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CAZyme Information: MGYG000002403_05739

You are here: Home > Sequence: MGYG000002403_05739

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Robinsoniella peoriensis
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Robinsoniella; Robinsoniella peoriensis
CAZyme ID MGYG000002403_05739
CAZy Family GH4
CAZyme Description Alpha-galactosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
494 55948.92 4.9209
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002403 7202103 Isolate not provided not provided
Gene Location Start: 160;  End: 1644  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.22

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH4 4 183 1.7e-58 0.9888268156424581

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd05297 GH4_alpha_glucosidase_galactosidase 0.0 3 430 1 423
Glycoside Hydrolases Family 4; Alpha-glucosidases and alpha-galactosidases. linked to 3D####ucture
PRK15076 PRK15076 0.0 2 441 1 431
alpha-galactosidase; Provisional
COG1486 CelF 4.44e-153 1 441 2 440
Alpha-galactosidase/6-phospho-beta-glucosidase, family 4 of glycosyl hydrolase [Carbohydrate transport and metabolism].
cd05296 GH4_P_beta_glucosidase 1.37e-71 4 432 2 414
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 1.48e-69 3 432 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BCJ98706.1 1.85e-267 1 481 1 482
SQI62161.1 1.40e-248 1 490 1 492
ALS29172.1 5.89e-248 1 486 1 488
QNF29664.1 1.13e-245 1 486 1 488
QNK60110.1 1.92e-245 2 486 3 489

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1U8X_X 1.86e-30 2 451 28 471
CrystalStructure Of Glva From Bacillus Subtilis, A Metal-requiring, Nad-dependent 6-phospho-alpha-glucosidase [Bacillus subtilis]
1UP7_A 4.37e-30 4 437 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]
3FEF_A 4.95e-30 4 412 7 420
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]
1UP4_A 5.80e-30 4 437 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 5.88e-30 4 437 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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9X4Y0 3.42e-185 2 485 3 488
Alpha-galactosidase OS=Rhizobium meliloti (strain 1021) OX=266834 GN=melA PE=3 SV=1
O34645 3.40e-77 4 440 3 431
Alpha-galactosidase OS=Bacillus subtilis (strain 168) OX=224308 GN=melA PE=1 SV=1
P06720 1.56e-67 4 438 6 446
Alpha-galactosidase OS=Escherichia coli (strain K12) OX=83333 GN=melA PE=1 SV=1
P30877 1.67e-66 4 438 6 446
Alpha-galactosidase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=melA PE=3 SV=2
P46320 5.09e-46 4 445 6 441
Probable 6-phospho-beta-glucosidase OS=Bacillus subtilis (strain 168) OX=224308 GN=licH PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

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

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002403_05739.