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 10-APR-2019, entry version 142. 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; OC 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 RT genes from the mesophilic cyanobacterium Synechocystis sp. PCC 6803 RT and the 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 RT PCC6803 support the occurrence of horizontal DNA transfer among RT 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 RT region 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., RA Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., RA Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., RA Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the RT entire 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 RT PCC 6803."; RL Biochim. Biophys. Acta 1101:48-56(1992). RN [6] 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 RT tertiary fold of [2Fe-2S] ferredoxin from Synechocystis sp. PCC RT 6803."; RL Biochemistry 34:14462-14473(1995). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 2-97 IN COMPLEXES WITH FTRC; RP FTRV AND TRX-F, AND SUBUNIT. RX PubMed=17611542; DOI=10.1038/nature05937; RA Dai S., Friemann R., Glauser D.A., Bourquin F., Manieri W., RA Schurmann P., Eklund H.; RT "Structural snapshots along the reaction pathway of ferredoxin- RT thioredoxin reductase."; RL Nature 448:92-96(2007). 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 -!- 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 Q55389:ftrC; NbExp=4; IntAct=EBI-863421, EBI-863211; CC Q55781:ftrV; NbExp=4; IntAct=EBI-863421, EBI-863219; CC 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 ProteinModelPortal; P27320; -. DR SMR; P27320; -. DR DIP; DIP-35027N; -. DR IntAct; P27320; 7. DR MINT; P27320; -. DR STRING; 1148.1001570; -. DR PaxDb; P27320; -. DR PRIDE; P27320; -. DR EnsemblBacteria; BAA10197; BAA10197; BAA10197. DR KEGG; syn:ssl0020; -. DR HOGENOM; HOG000217152; -. DR InParanoid; P27320; -. DR KO; K02639; -. DR OMA; CTIITHQ; -. DR PhylomeDB; P27320; -. DR EvolutionaryTrace; P27320; -. DR Proteomes; UP000001425; Chromosome. 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; Complete proteome; Direct protein sequencing; KW Disulfide bond; Electron transport; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; Transport. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1633177}. FT CHAIN 2 97 Ferredoxin-1. FT /FTId=PRO_0000189381. FT DOMAIN 4 94 2Fe-2S ferredoxin-type. FT {ECO:0000255|PROSITE-ProRule:PRU00465}. FT METAL 40 40 Iron-sulfur (2Fe-2S). FT {ECO:0000255|PROSITE-ProRule:PRU00465, FT ECO:0000269|PubMed:7578051}. FT METAL 45 45 Iron-sulfur (2Fe-2S). FT {ECO:0000255|PROSITE-ProRule:PRU00465, FT ECO:0000269|PubMed:7578051}. FT METAL 48 48 Iron-sulfur (2Fe-2S). FT {ECO:0000255|PROSITE-ProRule:PRU00465, FT ECO:0000269|PubMed:7578051}. FT METAL 78 78 Iron-sulfur (2Fe-2S). FT {ECO:0000255|PROSITE-ProRule:PRU00465, FT ECO:0000269|PubMed:7578051}. FT DISULFID 19 86 {ECO:0000305}. FT STRAND 3 10 {ECO:0000244|PDB:5AUK}. FT STRAND 13 20 {ECO:0000244|PDB:5AUK}. FT HELIX 25 32 {ECO:0000244|PDB:5AUK}. FT STRAND 39 46 {ECO:0000244|PDB:5AUK}. FT STRAND 49 55 {ECO:0000244|PDB:5AUK}. FT STRAND 63 66 {ECO:0000244|PDB:1DOX}. FT HELIX 67 71 {ECO:0000244|PDB:5AUK}. FT STRAND 74 76 {ECO:0000244|PDB:5AUK}. FT HELIX 77 79 {ECO:0000244|PDB:5AUK}. FT STRAND 81 89 {ECO:0000244|PDB:5AUK}. FT HELIX 93 95 {ECO:0000244|PDB:5AUK}. SQ SEQUENCE 97 AA; 10363 MW; 137FFD4F87A66DA1 CRC64; MASYTVKLIT PDGESSIECS DDTYILDAAE EAGLDLPYSC RAGACSTCAG KITAGSVDQS DQSFLDDDQI EAGYVLTCVA YPTSDCTIET HKEEDLY //