IED ID | IndEnz0009000047 |
Enzyme Type ID | chitinase000047 |
Protein Name |
Endochitinase 3 EC 3.2.1.14 |
Gene Name | CHN14 |
Organism | Nicotiana tabacum (Common tobacco) |
Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae asterids lamiids Solanales Solanaceae Nicotianoideae Nicotianeae Nicotiana Nicotiana tabacum (Common tobacco) |
Enzyme Sequence | MRLLEFTALSSLLVLFLLLAVSAEQCGKQAGGARCPSGMCCSNFGWCGNTQDYCGPGKCQSQCPSGPGPTPRPPTPTPGPSTGDISNIISSSMFDQMLKHRNDNTCQGKSFYTYNAFITAARSFRGFGTTGDTTRRKREVAAFFAQTSHETTGGWDTAPDGRYAWGYCYLREQGNPPSYCVQSSQWPCAPGQKYYGRGPIQISYNYNYGPCGRAIGQNLLNNPDLVATNAVVSFKSAIWFWMTAQSPKPSCHDVITGRWTPSAADRAANRLPGYGVITNIINGGLECGHGSDARVQDRIGFYRRYCSILGVSPGDNIDCGNQKSFNSGLLLETM |
Enzyme Length | 334 |
Uniprot Accession Number | P29059 |
Absorption | |
Active Site | ACT_SITE 150; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P29022 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14; |
DNA Binding | |
EC Number | 3.2.1.14 |
Enzyme Function | FUNCTION: Defense against chitin-containing fungal pathogens. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Compositional bias (1); Disulfide bond (7); Domain (1); Modified residue (3); Propeptide (1); Region (1); Signal peptide (1) |
Keywords | Carbohydrate metabolism;Chitin degradation;Chitin-binding;Disulfide bond;Glycosidase;Hydrolase;Hydroxylation;Plant defense;Polysaccharide degradation;Reference proteome;Signal;Vacuole |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Vacuole {ECO:0000305}. Note=Vacuolar and protoplast. {ECO:0000305}. |
Modified Residue | MOD_RES 73; /note=4-hydroxyproline; /evidence=ECO:0000250; MOD_RES 74; /note=4-hydroxyproline; /evidence=ECO:0000250; MOD_RES 76; /note=4-hydroxyproline; /evidence=ECO:0000250 |
Post Translational Modification | PTM: The 4-hydroxyproline residues are not glycosylated in this plant vacuolar protein. {ECO:0000250}. |
Signal Peptide | SIGNAL 1..23 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 36,221 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |