CAZyme Information: MGYG000001780_02190

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides
• CAZyme ID: MGYG000001780_02190
• CAZy Family: GH18
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
623	MGYG000001780_13|CGC1	68952.57	4.8973

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001780	6261722	MAG	Denmark	Europe

• Gene Location: Start: 99374; End: 101245 Strand: -

Full Sequence      

MKKIIFIAIAIMLGLSACHDDDYITGVPSFGPPEVNTMAEKVNGRIALGYVTYYGTALPD
PTYMTHINYAFAELYVKSNVYQKFDLQGNRERFDQVKKLKARNSDLKILLSFTNSVSNSG
NSQDGGFSALAKSPEMRKQFAQDCKKFVQQEGIDGIDIDWEFPGMTFGSNAYDELVDVEN
FTLLMKDLRETLGSSILLTYAGYCKNKQPQGAGWKYIDVKAVDPYVDFVNIMTYDLVGAP
GHQSPLNKPSASWDCKRSVDEYLNAGVPASKLVLGIPFYGRAHFNSGGSVNYKDIVNLSE
SSGYVIDNWDAEGSVPYVTKDGVFYCGYDNPRSIAAKGEWLLGLGMKGMMFWDYDGDDSK
GTLRNALWNAVMKNDSDPGLNEFLNNSEGYKALVANCEKMISSGQYMAGTLIEETTSYPN
YEGYPVKLYEYTTGKDAQTGVAKKGMVYMLNPTAEKLATWIATAVWKTKNSADTDAMATV
LKHIQGQSGAQFPVCGIVYEDMSGTGYYPYLFKDGVTVYAADKSKWATEDPTHPGNYSCT
DDQLNYAVKVTNSDLNTYTGKYARICGTLREEYTANGGTVAVGTSDSQETRNLKWLDVVR
DLYKEAWNSGENKLITAWAKANL

Enzyme Prediction     

No EC number prediction in MGYG000001780_02190.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	60	365	4.6e-64	0.8682432432432432

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	6.26e-91	49	357	3	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.
pfam00704	Glyco_hydro_18	8.65e-68	49	357	4	307	Glycosyl hydrolases family 18.
smart00636	Glyco_18	1.68e-66	48	357	3	334	Glyco_18 domain.
cd02872	GH18_chitolectin_chitotriosidase	7.64e-61	60	362	24	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	2.50e-47	20	367	12	432	Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDO69853.1	0.0	1	623	1	623
QMI82040.1	1.78e-212	2	373	3	374
QPH57581.1	7.22e-212	2	373	3	374
QBJ17256.1	2.92e-211	2	373	3	374
BBK88809.1	1.93e-209	2	373	3	374

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4NZC_A	1.27e-35	60	359	30	385	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	1.32e-35	60	359	27	382	Structuraland thermodynamic signatures of ligand binding to an enigmatic chitinase-D from Serratia proteamaculans [Serratia proteamaculans 568]
4PTM_A	1.39e-35	60	359	30	385	CrystalStructure of Chitinase D from Serratia proteamaculans in complex with N-acetyl glucosamine, a hydrolyzed product of hexasaccharide at 1.7 Angstrom resolution [Serratia proteamaculans 568]
4LGX_A	1.47e-35	60	359	33	388	Structureof Chitinase D from Serratia proteamaculans revealed an unusually constrained substrate binding site [Serratia proteamaculans 568]
6F8N_A	4.29e-35	60	359	35	390	Keyresidues affecting transglycosylation activity in family 18 chitinases - Insights into donor and acceptor subsites [Serratia proteamaculans 568],6F8N_B Key residues affecting transglycosylation activity in family 18 chitinases - Insights into donor and acceptor subsites [Serratia proteamaculans 568]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20533	1.49e-28	50	367	56	447	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
Q95M17	4.73e-28	60	365	47	373	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
Q1E3R8	4.96e-28	65	367	65	398	Endochitinase 1 OS=Coccidioides immitis (strain RS) OX=246410 GN=CTS1 PE=3 SV=1
P0CB51	4.96e-28	65	367	65	398	Endochitinase 1 OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=CTS1 PE=1 SV=1
C5P230	5.48e-27	65	367	65	398	Endochitinase 1 OS=Coccidioides posadasii (strain C735) OX=222929 GN=CTS1 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000010	1.000017	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001780_02190.