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CAZyme Information: MGYG000002473_00601
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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 | Victivallis vadensis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; Victivallis; Victivallis vadensis | |||||||||||
| CAZyme ID | MGYG000002473_00601 | |||||||||||
| CAZy Family | GH4 | |||||||||||
| CAZyme Description | Alpha-galactosidase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 35775; End: 37106 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH4 | 4 | 183 | 2e-59 | 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 | 4 | 428 | 2 | 423 | Glycoside Hydrolases Family 4; Alpha-glucosidases and alpha-galactosidases. linked to 3D####ucture |
| PRK15076 | PRK15076 | 0.0 | 2 | 435 | 1 | 427 | alpha-galactosidase; Provisional |
| COG1486 | CelF | 2.04e-128 | 1 | 439 | 2 | 440 | Alpha-galactosidase/6-phospho-beta-glucosidase, family 4 of glycosyl hydrolase [Carbohydrate transport and metabolism]. |
| cd05296 | GH4_P_beta_glucosidase | 1.96e-57 | 4 | 435 | 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. |
| pfam02056 | Glyco_hydro_4 | 1.13e-55 | 4 | 182 | 1 | 179 | Family 4 glycosyl hydrolase. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AVM43396.1 | 0.0 | 1 | 442 | 1 | 442 |
| AVM46579.1 | 3.94e-279 | 1 | 443 | 1 | 443 |
| AUS96821.1 | 1.97e-222 | 3 | 438 | 2 | 436 |
| QHT62813.1 | 6.43e-219 | 3 | 438 | 2 | 435 |
| QHT59435.1 | 2.05e-210 | 1 | 438 | 1 | 438 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5C3M_A | 1.18e-38 | 4 | 438 | 6 | 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] |
| 3FEF_A | 1.65e-37 | 4 | 419 | 7 | 429 | 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] |
| 1S6Y_A | 4.11e-36 | 4 | 438 | 9 | 440 | 2.3Acrystal structure of phospho-beta-glucosidase [Geobacillus stearothermophilus] |
| 1OBB_A | 7.51e-25 | 2 | 435 | 3 | 478 | alpha-glucosidaseA, AglA, from Thermotoga maritima in complex with maltose and NAD+ [Thermotoga maritima MSB8],1OBB_B alpha-glucosidase A, AglA, from Thermotoga maritima in complex with maltose and NAD+ [Thermotoga maritima MSB8] |
| 1U8X_X | 1.12e-18 | 2 | 434 | 28 | 460 | CrystalStructure Of Glva From Bacillus Subtilis, A Metal-requiring, Nad-dependent 6-phospho-alpha-glucosidase [Bacillus subtilis] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P06720 | 1.60e-89 | 4 | 439 | 6 | 450 | Alpha-galactosidase OS=Escherichia coli (strain K12) OX=83333 GN=melA PE=1 SV=1 |
| P30877 | 2.50e-88 | 4 | 435 | 6 | 445 | Alpha-galactosidase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=melA PE=3 SV=2 |
| Q9X4Y0 | 6.67e-82 | 2 | 443 | 3 | 448 | Alpha-galactosidase OS=Rhizobium meliloti (strain 1021) OX=266834 GN=melA PE=3 SV=1 |
| O34645 | 1.71e-76 | 3 | 435 | 2 | 428 | Alpha-galactosidase OS=Bacillus subtilis (strain 168) OX=224308 GN=melA PE=1 SV=1 |
| I3VRU1 | 3.77e-47 | 5 | 435 | 13 | 458 | Alpha-galacturonidase OS=Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485) OX=1094508 GN=Tsac_0200 PE=1 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 |
|---|---|---|---|---|---|
| 1.000086 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |