CAZyme Information: MGYG000000273_01547

Basic Information

• Species: Phocaeicola coprophilus
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola coprophilus
• CAZyme ID: MGYG000000273_01547
• CAZy Family: GH16
• CAZyme Description: Keratan-sulfate endo-1,4-beta-galactosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
267		31076.35	5.9688

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000273	3492533	Isolate	China	Asia

• Gene Location: Start: 74213; End: 75016 Strand: +

Full Sequence      

MKKLFLWVMVVLGWGGMISCLSPQKTSDWKLVWEDDFEGSGFDTLTWSKIPRWTPEWARH
MSDNEVCYEVKNGHLILKGVMNPDRNADTARFITGGVYTKYKKAFHGGRLEIRAKLQGAR
GAWPAIWLKPFEEEKYKWPSGGEIDIMERLNHDTIVYQTVHSVYTQHLNIRNNPPQGGTA
AIRPDDYNVYAVEMYPDSVVFFVNDRRTFAYPKIETDKEGQFPFDKPYYLLVDMQLEGGW
VGPVDTLDLPVEMSVDWVRYYQRDSKE

Enzyme Prediction     

No EC number prediction in MGYG000000273_01547.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	33	261	1.1e-50	0.9956521739130435

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08023	GH16_laminarinase_like	1.48e-69	33	261	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	3.82e-22	35	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.
cd02182	GH16_Strep_laminarinase_like	7.45e-21	29	262	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	1.40e-20	22	265	34	269	Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].
pfam00722	Glyco_hydro_16	9.51e-13	102	259	28	168	Glycosyl hydrolases family 16.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRO23309.1	2.55e-209	1	267	1	267
QUT87873.1	5.43e-117	8	262	5	256
QJR58998.1	5.43e-117	8	262	5	256
AII62548.1	5.43e-117	8	262	5	256
QJR56204.1	5.43e-117	8	262	5	256

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6T2R_AAA	8.09e-117	19	262	19	262	ChainAAA, Beta-glycosidase [Bacteroides caccae]
4DFS_A	6.48e-29	24	262	13	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	1.01e-28	24	262	5	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]
3ILN_A	1.25e-28	29	262	5	248	ChainA, Laminarinase [Rhodothermus marinus],3ILN_B Chain B, Laminarinase [Rhodothermus marinus]
5WUT_A	9.20e-28	30	262	6	235	Crystalstructure of laminarinase from Flavobacterium sp. UMI-01 [Flavobacterium sp.],5WUT_B Crystal structure of laminarinase from Flavobacterium sp. UMI-01 [Flavobacterium sp.]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9ZG90	6.79e-44	26	262	53	288	Keratan-sulfate endo-1,4-beta-galactosidase OS=Sphingobacterium multivorum OX=28454 PE=1 SV=1
P45798	8.54e-32	17	262	28	283	Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1
P23903	6.65e-22	31	262	425	680	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
Q27082	1.74e-18	10	262	8	253	Clotting factor G alpha subunit OS=Tachypleus tridentatus OX=6853 PE=1 SV=1
Q8N0N3	7.02e-08	104	205	143	253	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
0.002713	0.918679	0.077759	0.000317	0.000257	0.000243

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000273_01547.