CAZyme Information: MGYG000003773_01751

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-74; Firm-11
• CAZyme ID: MGYG000003773_01751
• CAZy Family: GH18
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
379	MGYG000003773_104|CGC1	40386.48	7.0326

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003773	3076411	MAG	Canada	North America

• Gene Location: Start: 8482; End: 9621 Strand: +

Full Sequence      

MKKPEARIARRFWWSSLALASLVWLGLGAGVSPVPLQAGESATASTGRRTAAYVYDRAGL
SFADSDAQHLNQLNFSFALIRNGEVSGSHWQGIEAYKAFVAKHPHILPVLSIGGWGADGF
SQAASTEDGRTRFVDSALLLMERHGFLGVDIDWEYPGSSVAGIASSPNDRRNFTLLLKAL
REGLNRLTDADGKPRMLGIAVGASPAHLRNIETSSVAALVDQINLMTYDLHTSGVASHHT
ALYASEGYPLSVDTAVQSAISAGFPKEKIMIGAAFYGHVFTLKASGSQPVFAPAADSGSR
TLTYDRIKSRLSSANAGFDEKAKAPYATDGATFITYDDAASIRSKGAYAAQKGLMGMMCW
EYGGDSSGELLAAMYESLN

Enzyme Prediction     

No EC number prediction in MGYG000003773_01751.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	55	372	1.2e-62	0.8918918918918919

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	4.20e-93	54	365	10	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	1.92e-78	63	365	19	334	Glyco_18 domain.
pfam00704	Glyco_hydro_18	6.47e-70	66	365	19	307	Glycosyl hydrolases family 18.
cd02872	GH18_chitolectin_chitotriosidase	3.28e-69	73	360	31	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.
COG3325	ChiA	1.33e-67	37	378	27	436	Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AUS97898.1	2.03e-78	51	379	13	348
QDM46973.1	2.46e-75	51	375	9	340
ANY73914.1	4.63e-75	51	378	7	341
SYX83526.1	3.89e-74	66	377	24	342
ACX68251.1	2.38e-73	51	378	7	341

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6INX_A	1.56e-71	51	378	8	342	Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
5GZU_A	8.77e-56	101	378	105	391	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	1.93e-55	101	378	356	642	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]
6BT9_A	6.93e-45	85	365	128	448	ChitinaseChiA74 from Bacillus thuringiensis [Bacillus thuringiensis],6BT9_B Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis]
6KXN_A	3.51e-44	63	378	26	370	Crystalstructure of W50A mutant of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis],6KXN_B Crystal structure of W50A mutant of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q13231	4.42e-38	64	360	45	358	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
P20533	3.12e-37	103	365	152	438	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
Q9D7Q1	1.07e-35	64	360	45	356	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2
Q9WTV1	1.93e-34	59	360	37	350	Chitinase-3-like protein 1 OS=Rattus norvegicus OX=10116 GN=Chi3l1 PE=2 SV=3
Q6RY07	8.04e-34	73	360	54	360	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.157091	0.750113	0.055379	0.031444	0.004262	0.001692

TMHMM  Annotations     

start	end
12	34