ID FDC1_ARATH Reviewed; 154 AA. AC O23344; Q8LD29; DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 08-MAY-2019, entry version 163. DE RecName: Full=Ferredoxin C 1, chloroplastic {ECO:0000303|PubMed:20966083}; DE Short=AtFdC1 {ECO:0000303|PubMed:20966083}; DE Flags: Precursor; GN Name=FDC1 {ECO:0000303|PubMed:20966083}; GN OrderedLocusNames=At4g14890 {ECO:0000312|Araport:AT4G14890}; GN ORFNames=dl3485w {ECO:0000312|EMBL:CAB10268.1}, GN FCAALL.7 {ECO:0000312|EMBL:CAB78531.1}; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., RA Langham S.-A., McCullagh B., Bilham L., Robben J., RA van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., RA van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., RA Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., RA Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., RA Chen E., Marra M.A., Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis RT thaliana."; RL Nature 402:769-777(1999). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana RT reference genome."; RL Plant J. 89:789-804(2017). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., RA Feldmann K.A.; RT "Full-length cDNA from Arabidopsis thaliana."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP GENE FAMILY. RX PubMed=14684843; DOI=10.1104/pp.103.032755; RA Hanke G.T., Kimata-Ariga Y., Taniguchi I., Hase T.; RT "A post genomic characterization of Arabidopsis ferredoxins."; RL Plant Physiol. 134:255-264(2004). RN [6] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION BY HIGH LIGHT, RP SUBCELLULAR LOCATION, COFACTOR, AND NOMENCLATURE. RC STRAIN=cv. Columbia, and cv. No-0; RX PubMed=20966083; DOI=10.1074/jbc.M110.161562; RA Voss I., Goss T., Murozuka E., Altmann B., McLean K.J., Rigby S.E.J., RA Munro A.W., Scheibe R., Hase T., Hanke G.T.; RT "FdC1, a novel ferredoxin protein capable of alternative electron RT partitioning, increases in conditions of acceptor limitation at RT photosystem I."; RL J. Biol. Chem. 286:50-59(2011). CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer CC electrons in a wide variety of metabolic reactions (Probable). CC Mediates alternative electron partitioning in conditions of CC acceptor limitation at photosystem I. Accepts electrons from CC photosystem I (PSI) and is capable of electron transfer with FNR, CC but cannot support photoreduction of NADP(+) (PubMed:20966083). CC {ECO:0000269|PubMed:20966083, ECO:0000305}. CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00465, CC ECO:0000269|PubMed:20966083}; CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000255|PROSITE- CC ProRule:PRU00465, ECO:0000269|PubMed:20966083}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Redox potential: CC E(0) is -280 mV. {ECO:0000269|PubMed:20966083}; CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast CC {ECO:0000269|PubMed:20966083}. CC -!- INDUCTION: Induced by high light at protein level, but not at CC transcript level. Strongly up-regulated in response to acceptor CC limitation at photosystem I (PSI) in plants lacking of CC photosynthetic [2Fe-2S] ferredoxin (Fd). CC {ECO:0000269|PubMed:20966083}. CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z97337; CAB10268.1; -; Genomic_DNA. DR EMBL; AL161540; CAB78531.1; -; Genomic_DNA. DR EMBL; CP002687; AEE83516.1; -; Genomic_DNA. DR EMBL; AY058112; AAL25529.1; -; mRNA. DR EMBL; AY101536; AAM26657.1; -; mRNA. DR EMBL; AY086239; AAM64315.1; -; mRNA. DR PIR; B71412; B71412. DR RefSeq; NP_193225.1; NM_117575.4. DR SMR; O23344; -. DR STRING; 3702.AT4G14890.1; -. DR PaxDb; O23344; -. DR PRIDE; O23344; -. DR EnsemblPlants; AT4G14890.1; AT4G14890.1; AT4G14890. DR GeneID; 827146; -. DR Gramene; AT4G14890.1; AT4G14890.1; AT4G14890. DR KEGG; ath:AT4G14890; -. DR Araport; AT4G14890; -. DR TAIR; locus:2130424; AT4G14890. DR eggNOG; ENOG410IXJT; Eukaryota. DR eggNOG; COG0633; LUCA. DR HOGENOM; HOG000217152; -. DR InParanoid; O23344; -. DR KO; K02639; -. DR OMA; CHAGVCT; -. DR OrthoDB; 679110at2759; -. DR PhylomeDB; O23344; -. DR PRO; PR:O23344; -. DR Proteomes; UP000006548; Chromosome 4. DR ExpressionAtlas; O23344; baseline and differential. DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:UniProtKB. DR GO; GO:0009055; F:electron transfer activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009644; P:response to high light intensity; IEP:UniProtKB. DR CDD; cd00207; fer2; 1. DR Gene3D; 3.10.20.30; -; 1. DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR012675; Beta-grasp_dom_sf. DR InterPro; IPR010241; Fd_pln. DR Pfam; PF00111; Fer2; 1. DR SUPFAM; SSF54292; SSF54292; 1. DR TIGRFAMs; TIGR02008; fdx_plant; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. PE 1: Evidence at protein level; KW 2Fe-2S; Chloroplast; Complete proteome; Electron transport; Iron; KW Iron-sulfur; Metal-binding; Plastid; Reference proteome; KW Transit peptide; Transport. FT TRANSIT 1 56 Chloroplast. {ECO:0000255}. FT CHAIN 57 154 Ferredoxin C 1, chloroplastic. FT {ECO:0000255}. FT /FTId=PRO_0000443798. FT DOMAIN 57 142 2Fe-2S ferredoxin-type. FT {ECO:0000255|PROSITE-ProRule:PRU00465}. FT METAL 89 89 Iron-sulfur (2Fe-2S). FT {ECO:0000255|PROSITE-ProRule:PRU00465}. FT METAL 94 94 Iron-sulfur (2Fe-2S). FT {ECO:0000255|PROSITE-ProRule:PRU00465}. FT METAL 97 97 Iron-sulfur (2Fe-2S). FT {ECO:0000255|PROSITE-ProRule:PRU00465}. FT METAL 126 126 Iron-sulfur (2Fe-2S). FT {ECO:0000255|PROSITE-ProRule:PRU00465}. FT CONFLICT 15 15 L -> P (in Ref. 4; AAM64315). FT {ECO:0000305}. FT CONFLICT 27 36 PLRNATLSTT -> QVRNTALSTA (in Ref. 4; FT AAM64315). {ECO:0000305}. FT CONFLICT 49 49 I -> V (in Ref. 4; AAM64315). FT {ECO:0000305}. SQ SEQUENCE 154 AA; 16732 MW; 88D7B91916349838 CRC64; MATLPLPTQT STISLPKPYL SNSFSFPLRN ATLSTTTNRR NFLTTGRIIA RAYKVVVEHD GKTTELEVEP DETILSKALD SGLDVPYDCN LGVCMTCPAK LVTGTVDQSG GMLSDDVVER GYTLLCASYP TSDCHIKMIP EEELLSLQLA TAND //