CAZyme Information: MGYG000001422_00752

Basic Information

• Species: Bacteroides oleiciplenus
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides oleiciplenus
• CAZyme ID: MGYG000001422_00752
• CAZy Family: GH18
• CAZyme Description: Endo-beta-N-acetylglucosaminidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
315	MGYG000001422_1|CGC9	34656.19	7.3406

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001422	7071122	Isolate	not provided	Asia

• Gene Location: Start: 840796; End: 841743 Strand: +

Full Sequence      

MKNLRHFFLLAAAMIAGAFITSCSNEDYTVETQQDTQPTTRSIDATKIPKLTAYIETNDI
NPLNAGEYYFTGTNPQEQVIDNVILFASNIRGTANTVQLYHNDNQTYILNNASTLIAPLQ
AKGIKVSLGLLGDHTGVGFCNLSPAMVESFAQQIAACVTKYKLDGVDFDDEYAKYWMAPA
NLPTPSTTIFGNLIKRVRQLLPGKLITVFHFGGYTNFDATTMNAISYMWPNFGIDQNPPA
GLGNGKWARMSIHCTNPIPSTSQIQSCAANYSGYGAIMMFNFRNTDHSGLMNNFASKVWG
GKTVSYTGNSYTKNY

Enzyme Prediction     

No EC number prediction in MGYG000001422_00752.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06542	GH18_EndoS-like	1.60e-36	49	284	1	240	Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of various asparagine (N)-linked glycans and glycoproteins. The endo-beta-N-acetylglucosaminidases have a glycosyl hydrolase family 18 (GH18) catalytic domain. Some members also have an additional C-terminal glycosyl hydrolase family 20 (GH20) domain while others have an N-terminal domain of unknown function (pfam08522). Members of this family include endo-beta-N-acetylglucosaminidase S (EndoS) from Streptococcus pyogenes, EndoF1, EndoF2, EndoF3, and EndoH from Flavobacterium meningosepticum, and EndoE from Enterococcus faecalis. EndoS is a secreted endoglycosidase from Streptococcus pyogenes that specifically hydrolyzes the glycan on human IgG between two core N-acetylglucosamine residues. EndoE is a secreted endoglycosidase, encoded by the ndoE gene in Enterococcus faecalis, that hydrolyzes the glycan on human RNase B.
pfam00704	Glyco_hydro_18	3.31e-10	83	221	27	158	Glycosyl hydrolases family 18.
cd00598	GH18_chitinase-like	4.20e-07	53	225	3	164	The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model.
cd02878	GH18_zymocin_alpha	2.26e-06	143	208	88	156	Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle progression. The zymocin alpha subunit has a chitinase activity that is essential for holoenzyme action from the cell exterior while the gamma subunit contains the intracellular toxin responsible for G1 phase cell cycle arrest. The zymocin alpha and beta subunits are thought to act from the cell's exterior by docking to the cell wall-associated chitin, thus mediating gamma-toxin translocation. The alpha subunit has an eight-stranded TIM barrel fold similar to that of family 18 glycosyl hydrolases such as hevamine, chitolectin, and chitobiase.
cd06548	GH18_chitinase	5.45e-04	142	228	105	201	The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant polymer of N-acetylglucosamine and have been identified in bacteria, fungi, insects, plants, viruses, and protozoan parasites. The structure of this domain is an eight-stranded alpha/beta barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDM12014.1	3.60e-176	1	315	1	315
BCA50677.1	1.81e-122	40	315	14	286
BCA50675.1	7.30e-105	34	315	9	286
QUT39058.1	1.00e-64	1	315	1	306
QQA10383.1	1.00e-64	1	315	1	306

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1EDT_A	5.92e-36	49	304	9	268	ChainA, ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H, ENDO H [Streptomyces plicatus]
6VE1_A	7.51e-36	49	304	13	272	ChainA, Endo-beta-N-acetylglucosaminidase H [Streptomyces plicatus],6VE1_B Chain B, Endo-beta-N-acetylglucosaminidase H [Streptomyces plicatus],6VE1_C Chain C, Endo-beta-N-acetylglucosaminidase H [Streptomyces plicatus],6VE1_D Chain D, Endo-beta-N-acetylglucosaminidase H [Streptomyces plicatus]
1C90_A	1.41e-35	49	304	4	263	ChainA, ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H [Streptomyces plicatus],1C90_B Chain B, ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H [Streptomyces plicatus]
1C91_A	1.41e-35	49	304	4	263	ChainA, ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H [Streptomyces plicatus]
1C8X_A	1.97e-35	49	304	4	263	ChainA, ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H [Streptomyces plicatus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P80036	1.31e-39	49	306	55	313	Endo-beta-N-acetylglucosaminidase OS=Flavobacterium sp. (strain SK1022) OX=148444 PE=1 SV=2
P04067	8.48e-35	49	304	51	310	Endo-beta-N-acetylglucosaminidase H OS=Streptomyces plicatus OX=1922 PE=1 SV=1
P36911	1.59e-30	50	228	61	242	Endo-beta-N-acetylglucosaminidase F1 OS=Elizabethkingia meningoseptica OX=238 GN=endOF1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000000	1.000065	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001422_00752.