CAZyme Information: MGYG000004006_00362

Basic Information

• Species: Alistipes sp000434235
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp000434235
• CAZyme ID: MGYG000004006_00362
• CAZy Family: GH16
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
489	MGYG000004006_1|CGC3	54365.87	4.2556

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004006	2755781	MAG	United Kingdom	Europe

• Gene Location: Start: 382090; End: 383559 Strand: +

Full Sequence      

MSQFKHSICQMATLGWWLMLSLAAVSCNDDDQSGGQLAAPTTMLTANSIGIDRFGIYWNS
VSGADSYEIRLNDEVLTTVQATEYTFTGLTEATTYTAGVRALSDTAEASEWSEIRVKTYS
SSEVTRLDTPTLTAPTSSVTQTGFTVAWEAVEHADYYTWTLDGGQETSTEELQVTCSQLN
PATTYTVRVRAESRVGSYAASEWSEIRVRTGSAESGSTDAPEGYRLVWSDEFDGNSLDES
IWNIEVNGSGGGNNELQYYCEKGVSVGVEPKSGRNCLILTATRENYQNKQFTSGRINSKG
KYSFTYGRLDAMIRMPKTANGLWPAFWLMGDDYGQVGWPACGETDIVEMGHATGMAQGTQ
DRFFNGACHWGPAWNNKGDYSRDTTAPYGMQDDFHLYTCIWTEDELAMYYDLDEDPNREP
YFRMTITRTAGYESNELHVGNYFHKPNFILFNLAVGGNFPGIYNTAQITALNDGPASMYV
DYVRLYVKE

Enzyme Prediction     

No EC number prediction in MGYG000004006_00362.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	228	486	4.1e-68	0.9956521739130435

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08023	GH16_laminarinase_like	3.71e-73	228	486	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	1.19e-33	223	487	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.
cd08024	GH16_CCF	7.31e-29	226	486	1	329	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.
COG2273	BglS	9.84e-23	209	487	26	264	Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].
cd00413	Glyco_hydrolase_16	4.78e-22	230	486	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
QIU93827.1	3.51e-99	205	488	32	313
BCS85795.1	2.01e-73	222	489	21	274
AEF82958.1	1.58e-64	214	488	35	315
QQO09996.1	1.46e-62	292	489	33	223
ASB49870.1	7.46e-58	224	489	25	275

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5NBO_A	3.48e-50	226	485	36	271	Bacteroidesovatus mixed linkage glucan PUL (MLGUL) GH16 [Bacteroides ovatus],5NBO_B Bacteroides ovatus mixed linkage glucan PUL (MLGUL) GH16 [Bacteroides ovatus],5NBP_A Bacteroides ovatus mixed linkage glucan PUL (MLGUL) GH16 in complex with G4G4G3G Product [Bacteroides ovatus],5NBP_B Bacteroides ovatus mixed linkage glucan PUL (MLGUL) GH16 in complex with G4G4G3G Product [Bacteroides ovatus],6VHO_AAA Chain AAA, Glycosyl hydrolase family 16 [Bacteroides ovatus ATCC 8483],6VHO_BBB Chain BBB, Glycosyl hydrolase family 16 [Bacteroides ovatus ATCC 8483]
7KR6_AAA	2.61e-49	226	485	36	271	ChainAAA, Glycoside hydrolase family 16 protein [Bacteroides ovatus],7KR6_BBB Chain BBB, Glycoside hydrolase family 16 protein [Bacteroides ovatus]
4DFS_A	7.61e-43	219	486	13	262	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	8.69e-43	219	486	5	254	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]
6JH5_A	5.83e-40	222	488	2	233	Structureof Marine bacterial laminarinase [Aquimarina]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P45798	6.37e-33	218	486	34	282	Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1
P23903	4.02e-32	223	489	422	682	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
Q27082	1.62e-28	224	486	25	252	Clotting factor G alpha subunit OS=Tachypleus tridentatus OX=6853 PE=1 SV=1
C1IE32	3.16e-27	226	461	22	242	Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1
Q9ZG90	6.34e-18	218	486	50	287	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 LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000589	0.058907	0.940283	0.000090	0.000069	0.000054

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004006_00362.