dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000000989_01076

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Basic Information help

Species

Niameybacter sp900549765

Lineage

Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Cellulosilyticaceae; Niameybacter; Niameybacter sp900549765

CAZyme ID

MGYG000000989_01076

CAZy Family

GH18

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
454	MGYG000000989_18\|CGC1	50588.96	4.5032

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000989	3436851	MAG	Denmark	Europe

Gene Location

Start: 24866; End: 26230 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000000989_01076.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH18	137	434	1.4e-58	0.8918918918918919

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	3.67e-86	134	425	18	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	1.56e-69	133	425	17	334	Glyco_18 domain.
cd02872	GH18_chitolectin_chitotriosidase	4.27e-65	133	425	19	341	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.
pfam00704	Glyco_hydro_18	6.12e-63	137	425	18	307	Glycosyl hydrolases family 18.
COG3325	ChiA	9.34e-59	133	434	56	432	Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADZ83387.1	2.90e-185	61	452	118	511
QEH68851.1	1.26e-181	61	452	118	511
CEJ73325.1	3.31e-146	104	452	233	582
QYE99248.1	4.85e-143	104	452	233	582
AUN13970.1	9.70e-143	104	452	233	582

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6TSB_AAA	1.73e-147	94	452	6	364	ChainAAA, Peroxiredoxin [Clostridioides difficile 630]
6T9M_AAA	3.33e-147	94	452	25	383	ChainAAA, Peroxiredoxin [Clostridioides difficile 630]
5GZU_A	3.86e-53	166	435	97	388	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	7.69e-53	166	435	348	639	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]
6INX_A	7.49e-52	142	435	27	339	Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20533	1.19e-44	166	434	142	447	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
Q9BZP6	4.20e-32	134	425	43	365	Acidic mammalian chitinase OS=Homo sapiens OX=9606 GN=CHIA PE=1 SV=1
P48827	1.36e-31	145	449	67	409	Endochitinase 42 OS=Trichoderma harzianum OX=5544 GN=chit42 PE=1 SV=1
A6N6J0	3.55e-30	145	449	68	416	Endochitinase 46 OS=Trichoderma harzianum OX=5544 GN=chit46 PE=1 SV=1
O35744	1.08e-29	134	425	43	365	Chitinase-like protein 3 OS=Mus musculus OX=10090 GN=Chil3 PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000066	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000000989_01076.