| Species | Bacteroides sp002491635 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp002491635 | |||||||||||
| CAZyme ID | MGYG000000057_03070 | |||||||||||
| CAZy Family | GH29 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 17436; End: 18740 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH29 | 14 | 350 | 3.7e-105 | 0.9450867052023122 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam01120 | Alpha_L_fucos | 2.21e-149 | 20 | 346 | 3 | 333 | Alpha-L-fucosidase. |
| smart00812 | Alpha_L_fucos | 4.54e-118 | 23 | 377 | 7 | 372 | Alpha-L-fucosidase. O-Glycosyl hydrolases (EC 3.2.1.-) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in 'clans'. Family 29 encompasses alpha-L-fucosidases, which is a lysosomal enzyme responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Deficiency of alpha-L-fucosidase results in the lysosomal storage disease fucosidosis. |
| COG3669 | AfuC | 3.90e-40 | 46 | 352 | 1 | 323 | Alpha-L-fucosidase [Carbohydrate transport and metabolism]. |
| pfam14871 | GHL6 | 3.92e-06 | 83 | 205 | 1 | 134 | Hypothetical glycosyl hydrolase 6. GHL6 is a family of hypothetical glycoside hydrolases. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QUT66745.1 | 0.0 | 1 | 434 | 1 | 434 |
| QUT35448.1 | 0.0 | 1 | 434 | 1 | 434 |
| QQA29138.1 | 0.0 | 1 | 434 | 1 | 434 |
| QUT98058.1 | 0.0 | 1 | 434 | 1 | 434 |
| QBJ19300.1 | 0.0 | 1 | 434 | 1 | 434 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6GN6_A | 3.16e-82 | 34 | 433 | 32 | 444 | Alpha-L-fucosidaseisoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus],6GN6_B Alpha-L-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus],6GN6_C Alpha-L-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus],6GN6_D Alpha-L-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus],6GN6_E Alpha-L-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus],6GN6_F Alpha-L-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus] |
| 7DB5_A | 1.03e-52 | 26 | 375 | 27 | 389 | ChainA, Alpha-L-fucosidase [Vibrio sp. EJY3] |
| 6O1J_A | 1.36e-50 | 36 | 334 | 8 | 332 | ChainA, AlfC [Lacticaseibacillus casei],6O1J_B Chain B, AlfC [Lacticaseibacillus casei],6O1J_C Chain C, AlfC [Lacticaseibacillus casei],6O1J_D Chain D, AlfC [Lacticaseibacillus casei],6O1J_E Chain E, AlfC [Lacticaseibacillus casei],6O1J_F Chain F, AlfC [Lacticaseibacillus casei],6O1J_G Chain G, AlfC [Lacticaseibacillus casei],6O1J_H Chain H, AlfC [Lacticaseibacillus casei] |
| 6O18_A | 1.36e-50 | 36 | 334 | 8 | 332 | ChainA, AlfC [Lacticaseibacillus casei],6O18_B Chain B, AlfC [Lacticaseibacillus casei],6O18_C Chain C, AlfC [Lacticaseibacillus casei],6O18_D Chain D, AlfC [Lacticaseibacillus casei],6O1A_A Chain A, AlfC [Lacticaseibacillus casei],6O1A_B Chain B, AlfC [Lacticaseibacillus casei],6O1A_C Chain C, AlfC [Lacticaseibacillus casei],6O1A_D Chain D, AlfC [Lacticaseibacillus casei] |
| 4PCS_A | 4.43e-50 | 23 | 369 | 6 | 368 | Crystalstructure of a bacterial fucosidase with iminosugar (2S,3S,4R,5S)-3,4-dihydroxy-2-[2'-phenyl]ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],4PCS_B Crystal structure of a bacterial fucosidase with iminosugar (2S,3S,4R,5S)-3,4-dihydroxy-2-[2'-phenyl]ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],4PCS_C Crystal structure of a bacterial fucosidase with iminosugar (2S,3S,4R,5S)-3,4-dihydroxy-2-[2'-phenyl]ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],4PCS_D Crystal structure of a bacterial fucosidase with iminosugar (2S,3S,4R,5S)-3,4-dihydroxy-2-[2'-phenyl]ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],4PCT_A Crystal structure of a bacterial fucosidase with iminocyclitol (2S,3S,4R,5S)-3,4-dihydroxy-2-ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],4PCT_B Crystal structure of a bacterial fucosidase with iminocyclitol (2S,3S,4R,5S)-3,4-dihydroxy-2-ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],4PCT_C Crystal structure of a bacterial fucosidase with iminocyclitol (2S,3S,4R,5S)-3,4-dihydroxy-2-ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],4PCT_D Crystal structure of a bacterial fucosidase with iminocyclitol (2S,3S,4R,5S)-3,4-dihydroxy-2-ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q9BTY2 | 1.15e-40 | 23 | 420 | 34 | 448 | Plasma alpha-L-fucosidase OS=Homo sapiens OX=9606 GN=FUCA2 PE=1 SV=2 |
| Q5RFI5 | 4.08e-40 | 23 | 420 | 32 | 446 | Plasma alpha-L-fucosidase OS=Pongo abelii OX=9601 GN=FUCA2 PE=2 SV=1 |
| Q6AYS4 | 3.59e-39 | 5 | 420 | 8 | 440 | Plasma alpha-L-fucosidase OS=Rattus norvegicus OX=10116 GN=Fuca2 PE=2 SV=1 |
| P10901 | 9.81e-39 | 18 | 420 | 16 | 443 | Alpha-L-fucosidase OS=Dictyostelium discoideum OX=44689 GN=alfA PE=3 SV=1 |
| Q99KR8 | 2.59e-38 | 22 | 390 | 27 | 401 | Plasma alpha-L-fucosidase OS=Mus musculus OX=10090 GN=Fuca2 PE=1 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000235 | 0.999147 | 0.000151 | 0.000161 | 0.000143 | 0.000134 |
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