Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; UBA1829; ; | |||||||||||
CAZyme ID | MGYG000001812_00202 | |||||||||||
CAZy Family | GH63 | |||||||||||
CAZyme Description | Cytoplasmic trehalase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 20117; End: 21667 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH63 | 251 | 431 | 4.7e-21 | 0.3894736842105263 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
PRK10137 | PRK10137 | 1.38e-18 | 231 | 387 | 578 | 742 | alpha-glucosidase; Provisional |
COG3408 | GDB1 | 2.86e-13 | 30 | 480 | 257 | 640 | Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism]. |
pfam01204 | Trehalase | 3.97e-10 | 244 | 429 | 318 | 497 | Trehalase. Trehalase (EC:3.2.1.28) is known to recycle trehalose to glucose. Trehalose is a physiological hallmark of heat-shock response in yeast and protects of proteins and membranes against a variety of stresses. This family is found in conjunction with pfam07492 in fungi. |
pfam03200 | Glyco_hydro_63 | 5.64e-10 | 163 | 431 | 195 | 487 | Glycosyl hydrolase family 63 C-terminal domain. This is a family of eukaryotic enzymes belonging to glycosyl hydrolase family 63. They catalyze the specific cleavage of the non-reducing terminal glucose residue from Glc(3)Man(9)GlcNAc(2). Mannosyl oligosaccharide glucosidase EC:3.2.1.106 is the first enzyme in the N-linked oligosaccharide processing pathway. This family represents the C-terminal catalytic domain. |
COG1626 | TreA | 5.80e-10 | 242 | 392 | 365 | 507 | Neutral trehalase [Carbohydrate transport and metabolism]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AVM44762.1 | 3.11e-212 | 1 | 510 | 84 | 590 |
QZT38129.1 | 1.43e-184 | 18 | 511 | 33 | 498 |
AOW82330.1 | 1.94e-163 | 11 | 516 | 39 | 515 |
QIU93173.1 | 5.49e-161 | 7 | 515 | 21 | 498 |
QWP09187.1 | 7.35e-158 | 10 | 515 | 2 | 476 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3W7S_A | 4.79e-10 | 231 | 406 | 551 | 731 | Escherichiacoli K12 YgjK complexed with glucose [Escherichia coli K-12],3W7S_B Escherichia coli K12 YgjK complexed with glucose [Escherichia coli K-12],3W7T_A Escherichia coli K12 YgjK complexed with mannose [Escherichia coli K-12],3W7T_B Escherichia coli K12 YgjK complexed with mannose [Escherichia coli K-12],3W7U_A Escherichia coli K12 YgjK complexed with galactose [Escherichia coli K-12],3W7U_B Escherichia coli K12 YgjK complexed with galactose [Escherichia coli K-12] |
3W7X_A | 4.79e-10 | 231 | 406 | 551 | 731 | Crystalstructure of E. coli YgjK D324N complexed with melibiose [Escherichia coli K-12],3W7X_B Crystal structure of E. coli YgjK D324N complexed with melibiose [Escherichia coli K-12],5CA3_A Crystal structure of the glycosynthase mutant D324N of Escherichia coli GH63 glycosidase in complex with glucose and lactose [Escherichia coli K-12],5CA3_B Crystal structure of the glycosynthase mutant D324N of Escherichia coli GH63 glycosidase in complex with glucose and lactose [Escherichia coli K-12] |
7PQQ_B | 5.14e-10 | 231 | 406 | 100 | 280 | ChainB, Anti-RON nanobody,Megabody 91,Glucosidase YgjK [Lama glama] |
6XUX_A | 5.15e-10 | 231 | 406 | 100 | 280 | ChainA, Nanobody,Glucosidase YgjK,Glucosidase YgjK,Nanobody [Escherichia coli K-12] |
7Q6Z_B | 5.17e-10 | 231 | 406 | 122 | 302 | ChainB, Megabody 177 [Escherichia coli K-12] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P94250 | 5.21e-32 | 14 | 500 | 3 | 451 | Uncharacterized protein BB_0381 OS=Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) OX=224326 GN=BB_0381 PE=4 SV=2 |
P42592 | 2.66e-09 | 231 | 406 | 574 | 754 | Glucosidase YgjK OS=Escherichia coli (strain K12) OX=83333 GN=ygjK PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000069 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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