Species | CAG-272 sp900556615 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; CAG-272; CAG-272; CAG-272 sp900556615 | |||||||||||
CAZyme ID | MGYG000000328_00070 | |||||||||||
CAZy Family | GH36 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 5386; End: 6942 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14791 | GH36 | 3.13e-27 | 171 | 473 | 2 | 295 | 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. |
COG3345 | GalA | 4.83e-06 | 164 | 318 | 285 | 451 | Alpha-galactosidase [Carbohydrate transport and metabolism]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BCK01268.1 | 7.03e-143 | 43 | 517 | 57 | 527 |
QGQ95278.1 | 1.76e-142 | 46 | 507 | 61 | 519 |
ANE49069.1 | 1.37e-137 | 41 | 509 | 5 | 475 |
BBH24190.1 | 2.33e-137 | 43 | 507 | 58 | 517 |
QCU01578.1 | 1.02e-136 | 30 | 514 | 61 | 546 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000068 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.