Detail Information for IndEnz0004000084
IED ID IndEnz0004000084
Enzyme Type ID xylanase000084
Protein Name PTI1-like tyrosine-protein kinase 2
PTI1-2
EC 2.7.10.2
Gene Name PTI12 At2g30740 T11J7.13
Organism Arabidopsis thaliana (Mouse-ear cress)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress)
Enzyme Sequence MRRWICCGDKKGDSDLSNEEVHLKSPWQNSEANQKNQKPQAVVKPEAQKEALPIEVPPLSVDEVKEKTDNFGSKSLIGEGSYGRVYYATLNDGKAVALKKLDVAPEAETNTEFLNQVSMVSRLKHENLIQLVGYCVDENLRVLAYEFATMGSLHDILHGRKGVQGAQPGPTLDWLTRVKIAVEAARGLEYLHEKVQPPVIHRDIRSSNVLLFEDYQAKVADFNLSNQAPDNAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMPRGQQSLVTWATPRLSEDKVKQCVDPKLKGEYPPKSVAKLAAVAALCVQYESEFRPNMSIVVKALQPLLKPPAPAPAPVPES
Enzyme Length 366
Uniprot Accession Number O49339
Absorption
Active Site ACT_SITE 203; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028"
Activity Regulation ACTIVITY REGULATION: Strongly activated in response to phosphatidic acid (PA) and xylanase in a OXI1- and PDK1-dependent manner, and, to a lesser extent, by hydrogen peroxide and flagellin in a OXI1-dependent manner. {ECO:0000269|PubMed:17040918}.
Binding Site BINDING 99; /note=ATP; /evidence=ECO:0000305
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
DNA Binding
EC Number 2.7.10.2
Enzyme Function FUNCTION: Probable tyrosine-protein kinase involved in oxidative burst-mediated signaling leading to specific genes expression. {ECO:0000269|PubMed:17040918}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 77..85; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00159
Features Active site (1); Binding site (1); Chain (1); Compositional bias (1); Domain (1); Mutagenesis (2); Nucleotide binding (1); Region (1)
Keywords ATP-binding;Kinase;Nucleotide-binding;Phosphoprotein;Plant defense;Reference proteome;Transferase;Tyrosine-protein kinase
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification PTM: Autophosphorylated and phosphorylated by OXI1. {ECO:0000269|PubMed:17040918}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 12169696; 15644463; 17317660; 22487254;
Motif
Gene Encoded By
Mass 40,500
Kinetics
Metal Binding
Rhea ID RHEA:10596
Cross Reference Brenda