CAZyme Information: MGYG000003362_02613

Basic Information

• Species: Dysgonomonas sp900079735
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae; Dysgonomonas; Dysgonomonas sp900079735
• CAZyme ID: MGYG000003362_02613
• CAZy Family: GH16
• CAZyme Description: Beta-glucanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
269	MGYG000003362_16|CGC6	30886.84	7.0698

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003362	3888864	MAG	United States	North America

• Gene Location: Start: 229184; End: 229993 Strand: +

Full Sequence      

MNHYIQKGIILIALILFILPKSLSSQSGDWKLVWSDEFEYRGLPDSTKWSFDTHGNSYGW
GNNELQWYTDRNINNARVCNGVLRITALKEESNGKQYTSARLRTKGKGDWLYGKVEVSAK
LPTGRGTWPAIWMLPTESKYGGWPRCGEIDIMEHVGFSPDSVFSTVHTETYNHTKGTQVG
KSIHAPLVTDRFHVYTMEWNEHQIRSYIDGIHYFTFNKQEGIDAWPFDQPFHLLLNLAIG
GGLGGIKGVDNTLFPHYFDIDYVRIYQKE

Enzyme Prediction     

EC	3.2.1.73	3.2.1.39

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	34	266	5.7e-86	0.9956521739130435

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08023	GH16_laminarinase_like	5.51e-87	34	266	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	2.06e-39	32	232	1	267	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	2.70e-37	30	225	2	214	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	9.56e-33	29	232	40	234	Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].
cd00413	Glyco_hydrolase_16	1.61e-25	36	266	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QIK58538.1	1.69e-127	30	269	33	273
QGY45605.1	1.07e-119	29	269	34	275
BAR47759.1	3.47e-114	27	269	40	283
QCY58138.1	8.43e-114	22	268	29	276
QUT52130.1	8.43e-114	22	268	29	276

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3ILN_A	8.40e-95	30	267	5	248	ChainA, Laminarinase [Rhodothermus marinus],3ILN_B Chain B, Laminarinase [Rhodothermus marinus]
6XOF_A	3.87e-72	29	268	23	268	ChainA, GH16 family protein [uncultured bacterium]
6XQF_A	2.20e-71	29	268	23	268	ChainA, GH16 family protein [uncultured bacterium],6XQG_A Chain A, GH16 family protein [uncultured bacterium],6XQH_A Chain A, GH16 family protein [uncultured bacterium],6XQL_A Chain A, GH16 family protein [uncultured bacterium],6XQM_A Chain A, GH16 family protein [uncultured bacterium]
5WUT_A	1.23e-62	31	267	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.]
4DFS_A	2.08e-60	29	269	17	265	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P45798	1.28e-94	24	267	34	283	Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1
C1IE32	5.39e-46	28	264	18	265	Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1
P23903	6.60e-45	32	269	425	682	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
Q9ZG90	2.77e-43	29	267	55	288	Keratan-sulfate endo-1,4-beta-galactosidase OS=Sphingobacterium multivorum OX=28454 PE=1 SV=1
Q27082	4.01e-43	25	267	20	253	Clotting factor G alpha subunit OS=Tachypleus tridentatus OX=6853 PE=1 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
0.000202	0.999201	0.000158	0.000145	0.000136	0.000131

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003362_02613.