42 | 691 | Beta-mannosidase OS=Bos taurus OX=9913 GN=MANBA PE=1 SV=1 |
O00462 | 3.66e-44 | 25 | 610 | 44 | 691 | Beta-mannosidase OS=Homo sapiens OX=9606 GN=MANBA PE=1 SV=3 |
Q95327 | 3.73e-43 | 23 | 610 | 42 | 691 | Beta-mannosidase OS=Capra hircus OX=9925 GN=MANBA PE=1 SV=1 |
Q5H7P5 | 1.99e-42 | 23 | 651 | 41 | 726 | Mannosylglycoprotein endo-beta-mannosidase OS=Lilium longiflorum OX=4690 GN=EBM PE=1 SV=4 |
Q4FZV0 | 2.85e-42 | 23 | 610 | 42 | 691 | 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 |
---|---|---|---|---|---|
1.000008 | 0.000018 | 0.000008 | 0.000000 | 0.000000 | 0.000000 |
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