| Species | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UBA737; | |||||||||||
| CAZyme ID | MGYG000004470_00854 | |||||||||||
| CAZy Family | GH63 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 2140; End: 3420 Strand: - | |||||||||||
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| PRK10137 | PRK10137 | 1.13e-16 | 58 | 313 | 417 | 759 | alpha-glucosidase; Provisional |
| COG3408 | GDB1 | 9.24e-11 | 1 | 357 | 290 | 615 | Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism]. |
| pfam03200 | Glyco_hydro_63 | 1.16e-10 | 80 | 347 | 188 | 494 | 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. |
| pfam01204 | Trehalase | 5.37e-04 | 154 | 310 | 311 | 473 | 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. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AIQ57834.1 | 1.35e-170 | 1 | 425 | 88 | 499 |
| QHT63246.1 | 7.47e-164 | 1 | 416 | 111 | 516 |
| QHT63247.1 | 7.94e-153 | 1 | 424 | 109 | 522 |
| QIN83484.1 | 1.42e-152 | 1 | 422 | 92 | 508 |
| BAX79981.1 | 7.48e-152 | 1 | 425 | 124 | 534 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3W7S_A | 7.93e-07 | 154 | 312 | 564 | 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 | 7.93e-07 | 154 | 312 | 564 | 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 | 8.35e-07 | 154 | 312 | 113 | 280 | ChainB, Anti-RON nanobody,Megabody 91,Glucosidase YgjK [Lama glama] |
| 6XUX_A | 8.36e-07 | 154 | 312 | 113 | 280 | ChainA, Nanobody,Glucosidase YgjK,Glucosidase YgjK,Nanobody [Escherichia coli K-12] |
| 7Q6Z_B | 8.39e-07 | 154 | 312 | 135 | 302 | ChainB, Megabody 177 [Escherichia coli K-12] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P94250 | 2.60e-29 | 4 | 390 | 62 | 431 | Uncharacterized protein BB_0381 OS=Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) OX=224326 GN=BB_0381 PE=4 SV=2 |
| O14255 | 3.60e-12 | 78 | 347 | 526 | 806 | Probable mannosyl-oligosaccharide glucosidase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPAC6G10.09 PE=3 SV=1 |
| P42592 | 4.38e-06 | 154 | 312 | 587 | 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 |
|---|---|---|---|---|---|
| 1.000039 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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