| Species | Parabacteroides sp000436495 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides sp000436495 | |||||||||||
| CAZyme ID | MGYG000002218_00369 | |||||||||||
| CAZy Family | GH29 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 189334; End: 190881 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH29 | 35 | 385 | 4e-117 | 0.930635838150289 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| smart00812 | Alpha_L_fucos | 2.16e-144 | 33 | 443 | 1 | 384 | 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 | 3.84e-131 | 36 | 381 | 3 | 333 | Alpha-L-fucosidase. |
| COG3669 | AfuC | 9.57e-112 | 66 | 474 | 1 | 416 | Alpha-L-fucosidase [Carbohydrate transport and metabolism]. |
| pfam16757 | Fucosidase_C | 1.19e-16 | 416 | 493 | 8 | 90 | 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 | 4.21e-273 | 1 | 513 | 1 | 512 |
| QUT88749.1 | 2.43e-272 | 1 | 513 | 1 | 512 |
| ALJ59513.1 | 8.31e-240 | 3 | 498 | 2 | 498 |
| QUT89444.1 | 2.29e-239 | 1 | 498 | 1 | 497 |
| EDY95436.1 | 5.01e-218 | 3 | 508 | 7 | 519 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 7LJJ_A | 1.21e-215 | 29 | 508 | 33 | 521 | ChainA, Exo-alpha-L-galactosidase [Phocaeicola plebeius DSM 17135],7LK7_A Chain A, Exo-alpha-L-galactosidase [Phocaeicola plebeius DSM 17135] |
| 7LNP_A | 6.94e-215 | 29 | 508 | 33 | 521 | 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 | 2.89e-90 | 34 | 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 | 3.11e-69 | 39 | 481 | 8 | 433 | 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 | 3.63e-69 | 39 | 481 | 8 | 433 | 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 |
|---|---|---|---|---|---|---|
| P04066 | 2.22e-65 | 53 | 493 | 50 | 463 | Tissue alpha-L-fucosidase OS=Homo sapiens OX=9606 GN=FUCA1 PE=1 SV=4 |
| P17164 | 2.82e-65 | 53 | 493 | 46 | 459 | Tissue alpha-L-fucosidase OS=Rattus norvegicus OX=10116 GN=Fuca1 PE=1 SV=1 |
| Q99LJ1 | 1.18e-64 | 39 | 493 | 23 | 449 | Tissue alpha-L-fucosidase OS=Mus musculus OX=10090 GN=Fuca1 PE=1 SV=1 |
| Q60HF8 | 1.75e-64 | 53 | 493 | 52 | 465 | Tissue alpha-L-fucosidase OS=Macaca fascicularis OX=9541 GN=FUCA1 PE=2 SV=1 |
| Q2KIM0 | 9.40e-64 | 53 | 493 | 53 | 465 | Tissue alpha-L-fucosidase OS=Bos taurus OX=9913 GN=FUCA1 PE=2 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000000 | 0.000005 | 1.000030 | 0.000000 | 0.000000 | 0.000000 |
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