Species | Parabacteroides goldsteinii | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides goldsteinii | |||||||||||
CAZyme ID | MGYG000001489_04400 | |||||||||||
CAZy Family | GH156 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 2099983; End: 2101599 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH156 | 29 | 532 | 3.9e-115 | 0.9239130434782609 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG1649 | YddW | 1.39e-05 | 124 | 301 | 113 | 309 | Uncharacterized lipoprotein YddW, UPF0748 family [Function unknown]. |
cd14791 | GH36 | 3.42e-05 | 165 | 254 | 94 | 192 | 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 |
---|---|---|---|---|---|
QUT49878.1 | 3.54e-232 | 28 | 538 | 32 | 550 |
BBD44721.1 | 4.51e-206 | 55 | 538 | 3 | 491 |
BCG53795.1 | 1.50e-187 | 15 | 538 | 4 | 543 |
QGA27036.1 | 1.19e-182 | 10 | 538 | 16 | 557 |
QDU82332.1 | 2.38e-41 | 17 | 376 | 17 | 389 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6RZD_A | 8.46e-36 | 49 | 531 | 25 | 497 | 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 | 8.73e-32 | 49 | 410 | 25 | 383 | 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 |
---|---|---|---|---|---|
0.000280 | 0.121037 | 0.878416 | 0.000098 | 0.000100 | 0.000076 |
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