Species | Hungatella sp005845265 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Hungatella; Hungatella sp005845265 | |||||||||||
CAZyme ID | MGYG000000150_03296 | |||||||||||
CAZy Family | GH4 | |||||||||||
CAZyme Description | 6-phospho-alpha-glucosidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 44330; End: 45667 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH4 | 8 | 185 | 3.1e-70 | 0.9888268156424581 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd05298 | GH4_GlvA_pagL_like | 0.0 | 6 | 445 | 1 | 437 | 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 | 0.0 | 4 | 445 | 2 | 440 | Alpha-galactosidase/6-phospho-beta-glucosidase, family 4 of glycosyl hydrolase [Carbohydrate transport and metabolism]. |
cd05197 | GH4_glycoside_hydrolases | 1.26e-148 | 6 | 436 | 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. |
cd05296 | GH4_P_beta_glucosidase | 7.26e-122 | 8 | 440 | 3 | 418 | 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 | 4.04e-70 | 7 | 186 | 1 | 182 | Family 4 glycosyl hydrolase. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QOY59816.1 | 1.31e-267 | 3 | 444 | 6 | 446 |
AXU82109.1 | 2.03e-242 | 4 | 444 | 2 | 441 |
AXU30711.1 | 2.89e-242 | 4 | 444 | 2 | 441 |
AXU26852.1 | 2.89e-242 | 4 | 444 | 2 | 441 |
AXU34499.1 | 2.89e-242 | 4 | 444 | 2 | 441 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6DUX_A | 2.90e-213 | 2 | 444 | 3 | 442 | 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 | 1.76e-202 | 3 | 444 | 26 | 464 | CrystalStructure Of Glva From Bacillus Subtilis, A Metal-requiring, Nad-dependent 6-phospho-alpha-glucosidase [Bacillus subtilis] |
6VC6_A | 2.14e-120 | 4 | 445 | 2 | 441 | 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] |
5C3M_A | 1.96e-72 | 4 | 443 | 3 | 436 | 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 | 1.77e-70 | 3 | 443 | 5 | 439 | 2.3Acrystal structure of phospho-beta-glucosidase [Geobacillus stearothermophilus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q97LM4 | 4.09e-224 | 4 | 444 | 2 | 440 | Maltose-6'-phosphate glucosidase MalH OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=malH PE=1 SV=1 |
Q9AGA6 | 1.60e-223 | 4 | 444 | 2 | 439 | 6-phospho-alpha-glucosidase OS=Klebsiella pneumoniae OX=573 GN=aglB PE=1 SV=1 |
O06901 | 7.41e-220 | 4 | 445 | 2 | 441 | Maltose-6'-phosphate glucosidase OS=Fusobacterium mortiferum OX=850 GN=malH PE=1 SV=1 |
C7NB67 | 2.37e-218 | 4 | 445 | 2 | 440 | 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 |
P54716 | 7.27e-215 | 1 | 444 | 1 | 441 | Maltose-6'-phosphate glucosidase OS=Bacillus subtilis (strain 168) OX=224308 GN=glvA PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000086 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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