CAZyme Information: MGYG000001451_03940

Basic Information

• Species: Paenibacillus_A antibioticophila
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A antibioticophila
• CAZyme ID: MGYG000001451_03940
• CAZy Family: GH16
• CAZyme Description: Glucan endo-1,3-beta-glucosidase A1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
786	MGYG000001451_3|CGC13	85957.02	4.206

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001451	5573040	Isolate	not provided	not provided

• Gene Location: Start: 494602; End: 496962 Strand: -

Full Sequence      

MRRYQQRMLSLILAVVMVAGIGLLPGGKAQAADAGTITSMAYFSAADGPVISKSGVGQAS
YGFVMPVFNGGAATWNQVSGDLGVKVKVAGNWVDIDSAAGYVYNQNWGHWSDGGFNGFWF
TLSATTEIQLYSKANGVTLDYTLVFQNMNTTTITSMTPTQGPGITAGFTGGAGFTYPIFN
NDPAITYEAVADDLKVYVKPVNSNTWIDIDNNAASGWIYDSNFGQFTEGGGGYWFTVTES
IHVKLESKTSSADLIYTITFNEPVRNSYTLTPYEGTTFTANESGSIGLPLPKIDGSAPIA
SELGKFVYEININGQWVELSNSALSGFIYSGNGYNNMSDANQWGYWADYVYGLWFQPIQV
DMQIRIGYPQNGQAGGSVGNNFVYYTFIGNPNAPRPDVTDQEDIEIGTPSNPAIDGMTLV
WQDEFTGTQLDTSKWSYETGYYISDDPNSWGWGNAELEHYTNSEQNVFVQNGVLNIRALN
DPKSFPQDPSRYAQYSSGKINTKDHFTFQYGRVDFRAKLPTGNGIWPALWMLPENSVYGA
WAASGEIDVMEAKGRLPGTTSGAVHFGGQWPVNRYLAGEYYFPEGQTFANDYHVYTLIWE
EDNFKWYVDGKFFFKVTRDQWYSVAAPNNPNAPFDQPFYIIMNLAIGGHFDGGLAPSPSD
IPATMQVDYVRVYNAGSTGGGGENPGPGQGSVIIGDAVRGLKKTDDDLLFYVNGATFADL
HYKINNGGQMNVAMISDGNGNYTYPVNNLQAGDTVEYFFTYNPGQGALDTPWQTYIHGVT
QGVPAE

Enzyme Prediction     

EC	3.2.1.39

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	421	673	3.7e-81	0.9956521739130435
CBM56	697	782	6.8e-34	0.5345911949685535

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08023	GH16_laminarinase_like	3.57e-90	421	673	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.
cd08024	GH16_CCF	8.55e-59	419	673	1	329	Coelomic cytolytic factor, member of glycosyl hydrolase family 16. Subgroup of glucanases of unknown function that are related to beta-GRP (beta-1,3-glucan recognition protein), but contain active site residues. Beta-GRPs are one group of pattern recognition receptors (PRRs), also referred to as biosensor proteins, that complexes with pathogen-associated beta-1,3-glucans and then transduces signals necessary for activation of an appropriate innate immune response. Beta-GRPs are present in insects and lack all catalytic residues. This subgroup contains related proteins that still contain the active site and are widely distributed in eukaryotes. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic residues, like those of other glycosyl hydrolase family 16 members.
cd02182	GH16_Strep_laminarinase_like	2.09e-40	416	674	1	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.
cd02179	GH16_beta_GRP	7.70e-35	419	673	1	320	beta-1,3-glucan recognition protein, member of glycosyl hydrolase family 16. Beta-GRP (beta-1,3-glucan recognition protein) is one of several pattern recognition receptors (PRRs), also referred to as biosensor proteins, that complexes with pathogen-associated beta-1,3-glucans and then transduces signals necessary for activation of an appropriate innate immune response. They are present in insects and lack all catalytic residues. This subgroup also contains related proteins of unknown function that still contain the active site. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic residues, like those of other glycosyl hydrolase family 16 members.
cd00413	Glyco_hydrolase_16	2.56e-30	423	673	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AZS13848.1	0.0	1	782	3	867
QJD86331.1	0.0	3	784	10	874
ANY73748.1	0.0	2	784	11	878
AAC60453.1	0.0	2	784	9	876
BAA04469.1	0.0	2	784	9	876

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4DFS_A	1.40e-50	414	673	15	262	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	1.61e-50	414	673	7	254	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]
2VY0_A	6.34e-50	419	674	15	260	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]
3ATG_A	1.57e-47	419	690	5	253	endo-1,3-beta-glucanasefrom Cellulosimicrobium cellulans [Cellulosimicrobium cellulans]
3ILN_A	2.37e-46	419	673	7	247	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
P23903	0.0	2	673	9	679	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
P45798	2.74e-46	419	673	42	282	Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1
C1IE32	5.27e-41	419	673	22	267	Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1
Q8N0N3	1.77e-31	419	678	32	364	Beta-1,3-glucan-binding protein OS=Penaeus monodon OX=6687 PE=2 SV=1
Q27082	9.91e-30	419	678	27	257	Clotting factor G alpha subunit OS=Tachypleus tridentatus OX=6853 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
0.000388	0.998762	0.000235	0.000232	0.000180	0.000160

TMHMM  Annotations     

start	end
7	26