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/ Complex formation between ferredoxin and Synechococcus ferredoxin: nitrate oxidoreductase. Complex formation between ferredoxin and Synechococcus ferredoxin: nitrate oxidoreductase. Biochim. Biophys. Acta (0006-3002) 2004 imex curation Hirasawa M., Rubio LM., Griffin JL., Flores E., Herrero A., Li J., Kim SK., Hurley JK., Tollin G., Knaff DB. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species Enzymatic acitivity measurments are done monitoring the speed of nitrate reduction. One unit of activity correspond to 1 microMole of nitrate reduced per minute. Fig.1, table1, fig.5 and fig.6 knaff@ttu.edu Only protein-protein interactions in vitro In vitro enzymatic study enzymatic study predetermined predetermined participant predetermined Hirasawa M., Rubio LM., Griffin JL., Flores E., Herrero A., Li J., Kim SK., Hurley JK., Tollin G., Knaff DB. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species Enzymatic acitivity measurments are done monitoring the speed of nitrate reduction. One unit of activity correspond to 1 microMole of nitrate reduced per minute. Fig.1, table1, fig.5 and fig.6 knaff@ttu.edu Accepted 2006-JUL-5 by DAVET. Biochim. Biophys. Acta (0006-3002) 2004 Only protein-protein interactions imex curation Complex formation between ferredoxin and Synechococcus ferredoxin: nitrate oxidoreductase. Complex formation between ferredoxin and Synechococcus ferredoxin: nitrate oxidoreductase. Biochim. Biophys. Acta (0006-3002) 2004 imex curation Hirasawa M., Rubio LM., Griffin JL., Flores E., Herrero A., Li J., Kim SK., Hurley JK., Tollin G., Knaff DB. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species Enzymatic acitivity measurments are done monitoring the speed of nitrate reduction. One unit of activity correspond to 1 microMole of nitrate reduced per minute. Fig.1, table1, fig.5 and fig.6 knaff@ttu.edu Only protein-protein interactions in vitro In vitro cd circular dichroism CD CD cd predetermined predetermined participant predetermined Hirasawa M., Rubio LM., Griffin JL., Flores E., Herrero A., Li J., Kim SK., Hurley JK., Tollin G., Knaff DB. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species Enzymatic acitivity measurments are done monitoring the speed of nitrate reduction. One unit of activity correspond to 1 microMole of nitrate reduced per minute. Fig.1, table1, fig.5 and fig.6 knaff@ttu.edu Accepted 2006-JUL-5 by DAVET. Biochim. Biophys. Acta (0006-3002) 2004 Only protein-protein interactions imex curation fer1_nosso Ferredoxin-1 Ferredoxin I petF fdxV protein protein anaso Anabaena sp. (strain PCC 7119) MATFKVTLINEAEGTKHEIEVPDDEYILDAAEEQGYDLPFSCRAGACSTCAGKLVSGTVDQSDQSFLDDDQIEAGYVLTCVAYPTSDVVIQTHKEEDLY 874FD6365346BFFF fer1_spiol Ferredoxin-1, chloroplastic Ferredoxin I PETF protein protein spiol Spinacia oleracea (Spinach) Spinach MAATTTTMMGMATTFVPKPQAPPMMAALPSNTGRSLFGLKTGSRGGRMTMAAYKVTLVTPTGNVEFQCPDDVYILDAAEEEGIDLPYSCRAGSCSSCAGKLKTGSLNQDDQSFLDDDQIDEGWVLTCAAYPVSDVTIETHKEEELTA 76045050A0AA8697 narb_syne7 Nitrate reductase narB Synpcc7942_1235 protein protein syne7 Synechococcus elongatus (strain PCC 7942) Anacystis nidulans R2 MFDLSKFLPVITPLMIDTAKTLCPYCGVGCGLEAVPPAQPGRATVRDREGTPIWQIRGDRQHPSSQGMVCVKGATVAESVSKSRLKYPMFRASLDDPFTEISWDEALDRLCDRIQQTQADYGKDGICFYGSGQFQTEDYYIAQKLVKGCLGTNNFDTNSRLCMSSAVSAYSLCLGSDGPPACYEDLDLADCLLIVGSNTAECHPILFNRYRKRHKQGGTNLIVVDPRCTPTAEVADLHLALKPGSDVALLNGLGWLLYQMGYVKKDFIANQTEGFEDWLAIIEDYPPQRTAELTGLAVAELVRAADLIASAQRWLSLWSMGVNQSIQGTAKATSLINLHLLTRQIGLPGCGPFSLTGQPNAMGGRETGGLAHLLPGYRKVIDPQHRADVETIWGLPMGSISPQPGRTAWQMIEGLEQGAVGFLWVAATNPAVSLPDVKRAQAALKRSPFTVLQDAYHPTETTTYAHLLLPAAQWSEKTGTMTNSERRVTLCQAFRQPPGEARADWQIFAEVGRRLGFAFDYTDAAAVFAEYVQVTAGRLCDLSGLSHELLAQAGPQQWPFPAGAEPTTESKRLYTKHHFAYADGRARFQPFHHLGVAEPPDDRYPLVLTVGRLYGHWHTQTRTGRIDKINKLHPSAFVEIHPRDADRYNISEGQAVVIRSRRGEGCFPAKVTTAISPGVLFVPMHWGALWGDRTEANALTHPAACPISGEPELKACAVQIEAASSTFTI 455798C8631755A6 narb-fer1-1 2 4 unspecified role unspecified role neutral component neutral component 5 unspecified role unspecified role neutral component neutral component region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) direct interaction direct interaction Authors mention spinach ferredoxin without specifying if they refer to the ferredoxin1(P00221) or the ferredoxin 2(P00224). P39458 purified P00221 purified Titration curves of ferredoxin and Narb are consistent with a 1:1 stoichiometry. Treatment of NarB with arginine-modifying reagent, reducing the positive charges of its accessible arginines, strongly affect its aggregation with the negatively charged ferredoxin. narb-fer1-2 1 5 electron acceptor electron acceptor unspecified role unspecified role region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) 4 electron donor electron donor unspecified role unspecified role direct interaction direct interaction Authors mention spinach ferredoxin without specifying if they refer to the ferredoxin1(P00221) or the ferredoxin 2(P00224). The activity of NarB is strongly inhibited by an increase in ionic strength (independently of the ion used) in the assay mixture. Treatment of NarB with arginine-modifying reagent or with lysine-modifying reagent (both reduce the positive charges of its accessible residues) also strongly affect its nitrate reductase activity by preventing its aggregation with the negatively charged ferredoxin. Km estimated to be 50 10e-6 M P39458 purified P00221 purified narb-fer1-3 1 5 electron acceptor electron acceptor unspecified role unspecified role region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) 3 electron donor electron donor unspecified role unspecified role P0A3C8:p.Glu96Lys mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain E K Wed May 02 15:39:21 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu96lys' Tue Jun 30 16:02:43 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu96Lys' P0A3C8:p.Glu95Lys mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain E K Wed May 02 16:47:05 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu95lys' Tue Jun 30 16:34:18 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu95Lys' P0A3C8:p.Glu95_Glu96delinsLysLys mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain EE KK Fri Jul 22 11:06:46 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'glu95lys,glu96lys' Wed May 02 17:18:34 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu_glu95-96lys_lys' Wed May 02 19:36:01 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu_glu95-96lys_lys' Tue Jun 30 19:22:00 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu95_Glu96delinsLysLys' direct interaction direct interaction P39458 purified P0A3C8 purified Unlike the results obtained previously, using these same ferredoxins as electron donors to spinach glutamate synthase [41], E94K and E95K charge-reversal variants of Anabaena ferredoxin were both much impaired in their ability to serve as electron donors to Synechococcus nitrate reductase (Table 1), even though the effect with the E94K variant (with a relative activity of 19% of the wild-type control) was somewhat greater than that observed with the E95K variant (with a relative activity of 38% of the wildtype control).