| Species | Butyricimonas faecalis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Marinifilaceae; Butyricimonas; Butyricimonas faecalis | |||||||||||
| CAZyme ID | MGYG000001655_03148 | |||||||||||
| CAZy Family | GH29 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 4; End: 726 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH29 | 2 | 140 | 2.3e-46 | 0.38439306358381503 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam01120 | Alpha_L_fucos | 2.11e-54 | 2 | 136 | 195 | 333 | Alpha-L-fucosidase. |
| smart00812 | Alpha_L_fucos | 1.64e-51 | 2 | 170 | 195 | 373 | 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. |
| COG3669 | AfuC | 2.22e-23 | 2 | 150 | 166 | 331 | Alpha-L-fucosidase [Carbohydrate transport and metabolism]. |
| pfam16757 | Fucosidase_C | 2.72e-11 | 152 | 231 | 9 | 87 | 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 |
|---|---|---|---|---|---|
| QRO50063.1 | 3.92e-182 | 1 | 240 | 228 | 467 |
| ASZ09523.1 | 2.81e-83 | 1 | 238 | 230 | 478 |
| ACU64455.1 | 9.53e-83 | 1 | 236 | 232 | 484 |
| QHS60762.1 | 9.53e-83 | 1 | 234 | 232 | 482 |
| QJB41770.1 | 9.10e-82 | 1 | 216 | 230 | 457 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6GN6_A | 1.00e-23 | 1 | 169 | 201 | 380 | Alpha-L-fucosidaseisoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus],6GN6_B Alpha-L-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus],6GN6_C Alpha-L-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus],6GN6_D Alpha-L-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus],6GN6_E Alpha-L-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus],6GN6_F Alpha-L-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus] |
| 7DB5_A | 3.45e-18 | 4 | 141 | 216 | 362 | ChainA, Alpha-L-fucosidase [Vibrio sp. EJY3] |
| 7LJJ_A | 1.56e-17 | 63 | 228 | 323 | 503 | ChainA, Exo-alpha-L-galactosidase [Phocaeicola plebeius DSM 17135],7LK7_A Chain A, Exo-alpha-L-galactosidase [Phocaeicola plebeius DSM 17135] |
| 7LNP_A | 1.56e-17 | 63 | 228 | 323 | 503 | 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] |
| 1HL8_A | 4.29e-17 | 2 | 221 | 219 | 436 | 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] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q99LJ1 | 5.15e-22 | 2 | 237 | 211 | 452 | Tissue alpha-L-fucosidase OS=Mus musculus OX=10090 GN=Fuca1 PE=1 SV=1 |
| P17164 | 1.91e-21 | 2 | 237 | 221 | 462 | Tissue alpha-L-fucosidase OS=Rattus norvegicus OX=10116 GN=Fuca1 PE=1 SV=1 |
| C3YWU0 | 4.56e-21 | 2 | 236 | 208 | 448 | Alpha-L-fucosidase OS=Branchiostoma floridae OX=7739 GN=BRAFLDRAFT_56888 PE=3 SV=2 |
| Q6AYS4 | 8.97e-21 | 2 | 236 | 215 | 458 | Plasma alpha-L-fucosidase OS=Rattus norvegicus OX=10116 GN=Fuca2 PE=2 SV=1 |
| Q99KR8 | 1.24e-20 | 2 | 236 | 217 | 460 | 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 |
|---|---|---|---|---|---|
| 1.000046 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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