| Species | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; CAG-272; ; | |||||||||||
| CAZyme ID | MGYG000000350_00163 | |||||||||||
| CAZy Family | GH39 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
|
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| Genome Property |
|
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| Gene Location | Start: 6393; End: 7829 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH39 | 62 | 231 | 5.7e-30 | 0.38979118329466356 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam01229 | Glyco_hydro_39 | 2.06e-11 | 47 | 236 | 46 | 239 | Glycosyl hydrolases family 39. |
| pfam02449 | Glyco_hydro_42 | 1.43e-05 | 27 | 90 | 4 | 66 | Beta-galactosidase. This group of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. The enzyme catalyzes the hydrolysis of terminal, non-reducing terminal beta-D-galactosidase residues. |
| cd21510 | agarase_cat | 0.007 | 126 | 223 | 82 | 187 | alpha-beta barrel catalytic domain of agarase, such as GH86-like endo-acting agarases identified in non-marine organisms. Typically, agarases (E.C. 3.2.1.81) are found in ocean-dwelling bacteria since agarose is a principle component of red algae cell wall polysaccharides. Agarose is a linear polymer of alternating D-galactose and 3,6-anhydro-L-galactopyranose. Endo-acting agarases, such as glycoside hydrolase 16 (GH16) and GH86 hydrolyze internal beta-1,4 linkages. GH86-like endo-acting agarase of this protein family has been identified in the human intestinal bacterium Bacteroides uniformis. This acquired metabolic pathway, as demonstrated by the prevalence of agar-specific genetic cluster called polysaccharide utilization loci (PULs), varies considerably between human populations, being much more prevalent in a Japanese sample than in North America, European, or Chinese samples. Agarase activity was also identified in the non-marine bacterium Cellvibrio sp. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QYY35369.1 | 3.24e-159 | 1 | 477 | 1 | 474 |
| AVM45335.1 | 1.59e-143 | 1 | 476 | 10 | 477 |
| AWI10371.1 | 4.41e-143 | 4 | 477 | 61 | 529 |
| QNN22730.1 | 8.84e-66 | 8 | 472 | 51 | 479 |
| ASV73290.1 | 3.71e-61 | 7 | 472 | 70 | 522 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 4EKJ_A | 1.06e-06 | 44 | 226 | 51 | 234 | ChainA, Beta-xylosidase [Caulobacter vibrioides] |
| 4M29_A | 1.06e-06 | 44 | 226 | 51 | 234 | Structureof a GH39 Beta-xylosidase from Caulobacter crescentus [Caulobacter vibrioides CB15] |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000055 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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