| IED ID | IndEnz0018000323 |
| Enzyme Type ID | peroxidase000323 |
| Protein Name |
Respiratory burst oxidase homolog protein D EC 1.11.1.- EC 1.6.3.- NADPH oxidase RBOHD AtRBOHD |
| Gene Name | RBOHD At5g47910 MCA23.25 |
| 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 | MKMRRGNSSNDHELGILRGANSDTNSDTESIASDRGAFSGPLGRPKRASKKNARFADDLPKRSNSVAGGRGDDDEYVEITLDIRDDSVAVHSVQQAAGGGGHLEDPELALLTKKTLESSLNNTTSLSFFRSTSSRIKNASRELRRVFSRRPSPAVRRFDRTSSAAIHALKGLKFIATKTAAWPAVDQRFDKLSADSNGLLLSAKFWECLGMNKESKDFADQLFRALARRNNVSGDAITKEQLRIFWEQISDESFDAKLQVFFDMVDKDEDGRVTEEEVAEIISLSASANKLSNIQKQAKEYAALIMEELDPDNAGFIMIENLEMLLLQAPNQSVRMGDSRILSQMLSQKLRPAKESNPLVRWSEKIKYFILDNWQRLWIMMLWLGICGGLFTYKFIQYKNKAAYGVMGYCVCVAKGGAETLKFNMALILLPVCRNTITWLRNKTKLGTVVPFDDSLNFHKVIASGIVVGVLLHAGAHLTCDFPRLIAADEDTYEPMEKYFGDQPTSYWWFVKGVEGWTGIVMVVLMAIAFTLATPWFRRNKLNLPNFLKKLTGFNAFWYTHHLFIIVYALLIVHGIKLYLTKIWYQKTTWMYLAVPILLYASERLLRAFRSSIKPVKMIKVAVYPGNVLSLHMTKPQGFKYKSGQFMLVNCRAVSPFEWHPFSITSAPGDDYLSVHIRTLGDWTRKLRTVFSEVCKPPTAGKSGLLRADGGDGNLPFPKVLIDGPYGAPAQDYKKYDVVLLVGLGIGATPMISILKDIINNMKGPDRDSDIENNNSNNNSKGFKTRKAYFYWVTREQGSFEWFKGIMDEISELDEEGIIELHNYCTSVYEEGDARVALIAMLQSLQHAKNGVDVVSGTRVKSHFAKPNWRQVYKKIAVQHPGKRIGVFYCGMPGMIKELKNLALDFSRKTTTKFDFHKENF |
| Enzyme Length | 921 |
| Uniprot Accession Number | Q9FIJ0 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by diphenylene iodinium (DPI). {ECO:0000269|PubMed:17601167}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 1.11.1.-; 1.6.3.- |
| Enzyme Function | FUNCTION: Calcium-dependent NADPH oxidase that generates superoxide. Involved in the generation of reactive oxygen species (ROS) during incompatible interactions with pathogens, in response to pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) signaling and in UV-B and abscisic acid ROS-dependent signaling and via SIK1 mediated activation by phosphorylation (PubMed:30212650). Might be required for ROS signal amplification during light stress. {ECO:0000269|PubMed:11756663, ECO:0000269|PubMed:12773379, ECO:0000269|PubMed:15608336, ECO:0000269|PubMed:16428598, ECO:0000269|PubMed:16913867, ECO:0000269|PubMed:17601167, ECO:0000269|PubMed:30212650}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (1); Domain (4); Metal binding (5); Modified residue (7); Region (3); Topological domain (7); Transmembrane (6) |
| Keywords | Calcium;FAD;Flavoprotein;Membrane;Metal-binding;NADP;Oxidoreductase;Peroxidase;Phosphoprotein;Plant defense;Reference proteome;Repeat;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | INDUCTION: Up-regulated by pathogen infection and by abscisic acid. {ECO:0000269|PubMed:12773379, ECO:0000269|PubMed:17601167}. |
| Subcellular Location | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. |
| Modified Residue | MOD_RES 8; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:30212650"; MOD_RES 9; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:30212650"; MOD_RES 26; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17651370"; MOD_RES 39; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:24629339, ECO:0007744|PubMed:19245862, ECO:0007744|PubMed:19376835"; MOD_RES 339; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:30212650"; MOD_RES 343; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:24629339, ECO:0007744|PubMed:17651370"; MOD_RES 347; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:24629339, ECO:0000269|PubMed:30212650, ECO:0007744|PubMed:17651370" |
| Post Translational Modification | PTM: Phosphorylated at Ser-39, Ser-343 and Ser-347 by BIK1 upon flagellin (flg22) treatment (PubMed:24629339). Activated by phosphorylation at Ser-347 mediated by SIK1 and at Ser-8, Ser-9 and Ser-339 upon flagellin (e.g. flg22) perception (PubMed:30212650). {ECO:0000269|PubMed:24629339, ECO:0000269|PubMed:30212650}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 15705948; 15923322; 16170317; 16367958; 16415066; 17160388; 17317660; 18212028; 18218618; 18467450; 18643991; 18790995; 19170932; 19321706; 19574254; 19690149; 19690331; 19704701; 19726575; 20023407; 20163553; 20592040; 20615112; 20820881; 20876608; 20951600; 20955078; 21071853; 21205037; 21261469; 21419340; 21421415; 21447999; 21492976; 21546454; 21668535; 21707649; 21802603; 21856300; 21937678; 21940718; 21964330; 21984648; 21985584; 22001402; 22007023; 22138967; 22155845; 22408091; 22422940; 22437147; 22645532; 22730426; 22751316; 22788984; 23095998; 23264520; 23314084; 23341360; 23365132; 23400703; 23441575; 23448237; 23500715; 23580750; 23649257; 23650383; 23709674; 23940555; 23952703; 23963673; 24033256; 24038652; 24085708; 24088017; 24098330; 24245741; 24372484; 24444075; 24477528; 24502504; 24510762; 24630626; 24699527; 24714570; 24755455; 25399352; 25462961; 25521759; 25704231; 25826261; 26039480; 26180024; 26649488; 26704641; 26765289; 26798024; 26883222; 27085087; 27247031; 27251529; 27261066; 27269509; 27288360; 27398933; 27494702; 27837091; 27909046; 27925401; 28018388; 28134437; 28164334; 28254779; 28337518; 28338729; 28537474; 28696275; 28698136; 28716416; 28716423; 28827453; 29071531; 29163585; 29166881; 29301018; 29398214; 29438048; 29463779; 29576081; 29868082; 29891679; 30013580; 30097007; 30188766; 30218537; 30238451; 30279198; 30300945; 30387369; 30426643; 30796836; 30873191; 30963238; 31067654; 31318449; 31379142; 31379894; 31488841; 31490027; 31515446; 31519798; 31666300; 32005378; 32024687; 32034035; 32059380; 32086363; 32234220; 32290990; 32296141; 32519347; 32530625; 32605179; 32680933; 32695131; 32910883; 32938754; 33101341; 33198167; 33210579; 34194036; 34797009; 35163000; |
| Motif | |
| Gene Encoded By | |
| Mass | 103,909 |
| Kinetics | |
| Metal Binding | METAL 266; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 268; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 270; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 272; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 277; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448 |
| Rhea ID | |
| Cross Reference Brenda | 1.6.3.1; |