MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it http://mint.bio.uniroma2.it/mint frick-2013-1 Structural basis for pH gating of plant aquaporins. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction experimental particp experimental participant identification experimental particp Frick A., Järvå M., Törnroth-Horsefield S. FEBS Lett. (0014-5793) 2013 groth-2001-1 The structure of the chloroplast F1-ATPase at 3.2 A resolution. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Groth G., Pohl E. georg.groth@uniduesseldorf.de J. Biol. Chem. (0021-9258) 2001 taylor-1997a-1 Structure of a product complex of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Taylor TC., Andersson I. Biochemistry (0006-2960) 1997 ubbink-1998-1 The structure of the complex of plastocyanin and cytochrome f, determined by paramagnetic NMR and restrained rigid-body molecular dynamics. in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Ubbink M., Ejdebäck M., Karlsson BG., Bendall DS. m.ubbink@chem.leidenuniv.nl Structure (0969-2126) 1998 farkas-2011-1 Thioredoxin-mediated reduction of the photosystem I subunit PsaF and activation through oxidation by the interaction partner plastocyanin. in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Farkas D., Hansson O. FEBS Lett. (0014-5793) 2011 Only protein-protein interactions imex curation atpb_spiol ATP synthase subunit beta, chloroplastic atpB F-ATPase subunit beta ATP synthase F1 sector subunit beta protein protein spiol Spinacia oleracea (Spinach) Spinach MRINPTTSDPGVSTLEKKNLGRIAQIIGPVLDVAFPPGKMPNIYNALIVKGRDTAGQPMNVTCEVQQLLGNNRVRAVAMSATDGLTRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYEIAQRVKETLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDSLPEQAFYLVGNIDEATAKAMNLEMESKLKK mint Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits atpa_spiol ATP synthase subunit alpha, chloroplastic atpA F-ATPase subunit alpha ATP synthase F1 sector subunit alpha protein protein spiol Spinacia oleracea (Spinach) Spinach MATIRADEISKIIRERIEGYNREVKVVNTGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEITASESRLIESPAPGIMSRRSVYEPLQTGLIAIDAMIPVGRGQRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVTNFQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSLLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKKVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLKQPQSAPLTVEEQVMTIYTGTNGYLDSLELDQVRKYLVELRTYVKTNKPEFQEIISSTKTFTEEAEALLKEAIQEQMERFLLQEQA mint Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit rbs2_spiol Ribulose bisphosphate carboxylase small subunit, chloroplastic 2 RBCS2 protein protein spiol Spinacia oleracea (Spinach) Spinach MASSVLSSAAVATVSRTPAQASMVAPFTGLKSTVGFPATKKNDDITSLASNGGRVQCMKVWPTQNMKRYETLSYLPPLTTDQLARQVDYLLNNKWVPCLEFETDHGFVYREHHNSPGYYDGRYWTMWKLPMFGCTDPAQVLNELEECKKEYPNAFIRIIGFDSNRQVQCVSFIAYKPAGY rbl_spiol Ribulose bisphosphate carboxylase large chain rbcL protein protein spiol Spinacia oleracea (Spinach) Spinach MSPQTETKASVEFKAGVKDYKLTYYTPEYETLDTDILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTNLDRYKGRCYHIEPVAGEENQYICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEDMMKRAVFARELGVPIVMHDYLTGGFTANTTLSHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDYTEKDRSRGIYFTQSWVSTPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNTIIREATKWSPELAAACEVWKEIKFEFPAMDTV mint RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site plas_spiol Plastocyanin, chloroplastic PETE protein protein spiol Spinacia oleracea (Spinach) Spinach MATVASSAAVAVPSFTGLKASGSIKPTTAKIIPTTTAVPRLSVKASLKNVGAAVVATAAAGLLAGNAMAVEVLLGGGDGSLAFLPGDFSVASGEEIVFKNNAGFPHNVVFDEDEIPSGVDAAKISMSEEDLLNAPGETYKVTLTEKGTYKFYCSPHQGAGMVGKVTVN Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I mint cyf_brarr Cytochrome f petA protein protein turnip Brassica rapa MQTRNTFSWIREEITRSISVSLMIYIITWASISSAYPIFAQQNYENPREATGRIVCANCHLASKPVDIEVPQAVLPDTVFEAVVKIPYDMQLKQVLANGKKGALNVGAVLILPEGFELAPPDRISPEMKEKIGNLSFQNYRPNKKNILVIGPVPGQKYSEITFPILAPDPATNKDVHFLKYPIYVGGNRGRGQIYPDGSKSNNTVYNATAGGIISKILRKEKGGYEITIVDASNERQVIDIIPRGLELLVSEGESIKLDQPLTSNPNVGGFGQGDAEIVLQDPLRVQGLLFFLGSVVLAQIFLVLKKKQFEKVQLSEMNF mint Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions q41372_spiol SOVF_195660 protein protein spiol Spinacia oleracea (Spinach) Spinach MSKEVSEEAQAHQHGKDYVDPPPAPFFDLGELKLWSFWRAAIAEFIATLLFLYITVATVIGHSKETVVCGSVGLLGIAWAFGGMIFVLVYCTAGISGGHINPAVTFGLFLARKVSLLRALVYMIAQCLGAICGVGLVKAFMKGPYNQFGGGANSVALGYNKGTALGAEIIGTFVLVYTVFSATDPKRSARDSHVPILAPLPIGFAVFMVHLATIPITGTGINPARSFGAAVIFNSNKVWDDQWIFWVGPFIGAAVAAAYHQYVLRAAAIKALGSFRSNPTN mint psaf_spiol Photosystem I reaction center subunit III, chloroplastic PSAF Light-harvesting complex I 17 kDa protein PSI-F protein protein spiol Spinacia oleracea (Spinach) Spinach MSFTIPTNLYKPLATKPKHLSSSSFAPRSKIVCQQENDQQQPKKLELAKVGANAAAALALSSVLLSSWSVAPDAAMADIAGLTPCKESKQFAKREKQALKKLQASLKLYADDSAPALAIKATMEKTKKRFDNYGKYGLLCGSDGLPHLIVSGDQRHWGEFITPGILFLYIAGWIGWVGRSYLIAIRDEKKPTQKEIIIDVPLASSLLFRGFSWPVAAYRELLNGELVDNNF 270E1BAC159D79B4 mint q41372 1365398 q41372_spiol SoPIP2;1 1365399 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 4.0 direct interaction direct interaction false false false mint t1 f2 sf2 atpa-atpb-1 100429 atpa_spiol 100430 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 atpb_spiol 100431 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 direct interaction direct interaction false false false In the xray complex 1fx0, P06450 is chain A and P00825 is chain B Resolution 3.200 mint rbcl-rbcs2 101215 rbl_spiol 101216 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 rbs2_spiol 101217 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 direct interaction direct interaction false false false In the xray complex 1aus, P00875 is chain L and Q43832 is chain S Resolution 2.200 mint peta-pete 101710 plas_spiol 101711 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 cyf_brara 101712 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 direct interaction direct interaction false false false In the xray complex 2pcf, P00289 is chain A and P36438 is chain B Resolution mint pete-psaf 1142317 plas_spiol Pc 101711 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified psaf_spiol PsaF 1142319 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false Lumen Exposed domain direct interaction direct interaction false false false mint f1 f2 DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ azevedo-2008-1 yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Azevedo J., Courtois F., Hakimi MA., Demarsy E., Lagrange T., Alcaraz JP., Jaiswal P., Maréchal-Drouard L., Lerbs-Mache S. DIP original experiment: DIP-111162X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Intraplastidial trafficking of a phage-type RNA polymerase is mediated by a thylakoid RING-H2 protein. Azevedo J., Courtois F., Hakimi MA., Demarsy E., Lagrange T., Alcaraz JP., Jaiswal P., Maréchal-Drouard L., Lerbs-Mache S. Only protein-protein interactions imex curation azevedo-2008-2 spiol Spinacia oleracea (Spinach) Spinach molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column western blot western blot Immuno blot Immuno blot Azevedo J., Courtois F., Hakimi MA., Demarsy E., Lagrange T., Alcaraz JP., Jaiswal P., Maréchal-Drouard L., Lerbs-Mache S. DIP original experiment: DIP-111165X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Intraplastidial trafficking of a phage-type RNA polymerase is mediated by a thylakoid RING-H2 protein. Azevedo J., Courtois F., Hakimi MA., Demarsy E., Lagrange T., Alcaraz JP., Jaiswal P., Maréchal-Drouard L., Lerbs-Mache S. Only protein-protein interactions imex curation azevedo-2008-3 yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Azevedo J., Courtois F., Hakimi MA., Demarsy E., Lagrange T., Alcaraz JP., Jaiswal P., Maréchal-Drouard L., Lerbs-Mache S. DIP original experiment: DIP-111163X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Intraplastidial trafficking of a phage-type RNA polymerase is mediated by a thylakoid RING-H2 protein. Azevedo J., Courtois F., Hakimi MA., Demarsy E., Lagrange T., Alcaraz JP., Jaiswal P., Maréchal-Drouard L., Lerbs-Mache S. Only protein-protein interactions imex curation azevedo-2008-4 yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Azevedo J., Courtois F., Hakimi MA., Demarsy E., Lagrange T., Alcaraz JP., Jaiswal P., Maréchal-Drouard L., Lerbs-Mache S. DIP original experiment: DIP-111164X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Intraplastidial trafficking of a phage-type RNA polymerase is mediated by a thylakoid RING-H2 protein. Azevedo J., Courtois F., Hakimi MA., Demarsy E., Lagrange T., Alcaraz JP., Jaiswal P., Maréchal-Drouard L., Lerbs-Mache S. Only protein-protein interactions imex curation trnroth_horsefield-2006-1 picpa Pichia pastoris (Yeast) Yeast Pichia pastoris x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Törnroth-Horsefield S., Wang Y., Hedfalk K., Johanson U., Karlsson M., Tajkhorshid E., Neutze R., Kjellbom P. DIP original experiment: DIP-253738X Nature 2006 IMEx Structural mechanism of plant aquaporin gating. Törnroth-Horsefield S., Wang Y., Hedfalk K., Johanson U., Karlsson M., Tajkhorshid E., Neutze R., Kjellbom P. Only protein-protein interactions imex curation qin-2015-1 pea Pisum sativum (Garden pea) Garden pea x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Qin X., Suga M., Kuang T., Shen JR. DIP original experiment: DIP-266248X Science (New York, N.Y.) 2015 IMEx Photosynthesis. Structural basis for energy transfer pathways in the plant PSI-LHCI supercomplex. Qin X., Suga M., Kuang T., Shen JR. Only protein-protein interactions imex curation wei-2016-21 spiol Spinacia oleracea (Spinach) Spinach 3d-em 3D electron microscopy 3D-EM electron tomog predetermined predetermined participant predetermined Wei X., Su X., Cao P., Liu X., Chang W., Li M., Zhang X., Liu Z. DIP original experiment: DIP-269085X Nature 2016 IMEx Structure of spinach photosystem II-LHCII supercomplex at 3.2 Å resolution. Wei X., Su X., Cao P., Liu X., Chang W., Li M., Zhang X., Liu Z. Only protein-protein interactions imex curation amunts-2010-1 pea Pisum sativum (Garden pea) Garden pea x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Amunts A., Toporik H., Borovikova A., Nelson N. Three out of four PDBe entries use Uniprot identifiers from several species of plants other than the one stated to have been used - PEA. nelson@post.tau.ac.il The Journal of biological chemistry 2010 imex curation Only protein-protein interactions imex curation amunts-2010-2 pea Pisum sativum (Garden pea) Garden pea molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column weight by staining molecular weight estimation by staining weight by staining Amunts A., Toporik H., Borovikova A., Nelson N. nelson@post.tau.ac.il The Journal of biological chemistry 2010 imex curation Only protein-protein interactions imex curation liu-2004-9 spiol Spinacia oleracea (Spinach) Spinach x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Liu Z., Yan H., Wang K., Kuang T., Zhang J., Gui L., An X., Chang W. wrchang@sun5.ibp.ac.cn Nature 2004 imex curation Only protein-protein interactions imex curation raunser-2009-1 in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Raunser S., Magnani R., Huang Z., Houtz RL., Trievel RC., Penczek PA., Walz T. DIP original experiment: DIP-133789X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Rubisco in complex with Rubisco large subunit methyltransferase. Raunser S., Magnani R., Huang Z., Houtz RL., Trievel RC., Penczek PA., Walz T. Only protein-protein interactions imex curation raunser-2009-2 in vitro In vitro 3d-em 3D electron microscopy 3D-EM electron tomog predetermined predetermined participant predetermined Raunser S., Magnani R., Huang Z., Houtz RL., Trievel RC., Penczek PA., Walz T. DIP original experiment: DIP-133787X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Rubisco in complex with Rubisco large subunit methyltransferase. Raunser S., Magnani R., Huang Z., Houtz RL., Trievel RC., Penczek PA., Walz T. Only protein-protein interactions imex curation fan-2015-1 spiol Spinacia oleracea (Spinach) Spinach x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Fan M., Li M., Liu Z., Cao P., Pan X., Zhang H., Zhao X., Zhang J., Chang W. DIP original experiment: DIP-266542X Nature structural & molecular biology 2015 IMEx Crystal structures of the PsbS protein essential for photoprotection in plants. Fan M., Li M., Liu Z., Cao P., Pan X., Zhang H., Zhao X., Zhang J., Chang W. Only protein-protein interactions imex curation fan-2015-2 spiol Spinacia oleracea (Spinach) Spinach molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Fan M., Li M., Liu Z., Cao P., Pan X., Zhang H., Zhao X., Zhang J., Chang W. DIP original experiment: DIP-266543X Nature structural & molecular biology 2015 IMEx Crystal structures of the PsbS protein essential for photoprotection in plants. Fan M., Li M., Liu Z., Cao P., Pan X., Zhang H., Zhao X., Zhang J., Chang W. Only protein-protein interactions imex curation fan-2015-3 spiol Spinacia oleracea (Spinach) Spinach crosslink cross-linking study crosslink weight by staining molecular weight estimation by staining weight by staining Fan M., Li M., Liu Z., Cao P., Pan X., Zhang H., Zhao X., Zhang J., Chang W. DIP original experiment: DIP-266544X Nature structural & molecular biology 2015 IMEx Crystal structures of the PsbS protein essential for photoprotection in plants. Fan M., Li M., Liu Z., Cao P., Pan X., Zhang H., Zhao X., Zhang J., Chang W. Only protein-protein interactions imex curation guy-2011-1 in vitro In vitro ms of complexes mass spectrometry studies of complexes ms of complexes predetermined predetermined participant predetermined Guy JE., Whittle E., Moche M., Lengqvist J., Lindqvist Y., Shanklin J. DIP original experiment: DIP-253836X Proceedings of the National Academy of Sciences of the United States of America 2011 IMEx Remote control of regioselectivity in acyl-acyl carrier protein-desaturases. Guy JE., Whittle E., Moche M., Lengqvist J., Lindqvist Y., Shanklin J. Only protein-protein interactions imex curation guy-2011-2 in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Guy JE., Whittle E., Moche M., Lengqvist J., Lindqvist Y., Shanklin J. DIP original experiment: DIP-253837X Proceedings of the National Academy of Sciences of the United States of America 2011 IMEx Remote control of regioselectivity in acyl-acyl carrier protein-desaturases. Guy JE., Whittle E., Moche M., Lengqvist J., Lindqvist Y., Shanklin J. Only protein-protein interactions imex curation dai-2007-5 in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Dai S., Friemann R., Glauser DA., Bourquin F., Manieri W., Schürmann P., Eklund H. DIP original experiment: DIP-253199X Nature 2007 IMEx Structural snapshots along the reaction pathway of ferredoxin-thioredoxin reductase. Dai S., Friemann R., Glauser DA., Bourquin F., Manieri W., Schürmann P., Eklund H. Only protein-protein interactions imex curation dai-2007-7 in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Dai S., Friemann R., Glauser DA., Bourquin F., Manieri W., Schürmann P., Eklund H. DIP original experiment: DIP-253198X Nature 2007 IMEx Structural snapshots along the reaction pathway of ferredoxin-thioredoxin reductase. Dai S., Friemann R., Glauser DA., Bourquin F., Manieri W., Schürmann P., Eklund H. Only protein-protein interactions imex curation dai-2007-8 in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Dai S., Friemann R., Glauser DA., Bourquin F., Manieri W., Schürmann P., Eklund H. DIP original experiment: DIP-253197X Nature 2007 IMEx Structural snapshots along the reaction pathway of ferredoxin-thioredoxin reductase. Dai S., Friemann R., Glauser DA., Bourquin F., Manieri W., Schürmann P., Eklund H. Only protein-protein interactions imex curation hahn-2018-1 spiol Spinacia oleracea (Spinach) Spinach 3d-em 3D electron microscopy 3D-EM electron tomog structure determination identification by structure determination identification by structure determination structure determination Hahn A., Vonck J., Mills DJ., Meier T., Kühlbrandt W. werner.kuehlbrandt@biophys.mpg.de Science (New York, N.Y.) 2018 imex curation Only protein-protein interactions imex curation fermani-2007-1 spiol Spinacia oleracea (Spinach) Spinach x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Fermani S., Sparla F., Falini G., Martelli PL., Casadio R., Pupillo P., Ripamonti A., Trost P. DIP original experiment: DIP-261640X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Molecular mechanism of thioredoxin regulation in photosynthetic A2B2-glyceraldehyde-3-phosphate dehydrogenase. Fermani S., Sparla F., Falini G., Martelli PL., Casadio R., Pupillo P., Ripamonti A., Trost P. Only protein-protein interactions imex curation malone-2019-1 spiol Spinacia oleracea (Spinach) Spinach 3d-em-single electron microscopy 3D single particle reconstruction 3D-EM-single experimental particp experimental participant identification experimental particp Malone LA., Qian P., Mayneord GE., Hitchcock A., Farmer DA., Thompson RF., Swainsbury DJK., Ranson NA., Hunter CN., Johnson MP. matt.johnson@sheffield.ac.uk Nature 2019 imex curation Only protein-protein interactions imex curation malone-2019-2 spiol Spinacia oleracea (Spinach) Spinach molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column experimental particp experimental participant identification experimental particp Malone LA., Qian P., Mayneord GE., Hitchcock A., Farmer DA., Thompson RF., Swainsbury DJK., Ranson NA., Hunter CN., Johnson MP. matt.johnson@sheffield.ac.uk Nature 2019 imex curation Only protein-protein interactions imex curation graf-2017-1 spiol Spinacia oleracea (Spinach) Spinach 3d-em 3D electron microscopy 3D-EM electron tomog experimental particp experimental participant identification experimental particp Graf M., Arenz S., Huter P., Dönhöfer A., Novácek J., Wilson DN. wilson@lmb.uni-muenchen.de Nucleic acids research 2017 Only protein-protein interactions imex curation imex curation ahmed-2016-1 spiol Spinacia oleracea (Spinach) Spinach 3d-em 3D electron microscopy 3D-EM electron tomog experimental particp experimental participant identification experimental particp Ahmed T., Yin Z., Bhushan S. sbhushan@ntu.edu.sg Scientific reports 2016 imex curation Only protein-protein interactions imex curation rk5_spiol 50S ribosomal protein L5, chloroplastic Chloroplastic large ribosomal subunit protein uL5c RPL5 PrpL5 SOVF_057730 protein protein spiol Spinacia oleracea (Spinach) Spinach MASTSLLQSTSSSFAGVRFHCRTSAAPRVGLSSFTVKAAAGTAVFVDKAEAETINRLKTNYIEKMVPLLKEEFSYSNILEVPKVVKIVVNCGIGDASQNAKGLDAAINELALITGQRPVKTKAKTSIAGFKVREGMTLGIAVTLRGNLMYSFLDRLINLALPRTRDFQGVNPNSFDGHGNYSVGFREQSVFPEIKPEIVGKARGMDVCITTTAKTDKEAYKLLSLMGMPFREGSGPSTLVRKKKLKSHHFDAKKGRRY rk4_spiol 50S ribosomal protein L4, chloroplastic Chloroplastic large ribosomal subunit protein uL4c SOVF_029280 RPL4 protein protein spiol Spinacia oleracea (Spinach) Spinach MATSTSSSLSLSFFSSSLFSSKSRNFSSKPILKLPSSSHSQTSLSLSIKSELIPLPILNFSGEKVGETFLNLKTAPPEKARAVVHRGLITHLQNKRRGTASTLTRAEVRGGGRKPYPQKKTGRARRGSQGSPLRPGGGVIFGPKPRDWTIKMNKKERRLALSTAIASAVGNSFVVEEFAENFEKPKTKDFIAAMQRWGLDPAEKSLFFLMDLVENVEKSGRNIRTLKLLTPRSLNLFDVLNAEKLVFTEGTIQYLNQRYGVDTLEDEDEEEEEEEEGEEVDDGVEDGTPEPAE rk3_spiol 50S ribosomal protein L3, chloroplastic Chloroplastic large ribosomal subunit protein uL3c SOVF_195350 RPL3 protein protein spiol Spinacia oleracea (Spinach) Spinach MAAILPTFSIKSSSCTYSSSKRSLSSPKAVSLSSSVNGTPKVQSLRLSTSFVCSPNQIIKLKSVSPSRSTQLRRAVGGLEIKMMSVDAGIGVMGTKLGMMSFFEEDGTVVPVTVIGFKEGNIVTQVKTESTDGYNAVQVGYERLRDRKLTMPERGHLNKAGVIPMRHLQEFRLVSVDDFTPSQKLLFEELFKEGDMVDISGTTIGKGFQGGIKRHNFKRGLMTHGSKSHRALGSIGAGTTPGHVYKGKKMPGRMGGTKTKIRKLKIMKIDTDLRVVMIKGAVPGKPGNLLRLAPAKIVGKNIPKN rk2_spiol 50S ribosomal protein L2, chloroplastic Chloroplastic large ribosomal subunit protein uL2c Ribosomal protein CS-L4 rpl2-A rpl2-B protein protein spiol Spinacia oleracea (Spinach) Spinach MAIHLYKTSTSSTRNGAVQVKSNPRNNLISGQRRCGKGRNARGIITARHRGGGHKRLYRKIDFRRNEKDIYGKIVTIEYDPNRNAYICLIHYGDGEKRYILHPRGAIIGDTIVSGTEVPIKMGNALPLTDMPLGTAIHNIEITLGRGGQLARAAGAVAKLIAKEGKSATLKLPSGEVRLISKNCSATVGQVGNVGVNQKRLGRAGSKRWLGKRPVVRGVVMNPVDHPHGGGEGRAPIGRKSPTTPWGYPALGRRSRKRNKYSDNFIIRRRSK rk14_spiol 50S ribosomal protein L14, chloroplastic Chloroplastic large ribosomal subunit protein uL14c Ribosomal protein CS-L29 rpl14 protein protein spiol Spinacia oleracea (Spinach) Spinach MIQPQTHLNVADNSGARELMCIRIIGASNRRYARIGDVIVAVIKEAIPNTPLERSEVIRAVVVRTCKELKRDNGMIIRYDDNAAVIIDQEGNPKGTRIFGAIARELRQKFAKIVSLAPEVL rk13_spiol 50S ribosomal protein L13, chloroplastic CL13 Chloroplastic large ribosomal subunit protein uL13c SOVF_093170 RPL13 protein protein spiol Spinacia oleracea (Spinach) Spinach MATMACASSLTFPSAQTQKSFFGTNVKQTPVLSFPRPTVAAAVAVSARKSTSASTKCTEEWRQLKEAVKKEFAIPHVPLDQRWMFTLEEATGPDIWNTTWYPKSADHVPTDKKWYVVDATDLILGRMASTIAIHIRGKNLASYTPSVDMGAFVIVVNADKVAVSGKKRTQKLYRRHSGRPGGLKEETFDQLQKRIPERIIEHAVRGMLPKGRLGRYLFNHLKVYKGAEHPHQAQQPIDLPLRDKRIRVEK rk9_spiol 50S ribosomal protein L9, chloroplastic CL9 Chloroplastic large ribosomal subunit protein bL9c SOVF_040960 RPL9 protein protein spiol Spinacia oleracea (Spinach) Spinach MASTTSTLSLSWSNSFHSFAGAISEPQKSPENCRVMLPIVAQKKVKKIRKIILKEDIPDLGKKGQLLDVRAGFLRNFLLPLGKAEVVTPLLLKEMKMEDERIEAEKKRVKEEAQQLARMFETVGAFKVKRKGGKGKQIFGSVTAQDLVDIIKAQLQRDVDKKVVFLPDIRETGEYIAELKLHPDVTAQVRVTVFAN rk6_spiol 50S ribosomal protein L6, chloroplastic Chloroplastic large ribosomal subunit protein uL6c SOVF_107200 RPL6 protein protein spiol Spinacia oleracea (Spinach) Spinach MSLPLPSHMKSVFLGMKVEISTSVPVTRIGFWRKSVDCKESRIGKQPITVPANVAIAMEGQDLKVKGPLGELSITYPREVLVEKQESGFLRVRKAVETRRANQMHGLFRTLTDNMVVGVSKGFEKKLQLVGVGYRATVEGKDLILSLGFSHPVRMAIPDELQVKVEENTKVTVSGRDKSVVGQFAATIRSWRPPEPYKGKGVRYVDEVVRRKEGKAGKKK rk18_spiol 50S ribosomal protein L18, chloroplastic CL18 Chloroplastic large ribosomal subunit protein uL18c RPL18 PRPL18 SOVF_159210 protein protein spiol Spinacia oleracea (Spinach) Spinach MAAATSLSFFHSTLASSSSSSVQQLSLPPKFVNFRPQTLPLIQAKAHTRREDRTARHVRIRKKVEGTPERPRLCVFRSNKHLYVQVIDDTKMHTLAAASTMQKAISENIDYSAGPTVEVAQKIGEMIAKSCLEKGITKVAFDRGGYPYHGRVKALADAAREHGLVF rk17_spiol 50S ribosomal protein L17, chloroplastic CL17 Chloroplastic large ribosomal subunit protein bL17c SOVF_059230 RPL17 protein protein spiol Spinacia oleracea (Spinach) Spinach MIDNGGRFFAMKHGRKIHRLSRPADQRRALLRGLTTQLLKHGRIKTTRAKASAMRKYVDKMITLAKEGSLHKRRQALGFIYEKQIVHALFAEVPERYGDRNGGYTRIIRTLPRRGDNAPMAYIELV rk16_spiol 50S ribosomal protein L16, chloroplastic Chloroplastic large ribosomal subunit protein uL16c Ribosomal protein CS-L24 rpl16 protein protein spiol Spinacia oleracea (Spinach) Spinach MLSPKRTRFRKQHRGRMKGISYRGNRICFGRYALQALEPAWITSRQIEAGRRAMTRNARRGGKIWVRIFPDKPVTVRPAETRMGSGKGSPEYWVAVVKPGRILYEISGVAENIARRAVAIAASKMPIRTQFIISG rk15_spiol 50S ribosomal protein L15, chloroplastic CL15 Chloroplastic large ribosomal subunit protein uL15c SOVF_177460 RPL15 protein protein spiol Spinacia oleracea (Spinach) Spinach MASLLSLSSTPPSTANSNNYPSSTFKGNINNFRINPFNFAPLKLHLRNIVKKESTRLVVVASASSSNVSPSIGSGSETRFRLDNLGPQPGSRKKGKRKGRGHAAGQGGSCGFGMRGQKSRSGPGIMRGFEGGQMPLYRRIPKLRGIAGGMRAGLPKYVPINLRDIEVAGFKEGEEVSLESLKAKGIINPSGRERRLPLKILGEGELSTKLQIKARAFSGSAKEKLEAAGCSVTVLPGRKKYIKESVRKNLARADEYFAKKRAASASEAESA rk22_spiol 50S ribosomal protein L22, chloroplastic Chloroplastic large ribosomal subunit protein uL22c Ribosomal protein CS-L13 rpl22 protein protein spiol Spinacia oleracea (Spinach) Spinach MGFFKKKEKKAEFDVFRLYGLHHPEPGKCDEITTRGYSISMSVDKARRVIDQIRGRSYAETLMILELMPYRACYPIFKLIYSAAANASHNKQFNKANLIISKAEVNKGITLKKVKPRARGRSYMIKRPTCHITIVLRDITHFDSYDKFLESLTPKKLIALLGLMSTGRRRELLCGRFRENHKIKSFLYKIALFKRYEVM rk21_spiol 50S ribosomal protein L21, chloroplastic CL21 CS-L7 Chloroplastic large ribosomal subunit protein bL21c SOVF_056040 RPL21 protein protein spiol Spinacia oleracea (Spinach) Spinach MASATLAFSCSSLCATLKLPQNLNPLLLNVPPLSKPFSGVVSPPSLSRLSLLPVAAKRRRFQEIPEELKAEFEEFQRPPNQKPQLSDVLPDDFQAPEPGTPEYNDIINQFLPKKGPPPPREEIFAVVVIGSRQYIVIPGRWIYTQRLKGATVNDKIVLNKVLLVGTKASTYIGTPIVTNAAVHAVVEEQLLDDKVIVFKYKKKKNYRRNIGHRQPITRIKITGITGYEDYPASTLEAEVEAKEEAEAEAEAEAVPV rk20_spiol 50S ribosomal protein L20, chloroplastic Chloroplastic large ribosomal subunit protein bL20c rpl20 protein protein spiol Spinacia oleracea (Spinach) Spinach MTRVKRGYIARRRRKKIRFFASSFRGAHSRLTRTIAQQKIRALVSAHRDRDRQKRDFRRLWITRINAAIRERGVYYNYSKFIHDLYKRQLLLNRKILAQIAILNPNCIYMIYNEIIKKEDCKKYLEII rk19_spiol 50S ribosomal protein L19, chloroplastic CL19 Chloroplastic large ribosomal subunit protein bL19c RPL19 PRPL19 SOVF_150800 protein protein spiol Spinacia oleracea (Spinach) Spinach MASKVLPQALLVIPSNHSLQCPPLKKQLGFPIDSNRRFSLSSNCRSNLMVSRASSNLFSSNFSSIFSFPARNSFVVRSEAEDSSDAPAESVAVVAEEELPVESEAEAEERPPRQQRVKLGDIMGILNKKAVHAAEELRPVPGIRTGDIVQIRLEVPENKRRLSVYKGIVISRQNAGIHTTIRIRRIIAGVGVEIVFPLYSPNIKEIKVVSHRKVRKARLYYLRDKLPRLSTFK rk28_spiol 50S ribosomal protein L28, chloroplastic CL28 Chloroplastic large ribosomal subunit protein bL28c SOVF_085320 RPL28 protein protein spiol Spinacia oleracea (Spinach) Spinach MAASGMLISNPSNVCFRKPQFSCSLKPKATVSELGFLTSQLSGIQISPSPLFPIISKPISAPLKPSLQPVARRICPFTGKKSNKANRVSHSNHKTKRLQFVNLQYKRVWWEAGKRFVKLRLSTKALKTIEKNGLDAVAKKAGIDLRKE rk27_spiol 50S ribosomal protein L27, chloroplastic CL27 Chloroplastic large ribosomal subunit protein bL27c SOVF_107450 RPL27 protein protein spiol Spinacia oleracea (Spinach) Spinach MAVTTSMSFNLMASFRGMSLSSSSSSSFFKGEFGPSSLRLPNKSPLSVSPFPLTIESAHKKGAGSTKNGRDSKGQRLGVKIYGDQVAKPGAIIIRQRGTKFHPGKNVGIGKDHTIFALIDGLVKFEKYGPDKKKVSVYPREIQPENPNSYRARKRENFRLQREKKKARREGYSFQPQLILASAATDNADESAVC rk24_spiol 50S ribosomal protein L24, chloroplastic CL24 Chloroplastic large ribosomal subunit protein uL24c SOVF_183870 RPL24 protein protein spiol Spinacia oleracea (Spinach) Spinach MAAMAALQSSFTSLSLSSNSFLGQRLFPSPTTLQVKTEGHSPCLIVMRIKRWERKDCKPNSLPKLHKMHVKVGDTVKVISGGEKGKIGEISKIHKHNSTVIIKDLNLKTKHVKSKEEGEQGQIIKIEAAIHSSNVMLYSKEQEVASRVGHKILEDGRKVRYLIKTGEIVDTPDRWKEIQNKKESETAVAVAA rk23_spiol 50S ribosomal protein L23, chloroplastic Chloroplastic large ribosomal subunit protein uL23c PRPL23 SOVF_109700 RPL23 protein protein spiol Spinacia oleracea (Spinach) Spinach MATTAPNLHSLSSSFAFSNPSSNVSATSFTFQIPNKKAQISCISSKKLHTQKSFNFHDAVTPMNKPSFGRDLMVAQATEAVAPTTEEAATSQPKTSKKAKKLKYPRRILDVYQILQSPIITEAAIKNIADENSLLFTVDVRADKKMIREAISNFFGVKVRKVNTLIRPDGTKKAYIMLNKEYNASELAKKIGIFPGGN rk34_spiol 50S ribosomal protein L34, chloroplastic CL34 Chloroplastic large ribosomal subunit protein bL34c SOVF_073030 RPL34 protein protein spiol Spinacia oleracea (Spinach) Spinach MATLSLLSTGVGAAITNRTPSASLTFITGSRTTNKRVSFNGGSARSGSLHCSFLAPSSSLSSNFSGLSLGLDLTSNTGVSTDRCRRFVVRAGKAALCLTKRSRSRKSLARTHGFRLRMSTTSGRALLKRRRAKGRKILCTKTNPSSGKRASP rk33_spiol 50S ribosomal protein L33, chloroplastic Chloroplastic large ribosomal subunit protein bL33c rpl33 protein protein spiol Spinacia oleracea (Spinach) Spinach MAKGKDVRVKVILECTGCVRKSVNKGSRGVSRYITQKNRHNTPSRLELRKFCPYCYKHTIHGEIKK rk32_spiol 50S ribosomal protein L32, chloroplastic Chloroplastic large ribosomal subunit protein bL32c rpl32 protein protein spiol Spinacia oleracea (Spinach) Spinach MAVPKKRTSIYKKRIRKNIWKKKGYWAALKAFSLAKSLSTGNSKSFFVRKISNQTLE rk29_spiol 50S ribosomal protein L29, chloroplastic CL29 Chloroplastic large ribosomal subunit protein uL29c SOVF_096810 RPL29 protein protein spiol Spinacia oleracea (Spinach) Spinach MLAIHSLSSTPCSSGLTSPPKSTLLTKSSFHGLRLPSVNLSSSLRLRVQTPPSSVVVMVKKEDELKELRTKTNEQLNEEILQLKGELFMLRLQRSARENFKPSDFGRMRKRVARMLTVKREREIEQGVGKRLSRKLDKAWKRSIVVRPPPSLKKLQEKATAEAEAEKA psrp6_spiol 50S ribosomal protein 6, chloroplastic CL25 Chloroplastic large ribosomal subunit protein cL38 Plastid-specific 50S ribosomal protein 6 SOVF_082300 PSRP6 protein protein spiol Spinacia oleracea (Spinach) Spinach MSVSAIFGARVVTIPSVLRTSSVDGRTVKLQPSTGGSCGGGVITIECSSRPQKKGTAHHMKTRPKKTARWDIKRGPAVYPPLPPLPAEWTIVSSAVDEADSSSSTTSSSAEIAQSA rrfc_spiol Ribosome-recycling factor, chloroplastic CpFrr RRFHCP Ribosome-releasing factor, chloroplastic RRF FRRHCP protein protein spiol Spinacia oleracea (Spinach) Spinach MAASSLSSATSYLHSFRRRNSCVSLQGVSDMECNIARTNVSVWRSSANYVRMDCGVKKFSGKAVVVKQLQNRAGTFRCATMEEVEAEKSLIETNTKQRMEKTIETIRSNFNSVRTNRASPTMLDRIEVEYYGTPVSLKSIAQISTPDASSLLISPYDKSSLKAIEKAIVTSQLGVSPNNDGEVIRLSLPPLTSDRRKELAKVVSKLAEEGKVAVRNIRRDALKSYEKLEKEKKLSEDNVKDLSADLQKLTDEYMKKVESIYKQKEQELMKV rk36_spiol 50S ribosomal protein L36, chloroplastic Chloroplastic large ribosomal subunit protein bL36c rpl36 protein protein spiol Spinacia oleracea (Spinach) Spinach MKIRASVRPICEKCRLIRRRGRIIVICSNPKHKQRQG rk35_spiol 50S ribosomal protein L35, chloroplastic CL35 Chloroplastic large ribosomal subunit protein bL35c SOVF_080710 RPL35 protein protein spiol Spinacia oleracea (Spinach) Spinach MAMASATATLSFKTPSLSLSPPSTRCSAAQGISLTHFNKQLKSTLNLSSSSSISSSKVQPIVLKNKRISTVDSSVSTSSPSFTVFAAKGYKMKTHKASAKRFRVTGKGKIVRRRAGKQHLLAKKNTKRKNRLSKLIQVDRSDYDNVIGALPYLKVNRKV psrp5_spiol 50S ribosomal protein 5 alpha, chloroplastic 50S ribosomal protein L40 CL40 Chloroplastic large ribosomal subunit protein cL37 Plastid-specific 50S ribosomal protein 5 alpha PSRP5 RPL40 SOVF_000530 protein protein spiol Spinacia oleracea (Spinach) Spinach MALLSPLLSLSSVPPITSIAVSSSSFPIKLQNVSVALLPSFGQRLVAHGPVIAQKRGTVVAMVSAAAEETAGEDGDQSKVEEANISVQNLPLESKLQLKLEQKIKMKMAKKIRLRRNRLMRKRKLRKRGAWPPSKMKKLKNV rk31_spiol 50S ribosomal protein L31, chloroplastic CL31 Chloroplastic large ribosomal subunit protein bL31c SOVF_125040 RPL31 protein protein spiol Spinacia oleracea (Spinach) Spinach MVLTLSNQFLAKIPATPKTLTLPKTSSSTLRPQWSCRKSDIHPEFREDAKVYCNGELVMTTGGTQKDYTVEVWSGNHPFYLGNRSALLLDADQVEKFRKKYGELTQIMEIPVLKGEIILPPKKKSKAKKK e1c9l2_pea Chlorophyll a-b binding protein, chloroplastic protein protein pea Pisum sativum (Garden pea) Garden pea SAPGDFGFDPLGLGEVPANLERYKESELIHCRWAMLAVPGILVPEALGYGNWVKAQEWAALPGGQATYLGNPVPWGTLPTILAIEFLAIAFVEHQRSMEKDPEKKKYPGGAFDPLGYSKDPKKLEELKVKEIKNGRLALLAFVGFCVQQSAYPGTGPLENLATHLADPWH e1c9l1_pea PSI subunit V protein protein pea Pisum sativum (Garden pea) Garden pea KPTYQVIQPINGDPFIGSLETPVTSSPLIAWYLSNLPAYRTAVSPLLRGIEVGLAHGYLLVGPFVKAGPLRNTEIAGQAGSLAAGGLVVILSLCLTIYGISSFNEGAPSTAPSLTLTGRKKEPDQLQTADGWAKFTGGFFFGGISGVIWAYFLLYVLDLPY psaf_spiol Photosystem I reaction center subunit III, chloroplastic PSAF Light-harvesting complex I 17 kDa protein PSI-F protein protein spiol Spinacia oleracea (Spinach) Spinach MSFTIPTNLYKPLATKPKHLSSSSFAPRSKIVCQQENDQQQPKKLELAKVGANAAAALALSSVLLSSWSVAPDAAMADIAGLTPCKESKQFAKREKQALKKLQASLKLYADDSAPALAIKATMEKTKKRFDNYGKYGLLCGSDGLPHLIVSGDQRHWGEFITPGILFLYIAGWIGWVGRSYLIAIRDEKKPTQKEIIIDVPLASSLLFRGFSWPVAAYRELLNGELVDNNF 270E1BAC159D79B4 mint e1c9k9_pea protein protein pea Pisum sativum (Garden pea) Garden pea DLEDLGNTTGQWDSYGSDAPSPYNPLQSKLFETFAAPFTKRGLLLKFLILGGGSTLAYLSATASGDILP psag_pea Photosystem I reaction center subunit V PSAG PSI-G Photosystem I 9 kDa protein protein protein pea Pisum sativum (Garden pea) Garden pea ELNPSLVISLSTGLSLFLGRFVFFNFQRENVAKQGLPEQ e1c9l3_pea PSI-K Photosystem I subunit X protein protein pea Pisum sativum (Garden pea) Garden pea DFIGSPTNLIMVTSTSLMLFAGRFGLAPSANRKATAGLKLEVRDSGLQTGDPAGFTLADTLACGVVGHIIGVGVVLGLKNIGAL e1c9l0_pea PSI-J Photosystem I reaction center subunit IX protein protein pea Pisum sativum (Garden pea) Garden pea MRDLKTYLSVAPVVSTLWFGALAGLLIEINRFFPDALIFPFF cb24_pea Chlorophyll a-b binding protein P4, chloroplastic lhcA-P4 LHCI type III CAB-P4 protein protein pea Pisum sativum (Garden pea) Garden pea MATVTTQASAAIFGPCGLKSRFLGGSSGKLNRGVAFRPVGCSPSASFKVEAKKGEWLPGLASPGYLTGSLPGDNGFDPLGLAEDPENLRWFVQAELVNGRWAMLGVAGMLLPEVFTSIGIINVPKWYAAGKEEYFASSSTLFVIEFILSHYVEIRRWQDIKNPGSVNQDPIFKQYSLPAGEVGYPGGIFNPLNFAPTLEAKEKEIANGRLAMLAFLGFIIQHNVTGKGPFDNLLQHISDPWHNTIVQTLGGN cb23_pea Chlorophyll a-b binding protein 3, chloroplastic lhca3 LHCII type III CAB-3 protein protein pea Pisum sativum (Garden pea) Garden pea MATQALVSSSSLTFAAEAVRQSFRARSLPSSVGCSRKGLVRAAATPPVKQGGVDRPLWFASKQSLSYLDGSLPGDYGFDPLGLSDPEGTGGFIEPRWLAYGEVINGRFAMLGAVGAIAPEYLGKVGLIPQETALAWFQTGVIPPAGTYNYWADNYTLFVLEMALMGFAEHRRFQDWAKPGSMGKQYFLGLEKGFGGSGNPAYPGGPFFNPLGFGKDEKSLKELKLKEVKNGRLAMLAILGYFIQGLVTGVGPYQNLLDHVADPVNNNVLTSLKFH e1c9k6_pea protein protein pea Pisum sativum (Garden pea) Garden pea IGPKRGAKVKILRKESYWYKGTGSVVAVDQDPNTRYPVVVRFNKVNYANVSTNNYALDEIVEVE e1c9k8_pea protein protein pea Pisum sativum (Garden pea) Garden pea ELDPNTPSPIFGGSTGGLLRKAQVEEFYVITWDSPKEQIFEMPTGGAAIMREGPNLLKLARKEQCLALGTRLRSKYKIKYQFYRVFPNGEVQYLHPKDGVYPEKVNAGRQGVGQNFRSIGKNVSPIEVKFTGKQPYDL psac_pea Photosystem I iron-sulfur center psaC 9 kDa polypeptide PSI-C Photosystem I subunit VII PsaC frxA protein protein pea Pisum sativum (Garden pea) Garden pea MSHSVKIYDTCIGCTQCVRACPTDVLEMIPWGGCKAKQIASAPRTEDCVGCKRCESACPTDFLSVRVYLWHETTRSMGLAY psab_pea Photosystem I P700 chlorophyll a apoprotein A2 psaB PSI-B PsaB psaA2 protein protein pea Pisum sativum (Garden pea) Garden pea MALRIPRFSQGIAQDPTTRRIWFGIATAHDFESHDDITEGRLYQNIFASHFGQLAIIFLWTSGNLFHVAWQGNFEAWVQDPFHVRPIAHAIWDPHFGQPAVEAFTRGGALGPVNNAYSGVYQWWYTIGLRTNEDLYTGAIFLLFLSFISLLAGWLHLQPKWKPSVSWFKNAESRLNHHLSGLFGVSSLAWAGHLVHVAIPGSRGEYVRWNNFLDVLPYPQGLGPLLTGQWNLYAQNPSSSNHLFGTTQGAGTAILTILGGFHPQTQSLWLTDVAHHHLAIAFLFLIGGLMYRTNFGIGHSIKYILEAHIPPGGRLGRGHKGLYDTINNSIHFQLGLALASLGVITSLVAQHMYSLPAYAFIAQDFTTQAALYTHHQYIAGFIMTGAFAHGPIFFIRDYNPEQNADNVLARMLEHKEAIISHLSWASLFLGFHTLGLYVHNDVMLAFGTPEKQILIEPIFAQWIQSAHGKTTYGFDIPLSSTNGPALNAGRNIWLPGWLNAINENSNSLFLTIGPGDFLVHHAIALGLHTTTLILVKGALDARGSKLMPDKKDFGYSFPCDGPGRGGTCDISAWDDFYLAVFWMLNTIGWVTFYWHWKHITLWRGNVSQFNESSTYLMGWLRDYLWLNSSQLINGITPLVCNSLSVWAWMFLFGHLVWATGFMFLISWRGYWQELIETLAWAHERTPLANLIRWRDKPVALSIVQARLVGLVHFSVGYIFTYAAFLIASTSGKFG q41038_pea Chlorophyll a-b binding protein, chloroplastic lhaB protein protein pea Pisum sativum (Garden pea) Garden pea MASACASSAIAAVAISTPSSQKNGSPSGTSKAFLGRKLKVNSSTASPSRVRSTSTVCTVAEPDRPLWFPGSTPPPWLDGSLPGDFGFDPLGLGSDPESLRWNVQAELVHSRWAMLGAAGIFIPEFLTKLGILNTPSWYTAGEQEYFTDTTTLFIVELVFIGWAEGRRWADILNPGCVNTDPIFPNNKLTGTDVGYPGGLWFDPLGWGSASPQKLKELRTKEIKNGRLAMLAVMGAWFQHIYTGTGPIDNLFAHLADPGHATIFAAFTPK psai_pea Photosystem I reaction center subunit VIII psaI protein protein pea Pisum sativum (Garden pea) Garden pea MINLPSLFVPLVGLLFPAVAMASLFLHVEKRLLFSTKKIN psaa_pea Photosystem I P700 chlorophyll a apoprotein A1 psaA PSI-A PsaA psaA1 protein protein pea Pisum sativum (Garden pea) Garden pea MIIRSPEPKVQILADPEVKILVDRDPIKTSFEQWAKPGHFSRTIAKGPDTTTWIWNLHADAHDFDSHTSDLEEISRKVFSAHFGQLSIIFLWLSGMYFHGARFSNYEAWLNDPTHIGPSAQVVWPIVGQEILNGDVGGGFRGIQITSGFFQIWRASGITSELQLYCTAIGALVFAGLMLFAGWFHYHKAAPKLAWFQDVESMLNHHLAGLLGLGSLSWARHQVHVSLPINQFLNAGVDPKEIPLPHEFILNRDLLAQLYPSFAEGATPFFTLNWSKYADFLTFRGGLDPLTGGLWLTDIAHHHLAIAILFLIAGHMYRTNWGIGHGIKDILEAHKGPFTGQGHKGLYEILTTSWHAQLSINLAMLGSLTIVVAQHMYSMPPYPYLATDYATQLSLFTHHMWIGGFLIVGAAAHAAIFMVRDYDPTTRYNDLLDRVLRHRDAIISHLNWVCIFLGFHSFGLYIHNDTMSALGRPQDMFSDTAIQLQPVFAQWIQNTHALAPGTTAPGATASTSLTWGGGDLVAVGNKVALLPIPLGTADFLVHHIHAFTIHVTVLILLKGVLFARSSRLIPDKANLGFRFPCDGPGRGGTCQVSAWDHVFLGLFWMYNSISVVIFHFSWKMQSDVWGTINDQGVVTHITAGNFAQSSITINGWLRDFLWAQASQVIQSYGSSLSAYGLFFLGAHFVWAFSLMFLFSGRGYWQELIESIVWAHNKLKVAPATQPRALSIVQGRAVGVTHYLLGGIATTWAFFLARIIAVG acp1_spiol Acyl carrier protein 1, chloroplastic ACL1.1 protein protein spiol Spinacia oleracea (Spinach) Spinach MASLSATTTVRVQPSSSSLHKLSQGNGRCSSIVCLDWGKSSFPTLRTSRRRSFISAAKKETIDKVCDIVKEKLALGADVVVTADSEFSKLGADSLDTVEIVMNLEEEFGINVDEDKAQDISTIQQAADVIESLLEKKA stad_ricco Stearoyl-[acyl-carrier-protein] 9-desaturase, chloroplastic Acyl-[acyl-carrier-protein] desaturase Delta(9) stearoyl-acyl carrier protein desaturase protein protein castor bean Ricinus communis Castor bean MALKLNPFLSQTQKLPSFALPPMASTRSPKFYMASTLKSGSKEVENLKKPFMPPREVHVQVTHSMPPQKIEIFKSLDNWAEENILVHLKPVEKCWQPQDFLPDPASDGFDEQVRELRERAKEIPDDYFVVLVGDMITEEALPTYQTMLNTLDGVRDETGASPTSWAIWTRAWTAEENRHGDLLNKYLYLSGRVDMRQIEKTIQYLIGSGMDPRTENSPYLGFIYTSFQERATFISHGNTARQAKEHGDIKLAQICGTIAADEKRHETAYTKIVEKLFEIDPDGTVLAFADMMRKKISMPAHLMYDGRDDNLFDHFSAVAQRLGVYTAKDYADILEFLVGRWKVDKLTGLSAEGQKAQDYVCRLPPRIRRLEERAQGRAKEAPTMPFSWIFDRQVKL psbs_spiol Photosystem II 22 kDa protein, chloroplastic PSBS CP22 protein protein spiol Spinacia oleracea (Spinach) Spinach MAQAMLLMMPGVSTTNTIDLKRNALLKLQIQKIKPKSSTSNLFFSPLPSSSSSSSTVFKTLALFKSKAKAPKKVEKPKLKVEDGLFGTSGGIGFTKENELFVGRVAMIGFAASLLGEGITGKGILSQLNLETGIPIYEAEPLLLFFILFTLLGAIGALGDRGRFVDEPTTGLEKAVIPPGKDVRSALGLKTKGPLFGFTKSNELFVGRLAQLGFAFSLIGEIITGKGALAQLNIETGVPINEIEPLVLLNVVFFFIAAINPGTGKFITDDEEED rbl_spiol Ribulose bisphosphate carboxylase large chain rbcL protein protein spiol Spinacia oleracea (Spinach) Spinach MSPQTETKASVEFKAGVKDYKLTYYTPEYETLDTDILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTNLDRYKGRCYHIEPVAGEENQYICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEDMMKRAVFARELGVPIVMHDYLTGGFTANTTLSHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDYTEKDRSRGIYFTQSWVSTPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNTIIREATKWSPELAAACEVWKEIKFEFPAMDTV mint RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site rbcmt_pea Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplastic RBCMT [Fructose-bisphosphate aldolase]-lysine N-methyltransferase [Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase protein protein pea Pisum sativum (Garden pea) Garden pea MATIFSGGSVSPFLFHTNKGTSFTPKAPILHLKRSFSAKSVASVGTEPSLSPAVQTFWKWLQEEGVITAKTPVKASVVTEGLGLVALKDISRNDVILQVPKRLWINPDAVAASEIGRVCSELKPWLSVILFLIRERSREDSVWKHYFGILPQETDSTIYWSEEELQELQGSQLLKTTVSVKEYVKNECLKLEQEIILPNKRLFPDPVTLDDFFWAFGILRSRAFSRLRNENLVVVPMADLINHSAGVTTEDHAYEVKGAAGLFSWDYLFSLKSPLSVKAGEQVYIQYDLNKSNAELALDYGFIEPNENRHAYTLTLEISESDPFFDDKLDVAESNGFAQTAYFDIFYNRTLPPGLLPYLRLVALGGTDAFLLESLFRDTIWGHLELSVSRDNEELLCKAVREACKSALAGYHTTIEQDRELKEGNLDSRLAIAVGIREGEKMVLQQIDGIFEQKELELDQLEYYQERRLKDLGLCGENGDILGDLGKFF rbs1_spiol Ribulose bisphosphate carboxylase small subunit, chloroplastic 1 RBCS1 RBCS protein protein spiol Spinacia oleracea (Spinach) Spinach MQVWPPLGLKKFETLSYLPPLTTEQLLAEVNYLLVKGWIPPLEFEVKDGFVYREHDKSPGYYDGRYWTMWKLPMFGGTDPAQVVNEVEEVKKAPPDAFVRFIGFNDKREVQCISFIAYKPAGY e1c9k7_pea protein protein pea Pisum sativum (Garden pea) Garden pea GVIEEYLEKSKTNKELNDKKRLATTGANFARAYTVEFGSCKFPENFTGCQDLAKQKKVPFLSDDLDLECEGKDKYKCGSNVFWKW q41372_spiol SOVF_195660 protein protein spiol Spinacia oleracea (Spinach) Spinach MSKEVSEEAQAHQHGKDYVDPPPAPFFDLGELKLWSFWRAAIAEFIATLLFLYITVATVIGHSKETVVCGSVGLLGIAWAFGGMIFVLVYCTAGISGGHINPAVTFGLFLARKVSLLRALVYMIAQCLGAICGVGLVKAFMKGPYNQFGGGANSVALGYNKGTALGAEIIGTFVLVYTVFSATDPKRSARDSHVPILAPLPIGFAVFMVHLATIPITGTGINPARSFGAAVIFNSNKVWDDQWIFWVGPFIGAAVAAAYHQYVLRAAAIKALGSFRSNPTN mint nip1_arath NEP1-interacting protein 1 NIP1 ATL26 F4B14.110 At4g35840 RING-H2 finger protein ATL26 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MASSRFQSGFCPISSCPSLENFIERIKDACRFTLSAVLGTILSAVLTFFFALVGTLLGALTGALIGQETESGFIRGAAVGAISGAVFSIEVFESSLVLWKSNESRFGCLLYLIDVIVSLISGRLVRERIGPAMLSAVQSQMGAVDSTFEELSSIFDTGGSKGLTGDLVDKIPKIKITGKNNLDASGNKDSCSVCLQDFQLGETVRSLPHCHHMFHLPCIDNWLFRHGSCPMCRRDL q52gz4_spiol DNA-directed RNA polymerase rpoT2 protein protein spiol Spinacia oleracea (Spinach) Spinach MSSSNISSFPAVLSQNFDPYIQIYKSRSNFLINPCFDSTIMWRNFAKQAISRTPNLCLRKFSISRSYSFLGGTHDCGFSDRLKFRPFELGFCKNRSFSEVGFCREGGSLVKEGIGERPVSGCLGNRLNFNVVCPKGYASVVEAEVDSSTDLEDDVSVFDEIQELVEEMRKEEKRAKWRESHQRQQKMVAGMPLYKYQKLRNRQIKLETESWQQAANEYKELLADMCKLKLAPNLPYVKSLFLGWFEPFRDSIIEDQELIRQGKCRGAYGTYFDQLPADMMAIITMHKLMGMLMTGSGHGSVKVVQAACALGEAIEQEVRIHTFLEKAKKKKGDRSKKPDDAASDAEIQEQQHLRKNVNNLIKKQKRRQALKIVDSQGDLKPWGSETRAKVGSRLIELLIQTAYIQPPASQSACDPPDLRPAFVHSLKSVGPENKKTGRRFGMIECDPLIIKGLEKTPRHIVIPYMPMLVPPEKWTGYDKGAYLVLRSFVMRTHGSKHQRVAVRRASEEQLKSVFEALDTLGNTKWRVNKKVLSIVDRVWANGGRLADLVDRDDVPLPEKPDTEDESELKRWKWKVRSLKKENRERHSQRCDVELKLAVARKMKDEEGFFYPHNVDFRGRAYPMHPYLNHLGSDMCRGILEFAEGRAVGKSGLRWLKIHVANLYAGGIDKLSLEGRIAFTENHLDDIFDSVDKPLEGRCWWLKAEDPFQCLAVCIELAEALRSTRPEAFKSHIPVHQDGSCNGLQHYAALGRDELGATAVNLVAGEKPADVYSGIASRVLSIMEADAKKDPTDFPDTVLARKLINQVDRKLVKQTVMTSVYGVTYIGAREQIKRRLKERAAFSDDTEIYGAACYVARITLTALGEMFQAARSIMSWLGDCAKIIASENQPVRWITPLGLPVVQPYCKKGRHLIKTSLQMLTLEKETEKIMVRRQKSAFPPNFVHSLDGSHMMMTAVACKHAGLNFAGVHDSYWTHACDVDQMSSILREKFVELYDQPILENLLETFQQSYPTLSFPPLPDRGDFELRDVLDSPYFFN a8e124_spiol nip SOVF_186590 protein protein spiol Spinacia oleracea (Spinach) Spinach MEFYSYPSQRIASSSSILCDLGEKIRGTLSFAVSVTLGSLFSAFFTFCFALVGTLLGAMTGALIGQETESGFVRGAAIGAISGAVFSIEVFESSVVLWRSDESGIGCILYLIDVIASLLSGRLVRERIGPAMLSAVQSQMGAVETNFEDITNIFDTGSVKGLSGDLVEKIPKIKITKNNNNDASGERVSCSVCLQDFQIGETVRSLPDCHHLFHLPCIDKWLLKHASCPLCRRDL nip2_arath NEP1-interacting protein 2 NIP2 ATL25 T17A5.9 At2g17730 RING-H2 finger protein ATL25 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MASSSSSSYRFQSGSYPLSSSPSLGNFVERIKDACHFLVSAVLGTIISAILTFFFALVGTLLGALTGALIGQETESGFIRGAAIGAISGAVFSIEVFESSLDLWKSDESGFGCFLYLIDVIVSLLSGRLVRERIGPAMLSAVQSQMGAVDTAFDDHTSLFDTGGSKGLTGDLVEKIPKMTITGNNNTDASENTDSCSVCLQDFQLGETVRSLPHCHHMFHLPCIDNWLLRHGSCPMCRRDI g3pb_spiol Glyceraldehyde-3-phosphate dehydrogenase B, chloroplastic NADP-dependent glyceraldehydephosphate dehydrogenase subunit B GAPB GPB1 protein protein spiol Spinacia oleracea (Spinach) Spinach MASHAALAPSRIPASTRLASKASQQYSFLTQCSFKRLDVADFSGLRSSNSVTFTREASFHDVIAAQLTTKPTGAAPVRGETVAKLKVAINGFGRIGRNFLRCWHGRKDSPLDVVVVNDSGGVKSATHLLKYDSILGTFKADVKIIDNETFSIDGKPIKVVSNRDPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAKGSDIPTYVVGVNEKDYGHDVANIISNASCTTNCLAPFVKVLDEELGIVKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTPNVSVVDLVVNIEKVGVTAEDVNNAFRKAAAGPLKGVLDVCDIPLVSVDFRCSDFSSTIDSSLTMVMGGDMVKVVAWYDNEWGYSQRVVDLADLVANKWPGLEGSVASGDPLEDFCKDNPADEECKLYE g3pa_spiol Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic GAPA GPA1 NADP-dependent glyceraldehydephosphate dehydrogenase subunit A protein protein spiol Spinacia oleracea (Spinach) Spinach MASNMLSIANPSLRVYNKGFSEFSGLHTSSLPFGRKGSDDLMAFVSFQTNAVGGKRSSQNGVVEAKLKVAINGFGRIGRNFLRCWHGRKDSPLDVVVINDTGGVKQASHLLKYDSILGTFDADVKTAGDSAISVDGKVIKVVSDRNPVNLPWGDMGIDLVIEGTGVFVDRDGAGKHLQAGAKKVLITAPGKGDIPTYVVGVNEEGYTHADTIISNASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAACLNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQVSKKTFAEEVNAAFRESADNELKGILSVCDEPLVSIDFRCTDVSSTIDSSLTMVMGDDMVKVIAWYDNEWGYSQRVVDLADIVANKWQ petd_spiol Cytochrome b6-f complex subunit 4 petD 17 kDa polypeptide protein protein spiol Spinacia oleracea (Spinach) Spinach MGVTKKPDLNDPVLRAKLAKGMGHNYYGEPAWPNDLLYIFPVVILGTIACNVGLAVLEPSMIGEPADPFATPLEILPEWYFFPVFQILRTVPNKLLGVLLMASVPAGLLTVPFLENVNKFQNPFRRPVATTVFLVGTVVALWLGIGATLPIDKSLTLGLF cyf_spiol Cytochrome f petA protein protein spiol Spinacia oleracea (Spinach) Spinach MQTINTFSWIKEQITRSISISLILYIITRSSIANAYPIFAQQGYENPREATGRIVCANCHLANKPVDIEVPQAVLPDTVFEAVVRIPYDMQLKQVLANGKKGGLNVGAVLILPEGFELAPPDRISPEMKEKMGNLSFQSYRPNKQNILVIGPVPGQKYSEITFPILAPDPATKKDVHFLKYPIYVGGNRGRGQIYPDGSKSNNTVYNSTATGIVKKIVRKEKGGYEINIADASDGREVVDIIPRGPELLVSEGESIKLDQPLTSNPNVGGFGQGDAEVVLQDPLRIQGLLFFFASVILAQIFLVLKKKQFEKVQLSEMNF ucria_spiol Cytochrome b6-f complex iron-sulfur subunit, chloroplastic petC Plastohydroquinone:plastocyanin oxidoreductase iron-sulfur protein Rieske iron-sulfur protein protein protein spiol Spinacia oleracea (Spinach) Spinach MASFTLSSATPSQLCSSKNGMFAPSLALAKAGRVNVLISKERIRGMKLTCQATSIPADNVPDMQKRETLNLLLLGALSLPTGYMLLPYASFFVPPGGGAGTGGTIAKDALGNDVIAAEWLKTHAPGDRTLTQGLKGDPTYLVVESDKTLATFGINAVCTHLGCVVPFNAAENKFICPCHGSQYNNQGRVVRGPAPLSLALAHCDVDDGKVVFVPWTETDFRTGEAPWWSA petl_spiol Cytochrome b6-f complex subunit 6 petL Cytochrome b6-f complex subunit PetL Cytochrome b6-f complex subunit VI protein protein spiol Spinacia oleracea (Spinach) Spinach MFTLTSYFGFLLAALTITSALFIGLNKIRLI petm_spiol Cytochrome b6-f complex subunit 7 petM Cytochrome b6-f complex subunit PetM Cytochrome b6-f complex subunit VII protein protein spiol Spinacia oleracea (Spinach) Spinach NAAAEIFRIAAVMNGLTLVGVAIGFVLLRIEATVEE petg_spiol Cytochrome b6-f complex subunit 5 Cytochrome b6-f complex subunit PetG Cytochrome b6-f complex subunit V petG petE protein protein spiol Spinacia oleracea (Spinach) Spinach MIEVFLFGIVLGLIPITLAGLFVTAYLQYRRGDQLDL petn_spiol Cytochrome b6-f complex subunit 8 petN ycf6 Cytochrome b6-f complex subunit PetN Cytochrome b6-f complex subunit VIII protein protein spiol Spinacia oleracea (Spinach) Spinach MDIVSLAWAALMVVFTFSLSLVVWGRSGL cyb6_spiol Cytochrome b6 petB protein protein spiol Spinacia oleracea (Spinach) Spinach MSKVYDWFEERLEIQAIADDITSKYVPPHVNIFYCLGGITLTCFLVQVATGFAMTFYYRPTVTDAFASVQYIMTEVNFGWLIRSVHRWSASMMVLMMILHVFRVYLTGGFKKPRELTWVTGVVLGVLTASFGVTGYSLPWDQIGYWAVKIVTGVPDAIPVIGSPLVELLRGSASVGQSTLTRFYSLHTFVLPLLTAVFMLMHFLMIRKQGISGPL ftrc_syny3 Ferredoxin-thioredoxin reductase, catalytic chain ftrC Ferredoxin-thioredoxin reductase subunit B sll0554 protein protein syny3 Synechocystis sp. (strain PCC 6803 / Kazusa) MTSSDTQNNKTLAAMKNFAEQYAKRTDTYFCSDLSVTAVVIEGLARHKEELGSPLCPCRHYEDKEAEVKNTFWNCPCVPMRERKECHCMLFLTPDNDFAGDAQDIPMETLEEVKASMA ftrv_syny3 Ferredoxin-thioredoxin reductase, variable chain ftrV Ferredoxin-thioredoxin reductase subunit A ssr0330 protein protein syny3 Synechocystis sp. (strain PCC 6803 / Kazusa) MNVGDRVRVTSSVVVYHHPEHKKTAFDLQGMEGEVAAVLTEWQGRPISANLPVLVKFEQRFKAHFRPDEVTLIED trxm_spiol Thioredoxin M-type, chloroplastic protein protein spiol Spinacia oleracea (Spinach) Spinach MAIENCLQLSTSASVGTVAVKSHVHHLQPSSKVNVPTFRGLKRSFPALSSSVSSSSPRQFRYSSVVCKASEAVKEVQDVNDSSWKEFVLESEVPVMVDFWAPWCGPCKLIAPVIDELAKEYSGKIAVYKLNTDEAPGIATQYNIRSIPTVLFFKNGERKESIIGAVPKSTLTDSIEKYLSP fer_syny3 Ferredoxin-1 Ferredoxin I petF fed ssl0020 protein protein syny3 Synechocystis sp. (strain PCC 6803 / Kazusa) MASYTVKLITPDGESSIECSDDTYILDAAEEAGLDLPYSCRAGACSTCAGKITAGSVDQSDQSFLDDDQIEAGYVLTCVAYPTSDCTIETHKEEDLY trxf_spiol Thioredoxin F-type, chloroplastic protein protein spiol Spinacia oleracea (Spinach) Spinach MALHLSLSHQSWTSPAHPITSSDPTRSSVPGTGLSRRVDFLGSCKINGVFVVKRKDRRRMRGGEVRASMEQALGTQEMEAIVGKVTEVNKDTFWPIVKAAGDKPVVLDMFTQWCGPCKAMAPKYEKLAEEYLDVIFLKLDCNQENKTLAKELGIRVVPTFKILKENSVVGEVTGAKYDKLLEAIQAARSS psbj_spiol Photosystem II reaction center protein J psbJ protein protein spiol Spinacia oleracea (Spinach) Spinach MADTTGRIPLWIIGTVAGILVIGLVGIFFYGSYSGLGSSL psbi_spiol Photosystem II reaction center protein I psbI PSII 4.8 kDa protein protein protein spiol Spinacia oleracea (Spinach) Spinach MLTLKLFVYTVVIFFVSLFIFGFLSNDPGRNPGREE psbl_spiol Photosystem II reaction center protein L psbL protein protein spiol Spinacia oleracea (Spinach) Spinach MTQSNPNEQNVELNRTSLYWGLLLIFVLAVLFSNYFFN psbk_spiol Photosystem II reaction center protein K psbK protein protein spiol Spinacia oleracea (Spinach) Spinach MLNIFSLICLNSALYSSSFFFGKLPEAYAFLSPIVDFMPVIPLFFFLLAFVWQAAVSFR psbf_spiol Cytochrome b559 subunit beta psbF PSII reaction center subunit VI protein protein spiol Spinacia oleracea (Spinach) Spinach MTIDRTYPIFTVRWLAIHGLAVPTVFFLGSISAMQFIQR psbe_spiol Cytochrome b559 subunit alpha psbE PSII reaction center subunit V protein protein spiol Spinacia oleracea (Spinach) Spinach MSGSTGERSFADIITSIRYWVIHSITIPSLFIAGWLFVSTGLAYDVFGSPRPNEYFTESRQGIPLITGRFDSLEQLDEFSRSF psbh_spiol Photosystem II reaction center protein H psbH Photosystem II 10 kDa phosphoprotein protein protein spiol Spinacia oleracea (Spinach) Spinach MATQTVESSSRSRPKPTTVGALLKPLNSEYGKVAPGWGTTPLMGVAMALFAVFLSIILEIYNSSVLLDGISMN cb2a_spiol Chlorophyll a-b binding protein, chloroplastic LHCII type I CAB protein protein spiol Spinacia oleracea (Spinach) Spinach MASSTMALSSPSLAGKAVKLGPTASEIIGEGRITMRKTAGKPKTVQSSSPWYGPDRVKYLGPFSGESPSYLTGEFPGDYGWDTAGLSADPETFAKNRELEVIHCRWAMLGALGCVFPELLARNGVKFGEAVWFKAGSQIFSEGGLDYLGNPSLVHAQSILAIWACQVILMGAVEGYRIAGGPLGEVVDPLYPGGSFDPLGLADDPEAFAELKVKEIKNGRLAMFSMFGFFVQAIVTGKGPLENLADHLADPVNNNAWNFATNFVPGK psbb_spiol Photosystem II CP47 reaction center protein psbB PSII 47 kDa protein Protein CP-47 protein protein spiol Spinacia oleracea (Spinach) Spinach MGLPWYRVHTVVLNDPGRLISVHIMHTALVAGWAGSMALYELAVFDPSDPVLDPMWRQGMFVIPFMTRLGITNSWGGWSITGGTITDPGIWSYEGVAGAHIMFSGLCFLAAIWHWVYWDLEIFSDERTGKPSLDLPKIFGIHLFLSGVACFGFGAFHVTGLYGPGIWVSDPYGLTGKVQPVSPAWGVEGFDPFVPGGIASHHIAAGTLGILAGLFHLSVRPPQRLYKGLRMGNIETVLSSSIAAVFFAAFVVAGTMWYGSATTPIELFGPTRYQWDQGYFQQEIYRRVSAGLAENQSFSEAWSKIPEKLAFYDYIGNNPAKGGLFRAGSMDNGDGIAVGWLGHPIFRDKEGRELFVRRMPTFFETFPVVLIDGDGIVRADVPFRRAESKYSVEQVGVTVEFYGGELNGVSYSDPATVKKYARRAQLGEIFELDRATLKSDGVFRSSPRGWFTFGHASFALLFFFGHIWHGSRTLFRDVFAGIDPDLDVQVEFGAFQKIGDPTTRRQGV psba_spiol Photosystem II protein D1 psbA 32 kDa thylakoid membrane protein Photosystem II Q(B) protein protein protein spiol Spinacia oleracea (Spinach) Spinach MTAILERRESESLWGRFCNWITSTENRLYIGWFGVLMIPTLLTATSVFIIAFIAAPPVDIDGIREPVSGSLLYGNNIISGAIIPTSAAIGLHFYPIWEAASVDEWLYNGGPYELIVLHFLLGVACYMGREWELSFRLGMRPWIAVAYSAPVAAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLIRETTENESANEGYRFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVVGIWFTALGISTMAFNLNGFNFNQSVVDSQGRVINTWADIINRANLGMEVMHERNAHNFPLDLAAIEAPSTNG psbd_spiol Photosystem II D2 protein psbD Photosystem Q(A) protein protein protein spiol Spinacia oleracea (Spinach) Spinach MTIAVGKFTKDEKDLFDSMDDWLRRDRFVFVGWSGLLLFPCAYFALGGWFTGTTFVTSWYTHGLASSYLEGCNFLTAAVSTPANSLAHSLLLLWGPEAQGDFTRWCQLGGLWAFVALHGAFALIGFMLRQFELARSVQLRPYNAIAFSGPIAVFVSVFLIYPLGQSGWFFAPSFGVAAIFRFILFFQGFHNWTLNPFHMMGVAGVLGAALLCAIHGATVENTLFEDGDGANTFRAFNPTQAEETYSMVTANRFWSQIFGVAFSNKRWLHFFMLFVPVTGLWMSALGVVGLALNLRAYDFVSQEIRAAEDPEFETFYTKNILLNEGIRAWMAAQDQPHENLIFPEEVLPRGNAL psbc_spiol Photosystem II CP43 reaction center protein psbC PSII 43 kDa protein Photosystem II 44 kDa chlorophyll apoprotein Protein CP-43 protein protein spiol Spinacia oleracea (Spinach) Spinach MKTLYSLRRFYPVETLFNGTLTLAGRDQETTGFAWWAGNARLINLSGKLLGAHVAHAGLIVFWAGAMNLFEVAHFVPEKPMYEQGLILLPHLATLGWGVGPGGEVIDTFPYFVSGVLHLISSAVLGFGGIYHALLGPETLEESFPFFGYVWKDRNKMTTILGIHLILLGIGAFLLVFKALYFGGVYDTWAPGGGDVRKITNVTLSPSIIFGCLLKSPFGGEGWIVSVDDLEDIIGGHVWIGVICILGGIWHILTKPFAWARRALVWSGEAYLSYSLAALSVFGFIACCFVWFNNTAYPSEFYGPTGPEASQAQAFTFLVRDQRLGANVGSAQGPTGLGKYLMRSPTGEVIFGGETMRFWDLRAPWLEPLRGPNGLDLSRLKKDIQPWQERRSAEYMTHAPLGSLNSVGGVATEINAVNYVSPRSWLSTSHFVLGFFLFVGHLWHAGRARAAAAGFEKGIDRDFEPVLSMTPLN a0a0k9rtu3_spiol SOVF_034940 protein protein spiol Spinacia oleracea (Spinach) Spinach MASISAVSMATPITTTTTKTTFFSPLPVVKPQRATLMGQKPRAMGLKVQASLKEKAVTGLTAAALTASMMVPDVAEAAELAPSLKNFLFSIAAGGVVLTAIVGAVVAVSNFDPVKRA psbw_spiol Photosystem II reaction center W protein, chloroplastic psbW PSII 6.1 kDa protein protein protein spiol Spinacia oleracea (Spinach) Spinach MATITASSSASLVARASLVHNSRVGVSSSPILGLPSMTKRSKVTCSIENKPSTTETTTTTNKSMGASLLAAAAAATISNPAMALVDERMSTEGTGLPFGLSNNLLGWILFGVFGLIWALYFVYASGLEEDEESGLSL psbz_spiol Photosystem II reaction center protein Z psbZ ycf9 protein protein spiol Spinacia oleracea (Spinach) Spinach MTIAFQLAVFALIATSSILLISVPVVFASPDGWSSNKNIVFSGTSLWLGLVFLVGILNSLIS a0a0k9quq7_spiol Chlorophyll a-b binding protein, chloroplastic SOVF_146400 protein protein spiol Spinacia oleracea (Spinach) Spinach MASVAASTAAACLGKSELLGNSLNLRSATSAPCSTPSVGPCKIVALFNFGKKAATPPAKSKAKVAVASPADDELAKWYGPDRRIFLPDGLLDRDDIPEYLNGEVPGDYGYDPFGLGKKPEDFAKYQAFELIHARWAMLGAAGCVIPEAFNKFGANCGPEAVWFKTGALLLDGNTLNYFGKNIPINLVLAVVAEVVLLGGAEYYRITNGLDFEDKLHPGGPFDPLGLAKDPDQAALLKVKEIKNGRLAMFSMFAFFIQAYVTGQGPVENLSAHLSDPFGNNLLTVIGGAAERVPTL f2z293_spiol Chlorophyll a-b binding protein, chloroplastic protein protein spiol Spinacia oleracea (Spinach) Spinach AQPKSGFSTDRPLWYPGAKAPEYLDGSLVGDYGFDPFGLGKPAEYLQYDYDGLDQNLAKNLAGDIIGTRTESADVKSTSLQPYSEVFGLQRFRECELIHGRWAMLATLGALTVEGLTGITWQDAGKVELIEGSSYLGQPLPFSMTTLIWIEVLVIGYIEFQRNAELDTEKRLYPGGTFDPLGLASDPEKKPILQLAEIKHARLAMVGFLGFAVQAAVTGKGPLNNWVTHLSDPLHTTILDRFL a0a0k9rhp1_spiol SOVF_065540 protein protein spiol Spinacia oleracea (Spinach) Spinach MASITMTASFLGTTVSKQPPTHHLRRGVVMAKAMPETTTTTKEETSSKRRDLVFAVAAAAACSVARIAMAEEPKRGTPEAKKKYAPVCVTMPSARICYK psbt_spiol Photosystem II reaction center protein T psbT ycf8 protein protein spiol Spinacia oleracea (Spinach) Spinach MEALVYTFLLVSTLGIIFFAIFFREPPKISTKK psbo_spiol Oxygen-evolving enhancer protein 1, chloroplastic PSBO 33 kDa subunit of oxygen evolving system of photosystem II 33 kDa thylakoid membrane protein OEC 33 kDa subunit protein protein spiol Spinacia oleracea (Spinach) Spinach MAASLQASTTFLQPTKVASRNTLQLRSTQNVCKAFGVESASSGGRLSLSLQSDLKELANKCVDATKLAGLALATSALIASGANAEGGKRLTYDEIQSKTYLEVKGTGTANQCPTVEGGVDSFAFKPGKYTAKKFCLEPTKFAVKAEGISKNSGPDFQNTKLMTRLTYTLDEIEGPFEVSSDGTVKFEEKDGIDYAAVTVQLPGGERVPFLFTIKQLVASGKPESFSGDFLVPSYRGSSFLDPKGRGGSTGYDNAVALPAGGRGDEEELQKENNKNVASSKGTITLSVTSSKPETGEVIGVFQSLQPSDTDLGAKVPKDVKIEGVWYAQLEQQ psbm_spiol Photosystem II reaction center protein M psbM protein protein spiol Spinacia oleracea (Spinach) Spinach MEVNILAFIATALFILVPTAFLLIIYVKTVSQND psbq_spiol Oxygen-evolving enhancer protein 3, chloroplastic PSBQ 16 kDa subunit of oxygen evolving system of photosystem II OEC 16 kDa subunit protein protein spiol Spinacia oleracea (Spinach) Spinach MAQAMASMAGLRGASQAVLEGSLQISGSNRLSGPTTSRVAVPKMGLNIRAQQVSAEAETSRRAMLGFVAAGLASGSFVKAVLAEARPIVVGPPPPLSGGLPGTENSDQARDGTLPYTKDRFYLQPLPPTEAAQRAKVSASEILNVKQFIDRKAWPSLQNDLRLRASYLRYDLKTVISAKPKDEKKSLQELTSKLFSSIDNLDHAAKIKSPTEAEKYYGQTVSNINEVLAKLG psbp_spiol Oxygen-evolving enhancer protein 2, chloroplastic PSBP 23 kDa subunit of oxygen evolving system of photosystem II 23 kDa thylakoid membrane protein OEC 23 kDa subunit protein protein spiol Spinacia oleracea (Spinach) Spinach MASTACFLHHHAAISSPAAGRGSAAQRYQAVSIKPNQIVCKAQKQDDNEANVLNSGVSRRLALTVLIGAAAVGSKVSPADAAYGEAANVFGKPKKNTEFMPYNGDGFKLLVPSKWNPSKEKEFPGQVLRYEDNFDATSNLSVLVQPTDKKSITDFGSPEDFLSQVDYLLGKQAYFGKTDSEGGFDSGVVASANVLESSTPVVDGKQYYSITVLTRTADGDEGGKHQVIAATVKDGKLYICKAQAGDKRWFKGAKKFVESATSSFSVA atpf2_spiol ATP synthase subunit b', chloroplastic ATPF2 ATP synthase F(0) sector subunit b' ATPG ATPase subunit II protein protein spiol Spinacia oleracea (Spinach) Spinach MANMLVASSSKTLPTTTTTTITPKPKFPLLKTPLLKLSPPQLPPLKHLNLSVLKSAAITATPLTLSFLLPYPSLAEEIEKASLFDFNLTLPIIMAEFLFLMFALDKIYYTPLGDFMDKRDASIKEQLSGVKDTSSEVKQLEEQANAVMRAARAEISAALNKMKKETQLEVEAKLAEGRKKIEVELQEALGSLEQQKEDTIKSLDSQISALSDDIVKKVLPVS atpg_spiol ATP synthase gamma chain, chloroplastic ATPC F-ATPase gamma subunit protein protein spiol Spinacia oleracea (Spinach) Spinach MACSLSFSSSVSTFHLPTTTQSTQAPPNNATTLPTTNPIQCANLRELRDRIGSVKNTQKITEAMKLVAAAKVRRAQEAVVNGRPFSETLVEVLYNMNEQLQTEDVDVPLTKIRTVKKVALMVVTGDRGLCGGFNNMLLKKAESRIAELKKLGVDYTIISIGKKGNTYFIRRPEIPVDRYFDGTNLPTAKEAQAIADDVFSLFVSEEVDKVEMLYTKFVSLVKSDPVIHTLLPLSPKGEICDINGKCVDAAEDELFRLTTKEGKLTVERDMIKTETPAFSPILEFEQDPAQILDALLPLYLNSQILRALQESLASELAARMTAMSNATDNANELKKTLSINYNRARQAKITGEILEIVAGANACV atpe_spiol ATP synthase epsilon chain, chloroplastic atpE ATP synthase F1 sector epsilon subunit F-ATPase epsilon subunit protein protein spiol Spinacia oleracea (Spinach) Spinach MTLNLCVLTPNRSIWNSEVKEIILSTNSGQIGVLPNHAPTATAVDIGILRIRLNDQWLTLALMGGFARIGNNEITILVNDAERGSDIDPQEAQQTLEIAEANLRKAEGKRQKIEANLALRRARTRVEASNTISS atpd_spiol ATP synthase delta chain, chloroplastic ATPD F-ATPase delta chain protein protein spiol Spinacia oleracea (Spinach) Spinach MAALQNPVALQSRTTTAVAALSTSSTTSTPKPFSLSFSSSTATFNPLRLKILTASKLTAKPRGGALGTRMVDSTASRYASALADVADVTGTLEATNSDVEKLIRIFSEEPVYYFFANPVISIDNKRSVLDEIITTSGLQPHTANFINILIDSERINLVKEILNEFEDVFNKITGTEVAVVTSVVKLENDHLAQIAKGVQKITGAKNVRIKTVIDPSLVAGFTIRYGNEGSKLVDMSVKKQLEEIAAQLEMDDVTLAV atpb_spiol ATP synthase subunit beta, chloroplastic atpB F-ATPase subunit beta ATP synthase F1 sector subunit beta protein protein spiol Spinacia oleracea (Spinach) Spinach MRINPTTSDPGVSTLEKKNLGRIAQIIGPVLDVAFPPGKMPNIYNALIVKGRDTAGQPMNVTCEVQQLLGNNRVRAVAMSATDGLTRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYEIAQRVKETLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDSLPEQAFYLVGNIDEATAKAMNLEMESKLKK mint Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits atpa_spiol ATP synthase subunit alpha, chloroplastic atpA F-ATPase subunit alpha ATP synthase F1 sector subunit alpha protein protein spiol Spinacia oleracea (Spinach) Spinach MATIRADEISKIIRERIEGYNREVKVVNTGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEITASESRLIESPAPGIMSRRSVYEPLQTGLIAIDAMIPVGRGQRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVTNFQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSLLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKKVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLKQPQSAPLTVEEQVMTIYTGTNGYLDSLELDQVRKYLVELRTYVKTNKPEFQEIISSTKTFTEEAEALLKEAIQEQMERFLLQEQA mint Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit atpf_spiol ATP synthase subunit b, chloroplastic atpF ATP synthase F(0) sector subunit b ATPase subunit I protein protein spiol Spinacia oleracea (Spinach) Spinach MKNVTDSFVFLGHWPSAGSFGFNTDILATNLINLSVVLGVLIFFGKGVLSDLLDNRKQRILNTIRNSEELRGKAIEQLEKARARLKKVEMDADQFRVNGYSEIEREKMNLINSTYKTLEQFENYKNETIQFEQQKAINQVRQRVFQQALQGALGTLNSCLNNELHLRTINANIGMFGAMNEITD atpi_spiol ATP synthase subunit a, chloroplastic atpI ATP synthase F0 sector subunit a F-ATPase subunit IV protein protein spiol Spinacia oleracea (Spinach) Spinach MNVLSYSINPLKGLYAISGVEVGQHFYWQIGGFQIHGQVLITSWVVIAILLGSAAIAVRSPQTIPTGGQNFFEYVLEFIRDVSKTQIGEEYRPWVPFIGTMFLFIFVSNWSGALLPWKIIQLPHGELAAPTNDINTTVALALLTSVAYFYAGLTKKGLGYFGKYIQPTPILLPINILEDFTKPLSLSFRLFGNILADELVVVVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIGESLEGHH atph_spiol ATP synthase subunit c, chloroplastic atpH ATP synthase F(0) sector subunit c ATPase subunit III F-type ATPase subunit c Lipid-binding protein protein protein spiol Spinacia oleracea (Spinach) Spinach MNPLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQPEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV rpot2-nip1-1 3173476 N/A 3173480 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast N/A 3173481 unspecified role unspecified role bait bait Region 46-1036 Region 46-1036 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast direct interaction direct interaction false false false nip-rpot2-1 3173477 N/A 3173481 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach N/A 3173482 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach physical association physical association false false false rpot2-nip2-1 3173478 N/A 3173483 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast N/A 3173481 unspecified role unspecified role bait bait Region 46-1036 Region 46-1036 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast direct interaction direct interaction false false false nip1-nip-1 3173479 N/A 3173482 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast N/A 3173480 unspecified role unspecified role bait bait yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast direct interaction direct interaction false false false q41372_spiol-1 3139930 N/A 3139931 unspecified role unspecified role unspecified role unspecified role picpa Pichia pastoris (Yeast) Yeast Pichia pastoris direct interaction direct interaction false false false e1c9k6_pea-e1c9k8_pea-1 3279156 N/A 3279157 unspecified role unspecified role unspecified role unspecified role pea Pisum sativum (Garden pea) Garden pea N/A 3279158 unspecified role unspecified role unspecified role unspecified role pea Pisum sativum (Garden pea) Garden pea N/A 3279159 unspecified role unspecified role unspecified role unspecified role pea Pisum sativum (Garden pea) Garden pea N/A 3279160 unspecified role unspecified role unspecified role unspecified role pea Pisum sativum (Garden pea) Garden pea N/A 3279161 unspecified role unspecified role unspecified role unspecified role pea Pisum sativum (Garden pea) Garden pea N/A 3279162 unspecified role unspecified role unspecified role unspecified role pea Pisum sativum (Garden pea) Garden pea N/A 3279163 unspecified role unspecified role unspecified role unspecified role pea Pisum sativum (Garden pea) Garden pea N/A 3279164 unspecified role unspecified role unspecified role unspecified role pea Pisum sativum (Garden pea) Garden pea N/A 3279165 unspecified role unspecified role unspecified role unspecified role pea Pisum sativum (Garden pea) Garden pea N/A 3279166 unspecified role unspecified role unspecified role unspecified role pea Pisum sativum (Garden pea) Garden pea N/A 3279167 unspecified role unspecified role unspecified role unspecified role pea Pisum sativum (Garden pea) Garden pea N/A 3279168 unspecified role unspecified role unspecified role unspecified role pea Pisum sativum (Garden pea) Garden pea N/A 3279169 unspecified role unspecified role unspecified role unspecified role pea Pisum sativum (Garden pea) Garden pea N/A 3279170 unspecified role unspecified role unspecified role unspecified role pea Pisum sativum (Garden pea) Garden pea N/A 3279171 unspecified role unspecified role unspecified role unspecified role pea Pisum sativum (Garden pea) Garden pea N/A 3279172 unspecified role unspecified role unspecified role unspecified role pea Pisum sativum (Garden pea) Garden pea physical association physical association false false false a0a0k9quq7_spiol-a0a0k9rhp1_spiol-1 3291940 N/A 3291941 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach N/A 3291942 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach N/A 3291943 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach N/A 3291944 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach N/A 3291945 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach N/A 3291946 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach N/A 3291947 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach N/A 3291948 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach N/A 3291949 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach N/A 3291950 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach N/A 3291951 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach N/A 3291952 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach N/A 3291953 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach N/A 3291954 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach N/A 3291955 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach N/A 3291956 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach N/A 3291957 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach N/A 3291958 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach N/A 3291959 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach N/A 3291960 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach N/A 3291961 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach N/A 3291962 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach N/A 3291963 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach physical association physical association false false false e1c9k6_pea-e1c9k7_pea-2 4055684 N/A 3279157 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279158 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 4055688 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279159 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279160 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279161 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279162 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279163 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279164 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279165 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279166 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279167 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279168 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279169 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279170 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279171 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279172 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 physical association physical association false false false Fig 1, Supplementary Table 1 e1c9k6_pea-e1c9k7_pea-3 4055685 N/A 3279157 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279158 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 4055688 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279159 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279160 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279161 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279162 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279163 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279164 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279165 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279166 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279167 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279168 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279169 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279170 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279171 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3279172 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 physical association physical association false false false Supplementary Fig S2 cb2a_spiol-1 4053722 N/A 3291957 unspecified role unspecified role neutral component neutral component purified purified binding region binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false in vitro In vitro Stoichiometry: 60.0 physical association physical association false false false Fig 1, Table 1 rbcl-rbcmt-1 3184068 N/A 3184072 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach N/A 3184073 unspecified role unspecified role unspecified role unspecified role Region 38-485 Region 38-485 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli N/A 3184074 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach physical association physical association false false false rbcl-rbcmt-2 3184069 N/A 3184072 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach N/A 3184073 unspecified role unspecified role unspecified role unspecified role Region 38-485 Region 38-485 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli N/A 3184074 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach physical association physical association false false false psbs-1 3282029 N/A 3282032 unspecified role unspecified role unspecified role unspecified role Region 68-274 Region 68-274 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false spiol Spinacia oleracea (Spinach) Spinach direct interaction direct interaction false false false psbs-2 3282030 N/A 3282032 unspecified role unspecified role unspecified role unspecified role Region 68-274 Region 68-274 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false spiol Spinacia oleracea (Spinach) Spinach direct interaction direct interaction false false false psbs-3 3282031 N/A 3282032 unspecified role unspecified role unspecified role unspecified role Region 68-274 Region 68-274 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false spiol Spinacia oleracea (Spinach) Spinach direct interaction direct interaction false false false acl1.1-stad_ricco-1 3230570 N/A 3230572 unspecified role unspecified role unspecified role unspecified role Mature protein Region 34-396 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli N/A 3230573 unspecified role unspecified role unspecified role unspecified role Mature protein Region 57-138 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false acl1.1-stad_ricco-2 3230571 N/A 3230572 unspecified role unspecified role unspecified role unspecified role Mature protein Region 34-396 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli N/A 3230573 unspecified role unspecified role unspecified role unspecified role Mature protein Region 57-138 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false ftrc-ftrv-2 3158579 N/A 3158585 unspecified role unspecified role unspecified role unspecified role Region 75-180 Region 75-180 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli N/A 3158583 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3158584 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association false false false ftrc-ftrv-4 3158581 N/A 3158587 unspecified role unspecified role unspecified role unspecified role Region 79-189 Region 79-189 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli N/A 3158583 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3158584 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association false false false ftrc-ftrv-5 3158582 N/A 3158587 unspecified role unspecified role unspecified role unspecified role Region 79-189 Region 79-189 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli N/A 3158586 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3158583 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3158584 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association false false false atpa-atpb-4 3439473 N/A 3439474 unspecified role unspecified role neutral component neutral component purified purified spiol Spinacia oleracea (Spinach) Spinach Stoichiometry: 3.0 N/A 3439475 unspecified role unspecified role neutral component neutral component purified purified spiol Spinacia oleracea (Spinach) Spinach Stoichiometry: 3.0 N/A 3439476 unspecified role unspecified role neutral component neutral component purified purified spiol Spinacia oleracea (Spinach) Spinach Stoichiometry: 1.0 N/A 3439477 unspecified role unspecified role neutral component neutral component purified purified spiol Spinacia oleracea (Spinach) Spinach Stoichiometry: 1.0 N/A 3439478 unspecified role unspecified role neutral component neutral component purified purified spiol Spinacia oleracea (Spinach) Spinach Stoichiometry: 1.0 N/A 3439479 unspecified role unspecified role neutral component neutral component purified purified spiol Spinacia oleracea (Spinach) Spinach Stoichiometry: 1.0 N/A 3439480 unspecified role unspecified role neutral component neutral component purified purified spiol Spinacia oleracea (Spinach) Spinach Stoichiometry: 1.0 N/A 3439481 unspecified role unspecified role neutral component neutral component purified purified spiol Spinacia oleracea (Spinach) Spinach Stoichiometry: 1.0 N/A 3439482 unspecified role unspecified role neutral component neutral component purified purified spiol Spinacia oleracea (Spinach) Spinach Stoichiometry: 14.0 physical association physical association false false false Figure 1 gapa-gapb-1 3157786 N/A 3157787 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach N/A 3157788 unspecified role unspecified role unspecified role unspecified role spiol Spinacia oleracea (Spinach) Spinach direct interaction direct interaction false false false peta-petb-5 3649439 N/A 3649441 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified spiol Spinacia oleracea (Spinach) Spinach N/A 3649442 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified spiol Spinacia oleracea (Spinach) Spinach N/A 3649443 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified spiol Spinacia oleracea (Spinach) Spinach N/A 3649444 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified spiol Spinacia oleracea (Spinach) Spinach N/A 3649445 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false spiol Spinacia oleracea (Spinach) Spinach N/A 3649446 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified spiol Spinacia oleracea (Spinach) Spinach N/A 3649447 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified spiol Spinacia oleracea (Spinach) Spinach N/A 3649448 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified spiol Spinacia oleracea (Spinach) Spinach physical association physical association false false false Fig 1, Ext Tab 1 peta-petb-6 3649440 N/A 3649441 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified spiol Spinacia oleracea (Spinach) Spinach N/A 3649442 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified spiol Spinacia oleracea (Spinach) Spinach N/A 3649443 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified spiol Spinacia oleracea (Spinach) Spinach N/A 3649444 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified spiol Spinacia oleracea (Spinach) Spinach N/A 3649445 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false spiol Spinacia oleracea (Spinach) Spinach N/A 3649446 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified spiol Spinacia oleracea (Spinach) Spinach N/A 3649447 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified spiol Spinacia oleracea (Spinach) Spinach N/A 3649448 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified spiol Spinacia oleracea (Spinach) Spinach physical association physical association false false false Ext Fig 1a psrp5-psrp6-3 3965026 N/A 3965027 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3965028 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3965029 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3965030 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3965031 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3965032 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3965033 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3965034 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3965035 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3965036 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3965037 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3965038 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3965039 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3965040 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3965041 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3965042 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3965043 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3965044 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3965045 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3965046 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3965047 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3965048 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3965049 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3965050 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3965051 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3965052 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3965053 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3965054 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 3965055 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 physical association physical association false false false Fig 1, Fig S2, Supplementary Table S1 psrp5-psrp6-2 3965086 N/A 3965028 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 N/A 3965088 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 N/A 3965027 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 N/A 3965050 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 N/A 3965051 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 N/A 3965052 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 N/A 3965053 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 N/A 3965054 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 N/A 3965030 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 N/A 3965031 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 N/A 3965032 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 N/A 3965033 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 N/A 3965034 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 N/A 3965055 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 N/A 3965035 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 N/A 3965036 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 N/A 3965037 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 N/A 3965038 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 N/A 3965039 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 N/A 3965040 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 N/A 3965041 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 N/A 3965042 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 N/A 3965043 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 N/A 3965044 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 N/A 3965045 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 N/A 3965046 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 N/A 3965047 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 N/A 3965048 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 N/A 3965049 predetermined predetermined participant predetermined structure determination identification by structure determination identification by structure determination structure determination unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro Stoichiometry: 1.0 physical association physical association false false false Fig 1, Fig S1, Table S2 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/ glauser-2004-1 Characterization of ferredoxin:thioredoxin reductase modified by site-directed mutagenesis. in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Glauser DA., Bourquin F., Manieri W., Schurmann P. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species fig 2, fig 3, Table 1 peter.schurmann@unine.ch J. Biol. Chem. (0021-9258) 2004 Only protein-protein interactions imex curation glauser-2004-2 Characterization of ferredoxin:thioredoxin reductase modified by site-directed mutagenesis. in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Glauser DA., Bourquin F., Manieri W., Schurmann P. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species After mixing the purified proteins, the complex formation was analyzed by Gel filtration using Superdex 75 HR column. fig 2, fig 3, Table 1 peter.schurmann@unine.ch J. Biol. Chem. (0021-9258) 2004 Only protein-protein interactions imex curation glauser-2004-4 Characterization of ferredoxin:thioredoxin reductase modified by site-directed mutagenesis. in vitro In vitro bn-page blue native page bn-page predetermined predetermined participant predetermined Glauser DA., Bourquin F., Manieri W., Schurmann P. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species After mixing the purified proteins, the complex formation was analyzed by native-gel eletrophoresis. fig 2, fig 3, Table 1 peter.schurmann@unine.ch J. Biol. Chem. (0021-9258) 2004 Only protein-protein interactions imex curation glauser-2004-3 Characterization of ferredoxin:thioredoxin reductase modified by site-directed mutagenesis. in vitro In vitro ion exchange chrom ion exchange chromatography IEC IEC ion exchange chrom predetermined predetermined participant predetermined Glauser DA., Bourquin F., Manieri W., Schurmann P. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species After mixing the purified proteeins, the complex formation was analyzed by ion exchange chromatography on a FPLC MonoQ HP 5/5 column fig 2, fig 3, Table 1 peter.schurmann@unine.ch J. Biol. Chem. (0021-9258) 2004 Only protein-protein interactions imex curation 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 balmer-2004-1 Thioredoxin links redox to the regulation of fundamental processes of plant mitochondria. in vitro In vitro affinity chrom affinity chromatography technology Affinity purification Affinity purification affinity chrom fingerprinting peptide massfingerprinting fingerprinting Balmer Y., Vensel WH., Tanaka CK., Hurkman WJ., Gelhaye E., Rouhier N., Jacquot JP., Manieri W., Schurmann P., Droux M., Buchanan BB. NDPK - Interactions involving proteins containing InterPro domain IPR001564, Nucleoside diphosphate kinase, core. A mutant form of spinach Trxm which lacked a cystiene residue at position C40 was used in these studies because of its availability and similarity to mitochondrial Trxo. Proc. Natl. Acad. Sci. U.S.A. (0027-8424) 2004 IMEx Only protein-protein interactions imex curation imex curation hirasawa-2004-1 Complex formation between ferredoxin and Synechococcus ferredoxin: nitrate oxidoreductase. 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 Biochim. Biophys. Acta (0006-3002) 2004 Only protein-protein interactions imex curation hirasawa-2004-2 Complex formation between ferredoxin and Synechococcus ferredoxin: nitrate oxidoreductase. 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 Biochim. Biophys. Acta (0006-3002) 2004 Only protein-protein interactions imex curation gruhler-2005-1 Stable isotope labeling of Arabidopsis thaliana cells and quantitative proteomics by mass spectrometry. arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress pull down pull down ms participant Identification by mass spectrometry ms participant Gruhler A., Schulze WX., Matthiesen R., Mann M., Jensen ON. figure 4 jenseno@bmb.sdu.dk Mol. Cell Proteomics (1535-9476) 2005 pandini-1999-1 Interaction of the soluble recombinant PsaD subunit of spinach photosystem I with ferredoxin I. in vitro In vitro crosslink cross-linking study crosslink predetermined predetermined participant predetermined Pandini V., Aliverti A., Zanetti G. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species Cross-linking of purified proteins using 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC). fig 4, fig 8 gzanetti@unimi.it Biochemistry (0006-2960) 1999 pandini-1999-2 Interaction of the soluble recombinant PsaD subunit of spinach photosystem I with ferredoxin I. in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Pandini V., Aliverti A., Zanetti G. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species Cross-linking of purified proteins using 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC). fig 4, fig 8 gzanetti@unimi.it Biochemistry (0006-2960) 1999 motohashi-2001-1 Comprehensive survey of proteins targeted by chloroplast thioredoxin. in vitro In vitro affinity chrom affinity chromatography technology Affinity purification Affinity purification affinity chrom edman degradation edman degradation Motohashi K., Kondoh A., Stumpp MT., Hisabori T. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species A mutant form of thioredoxin m (Trx-m) was utilised in these experiments which lacks the second cysteine residue within the active site. Proc. Natl. Acad. Sci. U.S.A. (0027-8424) 2001 IMEx Motohashi K., Kondoh A., Stumpp MT., Hisabori T., Motohashi K., Kondoh A., Stumpp MT., Hisabori T. Only protein-protein interactions imex curation imex curation motohashi-2001-2 Comprehensive survey of proteins targeted by chloroplast thioredoxin. in vitro In vitro comig non denat gel comigration in non denaturing gel electrophoresis comig non denat gel predetermined predetermined participant predetermined Motohashi K., Kondoh A., Stumpp MT., Hisabori T. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species A mutant form of thioredoxin m (Trx-m) was utilised in these experiments which lacks the second cysteine residue within the active site. Proc. Natl. Acad. Sci. U.S.A. (0027-8424) 2001 IMEx Motohashi K., Kondoh A., Stumpp MT., Hisabori T., Motohashi K., Kondoh A., Stumpp MT., Hisabori T. Only protein-protein interactions imex curation imex curation motohashi-2001-3 Comprehensive survey of proteins targeted by chloroplast thioredoxin. in vitro In vitro enzymatic study enzymatic study predetermined predetermined participant predetermined Motohashi K., Kondoh A., Stumpp MT., Hisabori T. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species A mutant form of thioredoxin m (Trx-m) was utilised in these experiments which lacks the second cysteine residue within the active site. Proc. Natl. Acad. Sci. U.S.A. (0027-8424) 2001 IMEx Motohashi K., Kondoh A., Stumpp MT., Hisabori T., Motohashi K., Kondoh A., Stumpp MT., Hisabori T. Only protein-protein interactions imex curation imex curation gcsh_pea Glycine cleavage system H protein, mitochondrial GDCSH GCDH protein protein pea Pisum sativum (Garden pea) Garden pea MALRMWASSTANALKLSSSSRLHLSPTFSISRCFSNVLDGLKYAPSHEWVKHEGSVATIGITDHAQDHLGEVVFVELPEPGVSVTKGKGFGAVESVKATSDVNSPISGEVIEVNTGLTGKPGLINSSPYEDGWMIKIKPTSPDELESLLGAKEYTKFCEEEDAAH odpa_pea Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial protein protein pea Pisum sativum (Garden pea) Garden pea MALSRLSSSSSSSNGSNLFNPFSAAFTLNRPISSDTTATLTIETSLPFTAHNCDPPSRSVTTSPSELLSFFRTMALMRRMEIAADSLYKANLIRGFCHLYDGQEAVAVGMEAGTTKKDCIITAYRDHCTFLGRGGTLLRVYAELMGRRDGCSKGKGGSMHFYKKDSGFYGGHGIVGAQVPLGCGLAFGQKYLKDESVTFALYGDGAANQGQLFEALNISALWDLPAILVCENNHYGMGTATWRSAKSPAYFKRGDYVPGLKVDGMDALAVKQACKFAKEHALKNGPIILEMDTYRYHGHSMSDPGSTYRTRDEISGVRQERDPIERVRKLLLSHDIATEKELKDTEKEVRKEVDEAIAKAKDSPMPDPSDLFSNVYVKGYGVEAFGVDRKEVRVTLP q9sp13_pea Nucleoside diphosphate kinase ndpk protein protein pea Pisum sativum (Garden pea) Garden pea MASHLCKSASRAARSLLSASFHSQGRAVAAAAAVASIRKVPVFAPNYRRTGSGNGPSSWIAGALALPAAAYMLQDQEVHAAELERTFIAIKPDGVQRGLISEIISRFERKGFKLVGIKVLIPTKQFAQQHYHDLKERPFFNGLCDFLSSGPVIAMVWEGEGVITYGRKLIGATDPQKSAPGTIRGDLAVVVGRNIIHGSDGPETAKDEIKLWFKPEELVSFTSNSEKWIYGDN q9sm62_pea abp44/ivdh protein protein pea Pisum sativum (Garden pea) Garden pea MLRTRINTARSIFSSIFRINSSSYSTSFLFDDTQIQFKESVAQFANENIAPHASKIDHTNYFPQEVNLWKSMGEFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCINQLVRNGSHAQKQKYLPKLISGDHVGALAMSEPNSGSDVVGMKCKADRVDGGYVLNGNKMWCTNGTVAQTLVVYAKTDITAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPDENVLGKEGKGVYVMMSGLDLERLVLSGGPLGIMQACLDVVLPYTRQREQFGHPIGEFQFIQGKVADMFTSLQSSRSYVYSVARDCDNGKVDPKDCAGVILCAAERATQVALQAIQCLGGNGYVNEYPTGCLLRDAKLYEIGAGTSEIRRMIIGRELFKEQ glym_pea Serine hydroxymethyltransferase, mitochondrial Glycine hydroxymethyltransferase Serine methylase protein protein pea Pisum sativum (Garden pea) Garden pea MAMAMALRKLSSSVNKSSRPLFSASSLYYKSSLPDEAVYDKENPRVTWPKQLNSPLEVIDPEIADIIELEKARQWKGLELIPSENFTSLSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDMAETLCQKRALEAFRLDPAKWGVNVQPLSGSPSNFQVYTALLKPHDRIMALDLPHGGHLSHGYQTDTKKISAVSIFFETMPYRLDESTGYIDYDQLEKSATLFRPKLIVAGASAYARLYDYARIRKVCDKQKAVLLADMAHISGLVAAGVIPSPFDYADVVTTTTHKSLRGPRGAMIFFRKGLKEVNKQGKEVFYDYEDKINQAVFPGLQGGPHNHTITGLAVALKQATTPEYRAYQEQVLSNSSKFAKALSEKGYDLVSGGTENHLVLVNLKNKGIDGSRVEKVLELVHIAANKNTVPGDVSAMVPGGIRMGTPALTSRGFVEEDFVKVAEYFDAAVSLALKVKAESKGTKLKDFVEALQTSSYVQSEISKLKHDVEEFAKQFPTIGFEKATMKYNK odpb_pea Pyruvate dehydrogenase E1 component subunit beta, mitochondrial protein protein pea Pisum sativum (Garden pea) Garden pea MLGVIRNKTIRPSFSAFRFFSSAKQMTVRDALNSALDVEMSADSKVFLMGEEVGEYQGAYKVTKGLLEKYGPERVLDTPITEAGFTGIGVGAAYYGLKPVVEFMTFNFSMQAIDHIINSAAKSNYMSAGQISVPIVFRGLNGDAAGVGAQHSHCYASWYGSCPGLKVLVPHSAEDARGLLKAAIRDPDPVVFLENELLYGESFPVSAEVLDSSFWLPIGKAKIEREGKDVTITAFSKMVGFALKAAEILEKEGISAEVINLRSIRPLDRPTINASVRKTNRLVTVEEGFPQHGVGAEICTSVIEESFGYLDATVERIGGADVPMPYAGNLERLVVPHVEDIVRAAKRACHRSVPLAAAA gcst_pea Aminomethyltransferase, mitochondrial Glycine cleavage system T protein GDCST GDCT protein protein pea Pisum sativum (Garden pea) Garden pea MRGGLWQLGQSITRRLANGGDKKAVARRCFATESELKKTVLYDFHVAHGGKMVPFAGWSMPIQYKDSIMDSTLNCRQNGSLFDVSHMCGLSLKGKDVVSFLEKLVIADVAALAHGTGTLTVFTNEKGGAIDDSVITKVTDDHLYLVVNAGCRDKDLAHIEEHMKAFKAKGGDVSWHIHDERSLLALQGPLAAPVLQHLTKEDLSKLYFGEFRVLDINGSQCFLTRTGYTGEDGFEISVPSEHGVELAKALLEKSEGKIRLTGLGARDSLRLEAGLCLYGNDLEQHITPIEAGLTWAIGKRRRAEGGFLGADVILKQLADGPSIRRVGFISSGPPPRSHSEIQDEGGNNIGEVTSGGFSPCLKKNIAIGYVKSGLHKAGTKVKIIIRGKQNEGVVTKMPFVPTKYYKPS gcsp_pea Glycine dehydrogenase (decarboxylating), mitochondrial Glycine decarboxylase Glycine cleavage system P protein GDCSP GDCP Glycine dehydrogenase (aminomethyl-transferring) protein protein pea Pisum sativum (Garden pea) Garden pea MERARRLANRATLKRLLSEAKQNRKTESTSTTTTTPLPFSLSGSSSRYVSSVSNSILRGRGSKPDNNVSRRVGGFLGVGYPSQSRSISVEALKPSDTFPRRHNSATPDEQTKMAESVGFDTLDSLVDATVPKSIRLKEMKFNKFDGGLTEGQMIEHMKDLASKNKVFKSFIGMGYYNTHVPPVILRNIMENPAWYTQYTPYQAEISQGRLESLLNFQTMITDLTGLPMSNASLLDEGTAAAEAMSMCNNIQKGKKKTFIIASNCHPQTIDICQTRADGFELKVVVKDLKDIDYKSGDVCGVLVQYPGTEGEVLDYGEFIKKAHANEVKVVMASDLLALTVLKPPGEFGADIVVGSAQRFGVPMGYGGPHAAFLATSQEYKRMMPGRIIGVSVDSSGKQALRMAMQTREQHIRRDKATSNICTAQALLANMAAMYAVYHGPEGLKAIAQRVHGLAGVFALGLKKLGLEVQDLGFFDTVKVKTSNAKAIADAAIKSEINLRVVDGNTITAAFDETTTLEDVDKLFKVFAGGKPVSFTAASLAPEFQNAIPSGLVRESPYLTHPIFNTYQTEHELLRYIHRLQSKDLSLCHSMIPLGSCTMKLNATTEMMPVTWPSFTDLHPFAPTEQAQGYQEMFNNLGDLLCTITGFDSFSLQPNAGAAGEYAGLMVIRAYHLSRGDHHRNVCIIPASAHGTNPASAAMVGMKIVTIGTDAKGNINIEELKKAAEKHKDNLSAFMVTYPSTHGVYEEGIDDICKIIHDNGGQVYMDGANMNAQVGLTSPGWIGADVCHLNLHKTFCIPHGGGGPGMGPIGVKKHLAPFLPSHPVVPTGGIPAPENPQPLGSISAAPWGSALILPISYTYIAMMGSQGLTDASKIAILNANYMAKRLESYYPVLFRGVNGTVAHEFIIDLRGFKNTAGIEPEDVAKRLMDYGFHGPTMSWPVAGTLMIEPTESESKAELDRFCDALISIRKEIAEVEKGNADVHNNVLKGAPHPPSLLMADAWTKPYSREYAAFPAAWLRGAKFWPTTGRVDNVYGDRNLVCTLLPASQAVEEQAAATA dldh_pea Dihydrolipoyl dehydrogenase, mitochondrial Dihydrolipoamide dehydrogenase Pyruvate dehydrogenase complex E3 subunit Glycine cleavage system L protein LPD protein protein pea Pisum sativum (Garden pea) Garden pea MAMANLARRKGYSLLSSETLRYSFSLRSRAFASGSDENDVVIIGGGPGGYVAAIKAAQLGFKTTCIEKRGALGGTCLNVGCIPSKALLHSSHMYHEAKHSFANHGVKVSNVEIDLAAMMGQKDKAVSNLTRGIEGLFKKNKVTYVKGYGKFVSPSEISVDTIEGENTVVKGKHIIIATGSDVKSLPGVTIDEKKIVSSTGALALSEIPKKLVVIGAGYIGLEMGSVWGRIGSEVTVVEFASEIVPTMDAEIRKQFQRSLEKQGMKFKLKTKVVGVDTSGDGVKLTVEPSAGGEQTIIEADVVLVSAGRTPFTSGLNLDKIGVETDKLGRILVNERFSTNVSGVYAIGDVIPGPMLAHKAEEDGVACVEYLAGKVGHVDYDKVPGVVYTNPEVASVGKTEEQVKETGVEYRVGKFPFMANSRAKAIDNAEGLVKIIAEKETDKILGVHIMAPNAGELIHEAAIALQYDASSEDIARVCHAHPTMSEAIKEAAMATYDKPIHI ndk3_spiol Nucleoside diphosphate kinase 3 Nucleoside diphosphate kinase III protein protein spiol Spinacia oleracea (Spinach) Spinach AEFERTFIAIKPDGVQRGLISEIVARFERKGFSLVAIKVVIPSRPFAQKHYADLKDKPFYVGLVAYWSSGPVVAMVWEGEGVIKYGRKLIGATDPQKSEPGTIRGDLAVVNGRNIIHGSDGPETAKDEIKLWFKPEELVNYTHNAEKWIYGDN hsp7m_pea Heat shock 70 kDa protein, mitochondrial HSP1 protein protein pea Pisum sativum (Garden pea) Garden pea MAATLLRSLQRRNLSSSSVSAFRSLTGSTKTSYATHKLASLTRPFSSRPAGNDVIGIDLGTTNSCVSVMEGKNPKVIENSEGARTTPSVVAFNQKSELLVGTPAKRQAVTNPTNTLFGTKRLIGRRFDDAQTQKEMKMVPYKIVRAPNGDAWVEANGQQYSPSQIGAFVLTKIKETAEAYLGKTISKAVVTVPAYFNDAQRQATKDAGRIAGLDVQRIINEPTAAALSYGMNNKEGLIAVFDLGGGTFDVSILEISNGVFEVKATNGDTFLGGEDFDNALLDFLVSEFKRTESIDLAKDKLALQRLREAAEKAKIELSSTSQTEINLPFISADASGAKHLNITLTRSKFEALVNNLIERTKAPCKSCLKDANISIKDVDEVLLVGGMTRVPKVQQVVSEIFGKSPSKGVNPDEAVAMGAALQGGILRGDVKELLLLDVTPLSLGIETLGGIFTRLISRNTTIPTKKSQVFSTAADNQTQVGIKVLQGEREMAADNKSLGEFDLVGIPPAPRGLPQIEVTFDIDANGIVTVSAKDKSTGKEQQITIRSSGGLSDDEIDKMVKEAELHAQRDQERKALIDIRNSADTSIYSIEKSLAEYREKIPAEVAKEIEDAVSDLRTAMAGENADDIKAKLDAANKAVSKIGQHMSGGSSGGPSEGGSQGGEQAPEAEYEEVKK atpam_pea ATP synthase subunit alpha, mitochondrial ATPA protein protein pea Pisum sativum (Garden pea) Garden pea MEFSVRAAELTTLLESRITNFYTNFQVDEIGRVVSVGDGIARVYGLNEIQAGELVEFASGVKGIALNLENENVGIVVFGSDTSIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGRGALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQMNSRATSESETLYCVYVAIGQKRSTVAQLVQILSEANALEYSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKRSDQTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRVGSAAQLKAMKQVCGSLKLELAQYREVAAFAQFGSDLDAATQALLNRGARLTEVLKQPQYAPLPIEKQILVIYAAVNGFCDRMPLDKIAQYERDILSTIKQELLQSLKGGLTGERKIEPDAFLKEKALSLI gpx4_spiol Probable phospholipid hydroperoxide glutathione peroxidase protein protein spiol Spinacia oleracea (Spinach) Spinach MASDSSAQPKSVHEFVVRDARGNDVDLSIYKGKVLLIVNVASQCGLTNSNYTEMTELYEKYRELGLEILAFPCNQFGNQEPGSNEEVLEFACTRFKAEYPIFDKVDVNGSNAAPIYKFLKSSKGGLFGDGLKWNFTKFLVDKDGNVVDRYAPTTSPKSIEKDVKKLLGIQK cysc_spiol Bifunctional L-3-cyanoalanine synthase/cysteine synthase, mitochondrial CYSC Beta-cyanoalanine synthase Beta-substituted Ala synthase 3-1 CAS CSase C Cysteine synthase C protein protein spiol Spinacia oleracea (Spinach) Spinach MATVSSCLLRRSRTASRIFKTSLRCFSTTSSSAQTVSGSSPFPFTGTNIKTNVSQLIGRTPLVYLSKISEGSGAYIAVKQEMMQPTASVKDRPALAMIEDAEKKGLISPGKTVLIEPTSGNMGISMAFMAAMKGYKMVLTMPSYTSMERRVVMRAFGADLILTDPDKGMGGTVKKANQLLDSTPDGFMLQQFNNPANTQVHFETTGPEIWEDTQGKVDIFVMGIGSGGTVSGVGRYLKSQNPNVKIYGVEPAESNILNGGKPGPHLITGNGVGFKPEILDMDVMDAVLEVKSDDAVKMARQLALQEGLLVGISSGANTIAALDLAKRPENKGKLIVTIHPSFGERYLSSALFKELREEAENMQPVPVE q41368_spiol SVDAC1 SOVF_032670 protein protein spiol Spinacia oleracea (Spinach) Spinach MVKGPGLYSDIGKRARDLLYRDYQSDHKFTLTTYTANGVAITSTGTKKGELFLADVSTKLTNKNITTDVKVDTNSNLFTTITVDEPAPGLKAIFSFRVPDQRSGKVELQYLHEYAGISTSLGLTANPIVNFSGVFGNSTLALGTDLSFDTASGNFTKCNAGLSFTNDDLIASVNVNDKLDILNASYYHIVSPLTNTAVGAELSHSFSSNENTLNIGTQHALDPLTSVKARVNNYGKASALIQHEWRPKSIVTISGEVDTSAIEKSAKLGLALVLKP o50047_spiol HSC70-11 protein protein spiol Spinacia oleracea (Spinach) Spinach MATALRRCLRPEQFRSFPAFKSLAGNASPSLSSPYMAQRLASLVRPFSSRPAGNDVIGIDLGTTNSCVSVMEGKSAKVIENAEGARTTPSVVAFNPKGELLVGTPAKRQAVTNPTNTIFGTKRLIGRVFSDPQTQKEMKMVPYKIVKAPNGDAWVEANGQQYSPSQVGAFVLTKMKETAEAYLGKTVSKAVVTVPAYFNDAQRQATKDAGKIAGLDVQRIINEPTAAALSYGMTNKEGLIAVFDLGGGTFDVSILEISNGVFEVKATNGDTFLGGEDFDNTLLEFLVSEFKKTEGIDLSSDRLALQRLREAAEKAKIELSSTSQTDISLPFISADSSGAKHLNITLSRSKFESLVGNLIERTRAPCKNCLKDAGVSLNEVDEVLLVGGMTRVPKVQEIVQEIFGKSPSKGVNPDEAVAMGAAIQGGILRGDVKDLLLLDVTPLSLGIETLGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVLQGEREMASDNKMLGEFELQGIPPAPRGLPQIEVTFDIDANGIVTVSAKDKATNKEQNITIKSSGGLSEHEIEKMVKEAEIHAQKDQERKSLIDARNTADTTIYSVEKSLGEYREKIPTEIAKEIEDAVSDLRSAMQNDNLEEIKAKTDAANKAVSKIGEHMSGGQGGGSSSSGGADQTPEAEYEEAKK gcst_soltu Aminomethyltransferase, mitochondrial Glycine cleavage system T protein GDCST protein protein soltu Solanum tuberosum (Potato) Potato MRGGLWQLGQSITRRLAQADKKTIGRRCFASDADLKKTVLYDFHVVNGGKMVPFAGWSMPIQYKDSIMDSTVNCRENGSLFDVSHMCGLSLKGKDTIPFLEKLVIADVAGLAPGTGSLTVFTNEKGGAIDDSVVTKVTNDHIYLVVNAGCRDKDLAHIEEHMKSFKSKGGDVSWHIHDERSLLALQGPLAAPVLQYLTKDDLSKMYFGEFRVLDINGAPCFLTRTGYTGEDGFEISVPSENALDLAKALLEKSEGKIRLTGLGARDSLRLEAGLCLYGNDMEQHTTPVEAGLTWAIGKRRRAEGGFLGAEVILKQIEEGPKIRRVGFFSSGPPPRSHSEIQDSNGQNIGEITSGGFSPCLKKNIAMGYVKTGNHKAGTNVKIVIRGKSYDGVVTKMPFVPTKYYKP gcsp_soltu Glycine dehydrogenase (decarboxylating), mitochondrial Glycine decarboxylase Glycine cleavage system P protein GDCSP Glycine dehydrogenase (aminomethyl-transferring) protein protein soltu Solanum tuberosum (Potato) Potato MERARKLANRAILKRLVSQSKQSRSNEIPSSSLYRPSRYVSSLSPYTFQARNNAKSFNTQQARSISVEALKPSDTFPRRHNSATPEEQTKMAEFCGFQSLDALIDATVPQSIRSESMKLPKFDSGLTESQMIEHMQNLASKNKVFKSYIGMGYYNTYVPPVILRNLLENPAWYTQYTPYQAEISQGRLESLLNYQTMITDLTGLPMSNASLLDEGTAAAEAMAMCNNILKGKKKTFLIASNCHPQTIDICKTRADGFDLKVVTVDLKDIDYKSGDVCGVLVQYPGTEGEILDYGEFIKNAHAHGVKVVMASDLLALTMLKPPGELGADIVVGSAQRFGVPMGYGGPHAAFLATSQEYKRMMPGRIIGLSVDSTGKPALRMAMQTREQHIRRDKATSNICTAQALLANMAAMYAVYHGPEGLKTIGQRVHGLAGTFSAGLKKLGTVEVQDLPFFDTVKVKCSDAKAIADVANKNDINLRIVDNNTITVSFDETTTLEDVDDLFKVFALGKPVPFTAQSIAQEVENLIPSGLTRETPFLTHQIFNSYHTEHELLRYLHKLQSKDLSLCHSMIPLGSCTMKLNATTEMMPVTWPSFANIHPFAPTEQAAGYQEMFDDLGALLCTITGFDSFSLQPNAGAAGEYAGLMVIRAYHMSRGDHHRNVCIIPVSAHGTNPASAAMCGMKIVAVGTDAKGNINIEELRKAAEANKDNLAALMVTYPSTHGVYEEGIDEICKIIHDNGGQVYMDGANMNAQVGLTSPGFIGADVCHLNLHKTFCIPHGGGGPGMGPIGVKKHLAPYLPSHPVVPTGGIPSPDKSEPLGAISAAPWGSALILPISYTYIAMMGSKGLTDASKIAILSANYMAKRLEKHYPVLFRGVNGTCAHEFIIDLRGFKNTAGIEPEDVAKRLIDYGFHGPTMSWPVPGTLMIEPTESESKAELDRFCDALISIREEIAQIEKGNVDINNNVLKGAPHPPSMLMADAWTKPYSREYAAYPAPWLRSAKFWPTTGRVDNVYGDRNLICTLLPVSEMAEEKAATA hsp7m_soltu Heat shock 70 kDa protein, mitochondrial HSP68 protein protein soltu Solanum tuberosum (Potato) Potato MATAALLRSLRRREFATSSISAYRTLASNTKPSWCPSLVGAKWAGLARPFSSKPAGNEIIGIDLGTTNSCVAVMEGKNPKVIENSEGARTTPSVVAFNQKGELLVGTPAKRQAVTNPTNTLSGTKRLIGRRFDDPQTQKEMKMVPYKIVRGSNGDAWVEANGQQYSPTQIGAFILTKMKETAEAYLGKSINKAVITVPAYFNDAQRQAIKDAGAIAGLDVQRIINEPTAAALSYGMNSKEGLVAVFDLGGGTFDVSILEISNGVFEVKATNGDTFLGGEDFDNALLEFLVSEFKRTEGIDLSKDKLALQRLREAAEKAKIELSSTSQTDINLPFITADASGAKHLNITLTRSKFETLVNHLIERTRNPCKNCLKDAGVSLKDVDEVLLVGGMTRVPKVQEIVSEIFGKSPSKGVNPDEAVAMGAALQGGILRGDVKELLLLDVTPLARGIETLGGIFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVLQGEREMASDNKLLGEFDLVGIPPAPKGYCPQIEVIFDIDANGMVTVSAKDKATSKEQQITIRSSGGLSEDEIDKMVREAEMHAQRIKNARHLLISGIVQSTTIYSIEKSLSEYKEKVPKEVVTEIETAISDLRAAMGTENIDDIKAKLDAANKAVSKIGEHMAGGSSGGASGGGGAQGGDQPPEAEYEEVKK glym_soltu Serine hydroxymethyltransferase, mitochondrial Glycine hydroxymethyltransferase Serine methylase protein protein soltu Solanum tuberosum (Potato) Potato MAMAIALRRLSATVDKPVKSLYNGGSLYYMSSLPNEAVYDKEKSGVAWPKQLNAPLEVVDPEIADIIEHEKARQWKGLELIPSENFTSVSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDMAETLCQKRALEAFRLDPAKWGVNVQPLSGSPANFQVYTALLKPHERIMALDLPHGGHLSHGYQTDTKKISAVSIFFETMPYRLDESTGYIDYDQLEKSATLFRPKLIVAGASAYARLYDYDRIRKVCNKQKAILLADMAHISGLVAAGVIPSPFDYADVVTTTTHKSLRGPRGAMIFYRKGVKEVNKQGKEVFYDYEDKINQAVFPGLQGGPHNHTITGLAVALKQATTPEYRAYQEQVLSNSSKFAQALGEKGYELVSGGTDNHLVLVNMKNKGIDGSRVEKVLEAVHIAANKNTVPGDVSAMVPGGIRMGTPALTSRGFLEEDFVKVADFFDAAVKIAVKVKAETQGTKLKDFVATLESSAPIKSEIAKLRHDVEEYAKQFPTIGFEKETMKYKN vdac2_soltu Mitochondrial outer membrane protein porin of 36 kDa Voltage-dependent anion-selective channel protein POM 36 protein protein soltu Solanum tuberosum (Potato) Potato MVKGPGLYSDIGKKARDLLYRDYVSDHKFTVTTYSTTGVAITASGLKKGELFLADVSTQLKNKNITTDVKVDTNSNVYTTITVDEPAPGLKTIFSFVVPDQKSGKVELQYLHEYAGINTSIGLTASPLVNFSGVAGNNTVALGTDLSFDTATGNFTKCNAGLSFSSSDLIASLALNDKGDTVSASYYHTVKPVTNTAVGAELTHSFSSNENTLTIGTQHLLDPLTTVKARVNSYGKASALIQHEWRPKSLFTISGEVDTRAIEKSAKIGLAVALKP vdac1_soltu Mitochondrial outer membrane protein porin of 34 kDa Voltage-dependent anion-selective channel protein POM 34 protein protein soltu Solanum tuberosum (Potato) Potato MGKGPGLYTEIGKKARDLLYKDYQSDHKFSITTYSPTGVVITSSGSKKGDLFLADVNTQLKNKNVTTDIKVDTNSNLFTTITVDEAAPGLKTILSFRVPDQRSGKLEVQYLHDYAGICTSVGLTANPIVNFSGVVGTNIIALGTDVSFDTKTGDFTKCNAGLSFTNADLVASLNLNNKGDNLTASYYHTVSPLTSTAVGAEVNHSFSTNENIITVGTQHRLDPLTSVKARINNFGKASALLQHEWRPKSLFTVSGEVDTKSVDKGAKFGLALALKP ivd_soltu Isovaleryl-CoA dehydrogenase, mitochondrial IVD IVD2 Isovaleryl-CoA dehydrogenase 2 PGSC0003DMG400008113 protein protein soltu Solanum tuberosum (Potato) Potato MHKLFVARSVKSALFRIKNHQKPQFAAFSTSLLFDDTQKQFKESVAQFAQENIAPHAEKIDRTNYFPQDVNLWKLMGNFNLLGITVPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHTNLCINQLVRNGTHEQKQKYLPKLISGEHVGALAMSEPNAGSDVVSMKCKADRVEGGYVLNGNKMWCTNGPTAQTLVVYAKTDVTAGSKGITAFIIEKGMTGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQVGRGVYVLMSGLDLERLVLASGPVGIMQACLDVVLPYVKQREQFGRPIGEFQFVQGKVADMYTSMQSSRSYLYSVARECDSGTINTKDCAGVILSAAERATQVALQAIQCLGGNGYVNEYPTGRFLRDAKLYEIGAGTSEIRRMIIGRELFKEQ q9fen7_soltu Dihydrolipoyl dehydrogenase lpd2 protein protein soltu Solanum tuberosum (Potato) Potato MAISTLARRKATTFLSSRLLYSTSKYSFSLTRGFASGSDENDVVVIGGGPGGYVAAIKAAQLGLKTTCIEKRGTLGGTCLNVGCIPSKALLHSSHMFHEAQHSFANHGVKFSSVEVDLPAMMGQKDKAVSNLTRGIEGLFKKNKVNYVKGYGKFLSPSEISVDTVEGGNSVVKGKNIIIATGSDVKGLPGITIDEKKIVSSTGALALTEIPKRLVVIGAGYIGLEMGSVWGRLGSEVTVVEFASDIVPTMDGEVRKQFQRALEKQKMKFMLNTKVVSVDATGDGVKLTLEPSAGGDQTILEADVVLVSAGRVPFTSGLGLDTIGVETDKAGRILVNERFATNVPGVHAIGDVIPGPMLAHKAEEDGVACVEFIAGKEGHVDYDMVPGVVYTHPEVAYVGKTEEQVKSLGVDYRVGKFPFLANSRAKAIDDAEGIVKVIAEKESDKILGVHIMSPNAGELIHEAVLALQYGASSEDIARTCHAHPTMSEALKEAAMATYDKPIHM q8l5a6_soltu Malate dehydrogenase mMDH protein protein soltu Solanum tuberosum (Potato) Potato MLKSIVRRSSTAGASYVSRRGFASGSAPERKVAVLGAAGGIGQPLSLLMKLNPLVSSLSLYDIAGTPGVAADVSHINTRSEVVGFAGEEQLGKALEGADIVIIPAGVPRKPGMTRDDLFNINAGIVKSLCTAIAKYCPNALVNMISNPVNSTVPIAAEVFKKAGTYDEKKLFGVTMLDVVRAKTFYAGKAKVNVAEVNLPVVGGHAGITILPLFSQATPKANLSNEEIVALTKRTQDGGTEVVEAKAGKGSATLSMAYAGAIFADACLKGLNGVPDVVECAFVQSNVTELPFFASKVRLGKNGVEEVLGLGPLNEYEKQGLEALKPELLSSIEKGIKFAKEN fdh_soltu Formate dehydrogenase, mitochondrial NAD-dependent formate dehydrogenase FDH1 protein protein soltu Solanum tuberosum (Potato) Potato MAMSRVASTAARAITSPSSLVFTRELQASPGPKKIVGVFYKANEYAEMNPNFLGCAENALGIREWLESKGHQYIVTPDKEGPDCELEKHIPDLHVLISTPFHPAYVTAERIKKAKNLQLLLTAGIGSDHVDLKAAAAAGLTVAEVTGSNTVSVAEDELMRILILVRNFLPGHHQVINGEWNVAAIAHRAYDLEGKTVGTVGAGRIGRLLLQRLKPFNCNLLYHDRLKMDSELENQIGAKFEEDLDKMLSKCDIVVINTPLTEKTKGMFDKERIAKLKKGVLIVNNARGAIMDTQAVVDACNSGHIAGYSGDVWYPQPAPKDHPWRYMPNQAMTPHISGTTIDAQLRYAAGTKDMLDRYFKGEDFPAENYIVKDGELAPQYR odpa_soltu Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial protein protein soltu Solanum tuberosum (Potato) Potato MALSTSRAINHIMKPLSAAVCATRRLSSDSTATITVETSLPFTSHNIDPPSRSVETSPKELMTFFKDMTEMRRMEIAADSLYKAKLIRGFCHLYDGQEAVAVGMEAAITKKDCIITAYRDHCIFLGRGGTLVEAFAELMGRRDGCSRGKGGSMHFYKKESGFYGGHGIVGAQVPLGIGLAFAQKYKKEDYVTFAMYGDGAANQGQLFEALNMAALWDLPAILVCENNHYGMGTAEWRAAKSPAYYKRGDYVPGLRVDGMDVFAVKQACTFAKQHALKNGPIILEMDTYRYHGHSMSDPGSTYRTRDEISGVRQERDPVERIRSLILAHNIATEAELKDIEKENRKVVDEAIAKAKESPMPDPSELFTNVYVKGFGVEAYGADRKELRATLP ndus1_soltu NADH dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrial 76 kDa mitochondrial complex I subunit Complex I-76kD NADH-ubiquinone oxidoreductase 76 kDa subunit protein protein soltu Solanum tuberosum (Potato) Potato MGLGLLASRALRSSRIIRNSTRTIVSTPELKNADAAAAAAAADAPSDLPKRHPVGGARVHLPNPEDVIEVFVDGYPVKIPKGMTVLQACEIAGVDIPRFCYHSRLSIAGNCRMCLVEVEKSPKPVASCAMPALPGMKIKTDTPIAKKAREGVMEFLLMNHPLDCPICDQGGECDLQDQSMAFGSDRGRFTEMKRSVVDKNLGPLVKTVMTRCIQCTRCVRFASEVAGVEDLGMLGRGSGEEIGTYVEKLMTSELSGNVIDICPVGALTSKPFAFKARNWELKGTESIDVTDAVGSNIRIDSRGPEVMRVVPRLNEDINEEWISDKTRFFYDGLKRQRLNDPMIRGADGRFQAVSWRDALAIVAEVMHQIKPEEIVGVAGKLSDAESMMALKDLLNKMGSNNIFCEGNGMHPNADLRSGYIMNTSISGLEKADAFLLVGTQPRVEAAMVNARIHKTVKATNAKVGYVGPAADFNYDHEHLGTDPQTLVEIAEGRHPFSSALKNAKNPVIIVGAGVFDRDDKDAVFAAVDTIAKNNNVVRPDWNGLNVLLLNAAQVAALDLGLVPESDKCIESAKFVYLMGADDVNLDKLPDDAFVVYQGHHGDRGVYRANVILPASAFTEKEGIYENTEGCAQITLPAVPTVGDARDDWKIVRALSEVAGVGLPYDSLGAIRSRIKTVAPNLLEVDERQPATFSTSLRPEVSQKVSATPFTPAVENFYMTDAITRASKIMAQCSALLKK mppa_soltu Mitochondrial-processing peptidase subunit alpha Alpha-MPP Ubiquinol-cytochrome-c reductase subunit II Inactive zinc metalloprotease alpha MPP protein protein soltu Solanum tuberosum (Potato) Potato MYRCASSRLSSLKARQGNRVLTRFSSSAAVATKPSGGLFSWITGDTSSSVTPLDFPLNDVKLSPPLPDYVEPAKTQITTLANGLKVASEASVNPAASIGLYVDCGSIYETPASYGATHLLERMAFKSTLNRSHLRIVREIEAIGGNVTASASREHMIYTYDALKTYVPQMVEMLADCVRNPAFLDWEVKEQLEKVKAEISEYSKNPQHLLLEAVHSAGYAGPYGNSLMATEATINRLNSTVLEEFVAENYTAPRMVLAASGVEHEEFLKVAEPLLSDLPKVATIEEPKPVYVGGDYRCQADAEMTHFALAFEVPGGWMSEKESMTLTVLQMLMGGGGSFSAGGPGKGMYSRLYLRVLNQYPQIHAFSAFSSIYNNTGLFGIQGTTSSDFGPQAVDVAVKELIAVANPSEVDQVQLNRAKQATKSAILMNLESRMVASEDIGRQLLTYGERNPVEHFLKAIDAVSAKDIASVVQKLISSPLTMASYGDVLSLPSYDAVSSRFRSK q8h1x5_soltu Allene-oxide cyclase protein protein soltu Solanum tuberosum (Potato) Potato MATVSSASAALRAISSSSYKLPSAFQITSLSQKIQSLKLPNPLISQTHKLTTTSTTASRSFSCKSQNSSTDSTNTEVQELSVYELNERDRGSPAYLRLSQKNVNSLGDLVPFSNKLYTADLKKRIGITAGLCILIKHEEEKKGDRYEAVYSFYFGDYGQIAVQGSYLTYEDSYLAVTGGSGIFAGVSGQVKLQQLIFPFKLFYTFYLKGIPDLPSELLCTAVPPSPTVEPTPEAKACEDGAALKNY cata2_soltu Catalase isozyme 2 CAT2 protein protein soltu Solanum tuberosum (Potato) Potato MDPSKYRPSSAYDTPFLTTNAGGPVYNNVSSLTVGPRGPVLLEDYYLIEKLATFDREKIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGAQTPVICRFSTVVHERGSPESIRDIRGFAVKFYTREGNFDLVGNNVPVFFNRDAKSFPDTIRALKPNPKSHIQENWRILDFFSFLPESLHTFAFFYDDVCLPTDYRHMEGFGVHAYQLINKEGKAHYVKFHWKPTCGVKSMSEEEAIRVGGTNHSHATKDLYDSIAAGNYPEWKLFIQTMDPEDVDKFDFDPLDVTKTWPEDLLPLIPVGRLVLNRNIDNFFAENEQLAFNPGHIVPGIYYSEDKLLQTRIFAYADTQRHRIGPNYMQLPVNAPKCGHHNNHRDGAMNMTHRDEEVDYLPSRFDPCRPAEQYPIPACVLNGRRTNCVIPKENNFKQAGERYRSWESDRQDRYITKWVESLSDPRVTHEIRSIWISYLSQADKSCGQKVASRLTVKPTM cas1_soltu Bifunctional L-3-cyanoalanine synthase/cysteine synthase 1, mitochondrial PCAS-1 protein protein soltu Solanum tuberosum (Potato) Potato MASLLRRRFYSSESSFAQRLRDLPKYLPGTNIKTQVSQLIGKTPLVYLNKVSEGCGAYIAVKQEMMQPTSSIKDRPAFAMINDAEKKGLITPGKTTLIEPTSGNMGISMAFMAAMKGYKMILTMPSYTSLERRVTMRAFGADLVTTDPTKGMGGTIKKAYDLLESTPNAYMLQQFSNPANTQAHFETTGPEIWEDTQGNVDIFVMGIGSGGTVSGVGQYLKSKNPNVKIYGIEPTESNVLNGGNPGPHEITGNGVGFKPDILDMDVMEEVLMVSSEESVNMARELALKEGLMVGISSGANTVAALRLANRPENKGKLIVTIHPSFGERYLSSVLYEDIRKEAQNMQPVSVD maon_soltu NAD-dependent malic enzyme 59 kDa isoform, mitochondrial protein protein soltu Solanum tuberosum (Potato) Potato MWRVARSAASTFRRTRRLSTAISAPCIVHKRGADILHDPWFNKDTGFPMTERDRLGLRGLLPPRVISFEQQYDRFMESFRSLEKNTEGQPDSVVSLAKWRILNRLHDRNETLYYRVLIDNIKDFAPIIYTPTVGLVCQNYSGLFRRPRGMYFSAKDKGEMMSMIFNWPSTQVDMIVLTDGSRILGLGDLGVQGIGIPIGKLDMYVAAAGINPQRVLPVMLDVGTNNQKLLEDPLYLGLRQPRLEGEEYLSIVDEFVEAVHARWPKAVVQFEDFQAKWAFETLDRYRKKFCMFNDDIQGTAGVALAGLLGTVRAQGRPLTDFANQKIVVVGAGSAGLGVLKMALQAVSRMTGPSADPHFFLLDKNGLITKDRKDIDPAALPFAKAHHEIEGLGLQEGAGLAEVVKKVKPHVLLGLSGVGGIFHEEVLRAMKESDSVRPAIFAMSNPTNNAECCPVDAFKLAGEDIVFASGSPFANVDLGNGKIGHVNQANNMYLFPGIGLGALLSGARNISDTMLEAAAECLASYMSDDEINRGILYPSIDDIRDITAEVGAAVLRAAVAEDLAEGHGDVGVKELQHMSKEETIEHVRQNMWYPVYGPLVHE fer_syny3 Ferredoxin-1 Ferredoxin I petF fed ssl0020 protein protein syny3 Synechocystis sp. (strain PCC 6803 / Kazusa) MASYTVKLITPDGESSIECSDDTYILDAAEEAGLDLPYSCRAGACSTCAGKITAGSVDQSDQSFLDDDQIEAGYVLTCVAYPTSDCTIETHKEEDLY trxf_spiol Thioredoxin F-type, chloroplastic protein protein spiol Spinacia oleracea (Spinach) Spinach MALHLSLSHQSWTSPAHPITSSDPTRSSVPGTGLSRRVDFLGSCKINGVFVVKRKDRRRMRGGEVRASMEQALGTQEMEAIVGKVTEVNKDTFWPIVKAAGDKPVVLDMFTQWCGPCKAMAPKYEKLAEEYLDVIFLKLDCNQENKTLAKELGIRVVPTFKILKENSVVGEVTGAKYDKLLEAIQAARSS ftrc_syny3 Ferredoxin-thioredoxin reductase, catalytic chain ftrC Ferredoxin-thioredoxin reductase subunit B sll0554 protein protein syny3 Synechocystis sp. (strain PCC 6803 / Kazusa) MTSSDTQNNKTLAAMKNFAEQYAKRTDTYFCSDLSVTAVVIEGLARHKEELGSPLCPCRHYEDKEAEVKNTFWNCPCVPMRERKECHCMLFLTPDNDFAGDAQDIPMETLEEVKASMA trxm_spiol Thioredoxin M-type, chloroplastic protein protein spiol Spinacia oleracea (Spinach) Spinach MAIENCLQLSTSASVGTVAVKSHVHHLQPSSKVNVPTFRGLKRSFPALSSSVSSSSPRQFRYSSVVCKASEAVKEVQDVNDSSWKEFVLESEVPVMVDFWAPWCGPCKLIAPVIDELAKEYSGKIAVYKLNTDEAPGIATQYNIRSIPTVLFFKNGERKESIIGAVPKSTLTDSIEKYLSP psad_spiol Photosystem I reaction center subunit II, chloroplastic Photosystem I 20 kDa subunit psaD protein protein spiol Spinacia oleracea (Spinach) Spinach MAMATQATLFSPSSLSSAKPIDTRLTTSFKQPSAVTFASKPASRHHSIRAAAAAEGKAAAATETKEAPKGFTPPELDPNTPSPIFAGSTGGLLRKAQVEEFYVITWESPKEQIFEMPTGGAAIMREGPNLLKLARKEQCLALGTRLRSKYKIKYQFYRVFPSGEVQYLHPKDGVYPEKVNPGRQGVGLNMRSIGKNVSPIEVKFTGKQPYDL fenr_spiol Ferredoxin--NADP reductase, chloroplastic PETH protein protein spiol Spinacia oleracea (Spinach) Spinach MTTAVTAAVSFPSTKTTSLSARSSSVISPDKISYKKVPLYYRNVSATGKMGPIRAQIASDVEAPPPAPAKVEKHSKKMEEGITVNKFKPKTPYVGRCLLNTKITGDDAPGETWHMVFSHEGEIPYREGQSVGVIPDGEDKNGKPHKLRLYSIASSALGDFGDAKSVSLCVKRLIYTNDAGETIKGVCSNFLCDLKPGAEVKLTGPVGKEMLMPKDPNATIIMLGTGTGIAPFRSFLWKMFFEKHDDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPDNFRLDFAVSREQTNEKGEKMYIQTRMAQYAVELWEMLKKDNTYFYMCGLKGMEKGIDDIMVSLAAAEGIDWIEYKRQLKKAEQWNVEVY fer1_spiol Ferredoxin-1, chloroplastic Ferredoxin I PETF protein protein spiol Spinacia oleracea (Spinach) Spinach MAATTTTMMGMATTFVPKPQAPPMMAALPSNTGRSLFGLKTGSRGGRMTMAAYKVTLVTPTGNVEFQCPDDVYILDAAEEEGIDLPYSCRAGSCSSCAGKLKTGSLNQDDQSFLDDDQIDEGWVLTCAAYPVSDVTIETHKEEELTA cyc_horse Cytochrome c CYCS CYC protein protein horse Equus caballus (Horse) Horse MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWKEETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE narb_syne7 Nitrate reductase narB Synpcc7942_1235 protein protein syne7 Synechococcus elongatus (strain PCC 7942) Anacystis nidulans R2 MFDLSKFLPVITPLMIDTAKTLCPYCGVGCGLEAVPPAQPGRATVRDREGTPIWQIRGDRQHPSSQGMVCVKGATVAESVSKSRLKYPMFRASLDDPFTEISWDEALDRLCDRIQQTQADYGKDGICFYGSGQFQTEDYYIAQKLVKGCLGTNNFDTNSRLCMSSAVSAYSLCLGSDGPPACYEDLDLADCLLIVGSNTAECHPILFNRYRKRHKQGGTNLIVVDPRCTPTAEVADLHLALKPGSDVALLNGLGWLLYQMGYVKKDFIANQTEGFEDWLAIIEDYPPQRTAELTGLAVAELVRAADLIASAQRWLSLWSMGVNQSIQGTAKATSLINLHLLTRQIGLPGCGPFSLTGQPNAMGGRETGGLAHLLPGYRKVIDPQHRADVETIWGLPMGSISPQPGRTAWQMIEGLEQGAVGFLWVAATNPAVSLPDVKRAQAALKRSPFTVLQDAYHPTETTTYAHLLLPAAQWSEKTGTMTNSERRVTLCQAFRQPPGEARADWQIFAEVGRRLGFAFDYTDAAAVFAEYVQVTAGRLCDLSGLSHELLAQAGPQQWPFPAGAEPTTESKRLYTKHHFAYADGRARFQPFHHLGVAEPPDDRYPLVLTVGRLYGHWHTQTRTGRIDKINKLHPSAFVEIHPRDADRYNISEGQAVVIRSRRGEGCFPAKVTTAISPGVLFVPMHWGALWGDRTEANALTHPAACPISGEPELKACAVQIEAASSTFTI fer1_nosso Ferredoxin-1 Ferredoxin I petF fdxV protein protein anaso Anabaena sp. (strain PCC 7119) MATFKVTLINEAEGTKHEIEVPDDEYILDAAEEQGYDLPFSCRAGACSTCAGKLVSGTVDQSDQSFLDDDQIEAGYVLTCVAYPTSDVVIQTHKEEDLY nia_spiol Nitrate reductase [NADH] NIA protein protein spiol Spinacia oleracea (Spinach) Spinach MAASVDRQYHPAPMSGVVRTPFSNHHRSDSPVRNGYTFSNPPSSNGVVKPGEKIKLVDNNSNSNNGSNNNNNRYDSDSEEDDDENEMNVWNEMIKKGNSELEPSSVDSRDEGTADQWIERNPSMIRLTGKHPFNSEPPLTRLMHHGFLTPVPLHYVRNHGPVPNAKWEDWTVEVTGLVKRPIRFTMDQLVNDFQSREFPVTLVCAGNRRKEQNMTKQSIGFNWGSAAVSTSVWRGVPLRDVLKRCGVMSSLKGALNVCFEGAEDLPGGGGSKYGTSVKREFAMDPARDIILAYMQNGEKLSPDHGYPVRMIIPGFIGGRMVKWLKRIIVTTTESDNYYHYKDNRVLPSHVDAELANSEAWWYKQEYIINELNVNSVITSPCHEEILPINAWTTQRPYTMRGYAYSGGGRKVTRVEVTMDGGDTWDICELDHQERGSKYGKFWCWCFWSLEVEVLDLLGAKEIGVRAWDESLNTQPEKLIWNVMGMMNNCWFRVKTNVCKPHKGEIGIVFEHPTQPGNKSGGWMARERHLEISDSGPTLKRTASTPFMNTTSKMYSMSEVKKHNTADSAWIVVHGNVYNATRFLKDHPGGSDSILINAGTDCTEEFDAIHSDKAKRLLEDFRIGELISTGYTSDSSSPGNSVHGGSVYSGLAGLAPITEAVPLRNVALNPRVKIPCKLIEKVSLSHDVRRFRFGLPSEDQVLGLPVGKHIFLCANVDDKLCMRAYTPSSTIDVVGYFDLVVKVYFKDVHPRFPNGGVMSQHLDSLSLGSIVDVKGPLGHIEYLGKGNFTVHGKPKFAKKLAMISGGTGITPIYQVMQAILKDPEDKTEMHVVYANRTEEDILLREELDKWADEFRDRVKVWYVVEKAEEGWKYDTGFISEKILRDHVPAVGDDVLALTCGPPPMIQFAVQPNLDKMGFDIKEQLLIF 14331_arath 14-3-3-like protein GF14 chi General regulatory factor 1 At4g09000 GRF1 F23J3.30 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MATPGASSARDEFVYMAKLAEQAERYEEMVEFMEKVAKAVDKDELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEESRGNDDHVSLIRDYRSKIETELSDICDGILKLLDTILVPAAASGDSKVFYLKMKGDYHRYLAEFKSGQERKDAAEHTLTAYKAAQDIANSELAPTHPIRLGLALNFSVFYYEILNSPDRACNLAKQAFDEAIAELDTLGEESYKDSTLIMQLLRDNLTLWTSDMQDDVADDIKEAAPAAAKPADEQQS spsa_spiol Sucrose-phosphate synthase UDP-glucose-fructose-phosphate glucosyltransferase SPS1 protein protein spiol Spinacia oleracea (Spinach) Spinach MAGNDWINSYLEAILDVGGQGIDASTGKTSTAPPSLLLRERGHFSPSRYFVEEVISGFDETDLHRSWVRAASTRSPQERNTRLENLCWRIWNLARKKKQIEGEEAQRLAKRHVERERGRREATADMSEDLSEGERGDTVADMLFASESTKGRMRRISSVEMMDNWANTFKEKKLYVVLISLHGLIRGENMELGRDSDTGGQVKYVVELARALGSMPGVYRVDLLTRQVSAPGVDWSYGEPTEMLSSRNSENSTEQLGESSGAYIIRIPFGPKDKYVAKELLWPYIPEFVDGALSHIKQMSKVLGEQIGGGLPVWPASVHGHYADAGDSAALLSGALNVPMVFTGHSLGRDKLDQLLKQGRLSREEVDATYKIMRRIEAEELCLDASEIVITSTRQEIEEQWQLYHGFDLVLERKLRARMRRGVSCHGRFMPRMAKIPPGMEFNHIAPEDADMDTDIDGHKESNANPDPVIWSEIMRFFSNGRKPMILALARPDPKKNLTTLVKAFGECRPLRELANLTLIIGNRDDIDEMSTTSSSVLISILKLIDKYDLYGQVAYPKHHKQSDVPDIYRLAAKTKGVFINPAFIEPFGLTLIEAAAYGLPIVATKNGGPVDIIGVLDNGLLIDPHDQKSIADALLKLVADKHLWTKCRQNGLKNIHLFSWPEHCKNYLSRIASCKPRQPNWQRIDEGSENSDTDSAGDSLRDIQDISLNLKLSLDAERTEGGNSFDDSLDSEEANAKRKIENAVAKLSKSMDKAQVDVGNLKFPAIRRRKCIFVIALDCDVTSDLLQVIKTVISIVGEQRPTGSIGFILSTSMTLSEVDSLLDSGGLRPADFDAFICNSGSELYYPSTDYSESPFVLDQDYYSHIDYRWGGEGLWKTLVKWAASVNEKKGENAPNIVIADETSSTTHCYAFKVNDFTLAPPAKELRKMMRIQALRCHAIYCQNGTRLNVIPVLASRSQALRYLFMRWGVELSNFVVFVGESGDTDYEGLLGGVHKTVILKGIGSNTSNFHATRAYPMEHVMPVDSPNMFQTGGCNIDDISDALSKIGCLKAQKSL p10871-2 Ribulose bisphosphate carboxylase/oxygenase activase, chloroplastic 41 kDa protein protein spiol Spinacia oleracea (Spinach) Spinach MATAVSTVGAATRAPLNLNGSSAGASVPTSGFLGSSLKKHTNVRFPSSSRTTSMTVKAAENEEKNTDKWAHLAKDFSDDQLDIRRGKGMVDSLFQAPADAGTHVPIQSSFEYESQGLRKYDIDNMLGDFYIAPAFMDKLVVHITKNFLNLPNIKIPLILGVWGGKGQGKSFQCELVFAKLGINPIMMSAGELESGNAGEPAKLIRQRYREAADLIAKGKMCALFINDLEPGAGRMGGTTQYTVNNQMVNATLMNIADNPTNVQLPGMYNKQDNARVPIIVTGNDFSTLYAPLIRDGRMEKFYWAPTREDRIGVCTGIFKTDKVPAEHVVKLVDAFPGQSIDFFGALRARVYHDEVRKWVNSVGVDNVGKKLVNSKDGPPVFEQPEMTLQKLMEYGNMLVQEQENVKRVQLADQYMSSAALGDANKDAIDRGTFFG s17p_spiol Sedoheptulose-1,7-bisphosphatase, chloroplastic SED(1,7)P2ase Sedoheptulose bisphosphatase protein protein spiol Spinacia oleracea (Spinach) Spinach METSMACCSRSIVLPRVSPQHSSALVPSSINLKSLKSSSLFGESLRMTTKSSVRVNKAKNSSLVTKCELGDSLEEFLAKATTDKGLIRLMMCMGEALRTIGFKVRTASCGGTQCVNTFGDEQLAIDVLADKLLFEALNYSHFCKYACSEELPELQDMGGPVDGGFSVAFDPLDGSSIVDTNFSVGTIFGVWPGDKLTGVTGRDQVAAAMGIYGPRTTYVLALKDYPGTHEFLLLDEGKWQHVKETTEINEGKLFCPGNLRATSDNADYAKLIQYYIKEKYTLRYTGGMVPDVNQIIVKEKGIFTNVISPTAKAKLRLLFEVAPLGFLIEKAGGHSSEGTKSVLDIEVKNLDDRTQVAYGSLNEIIRFEKTLYGSSRLEEPVPVGAAA bas1_spiol 2-Cys peroxiredoxin BAS1, chloroplastic Thiol-specific antioxidant protein Thioredoxin-dependent peroxiredoxin BAS1 BAS1 protein protein spiol Spinacia oleracea (Spinach) Spinach MACVASSTTLISSPSSRVFPAKSSLSSPSVSFLRTLSSPSASASLRSGFARRSSLSSTSRRSFAVKAQADDLPLVGNKAPDFEAEAVFDQEFIKVKLSDYIGKKYVILFFYPLDFTFVCPTEITAFSDRHSEFEKLNTEVLGVSVDSVFSHLAWVQTDRKSGGLGDLNYPLISDVTKSISKSFGVLIHDQGIALRGLFIIDKEGVIQHSTINNLGIGRSVDETMRTLQALQYTGNPDEVCPAGWKPGEKSMKPDPKLSKEYFSAI g3pb_spiol Glyceraldehyde-3-phosphate dehydrogenase B, chloroplastic NADP-dependent glyceraldehydephosphate dehydrogenase subunit B GAPB GPB1 protein protein spiol Spinacia oleracea (Spinach) Spinach MASHAALAPSRIPASTRLASKASQQYSFLTQCSFKRLDVADFSGLRSSNSVTFTREASFHDVIAAQLTTKPTGAAPVRGETVAKLKVAINGFGRIGRNFLRCWHGRKDSPLDVVVVNDSGGVKSATHLLKYDSILGTFKADVKIIDNETFSIDGKPIKVVSNRDPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAKGSDIPTYVVGVNEKDYGHDVANIISNASCTTNCLAPFVKVLDEELGIVKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTPNVSVVDLVVNIEKVGVTAEDVNNAFRKAAAGPLKGVLDVCDIPLVSVDFRCSDFSSTIDSSLTMVMGGDMVKVVAWYDNEWGYSQRVVDLADLVANKWPGLEGSVASGDPLEDFCKDNPADEECKLYE prxq_arath Peroxiredoxin Q, chloroplastic Thioredoxin-dependent peroxiredoxin Q MPE11_21 At3g26060 PRXQ Thioredoxin peroxidase protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MAASSSSFTLCNHTTLRTLPLRKTLVTKTQFSVPTKSSESNFFGSTLTHSSYISPVSSSSLKGLIFAKVNKGQAAPDFTLKDQNGKPVSLKKYKGKPVVLYFYPADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDSASHKAFASKYKLPYTLLSDEGNKVRKDWGVPGDLFGALPGRQTYVLDKNGVVQLIYNNQFQPEKHIDETLKFLKAA cp20c_arath Peptidyl-prolyl cis-trans isomerase CYP20-3, chloroplastic Rotamase cyclophilin-4 Cyclophilin of 20 kDa 3 Cyclosporin A-binding protein CYP20-3 At3g62030 F21F14.200 ROC4 Rotamase CYP20-3 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MASSSSMQMVHTSRSIAQIGFGVKSQLVSANRTTQSVCFGARSSGIALSSRLHYASPIKQFSGVYATTKHQRTACVKSMAAEEEEVIEPQAKVTNKVYFDVEIGGEVAGRIVMGLFGEVVPKTVENFRALCTGEKKYGYKGSSFHRIIKDFMIQGGDFTEGNGTGGISIYGAKFEDENFTLKHTGPGILSMANAGPNTNGSQFFICTVKTSWLDNKHVVFGQVIEGMKLVRTLESQETRAFDVPKKGCRIYACGELPLDA tlp20_spiol Peptidyl-prolyl cis-trans isomerase TLP20, chloroplastic Thylakoid lumen PPIase of 20 kDa Thylakoid lumenal 18 kDa protein P18 Rotamase protein protein spiol Spinacia oleracea (Spinach) Spinach SAEETPLQSKVTNKVYFDISIGNPVGKVVIGLFGDDVPQTAENFR rbs2_spiol Ribulose bisphosphate carboxylase small subunit, chloroplastic 2 RBCS2 protein protein spiol Spinacia oleracea (Spinach) Spinach MASSVLSSAAVATVSRTPAQASMVAPFTGLKSTVGFPATKKNDDITSLASNGGRVQCMKVWPTQNMKRYETLSYLPPLTTDQLARQVDYLLNNKWVPCLEFETDHGFVYREHHNSPGYYDGRYWTMWKLPMFGCTDPAQVLNELEECKKEYPNAFIRIIGFDSNRQVQCVSFIAYKPAGY ftrc-petf-1 Titration of FTR by ferredoxin detected by fluorescence 332193 N/A 332197 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) N/A 332198 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) direct interaction direct interaction false false false Titration shows the formation of a 1:1 complex ftrc-trxf-1 Interaction of synechocystis FTR with thioredoxin (Spinach Trx f) studied by fluorescence analysis 332193 N/A 332199 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) N/A 332198 unspecified role unspecified role neutral component neutral component Q55389:p.Cys58Ser mutation increasing mutation increasing interaction mutation increasing certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) direct interaction direct interaction false false false The intermediate complex between FTR and ferredoxin is stablized by using mutants in which one or both non-accessible cysteines participating in the disulfide bridges are modified. ftrc-trxm-1 Interaction of synechocystis FTR with thioredoxin (Spinach Trx m) studied by fluorescence analysis 332193 N/A 332200 unspecified role unspecified role neutral component neutral component P07591:p.Cys107Ser mutation increasing mutation increasing interaction mutation increasing certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) N/A 332198 unspecified role unspecified role neutral component neutral component Q55389:p.His87Tyr 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) direct interaction direct interaction false false false The intermediate complex between FTR and ferredoxin is stablized by using mutants in which one or both non-accessible cysteines participating in the disulfide bridges are modified. The H86Y FTR mutant reacts more slowly with Trx m. ftrc-trxf-2 Synechocystis FTR - thioredoxin (Spinach Trx f) heteroduplex 332194 N/A 332199 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) N/A 332198 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) direct interaction direct interaction false false false ftrc-trxm-3 Synechocysytis ferredoxin-FTR- thioredoxin (Spinach Trx m) triplex 332194 N/A 332197 unspecified role unspecified role neutral component neutral component N/A 332200 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) N/A 332198 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) direct interaction direct interaction false false false ftrc-trxm-4 Synechocysytis FTR- thioredoxin (Spinach Trx m) heteroduplex 332194 N/A 332200 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) N/A 332198 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) direct interaction direct interaction false false false ftrc-trxf-4 Analysis of synechocystis FTR - thioredoxin (Spinach Trx f) heteroduplex by native electrophoresis 332195 N/A 332199 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) N/A 332198 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) direct interaction direct interaction false false false Effect of chemical reductants on the dissociation of FTR-Trx f. Dithionite was the most efficient. DTT also had effect. Meracaptoethanol had only a weak effect. The heteroduplex between FTR and Trx represents a stable intermediate with an oxidized Fe-S cluster. Its reduction dissociate Trx from FTR. ftrc-trxm-2 Analysis of synechocystis FTR - thioredoxin (Spinach Trx m) heteroduplex by native electrophoresis 332195 N/A 332200 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) N/A 332198 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) direct interaction direct interaction false false false Effect of chemical reductants on the dissociation of FTR-Trx m. Dithionite was the most efficient. DTT also had effect. Mercaptoethanol had only a weak effect. The heteroduplex between FTR and Trx represents a stable intermediate with an oxidized Fe-S cluster. Its reduction dissociate Trx from FTR. ftrc-trxf-3 Chromatographic analyzes of synechocystis FTR - thioredoxin (Spinach Trx f) heteroduplex 332196 N/A 332198 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) N/A 332199 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) direct interaction direct interaction false false false 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 trxm-atpam-1 Affinity chromotography reveals interaction between thioredoxin (m-type) (Trxm) and ATP synthase alpha chain, mitochondrial protein 180390 N/A 180391 unspecified role unspecified role prey prey pea Pisum sativum (Garden pea) Garden pea N/A 180392 unspecified role unspecified role prey prey pea Pisum sativum (Garden pea) Garden pea N/A 180393 unspecified role unspecified role prey prey pea Pisum sativum (Garden pea) Garden pea N/A 180394 unspecified role unspecified role prey prey pea Pisum sativum (Garden pea) Garden pea N/A 180395 unspecified role unspecified role prey prey pea Pisum sativum (Garden pea) Garden pea N/A 180396 unspecified role unspecified role prey prey pea Pisum sativum (Garden pea) Garden pea N/A 180397 unspecified role unspecified role prey prey pea Pisum sativum (Garden pea) Garden pea N/A 180398 unspecified role unspecified role prey prey pea Pisum sativum (Garden pea) Garden pea N/A 180399 unspecified role unspecified role prey prey pea Pisum sativum (Garden pea) Garden pea N/A 180400 unspecified role unspecified role prey prey pea Pisum sativum (Garden pea) Garden pea N/A 180401 unspecified role unspecified role prey prey pea Pisum sativum (Garden pea) Garden pea N/A 332200 unspecified role unspecified role bait bait P07591:p.Cys107Ala mutation mutation certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) association association false false false Table 1 trxm-cs-1 Affinity chromotography reveals interaction between thioredoxin (m-type) (Trxm) and a cysteine synthase protein 180390 N/A 180403 unspecified role unspecified role prey prey spiol Spinacia oleracea (Spinach) Spinach N/A 180404 unspecified role unspecified role prey prey spiol Spinacia oleracea (Spinach) Spinach N/A 180405 unspecified role unspecified role prey prey spiol Spinacia oleracea (Spinach) Spinach N/A 332200 unspecified role unspecified role bait bait P07591:p.Cys107Ala mutation mutation certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) N/A 180406 unspecified role unspecified role prey prey spiol Spinacia oleracea (Spinach) Spinach N/A 180407 unspecified role unspecified role prey prey spiol Spinacia oleracea (Spinach) Spinach association association false false false Table 1 trxm-aoc-1 Affinity chromotography reveals interaction between thioredoxin (m-type) (Trxm) and allene oxide cyclase protein 180390 N/A 180408 unspecified role unspecified role prey prey soltu Solanum tuberosum (Potato) Potato N/A 180409 unspecified role unspecified role prey prey soltu Solanum tuberosum (Potato) Potato N/A 180410 unspecified role unspecified role prey prey soltu Solanum tuberosum (Potato) Potato N/A 180411 unspecified role unspecified role prey prey soltu Solanum tuberosum (Potato) Potato N/A 180412 unspecified role unspecified role prey prey soltu Solanum tuberosum (Potato) Potato N/A 180413 unspecified role unspecified role prey prey soltu Solanum tuberosum (Potato) Potato N/A 180414 unspecified role unspecified role prey prey soltu Solanum tuberosum (Potato) Potato N/A 180415 unspecified role unspecified role prey prey soltu Solanum tuberosum (Potato) Potato N/A 180416 unspecified role unspecified role prey prey soltu Solanum tuberosum (Potato) Potato N/A 180417 unspecified role unspecified role prey prey soltu Solanum tuberosum (Potato) Potato N/A 180418 unspecified role unspecified role prey prey soltu Solanum tuberosum (Potato) Potato N/A 180419 unspecified role unspecified role prey prey soltu Solanum tuberosum (Potato) Potato N/A 180420 unspecified role unspecified role prey prey soltu Solanum tuberosum (Potato) Potato N/A 180421 unspecified role unspecified role prey prey soltu Solanum tuberosum (Potato) Potato N/A 180422 unspecified role unspecified role prey prey soltu Solanum tuberosum (Potato) Potato N/A 180423 unspecified role unspecified role prey prey soltu Solanum tuberosum (Potato) Potato N/A 332200 unspecified role unspecified role bait bait P07591:p.Cys107Ala mutation mutation certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) N/A 180424 unspecified role unspecified role prey prey soltu Solanum tuberosum (Potato) Potato association association false false false Table 1 narb-fer1-2 Synechococcus nitrate reductase interaction with spinach ferredoxin detected by activity measurment 367058 N/A 367060 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 false ecoli Escherichia coli (strain K12) N/A 332348 electron donor electron donor unspecified role unspecified role direct interaction direct interaction false false false 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 Synechococcus nitrate reductase interaction with anabaena ferredoxin detected by activity measurment 367058 N/A 367060 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 false ecoli Escherichia coli (strain K12) N/A 367062 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 false P0A3C8:p.Glu95Lys mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain false P0A3C8:p.Glu95_Glu96delinsLysLys mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain false direct interaction direct interaction false false false P39458 purified P0A3C8 purified narb-fer1-1 Synechococcus nitrate reductase interaction with ferredoxin detected by cirular dichroism 367059 N/A 332348 unspecified role unspecified role neutral component neutral component Stoichiometry: 1.0 N/A 367060 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 false ecoli Escherichia coli (strain K12) Stoichiometry: 1.0 direct interaction direct interaction false false false Authors mention spinach ferredoxin without specifying if they refer to the ferredoxin1(P00221) or the ferredoxin 2(P00224). P39458 purified P00221 purified Treatment of NarB with arginine-modifying reagent, reducing the positive charges of its accessible arginines, strongly affect its aggregation with the negatively charged ferredoxin. nia1-grf1 336797 N/A 336798 unspecified role unspecified role prey prey N/A 336799 unspecified role unspecified role bait bait region synthetic phosphopeptide of this sequence was used for pull-down experiment sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false region phosphorylation required for binding opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations certain certain sequence position certain certain certain sequence position certain false physical association physical association false false false Sequence coverage of 14-3-3 protein not sufficient to distinguish between different isoforms sps1-grf1 336797 N/A 336798 unspecified role unspecified role prey prey N/A 336800 unspecified role unspecified role bait bait region synthetic phosphopeptide used for pull-down sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false region phosphorylation required for binding opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations certain certain sequence position certain certain certain sequence position certain false physical association physical association false false false Sequence coverage of 14-3-3 protein not sufficient to distinguish between different isoforms psad-petf-1 Cross-linking of Spinach PsaD and Ferredoxin 332284 N/A 332348 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) N/A 332287 unspecified role unspecified role neutral component neutral component extension tag tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range false ecoli Escherichia coli (strain K12) physical association physical association false false false The psaD was expressed in E. coli with a 14 amino-acids extension at the N-terminus to avoid proteolysis . peth-petft-1 Cross-linking of Spinach ferredoxin and FNR 332284 N/A 332348 unspecified role unspecified role neutral component neutral component N/A 332349 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) physical association physical association false false false The psaD was expressed in E. coli with a 14 amino-acids extension at the N-terminus to avoid proteolysis . psad-petf-2 Study Spinach PsaD interaction with Ferredoxin by fluorescence spectroscopy 332285 N/A 332287 unspecified role unspecified role neutral component neutral component extension tag tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range false ecoli Escherichia coli (strain K12) N/A 332348 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) physical association physical association false false false The psaD was expressed in E. coli with a 14 amino-acids extension at the N-terminus to avoid proteolysis . Electrostatic interactions may be involved in stabilizing the complex PsaD and Fd because the increase of the medium ionic strength highly promoted complex dissociation high ionic strength. trxm-atpam-2 Affinity chromotography reveals interaction between thioredoxin (m-type) (Trxm) and the ATP synthase alpha chain, mitochondrial protein 180056 N/A 180059 unspecified role unspecified role prey prey spiol Spinacia oleracea (Spinach) Spinach N/A 332200 unspecified role unspecified role bait bait p.Cys107Ser Cysteine to serine subsititution at postion 41within the active site mutation mutation certain certain sequence position certain certain certain sequence position certain false ecobb Escherichia coli (strain B / BL21) physical association physical association false false false trxm-gapb-1 Affinity chromotography reveals interaction between thioredoxin (m-type) (Trxm) and glyceraldehyde-3-phosphate dehydrogenase B 180056 N/A 180061 unspecified role unspecified role prey prey spiol Spinacia oleracea (Spinach) Spinach N/A 332200 unspecified role unspecified role bait bait P07591:p.Cys107Ser Cysteine to serine subsititution at postion 41within the active site mutation mutation certain certain sequence position certain certain certain sequence position certain false ecobb Escherichia coli (strain B / BL21) physical association physical association false false false trxm-s17p-1 Affinity chromotography reveals interaction between thioredoxin (m-type) (Trxm) and sedoheptulose-1,7-bisphosphatase 180056 N/A 180062 unspecified role unspecified role prey prey spiol Spinacia oleracea (Spinach) Spinach N/A 332200 unspecified role unspecified role bait bait P07591:p.Cys107Ser Cysteine to serine subsititution at postion 41within the active site mutation mutation certain certain sequence position certain certain certain sequence position certain false ecobb Escherichia coli (strain B / BL21) physical association physical association false false false trxm-bas1-1 Affinity chromotography reveals interaction between thioredoxin (m-type) (Trxm) and 2-cys peroxiredoxin (BAS1) 180056 N/A 180063 unspecified role unspecified role prey prey spiol Spinacia oleracea (Spinach) Spinach N/A 332200 unspecified role unspecified role bait bait P07591:p.Cys107Ser Cysteine to serine subsititution at postion 41within the active site mutation mutation certain certain sequence position certain certain certain sequence position certain false ecobb Escherichia coli (strain B / BL21) physical association physical association false false false trxm-tlp20-1 Affinity chromotography reveals interaction between thioredoxin (m-type) (Trxm) and Peptidyl-prolyl cis-trans isomerase (TLP20) 180056 N/A 332200 unspecified role unspecified role bait bait P07591:p.Cys107Ser Cysteine to serine subsititution at postion 41within the active site mutation mutation certain certain sequence position certain certain certain sequence position certain false ecobb Escherichia coli (strain B / BL21) N/A 180064 unspecified role unspecified role prey prey spiol Spinacia oleracea (Spinach) Spinach physical association physical association false false false trxm-rbs2-1 Affinity chromotography reveals interaction between thioredoxin (m-type) (Trxm) and ribulose bisphosphate carboxylase small chain 2 180056 N/A 180065 unspecified role unspecified role prey prey spiol Spinacia oleracea (Spinach) Spinach N/A 332200 unspecified role unspecified role bait bait P07591:p.Cys107Ser Cysteine to serine subsititution at postion 41within the active site mutation mutation certain certain sequence position certain certain certain sequence position certain false ecobb Escherichia coli (strain B / BL21) physical association physical association false false false trxm-prxq-2 In vitro reduction of 2-Cys-type peridoxin (Prx) by thioredoxin (m-type) (Trxm). 180057 N/A 180066 unspecified role unspecified role neutral component neutral component ecobb Escherichia coli (strain B / BL21) N/A 332200 unspecified role unspecified role neutral component neutral component ecobb Escherichia coli (strain B / BL21) physical association physical association false false false trxm-cyp-1 In vitro reduction of Cyclophilin (Cpy) by thioredoxin (m-type) (Trxm). 180057 N/A 332200 unspecified role unspecified role neutral component neutral component ecobb Escherichia coli (strain B / BL21) N/A 180067 unspecified role unspecified role neutral component neutral component ecobb Escherichia coli (strain B / BL21) physical association physical association false false false trxm-prxq-1 Reduction of peroxidase acitivity of 2-Cys-type peridoxin (Prx) by thioredoxin (m-type) (Trxm). 180058 N/A 180066 unspecified role unspecified role neutral component neutral component ecobb Escherichia coli (strain B / BL21) N/A 332200 unspecified role unspecified role neutral component neutral component ecobb Escherichia coli (strain B / BL21) physical association physical association false false false