CAZyme Information: MGYG000001508_01340

Basic Information

• Species: Thalassobacillus devorans
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales_D; Halobacillaceae; Thalassobacillus; Thalassobacillus devorans
• CAZyme ID: MGYG000001508_01340
• CAZy Family: GH16
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
283	MGYG000001508_5|CGC4	33176.53	4.8387

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001508	4066265	Isolate	not provided	not provided

• Gene Location: Start: 452455; End: 453306 Strand: -

Full Sequence      

MKKIIVVMFTVLIIILFLGWGYFFISNSEANSIKKYSFTSHSLRGEFAKMNYSFITNGWE
LVWHDEFSGNDLNSTYWNLENWPAEKNNELQYYVPQNVLLEDGSLKILSKREDFKGRNYT
SGALHTKGKFSFLYGKAEIRAKLPEGQGLFPAFWMMPDKDNIWLPEIDILEMLGHKTNEI
WMVLHWHDENKQMQNVSASYSGENYAEGFHTFGIEWSPERITWFIDGEERFTTSAFIPEE
QMYLYLNTAIGGDWPGSPDETTVFPQYFIIDYVRVYKKWGGNE

Enzyme Prediction     

No EC number prediction in MGYG000001508_01340.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	63	276	4.4e-68	0.9956521739130435

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08023	GH16_laminarinase_like	3.50e-80	63	276	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.
COG2273	BglS	7.60e-41	59	276	41	263	Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].
cd00413	Glyco_hydrolase_16	3.72e-40	65	276	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.
cd02182	GH16_Strep_laminarinase_like	3.76e-28	58	276	1	258	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.
cd02180	GH16_fungal_KRE6_glucanase	7.05e-26	61	276	1	294	Saccharomyces cerevisiae KRE6 and related glucanses, member of glycosyl hydrolase family 16. KRE6 is a Saccharomyces cerevisiae glucanase that participates in the synthesis of beta-1,6-glucan, a major structural component of the cell wall. It is a golgi membrane protein required for normal beta-1,6-glucan levels in the cell wall. KRE6 is closely realted to laminarinase, 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDP42265.1	2.31e-114	30	280	27	283
QED46832.1	2.09e-112	57	281	69	293
ADU29693.1	4.04e-110	52	278	72	299
BAK15059.1	5.76e-108	59	278	83	302
QTN01430.1	3.55e-104	48	283	47	282

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3AZX_A	9.49e-52	59	277	10	255	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]
4DFS_A	3.27e-51	59	277	18	263	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]
2VY0_A	1.47e-48	59	281	13	264	TheX-ray structure of endo-beta-1,3-glucanase from Pyrococcus furiosus [Pyrococcus furiosus],2VY0_B The X-ray structure of endo-beta-1,3-glucanase from Pyrococcus furiosus [Pyrococcus furiosus]
6JHJ_A	1.74e-44	59	278	4	233	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.]
6JH5_A	2.46e-44	59	278	4	233	Structureof Marine bacterial laminarinase [Aquimarina]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P45798	4.53e-38	59	277	40	283	Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1
Q27082	1.10e-34	59	277	25	253	Clotting factor G alpha subunit OS=Tachypleus tridentatus OX=6853 PE=1 SV=1
P23903	2.13e-34	58	278	422	681	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
C1IE32	1.97e-29	53	282	14	270	Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1
Q9Z3Q2	1.04e-27	76	276	243	457	Endo-1,3-1,4-beta-glycanase EglC OS=Rhizobium meliloti (strain 1021) OX=266834 GN=eglC PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.820417	0.164353	0.013081	0.000475	0.000231	0.001456

TMHMM  Annotations     

start	end
4	26