CAZyme Information: MGYG000000139_00150

Basic Information

• Species: Eubacterium_G sp000434315
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eubacterium_G; Eubacterium_G sp000434315
• CAZyme ID: MGYG000000139_00150
• CAZy Family: GH16
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
876	MGYG000000139_1|CGC3	97975.95	9.3229

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000139	2758071	Isolate	United Kingdom	Europe

• Gene Location: Start: 157111; End: 159741 Strand: +

Full Sequence      

MKRNYVKRFMSVVLAIALVLTTIGTTGLFIAKDVTDVSAAATVVTSMDYFSANDGPTIKH
SGVGTVSYGFVMPKFNGKDSSELSIADVKDDIQVYVKQESGTNGEWKKIEDVSYFKWNDT
WAWEHQSWGGWVCWMKLTETTYFRFHGKTNDINCDYLLELEKLPKYKLSAISTTEADIKA
DTTGGSATHWGAWTFNGDKNIKYEQVQDDINITVDNNDGKGFVQFLSNAGSGFRWDQNFG
YYTDGDGGYWFTNINWSFTLRFASKSNPSVYQDVKVTYTKPERTNYKLTAFGGTTLDASA
SATASVGVPLPKIGGTEPVKDDLDLFKYEIKVDGKWLPLTDVAATGWVYEGSGYNKYSLS
SQWGYFVDHVYGLWFQPVREDTEIKITYPIDGKKGGDASNNYVLYTIKGNTSYSPTLPED
MTDIKIQDSSDSYTPDGWKMIFNDEFDGTSLDTSKWSYDEGFLLDENDINTAGWGNQELE
YYTRDNVSVKEGALNINMKKQLKEFTQKNDSSKKATAQYSSGKITTKDKFSVKYGRVDFR
AKMPIGTGVWPAMWMLPNDSRYGSWPLSGEIDVFEGRGRTPNMVFGTLHYGAQWPDNINM
SDAFNITRDGYKKTGIDDWHVYSVQWDAQNIKIYCDGKCYFKCTYAEWFSGSDRGNAYAP
FDQRFYLILNLAAGGTFDSGYVPDSSFTSGTMLVDYVRVYQRMVKAGENEEPDKNPGVST
DGAKDGLYGDYKLGTGSTPIEKPTTGTAENPTSSNNNGSSNITNNNGNSANKSSQSVQGQ
SGSSSRVLGVTSIKKATKKKASSKIKLTFKKVLGASKYQVQISTTKKFKKILVKKTVKKV
RLTIKSKKLKNKKKLYVRVRAFGAAKWSKIKKVKIK

Enzyme Prediction     

No EC number prediction in MGYG000000139_00150.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	443	700	1.3e-72	0.991304347826087

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08023	GH16_laminarinase_like	2.31e-80	442	700	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	3.90e-50	440	701	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	1.07e-34	437	701	1	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.
cd02179	GH16_beta_GRP	1.05e-29	440	700	1	320	beta-1,3-glucan recognition protein, member of glycosyl hydrolase family 16. Beta-GRP (beta-1,3-glucan recognition protein) is one of several 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. They are present in insects and lack all catalytic residues. This subgroup also contains related proteins of unknown function that still contain the active site. 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	3.40e-27	444	700	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
QJU43053.1	2.36e-193	46	715	95	746
QSX02439.1	2.36e-193	46	715	95	746
QCJ05886.1	2.36e-193	46	715	95	746
QGH23594.1	3.34e-193	46	715	95	746
QGH27640.1	3.34e-193	46	715	95	746

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4DFS_A	4.23e-46	438	716	18	267	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	4.87e-46	438	703	10	257	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]
3ILN_A	1.28e-45	438	701	5	248	ChainA, Laminarinase [Rhodothermus marinus],3ILN_B Chain B, Laminarinase [Rhodothermus marinus]
5WUT_A	3.42e-44	437	701	4	235	Crystalstructure of laminarinase from Flavobacterium sp. UMI-01 [Flavobacterium sp.],5WUT_B Crystal structure of laminarinase from Flavobacterium sp. UMI-01 [Flavobacterium sp.]
4CRQ_A	3.02e-41	438	702	3	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P23903	6.58e-187	7	701	9	680	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
P45798	2.25e-43	438	701	40	283	Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1
C1IE32	4.11e-35	438	698	20	265	Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1
Q27082	2.49e-32	438	701	25	253	Clotting factor G alpha subunit OS=Tachypleus tridentatus OX=6853 PE=1 SV=1
Q8N0N3	2.38e-30	440	709	32	343	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
0.217947	0.771306	0.009789	0.000405	0.000266	0.000266

TMHMM  Annotations     

start	end
9	31