ID FER_SYNY3 STANDARD; PRT; 96 AA. AC P27320; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Ferredoxin I. GN PETF OR FED OR SLL0011. OS Synechocystis sp. (strain PCC 6803). OC Bacteria; Cyanobacteria; Chroococcales; Synechocystis. OX NCBI_TaxID=1148; RN [1] RP SEQUENCE FROM N.A. 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 SEQUENCE FROM N.A. RX MEDLINE=96127529; PubMed=8590279; 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 [3] RP SEQUENCE FROM N.A. RA Cassier-Chauvat C., Poncelet M., Villoing S., Chauvat F.; RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE. RX MEDLINE=92338182; PubMed=1633177; 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 [5] RP STRUCTURE BY NMR. RX MEDLINE=96062510; PubMed=7578051; 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 -!- MISCELLANEOUS: THE MIDPOINT REDOX POTENTIAL FOR THIS PROTEIN IS CC -412 MV. CC -!- SIMILARITY: BELONGS TO THE 2FE2S PLANT-TYPE FERREDOXIN FAMILY. 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; -. DR EMBL; U38802; AAB72025.1; -. DR EMBL; D64000; BAA10197.1; -. DR PIR; S76345; FEYB6. DR PDB; 1DOX; 08-MAR-96. DR PDB; 1DOY; 08-MAR-96. DR InterPro; IPR006057; 2Fe2S. DR InterPro; IPR006058; 2Fe2S_ferredoxin. DR InterPro; IPR001041; Ferredoxin. DR Pfam; PF00111; fer2; 1. DR PRINTS; PR00159; 2FE2SFRDOXIN. DR PROSITE; PS00197; 2FE2S_FERREDOXIN; 1. KW Electron transport; Metal-binding; Iron-sulfur; Iron; 2Fe-2S; KW 3D-structure; Complete proteome. FT INIT_MET 0 0 FT METAL 39 39 IRON-SULFUR (2FE-2S). FT METAL 44 44 IRON-SULFUR (2FE-2S). FT METAL 47 47 IRON-SULFUR (2FE-2S). FT METAL 77 77 IRON-SULFUR (2FE-2S). FT DISULFID 18 85 PROBABLE. FT STRAND 6 8 FT STRAND 13 15 FT HELIX 25 31 FT TURN 32 32 FT TURN 50 51 FT STRAND 62 62 FT TURN 76 77 FT STRAND 79 79 FT STRAND 87 88 FT TURN 89 94 SQ SEQUENCE 96 AA; 10232 MW; 73866DD68E369451 CRC64; ASYTVKLITP DGESSIECSD DTYILDAAEE AGLDLPYSCR AGACSTCAGK ITAGSVDQSD QSFLDDDQIE AGYVLTCVAY PTSDCTIETH KEEDLY //