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/ Lys75 of Anabaena ferredoxin-NADP+ reductase is a critical residue for binding ferredoxin and flavodoxin during electron transfer. Lys75 of Anabaena ferredoxin-NADP+ reductase is a critical residue for binding ferredoxin and flavodoxin during electron transfer. Biochemistry (0006-2960) 1998 imex curation Martinez-Julvez M., Medina M., Hurley JK., Hafezi R., Brodie TB., Tollin G., Gomez-Moreno C. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species Table 3 gomezm@pota.unizar.es Only protein-protein interactions imex curation in vitro In vitro oxidoreduct assay oxidoreductase assay oxidoreduct assay predetermined predetermined participant predetermined Martinez-Julvez M., Medina M., Hurley JK., Hafezi R., Brodie TB., Tollin G., Gomez-Moreno C. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species Electron transfer detected by NADPH-Dependant Cytochrome c Reductase activity. The steady state catalytic behaviours of the different FNR mutants were determined. Table 3 gomezm@pota.unizar.es Accepted 2010-JAN-10 by SKERRIEN (applied to all records created before 2005-Sep-01). Biochemistry (0006-2960) 1998 IMEx Lys75 of Anabaena ferredoxin-NADP+ reductase is a critical residue for binding ferredoxin and flavodoxin during electron transfer. Lys75 of Anabaena ferredoxin-NADP+ reductase is a critical residue for binding ferredoxin and flavodoxin during electron transfer. Biochemistry (0006-2960) 1998 imex curation Martinez-Julvez M., Medina M., Hurley JK., Hafezi R., Brodie TB., Tollin G., Gomez-Moreno C. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species Table 3 gomezm@pota.unizar.es Only protein-protein interactions imex curation in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Martinez-Julvez M., Medina M., Hurley JK., Hafezi R., Brodie TB., Tollin G., Gomez-Moreno C. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species Table 3 gomezm@pota.unizar.es Accepted 2010-JAN-10 by SKERRIEN (applied to all records created before 2005-Sep-01). Biochemistry (0006-2960) 1998 IMEx fer1_nosso Ferredoxin-1 Ferredoxin I petF fdxV protein protein anaso Anabaena sp. (strain PCC 7119) MATFKVTLINEAEGTKHEIEVPDDEYILDAAEEQGYDLPFSCRAGACSTCAGKLVSGTVDQSDQSFLDDDQIEAGYVLTCVAYPTSDVVIQTHKEEDLY 874FD6365346BFFF fenr_nosso Ferredoxin--NADP reductase petH protein protein anaso Anabaena sp. (strain PCC 7119) MSNQGAFDGAANVESGSRVFVYEVVGMRQNEETDQTNYPIRKSGSVFIRVPYNRMNQEMQRITRLGGKIVTIQTVSALQQLNGRTTIATVTDASSEIAKSEGNGKATPVKTDSGAKAFAKPPAEEQLKKKDNKGNTMTQAKAKHADVPVNLYRPNAPFIGKVISNEPLVKEGGIGIVQHIKFDLTGGNLKYIEGQSIGIIPPGVDKNGKPEKLRLYSIASTRHGDDVDDKTISLCVRQLEYKHPESGETVYGVCSTYLTHIEPGSEVKITGPVGKEMLLPDDPEANVIMLATGTGIAPMRTYLWRMFKDAERAANPEYQFKGFSWLVFGVPTTPNILYKEELEEIQQKYPDNFRLTYAISREQKNPQGGRMYIQDRVAEHADELWQLIKNQKTHTYICGLRGMEEGIDAALSAAAAKEGVTWSDYQKDLKKAGRWHVETY 8E1F61D0F09338B6 flav_nosso Flavodoxin isiB protein protein anaso Anabaena sp. (strain PCC 7119) MSKKIGLFYGTQTGKTESVAEIIRDEFGNDVVTLHDVSQAEVTDLNDYQYLIIGCPTWNIGELQSDWEGLYSELDDVDFNGKLVAYFGTGDQIGYADNFQDAIGILEEKISQRGGKTVGYWSTDGYDFNDSKALRNGKFVGLALDEDNQSDLTDDRIKSWVAQLKSEFGL 069E8DEBA9E33302 peth-petf-1 2 3 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role neutral component neutral component P21890:p.Lys206Gln mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain K Q Wed May 02 16:08:05 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys206gln' Tue Jun 30 16:27:58 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys206Gln' P21890:p.Lys206Ser mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain K S Wed May 02 17:07:37 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys206ser' Tue Jun 30 20:22:09 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys206Ser' P21890:p.Lys206Glu mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain K E Wed May 02 14:59:27 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys206glu' Tue Jun 30 16:13:04 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys206Glu' ecoli Escherichia coli (strain K12) physical association physical association Mutations of the positively charged lysine 75 of FNR into neutral amino acid lys75Gln or lys75Ser increase the Kd respectively to Kd = 3.8.10-4 and Kd = 2.10-4. For the mutation of Lysine 75 into a negatively charged amino-acid Lys75Glu, the Kd could not be determined as no binding was detected. Both proteins are in oxidized form. peth-isib-1 1 5 unspecified role unspecified role neutral component neutral component 4 unspecified role unspecified role neutral component neutral component P21890:p.Lys206Gln mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K Q Wed May 02 18:07:49 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys206gln' Tue Jun 30 16:20:47 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys206Gln' P21890:p.Lys206Glu mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K E Wed May 02 16:14:48 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys206glu' Tue Jun 30 19:52:54 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys206Glu' P21890:p.Lys206Ser mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K S Thu Jul 07 12:06:51 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was lys206ser Wed May 02 14:27:37 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys206ser' Tue Jun 30 18:28:25 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys206Ser' ecoli Escherichia coli (strain K12) redox reaction oxidoreductase activity electron transfer reaction redox reaction Fig. 5 to be remapped when oxido-reduction available All the kinetics parameters were obtained by fitting the data to the equation for a ping-pong mechanism. The steady state parameters are: kcat= 23 s-1, Km = 33.10-6 M. For the mutants Lys75Gln and Lys75Ser of FNR, the kcat are respectively 27 s-1 and 50 s-1. For the mutants Lys75Gln and Lys75Ser of FNR, The Km are respectively 632.10-6 M and 800.10-6 M. No reaction was observed for Lys75Glu. peth-petf-3 1 4 unspecified role unspecified role neutral component neutral component P21890:p.Lys206Gln mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K Q Wed May 02 14:40:23 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys206gln' Tue Jun 30 16:46:03 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys206Gln' P21890:p.Lys206Ser mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K S Wed May 02 19:16:26 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys206ser' Tue Jun 30 19:48:15 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys206Ser' P21890:p.Lys206Glu mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K E Wed May 02 16:04:35 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys206glu' Tue Jun 30 20:19:31 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys206Glu' ecoli Escherichia coli (strain K12) 3 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) physical association physical association to be remapped when oxido-reduction available All the kinetics parameters were obtained by fitting the data to the equation for a ping-pong mechanism. The steady state parameters are: kcat= 200 s-1, Km = 11.10-6 M. For the mutants Lys75Gln and Lys75Ser of FNR, the kcat are respectively 190 s-1 and 200 s-1. The Km could not be measured. No reaction was observed for Lys75Glu FNR.