Species | Fournierella sp900543285 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Fournierella; Fournierella sp900543285 | |||||||||||
CAZyme ID | MGYG000004126_00847 | |||||||||||
CAZy Family | GH16 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 62302; End: 64092 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH16 | 51 | 291 | 1.9e-73 | 0.991701244813278 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd00413 | Glyco_hydrolase_16 | 1.43e-27 | 51 | 291 | 1 | 210 | glycosyl hydrolase family 16. The O-Glycosyl hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A glycosyl hydrolase classification system based on sequence similarity has led to the definition of more than 95 different families inlcuding glycosyl hydrolase family 16. Family 16 includes lichenase, xyloglucan endotransglycosylase (XET), beta-agarase, kappa-carrageenase, endo-beta-1,3-glucanase, endo-beta-1,3-1,4-glucanase, and endo-beta-galactosidase, all of which have a conserved jelly roll fold with a deep active site channel harboring the catalytic residues. |
cd08023 | GH16_laminarinase_like | 1.28e-21 | 139 | 291 | 75 | 235 | Laminarinase, member of the glycosyl hydrolase family 16. Laminarinase, also known as glucan endo-1,3-beta-D-glucosidase, is a glycosyl hydrolase family 16 member that hydrolyzes 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans such as laminarins, curdlans, paramylons, and pachymans, with very limited action on mixed-link (1,3-1,4-)-beta-D-glucans. |
cd02178 | GH16_beta_agarase | 1.51e-17 | 28 | 292 | 1 | 258 | Beta-agarase, member of glycosyl hydrolase family 16. Beta-agarase is a glycosyl hydrolase family 16 (GH16) member that hydrolyzes the internal beta-1,4-linkage of agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea, marine red algae. Agarose is a linear chain of galactose units linked by alternating L-alpha-1,3- and D-beta-1,4-linkages that are additionally modified by a 3,6-anhydro-bridge. Agarose forms thermo-reversible gels that are widely used in the food industry or as a laboratory medium. While beta-agarases are also found in two other families derived from the sequence-based classification of glycosyl hydrolases (GH50, and GH86) the GH16 members are most abundant. This domain adopts a curved beta-sandwich conformation, with a tunnel-shaped active site cavity, referred to as a jellyroll fold. |
pfam00722 | Glyco_hydro_16 | 1.12e-08 | 137 | 287 | 27 | 166 | Glycosyl hydrolases family 16. |
COG2273 | BglS | 2.24e-08 | 12 | 291 | 20 | 263 | Beta-glucanase, GH16 family [Carbohydrate transport and metabolism]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AVM42672.1 | 2.70e-143 | 36 | 447 | 59 | 490 |
QJC21524.1 | 8.68e-62 | 39 | 292 | 19 | 279 |
AIE83322.1 | 8.44e-59 | 1 | 335 | 7 | 353 |
AJC70391.1 | 5.21e-58 | 37 | 295 | 47 | 312 |
AZR06925.1 | 1.01e-57 | 37 | 295 | 47 | 312 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1UPS_A | 2.36e-45 | 32 | 292 | 17 | 278 | GlcNAc[alpha]1-4Galreleasing endo-[beta]-galactosidase from Clostridium perfringens [Clostridium perfringens],1UPS_B GlcNAc[alpha]1-4Gal releasing endo-[beta]-galactosidase from Clostridium perfringens [Clostridium perfringens] |
3AZX_A | 1.82e-15 | 45 | 292 | 10 | 255 | Crystalstructure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZX_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZY_A Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZY_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZY_C Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZY_D Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZZ_A Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone [Thermotoga maritima MSB8],3AZZ_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone [Thermotoga maritima MSB8],3AZZ_C Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone [Thermotoga maritima MSB8],3AZZ_D Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone [Thermotoga maritima MSB8],3B00_A Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with cetyltrimethylammonium bromide [Thermotoga maritima MSB8],3B00_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with cetyltrimethylammonium bromide [Thermotoga maritima MSB8],3B00_C Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with cetyltrimethylammonium bromide [Thermotoga maritima MSB8],3B00_D Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with cetyltrimethylammonium bromide [Thermotoga maritima MSB8],3B01_A Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3B01_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3B01_C Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3B01_D Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8] |
4DFS_A | 5.59e-15 | 45 | 292 | 18 | 263 | Structureof the catalytic domain of an endo-1,3-beta-glucanase (laminarinase) from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],4DFS_B Structure of the catalytic domain of an endo-1,3-beta-glucanase (laminarinase) from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1] |
5WUT_A | 5.58e-10 | 140 | 292 | 79 | 235 | Crystalstructure of laminarinase from Flavobacterium sp. UMI-01 [Flavobacterium sp.],5WUT_B Crystal structure of laminarinase from Flavobacterium sp. UMI-01 [Flavobacterium sp.] |
4BOW_A | 9.76e-10 | 134 | 292 | 86 | 256 | Crystalstructure of LamA_E269S from Z. galactanivorans in complex with laminaritriose and laminaritetraose [Zobellia galactanivorans],4BOW_B Crystal structure of LamA_E269S from Z. galactanivorans in complex with laminaritriose and laminaritetraose [Zobellia galactanivorans],4BPZ_A Crystal structure of lamA_E269S from Zobellia galactanivorans in complex with a trisaccharide of 1,3-1,4-beta-D-glucan. [Zobellia galactanivorans],4BPZ_B Crystal structure of lamA_E269S from Zobellia galactanivorans in complex with a trisaccharide of 1,3-1,4-beta-D-glucan. [Zobellia galactanivorans] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P23903 | 3.88e-08 | 35 | 292 | 414 | 680 | Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1 |
C1IE32 | 4.86e-08 | 134 | 265 | 92 | 220 | Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1 |
A3DBX3 | 5.72e-07 | 128 | 291 | 90 | 243 | Beta-glucanase OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=licB PE=1 SV=1 |
Q84C00 | 7.60e-07 | 128 | 291 | 90 | 243 | Beta-glucanase OS=Acetivibrio thermocellus OX=1515 GN=licB PE=1 SV=1 |
P45798 | 1.36e-06 | 134 | 292 | 109 | 283 | Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.002101 | 0.599769 | 0.394043 | 0.002899 | 0.000746 | 0.000408 |
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