Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; UBA3282; | |||||||||||
CAZyme ID | MGYG000002256_01503 | |||||||||||
CAZy Family | GH2 | |||||||||||
CAZyme Description | Exo-beta-D-glucosaminidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 9467; End: 11926 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH2 | 3 | 684 | 3e-103 | 0.6768617021276596 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3250 | LacZ | 4.00e-93 | 3 | 799 | 14 | 792 | Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]. |
pfam17753 | Ig_mannosidase | 3.37e-19 | 736 | 815 | 1 | 77 | Ig-fold domain. This Ig-like fold domain is found in mannosidase enzymes. |
PRK10340 | ebgA | 2.04e-14 | 6 | 420 | 78 | 449 | cryptic beta-D-galactosidase subunit alpha; Reviewed |
pfam00703 | Glyco_hydro_2 | 1.15e-11 | 185 | 289 | 1 | 106 | Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities. |
pfam17786 | Mannosidase_ig | 1.37e-05 | 643 | 730 | 1 | 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 |
---|---|---|---|---|---|
ADZ84812.1 | 9.33e-297 | 4 | 817 | 6 | 821 |
QEH70285.1 | 1.32e-296 | 4 | 817 | 6 | 821 |
AUG59052.1 | 7.24e-260 | 1 | 813 | 2 | 813 |
ADU28568.1 | 1.15e-255 | 4 | 816 | 6 | 817 |
QUI24168.1 | 6.43e-254 | 4 | 817 | 6 | 822 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2VJX_A | 6.30e-152 | 4 | 795 | 11 | 820 | 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 | 6.66e-152 | 4 | 795 | 13 | 822 | 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 | 6.84e-152 | 4 | 795 | 13 | 822 | 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 | 1.80e-151 | 4 | 795 | 11 | 820 | 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 | 7.48e-150 | 4 | 795 | 11 | 820 | 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 |
---|---|---|---|---|---|---|
Q0CCA0 | 1.66e-109 | 9 | 798 | 17 | 833 | Beta-mannosidase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=mndB PE=3 SV=2 |
Q95327 | 5.16e-109 | 4 | 789 | 25 | 853 | Beta-mannosidase OS=Capra hircus OX=9925 GN=MANBA PE=1 SV=1 |
Q29444 | 5.16e-109 | 4 | 789 | 25 | 853 | Beta-mannosidase OS=Bos taurus OX=9913 GN=MANBA PE=1 SV=1 |
A1D911 | 4.88e-108 | 2 | 631 | 7 | 655 | Beta-mannosidase B OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=mndB PE=3 SV=1 |
Q4WAH4 | 7.04e-107 | 2 | 631 | 7 | 655 | Beta-mannosidase B OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=mndB PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000057 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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