CAZyme Information: MGYG000000316_00735

Basic Information

• Species: UBA945 sp900549675
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UBA945; UBA945 sp900549675
• CAZyme ID: MGYG000000316_00735
• CAZy Family: GH18
• CAZyme Description: Chitinase A1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
337	MGYG000000316_63|CGC1	38256.39	5.5959

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000316	2303090	MAG	Sweden	Europe

• Gene Location: Start: 7428; End: 8441 Strand: +

Full Sequence      

MNKILAYLTNRGGLTKEDAQKLTHIHLAFGKLDIDGSIDVSELSILEETPKIRQWNPKIK
LLLSLVTKHPDAFTRCAEDEELRKAVGISCSKILKEYHLDGIDFDWEYPCVPSNGMSSKK
EDKENFTLLLQAVRDEMKQTDPTALLSIAAGADLYYVKSVELPKIANLLDYICLMTYDLK
CGFHALSGHHTPLYSSTGDVFCNSCSQALQLFEQNGVPKEKLLMGAAFYSRQWENIADIN
HGFLQLSKTGGGYGPDFEVLQKDFIDKNGYTYFWDDEAKAPYLFNGSTFISYDNEQSLQE
KCRYVNQKQYGGLFYWEHSCDRTGTLLNAIYHARNLT

Enzyme Prediction     

No EC number prediction in MGYG000000316_00735.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	17	325	7.7e-62	0.8648648648648649

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	4.20e-81	18	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	1.66e-72	3	321	1	334	Glyco_18 domain.
pfam00704	Glyco_hydro_18	1.46e-67	3	317	1	303	Glycosyl hydrolases family 18.
cd02872	GH18_chitolectin_chitotriosidase	1.04e-62	23	316	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.
COG3325	ChiA	1.46e-61	3	330	39	432	Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDM46973.1	4.33e-106	14	332	20	341
QAV17545.1	4.54e-105	4	335	7	343
QBO56278.1	1.14e-103	14	331	19	339
AZS16398.1	4.30e-103	14	331	20	340
ANS77385.1	4.93e-103	3	333	13	348

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6INX_A	4.16e-105	14	331	19	339	Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
5GZU_A	3.28e-67	18	331	46	388	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	1.65e-66	18	331	297	639	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	1.32e-54	46	330	110	415	ChainA, Glycosyl Hydrolase [Niallia circulans]
6BT9_A	7.69e-51	48	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	8.34e-52	46	330	142	447	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
Q95M17	3.21e-35	23	328	52	373	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
Q9BZP6	2.37e-34	23	328	52	373	Acidic mammalian chitinase OS=Homo sapiens OX=9606 GN=CHIA PE=1 SV=1
P36362	1.07e-30	3	321	24	375	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
P11797	1.76e-30	14	330	36	418	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
1.000047	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000316_00735.