CAZyme Information: MGYG000004080_00565

Basic Information

• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Arcanobacterium_A
• CAZyme ID: MGYG000004080_00565
• CAZy Family: GH16
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
438	MGYG000004080_3|CGC2	49236.12	6.1493

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004080	1753974	MAG	United Kingdom	Europe

• Gene Location: Start: 70992; End: 72308 Strand: +

Full Sequence      

MKWNTRKIKLINLSLLTLICTVGFAFETSAFAAFCAPSLGLVSYPHQIIDPATPDKEGMV
LTASSEFNGTAINDSLFTDSYLPHWSSSEGTKANYEVSEGTLKLKITKDQKPWDPIYDGS
TRVSSLQTYQKDYLHEWTKYPGIAQHTEPFRGHVQKYGYFELRAKVANGGGLHSAWWMTG
AHQDIPEGTHGWSRQNGEVDIFEVLGRDNATTAQSAIHPWGDWGRLLPWTKKISTNNDLS
ADFHTYGFEWKASGMKVYIDGVEKFSTPLSPNYPMLTYLGIYEKQEENSWTGPFDPGIPY
PKIFEIDYFRAYQEIPTLPYSVFTTDGVMRGETRVDGTVTRWIGGEGNDVTLNSIYAPED
GIYQLGIEYRSGESRDLELHINGKRHMIAGLSTGSFSGSFSWSNISIHLDKGWNSVRLGN
THDPAPDVKRLRVEKVNP

Enzyme Prediction     

No EC number prediction in MGYG000004080_00565.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	66	312	1.2e-76	0.9875518672199171

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00413	Glyco_hydrolase_16	2.80e-34	66	312	2	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.
cd08023	GH16_laminarinase_like	1.95e-27	155	312	77	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.
cd02178	GH16_beta_agarase	1.37e-20	45	313	5	258	Beta-agarase, member of glycosyl hydrolase family 16. Beta-agarase is a glycosyl hydrolase family 16 (GH16) member that hydrolyzes the internal beta-1,4-linkage of agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea, marine red algae. Agarose is a linear chain of galactose units linked by alternating L-alpha-1,3- and D-beta-1,4-linkages that are additionally modified by a 3,6-anhydro-bridge. Agarose forms thermo-reversible gels that are widely used in the food industry or as a laboratory medium. While beta-agarases are also found in two other families derived from the sequence-based classification of glycosyl hydrolases (GH50, and GH86) the GH16 members are most abundant. This domain adopts a curved beta-sandwich conformation, with a tunnel-shaped active site cavity, referred to as a jellyroll fold.
pfam00722	Glyco_hydro_16	9.79e-13	157	262	33	123	Glycosyl hydrolases family 16.
cd08024	GH16_CCF	1.43e-10	156	295	113	263	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AIE83322.1	1.84e-245	36	434	35	437
QJC21524.1	9.68e-209	47	437	6	405
AZR05443.1	1.04e-193	43	433	39	430
QIU87147.1	1.04e-193	43	433	39	430
AWG03834.1	1.04e-193	43	433	39	430

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1UPS_A	1.84e-46	51	315	21	280	GlcNAc[alpha]1-4Galreleasing endo-[beta]-galactosidase from Clostridium perfringens [Clostridium perfringens],1UPS_B GlcNAc[alpha]1-4Gal releasing endo-[beta]-galactosidase from Clostridium perfringens [Clostridium perfringens]
4DFS_A	1.09e-11	156	314	103	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]
3AZX_A	1.16e-11	156	315	95	257	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]
4BQ1_A	1.30e-11	73	313	38	256	Crystalstructure of of LamAcat from Zobellia galactanivorans [Zobellia galactanivorans],4BQ1_B Crystal structure of of LamAcat from Zobellia galactanivorans [Zobellia galactanivorans]
4BOW_A	5.76e-11	73	313	38	256	Crystalstructure of LamA_E269S from Z. galactanivorans in complex with laminaritriose and laminaritetraose [Zobellia galactanivorans],4BOW_B Crystal structure of LamA_E269S from Z. galactanivorans in complex with laminaritriose and laminaritetraose [Zobellia galactanivorans],4BPZ_A Crystal structure of lamA_E269S from Zobellia galactanivorans in complex with a trisaccharide of 1,3-1,4-beta-D-glucan. [Zobellia galactanivorans],4BPZ_B Crystal structure of lamA_E269S from Zobellia galactanivorans in complex with a trisaccharide of 1,3-1,4-beta-D-glucan. [Zobellia galactanivorans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P23903	2.69e-12	51	314	415	681	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
Q84C00	1.99e-08	157	339	103	280	Beta-glucanase OS=Acetivibrio thermocellus OX=1515 GN=licB PE=1 SV=1
A3DBX3	8.39e-08	157	339	103	280	Beta-glucanase OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=licB PE=1 SV=1
C1IE32	3.33e-06	60	295	21	225	Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 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
0.000380	0.998923	0.000222	0.000173	0.000145	0.000142

TMHMM  Annotations     

start	end
12	34