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CAZyme Information: MGYG000002123_01806
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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 | UMGS1696 sp900763885 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; CAG-272; UMGS1696; UMGS1696 sp900763885 | |||||||||||
| CAZyme ID | MGYG000002123_01806 | |||||||||||
| CAZy Family | GH4 | |||||||||||
| CAZyme Description | Alpha-galactosidase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 7199; End: 8404 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH4 | 1 | 146 | 2.8e-48 | 0.8044692737430168 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| PRK15076 | PRK15076 | 0.0 | 1 | 400 | 36 | 431 | alpha-galactosidase; Provisional |
| cd05297 | GH4_alpha_glucosidase_galactosidase | 4.02e-163 | 1 | 389 | 35 | 423 | Glycoside Hydrolases Family 4; Alpha-glucosidases and alpha-galactosidases. linked to 3D####ucture |
| COG1486 | CelF | 2.39e-118 | 1 | 400 | 38 | 440 | Alpha-galactosidase/6-phospho-beta-glucosidase, family 4 of glycosyl hydrolase [Carbohydrate transport and metabolism]. |
| cd05296 | GH4_P_beta_glucosidase | 7.33e-63 | 1 | 396 | 35 | 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. |
| pfam11975 | Glyco_hydro_4C | 1.55e-47 | 158 | 372 | 1 | 168 | Family 4 glycosyl hydrolase C-terminal domain. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AUS96821.1 | 2.21e-189 | 1 | 401 | 36 | 438 |
| QHT62813.1 | 2.43e-179 | 1 | 400 | 36 | 436 |
| QHW31407.1 | 2.93e-177 | 1 | 400 | 37 | 439 |
| ANE45532.1 | 1.42e-175 | 1 | 399 | 36 | 436 |
| QHT59435.1 | 5.95e-175 | 1 | 400 | 37 | 439 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5C3M_A | 3.06e-34 | 6 | 399 | 46 | 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 | 1.27e-30 | 6 | 383 | 49 | 427 | 2.3Acrystal structure of phospho-beta-glucosidase [Geobacillus stearothermophilus] |
| 3FEF_A | 1.27e-30 | 16 | 371 | 50 | 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] |
| 6KCX_A | 4.21e-23 | 1 | 389 | 49 | 467 | Crystalstructure of citrate complex of alpha-glucuronidase (TM0752)from Thermotoga maritima [Thermotoga maritima MSB8],7CTD_A Chain A, Alpha-glucosidase, putative [Thermotoga maritima MSB8],7CTL_A Chain A, Alpha-glucosidase, putative [Thermotoga maritima MSB8] |
| 7BR4_A | 1.04e-22 | 1 | 389 | 49 | 466 | ChainA, Alpha-glucosidase, putative [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 |
|---|---|---|---|---|---|---|
| P06720 | 9.08e-86 | 1 | 396 | 39 | 445 | Alpha-galactosidase OS=Escherichia coli (strain K12) OX=83333 GN=melA PE=1 SV=1 |
| O34645 | 1.31e-83 | 2 | 400 | 37 | 432 | Alpha-galactosidase OS=Bacillus subtilis (strain 168) OX=224308 GN=melA PE=1 SV=1 |
| P30877 | 5.45e-81 | 1 | 396 | 39 | 445 | Alpha-galactosidase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=melA PE=3 SV=2 |
| Q9X4Y0 | 4.46e-72 | 2 | 399 | 39 | 442 | Alpha-galactosidase OS=Rhizobium meliloti (strain 1021) OX=266834 GN=melA PE=3 SV=1 |
| I3VRU1 | 1.65e-34 | 27 | 401 | 74 | 463 | 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 |
|---|---|---|---|---|---|
| 1.000062 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |