ID   FER_PHYAF               Reviewed;          97 AA.
AC   P83524;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Ferredoxin;
OS   Physalis alkekengi var. francheti (Japanese lantern) (Physalis franchetii).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Physaleae;
OC   Alkekengi.
OX   NCBI_TaxID=221454 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, COFACTOR, AND SUBCELLULAR LOCATION.
RC   TISSUE=Leaf;
RX   PubMed=9862138; DOI=10.1016/s0031-9422(98)00331-8;
RA   Mino Y., Yasuda K.;
RT   "Amino acid sequence of ferredoxin from Physalis alkekengi var.
RT   francheti.";
RL   Phytochemistry 49:1631-1636(1998).
CC   -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC       in a wide variety of metabolic reactions. {ECO:0000269|PubMed:9862138}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000269|PubMed:9862138};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:9862138};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:9862138}.
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; P83524; -.
DR   SMR; P83524; -.
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_0000189347"
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;  10363 MW;  E01D664C71EA42B8 CRC64;
     ATYKVKLITP DGPVVFDCPD NEYILDAAEE QGHDLPYSCR AGSCSSCAGK VTAGTVDQSD
     GNFLDDDQVA DGFVLTCVAY PQSDVTIETH KEEELTA