| IED ID | IndEnz0018001372 |
| Enzyme Type ID | peroxidase001372 |
| Protein Name |
Protein phosphatase 2C 77 AtPP2C77 EC 3.1.3.16 Protein ABSCISIC ACID-INSENSITIVE 2 Protein phosphatase 2C ABI2 PP2C ABI2 |
| Gene Name | ABI2 PP2C77 At5g57050 MHM17.19 |
| 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 | MDEVSPAVAVPFRPFTDPHAGLRGYCNGESRVTLPESSCSGDGAMKDSSFEINTRQDSLTSSSSAMAGVDISAGDEINGSDEFDPRSMNQSEKKVLSRTESRSLFEFKCVPLYGVTSICGRRPEMEDSVSTIPRFLQVSSSSLLDGRVTNGFNPHLSAHFFGVYDGHGGSQVANYCRERMHLALTEEIVKEKPEFCDGDTWQEKWKKALFNSFMRVDSEIETVAHAPETVGSTSVVAVVFPTHIFVANCGDSRAVLCRGKTPLALSVDHKPDRDDEAARIEAAGGKVIRWNGARVFGVLAMSRSIGDRYLKPSVIPDPEVTSVRRVKEDDCLILASDGLWDVMTNEEVCDLARKRILLWHKKNAMAGEALLPAEKRGEGKDPAAMSAAEYLSKMALQKGSKDNISVVVVDLKGIRKFKSKSLN |
| Enzyme Length | 423 |
| Uniprot Accession Number | O04719 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Phosphatase activity repressed by oxidized ATGPX3, free fatty acids (e.g. arachidonic acid (20:4) and Linolenic acid (18:3)) and by H(2)O(2). Repressed by PYR/PYL/RCAR ABA receptors in an ABA-dependent manner. {ECO:0000269|PubMed:11882947, ECO:0000269|PubMed:19407142, ECO:0000269|PubMed:19769575}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:11882947}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:11882947}; |
| DNA Binding | |
| EC Number | 3.1.3.16 |
| Enzyme Function | FUNCTION: Repressor of the abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as stomatal closure, osmotic water permeability of the plasma membrane (Pos), high light stress, response to glucose, seed germination and inhibition of vegetative growth. During the stomatal closure regulation, modulates the inward calcium-channel permeability as well as H(2)O(2) and oxidative burst in response to ABA and dehydration. Represses GHR1 and, to some extent, SRK2E/OST1, kinases involved in the regulation of SLAC1-dependent stomatal closure (PubMed:22730405). Controls negatively fibrillin that is involved in mediating ABA-induced photoprotection. May be implicated in ABA content regulation. Involved in acquired thermotolerance of root growth and seedling survival. Required for the Erwinia amylovora harpin-induced (HrpN) drought tolerance. Involved in the hydrotropic response. {ECO:0000269|PubMed:10488243, ECO:0000269|PubMed:10872217, ECO:0000269|PubMed:10950871, ECO:0000269|PubMed:11208021, ECO:0000269|PubMed:11701885, ECO:0000269|PubMed:11707572, ECO:0000269|PubMed:12119381, ECO:0000269|PubMed:12194854, ECO:0000269|PubMed:12232276, ECO:0000269|PubMed:12447533, ECO:0000269|PubMed:12609042, ECO:0000269|PubMed:14576281, ECO:0000269|PubMed:14596925, ECO:0000269|PubMed:15599761, ECO:0000269|PubMed:15923322, ECO:0000269|PubMed:16339784, ECO:0000269|PubMed:16571665, ECO:0000269|PubMed:18278579, ECO:0000269|PubMed:22730405, ECO:0000269|PubMed:8787023, ECO:0000269|PubMed:9090884, ECO:0000269|PubMed:9108297, ECO:0000269|PubMed:9165752, ECO:0000269|PubMed:9276963}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:11882947}; |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Beta strand (14); Chain (1); Compositional bias (1); Disulfide bond (1); Domain (1); Helix (13); Metal binding (7); Mutagenesis (1); Region (1); Site (1); Turn (2) |
| Keywords | 3D-structure;Abscisic acid signaling pathway;Alternative splicing;Disulfide bond;Hydrolase;Magnesium;Manganese;Metal-binding;Protein phosphatase;Reference proteome |
| Interact With | Q9LDI3; O81439; Q8H1R0; Q9FLB1; Q8S8E3; Q9FGM1; Q84MC7; O49686; Q84JG2; Q8VZS8; O80992; Q9SSM7; O80920; Q9FLB1; Q8S8E3; O49686; Q39192; Q940H6; Q39193 |
| Induction | INDUCTION: Repressed by MYB44 and ERF4. Induced by salt stress and ABA. {ECO:0000269|PubMed:14731256, ECO:0000269|PubMed:16021341, ECO:0000269|PubMed:16998070, ECO:0000269|PubMed:18162593}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 3NMV; 3UJK; 3UJL; |
| Mapped Pubmed ID | 10480396; 10527431; 10787063; 10972885; 11779861; 11851911; 12008902; 12232124; 12369629; 12417701; 12446847; 12468729; 12514244; 12662310; 12678559; 12857845; 12970481; 12970489; 14648119; 16280546; 16359384; 16365038; 16667813; 17427804; 1834244; 18365246; 19033529; 19240210; 19302418; 19458118; 19624469; 19855047; 20128877; 20519338; 20639406; 20699393; 20803085; 20930557; 21245191; 21478367; 21525137; 21610183; 21666226; 21692804; 21746700; 21798944; 21821598; 21837565; 21885535; 21976481; 22041934; 22121246; 22128331; 22311778; 22368268; 22516825; 22652060; 22705253; 22908257; 22968126; 22995285; 23007729; 23370718; 23437216; 23483290; 23590427; 23606412; 23658427; 23660402; 23766366; 24078097; 24098330; 24223981; 24279988; 24706923; 24808098; 24836325; 25447637; 25943353; 25948280; 25976841; 26290265; 26491145; 26667153; 26974851; 27192441; 27406784; 27486921; 27566404; 27577789; 28067583; 28174577; 28494202; 29490615; 29618630; 29852366; 30528785; 30740122; 30886115; 31207493; 31708935; 31733960; 32619606; 32933749; 34099554; 8492808; 8761454; 8771791; 8883386; 9112773; 9351242; 9765153; 9862504; 9869399; |
| Motif | |
| Gene Encoded By | |
| Mass | 46,306 |
| Kinetics | |
| Metal Binding | METAL 165; /note="Magnesium 1"; /evidence="ECO:0000269|PubMed:20729862, ECO:0000269|PubMed:22116026, ECO:0007744|PDB:3NMV, ECO:0007744|PDB:3UJL"; METAL 165; /note="Magnesium 2"; /evidence="ECO:0000269|PubMed:20729862, ECO:0000269|PubMed:22116026, ECO:0007744|PDB:3NMV, ECO:0007744|PDB:3UJK, ECO:0007744|PDB:3UJL"; METAL 251; /note="Magnesium 1"; /evidence="ECO:0000269|PubMed:20729862, ECO:0000269|PubMed:22116026, ECO:0007744|PDB:3NMV, ECO:0007744|PDB:3UJL"; METAL 252; /note="Magnesium 1"; /evidence="ECO:0000269|PubMed:20729862, ECO:0000269|PubMed:22116026, ECO:0007744|PDB:3NMV, ECO:0007744|PDB:3UJL"; METAL 337; /note="Magnesium 1; via amide nitrogen"; /evidence="ECO:0000269|PubMed:20729862, ECO:0000269|PubMed:22116026, ECO:0007744|PDB:3NMV, ECO:0007744|PDB:3UJL"; METAL 337; /note="Magnesium 2"; /evidence="ECO:0000269|PubMed:20729862, ECO:0000269|PubMed:22116026, ECO:0007744|PDB:3NMV, ECO:0007744|PDB:3UJK, ECO:0007744|PDB:3UJL"; METAL 402; /note="Magnesium 2"; /evidence="ECO:0000269|PubMed:20729862, ECO:0000269|PubMed:22116026, ECO:0007744|PDB:3NMV, ECO:0007744|PDB:3UJK, ECO:0007744|PDB:3UJL" |
| Rhea ID | RHEA:20629; RHEA:47004 |
| Cross Reference Brenda |