CAZyme Information: MGYG000000286_00427

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; CAG-274
• CAZyme ID: MGYG000000286_00427
• CAZy Family: GH18
• CAZyme Description: Chitinase A1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
337		37871.93	4.7696

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000286	1017072	MAG	Sweden	Europe

• Gene Location: Start: 222; End: 1235 Strand: -

Full Sequence      

MKTVIGYVGTKDFNLLKEEDVKALSIINIAFGHVKNGDVVWEPQEAPKYMKWAKEINPEL
KICLSVGGWSAGGFSTAASTKEGRERFAKTAVDILKQYDLDGIDIDWEYPCISIAGIDAS
PDDKVNFTLLLEALRNELDKVENKKCLLMVATGGDEYFLRCTEMDKASKYLDIVQIMTYD
LRGGFSKQTGHHTNLYTSPTDLNSVSAHNTISKFIEAGVPREKIIMGVAFYSRMWTGVPN
VDNGHMQMADSTGGYGPGYGELVKEYINKNGYTRYWDDDAKAPYLFNGNTFISYDDEDSI
KAKADYVKENGLCGLMYWEYCLDDTFTLTTYLRKVLS

Enzyme Prediction     

No EC number prediction in MGYG000000286_00427.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	2	325	1.7e-72	0.9425675675675675

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	1.13e-103	4	323	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	2.20e-90	3	323	1	334	Glyco_18 domain.
pfam00704	Glyco_hydro_18	6.68e-84	20	323	19	307	Glycosyl hydrolases family 18.
COG3325	ChiA	5.53e-79	54	336	121	436	Chitinase, GH18 family [Carbohydrate transport and metabolism].
cd02872	GH18_chitolectin_chitotriosidase	2.83e-77	54	336	65	362	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
BCJ95062.1	4.45e-149	1	337	1	337
BCJ97222.1	2.65e-143	1	337	1	337
QUI22308.1	3.66e-141	4	333	6	335
QOV20718.1	8.09e-137	1	337	1	337
AVM42081.1	5.20e-133	4	333	12	342

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6INX_A	5.99e-125	4	337	7	343	Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
5GZU_A	2.28e-85	20	323	46	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	4.56e-84	20	323	297	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	8.74e-68	54	333	117	416	ChainA, Glycosyl Hydrolase [Niallia circulans]
6KXN_A	3.05e-66	20	336	29	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	1.64e-64	54	333	149	448	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
Q13231	7.98e-44	41	324	71	364	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
Q91XA9	1.78e-42	30	337	57	388	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
Q6RY07	2.47e-42	30	337	57	388	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
Q9D7Q1	2.99e-41	54	324	84	362	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2

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
1.000066	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000286_00427.