ID FER_THEEB Reviewed; 98 AA. AC P0A3C9; P00256; P95742; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 26-NOV-2014, entry version 69. DE RecName: Full=Ferredoxin-1; DE AltName: Full=Ferredoxin I; GN Name=petF1; Synonyms=petF; OrderedLocusNames=tsl1009; OS Thermosynechococcus elongatus (strain BP-1). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Thermosynechococcus. OX NCBI_TaxID=197221; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BP-1; RX PubMed=12240834; DOI=10.1093/dnares/9.4.123; RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., RA Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.; RT "Complete genome structure of the thermophilic cyanobacterium RT Thermosynechococcus elongatus BP-1."; RL DNA Res. 9:123-130(2002). RN [2] RP PROTEIN SEQUENCE OF 2-98. RA Hase T., Matsubara H., Koike H., Katoh S.; RT "Amino acid sequence of ferredoxin from a thermophilic blue-green RT alga, Synechococcus sp."; RL Biochim. Biophys. Acta 744:46-52(1983). RN [3] RP STRUCTURE BY NMR, AND MASS SPECTROMETRY. RX PubMed=8841126; DOI=10.1021/bi961144m; RA Baumann B., Sticht H., Schaerpf M., Sutter M., Haehnel W., Roesch P.; RT "Structure of Synechococcus elongatus [Fe2S2] ferredoxin in RT solution."; RL Biochemistry 35:12831-12841(1996). RN [4] RP STRUCTURE BY NMR. RX PubMed=9180381; DOI=10.1006/jmbi.1997.1001; RA Hatanaka H., Tanimura R., Katoh S., Inagaki F.; RT "Solution structure of ferredoxin from the thermophilic cyanobacterium RT Synechococcus elongatus and its thermostability."; RL J. Mol. Biol. 268:922-933(1997). CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer CC electrons in a wide variety of metabolic reactions. CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; CC Note=Binds 1 [2Fe-2S] cluster.; CC -!- SUBUNIT: Forms a complex with heterodimeric ferredoxin-thioredoxin CC reductase (FTR) and thioredoxin. {ECO:0000250}. CC -!- INTERACTION: CC Q8DLW1:ho1; NbExp=2; IntAct=EBI-766786, EBI-6947306; CC Q8DK70:ispG; NbExp=3; IntAct=EBI-766786, EBI-766800; CC -!- MASS SPECTROMETRY: Mass=10715.7; Method=Electrospray; Range=2-98; CC Evidence={ECO:0000269|PubMed:8841126}; CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU00465}. 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; BA000039; BAC08561.1; -; Genomic_DNA. DR PIR; A00259; FEYCT. DR RefSeq; NP_681799.1; NC_004113.1. DR PDB; 1ROE; NMR; -; A=2-98. DR PDB; 2CJN; NMR; -; A=2-98. DR PDB; 2CJO; NMR; -; A=2-98. DR PDBsum; 1ROE; -. DR PDBsum; 2CJN; -. DR PDBsum; 2CJO; -. DR ProteinModelPortal; P0A3C9; -. DR SMR; P0A3C9; 2-98. DR IntAct; P0A3C9; 4. DR MINT; MINT-7014655; -. DR STRING; 197221.tsl1009; -. DR EnsemblBacteria; BAC08561; BAC08561; BAC08561. DR GeneID; 1011313; -. DR KEGG; tel:tsl1009; -. DR PATRIC; 23927318; VBITheElo119873_1059. DR eggNOG; COG0633; -. DR HOGENOM; HOG000217152; -. DR KO; K02639; -. DR OMA; THKEGEL; -. DR OrthoDB; EOG6GJC0W; -. DR EvolutionaryTrace; P0A3C9; -. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0022900; P:electron transport chain; IEA:InterPro. DR Gene3D; 3.10.20.30; -; 1. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR010241; Fd_pln. DR Pfam; PF00111; Fer2; 1. DR SUPFAM; SSF54292; SSF54292; 1. DR TIGRFAMs; TIGR02008; fdx_plant; 1. DR PROSITE; PS00197; 2FE2S_FER_1; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. PE 1: Evidence at protein level; KW 2Fe-2S; 3D-structure; Complete proteome; Direct protein sequencing; KW Electron transport; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; Transport. FT INIT_MET 1 1 Removed. {ECO:0000269|Ref.2}. FT CHAIN 2 98 Ferredoxin-1. FT /FTId=PRO_0000189372. FT DOMAIN 4 95 2Fe-2S ferredoxin-type. FT {ECO:0000255|PROSITE-ProRule:PRU00465}. FT METAL 41 41 Iron-sulfur (2Fe-2S). FT METAL 46 46 Iron-sulfur (2Fe-2S). FT METAL 49 49 Iron-sulfur (2Fe-2S). FT METAL 79 79 Iron-sulfur (2Fe-2S). FT STRAND 4 7 {ECO:0000244|PDB:2CJN}. FT STRAND 10 13 {ECO:0000244|PDB:1ROE}. FT STRAND 17 20 {ECO:0000244|PDB:2CJN}. FT STRAND 22 24 {ECO:0000244|PDB:1ROE}. FT HELIX 27 32 {ECO:0000244|PDB:1ROE}. FT STRAND 40 45 {ECO:0000244|PDB:2CJN}. FT STRAND 47 49 {ECO:0000244|PDB:1ROE}. FT STRAND 54 57 {ECO:0000244|PDB:1ROE}. FT STRAND 61 65 {ECO:0000244|PDB:2CJN}. FT TURN 68 70 {ECO:0000244|PDB:1ROE}. FT HELIX 71 73 {ECO:0000244|PDB:1ROE}. FT TURN 78 80 {ECO:0000244|PDB:1ROE}. FT STRAND 83 89 {ECO:0000244|PDB:2CJN}. FT HELIX 95 97 {ECO:0000244|PDB:1ROE}. SQ SEQUENCE 98 AA; 10847 MW; DE8198FFB127C7AF CRC64; MATYKVTLVR PDGSETTIDV PEDEYILDVA EEQGLDLPFS CRAGACSTCA GKLLEGEVDQ SDQSFLDDDQ IEKGFVLTCV AYPRSDCKIL TNQEEELY //