Species | Phocaeicola plebeius | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola plebeius | |||||||||||
CAZyme ID | MGYG000001364_01554 | |||||||||||
CAZy Family | GH16 | |||||||||||
CAZyme Description | Beta-porphyranase B | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 99486; End: 100451 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH16 | 52 | 314 | 9.6e-100 | 0.99581589958159 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd02178 | GH16_beta_agarase | 1.25e-96 | 27 | 315 | 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. |
cd00413 | Glyco_hydrolase_16 | 3.34e-22 | 53 | 314 | 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 | 2.68e-16 | 53 | 279 | 3 | 203 | 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. |
cd02175 | GH16_lichenase | 1.79e-08 | 51 | 312 | 1 | 209 | lichenase, member of glycosyl hydrolase family 16. Lichenase, also known as 1,3-1,4-beta-glucanase, is a member of glycosyl hydrolase family 16, that specifically cleaves 1,4-beta-D-glucosidic bonds in mixed-linked beta glucans that also contain 1,3-beta-D-glucosidic linkages. Natural substrates of beta-glucanase are beta-glucans from grain endosperm cell walls or lichenan from the Islandic moss, Cetraria islandica. This protein is found not only in bacteria but also in anaerobic fungi. This domain includes two seven-stranded antiparallel beta-sheets that are adjacent to one another forming a compact, jellyroll beta-sandwich structure. |
pfam00722 | Glyco_hydro_16 | 1.02e-06 | 112 | 281 | 18 | 147 | Glycosyl hydrolases family 16. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
EDY95423.1 | 1.36e-247 | 1 | 321 | 1 | 321 |
APA66218.1 | 4.89e-95 | 37 | 320 | 21 | 278 |
CBM41185.1 | 5.38e-92 | 40 | 321 | 24 | 279 |
CAZ97778.1 | 5.38e-92 | 40 | 321 | 24 | 279 |
AXT50215.1 | 2.57e-90 | 37 | 317 | 22 | 278 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4AWD_A | 2.94e-235 | 21 | 321 | 24 | 324 | ChainA, BETA-PORPHYRANASE [Phocaeicola plebeius],4AWD_B Chain B, BETA-PORPHYRANASE [Phocaeicola plebeius] |
3JUU_A | 2.08e-42 | 44 | 317 | 26 | 276 | Crystalstructure of porphyranase B (PorB) from Zobellia galactanivorans [Zobellia galactanivorans],3JUU_B Crystal structure of porphyranase B (PorB) from Zobellia galactanivorans [Zobellia galactanivorans] |
4ATE_A | 2.59e-33 | 36 | 317 | 9 | 262 | Highresolution crystal structure of beta-porphyranase A from Zobellia galactanivorans [Zobellia galactanivorans] |
3ILF_A | 1.56e-30 | 36 | 317 | 11 | 264 | Crystalstructure of porphyranase A (PorA) in complex with neo-porphyrotetraose [Zobellia galactanivorans] |
6HY3_A | 2.61e-18 | 37 | 317 | 22 | 270 | Three-dimensionalstructure of AgaC from Zobellia galactanivorans [Zobellia galactanivorans] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
B5CY92 | 2.73e-248 | 1 | 321 | 1 | 321 | Beta-porphyranase B OS=Phocaeicola plebeius (strain DSM 17135 / JCM 12973 / M2) OX=484018 GN=BACPLE_01689 PE=1 SV=1 |
D7GXG3 | 1.08e-92 | 40 | 321 | 24 | 279 | Beta-porphyranase E OS=Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij) OX=63186 GN=porE PE=3 SV=1 |
D7GXG2 | 1.62e-46 | 24 | 321 | 24 | 310 | Beta-porphyranase D OS=Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij) OX=63186 GN=porD PE=3 SV=1 |
D7GXF9 | 1.13e-41 | 7 | 317 | 7 | 289 | Beta-porphyranase B OS=Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij) OX=63186 GN=porB PE=1 SV=1 |
D7GXG0 | 7.15e-31 | 36 | 317 | 20 | 273 | Beta-porphyranase A OS=Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij) OX=63186 GN=porA PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.002220 | 0.327012 | 0.670119 | 0.000217 | 0.000237 | 0.000173 |
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