CAZyme Information: MGYG000003424_01834

Basic Information

• Species: SFTJ01 sp004557385
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; SFTJ01; SFTJ01 sp004557385
• CAZyme ID: MGYG000003424_01834
• CAZy Family: GH18
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
578		64532.26	6.4604

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003424	2699357	MAG	Fiji	Oceania

• Gene Location: Start: 281; End: 2017 Strand: -

Full Sequence      

MTLRYLLTTILASSLLFCHAGSSQAAPKTGKNAEKVVVAYVTSWSDVTPDPKFMTHINYA
FGGVNKTFDGVDISNPERLKMIAGLKKQAPELKVLLSIGGWGSGRFSEMAADTLLRASFA
AACRRVVDLYNLDGIDIDWEYPTSKAAGISASPDDTRNFTKLMRDIRQAIGADKLLTLAT
VHNGSYIDFHGILPYIDFVNIMTYDMGNPPYLHSALYDSPNTNGNTTEAGVRAHLAAGVP
PSMLVVGMPFYGRGKEPFHSFADYGKMKSLPKGFSEKWDEKALVPYITDTEGKLVLGFEN
ARSLQIKCDYVIDNGLRGAMYWEYSGDDDNNTLRSAVADHILDKADKKHVLVISEGGGQH
GAFTQAAMQWLIEQGKKKNFAVNEIHRANAISERFLADYDLVIQLDFPPYTWPEYAEAAF
MRYIEEGSGAWIGFHHATLLGEFDGYPLWQWFSDFMGGITFKNYVAQLADGTVMVEDAKH
PVMKGVSRKFVLPDDEWYTYNRSPRGNVRVLASVDEASYTPTSDVKMGDHPVIWTNEAVK
AKNVYFQFGHSPLLLENKWFKRLFSNAIEWSLDSKHTK

Enzyme Prediction     

No EC number prediction in MGYG000003424_01834.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	34	334	1.1e-69	0.9628378378378378

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	8.67e-95	37	327	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	5.64e-76	36	327	1	334	Glyco_18 domain.
pfam00704	Glyco_hydro_18	1.57e-70	36	327	1	307	Glycosyl hydrolases family 18.
cd02872	GH18_chitolectin_chitotriosidase	4.80e-64	37	332	1	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	8.40e-59	36	340	39	435	Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ALJ58703.1	4.93e-265	20	572	23	571
QUT90190.1	4.93e-265	20	572	23	571
QPH57945.1	1.60e-261	15	573	15	573
QUT62465.1	3.54e-261	15	573	8	566
QQA31016.1	4.56e-261	15	573	15	573

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4NZC_A	1.69e-53	33	341	4	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	1.78e-53	33	341	1	393	Structuraland thermodynamic signatures of ligand binding to an enigmatic chitinase-D from Serratia proteamaculans [Serratia proteamaculans 568]
4PTM_A	1.91e-53	33	341	4	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]
4LGX_A	2.05e-53	33	341	7	399	Structureof Chitinase D from Serratia proteamaculans revealed an unusually constrained substrate binding site [Serratia proteamaculans 568]
6F8N_A	6.66e-53	33	341	9	401	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	1.82e-38	13	335	21	445	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
Q9W092	3.93e-33	15	328	18	390	Probable chitinase 2 OS=Drosophila melanogaster OX=7227 GN=Cht2 PE=1 SV=1
Q13231	2.61e-30	37	328	24	364	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
Q95M17	1.44e-28	37	332	24	370	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
O35744	6.24e-28	37	328	24	366	Chitinase-like protein 3 OS=Mus musculus OX=10090 GN=Chil3 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000699	0.705315	0.292893	0.000604	0.000244	0.000203

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003424_01834.