ID   FER_PORPP               Reviewed;          32 AA.
AC   P18821;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Ferredoxin;
DE   Flags: Fragment;
OS   Porphyridium purpureum (Red alga) (Porphyridium cruentum).
OC   Eukaryota; Rhodophyta; Bangiophyceae; Porphyridiales; Porphyridiaceae;
OC   Porphyridium.
OX   NCBI_TaxID=35688;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Andrew P.W., Rogers L.J., Haslett B.G., Boulter D.;
RT   "Comparative properties of ferredoxins from a marine and freshwater species
RT   of Porphyridium.";
RL   Phytochemistry 20:1293-1298(1981).
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   -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC       {ECO:0000305}.
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DR   PIR; JT0017; JT0017.
DR   AlphaFoldDB; P18821; -.
DR   SMR; P18821; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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..>32
FT                   /note="Ferredoxin"
FT                   /id="PRO_0000189355"
FT   DOMAIN          3..>32
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   NON_TER         32
SQ   SEQUENCE   32 AA;  3502 MW;  D5595A4C89EFD69C CRC64;
     ATYKVRLLSE AEGIDVTIDC ADDVYILDAA EE