dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000000931_00433

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Basic Information help

Species

UMGS75 sp900538885

Lineage

Bacteria; Firmicutes; Bacilli; ML615J-28; CAG-313; UMGS75; UMGS75 sp900538885

CAZyme ID

MGYG000000931_00433

CAZy Family

GH18

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
530		58021.86	5.0758

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000931	1690546	MAG	Germany	Europe

Gene Location

Start: 13727; End: 15319 Strand: -

Full Sequence Download help

Enzyme Prediction help

EC	3.2.1.14

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH18	208	519	4.9e-65	0.9459459459459459

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00704	Glyco_hydro_18	9.43e-65	209	515	2	307	Glycosyl hydrolases family 18.
smart00636	Glyco_18	3.96e-64	209	515	2	334	Glyco_18 domain.
cd06548	GH18_chitinase	7.22e-62	209	515	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.
cd02872	GH18_chitolectin_chitotriosidase	3.00e-53	277	515	87	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.
COG3325	ChiA	4.98e-47	169	528	3	436	Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAA13974.1	2.27e-62	181	524	16	374
QLG42679.1	1.14e-61	194	524	10	357
QOS82416.1	6.02e-61	194	524	10	357
AUS97898.1	6.72e-56	206	529	9	348
AQM59229.1	8.06e-54	207	524	4	336

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6INX_A	1.50e-46	225	524	23	338	Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
5GZU_A	5.38e-46	225	516	46	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	7.98e-46	225	516	297	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]
6TSB_AAA	6.09e-40	220	529	45	351	ChainAAA, Peroxiredoxin [Clostridioides difficile 630]
6T9M_AAA	9.06e-40	220	529	64	370	ChainAAA, Peroxiredoxin [Clostridioides difficile 630]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q95M17	8.17e-32	234	515	56	365	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
Q6RY07	1.13e-31	234	530	56	385	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
Q91XA9	2.84e-29	234	530	56	385	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
Q9BZP6	9.94e-29	234	515	56	365	Acidic mammalian chitinase OS=Homo sapiens OX=9606 GN=CHIA PE=1 SV=1
Q9D7Q1	1.82e-27	225	515	47	361	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000224	0.142350	0.857256	0.000059	0.000071	0.000057

TMHMM Annotations help

There is no transmembrane helices in MGYG000000931_00433.