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CAZyme Information: MGYG000001735_00059

You are here: Home > Sequence: MGYG000001735_00059

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
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides;
CAZyme ID MGYG000001735_00059
CAZy Family GH16
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
392 MGYG000001735_1|CGC2 45196.33 6.4412
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001735 5309957 MAG Sweden Europe
Gene Location Start: 88932;  End: 90110  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001735_00059.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH16 43 281 1.1e-61 0.995850622406639

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00413 Glyco_hydrolase_16 1.65e-49 44 281 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 4.29e-33 42 281 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.
cd02178 GH16_beta_agarase 8.60e-18 44 282 27 258
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 1.32e-15 133 232 32 125
Glycosyl hydrolases family 16.
COG2273 BglS 1.11e-09 134 290 118 274
Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUT50278.1 5.44e-261 1 391 1 391
AWS25493.1 7.19e-112 15 387 232 603
ASY50995.1 7.19e-112 15 387 232 603
QCJ40812.1 3.11e-80 29 376 114 483
AIF44579.1 3.55e-77 29 378 111 482

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1UPS_A 1.35e-40 24 317 16 321
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]
5WUT_A 9.63e-17 36 282 3 235
Crystalstructure of laminarinase from Flavobacterium sp. UMI-01 [Flavobacterium sp.],5WUT_B Crystal structure of laminarinase from Flavobacterium sp. UMI-01 [Flavobacterium sp.]
2VY0_A 2.44e-15 33 281 8 259
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]
3AZX_A 3.47e-13 36 282 8 255
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 1.09e-12 36 282 16 263
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O33680 4.38e-10 124 281 308 457
Endo-1,3-1,4-beta-glycanase ExsH OS=Rhizobium meliloti (strain 1021) OX=266834 GN=exsH PE=1 SV=1
Q84C00 8.84e-10 134 281 103 243
Beta-glucanase OS=Acetivibrio thermocellus OX=1515 GN=licB PE=1 SV=1
A3DBX3 5.06e-09 134 281 103 243
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
Q9Z3Q2 1.78e-08 124 276 308 460
Endo-1,3-1,4-beta-glycanase EglC OS=Rhizobium meliloti (strain 1021) OX=266834 GN=eglC PE=3 SV=2
P23903 2.98e-08 37 283 422 681
Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1

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
0.000334 0.998944 0.000257 0.000158 0.000151 0.000138

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001735_00059.