| Species | Bacteroides caccae | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides caccae | |||||||||||
| CAZyme ID | MGYG000002549_02064 | |||||||||||
| CAZy Family | GH29 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 88293; End: 89768 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH29 | 14 | 367 | 9.5e-108 | 0.9421965317919075 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| smart00812 | Alpha_L_fucos | 4.21e-155 | 17 | 439 | 2 | 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 | 5.33e-146 | 19 | 363 | 3 | 333 | Alpha-L-fucosidase. |
| COG3669 | AfuC | 5.58e-60 | 48 | 402 | 1 | 359 | Alpha-L-fucosidase [Carbohydrate transport and metabolism]. |
| pfam16757 | Fucosidase_C | 1.37e-16 | 413 | 488 | 9 | 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 |
|---|---|---|---|---|---|
| ASM66891.1 | 0.0 | 1 | 491 | 1 | 491 |
| QUU09433.1 | 0.0 | 1 | 491 | 1 | 491 |
| QQT79872.1 | 0.0 | 17 | 491 | 1 | 475 |
| QRP59676.1 | 0.0 | 17 | 491 | 1 | 475 |
| QRM70622.1 | 0.0 | 1 | 490 | 1 | 490 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1ODU_A | 2.87e-87 | 22 | 471 | 8 | 432 | 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 | 3.40e-87 | 22 | 471 | 8 | 432 | 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 | 5.69e-87 | 22 | 471 | 8 | 432 | 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 | 2.24e-86 | 22 | 471 | 8 | 432 | 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 | 4.59e-57 | 13 | 491 | 34 | 514 | 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 |
|---|---|---|---|---|---|---|
| P04066 | 5.23e-123 | 20 | 490 | 35 | 465 | Tissue alpha-L-fucosidase OS=Homo sapiens OX=9606 GN=FUCA1 PE=1 SV=4 |
| Q2KIM0 | 1.42e-120 | 22 | 490 | 40 | 467 | Tissue alpha-L-fucosidase OS=Bos taurus OX=9913 GN=FUCA1 PE=2 SV=1 |
| Q60HF8 | 4.03e-120 | 20 | 490 | 37 | 467 | Tissue alpha-L-fucosidase OS=Macaca fascicularis OX=9541 GN=FUCA1 PE=2 SV=1 |
| P17164 | 9.42e-120 | 22 | 490 | 33 | 461 | Tissue alpha-L-fucosidase OS=Rattus norvegicus OX=10116 GN=Fuca1 PE=1 SV=1 |
| P48300 | 2.93e-119 | 20 | 490 | 35 | 464 | Tissue alpha-L-fucosidase OS=Canis lupus familiaris OX=9615 GN=FUCA1 PE=2 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000478 | 0.998794 | 0.000221 | 0.000178 | 0.000152 | 0.000147 |
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