Species | Alistipes provencensis | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes provencensis | |||||||||||
CAZyme ID | MGYG000001546_01945 | |||||||||||
CAZy Family | GH115 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 2473836; End: 2476784 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH115 | 38 | 666 | 7.1e-228 | 0.8436154949784792 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam15979 | Glyco_hydro_115 | 7.01e-166 | 191 | 533 | 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 | 3.05e-45 | 790 | 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 | 3.14e-04 | 717 | 774 | 28 | 81 | 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. |
pfam13004 | BACON | 6.54e-04 | 717 | 770 | 3 | 54 | Putative binding domain, N-terminal. The BACON (Bacteroidetes-Associated Carbohydrate-binding Often N-terminal) domain is an all-beta domain found in diverse architectures, principally in combination with carbohydrate-active enzymes and proteases. These architectures suggest a carbohydrate-binding function which is also supported by the nature of BACON's few conserved amino-acids. The phyletic distribution of BACON and other data tentatively suggest that it may frequently function to bind mucin. Further work with the characterized structure of a member of glycoside hydrolase family 5 enzyme, Structure 3ZMR, has found no evidence for carbohydrate-binding for this domain. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QUR45611.1 | 0.0 | 14 | 975 | 8 | 970 |
QUR45612.1 | 0.0 | 19 | 973 | 16 | 982 |
EDV06188.1 | 0.0 | 23 | 973 | 20 | 983 |
QDO71503.1 | 0.0 | 23 | 973 | 18 | 981 |
BCA48102.1 | 0.0 | 39 | 972 | 33 | 979 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4ZMH_A | 5.29e-158 | 41 | 972 | 16 | 933 | 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 | 3.33e-125 | 59 | 643 | 39 | 611 | Anovel family GH115 4-O-Methyl-alpha-glucuronidase, BtGH115A, with specificity for decorated arabinogalactans [Bacteroides thetaiotaomicron VPI-5482] |
4C90_A | 4.04e-113 | 7 | 662 | 13 | 658 | 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 | 4.20e-111 | 38 | 662 | 16 | 643 | ChainA, xylan alpha-1,2-glucuronidase [uncultured bacterium] |
7PXQ_A | 7.96e-111 | 38 | 662 | 15 | 642 | ChainA, xylan alpha-1,2-glucuronidase [uncultured bacterium] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.004968 | 0.938318 | 0.055106 | 0.000902 | 0.000368 | 0.000303 |
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