| Species | Victivallis sp002998355 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; Victivallis; Victivallis sp002998355 | |||||||||||
| CAZyme ID | MGYG000003237_00531 | |||||||||||
| CAZy Family | GH5 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 18092; End: 19606 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH5 | 203 | 473 | 2.1e-45 | 0.7345454545454545 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam00150 | Cellulase | 6.30e-23 | 208 | 469 | 28 | 271 | Cellulase (glycosyl hydrolase family 5). |
| COG2730 | BglC | 1.20e-13 | 208 | 482 | 77 | 375 | Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism]. |
| pfam02449 | Glyco_hydro_42 | 6.08e-05 | 252 | 321 | 49 | 138 | Beta-galactosidase. This group of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. The enzyme catalyzes the hydrolysis of terminal, non-reducing terminal beta-D-galactosidase residues. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AVM44501.1 | 0.0 | 1 | 504 | 1 | 504 |
| AVM45838.1 | 8.70e-160 | 1 | 503 | 18 | 529 |
| AVM43397.1 | 4.63e-150 | 12 | 504 | 10 | 508 |
| AVM46390.1 | 5.90e-140 | 45 | 504 | 33 | 503 |
| AVM45720.1 | 6.73e-137 | 38 | 504 | 87 | 563 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3AMC_A | 7.58e-16 | 250 | 471 | 74 | 288 | Crystalstructures of Thermotoga maritima Cel5A, apo form and dimer/au [Thermotoga maritima MSB8],3AMC_B Crystal structures of Thermotoga maritima Cel5A, apo form and dimer/au [Thermotoga maritima MSB8],3AMD_A Crystal structures of Thermotoga maritima Cel5A, apo form and tetramer/au [Thermotoga maritima MSB8],3AMD_B Crystal structures of Thermotoga maritima Cel5A, apo form and tetramer/au [Thermotoga maritima MSB8],3AMD_C Crystal structures of Thermotoga maritima Cel5A, apo form and tetramer/au [Thermotoga maritima MSB8],3AMD_D Crystal structures of Thermotoga maritima Cel5A, apo form and tetramer/au [Thermotoga maritima MSB8],3MMU_A Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_B Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_C Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_D Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_E Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_F Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_G Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_H Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMW_A Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMW_B Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMW_C Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMW_D Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima] |
| 3AMG_A | 4.48e-15 | 250 | 471 | 74 | 288 | Crystalstructures of Thermotoga maritima Cel5A in complex with Cellobiose substrate, mutant form [Thermotoga maritima MSB8],3AMG_B Crystal structures of Thermotoga maritima Cel5A in complex with Cellobiose substrate, mutant form [Thermotoga maritima MSB8] |
| 3AZR_A | 4.48e-15 | 250 | 471 | 74 | 288 | DiverseSubstrates Recognition Mechanism Revealed by Thermotoga maritima Cel5A Structures in Complex with Cellobiose [Thermotoga maritima MSB8],3AZR_B Diverse Substrates Recognition Mechanism Revealed by Thermotoga maritima Cel5A Structures in Complex with Cellobiose [Thermotoga maritima MSB8],3AZS_A Diverse Substrates Recognition Mechanism Revealed by Thermotoga maritima Cel5A Structures in Complex with Mannotriose [Thermotoga maritima MSB8],3AZS_B Diverse Substrates Recognition Mechanism Revealed by Thermotoga maritima Cel5A Structures in Complex with Mannotriose [Thermotoga maritima MSB8],3AZT_A Diverse Substrates Recognition Mechanism Revealed by Thermotoga maritima Cel5A Structures in Complex with Cellotetraose [Thermotoga maritima MSB8],3AZT_B Diverse Substrates Recognition Mechanism Revealed by Thermotoga maritima Cel5A Structures in Complex with Cellotetraose [Thermotoga maritima MSB8],3AZT_C Diverse Substrates Recognition Mechanism Revealed by Thermotoga maritima Cel5A Structures in Complex with Cellotetraose [Thermotoga maritima MSB8],3AZT_D Diverse Substrates Recognition Mechanism Revealed by Thermotoga maritima Cel5A Structures in Complex with Cellotetraose [Thermotoga maritima MSB8] |
| 3AOF_A | 2.07e-13 | 250 | 445 | 74 | 260 | Crystalstructures of Thermotoga maritima Cel5A in complex with Mannotriose substrate [Thermotoga maritima MSB8],3AOF_B Crystal structures of Thermotoga maritima Cel5A in complex with Mannotriose substrate [Thermotoga maritima MSB8] |
| 6KDD_A | 1.27e-12 | 249 | 471 | 81 | 295 | endoglucanase[Fervidobacterium pennivorans DSM 9078] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P16169 | 2.82e-15 | 203 | 463 | 29 | 285 | Cellodextrinase A OS=Ruminococcus flavefaciens OX=1265 GN=celA PE=3 SV=3 |
| W8QRE4 | 3.76e-13 | 250 | 442 | 111 | 296 | Beta-xylosidase OS=Phanerodontia chrysosporium OX=2822231 GN=Xyl5 PE=1 SV=2 |
| P23548 | 3.40e-09 | 198 | 384 | 63 | 277 | Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.001282 | 0.990334 | 0.007686 | 0.000235 | 0.000212 | 0.000224 |
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