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CAZyme Information: MGYG000002171_00333

You are here: Home > Sequence: MGYG000002171_00333

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 Phocaeicola sp002493165
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp002493165
CAZyme ID MGYG000002171_00333
CAZy Family GH16
CAZyme Description Keratan-sulfate endo-1,4-beta-galactosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
258 MGYG000002171_4|CGC1 29863.67 5.5199
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002171 3793747 MAG Denmark Europe
Gene Location Start: 25030;  End: 25806  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002171_00333.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH16 27 255 2e-51 0.9956521739130435

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd08023 GH16_laminarinase_like 1.40e-70 27 255 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 8.21e-23 29 255 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.
cd02182 GH16_Strep_laminarinase_like 2.25e-20 22 256 1 259
Streptomyces laminarinase-like, member of glycosyl hydrolase family 16. Proteins similar to Streptomyces sioyaensis beta-1,3-glucanase (laminarinase) present in Actinomycetales as well as Peziomycotina. Laminarinases belong to glycosyl hydrolase family 16 and hydrolyze the glycosidic bond of the 1,3-beta-linked glucan, a major component of fungal and plant cell walls and the structural and storage polysaccharides (laminarin) of marine macro-algae. Members of the GH16 family have a conserved jelly roll fold with an active site channel.
COG2273 BglS 1.42e-17 19 258 37 266
Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].
cd08024 GH16_CCF 3.16e-13 93 233 106 277
Coelomic cytolytic factor, member of glycosyl hydrolase family 16. Subgroup of glucanases of unknown function that are related to beta-GRP (beta-1,3-glucan recognition protein), but contain active site residues. Beta-GRPs are one group of pattern recognition receptors (PRRs), also referred to as biosensor proteins, that complexes with pathogen-associated beta-1,3-glucans and then transduces signals necessary for activation of an appropriate innate immune response. Beta-GRPs are present in insects and lack all catalytic residues. This subgroup contains related proteins that still contain the active site and are widely distributed in eukaryotes. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic residues, like those of other glycosyl hydrolase family 16 members.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUT87873.1 1.59e-169 1 257 1 257
QJR58998.1 1.59e-169 1 257 1 257
AII62548.1 1.59e-169 1 257 1 257
QJR56204.1 1.59e-169 1 257 1 257
QJR75855.1 6.47e-169 1 257 1 257

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6T2R_AAA 2.21e-165 15 257 21 263
ChainAAA, Beta-glycosidase [Bacteroides caccae]
3ILN_A 1.01e-33 21 257 3 249
ChainA, Laminarinase [Rhodothermus marinus],3ILN_B Chain B, Laminarinase [Rhodothermus marinus]
4DFS_A 8.54e-32 23 256 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]
3AZX_A 1.34e-31 23 256 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]
5WUT_A 3.75e-28 22 256 4 235
Crystalstructure of laminarinase from Flavobacterium sp. UMI-01 [Flavobacterium sp.],5WUT_B Crystal structure of laminarinase from Flavobacterium sp. UMI-01 [Flavobacterium sp.]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9ZG90 1.06e-42 23 256 56 288
Keratan-sulfate endo-1,4-beta-galactosidase OS=Sphingobacterium multivorum OX=28454 PE=1 SV=1
P45798 3.20e-33 9 257 18 284
Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1
Q27082 1.33e-21 15 256 17 253
Clotting factor G alpha subunit OS=Tachypleus tridentatus OX=6853 PE=1 SV=1
C1IE32 4.11e-15 17 257 13 269
Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1
Q8N0N3 1.21e-10 93 233 138 303
Beta-1,3-glucan-binding protein OS=Penaeus monodon OX=6687 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000003 0.002865 0.997178 0.000001 0.000001 0.000001

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002171_00333.