Species | Enorma sp900751795 | |||||||||||
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Lineage | Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Enorma; Enorma sp900751795 | |||||||||||
CAZyme ID | MGYG000004584_00430 | |||||||||||
CAZy Family | GH4 | |||||||||||
CAZyme Description | Phospho-alpha-glucosidase PagL | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 5449; End: 6855 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH4 | 6 | 176 | 1.4e-59 | 0.9441340782122905 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd05298 | GH4_GlvA_pagL_like | 0.0 | 4 | 467 | 1 | 436 | Glycoside Hydrolases Family 4; GlvA- and pagL-like glycosidases. Bacillus subtilis GlvA and Clostridium acetobutylicum pagL are 6-phospho-alpha-glucosidase, catalyzing the hydrolysis of alpha-glucopyranoside bonds to release glucose from oligosaccharides. The substrate specificities of other members of this subgroup are unknown. 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, which include 6-phospho-beta-glucosidases, 6-phospho-alpha-glucosidases, alpha-glucosidases/alpha-glucuronidases (only from Thermotoga), and alpha-galactosidases. Members of this subfamily 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. |
COG1486 | CelF | 5.50e-119 | 1 | 467 | 1 | 439 | Alpha-galactosidase/6-phospho-beta-glucosidase, family 4 of glycosyl hydrolase [Carbohydrate transport and metabolism]. |
cd05197 | GH4_glycoside_hydrolases | 8.58e-92 | 5 | 455 | 2 | 421 | 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. |
cd05296 | GH4_P_beta_glucosidase | 2.82e-90 | 1 | 460 | 1 | 415 | 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. |
pfam02056 | Glyco_hydro_4 | 1.97e-50 | 5 | 173 | 1 | 170 | Family 4 glycosyl hydrolase. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QSI24033.1 | 6.13e-207 | 1 | 467 | 1 | 465 |
QUO20878.1 | 2.47e-184 | 2 | 468 | 3 | 468 |
AGF59376.1 | 7.57e-158 | 1 | 466 | 1 | 443 |
AIU02399.1 | 2.16e-157 | 1 | 466 | 1 | 443 |
QUN35145.1 | 2.16e-157 | 1 | 466 | 1 | 443 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6VC6_A | 2.60e-130 | 2 | 466 | 2 | 439 | 2.1Angstrom Resolution Crystal Structure of 6-phospho-alpha-glucosidase from Gut Microorganisms in Complex with NAD and Mn2+ [Merdibacter massiliensis],6VC6_B 2.1 Angstrom Resolution Crystal Structure of 6-phospho-alpha-glucosidase from Gut Microorganisms in Complex with NAD and Mn2+ [Merdibacter massiliensis],6VC6_C 2.1 Angstrom Resolution Crystal Structure of 6-phospho-alpha-glucosidase from Gut Microorganisms in Complex with NAD and Mn2+ [Merdibacter massiliensis],6VC6_D 2.1 Angstrom Resolution Crystal Structure of 6-phospho-alpha-glucosidase from Gut Microorganisms in Complex with NAD and Mn2+ [Merdibacter massiliensis] |
6DUX_A | 3.31e-112 | 2 | 466 | 5 | 441 | ChainA, 6-phospho-alpha-glucosidase [Klebsiella pneumoniae],6DUX_B Chain B, 6-phospho-alpha-glucosidase [Klebsiella pneumoniae],6DVV_A Chain A, 6-phospho-alpha-glucosidase [Klebsiella pneumoniae],6DVV_B Chain B, 6-phospho-alpha-glucosidase [Klebsiella pneumoniae] |
1U8X_X | 1.29e-110 | 2 | 466 | 27 | 463 | CrystalStructure Of Glva From Bacillus Subtilis, A Metal-requiring, Nad-dependent 6-phospho-alpha-glucosidase [Bacillus subtilis] |
5C3M_A | 4.28e-49 | 2 | 467 | 3 | 437 | Crystalstructure of Gan4C, a GH4 6-phospho-glucosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5C3M_B Crystal structure of Gan4C, a GH4 6-phospho-glucosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5C3M_C Crystal structure of Gan4C, a GH4 6-phospho-glucosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5C3M_D Crystal structure of Gan4C, a GH4 6-phospho-glucosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus] |
1S6Y_A | 4.61e-46 | 2 | 467 | 6 | 440 | 2.3Acrystal structure of phospho-beta-glucosidase [Geobacillus stearothermophilus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q97DP6 | 1.22e-152 | 1 | 466 | 1 | 443 | Phospho-alpha-glucosidase PagL OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=pagL PE=1 SV=1 |
Q9AGA6 | 2.79e-118 | 1 | 466 | 1 | 438 | 6-phospho-alpha-glucosidase OS=Klebsiella pneumoniae OX=573 GN=aglB PE=1 SV=1 |
C7NB67 | 5.59e-118 | 1 | 465 | 1 | 437 | 6-phospho-alpha-glucosidase OS=Leptotrichia buccalis (strain ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b) OX=523794 GN=pagL PE=1 SV=1 |
Q03C44 | 9.54e-117 | 2 | 466 | 4 | 440 | 6-phospho-alpha-glucosidase 1 OS=Lacticaseibacillus paracasei (strain ATCC 334 / BCRC 17002 / CCUG 31169 / CIP 107868 / KCTC 3260 / NRRL B-441) OX=321967 GN=simA PE=1 SV=1 |
O06901 | 3.70e-116 | 1 | 465 | 1 | 438 | Maltose-6'-phosphate glucosidase OS=Fusobacterium mortiferum OX=850 GN=malH PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
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1.000044 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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