| Species | CAG-841 sp000437375 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; CAG-272; CAG-841; CAG-841 sp000437375 | |||||||||||
| CAZyme ID | MGYG000000463_00414 | |||||||||||
| CAZy Family | GH156 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 179015; End: 180526 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH156 | 2 | 460 | 1.1e-95 | 0.8134057971014492 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd14791 | GH36 | 5.85e-08 | 106 | 201 | 71 | 160 | glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| PWL98936.1 | 2.61e-176 | 3 | 502 | 4 | 510 |
| AYA93387.1 | 1.60e-83 | 2 | 503 | 8 | 501 |
| RAV19586.1 | 1.98e-76 | 2 | 429 | 3 | 424 |
| QOY88011.1 | 1.28e-74 | 6 | 500 | 30 | 506 |
| PKO20768.1 | 7.01e-72 | 2 | 449 | 3 | 448 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6RZD_A | 6.85e-85 | 2 | 503 | 8 | 501 | Crystalstructure of an inverting family GH156 exosialidase from uncultured bacterium pG7 [uncultured bacterium pG7],6RZD_B Crystal structure of an inverting family GH156 exosialidase from uncultured bacterium pG7 [uncultured bacterium pG7],6S00_A Crystal structure of an inverting family GH156 exosialidase from uncultured bacterium pG7 in complex with N-acetylneuraminic acid [uncultured bacterium pG7],6S00_B Crystal structure of an inverting family GH156 exosialidase from uncultured bacterium pG7 in complex with N-acetylneuraminic acid [uncultured bacterium pG7],6S0E_A Crystal structure of an inverting family GH156 exosialidase from uncultured bacterium pG7 in complex with N-Acetyl-2,3-dehydro-2-deoxyneuraminic acid [uncultured bacterium pG7],6S0E_B Crystal structure of an inverting family GH156 exosialidase from uncultured bacterium pG7 in complex with N-Acetyl-2,3-dehydro-2-deoxyneuraminic acid [uncultured bacterium pG7],6S0F_A Crystal structure of an inverting family GH156 exosialidase from uncultured bacterium pG7 in complex with 3-Deoxy-D-glycero-D-galacto-2-nonulosonic acid [uncultured bacterium pG7],6S0F_B Crystal structure of an inverting family GH156 exosialidase from uncultured bacterium pG7 in complex with 3-Deoxy-D-glycero-D-galacto-2-nonulosonic acid [uncultured bacterium pG7] |
| 6S04_A | 7.26e-80 | 2 | 503 | 8 | 501 | Crystalstructure of an inverting family GH156 exosialidase from uncultured bacterium pG7 in complex with N-glycolylneuraminic acid [uncultured bacterium pG7],6S04_B Crystal structure of an inverting family GH156 exosialidase from uncultured bacterium pG7 in complex with N-glycolylneuraminic acid [uncultured bacterium pG7] |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000063 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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