dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Vibrio parahaemolyticus

Lineage

Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Vibrionaceae; Vibrio; Vibrio parahaemolyticus

CAZyme ID

MGYG000002331_01194

CAZy Family

GH18

CAZyme Description

Chitinase A

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
430	MGYG000002331_3\|CGC14	47959.04	4.8414

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002331	5262465	Isolate	Bangladesh	Asia

Gene Location

Start: 1319721; End: 1321013 Strand: -

Enzyme Prediction help

No EC number prediction in MGYG000002331_01194.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH18	21	426	2e-77	0.9763513513513513

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	2.58e-130	24	415	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.
COG3325	ChiA	5.13e-104	20	426	36	434	Chitinase, GH18 family [Carbohydrate transport and metabolism].
smart00636	Glyco_18	4.42e-102	23	415	1	334	Glyco_18 domain.
pfam00704	Glyco_hydro_18	1.90e-82	23	415	1	307	Glycosyl hydrolases family 18.
cd02872	GH18_chitolectin_chitotriosidase	2.56e-65	27	412	4	338	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 help

Hit ID	Query Start	Query End	Hit Start	Hit End
APC90155.1	1	430	1	430
AMG08339.1	1	430	1	430
AGB12451.1	1	430	1	430
QLE33660.1	1	430	1	430
APU76314.1	1	430	1	430

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3ARO_A	6.23e-82	23	428	139	566	CrystalStructure Analysis of Chitinase A from Vibrio harveyi with novel inhibitors - apo structure [Vibrio harveyi],3ARP_A Crystal Structure Analysis of Chitinase A from Vibrio harveyi with novel inhibitors - complex structure with DEQUALINIUM [Vibrio harveyi],3ARQ_A Crystal Structure Analysis of Chitinase A from Vibrio harveyi with novel inhibitors - complex structure with IDARUBICIN [Vibrio harveyi],3ARR_A Crystal Structure Analysis of Chitinase A from Vibrio harveyi with novel inhibitors - complex structure with PENTOXIFYLLINE [Vibrio harveyi],3ARV_A Crystal Structure Analysis of Chitinase A from Vibrio harveyi with novel inhibitors - complex structure with Sanguinarine [Vibrio harveyi],3ARW_A Crystal Structure Analysis of Chitinase A from Vibrio harveyi with novel inhibitors - complex structure with chelerythrine [Vibrio harveyi],3ARX_A Crystal Structure Analysis of Chitinase A from Vibrio harveyi with novel inhibitors - complex structure with Propentofylline [Vibrio harveyi],3ARY_A Crystal Structure Analysis of Chitinase A from Vibrio harveyi with novel inhibitors - complex structure with 2-(imidazolin-2-yl)-5-isothiocyanatobenzofuran [Vibrio harveyi],3ARZ_A Crystal Structure Analysis of Chitinase A from Vibrio harveyi with novel inhibitors - complex structure with 2-(imidazolin-2-yl)-5-isothiocyanatobenzofuran [Vibrio harveyi],3B8S_A Crystal structure of wild-type chitinase A from Vibrio harveyi [Vibrio harveyi],3B8S_B Crystal structure of wild-type chitinase A from Vibrio harveyi [Vibrio harveyi]
3B9A_A	6.72e-81	23	428	139	566	ChainA, Chitinase A [Vibrio harveyi],3B9D_A Chain A, Chitinase A [Vibrio harveyi],3B9E_A Chain A, Chitinase A [Vibrio harveyi]
3ARS_A	5.16e-80	23	428	139	566	CrystalStructure Analysis of Chitinase A from Vibrio harveyi with novel inhibitors - apo structure of mutant W275G [Vibrio harveyi],3ART_A Crystal Structure Analysis of Chitinase A from Vibrio harveyi with novel inhibitors - W275G mutant complex structure with DEQUALINIUM [Vibrio harveyi],3ARU_A Crystal Structure Analysis of Chitinase A from Vibrio harveyi with novel inhibitors - W275G mutant complex structure with PENTOXIFYLLINE [Vibrio harveyi],3AS0_A Crystal Structure Analysis of Chitinase A from Vibrio harveyi with novel inhibitors - W275G mutant complex structure with Sanguinarine [Vibrio harveyi],3AS1_A Crystal Structure Analysis of Chitinase A from Vibrio harveyi with novel inhibitors - W275G mutant complex structure with chelerythrine [Vibrio harveyi],3AS2_A Crystal Structure Analysis of Chitinase A from Vibrio harveyi with novel inhibitors - W275G mutant complex structure with Propentofylline [Vibrio harveyi],3AS3_A Crystal Structure Analysis of Chitinase A from Vibrio harveyi with novel inhibitors - W275G mutant complex structure with 2-(imidazolin-2-yl)-5-isothiocyanatobenzofuran [Vibrio harveyi]
2WK2_A	6.28e-77	22	424	135	529	ChitinaseA from Serratia marcescens ATCC990 in complex with Chitotrio-thiazoline dithioamide. [Serratia marcescens]
2WLY_A	7.61e-77	22	424	135	529	ChitinaseA from Serratia marcescens ATCC990 in complex with Chitotrio-thiazoline. [Serratia marcescens],2WLZ_A Chitinase A from Serratia marcescens ATCC990 in complex with Chitobio- thiazoline. [Serratia marcescens],2WM0_A Chitinase A from Serratia marcescens ATCC990 in complex with Chitobio- thiazoline thioamide. [Serratia marcescens]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P32823	7.38e-80	22	425	158	582	Chitinase A OS=Pseudoalteromonas piscicida OX=43662 GN=chiA PE=1 SV=1
P07254	1.26e-74	22	424	158	552	Chitinase A OS=Serratia marcescens OX=615 GN=chiA PE=1 SV=3
O10363	7.42e-68	22	429	147	545	Probable endochitinase OS=Orgyia pseudotsugata multicapsid polyhedrosis virus OX=262177 GN=ORF124 PE=3 SV=1
P41684	2.44e-64	20	424	146	541	Chitinase OS=Autographa californica nuclear polyhedrosis virus OX=46015 GN=CHIA PE=1 SV=1
P20533	1.81e-56	19	415	41	438	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1

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
0.000448	0.998816	0.000246	0.000172	0.000157	0.000143

TMHMM Annotations help

There is no transmembrane helices in MGYG000002331_01194.

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