Species | Bacteroides eggerthii | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides eggerthii | |||||||||||
CAZyme ID | MGYG000001313_03185 | |||||||||||
CAZy Family | GH29 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 312676; End: 314340 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH29 | 40 | 441 | 5e-86 | 0.9364161849710982 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
smart00812 | Alpha_L_fucos | 6.86e-109 | 41 | 497 | 2 | 378 | 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 | 4.88e-95 | 41 | 437 | 1 | 333 | Alpha-L-fucosidase. |
COG3669 | AfuC | 1.63e-72 | 73 | 526 | 1 | 409 | Alpha-L-fucosidase [Carbohydrate transport and metabolism]. |
pfam16757 | Fucosidase_C | 9.46e-09 | 471 | 552 | 4 | 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 |
---|---|---|---|---|---|
QRQ49804.1 | 0.0 | 1 | 554 | 1 | 554 |
QUT45312.1 | 0.0 | 1 | 553 | 1 | 551 |
QZT37564.1 | 6.53e-120 | 49 | 554 | 33 | 522 |
QZE15226.1 | 2.93e-118 | 47 | 551 | 35 | 507 |
QOY86471.1 | 3.71e-114 | 4 | 551 | 6 | 523 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7LJJ_A | 1.55e-86 | 52 | 554 | 49 | 511 | ChainA, Exo-alpha-L-galactosidase [Phocaeicola plebeius DSM 17135],7LK7_A Chain A, Exo-alpha-L-galactosidase [Phocaeicola plebeius DSM 17135] |
7LNP_A | 8.39e-86 | 52 | 554 | 49 | 511 | 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 | 5.38e-56 | 42 | 552 | 3 | 490 | 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 | 3.90e-43 | 47 | 538 | 9 | 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 | 4.36e-43 | 47 | 538 | 9 | 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 |
---|---|---|---|---|---|---|
Q6AYS4 | 9.53e-38 | 47 | 542 | 27 | 442 | Plasma alpha-L-fucosidase OS=Rattus norvegicus OX=10116 GN=Fuca2 PE=2 SV=1 |
P17164 | 1.00e-37 | 60 | 552 | 46 | 459 | Tissue alpha-L-fucosidase OS=Rattus norvegicus OX=10116 GN=Fuca1 PE=1 SV=1 |
Q5RFI5 | 1.97e-37 | 47 | 538 | 33 | 444 | Plasma alpha-L-fucosidase OS=Pongo abelii OX=9601 GN=FUCA2 PE=2 SV=1 |
Q99LJ1 | 3.01e-37 | 60 | 552 | 36 | 449 | Tissue alpha-L-fucosidase OS=Mus musculus OX=10090 GN=Fuca1 PE=1 SV=1 |
Q99KR8 | 3.48e-37 | 47 | 542 | 29 | 444 | 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 |
---|---|---|---|---|---|
0.000238 | 0.999170 | 0.000162 | 0.000165 | 0.000140 | 0.000130 |
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