Species | ||||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; Christensenellaceae; ; | |||||||||||
CAZyme ID | MGYG000001822_00965 | |||||||||||
CAZy Family | GH4 | |||||||||||
CAZyme Description | Alpha-galactosidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 6350; End: 7825 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH4 | 7 | 185 | 3e-56 | 0.9832402234636871 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
PRK15076 | PRK15076 | 1.29e-155 | 6 | 450 | 2 | 431 | alpha-galactosidase; Provisional |
cd05297 | GH4_alpha_glucosidase_galactosidase | 3.77e-135 | 6 | 439 | 1 | 423 | Glycoside Hydrolases Family 4; Alpha-glucosidases and alpha-galactosidases. linked to 3D####ucture |
COG1486 | CelF | 3.58e-119 | 5 | 450 | 3 | 440 | Alpha-galactosidase/6-phospho-beta-glucosidase, family 4 of glycosyl hydrolase [Carbohydrate transport and metabolism]. |
cd05296 | GH4_P_beta_glucosidase | 5.85e-59 | 7 | 446 | 2 | 419 | Glycoside Hydrolases Family 4; Phospho-beta-glucosidase. Some bacteria simultaneously translocate and phosphorylate disaccharides via the phosphoenolpyruvate-dependent phosphotransferase system (PEP-PTS). After translocation, these phospho-disaccharides may be hydrolyzed by the GH4 glycoside hydrolases such as the phospho-beta-glucosidases. Other organisms (such as archaea and Thermotoga maritima ) lack the PEP-PTS system, but have several enzymes normally associated with the PEP-PTS operon. The 6-phospho-beta-glucosidase from Thermotoga maritima hydrolylzes cellobiose 6-phosphate (6P) into glucose-6P and glucose, in an NAD+ and Mn2+ dependent fashion. The Escherichia coli 6-phospho-beta-glucosidase (also called celF) hydrolyzes a variety of phospho-beta-glucosides including cellobiose-6P, salicin-6P, arbutin-6P, and gentobiose-6P. Phospho-beta-glucosidases are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others. |
cd05197 | GH4_glycoside_hydrolases | 5.17e-54 | 6 | 441 | 1 | 425 | Glycoside Hydrases Family 4. Glycoside hydrolases cleave glycosidic bonds to release smaller sugars from oligo- or polysaccharides. Some bacteria simultaneously translocate and phosphorylate disaccharides via the phosphoenolpyruvate-dependent phosphotransferase system (PEP-PTS). After translocation, these phospho-disaccharides may be hydrolyzed by GH4 glycoside hydrolases. Other organisms (such as archaea and Thermotoga maritima) lack the PEP-PTS system, but have several enzymes normally associated with the PEP-PTS operon. GH4 family members include 6-phospho-beta-glucosidases, 6-phospho-alpha-glucosidases, alpha-glucosidases/alpha-glucuronidases (only from Thermotoga), and alpha-galactosidases. They require two cofactors, NAD+ and a divalent metal (Mn2+, Ni2+, Mg2+), for activity. Some also require reducing conditions. GH4 glycoside hydrolases are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AYH41389.1 | 4.24e-297 | 1 | 491 | 1 | 486 |
AGA57655.1 | 1.26e-164 | 6 | 483 | 3 | 473 |
ALS29172.1 | 5.37e-160 | 6 | 483 | 3 | 469 |
QTL97026.1 | 2.51e-159 | 6 | 483 | 3 | 471 |
AZN39733.1 | 1.12e-158 | 6 | 483 | 3 | 470 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1UP7_A | 3.27e-26 | 7 | 446 | 4 | 414 | Structureof the 6-phospho-beta glucosidase from Thermotoga maritima at 2.4 Angstrom resolution in the tetragonal form with NAD and glucose-6-phosphate [Thermotoga maritima MSB8],1UP7_B Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.4 Angstrom resolution in the tetragonal form with NAD and glucose-6-phosphate [Thermotoga maritima MSB8],1UP7_C Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.4 Angstrom resolution in the tetragonal form with NAD and glucose-6-phosphate [Thermotoga maritima MSB8],1UP7_D Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.4 Angstrom resolution in the tetragonal form with NAD and glucose-6-phosphate [Thermotoga maritima MSB8],1UP7_E Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.4 Angstrom resolution in the tetragonal form with NAD and glucose-6-phosphate [Thermotoga maritima MSB8],1UP7_F Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.4 Angstrom resolution in the tetragonal form with NAD and glucose-6-phosphate [Thermotoga maritima MSB8],1UP7_G Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.4 Angstrom resolution in the tetragonal form with NAD and glucose-6-phosphate [Thermotoga maritima MSB8],1UP7_H Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.4 Angstrom resolution in the tetragonal form with NAD and glucose-6-phosphate [Thermotoga maritima MSB8] |
1UP4_A | 4.34e-26 | 7 | 446 | 2 | 412 | Structureof the 6-phospho-beta glucosidase from Thermotoga maritima at 2.85 Angstrom resolution in the monoclinic form [Thermotoga maritima MSB8],1UP4_B Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.85 Angstrom resolution in the monoclinic form [Thermotoga maritima MSB8],1UP4_C Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.85 Angstrom resolution in the monoclinic form [Thermotoga maritima MSB8],1UP4_D Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.85 Angstrom resolution in the monoclinic form [Thermotoga maritima MSB8],1UP4_E Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.85 Angstrom resolution in the monoclinic form [Thermotoga maritima MSB8],1UP4_F Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.85 Angstrom resolution in the monoclinic form [Thermotoga maritima MSB8],1UP4_G Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.85 Angstrom resolution in the monoclinic form [Thermotoga maritima MSB8],1UP4_H Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.85 Angstrom resolution in the monoclinic form [Thermotoga maritima MSB8] |
1UP6_A | 4.39e-26 | 7 | 446 | 3 | 413 | Structureof the 6-phospho-beta glucosidase from Thermotoga maritima at 2.55 Angstrom resolution in the tetragonal form with manganese, NAD+ and glucose-6-phosphate [Thermotoga maritima MSB8],1UP6_B Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.55 Angstrom resolution in the tetragonal form with manganese, NAD+ and glucose-6-phosphate [Thermotoga maritima MSB8],1UP6_C Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.55 Angstrom resolution in the tetragonal form with manganese, NAD+ and glucose-6-phosphate [Thermotoga maritima MSB8],1UP6_D Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.55 Angstrom resolution in the tetragonal form with manganese, NAD+ and glucose-6-phosphate [Thermotoga maritima MSB8],1UP6_E Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.55 Angstrom resolution in the tetragonal form with manganese, NAD+ and glucose-6-phosphate [Thermotoga maritima MSB8],1UP6_F Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.55 Angstrom resolution in the tetragonal form with manganese, NAD+ and glucose-6-phosphate [Thermotoga maritima MSB8],1UP6_G Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.55 Angstrom resolution in the tetragonal form with manganese, NAD+ and glucose-6-phosphate [Thermotoga maritima MSB8],1UP6_H Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.55 Angstrom resolution in the tetragonal form with manganese, NAD+ and glucose-6-phosphate [Thermotoga maritima MSB8] |
3FEF_A | 4.31e-24 | 7 | 439 | 7 | 436 | Crystalstructure of putative glucosidase lplD from bacillus subtilis [Bacillus subtilis],3FEF_B Crystal structure of putative glucosidase lplD from bacillus subtilis [Bacillus subtilis],3FEF_C Crystal structure of putative glucosidase lplD from bacillus subtilis [Bacillus subtilis],3FEF_D Crystal structure of putative glucosidase lplD from bacillus subtilis [Bacillus subtilis] |
7BR4_A | 1.94e-22 | 7 | 375 | 14 | 404 | ChainA, Alpha-glucosidase, putative [Thermotoga maritima MSB8] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q9X4Y0 | 5.68e-134 | 6 | 483 | 4 | 470 | Alpha-galactosidase OS=Rhizobium meliloti (strain 1021) OX=266834 GN=melA PE=3 SV=1 |
O34645 | 6.57e-62 | 7 | 450 | 3 | 432 | Alpha-galactosidase OS=Bacillus subtilis (strain 168) OX=224308 GN=melA PE=1 SV=1 |
P06720 | 1.76e-57 | 7 | 447 | 6 | 446 | Alpha-galactosidase OS=Escherichia coli (strain K12) OX=83333 GN=melA PE=1 SV=1 |
P30877 | 5.27e-54 | 7 | 447 | 6 | 446 | Alpha-galactosidase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=melA PE=3 SV=2 |
Q9AI65 | 5.81e-44 | 7 | 450 | 4 | 453 | Alpha-glucosidase OS=Erwinia rhapontici OX=55212 GN=palH PE=1 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000075 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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