IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Involvement of lysine-88 of spinach ferredoxin-NADP+ reductase in the interaction with ferredoxin. Involvement of lysine-88 of spinach ferredoxin-NADP+ reductase in the interaction with ferredoxin. FEBS Lett. (0014-5793) 1994 imex curation Aliverti A., Corrado ME., Zanetti G. Apoptosis - Interactions involving proteins with a function related to apoptosis Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species fig 1, table 2 Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Aliverti A., Corrado ME., Zanetti G. Apoptosis - Interactions involving proteins with a function related to apoptosis fig 1, table 2 Accepted 10-MAR-2006 by KROBBE. FEBS Lett. (0014-5793) 1994 Only protein-protein interactions imex curation Involvement of lysine-88 of spinach ferredoxin-NADP+ reductase in the interaction with ferredoxin. Involvement of lysine-88 of spinach ferredoxin-NADP+ reductase in the interaction with ferredoxin. FEBS Lett. (0014-5793) 1994 imex curation Aliverti A., Corrado ME., Zanetti G. Apoptosis - Interactions involving proteins with a function related to apoptosis Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species fig 1, table 2 Only protein-protein interactions in vitro In vitro enzymatic study enzymatic study predetermined predetermined participant predetermined Aliverti A., Corrado ME., Zanetti G. Apoptosis - Interactions involving proteins with a function related to apoptosis NADPH ferredoxin dependant cytochrome c reductase activity of FNR. fig 1, table 2 Accepted 10-MAR-2006 by KROBBE. FEBS Lett. (0014-5793) 1994 Only protein-protein interactions imex curation Involvement of lysine-88 of spinach ferredoxin-NADP+ reductase in the interaction with ferredoxin. Involvement of lysine-88 of spinach ferredoxin-NADP+ reductase in the interaction with ferredoxin. FEBS Lett. (0014-5793) 1994 imex curation Aliverti A., Corrado ME., Zanetti G. Apoptosis - Interactions involving proteins with a function related to apoptosis Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species fig 1, table 2 Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink predetermined predetermined participant predetermined Aliverti A., Corrado ME., Zanetti G. Apoptosis - Interactions involving proteins with a function related to apoptosis The purified proteins were cross-linked with EDC. The formation of the complex after cross-linking was assessed by measuring the ferredoxin dependant cytochrome c reductase activity of FNR. fig 1, table 2 Accepted 10-MAR-2006 by KROBBE. FEBS Lett. (0014-5793) 1994 Only protein-protein interactions imex curation fer1_spiol Ferredoxin-1, chloroplastic Ferredoxin I PETF protein protein spiol Spinacia oleracea (Spinach) Spinach MAATTTTMMGMATTFVPKPQAPPMMAALPSNTGRSLFGLKTGSRGGRMTMAAYKVTLVTPTGNVEFQCPDDVYILDAAEEEGIDLPYSCRAGSCSSCAGKLKTGSLNQDDQSFLDDDQIDEGWVLTCAAYPVSDVTIETHKEEELTA 76045050A0AA8697 fenr_spiol Ferredoxin--NADP reductase, chloroplastic PETH protein protein spiol Spinacia oleracea (Spinach) Spinach MTTAVTAAVSFPSTKTTSLSARSSSVISPDKISYKKVPLYYRNVSATGKMGPIRAQIASDVEAPPPAPAKVEKHSKKMEEGITVNKFKPKTPYVGRCLLNTKITGDDAPGETWHMVFSHEGEIPYREGQSVGVIPDGEDKNGKPHKLRLYSIASSALGDFGDAKSVSLCVKRLIYTNDAGETIKGVCSNFLCDLKPGAEVKLTGPVGKEMLMPKDPNATIIMLGTGTGIAPFRSFLWKMFFEKHDDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPDNFRLDFAVSREQTNEKGEKMYIQTRMAQYAVELWEMLKKDNTYFYMCGLKGMEKGIDDIMVSLAAAEGIDWIEYKRQLKKAEQWNVEVY 1D0432BA47438A28 cyc_horse Cytochrome c CYCS CYC protein protein horse Equus caballus (Horse) Horse MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWKEETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE DIP protein P00004 original sequence version: 99 659BA128E53C3868 peth-petf-2 1 4 unspecified role unspecified role neutral component neutral component spiol Spinacia oleracea (Spinach) Spinach 5 unspecified role unspecified role neutral component neutral component P00455:p.Lys88Gln mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain K Q Wed May 02 20:30:59 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys88gln' Tue Jun 30 17:14:50 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys88Gln' ecoli Escherichia coli (strain K12) physical association physical association High ionic strength. The mutant K88Q of FNR have a lower affinity for ferredoxin. The Km for the wild type protein is 0.4 10-6 M, and the Km is 3.5 10-6 M for the K88Q mutant. peth-petf-4 3 4 unspecified role unspecified role neutral component neutral component spiol Spinacia oleracea (Spinach) Spinach 5 unspecified role unspecified role neutral component neutral component P00455:p.Lys88Gln mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain K Q Wed May 02 16:11:41 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys88gln' Tue Jun 30 16:23:05 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys88Gln' ecoli Escherichia coli (strain K12) physical association physical association High ionic strength. The mutant K88Q of FNR have a lower affinity for ferredoxin. The Km for the wild type protein is 0.4 10-6 M, and the Km is 3.5 10-6 M for the K88Q mutant. peth-petf-5 2 5 enzyme enzyme unspecified role unspecified role P00455:p.Lys88Gln mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain K Q Wed May 02 19:03:14 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys88gln' Tue Jun 30 17:33:28 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys88Gln' ecoli Escherichia coli (strain K12) 6 enzyme target enzyme target substrate substrate unspecified role unspecified role ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role ancillary ancillary spiol Spinacia oleracea (Spinach) Spinach physical association physical association The kcat is deduced by varing both NADPH and Ferredoxin consnetration and fitting the data to a 'ping-pong mechanism'.The kcat for the wild type protein is 3800 U/FAD, and the kcat is 2200 for the K88Q mutant. ferredoxin is necessary