Species | Parabacteroides goldsteinii | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides goldsteinii | |||||||||||
CAZyme ID | MGYG000001489_00897 | |||||||||||
CAZy Family | GH29 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 1122991; End: 1124730 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH29 | 20 | 327 | 1.1e-61 | 0.884393063583815 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3669 | AfuC | 2.79e-48 | 27 | 430 | 9 | 430 | Alpha-L-fucosidase [Carbohydrate transport and metabolism]. |
395889 | pfam01120 | 5.96e-23 | 43 | 327 | 29 | 326 | Alpha_L_fucos Alpha-L-fucosidase. |
smart00812 | Alpha_L_fucos | 5.76e-21 | 36 | 344 | 23 | 349 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ACO32076.1 | 8.61e-158 | 28 | 491 | 46 | 502 |
QMV17947.1 | 5.48e-156 | 29 | 484 | 37 | 485 |
QTH43029.1 | 4.73e-147 | 25 | 569 | 4 | 524 |
AYQ34472.1 | 1.06e-140 | 1 | 484 | 1 | 481 |
AXE18560.1 | 1.35e-138 | 17 | 499 | 12 | 500 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3GZA_A | 7.30e-78 | 24 | 431 | 5 | 441 | Crystalstructure of putative alpha-L-fucosidase (NP_812709.1) from BACTEROIDES THETAIOTAOMICRON VPI-5482 at 1.60 A resolution [Bacteroides thetaiotaomicron VPI-5482],3GZA_B Crystal structure of putative alpha-L-fucosidase (NP_812709.1) from BACTEROIDES THETAIOTAOMICRON VPI-5482 at 1.60 A resolution [Bacteroides thetaiotaomicron VPI-5482] |
4ZRX_A | 9.26e-69 | 29 | 482 | 32 | 510 | Crystalstructure of a putative alpha-L-fucosidase (BACOVA_04357) from Bacteroides ovatus ATCC 8483 at 1.59 A resolution [Bacteroides ovatus ATCC 8483] |
5K9H_A | 5.67e-64 | 19 | 440 | 30 | 473 | Crystalstructure of a glycoside hydrolase 29 family member from an unknown rumen bacterium [unidentified] |
6ORG_A | 2.09e-60 | 27 | 432 | 9 | 450 | Crystalstructure of SpGH29 [Streptococcus pneumoniae TIGR4],6ORG_B Crystal structure of SpGH29 [Streptococcus pneumoniae TIGR4] |
6OR4_A | 2.91e-59 | 27 | 432 | 9 | 450 | Crystalstructure of SpGH29 [Streptococcus pneumoniae TIGR4],6OR4_B Crystal structure of SpGH29 [Streptococcus pneumoniae TIGR4],6ORH_A Crystal structure of SpGH29 [Streptococcus pneumoniae TIGR4],6ORH_B Crystal structure of SpGH29 [Streptococcus pneumoniae TIGR4] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q8GW72 | 7.22e-72 | 26 | 430 | 35 | 477 | Alpha-L-fucosidase 1 OS=Arabidopsis thaliana OX=3702 GN=FUC1 PE=1 SV=2 |
Q7XUR3 | 3.13e-66 | 26 | 430 | 37 | 476 | Putative alpha-L-fucosidase 1 OS=Oryza sativa subsp. japonica OX=39947 GN=Os04g0560400 PE=3 SV=2 |
Q99KR8 | 6.05e-07 | 73 | 340 | 107 | 364 | 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 |
---|---|---|---|---|---|
0.000187 | 0.999200 | 0.000148 | 0.000150 | 0.000137 | 0.000125 |
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