CAZyme Information: MGYG000001186_02578

Basic Information

• Species: Agathobacter sp900547695
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Agathobacter; Agathobacter sp900547695
• CAZyme ID: MGYG000001186_02578
• CAZy Family: GH16
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1247	MGYG000001186_20|CGC1	138394.73	4.3671

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001186	3291648	MAG	Austria	Europe

• Gene Location: Start: 36173; End: 39916 Strand: -

Full Sequence      

MKKRVLLALLVSAMTLTAMPGVTFAGSNADSADNGGLSYEGYTQVWGDEFNGDSLNRDDW
NVETHKKGWVNSELQEYVDSEENIQVKDGKLLINPVKKVTSVENNEEINLIKNADFSSEM
EGWTETIANWGGSDGSADAQRTTSDGKIIYNIKNPGTQDWNVQLKQTDIKLQKGHKYKVS
FKVLSTGNRKFKTGVMSDSYEWYGGCEPELEAGKEQEVSFDFEIDKETVADFYISLGKYD
KNDDTLSSDVTISDIKMIDLNASNEAVSYTSGRISTQNKQTFTYGRFECRAKVPKGQGYL
PAFWLMANDENIYGQWPRCGEIDCMEVMGQETNKVYGTIHYGNPHAESQGTYYTSDAEAD
FSDDFHTFTCDWEPGVIKWYVDGKLYHEESDWHSTTQGQGTLTYPAPFDQPFYIILNLAV
GGSWVGNPNEETSFDNNPYEIDYVRVYKKDSYNEDVKRPVKQVTLREPDANGNYINNGDF
SVKEDLTDETGWKFVTALEGEAAASIDGNTMTIKTTNEGTVDYSVQLVQPNLPLEKGATY
QVQFDAYASADREIGIDVKAPDHGYMSYMPHQDAKLTTKKQTYTYTFKMGESSDANGRLE
YNMGAKGSTADIYISNVSVKKIKDADPNEKEVKTVLANGNYVYNGSFQEGDKHLGYWTIV
NDENAQAGVTSFADNRRFKVTMNKDAKSAVIISQEDLAFAAGTPYRFSFSAESDMDNTIT
VSVGGYEYTADIKAGEMKEFAFDIPANAEYVNKNISITLGMNGTTWLDNVSLVENALIKN
GSFNAGTTGYTVYVDSSAKASYVVDSLKDGNALAVTIDDTGDQDWKVQIKQENIMLEKGK
TYKLKFKAKSSLERQIRVVMQGQEDRDWSVYSDDNIIDLTNEYQTFEDTFTMKEDTDKAA
FLSACLGKIGDDQITKQHEVRIDDISLEEIKADSKDDVKEDPKGDSDSDVKEDPKGDSDS
DVKEDPKGDSDSDVKEDPKGDSDSDVKDDSKSDFDNDAGAAIVDENKVLPAGTNIESTKI
EKTSETYKKIADILEKNDIKGKFVAFELNLLDSDNNKITKQPDGMIKVTLPIPEGLEVSA
DKTIVVYRVNDDGTLVKCNTTVENGKVIFETDHFSKYVFAEEEIKKEDAKDAPKSDEPKS
DEPKSDETKPDETKPDESKSDELKSDVSKSDMPKFDESKSDASKSDTSKTDMSKTGKSKA
SPKKPPVAAGKKAIATGDNSPIAIFLLAGLAGIFAVGTELIRKRKLK

Enzyme Prediction     

No EC number prediction in MGYG000001186_02578.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	259	447	4.1e-64	0.7956521739130434
CBM4	777	902	5.7e-34	0.9444444444444444
CBM4	473	604	2.1e-33	0.9920634920634921

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08023	GH16_laminarinase_like	2.32e-74	269	447	64	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	4.60e-41	271	448	101	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.
cd00413	Glyco_hydrolase_16	2.28e-36	221	447	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.
COG2273	BglS	4.75e-34	208	460	39	276	Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].
cd02182	GH16_Strep_laminarinase_like	7.57e-32	268	447	67	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNL98962.1	0.0	28	931	44	966
QAA34888.1	2.95e-246	15	932	300	1064
QWT52878.1	3.34e-240	37	931	244	973
QQQ91210.1	4.97e-218	30	938	250	997
ASU30685.1	4.97e-218	30	938	250	997

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3AZX_A	6.71e-44	269	448	81	255	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	1.99e-43	269	448	89	263	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]
2VY0_A	2.94e-40	269	447	85	259	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	2.04e-37	268	451	67	242	endo-1,3-beta-glucanasefrom Cellulosimicrobium cellulans [Cellulosimicrobium cellulans]
2HYK_A	9.54e-37	269	448	72	243	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	4.41e-37	264	449	496	681	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
C1IE32	1.02e-35	264	445	83	265	Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1
P45798	8.07e-32	265	448	101	283	Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1
Q9ZG90	3.70e-28	255	613	105	403	Keratan-sulfate endo-1,4-beta-galactosidase OS=Sphingobacterium multivorum OX=28454 PE=1 SV=1
Q27082	3.33e-24	265	448	82	253	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
0.000398	0.998506	0.000280	0.000307	0.000247	0.000215

TMHMM  Annotations     

start	end
5	27
1222	1241