| Basic Information | |
|---|---|
| Species | Vitis vinifera |
| Cazyme ID | GSVIVT01027027001 |
| Family | GH18 |
| Protein Properties | Length: 290 Molecular Weight: 30843.6 Isoelectric Point: 4.5095 |
| Chromosome | Chromosome/Scaffold: 15 Start: 18502075 End: 18503302 |
| Description | chitinase A |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH18 | 27 | 239 | 6.1e-30 |
| TITVYWGQNGNEGSLADTCSSGNYGIVNIGFLIVFGNNQTPQLNLAGHCSNDCTGLSNDIRACQNQGIKVLLSLGGAGGSPFLTSAEDARQVAEYLWNNF LGGQSSSRPLGDAVLDGIDFDIEGGTNQHWDELAKALSEYKQQRTVYLSAAPQCPFPDAWMGTAIATGLFDYVWVQFYNNDCQFSGNADKLISAWNQWTT IQAGQVFLGLPAA | |||
| Full Sequence |
|---|
| Protein Sequence Length: 290 Download |
| MAHRSLPSLA LLCLILVASI SNTRAGTITV YWGQNGNEGS LADTCSSGNY GIVNIGFLIV 60 FGNNQTPQLN LAGHCSNDCT GLSNDIRACQ NQGIKVLLSL GGAGGSPFLT SAEDARQVAE 120 YLWNNFLGGQ SSSRPLGDAV LDGIDFDIEG GTNQHWDELA KALSEYKQQR TVYLSAAPQC 180 PFPDAWMGTA IATGLFDYVW VQFYNNDCQF SGNADKLISA WNQWTTIQAG QVFLGLPAAP 240 EAAGSGYIAP DVLVSQVLPS IKTSPKYGGV MLWSKYYDNG YSAAIKSSV* 300 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00598 | GH18_chitinase-like | 7.0e-11 | 28 | 205 | 192 | + The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model. | ||
| COG3469 | COG3469 | 4.0e-11 | 85 | 280 | 232 | + Chitinase [Carbohydrate transport and metabolism] | ||
| cd02871 | GH18_chitinase_D-like | 2.0e-18 | 27 | 282 | 317 | + GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins. The domain architecture of ChiD includes a catalytic glycosyl hydrolase family 18 (GH18) domain, a chitin-binding domain, and a fibronectin type III domain. The chitin-binding and fibronectin type III domains are located either N-terminal or C-terminal to the catalytic domain. This family includes exochitinase Chi36 from Bacillus cereus. | ||
| pfam00704 | Glyco_hydro_18 | 4.0e-30 | 26 | 278 | 341 | + Glycosyl hydrolases family 18. | ||
| cd02877 | GH18_hevamine_XipI_class_III | 4.0e-133 | 26 | 287 | 280 | + This conserved domain family includes xylanase inhibitor Xip-I, and the class III plant chitinases such as hevamine, concanavalin B, and PPL2, all of which have a glycosyl hydrolase family 18 (GH18) domain. Hevamine is a class III endochitinase that hydrolyzes the linear polysaccharide chains of chitin and peptidoglycan and is important for defense against pathogenic bacteria and fungi. PPL2 (Parkia platycephala lectin 2) is a class III chitinase from Parkia platycephala seeds that hydrolyzes beta(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-beta-D-glucopyranose units in chitin. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
| GO:0005975 | carbohydrate metabolic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| Swiss-Prot | P29060 | 0 | 8 | 289 | 5 | 291 | CHIA_TOBAC RecName: Full=Acidic endochitinase; Flags: Precursor |
| RefSeq | XP_002276365.1 | 0 | 20 | 289 | 44 | 317 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002279661.1 | 0 | 1 | 289 | 1 | 289 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002316626.1 | 0 | 28 | 289 | 6 | 272 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002331829.1 | 0 | 8 | 289 | 7 | 294 | predicted protein [Populus trichocarpa] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2hvm_A | 0 | 26 | 289 | 1 | 273 | A Chain A, Hevamine Mutant D125aE127A IN COMPLEX WITH TETRA-Nag |
| PDB | 1llo_A | 0 | 26 | 289 | 1 | 273 | A Chain A, Hevamine Mutant D125aE127A IN COMPLEX WITH TETRA-Nag |
| PDB | 1hvq_A | 0 | 26 | 289 | 1 | 273 | A Chain A, Crystal Structures Of Hevamine, A Plant Defence Protein With Chitinase And Lysozyme Activity, And Its Complex With An Inhibitor |
| PDB | 1kr0_A | 0 | 26 | 289 | 1 | 273 | A Chain A, Hevamine Mutant D125aY183F IN COMPLEX WITH TETRA-Nag |
| PDB | 1kr1_A | 0 | 26 | 289 | 1 | 273 | A Chain A, Hevamine Mutant D125aE127A IN COMPLEX WITH TETRA-Nag |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| chitin degradation II | 3.2.1.14-RXN | EC-3.2.1.14 | chitinase |
| chitin degradation II | RXN-12623 | EC-3.2.1.14 | chitinase |
| chitin degradation II | RXN-12624 | EC-3.2.1.14 | chitinase |
| chitin degradation III (carnivorous plants) | 3.2.1.14-RXN | EC-3.2.1.14 | chitinase |
