ID   FER_GUITH               Reviewed;          97 AA.
AC   O78510;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Ferredoxin;
GN   Name=petF;
OS   Guillardia theta (Cryptophyte) (Cryptomonas phi).
OG   Plastid; Chloroplast.
OC   Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX   NCBI_TaxID=55529;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9929392; DOI=10.1007/pl00006462;
RA   Douglas S.E., Penny S.L.;
RT   "The plastid genome of the cryptophyte alga, Guillardia theta: complete
RT   sequence and conserved synteny groups confirm its common ancestry with red
RT   algae.";
RL   J. Mol. Evol. 48:236-244(1999).
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   -!- SUBUNIT: Forms a complex with heterodimeric ferredoxin-thioredoxin
CC       reductase (FTR) and thioredoxin. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
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   EMBL; AF041468; AAC35732.1; -; Genomic_DNA.
DR   RefSeq; NP_050798.1; NC_000926.1.
DR   AlphaFoldDB; O78510; -.
DR   SMR; O78510; -.
DR   GeneID; 857106; -.
DR   HOGENOM; CLU_082632_7_3_1; -.
DR   OMA; CAARMIS; -.
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   3: Inferred from homology;
KW   2Fe-2S; Chloroplast; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW   Plastid; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..97
FT                   /note="Ferredoxin"
FT                   /id="PRO_0000189335"
FT   DOMAIN          4..94
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         40
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         45
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         48
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         78
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ   SEQUENCE   97 AA;  10281 MW;  8C9BAC8DFC58D88D CRC64;
     MATYKVKLSG EGVDKTIDCP DDQYILDAAE EQGIDLPYSC RAGACSTCAG KVAAGSVDQS
     DQSFLDDSQI GDGFVLTCVA YPTSDCTILT HQEEGLY