CAZyme Information: MGYG000004536_01589

Basic Information

• Species: Alistipes sp900542505
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp900542505
• CAZyme ID: MGYG000004536_01589
• CAZy Family: GH18
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
375	MGYG000004536_20|CGC2	42510.46	4.7389

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004536	2335647	MAG	Israel	Asia

• Gene Location: Start: 38702; End: 39829 Strand: -

Full Sequence      

MKKKILNLGMLAFAAALLVGCSKWTEVEPNNYFEPRPEEYYQQLRDWKKTDHSVTFGWFG
NWTGQGASPVNCLMGLPDSVDFVSMWGNWYGLSPEKWADKREVKSKKGTRVTMCFIVANC
GDQTTPQSVRDNWQENGFASEEAAVKDFWGWVDGDQAAIDAAIAKYAKSIVDTINKYEWD
GFDFDYEANYGAPGNIAGPALGDTGNPETNRQRTNFLTFIKELGKYLGPKSGTDRLLVID
GEPQNMHPDARDYFDYYIIQAYACSSYSNLDSRYNRLLQGLEATEDEALKQMVTEKLIWC
ENFESYASDGGVSHTTRDGQRVNSLKGMAMWESQYGYRKGGVGTYHMEYEYSLSGHTIEY
PYLREASAIMNPPMK

Enzyme Prediction     

No EC number prediction in MGYG000004536_01589.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	46	326	9.8e-16	0.6081081081081081

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam16141	DUF4849	3.04e-75	25	369	1	318	Putative glycoside hydrolase Family 18, chitinase_18. This DUF is likely to be a form of glycosyl hydrolase from CAZy family 18, possibly chitinase 18. This would have the EC number of EC:3.2.1.14.
cd06542	GH18_EndoS-like	5.11e-50	54	354	2	245	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.
cd00598	GH18_chitinase-like	1.77e-06	168	262	94	176	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.
cd06548	GH18_chitinase	8.19e-04	168	262	115	209	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.
cd02878	GH18_zymocin_alpha	0.002	168	228	97	149	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AUI49102.1	1.46e-125	1	375	1	350
QCQ54233.1	4.15e-125	1	375	1	350
QTO27699.1	4.15e-125	1	375	1	350
QKH84627.1	4.15e-125	1	375	1	350
QCQ32084.1	4.15e-125	1	375	1	350

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6Q64_A	1.04e-49	4	366	2	351	BT1044SeMetE190Q [Bacteroides thetaiotaomicron]
6KPL_A	4.18e-08	42	372	19	297	CrystalStructure of endo-beta-N-acetylglucosaminidase from Cordyceps militaris in apo form [Cordyceps militaris CM01],6KPM_A Crystal Structure of endo-beta-N-acetylglucosaminidase from Cordyceps militaris in complex with L-fucose [Cordyceps militaris CM01]
6KPN_A	4.26e-07	42	372	19	297	CrystalStructure of endo-beta-N-acetylglucosaminidase from Cordyceps militaris D154N/E156Q mutant in complex with fucosyl-N-acetylglucosamine [Cordyceps militaris CM01],6KPO_A Crystal Structure of endo-beta-N-acetylglucosaminidase from Cordyceps militaris D154N/E156Q mutant in complex with fucosyl-N-acetylglucosamine-Asn [Cordyceps militaris CM01]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P36912	1.97e-08	47	372	55	335	Endo-beta-N-acetylglucosaminidase F2 OS=Elizabethkingia meningoseptica OX=238 GN=endOF2 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	1.000026	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004536_01589.