ID   FER_DATIN               Reviewed;          97 AA.
AC   P68163; P83521;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Ferredoxin;
OS   Datura inoxia (Downy thornapple) (Datura meteloides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Datureae; Datura.
OX   NCBI_TaxID=4075;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, COFACTOR, AND SUBCELLULAR LOCATION.
RC   TISSUE=Leaf;
RX   PubMed=7764481; DOI=10.1016/s0031-9422(00)94769-1;
RA   Mino Y.;
RT   "Identical amino acid sequence of ferredoxin from Datura metel and D.
RT   innoxia.";
RL   Phytochemistry 35:385-387(1994).
CC   -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC       in a wide variety of metabolic reactions. {ECO:0000269|PubMed:7764481}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000269|PubMed:7764481};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:7764481};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:7764481}.
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   AlphaFoldDB; P68163; -.
DR   SMR; P68163; -.
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_0000189322"
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;  10484 MW;  A329716ABA834394 CRC64;
     ATYKVKLVTP DGPVEFDCPD DVYILDRAEE EGHDLPYSCR AGSCSSCAGK VTAGTVDQSD
     GNYLDDDQMA EGFVLTCVAY PQSDVTIETH KEEELTG