CAZyme Information: MGYG000004849_00052

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; UMGS1826
• CAZyme ID: MGYG000004849_00052
• CAZy Family: GH18
• CAZyme Description: Chitinase A1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
334	MGYG000004849_1|CGC1	37368.32	5.6385

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004849	3246607	MAG	China	Asia

• Gene Location: Start: 60145; End: 61149 Strand: +

Full Sequence      

MKILGYVGNSGIVTEQDAKNLTHINVAFGNLRIDGSIEVDHLNIFGRMGQIRSWNPDIKI
VVSVVPKETDAFTVCAASQELRKKVGQSCVEMVKTYGFDGVDFDWEYPCVPSNGMNSTPA
DKKNFTLFCREVRRALDALGRHYLVTIAAGADLYYVESVELPELAKVLDYICVMTYDLKC
GFHALTGHHTALYSSTGDVFRNSCDQALRLFRESGVPKEQLLMGAGFYSRKWENIPDRNH
GFLQITGTGGGYGPNYSALEELAKGKDGFVRYWDNEAKAPWLFDGSTFLSYDDEESIRCK
SEYVKNNGYGGIFYWEHSCDPSGRLLGIMAEILK

Enzyme Prediction     

No EC number prediction in MGYG000004849_00052.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	12	320	7.8e-64	0.8986486486486487

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	1.47e-95	3	320	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	3.68e-83	2	320	1	334	Glyco_18 domain.
COG3325	ChiA	2.07e-78	2	333	39	436	Chitinase, GH18 family [Carbohydrate transport and metabolism].
pfam00704	Glyco_hydro_18	6.14e-75	2	316	1	303	Glycosyl hydrolases family 18.
cd02872	GH18_chitolectin_chitotriosidase	4.14e-65	22	315	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
QDM46973.1	2.58e-119	13	329	20	339
QTH44190.1	9.76e-119	3	334	7	343
QOS77321.1	6.16e-116	5	334	8	342
QHW32346.1	1.54e-115	4	331	8	340
ANS77385.1	4.92e-115	2	326	13	342

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6INX_A	3.79e-110	3	334	7	343	Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
5GZU_A	4.34e-69	5	334	521	882	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	2.52e-68	5	334	772	1133	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	1.04e-58	45	320	145	448	ChitinaseChiA74 from Bacillus thuringiensis [Bacillus thuringiensis],6BT9_B Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis]
6KXN_A	8.40e-54	5	333	17	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
P20533	2.49e-48	47	325	144	443	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
P36362	1.30e-38	7	334	39	389	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
Q95M17	2.27e-38	22	320	52	365	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
A6N6J0	1.62e-36	18	323	62	393	Endochitinase 46 OS=Trichoderma harzianum OX=5544 GN=chit46 PE=1 SV=1
Q11174	9.85e-36	8	334	68	421	Probable endochitinase OS=Caenorhabditis elegans OX=6239 GN=cht-1 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
1.000068	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004849_00052.