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/ http://www.ebi.ac.uk/ aliverti-1994-1 Involvement of lysine-88 of spinach ferredoxin-NADP+ reductase in the interaction with ferredoxin. 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 FEBS Lett. (0014-5793) 1994 Only protein-protein interactions imex curation Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species aliverti-1994-2 Involvement of lysine-88 of spinach ferredoxin-NADP+ reductase in the interaction with ferredoxin. 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 FEBS Lett. (0014-5793) 1994 Only protein-protein interactions imex curation Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species aliverti-1994-3 Involvement of lysine-88 of spinach ferredoxin-NADP+ reductase in the interaction with ferredoxin. 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 FEBS Lett. (0014-5793) 1994 Only protein-protein interactions imex curation Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species fer1_spiol Ferredoxin-1, chloroplastic Ferredoxin I PETF protein protein spiol Spinacia oleracea (Spinach) Spinach MAATTTTMMGMATTFVPKPQAPPMMAALPSNTGRSLFGLKTGSRGGRMTMAAYKVTLVTPTGNVEFQCPDDVYILDAAEEEGIDLPYSCRAGSCSSCAGKLKTGSLNQDDQSFLDDDQIDEGWVLTCAAYPVSDVTIETHKEEELTA fenr_spiol Ferredoxin--NADP reductase, chloroplastic PETH protein protein spiol Spinacia oleracea (Spinach) Spinach MTTAVTAAVSFPSTKTTSLSARSSSVISPDKISYKKVPLYYRNVSATGKMGPIRAQIASDVEAPPPAPAKVEKHSKKMEEGITVNKFKPKTPYVGRCLLNTKITGDDAPGETWHMVFSHEGEIPYREGQSVGVIPDGEDKNGKPHKLRLYSIASSALGDFGDAKSVSLCVKRLIYTNDAGETIKGVCSNFLCDLKPGAEVKLTGPVGKEMLMPKDPNATIIMLGTGTGIAPFRSFLWKMFFEKHDDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPDNFRLDFAVSREQTNEKGEKMYIQTRMAQYAVELWEMLKKDNTYFYMCGLKGMEKGIDDIMVSLAAAEGIDWIEYKRQLKKAEQWNVEVY cyc_horse Cytochrome c CYCS CYC protein protein horse Equus caballus (Horse) Horse MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWKEETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE peth-petf-2 Study of Spinach FNR and ferredoxin by fluorescence spectroscopy 332345 N/A 332348 unspecified role unspecified role neutral component neutral component spiol Spinacia oleracea (Spinach) Spinach N/A 332349 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 false ecoli Escherichia coli (strain K12) physical association physical association false false false 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 Cross-linking of Spinach FNR and ferredoxin 332346 N/A 332348 unspecified role unspecified role neutral component neutral component spiol Spinacia oleracea (Spinach) Spinach N/A 332349 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 false ecoli Escherichia coli (strain K12) physical association physical association false false false 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 NADPH ferredoxin dependant cytochrome c reductase activity of FNR 332347 N/A 332349 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 false ecoli Escherichia coli (strain K12) N/A 332350 enzyme target enzyme target substrate substrate unspecified role unspecified role ecoli Escherichia coli (strain K12) N/A 332348 unspecified role unspecified role ancillary ancillary spiol Spinacia oleracea (Spinach) Spinach physical association physical association false false false 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