CAZyme Information: MGYG000000360_03334

Basic Information

• Species: UBA1829 sp900548385
• Lineage: Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; UBA1829; UBA1829; UBA1829 sp900548385
• CAZyme ID: MGYG000000360_03334
• CAZy Family: GH16
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
307		35061.11	5.5324

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000360	4492877	MAG	Sweden	Europe

• Gene Location: Start: 91866; End: 92789 Strand: +

Full Sequence      

MQTFKLDGHADSFLPENKDWKLVWNDEFDGTELDTSKWGFRLNFWGQRLKTFTTEGVELD
GESHLRLHMIRKGDDFYSPHLQTGSLTYDTPKDSGGFWPFGKLEEPKFMHRYGFYEIRCR
LPKNRGWHAAFWLQAPGVGSHPDARFAGVECDIMENYRQHFDGKMIGGNLWGGYGKDARG
SGHFSWDYEETADGWHYYAVDWSPDGYDFYADGRLIGKVVPPEREAEKHLVLEKEGCGWL
REGSVAVGPVSQVEQFILVSTECHGYRGPGFMSAGTGHKAGTPAPVLEQAVLPDYFEVDH
VRVFDRM

Enzyme Prediction     

No EC number prediction in MGYG000000360_03334.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	24	303	1.4e-27	0.9841269841269841

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00413	Glyco_hydrolase_16	6.51e-22	26	304	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.
cd08023	GH16_laminarinase_like	3.37e-20	24	304	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.
cd02178	GH16_beta_agarase	4.50e-15	14	230	13	217	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	3.39e-09	107	216	28	125	Glycosyl hydrolases family 16.
COG2273	BglS	2.21e-07	17	223	38	222	Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QYY34338.1	1.29e-137	1	307	1	288
AQT67838.1	3.54e-37	13	305	282	506
QDU56912.1	4.97e-29	15	305	34	255
AQT67867.1	8.08e-29	14	305	382	605
ASV76034.1	7.95e-27	14	304	51	273

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3ATG_A	1.25e-12	22	306	5	240	endo-1,3-beta-glucanasefrom Cellulosimicrobium cellulans [Cellulosimicrobium cellulans]
5WUT_A	3.90e-11	21	304	6	234	Crystalstructure of laminarinase from Flavobacterium sp. UMI-01 [Flavobacterium sp.],5WUT_B Crystal structure of laminarinase from Flavobacterium sp. UMI-01 [Flavobacterium sp.]
3AZX_A	1.42e-10	18	307	8	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]
4DFS_A	1.84e-10	18	215	16	206	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]
6T2N_AAA	7.20e-08	20	219	52	248	ChainAAA, Glycoside hydrolase family 16 protein [Akkermansia muciniphila],6T2N_BBB Chain BBB, Glycoside hydrolase family 16 protein [Akkermansia muciniphila]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P23903	5.98e-11	22	219	425	622	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
P45798	2.60e-06	20	224	40	230	Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1
C1IE32	4.30e-06	20	215	20	202	Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000067	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000360_03334.