Detail Information for IndEnz0009000078
IED ID IndEnz0009000078
Enzyme Type ID chitinase000078
Protein Name Endochitinase B
CHN-B
EC 3.2.1.14
Gene Name CHN50
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 MRLREFTALSSLLFSLLLLSASAEQCGSQAGGARCASGLCCSKFGWCGNTNDYCGPGNCQSQCPGGPTPPGGGDLGSIISSSMFDQMLKHRNDNACQGKGFYSYNAFINAARSFPGFGTSGDTTARKREIAAFFAQTSHETTGGWATAPDGPYAWGYCWLREQGSPGDYCTPSGQWPCAPGRKYFGRGPIQISHNYNYGPCGRAIGVDLLNNPDLVATDPVISFKSALWFWMTPQSPKPSCHDVIIGRWQPSSADRAANRLPGFGVITNIINGGLECGRGTDSRVQDRIGFYRRYCSILGVSPGDNLDCGNQRSFGNGLLVDTM
Enzyme Length 324
Uniprot Accession Number P24091
Absorption
Active Site ACT_SITE 140; /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); Disulfide bond (7); Domain (1); Modified residue (2); Propeptide (1); Signal peptide (1)
Keywords Carbohydrate metabolism;Chitin degradation;Chitin-binding;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Hydroxylation;Hypersensitive response;Pathogenesis-related protein;Plant defense;Polysaccharide degradation;Reference proteome;Signal;Vacuole
Interact With
Induction INDUCTION: By ethylene.
Subcellular Location SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:1946457}. Note=Vacuolar and protoplast.
Modified Residue MOD_RES 67; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:1496378; MOD_RES 69; /note=4-hydroxyproline; /evidence=ECO:0000269|PubMed:1496378
Post Translational Modification PTM: The 4-hydroxyproline residues are not glycosylated in this plant vacuolar protein.
Signal Peptide SIGNAL 1..23; /evidence=ECO:0000269|PubMed:16593796
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 34,721
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda