CAZyme Information: MGYG000003161_00599

Basic Information

• Species: Eubacterium_R sp900540305
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Eubacterium_R; Eubacterium_R sp900540305
• CAZyme ID: MGYG000003161_00599
• CAZy Family: GH18
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
663		73464.93	4.4242

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003161	2037503	MAG	United States	North America

• Gene Location: Start: 8767; End: 10758 Strand: +

Full Sequence      

MKAIKKIAEAVNSRSGSFIFFTLALSAFTFFYSSDWAYGFIIELYPLGNGFITLMFCLTG
AAALVSLISIIINAFSKDRKQIRGIKIFNAIHIIFAIIGIIAFIYTFALLFGLDKGITAS
GFQNGFSSLLPNIGYWGTAVALGLALTVVSVPKKAAKALIACVLILALIISPIALAQIST
GAEIANAPEMNIQSENLLTGAKIVYESLKKGEKADAVNLLDDSKKCWTAQDPQRTPEEGH
PDANNSYVEIELDGEKTFNTAVIEEDGNEAQYFRLQALVGDEWTTIYQSEKIQAQRLCSF
DPVTTSRIRLSIDKFRDSDTPVKIKSIKIYNEEKRNADNFEVTAYQRLDGDVPTEILARG
EEYVSNYARFYDVYSTIIVFGAVSWDENGNMSFGEGGEENFARQIEALKEIIAHRSNPDH
EVKLIVTALADGTWGDEHNGVNAYMGKYWESIADKIVAFAEKYEFDGVDIDWEYPQTAED
WKCFDNFIERLDEGLKKTNPDSILSSALSAGSLGLSKETLDRIDQIQFMAYDGKDEDGYQ
SSLQQAQEGLADFIKNGADITKINIGIAAYGRPVNGSPYWASWRALEEANYWDNKYYNVH
DAGQVYEGTFCSPALAGDKTAYALLTGCGGVMVFRVACDKTMDDPNSVSCGIENALQRYF
NEW

Enzyme Prediction     

EC	3.2.1.14	3.2.1.-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	377	646	6e-30	0.8851351351351351

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00704	Glyco_hydro_18	4.07e-23	376	634	24	302	Glycosyl hydrolases family 18.
smart00636	Glyco_18	1.57e-19	365	639	10	334	Glyco_18 domain.
cd06548	GH18_chitinase	5.38e-19	366	632	30	315	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.
cd00598	GH18_chitinase-like	1.60e-14	377	532	27	177	The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model.
cd02872	GH18_chitolectin_chitotriosidase	5.68e-14	376	572	29	245	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
NP_001034515.1	2.64e-10	376	656	52	383
AAW67570.1	2.64e-10	376	656	52	383
AHX12961.1	3.32e-10	421	640	89	359
AAW67571.2	3.52e-10	376	656	52	383
AUB26577.1	1.09e-09	384	663	128	432

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6IGY_A	8.57e-07	356	640	52	362	Crystalstructure of Aspergillus niger chitinase B [Aspergillus niger]
6EPB_A	1.17e-06	450	640	148	384	Structureof Chitinase 42 from Trichoderma harzianum [Trichoderma harzianum]
3G6L_A	1.48e-06	384	644	80	371	Thecrystal structure of a chitinase CrChi1 from the nematophagous fungus Clonostachys rosea [Clonostachys rosea],3G6M_A crystal structure of a chitinase CrChi1 from the nematophagous fungus Clonostachys rosea in complex with a potent inhibitor caffeine [Clonostachys rosea]
1HKK_A	3.07e-06	388	572	42	248	Highresoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
1LG1_A	3.08e-06	388	572	42	248	CrystalStructure Of Human Chitotriosidase In Complex With Chitobiose [Homo sapiens],1LG2_A Crystal Structure Of Human Chitotriosidase In Complex With Ethylene Glycol [Homo sapiens],1LQ0_A Crystal Structure Of Human Chitotriosidase At 2.2 Angstrom Resolution [Homo sapiens],6ZE8_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_B Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_C Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_D Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_E Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_F Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q5AM60	3.35e-06	419	576	99	268	Chitinase 4 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=CHT4 PE=3 SV=1
P48827	6.39e-06	450	640	148	384	Endochitinase 42 OS=Trichoderma harzianum OX=5544 GN=chit42 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
1.000040	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
20	42
52	74
87	109
129	151
158	180