CAZyme Information: MGYG000003834_02392

Basic Information

• Species: Eisenbergiella sp900550285
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eisenbergiella; Eisenbergiella sp900550285
• CAZyme ID: MGYG000003834_02392
• CAZy Family: GH16
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
414	MGYG000003834_32|CGC1	45937.63	6.1853

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003834	2806677	MAG	United States	North America

• Gene Location: Start: 20415; End: 21659 Strand: +

Full Sequence      

MKKGKKAMLKKAAAGCTALLLIGGMKATADAAPPAGGSWTLLPAASDEFSGNALDSSKWK
NGIWYDVTTELAFSPDNVKVEDGNLVLEAKKEERNGKLFTAGAVESRFEVPGTDSYVEVR
AKVLDRRANVLSAIWMQSSPLNWAMNPNPEIDIMETFDYSKLTSTLHIWKQSPSIHMQVG
QNRWNTGLSDISADYHTYGLERRDGKMRFYFDGRLAWEKVSSWDSFVELSRHMVLSLEGH
LGHPNEEYLPSAFLVDYVRTYYNSDFAGVPTDGVYRLVNAESGKALAIKPGSTENASQLV
QTSGRGREESWMLKKNPDGTWSLRNMQTGKMADLTADRKVTENGNTVTQYDYHGGVNQKW
YVVPTENGRFKIISALSGKALCVKDAAASDGAPIIQWSWENPSALNDEWYFEGA

Enzyme Prediction     

No EC number prediction in MGYG000003834_02392.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	46	261	2.8e-33	0.991304347826087
CBM13	272	411	1.9e-22	0.6861702127659575

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08023	GH16_laminarinase_like	1.13e-30	46	261	2	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.
cd02178	GH16_beta_agarase	2.80e-29	32	262	12	258	Beta-agarase, member of glycosyl hydrolase family 16. Beta-agarase is a glycosyl hydrolase family 16 (GH16) member that hydrolyzes the internal beta-1,4-linkage of agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea, marine red algae. Agarose is a linear chain of galactose units linked by alternating L-alpha-1,3- and D-beta-1,4-linkages that are additionally modified by a 3,6-anhydro-bridge. Agarose forms thermo-reversible gels that are widely used in the food industry or as a laboratory medium. While beta-agarases are also found in two other families derived from the sequence-based classification of glycosyl hydrolases (GH50, and GH86) the GH16 members are most abundant. This domain adopts a curved beta-sandwich conformation, with a tunnel-shaped active site cavity, referred to as a jellyroll fold.
cd00413	Glyco_hydrolase_16	2.14e-24	47	261	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.
pfam14200	RicinB_lectin_2	8.84e-20	311	397	5	89	Ricin-type beta-trefoil lectin domain-like.
pfam14200	RicinB_lectin_2	6.77e-10	357	412	2	55	Ricin-type beta-trefoil lectin domain-like.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SNV18950.1	4.64e-88	33	414	43	413
QUC07808.1	1.06e-72	13	394	21	393
AAT83769.1	1.24e-69	39	394	40	388
AEH30360.1	1.24e-69	39	394	40	388
QQO76836.1	2.99e-68	39	394	43	390

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6XOF_A	2.22e-15	46	261	29	266	ChainA, GH16 family protein [uncultured bacterium]
6XQF_A	1.01e-14	46	261	29	266	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]
4DFS_A	7.94e-11	50	261	42	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	8.36e-11	50	261	34	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]
5OCQ_A	1.34e-09	36	261	12	270	Crystalstructure of the complex of the kappa-carrageenase from Pseudoalteromonas carrageenovora with an oligotetrasaccharide of kappa-carrageenan [Pseudoalteromonas carrageenovora],5OCQ_B Crystal structure of the complex of the kappa-carrageenase from Pseudoalteromonas carrageenovora with an oligotetrasaccharide of kappa-carrageenan [Pseudoalteromonas carrageenovora]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q27082	1.65e-11	39	308	25	303	Clotting factor G alpha subunit OS=Tachypleus tridentatus OX=6853 PE=1 SV=1
P43478	1.31e-09	19	261	16	294	Kappa-carrageenase OS=Pseudoalteromonas carrageenovora OX=227 GN=cgkA PE=1 SV=1
P45798	2.46e-07	39	261	40	282	Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1
Q84C00	1.34e-06	55	214	45	194	Beta-glucanase OS=Acetivibrio thermocellus OX=1515 GN=licB PE=1 SV=1
D7GXG3	4.32e-06	34	213	24	215	Beta-porphyranase E OS=Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij) OX=63186 GN=porE PE=3 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
0.001666	0.996364	0.000645	0.000543	0.000397	0.000360

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003834_02392.