CAZyme Information: MGYG000003072_03969

Basic Information

• Species: Paenibacillus amylolyticus
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus amylolyticus
• CAZyme ID: MGYG000003072_03969
• CAZy Family: GH16
• CAZyme Description: Beta-glucanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
237	MGYG000003072_18|CGC3	26775.85	7.874

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003072	7042795	MAG	China	Asia

• Gene Location: Start: 60998; End: 61711 Strand: +

Full Sequence      

MKRKSWYTLAVTGVISLFFSVSAFAGYVFWEPLTYFNASTWQKADGYSNGNMFNCTWRAN
NVNFTSDGKLKLGLTSSAQNKFDCGEYRSTNTYGYGLYEVSMKPAKNTGVVSSFFTYTGP
SHGTQWDEIDIEFLGKDTTKVQFNYYTNGVGNHEKIINLGFDASQGFHTYAFDWQPGHIK
WYVDGVLKHTATSNIPKTPGKIMMNLWNGTGVDSWLGPYNGANPLYAEYDWVKYTSN

Enzyme Prediction     

No EC number prediction in MGYG000003072_03969.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	34	233	3.8e-93	0.9805825242718447

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02175	GH16_lichenase	1.49e-121	29	235	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	5.02e-57	29	234	47	264	Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].
cd00413	Glyco_hydrolase_16	2.37e-53	37	235	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	3.17e-51	57	233	1	168	Glycosyl hydrolases family 16.
cd02176	GH16_XET	8.75e-28	53	215	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
ABD94065.1	2.16e-184	1	237	2	238
APO45948.1	2.95e-184	1	237	1	237
QZN78908.1	4.19e-184	1	237	1	237
QOS82755.1	5.28e-178	1	237	1	237
BAF49082.1	6.40e-177	1	237	2	238

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1MAC_A	2.26e-154	26	237	1	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	7.47e-149	29	237	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	6.13e-148	29	237	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	2.38e-130	29	235	30	236	CrystalStructure of the endo-beta-1,3-1,4 glucanase from Bacillus subtilis (strain 168) [Bacillus subtilis]
1GBG_A	8.34e-130	29	235	6	212	BacillusLicheniformis Beta-Glucanase [Bacillus licheniformis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P45797	2.29e-171	1	237	2	238	Beta-glucanase OS=Paenibacillus polymyxa OX=1406 GN=gluB PE=3 SV=1
P23904	5.35e-163	1	237	1	237	Beta-glucanase OS=Paenibacillus macerans OX=44252 PE=1 SV=2
P04957	5.49e-132	9	235	10	240	Beta-glucanase OS=Bacillus subtilis (strain 168) OX=224308 GN=bglS PE=1 SV=2
P07980	1.29e-127	9	234	14	236	Beta-glucanase OS=Bacillus amyloliquefaciens OX=1390 GN=bglA PE=3 SV=1
P27051	8.55e-127	9	235	11	241	Beta-glucanase OS=Bacillus licheniformis OX=1402 GN=bg1 PE=1 SV=1

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
0.634068	0.358870	0.003529	0.001471	0.000603	0.001456

TMHMM  Annotations     

start	end
7	29