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CAZyme Information: MGYG000002368_01597

You are here: Home > Sequence: MGYG000002368_01597

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Vibrio metoecus
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Vibrionaceae; Vibrio; Vibrio metoecus
CAZyme ID MGYG000002368_01597
CAZy Family GH18
CAZyme Description Chitinase A
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
848 MGYG000002368_13|CGC3 90401.11 4.6295
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002368 3946363 Isolate United States North America
Gene Location Start: 60529;  End: 63075  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.14

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 159 578 4.3e-74 0.9459459459459459

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3325 ChiA 0.0 122 591 1 440
Chitinase, GH18 family [Carbohydrate transport and metabolism].
smart00636 Glyco_18 2.03e-127 160 575 1 334
Glyco_18 domain.
cd06548 GH18_chitinase 9.93e-126 161 575 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.
pfam00704 Glyco_hydro_18 4.68e-90 160 575 1 307
Glycosyl hydrolases family 18.
cd02872 GH18_chitolectin_chitotriosidase 9.12e-67 161 575 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 E-Value Query Start Query End Hit Start Hit End
AET29241.1 0.0 1 848 1 849
ACQ62174.1 0.0 1 848 1 849
QHA23308.1 0.0 1 848 1 849
AVH54254.1 0.0 1 848 1 849
QTV03989.1 0.0 1 848 1 849

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3B9A_A 0.0 22 589 1 568
ChainA, Chitinase A [Vibrio harveyi],3B9D_A Chain A, Chitinase A [Vibrio harveyi],3B9E_A Chain A, Chitinase A [Vibrio harveyi]
3ARO_A 0.0 22 589 1 568
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]
3ARS_A 0.0 22 589 1 568
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 1.33e-194 21 590 1 536
ChitinaseA from Serratia marcescens ATCC990 in complex with Chitotrio-thiazoline dithioamide. [Serratia marcescens]
2WLY_A 1.75e-194 21 590 1 536
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 3.88e-286 15 834 15 815
Chitinase A OS=Pseudoalteromonas piscicida OX=43662 GN=chiA PE=1 SV=1
P07254 1.81e-192 5 590 16 559
Chitinase A OS=Serratia marcescens OX=615 GN=chiA PE=1 SV=3
P41684 1.22e-153 15 583 11 541
Chitinase OS=Autographa californica nuclear polyhedrosis virus OX=46015 GN=CHIA PE=1 SV=1
O10363 4.09e-151 18 585 13 542
Probable endochitinase OS=Orgyia pseudotsugata multicapsid polyhedrosis virus OX=262177 GN=ORF124 PE=3 SV=1
P20533 9.87e-67 160 818 46 676
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
0.000444 0.998196 0.000745 0.000223 0.000189 0.000170

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002368_01597.