Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Monoglobales_A; UBA9506; ; | |||||||||||
CAZyme ID | MGYG000002685_00299 | |||||||||||
CAZy Family | GH156 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 2370; End: 3950 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH156 | 3 | 511 | 4.4e-70 | 0.9003623188405797 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG1649 | YddW | 5.40e-05 | 30 | 191 | 61 | 212 | Uncharacterized lipoprotein YddW, UPF0748 family [Function unknown]. |
cd14791 | GH36 | 0.001 | 29 | 219 | 15 | 183 | 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 |
---|---|---|---|---|---|
QHI69841.1 | 9.67e-157 | 3 | 525 | 26 | 540 |
QIF01836.1 | 6.06e-110 | 2 | 514 | 45 | 553 |
QHI69840.1 | 1.02e-88 | 2 | 505 | 22 | 527 |
QGJ71964.1 | 1.40e-72 | 5 | 507 | 44 | 537 |
AQQ72137.1 | 1.30e-37 | 3 | 503 | 46 | 530 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6RZD_A | 5.27e-22 | 23 | 499 | 20 | 481 | 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 | 1.27e-18 | 23 | 499 | 20 | 481 | 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 |
---|---|---|---|---|---|
1.000076 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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