Species | CAG-1435 sp003537755 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-314; CAG-1435; CAG-1435 sp003537755 | |||||||||||
CAZyme ID | MGYG000003504_01339 | |||||||||||
CAZy Family | GH2 | |||||||||||
CAZyme Description | Exo-beta-D-glucosaminidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 225767; End: 228238 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH2 | 4 | 729 | 3.2e-91 | 0.699468085106383 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3250 | LacZ | 1.12e-52 | 1 | 722 | 10 | 705 | Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]. |
PRK10340 | ebgA | 8.18e-15 | 30 | 437 | 92 | 449 | cryptic beta-D-galactosidase subunit alpha; Reviewed |
pfam00703 | Glyco_hydro_2 | 1.87e-09 | 225 | 304 | 30 | 106 | Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities. |
PRK10150 | PRK10150 | 4.21e-09 | 55 | 469 | 61 | 444 | beta-D-glucuronidase; Provisional |
pfam17753 | Ig_mannosidase | 2.98e-06 | 750 | 814 | 5 | 68 | Ig-fold domain. This Ig-like fold domain is found in mannosidase enzymes. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QHI68839.1 | 2.86e-177 | 9 | 821 | 18 | 829 |
AQQ71581.1 | 2.98e-168 | 19 | 802 | 38 | 814 |
AKJ63700.1 | 7.62e-134 | 15 | 815 | 24 | 834 |
ACK43074.1 | 1.27e-115 | 1 | 688 | 1 | 670 |
ACI19676.1 | 3.65e-114 | 1 | 724 | 1 | 703 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5N6U_A | 4.73e-114 | 1 | 724 | 24 | 726 | 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 | 6.29e-101 | 6 | 700 | 11 | 704 | 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 | 6.56e-101 | 6 | 700 | 13 | 706 | 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 | 6.70e-101 | 6 | 700 | 13 | 706 | 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 | 1.73e-100 | 6 | 700 | 11 | 704 | 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 |
---|---|---|---|---|---|---|
I2C092 | 5.19e-84 | 15 | 808 | 22 | 844 | Beta-mannosidase B OS=Thermothelomyces thermophilus OX=78579 GN=man9 PE=1 SV=1 |
Q95327 | 3.47e-80 | 18 | 651 | 39 | 692 | Beta-mannosidase OS=Capra hircus OX=9925 GN=MANBA PE=1 SV=1 |
Q29444 | 6.26e-79 | 18 | 651 | 39 | 692 | Beta-mannosidase OS=Bos taurus OX=9913 GN=MANBA PE=1 SV=1 |
A1CGA8 | 5.48e-75 | 6 | 652 | 9 | 658 | Beta-mannosidase B OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=mndB PE=3 SV=1 |
Q8K2I4 | 9.18e-75 | 18 | 658 | 39 | 699 | 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 |
---|---|---|---|---|---|
1.000058 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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