Species | Alistipes_A sp900545315 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes_A; Alistipes_A sp900545315 | |||||||||||
CAZyme ID | MGYG000004469_00933 | |||||||||||
CAZy Family | GH156 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 93377; End: 95056 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH156 | 7 | 553 | 4.8e-111 | 0.9746376811594203 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14791 | GH36 | 5.38e-04 | 178 | 237 | 95 | 156 | 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. |
COG1649 | YddW | 0.002 | 186 | 319 | 164 | 315 | Uncharacterized lipoprotein YddW, UPF0748 family [Function unknown]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BCG53795.1 | 0.0 | 20 | 559 | 4 | 543 |
QUT49878.1 | 1.91e-195 | 24 | 559 | 20 | 550 |
QGA27036.1 | 9.79e-195 | 16 | 559 | 16 | 557 |
BBD44721.1 | 2.12e-182 | 62 | 559 | 3 | 491 |
PKO20768.1 | 1.46e-45 | 64 | 536 | 24 | 491 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6RZD_A | 2.93e-41 | 41 | 530 | 12 | 485 | 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 | 7.58e-38 | 41 | 530 | 12 | 485 | 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 |
---|---|---|---|---|---|
0.000006 | 0.002903 | 0.997151 | 0.000001 | 0.000002 | 0.000001 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.