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 23-OCT-2007, entry version 65. DE Ferredoxin-1 (Ferredoxin I). GN Name=petF; Synonyms=fed; OrderedLocusNames=ssl0020; OS Synechocystis sp. (strain PCC 6803). OC Bacteria; Cyanobacteria; Chroococcales; Synechocystis. OX NCBI_TaxID=1148; 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 MEDLINE=97449302; 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]. RX MEDLINE=96127529; 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]. RX MEDLINE=97061201; 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 MEDLINE=92338182; 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 MEDLINE=96062510; 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). CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer CC electrons in a wide variety of metabolic reactions. CC -!- COFACTOR: Binds 1 2Fe-2S cluster. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Redox potential: CC E(0) is -412 mV; CC -!- INTERACTION: CC Q55389:ftrC; NbExp=1; IntAct=EBI-863421, EBI-863211; CC P19569:psaD; NbExp=2; IntAct=EBI-863421, EBI-595298; CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family. CC -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain. 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 RefSeq; NP_442127.1; -. DR PDB; 1DOX; NMR; @=1-97. DR PDB; 1DOY; NMR; @=1-97. DR PDB; 1OFF; X-ray; A=1-97. DR IntAct; P27320; -. DR GeneID; 952540; -. DR GenomeReviews; BA000022_GR; ssl0020. DR KEGG; syn:ssl0020; -. DR BioCyc; SSP1148:SSL0020-MONOMER; -. DR LinkHub; P27320; -. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR012675; b-grasp_ferredoxin-like. DR InterPro; IPR010241; Fdx_pln. DR InterPro; IPR001041; Ferredoxin. DR Gene3D; G3DSA:3.10.20.30; Ferredoxin_fold; 1. DR Pfam; PF00111; Fer2; 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; Transport. FT INIT_MET 1 1 Removed. FT CHAIN 2 97 Ferredoxin-1. FT /FTId=PRO_0000189381. FT DOMAIN 4 94 2Fe-2S ferredoxin-type. FT METAL 40 40 Iron-sulfur (2Fe-2S). FT METAL 45 45 Iron-sulfur (2Fe-2S). FT METAL 48 48 Iron-sulfur (2Fe-2S). FT METAL 78 78 Iron-sulfur (2Fe-2S). FT DISULFID 19 86 Probable. FT STRAND 2 8 FT STRAND 13 19 FT HELIX 24 31 FT STRAND 38 45 FT STRAND 48 54 FT HELIX 66 70 FT STRAND 73 75 FT STRAND 80 88 FT HELIX 92 94 SQ SEQUENCE 97 AA; 10363 MW; 137FFD4F87A66DA1 CRC64; MASYTVKLIT PDGESSIECS DDTYILDAAE EAGLDLPYSC RAGACSTCAG KITAGSVDQS DQSFLDDDQI EAGYVLTCVA YPTSDCTIET HKEEDLY //