CAZyme Information: MGYG000002717_02178

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides
• CAZyme ID: MGYG000002717_02178
• CAZy Family: GH18
• CAZyme Description: Chitinase A1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
361		40270.62	4.7475

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002717	5602088	MAG	Canada	North America

• Gene Location: Start: 6954; End: 8039 Strand: +

Full Sequence      

MKYFLFSIVLLMIASMISCSSKDNELKDLPPLPDEPITEEPSPIPGSTDKIVIGYVTSWS
SHEVKPEYVTHINYAFGHVQGTFRGVRIDNEERLKSVVALKKQASHLKVLLSVGGWGSGN
FSEMAADADNRLAFAADCKRVIDEFGLDGIDIDWEFPTSNMADISSSPDDTRNYNLMMRD
IRQAIGSDKLLTLATVCSADYIDFEGIMPYIDFINIMAYDMDNPPKHNAPLYQSSKFPGW
FNCDMAVKAHRAKGVPASMLVLGMPFYGHGTDIYDHSTDFKNVKVPSGYTNCWDDEAKVP
YVTDKNGRFVLSYDNARSIGLKCDYILEYGLLGAMFWDDAGDDGNHTLHKAIANKLFVES
N

Enzyme Prediction     

No EC number prediction in MGYG000002717_02178.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	50	354	2.7e-72	0.9763513513513513

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	2.01e-102	52	342	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	1.73e-86	52	342	2	334	Glyco_18 domain.
pfam00704	Glyco_hydro_18	4.97e-77	52	342	2	307	Glycosyl hydrolases family 18.
cd02872	GH18_chitolectin_chitotriosidase	2.55e-69	52	356	1	362	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	4.69e-57	46	359	33	439	Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT34049.1	1.48e-248	6	361	4	359
QDO71383.1	3.39e-130	9	359	8	341
ADV45176.1	1.44e-126	47	359	31	342
QUT34047.1	2.09e-123	50	356	34	339
QUT90190.1	7.44e-123	48	356	32	340

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6INX_A	2.98e-51	47	356	2	342	Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
4NZC_A	4.35e-49	69	350	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	4.54e-49	69	350	31	388	Structuraland thermodynamic signatures of ligand binding to an enigmatic chitinase-D from Serratia proteamaculans [Serratia proteamaculans 568]
4PTM_A	4.86e-49	69	350	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	5.19e-49	69	350	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	7.76e-44	52	356	46	447	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
G5EAZ3	4.78e-36	53	359	7	366	Endochitinase B OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=chiB PE=1 SV=1
Q92222	4.78e-36	53	359	7	366	Endochitinase B OS=Emericella nidulans OX=162425 GN=chiB PE=1 SV=3
Q1E3R8	1.07e-34	55	356	43	398	Endochitinase 1 OS=Coccidioides immitis (strain RS) OX=246410 GN=CTS1 PE=3 SV=1
P0CB51	1.07e-34	55	356	43	398	Endochitinase 1 OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=CTS1 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
0.000002	0.000698	0.999315	0.000000	0.000001	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002717_02178.