CAZyme Information: MGYG000000312_01841

Basic Information

• Species: Eisenbergiella sp900539715
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eisenbergiella; Eisenbergiella sp900539715
• CAZyme ID: MGYG000000312_01841
• CAZy Family: GH18
• CAZyme Description: Chitinase A1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
335		37792.57	4.8633

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000312	2782709	MAG	Sweden	Europe

• Gene Location: Start: 8649; End: 9656 Strand: -

Full Sequence      

MKKVLGYVIQDSVVTKEQANILTHIHVAFGNLTMEGDIVFDYHPFLKQMDQVRTWNPDIK
IVLSVVPKEPDAFTVVSASEELRENVAKTCARLVSQDGFDGVDFDWEYPCVPSNGMNCTP
EDRHNYTLLCEAAKRGMESVGGGSVSVAAGADLYYIDSIEPERMAEVLDYVCLMTYDLKC
GFHALSGHHTALYSSTGDVFRNSCDQARRLFESAGFPKEKLLMGAAFYSRKWEDVPDRYH
GFLQLTKTGGGYGPNYDKLADEYINKNGYVRYWDDEAKAPFLFNGSTFISYDDEESLAHK
CAYVKREDIGGIFYWCHSGDTKGVLLRRIAKELEE

Enzyme Prediction     

No EC number prediction in MGYG000000312_01841.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	5	322	1.9e-52	0.9324324324324325

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	1.19e-77	4	320	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	5.81e-64	3	315	1	329	Glyco_18 domain.
COG3325	ChiA	2.10e-61	22	326	65	429	Chitinase, GH18 family [Carbohydrate transport and metabolism].
pfam00704	Glyco_hydro_18	1.39e-58	3	315	1	302	Glycosyl hydrolases family 18.
cd02872	GH18_chitolectin_chitotriosidase	5.92e-47	23	333	29	362	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
QAV17545.1	5.23e-106	4	335	7	344
QDM46973.1	3.26e-105	14	326	20	336
BBH21983.1	3.35e-103	4	334	22	358
SYX83526.1	8.57e-103	14	326	20	336
ACX68259.1	4.73e-102	12	333	18	342

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6INX_A	4.69e-101	4	334	7	343	Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
5GZU_A	1.05e-64	23	321	51	378	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	4.30e-64	23	321	302	629	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]
6BT9_A	3.94e-53	48	322	147	450	ChitinaseChiA74 from Bacillus thuringiensis [Bacillus thuringiensis],6BT9_B Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis]
1ITX_A	2.13e-51	46	333	110	419	ChainA, Glycosyl Hydrolase [Niallia circulans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20533	9.75e-49	46	333	142	451	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
Q11174	1.98e-30	23	315	83	394	Probable endochitinase OS=Caenorhabditis elegans OX=6239 GN=cht-1 PE=1 SV=1
Q9D7Q1	1.92e-28	20	315	49	356	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2
A6N6J0	1.15e-26	19	323	62	393	Endochitinase 46 OS=Trichoderma harzianum OX=5544 GN=chit46 PE=1 SV=1
Q95M17	2.36e-26	23	315	52	360	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA 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
1.000064	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000312_01841.