CAZyme Information: MGYG000000537_00571

Basic Information

• Species: UMGS1826 sp900555435
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; UMGS1826; UMGS1826 sp900555435
• CAZyme ID: MGYG000000537_00571
• CAZy Family: GH18
• CAZyme Description: Chitinase A1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
323	MGYG000000537_6|CGC2	35515.22	6.2418

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000537	2340074	MAG	Fiji	Oceania

• Gene Location: Start: 37877; End: 38848 Strand: -

Full Sequence      

MILGYVVDGNTVTEGDARRLTHIHCAFGYLTKEGELSVEKLNMLGQISLWRQWNPELKVV
LSAAAGEPGAFSFCAGRAELRKKTAASLKKAVEQYGFDGIDLDWEYPCVPTTNGGVAFPE
DQKNFTLLCRAIREALPEGKSLSIASGADEFYLRCVEPEALAGILNYVCVMTYDLRCQFH
ALTGHHTGLFPAVGDLFYNSCSRALRLFEEAGFKRGQLLLGTGFYSRKWENVPDKNHGFL
QATASGGGYGPIYRDLVPLAAGKDGFVRYWDEEAKAPWLFDGSTFLSYEDGQSVRFKAEY
VKARKDTAGSFTGSTGATLPGNF

Enzyme Prediction     

EC	3.2.1.14

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	16	309	9.6e-49	0.8108108108108109

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	3.49e-64	2	312	1	316	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	1.12e-56	2	304	2	321	Glyco_18 domain.
pfam00704	Glyco_hydro_18	2.11e-54	2	305	2	295	Glycosyl hydrolases family 18.
COG3325	ChiA	1.35e-52	44	312	114	417	Chitinase, GH18 family [Carbohydrate transport and metabolism].
cd02872	GH18_chitolectin_chitotriosidase	4.33e-42	21	302	29	326	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	4.44e-89	1	302	7	315
ANS77385.1	1.11e-84	2	302	14	321
QJC53938.1	8.16e-84	4	304	9	316
SYX83526.1	1.19e-83	1	301	7	314
QHT63670.1	2.31e-83	3	301	8	313

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6INX_A	2.47e-84	1	305	6	317	Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
5GZU_A	2.19e-49	1	302	514	853	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	3.18e-49	1	302	765	1104	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	5.22e-44	45	304	146	435	ChitinaseChiA74 from Bacillus thuringiensis [Bacillus thuringiensis],6BT9_B Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis]
1ITX_A	2.49e-40	44	304	110	393	ChainA, Glycosyl Hydrolase [Niallia circulans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20533	3.05e-38	44	304	142	425	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
P11797	3.28e-24	10	305	34	396	Chitinase B OS=Serratia marcescens OX=615 GN=chiB PE=1 SV=1
P36362	1.42e-23	19	304	51	362	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
Q95M17	8.42e-23	21	302	52	350	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
O81862	7.19e-20	12	304	41	340	Class V chitinase OS=Arabidopsis thaliana OX=3702 GN=ChiC 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
1.000059	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000537_00571.