CAZyme Information: MGYG000002606_01616

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-873
• CAZyme ID: MGYG000002606_01616
• CAZy Family: GH18
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
376		41266.83	5.2912

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002606	2480404	MAG	China	Asia

• Gene Location: Start: 5928; End: 7058 Strand: +

Full Sequence      

MKRLIPVLCMLLFASVAAMPSLTACSSGNDEPKKPVVKPDPEPEPDPEPGPAGTQVNEPA
DPMDDDHIVLAYFTSWSTGTPNPVYVTHINYAFGHVSDSFRSISIDSPDNLRKVAQLKKR
SSRLKVLLSIGGWESGNFSELCADADCRKAFAADCRRVLDEYGIDGIDIDWEYPGSSVAG
ISSSPDDPANFVLLLREIRDVLRDGELLTLASDATGLGLRFKELLPYVDYVSIMAYDLAE
PPRHHAPLYRSSTLAGHMTAAESVDKHLGAGVPAEKLVLGVPFYGRGSGVYKYSEPYSGI
TVRPGCTDRWDDVAKVPYITDATGAVVLGYENARSITCKRDYIKEKGLRGIMYWEYRYDD
TGNTLRRAAAGMLKMR

Enzyme Prediction     

No EC number prediction in MGYG000002606_01616.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	69	364	4.4e-67	0.9459459459459459

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	6.86e-95	69	359	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	6.46e-85	69	359	2	334	Glyco_18 domain.
pfam00704	Glyco_hydro_18	1.78e-80	69	359	2	307	Glycosyl hydrolases family 18.
cd02872	GH18_chitolectin_chitotriosidase	4.67e-68	72	364	4	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	3.96e-61	55	371	26	438	Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT34049.1	1.76e-116	21	373	13	354
AHW60606.1	1.21e-103	68	365	152	448
SCD19272.1	1.48e-103	68	368	36	336
QUT34047.1	6.56e-103	65	367	32	333
QRO23424.1	1.08e-101	65	369	27	330

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6INX_A	3.29e-55	86	372	27	342	Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
6TSB_AAA	1.43e-45	55	372	17	350	ChainAAA, Peroxiredoxin [Clostridioides difficile 630]
4NZC_A	1.45e-45	86	372	34	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]
6HM1_A	1.51e-45	86	372	31	393	Structuraland thermodynamic signatures of ligand binding to an enigmatic chitinase-D from Serratia proteamaculans [Serratia proteamaculans 568]
4PTM_A	1.61e-45	86	372	34	396	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20533	9.56e-42	65	355	42	434	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
Q91XA9	3.01e-35	69	360	24	366	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
Q6RY07	1.09e-34	69	360	24	366	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
Q95M17	2.84e-34	69	364	24	370	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
G5EAZ3	6.52e-34	70	373	7	361	Endochitinase B OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=chiB PE=1 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	0.000008	1.000041	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002606_01616.