CAZyme Information: MGYG000002699_02262

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-74; HGM11588
• CAZyme ID: MGYG000002699_02262
• CAZy Family: GH18
• CAZyme Description: Chitinase A1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
337	MGYG000002699_53|CGC1	37297.03	5.2265

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002699	3362623	MAG	Canada	North America

• Gene Location: Start: 357; End: 1370 Strand: +

Full Sequence      

MHNHVTLGYVTDSALASVSHEDANALTHINLAFGAIRDGLLDMSQLPHIREIDRIRDYNA
TLKVVLSIGGWGAGGFSPMVRRADARAAFLESCEKAVREYALDGIDIDWEYPCLDWAGIE
SDPADKENFTLLMEELRGALGGQKIVSIAAGAGRYFLENTQMDKVAKACSYVQIMTYDLR
SGFEQEAGHHTNLFTSPGDRLNGSVQSSVENFLAAGVPRDKIVIGAAFYARRWDGVPDVN
HGLFQRAETVGQYGPGYTGLCDEYINKNGFVRYWDDDAKAPYLFNGSTFISYDDPESIRL
KCAYLKKEGLLGIMYWEHGCDPSRRLLTAMAGAMRHA

Enzyme Prediction     

No EC number prediction in MGYG000002699_02262.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	17	323	7.7e-71	0.8716216216216216

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	4.49e-95	22	321	22	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-83	5	321	1	334	Glyco_18 domain.
pfam00704	Glyco_hydro_18	4.96e-80	22	317	19	303	Glycosyl hydrolases family 18.
COG3325	ChiA	5.23e-72	22	331	61	433	Chitinase, GH18 family [Carbohydrate transport and metabolism].
cd02872	GH18_chitolectin_chitotriosidase	8.95e-65	18	316	20	336	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANU54368.1	4.52e-135	7	327	6	325
ASB42412.1	4.52e-135	7	327	6	325
QQR31699.1	4.52e-135	7	327	6	325
QDM46973.1	1.07e-126	2	335	4	344
ACX68251.1	1.47e-122	1	330	1	337

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6INX_A	1.60e-122	3	330	4	338	Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
5GZU_A	3.62e-72	22	328	46	384	CrystalStructure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7],5GZU_B Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7],5GZV_A Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7],5GZV_B Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7]
5GZT_B	2.70e-71	22	328	297	635	CrystalStructure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7]
1ITX_A	3.86e-62	48	326	109	411	ChainA, Glycosyl Hydrolase [Niallia circulans]
6BT9_A	1.10e-61	51	321	147	448	ChitinaseChiA74 from Bacillus thuringiensis [Bacillus thuringiensis],6BT9_B Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20533	4.72e-59	48	326	141	443	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
Q9D7Q1	2.18e-39	22	321	47	361	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2
Q13231	4.33e-39	22	321	47	363	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
A6N6J0	2.43e-37	50	321	111	390	Endochitinase 46 OS=Trichoderma harzianum OX=5544 GN=chit46 PE=1 SV=1
P11797	6.73e-37	15	321	33	408	Chitinase B OS=Serratia marcescens OX=615 GN=chiB 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
0.999693	0.000327	0.000007	0.000001	0.000000	0.000001

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002699_02262.