| Species | Catenibacillus sp900557175 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Catenibacillus; Catenibacillus sp900557175 | |||||||||||
| CAZyme ID | MGYG000001252_00638 | |||||||||||
| CAZy Family | GH2 | |||||||||||
| CAZyme Description | Beta-galactosidase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 4117; End: 6624 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH2 | 3 | 670 | 8.7e-102 | 0.651595744680851 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG3250 | LacZ | 2.22e-106 | 1 | 805 | 10 | 787 | Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]. |
| pfam17753 | Ig_mannosidase | 3.78e-18 | 747 | 829 | 1 | 78 | Ig-fold domain. This Ig-like fold domain is found in mannosidase enzymes. |
| PRK10340 | ebgA | 4.15e-12 | 61 | 381 | 113 | 394 | cryptic beta-D-galactosidase subunit alpha; Reviewed |
| pfam17786 | Mannosidase_ig | 5.75e-09 | 650 | 742 | 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 | 1.16e-08 | 194 | 296 | 3 | 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 |
|---|---|---|---|---|---|
| CBL13897.1 | 3.03e-302 | 2 | 830 | 12 | 855 |
| VCV23589.1 | 5.47e-301 | 2 | 830 | 5 | 848 |
| CBL08662.1 | 5.47e-301 | 2 | 830 | 5 | 848 |
| QCU02115.1 | 1.84e-296 | 1 | 827 | 1 | 824 |
| CBL20579.1 | 1.96e-294 | 1 | 827 | 1 | 838 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6BYE_A | 5.00e-153 | 1 | 800 | 3 | 830 | 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 | 5.14e-153 | 1 | 800 | 3 | 830 | Crystalstructure of the GH2 exo-beta-mannanase from Xanthomonas axonopodis pv. citri [Xanthomonas citri pv. citri str. 306] |
| 6BYI_A | 3.66e-152 | 1 | 800 | 1 | 828 | 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 | 3.77e-152 | 1 | 800 | 3 | 830 | 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 | 1.02e-138 | 10 | 822 | 15 | 838 | 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 |
|---|---|---|---|---|---|---|
| Q95327 | 3.26e-122 | 6 | 830 | 25 | 878 | Beta-mannosidase OS=Capra hircus OX=9925 GN=MANBA PE=1 SV=1 |
| Q29444 | 9.84e-120 | 6 | 830 | 25 | 878 | Beta-mannosidase OS=Bos taurus OX=9913 GN=MANBA PE=1 SV=1 |
| Q4FZV0 | 1.91e-112 | 4 | 800 | 23 | 856 | Beta-mannosidase OS=Rattus norvegicus OX=10116 GN=Manba PE=2 SV=1 |
| Q8K2I4 | 7.41e-110 | 4 | 790 | 23 | 844 | Beta-mannosidase OS=Mus musculus OX=10090 GN=Manba PE=1 SV=1 |
| O00462 | 2.12e-107 | 4 | 790 | 23 | 844 | Beta-mannosidase OS=Homo sapiens OX=9606 GN=MANBA PE=1 SV=3 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000045 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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