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CAZyme Information: MGYG000002984_00244
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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 | UBA737 sp900554525 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UBA737; UBA737 sp900554525 | |||||||||||
| CAZyme ID | MGYG000002984_00244 | |||||||||||
| CAZy Family | GH4 | |||||||||||
| CAZyme Description | Alpha-galacturonidase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 7191; End: 8582 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH4 | 12 | 191 | 7.8e-55 | 0.9832402234636871 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd05297 | GH4_alpha_glucosidase_galactosidase | 8.61e-150 | 11 | 451 | 1 | 423 | Glycoside Hydrolases Family 4; Alpha-glucosidases and alpha-galactosidases. linked to 3D####ucture |
| COG1486 | CelF | 1.22e-96 | 8 | 458 | 1 | 436 | Alpha-galactosidase/6-phospho-beta-glucosidase, family 4 of glycosyl hydrolase [Carbohydrate transport and metabolism]. |
| PRK15076 | PRK15076 | 1.16e-62 | 12 | 462 | 3 | 431 | alpha-galactosidase; Provisional |
| pfam02056 | Glyco_hydro_4 | 1.32e-55 | 12 | 187 | 1 | 175 | Family 4 glycosyl hydrolase. |
| cd05296 | GH4_P_beta_glucosidase | 4.67e-47 | 11 | 458 | 1 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| ADZ85649.1 | 3.18e-223 | 1 | 458 | 1 | 458 |
| QEH67112.1 | 5.23e-222 | 1 | 458 | 1 | 458 |
| AFK85236.1 | 6.51e-221 | 1 | 463 | 1 | 463 |
| SNX53414.1 | 2.46e-220 | 1 | 463 | 1 | 463 |
| ADL69889.1 | 1.24e-218 | 1 | 463 | 1 | 463 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3FEF_A | 5.14e-167 | 7 | 452 | 2 | 437 | 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] |
| 5C3M_A | 2.87e-25 | 11 | 461 | 5 | 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 | 3.33e-24 | 11 | 461 | 8 | 440 | 2.3Acrystal structure of phospho-beta-glucosidase [Geobacillus stearothermophilus] |
| 1OBB_A | 3.67e-22 | 11 | 451 | 4 | 465 | 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 | 9.01e-21 | 43 | 248 | 62 | 268 | 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 |
|---|---|---|---|---|---|---|
| I3VRU1 | 1.30e-221 | 1 | 463 | 1 | 463 | Alpha-galacturonidase OS=Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485) OX=1094508 GN=Tsac_0200 PE=1 SV=1 |
| D3T426 | 1.28e-187 | 1 | 458 | 1 | 450 | Alpha-galacturonidase OS=Thermoanaerobacter italicus (strain DSM 9252 / Ab9) OX=580331 GN=Thit_1733 PE=1 SV=1 |
| A9KTB9 | 3.16e-179 | 1 | 458 | 1 | 460 | Alpha-galacturonidase OS=Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) OX=357809 GN=Cphy_3396 PE=1 SV=1 |
| P39130 | 2.81e-170 | 11 | 452 | 10 | 441 | Alpha-galacturonidase OS=Bacillus subtilis (strain 168) OX=224308 GN=lplD PE=1 SV=2 |
| O34645 | 7.54e-39 | 12 | 434 | 3 | 402 | Alpha-galactosidase OS=Bacillus subtilis (strain 168) OX=224308 GN=melA 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 |
|---|---|---|---|---|---|
| 1.000080 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |