CAZyme Information: MGYG000002097_01475

Basic Information

• Species: Firm-11 sp900553905
• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-74; Firm-11; Firm-11 sp900553905
• CAZyme ID: MGYG000002097_01475
• CAZy Family: GH18
• CAZyme Description: Chitinase A1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
387		41983.19	6.4283

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002097	2742547	MAG	Mongolia	Asia

• Gene Location: Start: 33; End: 1196 Strand: +

Full Sequence      

MKRFSLRPRRRFALRSLALASLMWLGTGIQASPGPFHPTEAEAAAASGKRTAAYVYDSAG
LTLRDSDAPHLDQLNYSFALIKNGEVSGSHWQSIDVFRRYVEKHSHILPVLAIGGWGADG
FSQAASTADGRARFVDSTLVLMERHGFLGVDIDWEYPGSSAAGIASSANDRTNFTLLLQA
LREGLDRLTAQDGKPRMLAVALGGDPWHIRNLDVKAIGALCDQVNLMTYDLQAEGVASHH
TPLYGASESYPQSVDLAVRSYVEAGLPRSKIMIGTAFYGRSFTLKQSTAQPVWTQAADTG
KSLTYDRLKTVLADAQTGFDEQAKAPYATDGTTFWTYDDPVSIHYKGAYALENGLMGMMC
WEYGGDSSGELLAAMHDSLSGNLTARP

Enzyme Prediction     

No EC number prediction in MGYG000002097_01475.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	67	370	4e-62	0.8547297297297297

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	1.01e-86	55	366	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	5.67e-78	62	366	17	334	Glyco_18 domain.
pfam00704	Glyco_hydro_18	6.85e-68	50	366	1	307	Glycosyl hydrolases family 18.
cd02872	GH18_chitolectin_chitotriosidase	2.17e-64	74	361	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	5.61e-64	56	384	50	441	Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDM68271.1	3.09e-71	54	379	8	340
QDM46973.1	1.38e-70	52	381	9	345
QJC53938.1	2.96e-69	52	381	8	344
QBN20710.1	4.17e-69	52	381	8	344
QGG58253.1	4.17e-69	52	381	8	344

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6INX_A	7.99e-64	52	379	8	342	Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
5GZU_A	1.38e-46	103	373	106	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	1.88e-46	103	373	357	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]
6TSB_AAA	4.30e-40	67	361	50	332	ChainAAA, Peroxiredoxin [Clostridioides difficile 630]
6T9M_AAA	6.33e-40	67	361	69	351	ChainAAA, Peroxiredoxin [Clostridioides difficile 630]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q13231	3.46e-35	64	361	44	358	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
P20533	3.85e-35	93	366	141	438	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
E9ERT9	6.51e-34	65	381	59	401	Endochitinase 1 OS=Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) OX=655844 GN=chit1 PE=3 SV=1
Q9D7Q1	1.60e-33	103	361	86	356	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2
Q95M17	6.40e-33	74	361	54	360	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 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
0.104691	0.470504	0.064937	0.343326	0.015884	0.000628

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002097_01475.