Species | AF33-28 sp003477885 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; AF33-28; AF33-28 sp003477885 | |||||||||||
CAZyme ID | MGYG000000202_00304 | |||||||||||
CAZy Family | GH115 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 374701; End: 378135 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH115 | 7 | 887 | 6.1e-186 | 0.9799139167862266 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam15979 | Glyco_hydro_115 | 4.65e-141 | 142 | 495 | 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 | 8.97e-14 | 758 | 908 | 4 | 172 | 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 | 1.14e-04 | 17 | 109 | 27 | 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). |
pfam17829 | GH115_C | 0.002 | 977 | 1131 | 1 | 161 | 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 | 0.003 | 661 | 719 | 13 | 79 | 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 |
---|---|---|---|---|---|
QOV19968.1 | 0.0 | 1 | 1141 | 2 | 1120 |
AIQ48273.1 | 0.0 | 4 | 1142 | 3 | 1201 |
AIQ53763.1 | 0.0 | 4 | 1142 | 3 | 1201 |
AIQ31286.1 | 0.0 | 10 | 1142 | 11 | 1202 |
AJE49570.1 | 0.0 | 4 | 1141 | 13 | 1207 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5BY3_A | 6.68e-93 | 2 | 562 | 19 | 577 | Anovel family GH115 4-O-Methyl-alpha-glucuronidase, BtGH115A, with specificity for decorated arabinogalactans [Bacteroides thetaiotaomicron VPI-5482] |
4ZMH_A | 5.78e-89 | 18 | 701 | 30 | 746 | 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] |
7PUG_A | 1.78e-82 | 15 | 611 | 30 | 626 | ChainA, xylan alpha-1,2-glucuronidase [uncultured bacterium] |
7PXQ_A | 4.85e-80 | 15 | 611 | 29 | 625 | ChainA, xylan alpha-1,2-glucuronidase [uncultured bacterium] |
4C90_A | 6.79e-76 | 15 | 610 | 57 | 640 | 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] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000038 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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