ID FER_SYNY3 Reviewed; 97 AA. AC P27320; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 07-OCT-2020, entry version 151. DE RecName: Full=Ferredoxin-1; DE AltName: Full=Ferredoxin I; GN Name=petF; Synonyms=fed; OrderedLocusNames=ssl0020; OS Synechocystis sp. (strain PCC 6803 / Kazusa). OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis; OC unclassified Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Nakamoto H., Suzuki T.; RT "Cloning, characterization and transcriptional studies of ferredoxin genes RT from the mesophilic cyanobacterium Synechocystis sp. PCC 6803 and the RT thermophilic cyanobacterium Synechococcus vulcanus."; RL Physiol. Plantarum 101:199-205(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9305771; DOI=10.1016/s0378-1119(97)00165-0; RA Cassier-Chauvat C., Poncelet M., Chauvat F.; RT "Three insertion sequences from the cyanobacterium Synechocystis PCC6803 RT support the occurrence of horizontal DNA transfer among bacteria."; RL Gene 195:257-266(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27184 / PCC 6803 / N-1; RX PubMed=8590279; DOI=10.1093/dnares/2.4.153; RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., RA Sugiura M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region RT from map positions 64% to 92% of the genome."; RL DNA Res. 2:153-166(1995). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). RN [5] RP PROTEIN SEQUENCE OF 2-97. RX PubMed=1633177; DOI=10.1016/0167-4838(92)90465-p; RA Bottin H., Lagoutte B.; RT "Ferredoxin and flavodoxin from the cyanobacterium Synechocystis sp PCC RT 6803."; RL Biochim. Biophys. Acta 1101:48-56(1992). RN [6] RP PROTEIN SEQUENCE OF 2-15. RX PubMed=9298645; DOI=10.1002/elps.1150180806; RA Sazuka T., Ohara O.; RT "Towards a proteome project of cyanobacterium Synechocystis sp. strain RT PCC6803: linking 130 protein spots with their respective genes."; RL Electrophoresis 18:1252-1258(1997). RN [7] RP STRUCTURE BY NMR. RX PubMed=7578051; DOI=10.1021/bi00044a024; RA Lelong C., Setif P., Bottin H., Andre F., Neumann J.-M.; RT "1H and 15N NMR sequential assignment, secondary structure, and tertiary RT fold of [2Fe-2S] ferredoxin from Synechocystis sp. PCC 6803."; RL Biochemistry 34:14462-14473(1995). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 2-97 IN COMPLEXES WITH FTRC; FTRV RP AND TRX-F, AND SUBUNIT. RX PubMed=17611542; DOI=10.1038/nature05937; RA Dai S., Friemann R., Glauser D.A., Bourquin F., Manieri W., Schurmann P., RA Eklund H.; RT "Structural snapshots along the reaction pathway of ferredoxin-thioredoxin RT reductase."; RL Nature 448:92-96(2007). CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons CC 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 -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Redox potential: CC E(0) is -412 mV.; CC -!- SUBUNIT: Forms a complex with heterodimeric ferredoxin-thioredoxin CC reductase (FTR) and thioredoxin. {ECO:0000269|PubMed:17611542}. CC -!- INTERACTION: CC P27320; Q55389: ftrC; NbExp=4; IntAct=EBI-863421, EBI-863211; CC P27320; Q55781: ftrV; NbExp=4; IntAct=EBI-863421, EBI-863219; CC P27320; P19569: psaD; NbExp=3; IntAct=EBI-863421, EBI-595298; 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; D85607; BAA24020.1; -; Genomic_DNA. DR EMBL; U38802; AAB72025.1; -; Genomic_DNA. DR EMBL; BA000022; BAA10197.1; -; Genomic_DNA. DR PIR; S76345; FEYB6. DR PDB; 1DOX; NMR; -; A=2-97. DR PDB; 1DOY; NMR; -; A=2-97. DR PDB; 1OFF; X-ray; 1.80 A; A=2-97. DR PDB; 2KAJ; NMR; -; A=2-97. DR PDB; 2PVG; X-ray; 2.40 A; C=2-97. DR PDB; 2PVO; X-ray; 3.40 A; D=2-97. DR PDB; 5AUK; X-ray; 1.62 A; A=2-97. DR PDBsum; 1DOX; -. DR PDBsum; 1DOY; -. DR PDBsum; 1OFF; -. DR PDBsum; 2KAJ; -. DR PDBsum; 2PVG; -. DR PDBsum; 2PVO; -. DR PDBsum; 5AUK; -. DR BMRB; P27320; -. DR SMR; P27320; -. DR DIP; DIP-35027N; -. DR IntAct; P27320; 7. DR MINT; P27320; -. DR STRING; 1148.1001570; -. DR PaxDb; P27320; -. DR EnsemblBacteria; BAA10197; BAA10197; BAA10197. DR KEGG; syn:ssl0020; -. DR eggNOG; COG1018; Bacteria. DR InParanoid; P27320; -. DR KO; K02639; -. DR OMA; CTIITHQ; -. DR PhylomeDB; P27320; -. DR EvolutionaryTrace; P27320; -. DR Proteomes; UP000001425; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:UniProtKB. DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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; IPR006058; 2Fe2S_fd_BS. 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; PS00197; 2FE2S_FER_1; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. PE 1: Evidence at protein level; KW 2Fe-2S; 3D-structure; Direct protein sequencing; Disulfide bond; KW Electron transport; Iron; Iron-sulfur; Metal-binding; Reference proteome; KW Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:1633177, FT ECO:0000269|PubMed:9298645" FT CHAIN 2..97 FT /note="Ferredoxin-1" FT /id="PRO_0000189381" FT DOMAIN 4..94 FT /note="2Fe-2S ferredoxin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465" FT METAL 40 FT /note="Iron-sulfur (2Fe-2S)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465, FT ECO:0000269|PubMed:7578051" FT METAL 45 FT /note="Iron-sulfur (2Fe-2S)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465, FT ECO:0000269|PubMed:7578051" FT METAL 48 FT /note="Iron-sulfur (2Fe-2S)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465, FT ECO:0000269|PubMed:7578051" FT METAL 78 FT /note="Iron-sulfur (2Fe-2S)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465, FT ECO:0000269|PubMed:7578051" FT DISULFID 19..86 FT /evidence="ECO:0000305" FT CONFLICT 15 FT /note="S -> N (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 3..10 FT /evidence="ECO:0000244|PDB:5AUK" FT STRAND 13..20 FT /evidence="ECO:0000244|PDB:5AUK" FT HELIX 25..32 FT /evidence="ECO:0000244|PDB:5AUK" FT STRAND 39..46 FT /evidence="ECO:0000244|PDB:5AUK" FT STRAND 49..55 FT /evidence="ECO:0000244|PDB:5AUK" FT STRAND 63..66 FT /evidence="ECO:0000244|PDB:1DOX" FT HELIX 67..71 FT /evidence="ECO:0000244|PDB:5AUK" FT STRAND 74..76 FT /evidence="ECO:0000244|PDB:5AUK" FT HELIX 77..79 FT /evidence="ECO:0000244|PDB:5AUK" FT STRAND 81..89 FT /evidence="ECO:0000244|PDB:5AUK" FT HELIX 93..95 FT /evidence="ECO:0000244|PDB:5AUK" SQ SEQUENCE 97 AA; 10363 MW; 137FFD4F87A66DA1 CRC64; MASYTVKLIT PDGESSIECS DDTYILDAAE EAGLDLPYSC RAGACSTCAG KITAGSVDQS DQSFLDDDQI EAGYVLTCVA YPTSDCTIET HKEEDLY //