CAZyme Information: MGYG000001507_04020

Basic Information

• Species: Paenibacillus ihuae
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus ihuae
• CAZyme ID: MGYG000001507_04020
• CAZy Family: GH16
• CAZyme Description: Beta-glucanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
240	MGYG000001507_1|CGC58	26496.6	8.6993

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001507	6631509	Isolate	not provided	not provided

• Gene Location: Start: 4163334; End: 4164056 Strand: +

Full Sequence      

MKRLKKFCGAGLTLLLVGLLAGAPSVSAATVFYEPLTYFNSATWQKADGYSNGGMFNCTW
RANNVSFTSGGQLRLALTSSSYNKFDGAEYRSTNKYGYGKYEVNMKPAKNSGIVSSFFTY
TGPSDGTPWDEIDIEFLGKDTTKVQFNYYTNGVGGHEKVVDLGFDASQGYHTYAFDWQAG
SIKWYVDGVLKHTATSNIPSRAGKIMMNLWNGTGVDSWLGSYNGANPLYAYYDWLKYTGN

Enzyme Prediction     

No EC number prediction in MGYG000001507_04020.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	37	235	8e-90	0.9757281553398058

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02175	GH16_lichenase	9.74e-120	32	238	1	211	lichenase, member of glycosyl hydrolase family 16. Lichenase, also known as 1,3-1,4-beta-glucanase, is a member of glycosyl hydrolase family 16, that specifically cleaves 1,4-beta-D-glucosidic bonds in mixed-linked beta glucans that also contain 1,3-beta-D-glucosidic linkages. Natural substrates of beta-glucanase are beta-glucans from grain endosperm cell walls or lichenan from the Islandic moss, Cetraria islandica. This protein is found not only in bacteria but also in anaerobic fungi. This domain includes two seven-stranded antiparallel beta-sheets that are adjacent to one another forming a compact, jellyroll beta-sandwich structure.
COG2273	BglS	5.45e-59	28	234	43	261	Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].
cd00413	Glyco_hydrolase_16	2.68e-50	40	238	9	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.
pfam00722	Glyco_hydro_16	1.05e-48	60	234	1	166	Glycosyl hydrolases family 16.
cd02176	GH16_XET	3.48e-27	56	218	10	175	Xyloglucan endotransglycosylase, member of glycosyl hydrolase family 16. Xyloglucan endotransglycosylases (XETs) cleave and religate xyloglucan polymers in plant cell walls via a transglycosylation mechanism. Xyloglucan is a soluble hemicellulose with a backbone of beta-1,4-linked glucose units, partially substituted with alpha-1,6-linked xylopyranose branches. It binds noncovalently to cellulose, cross-linking the adjacent cellulose microfibrils, giving it a key structural role as a matrix polymer. Therefore, XET plays an important role in all plant processes that require cell wall remodeling.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSF43970.1	2.42e-180	1	240	1	240
AIQ43119.1	7.71e-168	1	240	1	240
AIQ31818.1	3.14e-167	1	240	1	240
AIQ19991.1	6.59e-164	4	240	2	238
QUL53689.1	1.22e-162	2	240	3	241

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1MAC_A	3.13e-139	30	240	2	212	CrystalStructure And Site-Directed Mutagenesis Of Bacillus Macerans Endo-1,3-1,4-Beta-Glucanase [Paenibacillus macerans],1MAC_B Crystal Structure And Site-Directed Mutagenesis Of Bacillus Macerans Endo-1,3-1,4-Beta-Glucanase [Paenibacillus macerans]
1BYH_A	1.31e-136	32	240	6	214	MOLECULARAND ACTIVE-SITE STRUCTURE OF A BACILLUS (1-3,1-4)-BETA-GLUCANASE [synthetic construct],1GLH_A Cation Binding To A Bacillus (1,3-1,4)-Beta-Glucanase. Geometry, Affinity And Effect On Protein Stability [Paenibacillus macerans],2AYH_A Crystal And Molecular Structure At 1.6 Angstroms Resolution Of The Hybrid Bacillus Endo-1,3-1,4-Beta-D-Glucan 4- Glucanohydrolase H(A16-M) [hybrid]
1U0A_A	1.07e-135	32	240	6	214	ChainA, Beta-glucanase [Paenibacillus macerans],1U0A_B Chain B, Beta-glucanase [Paenibacillus macerans],1U0A_C Chain C, Beta-glucanase [Paenibacillus macerans],1U0A_D Chain D, Beta-glucanase [Paenibacillus macerans]
3O5S_A	3.63e-128	25	238	23	236	CrystalStructure of the endo-beta-1,3-1,4 glucanase from Bacillus subtilis (strain 168) [Bacillus subtilis]
1GBG_A	5.18e-127	32	238	6	212	BacillusLicheniformis Beta-Glucanase [Bacillus licheniformis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P23904	5.10e-139	25	240	22	237	Beta-glucanase OS=Paenibacillus macerans OX=44252 PE=1 SV=2
P45797	6.16e-138	13	240	9	238	Beta-glucanase OS=Paenibacillus polymyxa OX=1406 GN=gluB PE=3 SV=1
P04957	1.13e-127	15	238	15	240	Beta-glucanase OS=Bacillus subtilis (strain 168) OX=224308 GN=bglS PE=1 SV=2
P07980	8.36e-127	1	237	1	236	Beta-glucanase OS=Bacillus amyloliquefaciens OX=1390 GN=bglA PE=3 SV=1
P27051	1.76e-122	3	238	4	241	Beta-glucanase OS=Bacillus licheniformis OX=1402 GN=bg1 PE=1 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
0.000218	0.999154	0.000156	0.000172	0.000137	0.000131

TMHMM  Annotations     

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