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 03-AUG-2022, entry version 107. 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 ferredoxin."; RL Biochem. Biophys. Res. Commun. 69:759-765(1976). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=6801028; DOI=10.1093/oxfordjournals.jbchem.a133654; RA Tsukihara T., Fukuyama K., Nakamura M., Katsube Y., Tanaka N., Kakudo M., RA Wada K., Hase T., Matsubara H.; RT "X-ray analysis of a [2Fe-2S] ferrodoxin from Spirulina platensis. Main RT 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., Tanaka N., RA 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 electrons CC in a wide variety of metabolic reactions. CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; 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 AlphaFoldDB; P00246; -. DR SMR; P00246; -. DR EvolutionaryTrace; P00246; -. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. 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; Direct protein sequencing; Electron transport; Iron; KW Iron-sulfur; Metal-binding; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:817723" FT CHAIN 2..99 FT /note="Ferredoxin" FT /id="PRO_0000189371" FT DOMAIN 4..96 FT /note="2Fe-2S ferredoxin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465" FT BINDING 42 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT BINDING 47 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT BINDING 50 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT BINDING 80 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT STRAND 5..9 FT /evidence="ECO:0007829|PDB:4FXC" FT STRAND 16..20 FT /evidence="ECO:0007829|PDB:4FXC" FT HELIX 27..33 FT /evidence="ECO:0007829|PDB:4FXC" FT STRAND 41..46 FT /evidence="ECO:0007829|PDB:4FXC" FT STRAND 48..60 FT /evidence="ECO:0007829|PDB:4FXC" FT HELIX 69..73 FT /evidence="ECO:0007829|PDB:4FXC" FT HELIX 79..81 FT /evidence="ECO:0007829|PDB:4FXC" FT STRAND 83..93 FT /evidence="ECO:0007829|PDB:4FXC" FT TURN 95..97 FT /evidence="ECO:0007829|PDB:4FXC" SQ SEQUENCE 99 AA; 10634 MW; 71F9CA733DB03741 CRC64; MATYKVTLIN EAEGINETID CDDDTYILDA AEEAGLDLPY SCRAGACSTC AGTITSGTID QSDQSFLDDD QIEAGYVLTC VAYPTSDCTI KTHQEEGLY //