Species | CAG-110 sp900540635 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; CAG-110; CAG-110 sp900540635 | |||||||||||
CAZyme ID | MGYG000002589_00317 | |||||||||||
CAZy Family | GH2 | |||||||||||
CAZyme Description | Exo-beta-D-glucosaminidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 106486; End: 108876 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH2 | 49 | 648 | 4.3e-88 | 0.601063829787234 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3250 | LacZ | 4.45e-86 | 34 | 620 | 47 | 633 | Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]. |
pfam17753 | Ig_mannosidase | 1.15e-17 | 719 | 794 | 1 | 78 | Ig-fold domain. This Ig-like fold domain is found in mannosidase enzymes. |
pfam17786 | Mannosidase_ig | 4.79e-12 | 628 | 714 | 1 | 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. |
pfam00703 | Glyco_hydro_2 | 2.07e-08 | 189 | 275 | 24 | 106 | Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities. |
PRK10340 | ebgA | 7.08e-06 | 55 | 400 | 112 | 441 | cryptic beta-D-galactosidase subunit alpha; Reviewed |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AUS95659.1 | 7.46e-233 | 6 | 796 | 10 | 803 |
QNF27003.1 | 7.89e-226 | 14 | 795 | 19 | 819 |
QTE69834.1 | 2.14e-223 | 5 | 796 | 9 | 811 |
QTE73768.1 | 2.14e-223 | 5 | 796 | 9 | 811 |
AHF25065.1 | 8.30e-223 | 5 | 796 | 9 | 810 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6BYE_A | 2.19e-141 | 16 | 790 | 33 | 848 | Crystalstructure of the GH2 exo-beta-mannanase from Xanthomonas axonopodis pv. citri in complex with mannose [Xanthomonas citri pv. citri str. 306],6BYE_B Crystal structure of the GH2 exo-beta-mannanase from Xanthomonas axonopodis pv. citri in complex with mannose [Xanthomonas citri pv. citri str. 306] |
6BYC_A | 2.24e-141 | 16 | 790 | 33 | 848 | Crystalstructure of the GH2 exo-beta-mannanase from Xanthomonas axonopodis pv. citri [Xanthomonas citri pv. citri str. 306] |
2VJX_A | 8.07e-141 | 4 | 768 | 13 | 810 | 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 | 8.51e-141 | 4 | 768 | 15 | 812 | 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-141 | 4 | 768 | 15 | 812 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
I2C092 | 1.59e-100 | 19 | 772 | 30 | 836 | Beta-mannosidase B OS=Thermothelomyces thermophilus OX=78579 GN=man9 PE=1 SV=1 |
Q0CCA0 | 6.72e-98 | 19 | 773 | 31 | 825 | Beta-mannosidase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=mndB PE=3 SV=2 |
Q5B7W2 | 1.30e-97 | 20 | 639 | 32 | 676 | 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 |
A2QYN2 | 3.67e-95 | 8 | 639 | 21 | 676 | Beta-mannosidase B OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=mndB PE=3 SV=1 |
Q4WAH4 | 1.40e-94 | 11 | 648 | 24 | 698 | 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 |
---|---|---|---|---|---|
1.000047 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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