CAZyme Information: MGYG000001036_01124

Basic Information

• Species: CAG-1031 sp900752535
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-1031; CAG-1031 sp900752535
• CAZyme ID: MGYG000001036_01124
• CAZy Family: GH18
• CAZyme Description: Chitinase A1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
237		26689.08	4.607

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001036	3018511	MAG	Sweden	Europe

• Gene Location: Start: 22; End: 735 Strand: +

Full Sequence      

MASTDSTRRAFAADCRRVADTYGLDGIDIDWEYPTSSESGISSSPEDTENYTKLMRDLRE
ALGPDRMLTMASVCSAKYVDFPAILPYTDFINVMAYDMARVPLHSSPLYRSERTGMSADE
ATRAHLVAGVPREKIVLGLPFYGRGRAPYTDFIDFRDIRPFEGCTEEWDSVAMAPYMANS
DGELVLGFDNPRSMTLKLDYILDNSLRGAMYWDYHCDDDAGTLRRLVARKILGRPQP

Enzyme Prediction     

No EC number prediction in MGYG000001036_01124.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	1	220	7.8e-54	0.7094594594594594

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	2.37e-72	1	217	103	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	1.14e-60	1	217	85	334	Glyco_18 domain.
pfam00704	Glyco_hydro_18	8.65e-58	1	213	82	303	Glycosyl hydrolases family 18.
cd02872	GH18_chitolectin_chitotriosidase	1.12e-51	1	222	90	346	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.
COG3325	ChiA	3.43e-37	1	223	145	428	Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AIF26577.1	9.68e-97	1	231	114	348
SCD19272.1	1.29e-90	1	232	109	342
QUT34047.1	1.51e-89	1	234	108	342
ADV45176.1	1.51e-89	1	232	108	340
QUT62465.1	4.07e-87	1	235	102	338

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6TSB_AAA	1.19e-39	2	228	109	347	ChainAAA, Peroxiredoxin [Clostridioides difficile 630]
6T9M_AAA	1.72e-39	2	228	128	366	ChainAAA, Peroxiredoxin [Clostridioides difficile 630]
6INX_A	2.38e-37	2	217	81	329	Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
4NZC_A	2.65e-33	2	227	106	393	Crystalstructure of Chitinase D from Serratia proteamaculans at 1.45 Angstrom resolution [Serratia proteamaculans 568],4Q22_A Crystal structure of Chitinase D from Serratia proteamaculans in complex with N-acetyl glucosamine at 1.93 Angstrom resolution [Serratia proteamaculans 568]
6HM1_A	2.73e-33	2	227	103	390	Structuraland thermodynamic signatures of ligand binding to an enigmatic chitinase-D from Serratia proteamaculans [Serratia proteamaculans 568]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20533	1.93e-31	1	237	173	458	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
Q13231	3.60e-25	1	221	109	367	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
Q6RY07	1.84e-24	1	222	109	370	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
Q11174	2.20e-24	1	218	148	400	Probable endochitinase OS=Caenorhabditis elegans OX=6239 GN=cht-1 PE=1 SV=1
Q95M17	4.73e-24	1	222	109	370	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
1.000056	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001036_01124.