ID   FER2_RAPSA              Reviewed;          98 AA.
AC   P14937;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Ferredoxin, root R-B2;
OS   Raphanus sativus (Radish) (Raphanus raphanistrum var. sativus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Raphanus.
OX   NCBI_TaxID=3726;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=cv. Acantiformis Miyashige; TISSUE=White-root;
RX   PubMed=2760019; DOI=10.1093/oxfordjournals.jbchem.a122714;
RA   Wada K., Onda M., Matsubara H.;
RT   "Amino acid sequences of ferredoxin isoproteins from radish roots.";
RL   J. Biochem. 105:619-625(1989).
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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- MISCELLANEOUS: In radish there are 4 ferredoxins: 2 are root-specific
CC       (R-B1 and R-B2), one is present in both leaves and roots (L-A), and
CC       there is a minor form which is leaf specific (L-B).
CC   -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC       {ECO:0000305}.
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DR   PIR; JX0083; JX0083.
DR   AlphaFoldDB; P14937; -.
DR   SMR; P14937; -.
DR   Proteomes; UP000504610; Unplaced.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; Chloroplast; Direct protein sequencing; Electron transport; Iron;
KW   Iron-sulfur; Metal-binding; Plastid; Reference proteome; Transport.
FT   CHAIN           1..98
FT                   /note="Ferredoxin, root R-B2"
FT                   /id="PRO_0000189359"
FT   DOMAIN          4..95
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         41
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         46
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         49
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         79
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ   SEQUENCE   98 AA;  10735 MW;  D029B678E0F96AF0 CRC64;
     SAVYKVKLIG PEGEENEFEV QDDQFILDAA EEAGVDLPYS CRAGACSTCA GQIVKGQVDQ
     SEGSFLEDDH FEKGFVLTCV AYPQSDCVIH THKETELF