CAZyme Information: MGYG000003533_01966

Basic Information

• Species: SFTJ01 sp900769345
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; SFTJ01; SFTJ01 sp900769345
• CAZyme ID: MGYG000003533_01966
• CAZy Family: GH18
• CAZyme Description: Chitinase A1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
338	MGYG000003533_161|CGC1	37749.66	5.8234

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003533	2902010	MAG	Fiji	Oceania

• Gene Location: Start: 11437; End: 12453 Strand: +

Full Sequence      

MKRTILIAICVIAAIFVAKEVYETNFADRRVVVAYVTAGSDVMPDASLMTHINYAFGHVA
DSFDSLVISRPERLDQIVALKQQNKQLKVLISIGGWESGNFSEMAADSTLRTRFVQSCVD
AVNRHNLDGVDIDWEYPTSSAAGISSSPEDTQNFTRLMRDLRQALGSKVLLTFASVASAK
YVDFPAVLPYLDFVNVMSYDMAVVPRHHSALRSTDDDYMTIEKAVQCHLDAGVPVDKLVV
GLAFYGKGSIRPKRGTDIEVFKSENALTEHWNDEGQYAYLTDSLGNVVYSFDNAQSLAEK
CRFANSKHLRGAMYWEYSRNDSTHNLSRAVWDIISQDK

Enzyme Prediction     

No EC number prediction in MGYG000003533_01966.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	31	324	1.5e-67	0.9459459459459459

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	1.90e-97	32	318	1	320	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	7.11e-74	31	316	1	330	Glyco_18 domain.
pfam00704	Glyco_hydro_18	2.16e-73	31	318	1	305	Glycosyl hydrolases family 18.
cd02872	GH18_chitolectin_chitotriosidase	2.98e-72	45	315	24	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.
COG3325	ChiA	6.03e-56	28	331	36	436	Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SCD19272.1	3.20e-108	30	334	35	341
ADV45176.1	3.86e-108	30	338	34	343
QIK56154.1	6.49e-104	28	334	38	345
QUT34047.1	8.59e-104	28	338	32	343
QDO71383.1	1.18e-103	1	338	4	342

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6INX_A	1.22e-54	49	331	27	339	Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
5GZU_A	1.82e-49	45	331	46	388	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	2.68e-49	45	331	297	639	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	1.16e-45	74	329	110	417	ChainA, Glycosyl Hydrolase [Niallia circulans]
4NZC_A	1.10e-44	33	330	9	396	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20533	2.82e-43	74	329	142	449	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
Q9W092	1.55e-30	30	325	41	394	Probable chitinase 2 OS=Drosophila melanogaster OX=7227 GN=Cht2 PE=1 SV=1
Q9WTV1	6.68e-27	22	321	25	356	Chitinase-3-like protein 1 OS=Rattus norvegicus OX=10116 GN=Chi3l1 PE=2 SV=3
Q13231	9.28e-27	45	321	47	364	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
Q6TMG6	2.51e-26	45	336	26	360	Chitinase-3-like protein 1 OS=Ovis aries OX=9940 GN=CHI3L1 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
0.718584	0.276896	0.003710	0.000220	0.000179	0.000418

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003533_01966.