ID FER_ARTPT Reviewed; 99 AA. AC P00246; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 22-NOV-2017, entry version 98. DE RecName: Full=Ferredoxin; OS Arthrospira platensis (Spirulina platensis). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Microcoleaceae; Arthrospira. OX NCBI_TaxID=118562; RN [1] RP PROTEIN SEQUENCE OF 2-99. RX 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 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: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; CC Note=Binds 1 [2Fe-2S] cluster.; 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 PIR; A00250; FESGAL. DR PDB; 4FXC; X-ray; 2.50 A; A=2-99. DR PDBsum; 4FXC; -. DR ProteinModelPortal; P00246; -. DR SMR; P00246; -. DR eggNOG; ENOG410811Q; Bacteria. DR eggNOG; COG0633; LUCA. DR EvolutionaryTrace; P00246; -. 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0022900; P:electron transport chain; IEA:InterPro. 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; Electron transport; KW Iron; Iron-sulfur; Metal-binding; Transport. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:817723}. FT CHAIN 2 99 Ferredoxin. FT /FTId=PRO_0000189371. FT DOMAIN 4 96 2Fe-2S ferredoxin-type. FT {ECO:0000255|PROSITE-ProRule:PRU00465}. 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 {ECO:0000244|PDB:4FXC}. FT STRAND 16 20 {ECO:0000244|PDB:4FXC}. FT HELIX 27 33 {ECO:0000244|PDB:4FXC}. FT STRAND 41 46 {ECO:0000244|PDB:4FXC}. FT STRAND 48 60 {ECO:0000244|PDB:4FXC}. FT HELIX 69 73 {ECO:0000244|PDB:4FXC}. FT HELIX 79 81 {ECO:0000244|PDB:4FXC}. FT STRAND 83 93 {ECO:0000244|PDB:4FXC}. FT TURN 95 97 {ECO:0000244|PDB:4FXC}. SQ SEQUENCE 99 AA; 10634 MW; 71F9CA733DB03741 CRC64; MATYKVTLIN EAEGINETID CDDDTYILDA AEEAGLDLPY SCRAGACSTC AGTITSGTID QSDQSFLDDD QIEAGYVLTC VAYPTSDCTI KTHQEEGLY //