CAZyme Information: MGYG000001979_00683

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Acutalibacter
• CAZyme ID: MGYG000001979_00683
• CAZy Family: GH18
• CAZyme Description: Chitinase A1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
341		38030.13	5.5901

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001979	1528030	MAG	Spain	Europe

• Gene Location: Start: 1241; End: 2266 Strand: -

Full Sequence      

MKKMLLGYVGAQATVSQEDGQKLTHIHLAFGKVYPDGSVQAGQLPVLEQLEQLRCWNPGL
RCSVSLINGDPQAFTTVCGDPKLRQSFAQSCRELVETFQLDGIDLDWEYPCVTTNGSDAS
PDDRENFTLTLRALRRKLDTLPGKPSLSIAAAAEPFYTRCVDLQAIAPLLDYLCLMTYDL
KGNPHAVAGHHTALYETPGDIFPNSCAGALELFHRCGVPKEKLLLGAAFYSRKWVDLPDR
YHGLLQMSPQGGGYGPGYGELVRGFLNQNGFTYYWDETAKAPYLFDGSTFLSFDDPRSLE
EKCRYVRQEGYGGVFYWEHSCDPTGVLLHSLWEGLYPKKCQ

Enzyme Prediction     

EC	3.2.1.14

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	16	322	2.2e-59	0.8513513513513513

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	1.18e-87	19	322	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	9.54e-72	7	322	10	334	Glyco_18 domain.
pfam00704	Glyco_hydro_18	2.29e-66	5	318	2	303	Glycosyl hydrolases family 18.
COG3325	ChiA	1.46e-63	19	335	61	436	Chitinase, GH18 family [Carbohydrate transport and metabolism].
cd02872	GH18_chitolectin_chitotriosidase	2.86e-52	24	317	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
ANS77385.1	1.49e-100	5	331	14	345
SYX83526.1	1.81e-98	2	334	5	342
QDM46973.1	2.57e-98	2	334	5	342
QTH44190.1	3.89e-97	4	335	6	342
QBO56278.1	1.18e-96	4	335	6	342

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6INX_A	4.30e-98	4	335	6	342	Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
5GZU_A	2.53e-65	19	338	46	394	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	1.09e-64	19	338	297	645	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	5.85e-49	49	322	147	448	ChitinaseChiA74 from Bacillus thuringiensis [Bacillus thuringiensis],6BT9_B Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis]
1ITX_A	6.15e-47	47	331	110	415	ChainA, Glycosyl Hydrolase [Niallia circulans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20533	1.74e-44	47	331	142	447	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
O81862	5.57e-30	8	330	34	361	Class V chitinase OS=Arabidopsis thaliana OX=3702 GN=ChiC PE=1 SV=1
P32470	4.95e-28	7	335	48	398	Chitinase 1 OS=Aphanocladium album OX=12942 GN=CHI1 PE=1 SV=2
Q11174	7.78e-28	24	337	83	414	Probable endochitinase OS=Caenorhabditis elegans OX=6239 GN=cht-1 PE=1 SV=1
E9ERT9	3.40e-27	74	325	138	387	Endochitinase 1 OS=Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) OX=655844 GN=chit1 PE=3 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
0.999562	0.000484	0.000001	0.000001	0.000000	0.000001

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001979_00683.