CAZyme Information: MGYG000000526_00190

Basic Information

• Species: Prevotella sp900770395
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900770395
• CAZyme ID: MGYG000000526_00190
• CAZy Family: GH18
• CAZyme Description: Chitinase A1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
332	MGYG000000526_1|CGC4	37011.43	8.0784

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000526	3510035	MAG	Fiji	Oceania

• Gene Location: Start: 243921; End: 244919 Strand: +

Full Sequence      

MAVAVMFPCMGNAACKGKKKSDKVIVAYVTSWSKIMPDPQYMTHINYAFGSVSETFNGVT
VDNERRLCDIAAIKHRHPNLKVILSIGGWGSGRFSEMAADDALRKAFARDCRRVVDQYRL
DGIDIDWEYPTSNAAGISASPDDTGNFTLLMRDIRKAIGKKKLLTLATVASAQYIDLKAI
MPYVDFVNIMSYDMGGAPKHHSALYESANTGWMTAHGAVQAHIKAGVPAEKLVLGMPFYG
RGGTDYPNFQDYSKICKDKNYMECWDDEAKVPYLADKDGKLVCGYDNPRSLAIKCRYVWE
HGLLGAMYWDYAGDNDQNDLRRAVFDGIMKVK

Enzyme Prediction     

No EC number prediction in MGYG000000526_00190.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	23	320	2.7e-78	0.956081081081081

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	4.63e-108	25	314	1	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	9.06e-86	24	314	1	334	Glyco_18 domain.
pfam00704	Glyco_hydro_18	8.50e-83	24	314	1	307	Glycosyl hydrolases family 18.
cd02872	GH18_chitolectin_chitotriosidase	1.26e-78	25	313	1	345	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	3.24e-63	24	316	39	425	Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDO71383.1	7.40e-173	2	332	11	342
ADV45176.1	8.20e-170	2	332	11	343
QUT34047.1	6.17e-162	3	332	12	343
QUT62465.1	3.81e-153	20	329	25	335
QQA31016.1	4.76e-153	20	329	32	342

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6INX_A	7.39e-62	42	329	27	343	Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
3QOK_A	2.30e-54	38	328	50	416	ChainA, Putative chitinase II [Klebsiella pneumoniae subsp. pneumoniae MGH 78578]
4NZC_A	4.10e-53	38	328	30	396	Crystalstructure of Chitinase D from Serratia proteamaculans at 1.45 Angstrom resolution [Serratia proteamaculans 568],4Q22_A Crystal structure of Chitinase D from Serratia proteamaculans in complex with N-acetyl glucosamine at 1.93 Angstrom resolution [Serratia proteamaculans 568]
6HM1_A	4.30e-53	38	328	27	393	Structuraland thermodynamic signatures of ligand binding to an enigmatic chitinase-D from Serratia proteamaculans [Serratia proteamaculans 568]
4PTM_A	4.61e-53	38	328	30	396	CrystalStructure of Chitinase D from Serratia proteamaculans in complex with N-acetyl glucosamine, a hydrolyzed product of hexasaccharide at 1.7 Angstrom resolution [Serratia proteamaculans 568]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20533	4.69e-49	1	321	22	448	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
Q13231	3.80e-38	25	313	24	367	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
Q9W092	4.60e-35	22	315	40	390	Probable chitinase 2 OS=Drosophila melanogaster OX=7227 GN=Cht2 PE=1 SV=1
P36362	6.66e-34	25	317	25	378	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
Q95M17	6.99e-33	25	309	24	360	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA 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
1.000037	0.000006	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000526_00190.