ID FER_SPIPL Reviewed; 99 AA. AC P00246; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 15-DEC-2009, entry version 66. DE RecName: Full=Ferredoxin; OS Spirulina platensis. OC Bacteria; Cyanobacteria; Oscillatoriales; Arthrospira. OX NCBI_TaxID=118562; RN [1] RP PROTEIN SEQUENCE OF 2-99. RX MEDLINE=76184180; PubMed=817723; DOI=10.1016/0006-291X(76)90940-2; RA Tanaka M., Haniu M., Yasunobu K.T., Rao K.K., Hall D.O.; RT "The complete amino acid sequence of the Spirulina platensis RT ferredoxin."; RL Biochem. Biophys. Res. Commun. 69:759-765(1976). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX MEDLINE=82142259; PubMed=6801028; RA Tsukihara T., Fukuyama K., Nakamura M., Katsube Y., Tanaka N., RA Kakudo M., Wada K., Hase T., Matsubara H.; RT "X-ray analysis of a [2Fe-2S] ferrodoxin from Spirulina platensis. RT Main chain fold and location of side chains at 2.5-A resolution."; RL J. Biochem. 90:1763-1773(1981). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RA Fukuyama K., Hase T., Matsumoto S., Tsukihara T., Katsube Y., RA Tanaka N., Kakudo M., Wada K., Hase T., Matsubara H.; RT "Structure of S. platensis [2Fe-2S] ferredoxin and evolution of RT chloroplast-type ferrodoxins."; RL Nature 286:522-524(1980). 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 -!- 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 PIR; A00250; FESGAL. DR PDB; 4FXC; X-ray; 2.50 A; A=2-98. DR PDBsum; 4FXC; -. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 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 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; Electron transport; KW Iron; Iron-sulfur; Metal-binding; Transport. FT INIT_MET 1 1 Removed. FT CHAIN 2 99 Ferredoxin. FT /FTId=PRO_0000189371. FT DOMAIN 4 96 2Fe-2S ferredoxin-type. FT METAL 42 42 Iron-sulfur (2Fe-2S). FT METAL 47 47 Iron-sulfur (2Fe-2S). FT METAL 50 50 Iron-sulfur (2Fe-2S). FT METAL 80 80 Iron-sulfur (2Fe-2S). FT STRAND 5 9 FT STRAND 16 20 FT HELIX 27 33 FT STRAND 41 46 FT STRAND 48 60 FT HELIX 69 73 FT HELIX 79 81 FT STRAND 83 93 FT TURN 95 97 SQ SEQUENCE 99 AA; 10634 MW; 71F9CA733DB03741 CRC64; MATYKVTLIN EAEGINETID CDDDTYILDA AEEAGLDLPY SCRAGACSTC AGTITSGTID QSDQSFLDDD QIEAGYVLTC VAYPTSDCTI KTHQEEGLY //