CAZyme Information: MGYG000000745_01247

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-74
• CAZyme ID: MGYG000000745_01247
• CAZy Family: GH18
• CAZyme Description: Chitinase A1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
337	MGYG000000745_23|CGC1	37155.04	5.6096

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000745	2615728	MAG	Kazakhstan	Asia

• Gene Location: Start: 4017; End: 5030 Strand: +

Full Sequence      

MKKMILGYATSKGLDQMTAQDALRLTHVNLAFGVIRDGLLSMQGLPRLKEQLPRLRQFNP
SLRFVLSIGGWTADGFSLMARTEAGRRAFAASVERAMDEYALDGVDIDWEYPCSDAAGID
CDPSDKYNFTLLLQALRDVAGNRIVSIAAGGGAYFIRDTEMEKVAQILDYVQIMTYDLAT
GRSIAAHHTPLYAGDGCVPTANADTCVKIYEAAGVSREKLIIGAAFYSRIWHNVESDGGG
LGGHADGAAGFGPEYTELKARYIDQNGFVRHWDEKARAPYLFNGSTFITYDDPESIAEKC
RYVLREGLRGLMYWEHSCDRSGELLHVISDTLHGKQA

Enzyme Prediction     

No EC number prediction in MGYG000000745_01247.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	3	323	6.8e-67	0.9493243243243243

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	6.89e-93	21	319	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	4.88e-77	25	319	26	334	Glyco_18 domain.
pfam00704	Glyco_hydro_18	9.22e-77	5	315	2	303	Glycosyl hydrolases family 18.
COG3325	ChiA	4.73e-68	51	335	116	439	Chitinase, GH18 family [Carbohydrate transport and metabolism].
cd02872	GH18_chitolectin_chitotriosidase	9.73e-58	26	314	29	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	4.16e-116	1	332	1	332
ASB42412.1	4.16e-116	1	332	1	332
QQR31699.1	4.16e-116	1	332	1	332
SYX83526.1	7.12e-110	2	328	5	339
QBO56278.1	2.03e-109	4	328	6	338

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6INX_A	7.40e-111	4	328	6	338	Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
5GZU_A	1.30e-69	21	335	46	394	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	7.90e-69	21	335	297	645	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	1.47e-58	14	329	43	347	ChainAAA, Peroxiredoxin [Clostridioides difficile 630]
1ITX_A	1.93e-58	50	332	111	419	ChainA, Glycosyl Hydrolase [Niallia circulans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20533	1.73e-55	50	332	143	451	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
E9ERT9	1.57e-34	50	334	111	401	Endochitinase 1 OS=Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) OX=655844 GN=chit1 PE=3 SV=1
P11797	5.96e-34	14	328	33	418	Chitinase B OS=Serratia marcescens OX=615 GN=chiB PE=1 SV=1
A6N6J0	6.21e-33	50	322	111	393	Endochitinase 46 OS=Trichoderma harzianum OX=5544 GN=chit46 PE=1 SV=1
Q9D7Q1	2.58e-32	26	314	52	356	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2

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
0.999917	0.000127	0.000005	0.000001	0.000000	0.000001

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000745_01247.