CAZyme Information: MGYG000000670_01638

Basic Information

• Species: Faecalibacillus sp900544435
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Faecalibacillus; Faecalibacillus sp900544435
• CAZyme ID: MGYG000000670_01638
• CAZy Family: GH16
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
836		92709.56	4.5913

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000670	2790604	MAG	Kazakhstan	Asia

• Gene Location: Start: 36529; End: 39039 Strand: +

Full Sequence      

MKNKKISKVVLSVLTSMSMLSSYSAMVFAEPTNQGASQVAHEYDLVKLDRNGDLIVNGGF
NNNGASWLKTGTGTIGNDNGNYYGKLPSNSNNAAVYQNVSFKKNTDYVVKAKVKISNENG
QVFLAVKNSNLSAGLKDNNGEIIETNITSSKETANKYQDVEFTFNSGDNGSGSIAFIKWT
ERNGNQDIINEEVWIDDVSVKAVNETSEDDNYEMVWADDFNENQLDTSNWDYELGSIRGV
EQEHYVNDPENVYVKDGQLVLQVTDRDKEDQYKNPRGNRQVIYNSGSIRTHGKKEFLYGR
IEMKAKLPKGKGAFPAFWTLGSDFTLDGRISSEQGAPWPVCGEIDIMEMIGAADGDLNGK
SNRKVYQTVHAGSAQDVDHSRSVSTYTLPEGIFNDDYHIFGINWSKNKLEFYVDSTIVGS
IDYSNNEEYKRCFNRPQYIQLNLATGGNWAGDAGDNLAGQKYEVDYVYYGQNAQQKADSE
AYYKDAIKITGEHDVTMTEGETPDLLEGVTSDQDSILDYSIDNEYSFKSKGGLTSVDLVC
SGKNDTARLKNLKPGKYNLYYTAKSSTDATKPSTRRAVILTIEERTFEKDLEKSGLKLNG
FIGDTLDTIQLPKGWVFENPQEIITEETNEVAVKCVDLDKVQTAKINVQERAKIIAGENG
KYELKDSKPLKITINVSKEDILKVLVDGEELDSKYYTVENIAQSINGTADVILSEDYLKT
LSNGEHTIKITSTLGDVETLFTVDNSKDDDTNQKPGTGKDDDTNQKPGTGKGDDTNQKPN
TDKKDEVSDKTNNVTTNVKNNTTPKTGDRTPIELLTICSLVSLIVIVALKKKKVND

Enzyme Prediction     

No EC number prediction in MGYG000000670_01638.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	216	467	1.6e-113	0.9927007299270073

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08023	GH16_laminarinase_like	8.33e-73	216	467	1	232	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	4.38e-36	214	461	1	289	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.
cd00413	Glyco_hydrolase_16	4.95e-35	218	469	1	209	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.
cd02182	GH16_Strep_laminarinase_like	1.24e-30	212	467	2	255	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.
cd02178	GH16_beta_agarase	1.04e-23	209	467	12	254	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCL56802.1	0.0	1	834	13	1380
QQY27074.1	4.84e-190	10	685	10	690
QMW75560.1	1.92e-189	10	685	10	690
QPS14107.1	1.92e-189	10	685	10	690
QQV05979.1	3.82e-189	10	685	10	690

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4DFS_A	7.27e-39	199	467	3	259	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	2.10e-38	210	467	8	251	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]
5WUT_A	1.26e-37	214	467	7	231	Crystalstructure of laminarinase from Flavobacterium sp. UMI-01 [Flavobacterium sp.],5WUT_B Crystal structure of laminarinase from Flavobacterium sp. UMI-01 [Flavobacterium sp.]
2VY0_A	3.26e-34	212	467	13	256	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]
4BQ1_A	4.22e-33	214	467	13	252	Crystalstructure of of LamAcat from Zobellia galactanivorans [Zobellia galactanivorans],4BQ1_B Crystal structure of of LamAcat from Zobellia galactanivorans [Zobellia galactanivorans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P23903	7.54e-34	214	467	425	676	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
P45798	3.24e-21	212	454	40	264	Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1
Q9ZG90	9.60e-21	199	467	42	284	Keratan-sulfate endo-1,4-beta-galactosidase OS=Sphingobacterium multivorum OX=28454 PE=1 SV=1
C1IE32	4.91e-20	216	467	24	264	Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1
Q27082	2.01e-19	207	473	20	255	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
0.000280	0.999003	0.000189	0.000205	0.000169	0.000142

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000670_01638.