CAZyme Information: MGYG000004055_01172

Basic Information

• Species: Eubacterium_G sp900548465
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eubacterium_G; Eubacterium_G sp900548465
• CAZyme ID: MGYG000004055_01172
• CAZy Family: GH16
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
610	MGYG000004055_6|CGC2	68613.51	9.9579

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004055	2465387	MAG	United Kingdom	Europe

• Gene Location: Start: 43689; End: 45521 Strand: +

Full Sequence      

MRHTFRKILAGTLAVAMVVQVGVFSKHETSDVQAVDNWKLVWSDEFNGTSLDTSVWSYEI
GNGRDGWGNWEVEYYTNRTDNVRVSGGNLQIIAKKENYGGKQYTSGRILTKGKKWFKYGK
MVARIKVENGNQNGVWPAYWMMGENMNEGVSWPQCGEIDIMEHANSNNYLGGCLHWNYEG
INGSWDKHGSYGSGDAGKDYHFADGDSIENWHEYGLIWDENHMEWQVDGKTYFQQDITDN
NAYCFQKAQFFLFNLAIGGTGSGYTNYITADPNTFKTTTMYVDYLRVYQKSNGADQKETT
KTPTTPTTTKKQPTTQPVETVTKVSKVYTDLVADTNQVFGTYFDGLNGNWGGGVTGSVTN
ATNKGITVKLNKTGNNRWAAQTYIGPLTYYPGYTYKYNATITSDKDRTIVVKVVGNDDGM
HDSPKLKDETITVKAGKPYRLSMDVTIPSDYKSELYLYYGLGKGDGDTIGSEQQNIITIS
DVSFLTTRQVIESETVPQTIPQTTNKTTGKVTNPQTTKLLSTTVVKKATKKKKSKKISLR
FNRVQGAKKYQVQVAKNKKFTKVIAIKVVNKYKKVTISKKVFKKSKRLYVRVRAVGCNKW
SKAKKVKITV

Enzyme Prediction     

No EC number prediction in MGYG000004055_01172.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	42	288	2.2e-69	0.9956521739130435

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08023	GH16_laminarinase_like	2.69e-76	42	288	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.
cd02182	GH16_Strep_laminarinase_like	1.07e-46	38	289	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.
COG2273	BglS	1.07e-31	29	292	32	269	Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].
cd08024	GH16_CCF	1.03e-30	40	289	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.
cd00413	Glyco_hydrolase_16	2.83e-29	44	288	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
CUU48455.1	3.35e-67	29	289	24	264
QOS82717.1	4.98e-67	34	292	22	259
AGF56052.1	6.42e-67	6	295	4	270
AKU79213.1	2.49e-66	34	294	30	269
QLG40917.1	2.56e-66	34	292	33	270

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JH5_A	3.28e-52	35	292	1	235	Structureof Marine bacterial laminarinase [Aquimarina]
6JHJ_A	2.40e-51	35	292	1	235	Structureof Marine bacterial laminarinase mutant-E135A [Aquimarina],6JIA_A Marine bacterial laminarinase mutant E135A complex with laminaritetraose [Aquimarina sp.],6M6P_A Structure of Marine bacterial laminarinase mutant E135A in complex with 1,3-beta-cellotriosyl-glucose [Aquimarina sp.]
4CRQ_A	9.30e-51	37	290	2	232	Crystalstructure of the catalytic domain of the modular laminarinase ZgLamC mutant E142S [Zobellia galactanivorans],4CRQ_B Crystal structure of the catalytic domain of the modular laminarinase ZgLamC mutant E142S [Zobellia galactanivorans],4CTE_A Crystal structure of the catalytic domain of the modular laminarinase ZgLamC mutant E142S in complex with a thio-oligosaccharide [Zobellia galactanivorans],4CTE_B Crystal structure of the catalytic domain of the modular laminarinase ZgLamC mutant E142S in complex with a thio-oligosaccharide [Zobellia galactanivorans]
4DFS_A	9.42e-49	31	292	11	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	2.09e-48	31	292	3	258	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q27082	4.55e-42	38	292	25	256	Clotting factor G alpha subunit OS=Tachypleus tridentatus OX=6853 PE=1 SV=1
P23903	1.99e-37	34	290	419	681	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
P45798	7.74e-36	37	289	39	283	Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1
C1IE32	1.11e-27	38	286	20	265	Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1
Q9ZG90	6.01e-17	34	293	52	295	Keratan-sulfate endo-1,4-beta-galactosidase OS=Sphingobacterium multivorum OX=28454 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
0.001306	0.997682	0.000366	0.000257	0.000190	0.000178

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004055_01172.