| Species | RUG806 sp900313475 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; RUG806; RUG806 sp900313475 | |||||||||||
| CAZyme ID | MGYG000003484_01452 | |||||||||||
| CAZy Family | GH29 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 54710; End: 56002 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH29 | 3 | 339 | 1.8e-99 | 0.9161849710982659 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| smart00812 | Alpha_L_fucos | 1.02e-148 | 3 | 373 | 7 | 376 | 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 | 3.00e-145 | 3 | 336 | 6 | 333 | Alpha-L-fucosidase. |
| COG3669 | AfuC | 1.22e-52 | 29 | 352 | 1 | 336 | Alpha-L-fucosidase [Carbohydrate transport and metabolism]. |
| pfam16757 | Fucosidase_C | 8.99e-09 | 349 | 429 | 6 | 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 |
|---|---|---|---|---|---|
| AYB30516.1 | 8.74e-158 | 3 | 428 | 22 | 455 |
| QKZ15689.1 | 1.29e-156 | 3 | 428 | 15 | 452 |
| CCH00249.1 | 5.90e-155 | 3 | 428 | 24 | 462 |
| QJD77084.1 | 4.47e-154 | 3 | 428 | 24 | 460 |
| QGY43524.1 | 7.33e-154 | 3 | 428 | 22 | 454 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1ODU_A | 2.96e-82 | 3 | 379 | 8 | 399 | 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 | 3.49e-82 | 3 | 379 | 8 | 399 | 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] |
| 1HL8_A | 5.87e-82 | 3 | 379 | 8 | 399 | CrystalStructure Of Thermotoga Maritima Alpha-Fucosidase [Thermotoga maritima MSB8],1HL8_B Crystal Structure Of Thermotoga Maritima Alpha-Fucosidase [Thermotoga maritima MSB8],1HL9_A Crystal Structure Of Thermotoga Maritima Alpha-Fucosidase In Complex With A Mechanism Based Inhibitor [Thermotoga maritima MSB8],1HL9_B Crystal Structure Of Thermotoga Maritima Alpha-Fucosidase In Complex With A Mechanism Based Inhibitor [Thermotoga maritima MSB8] |
| 2WSP_A | 3.26e-81 | 3 | 379 | 8 | 399 | Thermotogamaritima alpha-L-fucosynthase, TmD224G, in complex with alpha-L-Fuc-(1-2)-beta-L-Fuc-N3 [Thermotoga maritima MSB8],2WSP_B Thermotoga maritima alpha-L-fucosynthase, TmD224G, in complex with alpha-L-Fuc-(1-2)-beta-L-Fuc-N3 [Thermotoga maritima MSB8] |
| 7LJJ_A | 5.15e-52 | 12 | 342 | 53 | 403 | ChainA, Exo-alpha-L-galactosidase [Phocaeicola plebeius DSM 17135],7LK7_A Chain A, Exo-alpha-L-galactosidase [Phocaeicola plebeius DSM 17135] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P10901 | 9.00e-123 | 3 | 429 | 21 | 458 | Alpha-L-fucosidase OS=Dictyostelium discoideum OX=44689 GN=alfA PE=3 SV=1 |
| Q6AYS4 | 5.11e-116 | 1 | 429 | 24 | 456 | Plasma alpha-L-fucosidase OS=Rattus norvegicus OX=10116 GN=Fuca2 PE=2 SV=1 |
| Q99KR8 | 3.08e-115 | 1 | 429 | 26 | 458 | Plasma alpha-L-fucosidase OS=Mus musculus OX=10090 GN=Fuca2 PE=1 SV=1 |
| Q5RFI5 | 4.94e-115 | 3 | 429 | 32 | 462 | Plasma alpha-L-fucosidase OS=Pongo abelii OX=9601 GN=FUCA2 PE=2 SV=1 |
| Q9BTY2 | 2.97e-114 | 3 | 429 | 34 | 464 | Plasma alpha-L-fucosidase OS=Homo sapiens OX=9606 GN=FUCA2 PE=1 SV=2 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000029 | 0.000013 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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