Species | Parabacteroides faecis | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides faecis | |||||||||||
CAZyme ID | MGYG000000174_01416 | |||||||||||
CAZy Family | GH29 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 26831; End: 28543 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH29 | 25 | 332 | 5e-50 | 0.869942196531792 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3669 | AfuC | 4.15e-38 | 27 | 435 | 9 | 430 | Alpha-L-fucosidase [Carbohydrate transport and metabolism]. |
smart00812 | Alpha_L_fucos | 2.87e-17 | 43 | 332 | 30 | 328 | 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 | 6.23e-14 | 40 | 332 | 57 | 326 | Alpha-L-fucosidase. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
CDN30832.1 | 3.13e-190 | 9 | 570 | 7 | 542 |
AYQ34472.1 | 3.81e-158 | 9 | 567 | 6 | 556 |
AXE18560.1 | 4.32e-157 | 24 | 495 | 19 | 486 |
AEI49018.1 | 3.47e-156 | 29 | 558 | 24 | 545 |
ACO32076.1 | 7.44e-137 | 29 | 490 | 47 | 495 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3GZA_A | 3.32e-81 | 21 | 437 | 2 | 442 | 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] |
5K9H_A | 2.31e-57 | 27 | 446 | 37 | 474 | Crystalstructure of a glycoside hydrolase 29 family member from an unknown rumen bacterium [unidentified] |
4ZRX_A | 7.38e-55 | 28 | 436 | 31 | 459 | Crystalstructure of a putative alpha-L-fucosidase (BACOVA_04357) from Bacteroides ovatus ATCC 8483 at 1.59 A resolution [Bacteroides ovatus ATCC 8483] |
6ORG_A | 1.31e-49 | 27 | 435 | 9 | 448 | Crystalstructure of SpGH29 [Streptococcus pneumoniae TIGR4],6ORG_B Crystal structure of SpGH29 [Streptococcus pneumoniae TIGR4] |
6OR4_A | 1.74e-48 | 27 | 435 | 9 | 448 | 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 | 2.38e-54 | 26 | 429 | 35 | 471 | Alpha-L-fucosidase 1 OS=Arabidopsis thaliana OX=3702 GN=FUC1 PE=1 SV=2 |
Q7XUR3 | 5.39e-51 | 26 | 435 | 37 | 476 | Putative alpha-L-fucosidase 1 OS=Oryza sativa subsp. japonica OX=39947 GN=Os04g0560400 PE=3 SV=2 |
Q9VTJ4 | 5.78e-06 | 17 | 319 | 30 | 345 | Putative alpha-L-fucosidase OS=Drosophila melanogaster OX=7227 GN=Fuca PE=2 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000235 | 0.999112 | 0.000190 | 0.000160 | 0.000150 | 0.000137 |
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