CAZyme Information: MGYG000000468_00045

Basic Information

• Species: UMGS1696 sp900554225
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; CAG-272; UMGS1696; UMGS1696 sp900554225
• CAZyme ID: MGYG000000468_00045
• CAZy Family: GH18
• CAZyme Description: Chitinase A1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
340		37376.11	5.0605

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000468	2935049	MAG	Fiji	Oceania

• Gene Location: Start: 55881; End: 56903 Strand: +

Full Sequence      

MLLCAYVFGHYDALTDEDAKKLDLINIAFGLIRDGRLHVPESVASPVWDRLRAANPSLRI
LLSIGGWGAGGFSTMAKAPSSRAVFIESCMCAVDEYALDGLDLDWEYPTIDSAGIDADPC
DRENFTCLLTELRHALDTRYPEKHKMLTIAAGGGEYYINAVEIPKIVPVLDYVSLMTYDL
AGTWTSAIHHTALYSTAVQPNSVDANVQRFMAAGVPAEKLVIGAAFYSRRWLHIPDGSTH
GLGQSATVSDPNSGNFGPGFGTLSGMRNRNGYTVYRDKTAHAPYLYNRETGEWISYDDPE
SVADKVRYAREHGLSGVMYWEHSCDPTRALLDAMFTAKGE

Enzyme Prediction     

EC	3.2.1.14

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	17	328	1.3e-68	0.8547297297297297

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	6.39e-102	11	325	15	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	1.13e-86	14	325	18	334	Glyco_18 domain.
COG3325	ChiA	1.09e-76	51	334	120	432	Chitinase, GH18 family [Carbohydrate transport and metabolism].
pfam00704	Glyco_hydro_18	2.15e-74	18	321	19	303	Glycosyl hydrolases family 18.
cd02872	GH18_chitolectin_chitotriosidase	7.78e-71	51	320	64	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
QOV20718.1	2.48e-91	14	330	16	328
ANU54368.1	1.20e-90	15	331	18	325
ASB42412.1	1.20e-90	15	331	18	325
QQR31699.1	1.20e-90	15	331	18	325
BCJ95062.1	8.79e-90	12	334	14	332

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6INX_A	9.41e-89	10	335	15	339	Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
5GZU_A	2.69e-68	3	325	28	377	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	1.48e-67	3	325	279	628	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	1.03e-54	20	330	72	411	ChainA, Glycosyl Hydrolase [Niallia circulans]
6KXN_A	1.82e-54	3	332	14	364	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	6.58e-52	20	330	104	443	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
P48827	6.04e-40	50	325	114	383	Endochitinase 42 OS=Trichoderma harzianum OX=5544 GN=chit42 PE=1 SV=1
A6N6J0	6.94e-39	50	325	115	390	Endochitinase 46 OS=Trichoderma harzianum OX=5544 GN=chit46 PE=1 SV=1
P32470	8.54e-39	51	323	115	381	Chitinase 1 OS=Aphanocladium album OX=12942 GN=CHI1 PE=1 SV=2
Q13231	2.41e-38	48	325	80	363	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 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
1.000025	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000468_00045.