Species | ||||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; Borkfalkiaceae; Borkfalkia; | |||||||||||
CAZyme ID | MGYG000000733_01413 | |||||||||||
CAZy Family | GH115 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 1115; End: 5560 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH115 | 55 | 687 | 2.3e-187 | 0.8192252510760402 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam15979 | Glyco_hydro_115 | 1.84e-123 | 207 | 568 | 2 | 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 | 1.67e-49 | 815 | 987 | 1 | 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. |
cd14948 | BACON | 6.01e-05 | 722 | 803 | 7 | 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. |
pfam03648 | Glyco_hydro_67N | 3.71e-04 | 42 | 170 | 4 | 118 | 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). |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ASA21655.1 | 1.93e-276 | 8 | 1462 | 7 | 1481 |
QUC63565.1 | 1.67e-205 | 68 | 997 | 45 | 956 |
ANS63447.1 | 1.82e-201 | 4 | 998 | 15 | 985 |
AXG52369.1 | 1.82e-201 | 4 | 998 | 15 | 985 |
QMV12190.1 | 1.92e-201 | 21 | 998 | 12 | 964 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4ZMH_A | 4.38e-131 | 34 | 988 | 1 | 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] |
6NPS_A | 1.12e-98 | 71 | 989 | 31 | 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] |
5BY3_A | 1.65e-90 | 45 | 777 | 21 | 714 | Anovel family GH115 4-O-Methyl-alpha-glucuronidase, BtGH115A, with specificity for decorated arabinogalactans [Bacteroides thetaiotaomicron VPI-5482] |
4C90_A | 4.57e-82 | 54 | 681 | 46 | 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] |
7PUG_A | 4.80e-82 | 43 | 681 | 17 | 625 | ChainA, xylan alpha-1,2-glucuronidase [uncultured bacterium] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000000 | 0.000003 | 1.000039 | 0.000000 | 0.000000 | 0.000000 |
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