CAZyme Information: MGYG000001095_00584

Basic Information

• Species: Chryseobacterium gambrini
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Flavobacteriales; Weeksellaceae; Chryseobacterium; Chryseobacterium gambrini
• CAZyme ID: MGYG000001095_00584
• CAZy Family: GH16
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
566		61869.45	6.1693

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001095	4128611	MAG	Sweden	Europe

• Gene Location: Start: 9266; End: 10966 Strand: +

Full Sequence      

MLKKLHHIVLFLFSTLYLAQVDVVYNDLVWSDEFSTNGAVDNVKWFHQTQLPVAGGWYNN
EQQHYTNLITNSFANNGELNIVAKKETFTDQGYTKNYTSARLNSKFAFKYGRIDVRAKVP
KNQGTWPAIWLLGKNVNEPGGYFASTYGNTNWPACGEIDMMEYGIFPSAPENFIQSTLHT
PSSSGNSVNHGGMLASSDITANYHIYSMNWSPNQITFLLDGVAYYTYNPLVKNASTWPFD
KEQYLLLNIAMGGVAGTIPSTFTDASMIIDYVRVYQNTTPDTVAPTNFTATVGAVTSDSV
ELLLNATDNFGAITYQISGGATQTVYGTSGVQKSEIISGLSPSTNYTFTISASDAAGNAA
ANNPITVNATTLSNINTACSGTSTLASQGAFSTGYKYDFQTIGTDVKITFELLDTDKTGV
VAYLWKQTPFTETPMTNVSGKKFSSTITGQTAGSTINYAVKFAYAGGMSVTKYYSYVVGD
ACISLGVTDFLKVKELLYPNPVENILNLKLPENKNTVTLYDFSGKKLFEKNVGTTLELDF
SSFTAGTYLIRIENSKAANTYKIVKK

Enzyme Prediction     

No EC number prediction in MGYG000001095_00584.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	30	275	9.1e-69	0.9956521739130435

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08023	GH16_laminarinase_like	5.37e-81	30	275	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	2.39e-41	28	276	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	3.18e-37	27	276	3	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.
cd00413	Glyco_hydrolase_16	9.85e-29	32	275	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	7.49e-24	28	275	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
QBN18061.1	1.23e-251	18	565	20	567
APY09488.1	2.12e-120	20	278	181	436
BAO76967.1	4.31e-117	21	277	182	435
QJP33554.1	7.76e-109	21	278	169	427
AUC78459.1	8.09e-109	21	278	182	440

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4BQ1_A	4.86e-73	25	276	10	256	Crystalstructure of of LamAcat from Zobellia galactanivorans [Zobellia galactanivorans],4BQ1_B Crystal structure of of LamAcat from Zobellia galactanivorans [Zobellia galactanivorans]
4BOW_A	2.67e-72	25	276	10	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]
3AZX_A	1.51e-43	28	283	12	262	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	1.31e-42	28	280	20	267	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	1.61e-41	27	276	6	248	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
P45798	7.93e-39	27	276	41	283	Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1
P23903	1.25e-33	27	276	424	680	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
Q9ZG90	6.67e-33	27	276	57	288	Keratan-sulfate endo-1,4-beta-galactosidase OS=Sphingobacterium multivorum OX=28454 PE=1 SV=1
C1IE32	1.98e-26	28	253	22	238	Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1
Q27082	3.79e-25	28	308	27	285	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
0.000699	0.998418	0.000238	0.000220	0.000200	0.000197

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001095_00584.