CAZyme Information: MGYG000003201_01104

Basic Information

• Species: CAG-873 sp900759825
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-873; CAG-873 sp900759825
• CAZyme ID: MGYG000003201_01104
• CAZy Family: GH18
• CAZyme Description: Chitinase A1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
362	MGYG000003201_225|CGC1	39821.83	4.8079

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003201	2637500	MAG	United States	North America

• Gene Location: Start: 137; End: 1225 Strand: +

Full Sequence      

MKSSNIFAATLLSIVSLISCSSKQDEPKTLAPLPDDPATEEPAPTPGSTDKIVVGYVTSW
SDHEVKPEYVTHINYAFGHVQGNFSSVGIANEGRLKEVVALKKQAPHLKVLLSIGGWGSG
NFSEMAADADNRLAFAADCRRVIDEYGLDGIDIDWEFPTSTSAGISASPDDTRNYNYMMR
DIRRAIGDDKLLTLATVCSADYIDFEGIMPYVDFVNIMAYDMDNPPRHNAPLYQSSKHGG
WFNCDKAVKAHLAKGVPASKLVLGMPFYGHGIDIYDNFTDFKNVKVPTGYTNCWDDEAMV
PYVTDKNGRFVLSYDNARSIGLKCDYVLEQGLLGAMFWDDGGDDSNHTLHKAIANKLFVK
AE

Enzyme Prediction     

No EC number prediction in MGYG000003201_01104.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	51	355	3.8e-75	0.9763513513513513

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	7.44e-107	53	343	1	322	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.
smart00636	Glyco_18	1.31e-90	53	343	2	334	Glyco_18 domain.
pfam00704	Glyco_hydro_18	1.77e-83	53	343	2	307	Glycosyl hydrolases family 18.
cd02872	GH18_chitolectin_chitotriosidase	1.05e-70	53	340	1	342	This conserved domain family includes a large number of catalytically inactive chitinase-like lectins (chitolectins) including YKL-39, YKL-40 (HCGP39), YM1, oviductin, and AMCase (acidic mammalian chitinase), as well as catalytically active chitotriosidases. The conserved domain is an eight-stranded alpha/beta barrel fold belonging to the family 18 glycosyl hydrolases. The fold has a pronounced active-site cleft at the C-terminal end of the beta-barrel. The chitolectins lack a key active site glutamate (the proton donor required for hydrolytic activity) but retain highly conserved residues involved in oligosaccharide binding. Chitotriosidase is a chitinolytic enzyme expressed in maturing macrophages, which suggests that it plays a part in antimicrobial defense. Chitotriosidase hydrolyzes chitotriose, as well as colloidal chitin to yield chitobiose and is therefore considered an exochitinase. Chitotriosidase occurs in two major forms, the large form being converted to the small form by either RNA or post-translational processing. Although the small form, containing the chitinase domain alone, is sufficient for the chitinolytic activity, the additional C-terminal chitin-binding domain of the large form plays a role in processing colloidal chitin. The chitotriosidase gene is nonessential in humans, as about 35% of the population are heterozygous and 6% homozygous for an inactivated form of the gene. HCGP39 is a 39-kDa human cartilage glycoprotein thought to play a role in connective tissue remodeling and defense against pathogens.
COG3325	ChiA	2.35e-59	37	362	23	441	Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT34049.1	6.70e-227	7	361	4	358
ADV45176.1	8.75e-134	1	357	1	339
QUT34047.1	2.48e-133	51	360	34	342
QDO71383.1	1.55e-131	1	357	1	338
QUT90190.1	9.65e-124	1	360	1	343

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6INX_A	1.72e-54	48	349	2	335	Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
4NZC_A	2.66e-52	70	351	34	391	Crystalstructure of Chitinase D from Serratia proteamaculans at 1.45 Angstrom resolution [Serratia proteamaculans 568],4Q22_A Crystal structure of Chitinase D from Serratia proteamaculans in complex with N-acetyl glucosamine at 1.93 Angstrom resolution [Serratia proteamaculans 568]
6HM1_A	2.79e-52	70	351	31	388	Structuraland thermodynamic signatures of ligand binding to an enigmatic chitinase-D from Serratia proteamaculans [Serratia proteamaculans 568]
4PTM_A	2.99e-52	70	351	34	391	CrystalStructure of Chitinase D from Serratia proteamaculans in complex with N-acetyl glucosamine, a hydrolyzed product of hexasaccharide at 1.7 Angstrom resolution [Serratia proteamaculans 568]
4LGX_A	3.21e-52	70	351	37	394	Structureof Chitinase D from Serratia proteamaculans revealed an unusually constrained substrate binding site [Serratia proteamaculans 568]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20533	1.86e-46	41	357	34	447	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
Q1E3R8	1.57e-37	11	357	8	398	Endochitinase 1 OS=Coccidioides immitis (strain RS) OX=246410 GN=CTS1 PE=3 SV=1
C5P230	4.20e-37	11	357	8	398	Endochitinase 1 OS=Coccidioides posadasii (strain C735) OX=222929 GN=CTS1 PE=3 SV=1
P0CB51	4.20e-37	11	357	8	398	Endochitinase 1 OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=CTS1 PE=1 SV=1
Q92222	6.78e-37	54	352	7	356	Endochitinase B OS=Emericella nidulans OX=162425 GN=chiB PE=1 SV=3

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	0.000003	1.000057	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003201_01104.