#ID(s) interactor A ID(s) interactor B Alt. ID(s) interactor A Alt. ID(s) interactor B Alias(es) interactor A Alias(es) interactor B Interaction detection method(s) Publication 1st author(s) Publication Identifier(s) Taxid interactor A Taxid interactor B Interaction type(s) Source database(s) Interaction identifier(s) Confidence value(s) Expansion method(s) Biological role(s) interactor A Biological role(s) interactor B Experimental role(s) interactor A Experimental role(s) interactor B Type(s) interactor A Type(s) interactor B Xref(s) interactor A Xref(s) interactor B Interaction Xref(s) Annotation(s) interactor A Annotation(s) interactor B Interaction annotation(s) Host organism(s) Interaction parameter(s) Creation date Update date Checksum(s) interactor A Checksum(s) interactor B Interaction Checksum(s) Negative Feature(s) interactor A Feature(s) interactor B Stoichiometry(s) interactor A Stoichiometry(s) interactor B Identification method participant A Identification method participant B uniprotkb:Q55389 uniprotkb:Q55781 intact:EBI-863211|intact:EBI-1608683|ensemblbacteria:BAA10479 intact:EBI-863219|ensemblbacteria:BAA10432 psi-mi:ftrc_syny3(display_long)|uniprotkb:ftrC(gene name)|psi-mi:ftrC(display_short)|uniprotkb:Ferredoxin-thioredoxin reductase subunit B(gene name synonym)|uniprotkb:sll0554(orf name) psi-mi:ftrv_syny3(display_long)|uniprotkb:ftrV(gene name)|psi-mi:ftrV(display_short)|uniprotkb:Ferredoxin-thioredoxin reductase subunit A(gene name synonym)|uniprotkb:ssr0330(locus name) psi-mi:"MI:0114"(x-ray crystallography) Dai et al. (2000) pubmed:10649999 taxid:1111708(syny3)|taxid:1111708("Synechocystis sp. (strain PCC 6803 / Kazusa)") taxid:1111708(syny3)|taxid:1111708("Synechocystis sp. (strain PCC 6803 / Kazusa)") psi-mi:"MI:0407"(direct interaction) psi-mi:"MI:0469"(IntAct) intact:EBI-863225|rcsb pdb:1dj7 - - psi-mi:"MI:0499"(unspecified role) psi-mi:"MI:0499"(unspecified role) psi-mi:"MI:0497"(neutral component) psi-mi:"MI:0497"(neutral component) psi-mi:"MI:0326"(protein) psi-mi:"MI:0326"(protein) dip:DIP-35307N|ensemblbacteria:BAA10479(gene)|ensemblbacteria:BAA10479(transcript)|go:"GO:0009055"(electron transfer activity)|go:"GO:0015979"(photosynthesis)|go:"GO:0016730"(oxidoreductase activity, acting on iron-sulfur proteins as donors)|go:"GO:0046872"(metal ion binding)|go:"GO:0051539"(4 iron, 4 sulfur cluster binding)|go:"GO:0103012"(ferredoxin-thioredoxin reductase activity)|interpro:IPR004209(Ferredoxin thioredoxin reductase, beta subunit)|interpro:IPR024707|interpro:IPR036644|rcsb pdb:1DJ7|rcsb pdb:2PU9|rcsb pdb:2PUK|rcsb pdb:2PUO|rcsb pdb:2PVD|rcsb pdb:2PVG|rcsb pdb:2PVO dip:DIP-35306N|mint:Q55781|ensemblbacteria:BAA10432(gene)|ensemblbacteria:BAA10432(transcript)|go:"GO:0015979"(photosynthesis)|go:"GO:0016491"(oxidoreductase activity)|interpro:IPR004207(Ferredoxin thioredoxin reductase, alpha chain)|interpro:IPR008990(Electron transport accessory protein)|interpro:IPR044166|rcsb pdb:1DJ7|rcsb pdb:2PU9|rcsb pdb:2PUK|rcsb pdb:2PUO|rcsb pdb:2PVD|rcsb pdb:2PVG|rcsb pdb:2PVO - - - 3d-resolution:1.60A|3d-r-factors:working 23.8%, free 27.8%|comment:FTR is an iron-sulfur enzume composed a conserved catalytic subunit and a varaiable subunit. The catalytic subunit contains a redox-active disulfide and a [4fe-4S] center. The interaction between the catalytic and variable chains involves the very thin center of the molecule where only a small hydrophobic core is formed. However, most of the interactions occur between charged and polar residues that form hydrogen bonds. One inmportant function of the variable subunit seems the stablization of the Fe-S cluster of the catalytic subunit.|comment:"Reduced ferredoxin produced by photosytem I during light is used by this heterodimer enzyme ferredoxin:thioredoxin reductase (FTR) to reduce the sulfide bond of thioredoxins which will the regulates many target enzymes. FTR is key enzyme sensing light-dependent redox potential changes transforming the electron signal to a thiol signal."|comment:The active-site disulfide bridge between Cys57 and Cys87 of catalytic subunit is in van der Waals contact with the iron center. This bridge is believed to be disrupted when ferrodoxin gives 1 electron. The Cys57 forms then a disulfid bond with thioredoxin by disrupting an internal disulfide bond in thioredoxin. A second electron given by a new ferrodoxin free the thioredoxin which is then reduced and the cys57 forms again an internal sulfid bond cys 87.|dataset:Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species taxid:-1(in vitro)|taxid:-1(In vitro) - 2006/02/20 2014/10/16 rogid:FYjurHurXNNTk+iXIzW9llR84D81111708 rogid:Qm4qDJ6gSQWuux1xdNhE6joM5MI1111708 intact-crc:00667D3C76A60E1B|rigid:qFckqA2rG6RMubuGbyP/+tVg/PE false binding-associated region:58-88 - - - psi-mi:"MI:0396"(predetermined participant) psi-mi:"MI:0396"(predetermined participant)