| IED ID | IndEnz0018000320 |
| Enzyme Type ID | peroxidase000320 |
| Protein Name |
Respiratory burst oxidase homolog protein B EC 1.11.1.- EC 1.6.3.- NADPH oxidase RBOHB StRBOHB |
| Gene Name | RBOHB |
| Organism | Solanum tuberosum (Potato) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae asterids lamiids Solanales Solanaceae Solanoideae Solaneae Solanum Solanum tuberosum (Potato) |
| Enzyme Sequence | MEIENTRDSDSMRGSRVGFSGSLVSGKKSARFKDDESYVEITLDVRDDSVSVQNIKGADHEAALLASRLEKRPNNTLGSQLSFHLRQVSKELKRMTSSNKFQKIDRSKSGAARALRGLQFMNKNVGTEGWSEVESRFDQLAVNGMLTKSLFGQCIGMKESSEFAEELFDALARKRCITSPAVTKDELREFWEQITDTSFDARLQTFFDMVDKDADGRITQEEVKEIISLSASANKLSKIQDNSDEYAALIMEELDPGNVGYIELYNLETLLLQAPSHSMNLSTNSRVLSRMLSQKLKPTKERNPFKRCKRRLDYFIEDNWKRIWVMALWLSICAGLFTWKFIQYKRRAVFDVMGYCVSVAKGGAETTKFNMALVLLPVCRNTITWLRSRTKLGKIIPFDDNINFHKVIAFGIAVGVGLHAISHLTCDFPRLLHATDEEYEPMKPFFGDERPNNYWWFVKGTEGWTGVVMVVLMIIAYVLAQPWFRRNRLNLPSTIKKLTGFNAFWYSHHLFVIVYVLFIIHGYFLYLSKKWYKKTTWMYIAVPMILYACERLLRAFRSGYKAVKILKVAVYPGNVMAVHMSKPQGFKYTSGQYIFVNCSDVSSFQWHPFTISSAPGDDYLSMHIRTLGDWTSQLKTLFSKVCEPPTGDQSGLLRADVAKADYKPRLPKLLIDGPYGAPAQDYKKYDVVLLVGLGIGATPLISIVKDVLNNIKQQKNIEDGTKGSKRSPFATKRAYFYWVTREQGSFEWFKGVMDEVSENDQEGLIELHNYCTSVYEEGDARSALITMLQSIQQAKSGVDIVSGTRVKTHFARPNWRQVFKRVTINHPDQRIGVFYCGPQGLVGELRHLSQDFSHKTGTKFEFHKENF |
| Enzyme Length | 867 |
| Uniprot Accession Number | Q948T9 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by diphenylene iodinium (DPI). {ECO:0000269|PubMed:11386368}. |
| 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 massive phase II oxidative burst induced by pathogen infection. {ECO:0000269|PubMed:11386368}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (4); Metal binding (5); Modified residue (2); Mutagenesis (3); Region (3); Topological domain (7); Transmembrane (6) |
| Keywords | Calcium;Cell membrane;FAD;Flavoprotein;Membrane;Metal-binding;NADP;Oxidoreductase;Peroxidase;Phosphoprotein;Reference proteome;Repeat;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | INDUCTION: By fungal elicitor, arachidonic acid and salicylic acid. {ECO:0000269|PubMed:11386368, ECO:0000269|PubMed:16551687}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16551687}; Multi-pass membrane protein {ECO:0000269|PubMed:16551687}. |
| Modified Residue | MOD_RES 82; /note=Phosphoserine; by CPK; /evidence=ECO:0000269|PubMed:17400895; MOD_RES 97; /note=Phosphoserine; by CPK; /evidence=ECO:0000269|PubMed:17400895 |
| Post Translational Modification | PTM: Phosphorylation at Ser-82 and Ser-97 is required for full activity of RBOHB. Not phosphorylated at Ser-89. Phosphorylation at Ser-82 is induced by fungal elicitor treatment. {ECO:0000269|PubMed:17400895}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 23569203; |
| Motif | |
| Gene Encoded By | |
| Mass | 99,051 |
| Kinetics | |
| Metal Binding | METAL 211; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 213; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 215; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 217; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 222; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448 |
| Rhea ID | |
| Cross Reference Brenda |