Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia_A; | |||||||||||
CAZyme ID | MGYG000001594_00952 | |||||||||||
CAZy Family | GH2 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 7329; End: 9767 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH2 | 3 | 701 | 1.8e-100 | 0.699468085106383 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3250 | LacZ | 1.10e-96 | 5 | 666 | 29 | 681 | Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]. |
PRK10150 | PRK10150 | 1.53e-13 | 75 | 314 | 83 | 296 | beta-D-glucuronidase; Provisional |
PRK10340 | ebgA | 6.15e-11 | 19 | 417 | 70 | 449 | cryptic beta-D-galactosidase subunit alpha; Reviewed |
pfam00703 | Glyco_hydro_2 | 4.16e-10 | 187 | 286 | 2 | 106 | Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities. |
pfam17753 | Ig_mannosidase | 2.24e-09 | 745 | 810 | 1 | 78 | 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 |
---|---|---|---|---|---|
AWY97345.1 | 0.0 | 1 | 812 | 1 | 811 |
ANU78706.2 | 0.0 | 10 | 812 | 40 | 849 |
ASU31771.1 | 0.0 | 10 | 812 | 40 | 849 |
QQQ95478.1 | 0.0 | 12 | 812 | 1 | 808 |
QJU17896.1 | 0.0 | 12 | 812 | 1 | 808 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6BYE_A | 4.24e-147 | 6 | 812 | 8 | 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 | 4.35e-147 | 6 | 812 | 8 | 848 | Crystalstructure of the GH2 exo-beta-mannanase from Xanthomonas axonopodis pv. citri [Xanthomonas citri pv. citri str. 306] |
6BYI_A | 3.10e-146 | 6 | 812 | 6 | 846 | Crystalstructure of the acid-base mutant (E477A) of the GH2 exo-beta-mannanase from Xanthomonas axonopodis pv. citri [Xanthomonas citri pv. citri str. 306],6BYI_B Crystal structure of the acid-base mutant (E477A) of the GH2 exo-beta-mannanase from Xanthomonas axonopodis pv. citri [Xanthomonas citri pv. citri str. 306] |
6BYG_A | 3.19e-146 | 6 | 812 | 8 | 848 | Crystalstructure of the nucleophile mutant (E575A) of the GH2 exo-beta-mannanase from Xanthomonas axonopodis pv. citri [Xanthomonas citri pv. citri str. 306],6BYG_B Crystal structure of the nucleophile mutant (E575A) of the GH2 exo-beta-mannanase from Xanthomonas axonopodis pv. citri [Xanthomonas citri pv. citri str. 306] |
2VJX_A | 3.34e-145 | 6 | 796 | 11 | 816 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q0CCA0 | 5.52e-116 | 23 | 795 | 30 | 826 | Beta-mannosidase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=mndB PE=3 SV=2 |
Q4WAH4 | 6.34e-114 | 6 | 637 | 9 | 663 | Beta-mannosidase B OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=mndB PE=3 SV=1 |
A1CGA8 | 1.73e-113 | 6 | 806 | 9 | 839 | 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 |
B0YBU9 | 2.42e-113 | 6 | 637 | 9 | 663 | Beta-mannosidase B OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=mndB PE=3 SV=1 |
A1D911 | 4.74e-113 | 6 | 637 | 9 | 663 | 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 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000023 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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