Species | Bacteroides oleiciplenus | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides oleiciplenus | |||||||||||
CAZyme ID | MGYG000001422_02682 | |||||||||||
CAZy Family | GH115 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 1418878; End: 1421805 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH115 | 38 | 675 | 9.3e-231 | 0.8378766140602583 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam15979 | Glyco_hydro_115 | 1.41e-171 | 191 | 531 | 1 | 333 | 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 | 7.58e-48 | 802 | 969 | 2 | 170 | 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. |
cd14948 | BACON | 5.67e-04 | 728 | 785 | 27 | 80 | Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
EDV07546.1 | 0.0 | 39 | 975 | 32 | 966 |
ALK86808.1 | 0.0 | 39 | 975 | 33 | 967 |
AYD49386.1 | 0.0 | 25 | 975 | 23 | 966 |
APZ45930.1 | 0.0 | 2 | 975 | 3 | 960 |
AUC19792.1 | 0.0 | 2 | 975 | 3 | 960 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4ZMH_A | 1.21e-166 | 49 | 970 | 24 | 931 | 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] |
5BY3_A | 4.52e-135 | 38 | 662 | 19 | 619 | Anovel family GH115 4-O-Methyl-alpha-glucuronidase, BtGH115A, with specificity for decorated arabinogalactans [Bacteroides thetaiotaomicron VPI-5482] |
6NPS_A | 3.25e-126 | 58 | 973 | 34 | 964 | 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] |
4C90_A | 1.20e-116 | 8 | 975 | 12 | 852 | 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 | 1.02e-101 | 39 | 659 | 17 | 626 | ChainA, xylan alpha-1,2-glucuronidase [uncultured bacterium] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000804 | 0.606474 | 0.391870 | 0.000342 | 0.000270 | 0.000220 |
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