CAZyme Information: MGYG000002585_00997

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides
• CAZyme ID: MGYG000002585_00997
• CAZy Family: GH16
• CAZyme Description: Beta-glucanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
288	MGYG000002585_16|CGC1	33335.82	7.1942

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002585	2701793	MAG	China	Asia

• Gene Location: Start: 13181; End: 14047 Strand: +

Full Sequence      

MLRKHSKRKMMFALLAWCALASVSAQEWKLVWSEEFNKKGRLNEATWNYENGYARNEEAQ
WYQPDNAFCKGGKLIIEARKEHRENPLYEAGSRDWRKKREFVEYTSSSVTTAGKFEFLYG
RLEVRAKIPTAGGAWPAIWLLGRDLPWPSCGEIDVMEYYRIKGVPHILANACWGGEKGHG
AVWNSKTVPFTHFTDRDPHWADKFHIWRMDWDETAIKIYLDDELLNDIPLSKTVNGSSAG
EGINPFHKPQYILLNLAIGGLNGGEIDDNALPMRYEVDYVRVYQKEHF

Enzyme Prediction     

No EC number prediction in MGYG000002585_00997.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	32	283	6.4e-65	0.9956521739130435

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08023	GH16_laminarinase_like	7.66e-82	32	283	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.
cd08024	GH16_CCF	4.24e-35	30	284	1	330	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.
cd02182	GH16_Strep_laminarinase_like	1.82e-29	28	284	2	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.
cd00413	Glyco_hydrolase_16	3.49e-27	34	283	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.
COG2273	BglS	1.52e-25	15	283	21	263	Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDO67480.1	1.64e-155	27	286	24	283
ANU56235.1	2.44e-149	20	286	20	286
QQR18927.1	2.44e-149	20	286	20	286
QUU07365.1	1.12e-147	20	286	20	286
QRP56726.1	1.12e-147	20	286	20	286

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6T2N_AAA	1.07e-48	4	287	17	307	ChainAAA, Glycoside hydrolase family 16 protein [Akkermansia muciniphila],6T2N_BBB Chain BBB, Glycoside hydrolase family 16 protein [Akkermansia muciniphila]
4DFS_A	1.32e-48	26	287	16	266	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	3.01e-48	26	284	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]
5WUT_A	5.77e-45	29	284	6	235	Crystalstructure of laminarinase from Flavobacterium sp. UMI-01 [Flavobacterium sp.],5WUT_B Crystal structure of laminarinase from Flavobacterium sp. UMI-01 [Flavobacterium sp.]
6JH5_A	4.42e-43	26	285	2	233	Structureof Marine bacterial laminarinase [Aquimarina]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P45798	9.53e-39	22	284	34	283	Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1
P23903	1.58e-33	30	286	425	682	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
Q27082	3.06e-29	27	284	24	253	Clotting factor G alpha subunit OS=Tachypleus tridentatus OX=6853 PE=1 SV=1
Q9ZG90	1.98e-27	22	284	50	288	Keratan-sulfate endo-1,4-beta-galactosidase OS=Sphingobacterium multivorum OX=28454 PE=1 SV=1
Q8N0N3	6.56e-26	105	263	132	305	Beta-1,3-glucan-binding protein OS=Penaeus monodon OX=6687 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000483	0.998777	0.000188	0.000196	0.000172	0.000164

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002585_00997.