dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000000151_00440

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Basic Information help

Species

Clostridium paraputrificum

Lineage

Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium paraputrificum

CAZyme ID

MGYG000000151_00440

CAZy Family

GH18

CAZyme Description

Chitinase A1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
475		53047	4.5375

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000151	3486414	Isolate	United Kingdom	Europe

Gene Location

Start: 465175; End: 466602 Strand: -

Full Sequence Download help

Enzyme Prediction help

EC	3.2.1.14

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH18	37	405	8e-64	0.9527027027027027

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	9.93e-88	39	400	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	1.19e-74	38	400	1	334	Glyco_18 domain.
pfam00704	Glyco_hydro_18	8.57e-67	38	400	1	307	Glycosyl hydrolases family 18.
cd02872	GH18_chitolectin_chitotriosidase	8.19e-55	48	395	18	336	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	4.73e-54	1	416	1	439	Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AWO79545.1	3.33e-105	18	417	10	422
BBO63336.1	9.40e-105	18	417	10	422
ASM17077.1	9.40e-105	18	417	10	422
QLJ22936.1	5.29e-104	18	417	10	422
QLJ31810.1	5.29e-104	18	417	10	422

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6HM1_A	6.31e-103	49	417	22	397	Structuraland thermodynamic signatures of ligand binding to an enigmatic chitinase-D from Serratia proteamaculans [Serratia proteamaculans 568]
4PTM_A	6.93e-103	49	417	25	400	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	7.62e-103	49	417	28	403	Structureof Chitinase D from Serratia proteamaculans revealed an unusually constrained substrate binding site [Serratia proteamaculans 568]
6F8N_A	2.76e-102	49	417	30	405	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]
4NZC_A	3.75e-101	49	415	25	398	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]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20533	1.09e-45	25	417	32	455	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
A6N6J0	3.73e-28	17	400	18	390	Endochitinase 46 OS=Trichoderma harzianum OX=5544 GN=chit46 PE=1 SV=1
Q873X9	5.28e-28	37	421	43	412	Endochitinase B1 OS=Neosartorya fumigata OX=746128 GN=chiB1 PE=1 SV=1
E9QRF2	5.28e-28	37	421	43	412	Endochitinase B1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=chiB1 PE=3 SV=1
P32470	8.66e-28	4	404	3	387	Chitinase 1 OS=Aphanocladium album OX=12942 GN=CHI1 PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.001553	0.997283	0.000305	0.000346	0.000265	0.000230

TMHMM Annotations download full data without filtering help

start	end
5	27
450	469