CAZyme Information: MGYG000003402_03903

Basic Information

• Species: Paenibacillus lactis
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus lactis
• CAZyme ID: MGYG000003402_03903
• CAZy Family: GH16
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
886		96426.88	4.6758

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003402	5924245	MAG	United States	North America

• Gene Location: Start: 28; End: 2688 Strand: +

Full Sequence      

MKRSHYHSTERRFRRKGLGLFLAIVLLVSLGLMPASKVQAAEEAGTTITSMSYFSAADGP
VITKSGVGQASYGFVMPVFNGGAATWNDVAQDLGVKVKVNGSWVDIDSVGSFVYNQNWGH
WNDGGFTGYWFTLSATTEIQLYSKANGVTLDYRLVFQNINKTTITAMTPTQGPQITAGFT
GGAGFTYPIFNNDPAITYEAVADDLKVYVKPVNSSEWIDIDNNAASGWIYDQNFGQFTDG
GGGYWFNVTESINVKLESKTSSANIVYTITFNEPVRNSYVLTPYEGTTFTADASGAIGIP
LPKIDGGAPIGTELGNFVYQININGQWVDLDNSSQSGFVYSASGYNNMSPANQWGYWADH
IYGLWFQPIQEDMQIRIGYPLNGQAGGSVGSNYVNYTLIGNPDAPRPDITDQEDIPIGTP
SNPTIAGMNLIWQDEFNGTTLDNSKWNYETGYYLNNDPNTWGWGNSELQHYTNSAQNVFV
QDGKLNIRALNEPKSFPQDPNRYAQFSSGKINTKDHFSLKYGRVDFRAKLPTGNGIWPAL
WMLPQDNVYGTWASSGEIDVMEARGRLPGVTSGAVHFGGQWPTNRHLSGEYHFPEGQTFA
NDYHVYSVVWEEDNIKWYVDGKFFFKVTRDQWYSAAAPNNPNAPFDQPFYLIMNLAIGGT
FDGGRTPDPSDIPATMQVDYVRVYKEGDGGGQNPGSVPVTGVTVNPSTAQVEVGQSVQLN
ANVAPSNATNKQVTWSVASGNIASVSPSGLVTGLAPGTTTVTATTADGTKTASSTITVVP
PPSTVIVIGDEVKGLKKIGNDLLFYVNGATFADLHYKVNNGVQLNVAMTPTGNGNYTYPV
NNLKHGDTVEYFFTYNPGQGALDTPWQTYVHGVTEGRVESKAGTIL

Enzyme Prediction     

EC	3.2.1.39

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	432	684	3e-83	0.9956521739130435
CBM56	691	875	3.8e-51	0.949685534591195

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08023	GH16_laminarinase_like	1.93e-92	432	684	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	3.21e-58	430	685	1	330	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	2.43e-36	427	684	1	258	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.
cd00413	Glyco_hydrolase_16	5.92e-31	434	684	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.
cd02179	GH16_beta_GRP	2.52e-29	430	684	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANY73748.1	0.0	1	879	1	879
AAC60453.1	0.0	1	879	1	877
BAA04469.1	0.0	1	879	1	877
AYB44075.1	0.0	1	879	1	872
QOT11987.1	0.0	1	879	1	872

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3AZX_A	2.70e-52	425	686	7	256	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]
4DFS_A	8.25e-52	425	686	15	264	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]
3ILN_A	8.01e-50	430	685	7	248	ChainA, Laminarinase [Rhodothermus marinus],3ILN_B Chain B, Laminarinase [Rhodothermus marinus]
3ATG_A	9.28e-50	429	702	4	254	endo-1,3-beta-glucanasefrom Cellulosimicrobium cellulans [Cellulosimicrobium cellulans]
2HYK_A	2.92e-48	430	687	9	245	Thecrystal structure of an endo-beta-1,3-glucanase from alkaliphilic Nocardiopsis sp.strain F96 [Nocardiopsis sp. F96]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P23903	0.0	1	686	1	681	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
P45798	9.72e-50	417	685	29	283	Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1
C1IE32	8.41e-47	430	684	22	267	Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1
Q27082	8.38e-35	430	686	27	254	Clotting factor G alpha subunit OS=Tachypleus tridentatus OX=6853 PE=1 SV=1
Q8N0N3	5.36e-31	430	685	32	360	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
0.000358	0.998876	0.000197	0.000212	0.000176	0.000154

TMHMM  Annotations     

start	end
17	36