| IED ID | IndEnz0004000027 |
| Enzyme Type ID | xylanase000027 |
| Protein Name |
3-phosphoinositide-dependent protein kinase 1 AtPDK1 EC 2.7.11.1 |
| Gene Name | PDPK1 PDK1 At5g04510 T32M21.110 |
| 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 | MLAMEKEFDSKLVLQGNSSNGANVSRSKSFSFKAPQENFTSHDFEFGKIYGVGSYSKVVRAKKKETGTVYALKIMDKKFITKENKTAYVKLERIVLDQLEHPGIIKLYFTFQDTSSLYMALESCEGGELFDQITRKGRLSEDEARFYTAEVVDALEYIHSMGLIHRDIKPENLLLTSDGHIKIADFGSVKPMQDSQITVLPNAASDDKACTFVGTAAYVPPEVLNSSPATFGNDLWALGCTLYQMLSGTSPFKDASEWLIFQRIIARDIKFPNHFSEAARDLIDRLLDTEPSRRPGAGSEGYVALKRHPFFNGVDWKNLRSQTPPKLAPDPASQTASPERDDTHGSPWNLTHIGDSLATQNEGHSAPPTSSESSGSITRLASIDSFDSRWQQFLEPGESVLMISAVKKLQKITSKKVQLILTNKPKLIYVDPSKLVVKGNIIWSDNSNDLNVVVTSPSHFKICTPKKVLSFEDAKQRASVWKKAIETLQNR |
| Enzyme Length | 491 |
| Uniprot Accession Number | Q9XF67 |
| Absorption | |
| Active Site | ACT_SITE 167; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" |
| Activity Regulation | ACTIVITY REGULATION: Activated by phosphatidic acid (PA) and in response to the fungal elicitor xylanase. {ECO:0000269|PubMed:17040918}. |
| Binding Site | BINDING 73; /note=ATP; /evidence=ECO:0000250|UniProtKB:O15530; BINDING 128; /note=ATP; /evidence=ECO:0000250|UniProtKB:O15530; BINDING 171; /note=ATP; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:O15530; BINDING 185; /note=ATP; /evidence=ECO:0000250|UniProtKB:O15530 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:15358101}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:15358101}; |
| DNA Binding | |
| EC Number | 2.7.11.1 |
| Enzyme Function | FUNCTION: May couple lipid signals to the activation-loop phosphorylation of several protein kinases of the so-called AGC kinase family. Interacts via its pleckstrin homology domain with phosphatidic acid, PtdIns3P and PtdIns(3,4)P2 and to a lesser extent with PtdIns(4,5)P2 and PtdIns4P. May play a general role in signaling processes controlling the pathogen/stress response, polar auxin transport and development. Transphosphorylates the AGC protein kinases OXI1/AGC2-1, PK1/S6K1, PK19/S6K2 and PID resulting in their activation. {ECO:0000269|PubMed:10371193, ECO:0000269|PubMed:14749726, ECO:0000269|PubMed:16377759, ECO:0000269|PubMed:16601102, ECO:0000269|PubMed:16973627}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 54..56; /note=ATP; /evidence=ECO:0000250|UniProtKB:O15530; NP_BIND 122..124; /note=ATP; /evidence=ECO:0000250|UniProtKB:O15530 |
| Features | Active site (1); Binding site (4); Chain (1); Compositional bias (1); Domain (2); Erroneous initiation (1); Modified residue (5); Mutagenesis (6); Nucleotide binding (2); Region (4) |
| Keywords | ATP-binding;Alternative splicing;Cytoplasm;Kinase;Membrane;Nucleotide-binding;Phosphoprotein;Reference proteome;Serine/threonine-protein kinase;Transferase |
| Interact With | Q9LTW5; Q1PFB9; Q9FG74; Q9SUA3; Q39183; Q05999; Q9SJM3; Q9LUK3; O64682; Q64FQ2; F4I4F2; Q9M1P3; Q8RY37 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Membrane-associated after cell stimulation. {ECO:0000250}. |
| Modified Residue | MOD_RES 177; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:16125835; MOD_RES 211; /note=Phosphothreonine; by autocatalysis; /evidence=ECO:0000269|PubMed:16125835; MOD_RES 276; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:16125835; MOD_RES 337; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:19376835; MOD_RES 382; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:16125835 |
| Post Translational Modification | PTM: Phosphorylation on Thr-211 in the activation loop is required for full activity. PDK1 itself can autophosphorylate Thr-211, leading to its own activation. {ECO:0000269|PubMed:16125835}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 18650403; 21477822; 21625539; 21798944; 27247031; 27480805; 30742613; 32393878; 32393881; |
| Motif | |
| Gene Encoded By | |
| Mass | 54,711 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:17989; RHEA:46608 |
| Cross Reference Brenda |