CAZyme Information: MGYG000000151_02217

Basic Information

• Species: Clostridium paraputrificum
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium paraputrificum
• CAZyme ID: MGYG000000151_02217
• CAZy Family: GH18
• CAZyme Description: Chitinase A1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
342		39219.33	6.4055

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000151	3486414	Isolate	United Kingdom	Europe

• Gene Location: Start: 213399; End: 214427 Strand: -

Full Sequence      

MKKKYVIAYMRDGGLETITEEDAKKLTHVNLAFGKIDSEGKIYTKLKNLNELERIRKYNP
EIKFLISLGGWGNGGFSEAAMTEESRKFFNEEAIRFMKEHKLDGIDIDWEYPTSSISGIT
SSPKDKENFTLLLKDLREALDKEGKKDNRHYLLTIAAGADEYFIRFTNMKKVQKYLDYVM
LMTYDFRGGFQILTGHHTNLYTSSGDIFPSSIMNSVKLFEAAGVPSEKLLIGSAFYSRSW
TGVPNVNNGYLQMAQSTGGISQDFTDLDRDYINKNGYTRYWDDEAKAPYLFNGDNFISYD
DEESISHKTKYVKDNNLRGIMFWLYDADKTGKLLNAIHEGLK

Enzyme Prediction     

No EC number prediction in MGYG000000151_02217.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	4	331	2.1e-77	0.9459459459459459

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	1.32e-114	22	328	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	2.17e-97	17	328	17	334	Glyco_18 domain.
COG3325	ChiA	1.31e-93	22	341	61	436	Chitinase, GH18 family [Carbohydrate transport and metabolism].
pfam00704	Glyco_hydro_18	5.50e-87	22	328	19	307	Glycosyl hydrolases family 18.
cd02872	GH18_chitolectin_chitotriosidase	1.31e-79	27	341	29	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
AQM59229.1	6.12e-160	1	342	1	341
AIY82874.1	8.69e-160	1	342	1	341
AJS60325.1	1.42e-144	1	341	1	342
QDM46973.1	2.24e-144	4	342	5	344
SYX83526.1	3.00e-142	3	339	5	341

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6INX_A	5.93e-141	1	342	1	343	Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
5GZU_A	3.45e-88	22	341	46	391	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	8.37e-87	22	341	297	642	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	8.16e-77	48	341	109	419	ChainA, Glycosyl Hydrolase [Niallia circulans]
6BT9_A	1.17e-73	43	328	139	448	ChitinaseChiA74 from Bacillus thuringiensis [Bacillus thuringiensis],6BT9_B Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20533	2.75e-73	48	341	141	451	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
A6N6J0	2.40e-44	51	341	112	405	Endochitinase 46 OS=Trichoderma harzianum OX=5544 GN=chit46 PE=1 SV=1
P11797	1.15e-42	15	337	33	418	Chitinase B OS=Serratia marcescens OX=615 GN=chiB PE=1 SV=1
P48827	4.35e-42	49	341	109	398	Endochitinase 42 OS=Trichoderma harzianum OX=5544 GN=chit42 PE=1 SV=1
Q95M17	7.48e-42	55	335	83	373	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA 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
1.000052	0.000014	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000151_02217.