| Species | Parabacteroides sp003480915 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides sp003480915 | |||||||||||
| CAZyme ID | MGYG000003701_04206 | |||||||||||
| CAZy Family | GH29 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 164950; End: 166500 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH29 | 36 | 385 | 6.4e-115 | 0.930635838150289 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| smart00812 | Alpha_L_fucos | 1.49e-138 | 34 | 440 | 1 | 380 | 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. |
| pfam01120 | Alpha_L_fucos | 2.85e-128 | 37 | 381 | 3 | 333 | Alpha-L-fucosidase. |
| COG3669 | AfuC | 9.55e-106 | 67 | 475 | 1 | 417 | Alpha-L-fucosidase [Carbohydrate transport and metabolism]. |
| pfam16757 | Fucosidase_C | 6.35e-15 | 416 | 492 | 8 | 89 | Alpha-L-fucosidase C-terminal domain. The C-terminal domain of Structure 1hl8 is constructed of eight anti-parallel-strands packed into two-sheets of five and three strands, respectively, forming a two-layer-sandwich containing a Greek key motif. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| ALJ60258.1 | 4.16e-292 | 1 | 514 | 1 | 513 |
| QUT88749.1 | 2.40e-291 | 1 | 514 | 1 | 513 |
| ALJ59513.1 | 6.47e-247 | 3 | 495 | 2 | 495 |
| QUT89444.1 | 1.02e-245 | 3 | 495 | 2 | 494 |
| EDY95436.1 | 1.40e-210 | 11 | 492 | 14 | 506 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 7LJJ_A | 1.46e-209 | 23 | 492 | 26 | 508 | ChainA, Exo-alpha-L-galactosidase [Phocaeicola plebeius DSM 17135],7LK7_A Chain A, Exo-alpha-L-galactosidase [Phocaeicola plebeius DSM 17135] |
| 7LNP_A | 8.34e-209 | 23 | 492 | 26 | 508 | ChainA, Exo-alpha-L-galactosidase [Phocaeicola plebeius DSM 17135],7LNP_C Chain C, Exo-alpha-L-galactosidase [Phocaeicola plebeius DSM 17135],7LNP_D Chain D, Exo-alpha-L-galactosidase [Phocaeicola plebeius DSM 17135],7LNP_E Chain E, Exo-alpha-L-galactosidase [Phocaeicola plebeius DSM 17135] |
| 4NI3_A | 9.91e-92 | 35 | 495 | 2 | 492 | ChainA, Alpha-fucosidase GH29 [Fusarium graminearum],4NI3_B Chain B, Alpha-fucosidase GH29 [Fusarium graminearum],4PSP_A Chain A, Alpha-fucosidase GH29 [Fusarium graminearum],4PSP_B Chain B, Alpha-fucosidase GH29 [Fusarium graminearum],4PSR_A Chain A, Alpha-fucosidase GH29 [Fusarium graminearum],4PSR_B Chain B, Alpha-fucosidase GH29 [Fusarium graminearum] |
| 1ODU_A | 1.23e-68 | 40 | 479 | 8 | 431 | CrystalStructure Of Thermotoga Maritima Alpha-Fucosidase In Complex With Fucose [Thermotoga maritima MSB8],1ODU_B Crystal Structure Of Thermotoga Maritima Alpha-Fucosidase In Complex With Fucose [Thermotoga maritima MSB8] |
| 2ZWY_A | 1.44e-68 | 40 | 479 | 8 | 431 | alpha-L-fucosidase[Thermotoga maritima],2ZWY_B alpha-L-fucosidase [Thermotoga maritima],2ZWZ_A alpha-L-fucosidase complexed with inhibitor, Core1 [Thermotoga maritima],2ZWZ_B alpha-L-fucosidase complexed with inhibitor, Core1 [Thermotoga maritima],2ZX5_A alpha-L-fucosidase complexed with inhibitor, F10 [Thermotoga maritima],2ZX5_B alpha-L-fucosidase complexed with inhibitor, F10 [Thermotoga maritima],2ZX6_A alpha-L-fucosidase complexed with inhibitor, F10-1C [Thermotoga maritima],2ZX6_B alpha-L-fucosidase complexed with inhibitor, F10-1C [Thermotoga maritima],2ZX7_A alpha-L-fucosidase complexed with inhibitor, F10-2C [Thermotoga maritima],2ZX7_B alpha-L-fucosidase complexed with inhibitor, F10-2C [Thermotoga maritima],2ZX8_A alpha-L-fucosidase complexed with inhibitor, F10-2C-O [Thermotoga maritima],2ZX8_B alpha-L-fucosidase complexed with inhibitor, F10-2C-O [Thermotoga maritima],2ZX9_A alpha-L-fucosidase complexed with inhibitor, B4 [Thermotoga maritima],2ZX9_B alpha-L-fucosidase complexed with inhibitor, B4 [Thermotoga maritima],2ZXA_A alpha-L-fucosidase complexed with inhibitor, FNJ-acetyl [Thermotoga maritima],2ZXA_B alpha-L-fucosidase complexed with inhibitor, FNJ-acetyl [Thermotoga maritima],2ZXB_A alpha-L-fucosidase complexed with inhibitor, ph-6FNJ [Thermotoga maritima],2ZXB_B alpha-L-fucosidase complexed with inhibitor, ph-6FNJ [Thermotoga maritima],2ZXD_A alpha-L-fucosidase complexed with inhibitor, iso-6FNJ [Thermotoga maritima],2ZXD_B alpha-L-fucosidase complexed with inhibitor, iso-6FNJ [Thermotoga maritima] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q9BTY2 | 8.49e-66 | 40 | 493 | 34 | 464 | Plasma alpha-L-fucosidase OS=Homo sapiens OX=9606 GN=FUCA2 PE=1 SV=2 |
| Q5RFI5 | 2.34e-64 | 40 | 493 | 32 | 462 | Plasma alpha-L-fucosidase OS=Pongo abelii OX=9601 GN=FUCA2 PE=2 SV=1 |
| Q99LJ1 | 6.85e-63 | 40 | 493 | 23 | 449 | Tissue alpha-L-fucosidase OS=Mus musculus OX=10090 GN=Fuca1 PE=1 SV=1 |
| P17164 | 1.22e-62 | 40 | 493 | 33 | 459 | Tissue alpha-L-fucosidase OS=Rattus norvegicus OX=10116 GN=Fuca1 PE=1 SV=1 |
| P04066 | 7.19e-62 | 40 | 493 | 37 | 463 | Tissue alpha-L-fucosidase OS=Homo sapiens OX=9606 GN=FUCA1 PE=1 SV=4 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000360 | 0.352183 | 0.646989 | 0.000176 | 0.000146 | 0.000130 |
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