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CAZyme Information: MGYG000001257_00562

You are here: Home > Sequence: MGYG000001257_00562

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 Massiliomicrobiota sp002160865
Lineage Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Massiliomicrobiota; Massiliomicrobiota sp002160865
CAZyme ID MGYG000001257_00562
CAZy Family GH16
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
606 68102.15 4.4258
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001257 2104226 MAG Austria Europe
Gene Location Start: 4368;  End: 6188  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001257_00562.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH16 254 500 2.8e-92 0.9963503649635036

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd08023 GH16_laminarinase_like 3.77e-79 254 499 1 232
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.
cd02182 GH16_Strep_laminarinase_like 4.16e-39 250 500 2 256
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.
cd08024 GH16_CCF 3.24e-37 253 526 2 318
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.
cd00413 Glyco_hydrolase_16 1.77e-31 256 499 1 207
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.
COG2273 BglS 6.52e-31 255 500 48 261
Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QBJ76369.1 3.33e-229 3 605 144 744
ATD54106.1 3.33e-229 3 605 144 744
SLK22633.1 3.33e-229 3 605 144 744
SQH51259.1 9.40e-95 71 596 29 548
BAM22870.1 9.92e-95 71 596 31 550

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4DFS_A 4.60e-48 253 499 21 259
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 5.30e-48 253 499 13 251
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]
2VY0_A 5.85e-47 246 499 9 256
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]
3ATG_A 1.89e-38 253 499 6 235
endo-1,3-beta-glucanasefrom Cellulosimicrobium cellulans [Cellulosimicrobium cellulans]
2HYK_A 9.67e-38 251 499 8 239
Thecrystal structure of an endo-beta-1,3-glucanase from alkaliphilic Nocardiopsis sp.strain F96 [Nocardiopsis sp. F96]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P23903 2.43e-34 253 499 426 676
Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
P45798 1.21e-30 253 499 43 279
Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1
Q27082 6.75e-26 249 515 24 270
Clotting factor G alpha subunit OS=Tachypleus tridentatus OX=6853 PE=1 SV=1
C1IE32 8.29e-26 254 482 24 242
Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1
Q8N0N3 6.55e-17 253 491 33 315
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 OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000063 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001257_00562.