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CAZyme Information: MGYG000000117_00149

You are here: Home > Sequence: MGYG000000117_00149

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Barnesiella sp003150885
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Barnesiellaceae; Barnesiella; Barnesiella sp003150885
CAZyme ID MGYG000000117_00149
CAZy Family GH16
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
484 53622.41 5.0346
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000117 3354558 Isolate Canada North America
Gene Location Start: 147902;  End: 149356  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000117_00149.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH16 141 388 5.8e-34 0.9911504424778761

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd08023 GH16_laminarinase_like 1.23e-21 138 388 1 235
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.
cd00413 Glyco_hydrolase_16 7.80e-18 140 388 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.
TIGR04183 Por_Secre_tail 2.94e-09 408 484 1 72
Por secretion system C-terminal sorting domain. Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.
cd02178 GH16_beta_agarase 1.45e-08 185 388 61 257
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.
cd02177 GH16_kappa_carrageenase 4.84e-08 222 388 94 268
Kappa-carrageenase, member of glycosyl hydrolase family 16. Kappa-carrageenase is a glycosyl hydrolase family 16 (GH16) member that hydrolyzes the internal beta-1,4-linkage of kappa-carrageenans, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea, marine red algae. Carrageenans are linear chains of galactose units linked by alternating D-alpha-1,3- and D-beta-1,4-linkages that are additionally modified by a 3,6-anhydro-bridge. Depending on the position and number of sulfate ester modifications they are subdivided into kappa-, iota-, and lambda-carrageenases, kappa being modified once. Carrageenans form thermo-reversible gels widely used for industrial applications. Kappa-carrageenases exist in bacteria belonging to at least three phylogenetically distant branches, including pseudoalteromonas, planctomycetes, and baceroidetes. This domain adopts a curved beta-sandwich conformation, with a tunnel-shaped active site cavity, referred to as a jellyroll fold.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QVL33586.1 5.96e-150 23 389 217 587
QEH37426.1 3.49e-140 23 388 205 574
QUE50368.1 7.58e-105 23 388 161 519
QGT72065.1 4.26e-92 23 390 46 415
AHF11964.1 2.56e-91 23 394 52 426

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2VY0_A 7.39e-11 187 389 68 260
TheX-ray structure of endo-beta-1,3-glucanase from Pyrococcus furiosus [Pyrococcus furiosus],2VY0_B The X-ray structure of endo-beta-1,3-glucanase from Pyrococcus furiosus [Pyrococcus furiosus]
5OCR_A 5.78e-08 222 391 101 286
Crystalstructure of the kappa-carrageenase zobellia_236 from Zobellia galactanivorans [Zobellia galactanivorans],5OCR_B Crystal structure of the kappa-carrageenase zobellia_236 from Zobellia galactanivorans [Zobellia galactanivorans],5OCR_C Crystal structure of the kappa-carrageenase zobellia_236 from Zobellia galactanivorans [Zobellia galactanivorans],5OCR_D Crystal structure of the kappa-carrageenase zobellia_236 from Zobellia galactanivorans [Zobellia galactanivorans]

Swiss-Prot Hits      help

has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000326 0.998994 0.000177 0.000170 0.000154 0.000148

TMHMM  Annotations      download full data without filtering help

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