ID   FER_SCOJA               Reviewed;          97 AA.
AC   P83525;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Ferredoxin;
OS   Scopolia japonica (Japanese belladonna).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Hyoscyameae;
OC   Scopolia.
OX   NCBI_TaxID=221162 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, COFACTOR, AND SUBCELLULAR LOCATION.
RC   TISSUE=Leaf;
RX   PubMed=12392097; DOI=10.1248/bpb.25.1367;
RA   Mino Y.;
RT   "Amino acid sequences of ferredoxins from Scopolia japonica and Lycium
RT   chinense: their similarities to that of Datura arborea.";
RL   Biol. Pharm. Bull. 25:1367-1369(2002).
CC   -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC       in a wide variety of metabolic reactions.
CC       {ECO:0000269|PubMed:12392097}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000269|PubMed:12392097};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:12392097};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:12392097}.
CC   -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P83525; -.
DR   SMR; P83525; -.
DR   GO; GO:0009507; C:chloroplast; TAS:UniProtKB.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB.
DR   GO; GO:0008198; F:ferrous iron binding; TAS:UniProtKB.
DR   GO; GO:0006124; P:ferredoxin metabolic process; TAS:UniProtKB.
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; Chloroplast; Direct protein sequencing; Electron transport; Iron;
KW   Iron-sulfur; Metal-binding; Plastid; Transport.
FT   CHAIN           1..97
FT                   /note="Ferredoxin"
FT                   /id="PRO_0000189364"
FT   DOMAIN          3..93
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         39
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         44
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         47
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         77
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ   SEQUENCE   97 AA;  10438 MW;  58CAAEA60915F79C CRC64;
     ATYKVKLVTP DGPVEFDCPD DVYILDQAEE EGHELPYSCR AGSCSSCAGK VSAGTVDQSD
     GNFLDDDQMA DGFVLTCVAY PQSDVIIETH KEEELTG