dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Plesiomonas shigelloides

Lineage

Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Plesiomonas; Plesiomonas shigelloides

CAZyme ID

MGYG000002536_02077

CAZy Family

GH18

CAZyme Description

Chitinase A

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
904	MGYG000002536_22\|CGC3	95739.91	5.4658

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002536	3653255	Isolate	not provided	not provided

Gene Location

Start: 209268; End: 211982 Strand: -

Enzyme Prediction help

EC	3.2.1.14

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH18	167	585	7.8e-77	0.9459459459459459

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3325	ChiA	1.28e-146	137	594	8	436	Chitinase, GH18 family [Carbohydrate transport and metabolism].
cd06548	GH18_chitinase	7.43e-127	169	582	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	8.56e-125	168	582	1	334	Glyco_18 domain.
pfam00704	Glyco_hydro_18	2.34e-94	168	582	1	307	Glycosyl hydrolases family 18.
cd02872	GH18_chitolectin_chitotriosidase	1.20e-66	169	582	1	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.

CAZyme Hits help

Hit ID	Query Start	Query End	Hit Start	Hit End
SBT61846.1	1	904	1	904
QOH79162.1	1	904	1	904
QWK96550.1	1	904	1	904
QWK93971.1	1	904	1	904
QIY08380.1	1	904	1	907

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5GPR_A	4.55e-213	23	596	16	551	Crystalstructure of chitinase-h from Ostrinia furnacalis [Ostrinia furnacalis],5GQB_A Crystal structure of chitinase-h from O. furnacalis in complex with chitohepatose [Ostrinia furnacalis],6JMN_A Crystal structure of Ostrinia furnacalis Chitinase h complexed with compound 2-8-s2 [Ostrinia furnacalis]
7VRG_A	8.15e-213	25	596	5	538	ChainA, Chitinase [Ostrinia furnacalis],7VRG_B Chain B, Chitinase [Ostrinia furnacalis]
3ARO_A	1.08e-211	23	595	1	567	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	1.22e-210	23	595	1	567	ChainA, Chitinase A [Vibrio harveyi],3B9D_A Chain A, Chitinase A [Vibrio harveyi],3B9E_A Chain A, Chitinase A [Vibrio harveyi]
3ARS_A	9.76e-210	23	595	1	567	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]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P32823	5.49e-256	21	845	17	818	Chitinase A OS=Pseudoalteromonas piscicida OX=43662 GN=chiA PE=1 SV=1
P07254	7.48e-206	1	596	1	558	Chitinase A OS=Serratia marcescens OX=615 GN=chiA PE=1 SV=3
O10363	1.69e-183	23	594	14	544	Probable endochitinase OS=Orgyia pseudotsugata multicapsid polyhedrosis virus OX=262177 GN=ORF124 PE=3 SV=1
P41684	4.41e-178	20	591	12	542	Chitinase OS=Autographa californica nuclear polyhedrosis virus OX=46015 GN=CHIA PE=1 SV=1
P20533	2.25e-61	172	826	49	676	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
0.000497	0.994570	0.004189	0.000293	0.000218	0.000196

TMHMM Annotations help

There is no transmembrane helices in MGYG000002536_02077.

You are here: Home > Sequence: MGYG000002536_02077