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CAZyme Information: MGYG000000553_02402
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Prevotella sp900548535 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900548535 | |||||||||||
| CAZyme ID | MGYG000000553_02402 | |||||||||||
| CAZy Family | GH115 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 4215; End: 6764 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH115 | 38 | 835 | 1.5e-273 | 0.9913916786226685 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam15979 | Glyco_hydro_115 | 0.0 | 183 | 519 | 1 | 334 | Glycosyl hydrolase family 115. Glyco_hydro_115 is a family of glycoside hydrolases likely to have the activity of xylan a-1,2-glucuronidase, EC:3.2.1.131, or a-(4-O-methyl)-glucuronidase EC:3.2.1.-. |
| pfam17829 | GH115_C | 3.50e-27 | 667 | 838 | 6 | 159 | Gylcosyl hydrolase family 115 C-terminal domain. This domain is found at the C-terminus of glycosyl hydrolase family 115 proteins. This domain has a beta-sandwich fold. |
| pfam03648 | Glyco_hydro_67N | 7.91e-06 | 77 | 150 | 49 | 120 | Glycosyl hydrolase family 67 N-terminus. Alpha-glucuronidases, components of an ensemble of enzymes central to the recycling of photosynthetic biomass, remove the alpha-1,2 linked 4-O-methyl glucuronic acid from xylans. This family represents the N-terminal region of alpha-glucuronidase. The N-terminal domain forms a two-layer sandwich, each layer being formed by a beta sheet of five strands. A further two helices form part of the interface with the central, catalytic, module (pfam07488). |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QNT66545.1 | 0.0 | 3 | 849 | 2 | 852 |
| BCS85271.1 | 0.0 | 18 | 838 | 14 | 814 |
| CCG34758.1 | 0.0 | 37 | 838 | 1 | 784 |
| AGB29053.1 | 0.0 | 18 | 838 | 21 | 817 |
| ADE81569.1 | 0.0 | 9 | 838 | 10 | 809 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 4C90_A | 0.0 | 1 | 844 | 6 | 841 | Evidencethat GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C90_B Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C91_A Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C91_B Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus] |
| 7PUG_A | 0.0 | 38 | 838 | 19 | 820 | ChainA, xylan alpha-1,2-glucuronidase [uncultured bacterium] |
| 7PXQ_A | 0.0 | 38 | 838 | 18 | 819 | ChainA, xylan alpha-1,2-glucuronidase [uncultured bacterium] |
| 4ZMH_A | 9.63e-185 | 29 | 726 | 5 | 694 | Crystalstructure of a five-domain GH115 alpha-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40T [Saccharophagus degradans 2-40],4ZMH_B Crystal structure of a five-domain GH115 alpha-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40T [Saccharophagus degradans 2-40] |
| 6NPS_A | 8.80e-123 | 31 | 647 | 6 | 652 | Crystalstructure of GH115 enzyme AxyAgu115A from Amphibacillus xylanus [Amphibacillus xylanus NBRC 15112],6NPS_B Crystal structure of GH115 enzyme AxyAgu115A from Amphibacillus xylanus [Amphibacillus xylanus NBRC 15112] |
Swiss-Prot Hits help
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000562 | 0.998627 | 0.000241 | 0.000199 | 0.000180 | 0.000166 |