CAZyme Information: MGYG000004443_01333

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Coprobacteraceae
• CAZyme ID: MGYG000004443_01333
• CAZy Family: GH16
• CAZyme Description: Keratan-sulfate endo-1,4-beta-galactosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
277	MGYG000004443_53|CGC1	31939.3	5.423

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004443	2430140	MAG	Israel	Asia

• Gene Location: Start: 4454; End: 5287 Strand: -

Full Sequence      

MINLSLYIKKTDNMKTNKFISFMAIALCMVVFTGCRSQEKWQLVWEEDFDKEGVIDESVW
SKIPRGSSDWNKYMSDYDALYDVKDGNLILTGMVNPGIPGDTVPYITGGIHTRDKKGFEN
GKIEIRAKLGNAQGAWPAFWLLPFDNGRWPYGGEIDIMERLNSDTIAYQTVHSHYTYNLK
MGNNPKQGATGPIRKDDYNIYSVELYADSLVFSINGKHTFTYPRIETDKEGQFPFDRSFY
LMLDMQLEGSWVGKADPKDLPVSMYIDWVRFYQKPEK

Enzyme Prediction     

No EC number prediction in MGYG000004443_01333.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	45	272	1.5e-53	0.9956521739130435

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08023	GH16_laminarinase_like	5.84e-76	45	272	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.
cd00413	Glyco_hydrolase_16	9.57e-25	47	272	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	2.99e-20	41	273	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	1.67e-19	41	272	41	263	Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].
pfam00722	Glyco_hydro_16	7.00e-16	108	270	23	168	Glycosyl hydrolases family 16.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCT76409.1	8.55e-125	14	274	1	262
CAH09812.1	8.55e-125	14	274	1	262
QUU04914.1	1.21e-124	14	274	1	262
CBW24642.1	1.21e-124	14	274	1	262
BAD51076.1	1.21e-124	14	274	1	262

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6T2R_AAA	7.40e-101	40	273	28	262	ChainAAA, Beta-glycosidase [Bacteroides caccae]
4DFS_A	1.48e-30	39	273	16	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]
3AZX_A	2.31e-30	39	273	8	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]
4CRQ_A	5.11e-30	39	274	1	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]
3ILN_A	2.99e-29	41	273	5	248	ChainA, Laminarinase [Rhodothermus marinus],3ILN_B Chain B, Laminarinase [Rhodothermus marinus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9ZG90	1.35e-48	41	275	56	290	Keratan-sulfate endo-1,4-beta-galactosidase OS=Sphingobacterium multivorum OX=28454 PE=1 SV=1
P45798	1.63e-30	14	273	13	283	Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1
P23903	1.62e-23	43	274	425	681	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
Q27082	4.54e-22	23	273	2	253	Clotting factor G alpha subunit OS=Tachypleus tridentatus OX=6853 PE=1 SV=1
Q8N0N3	5.17e-10	47	250	90	303	Beta-1,3-glucan-binding protein OS=Penaeus monodon OX=6687 PE=2 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
0.002324	0.257296	0.739963	0.000127	0.000169	0.000116

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004443_01333.