ID   FER1_MAIZE              Reviewed;         150 AA.
AC   P27787;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   24-JAN-2024, entry version 147.
DE   RecName: Full=Ferredoxin-1, chloroplastic {ECO:0000305};
DE   AltName: Full=Ferredoxin I {ECO:0000303|PubMed:16668188};
DE            Short=Fd I {ECO:0000303|PubMed:16668188};
DE   Flags: Precursor;
GN   Name=FDX1 {ECO:0000305}; Synonyms=pFD1 {ECO:0000303|PubMed:16668188};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 53-76.
RX   PubMed=16668188; DOI=10.1104/pp.96.1.77;
RA   Hase T., Kimatsa Y., Yonekura K., Matsumura T., Sakakibara H.;
RT   "Molecular cloning and differential expression of the maize ferredoxin gene
RT   family.";
RL   Plant Physiol. 96:77-83(1991).
RN   [2]
RP   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-117, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=cv. Golden cross Bantam T51;
RX   PubMed=9952443; DOI=10.1104/pp.119.2.481;
RA   Matsumura T., Kimata-Ariga Y., Sakakibara H., Sugiyama T., Murata H.,
RA   Takao T., Shimonishi Y., Hase T.;
RT   "Complementary DNA cloning and characterization of ferredoxin localized in
RT   bundle-sheath cells of maize leaves.";
RL   Plant Physiol. 119:481-488(1999).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX   PubMed=11175898; DOI=10.1038/84097;
RA   Kurisu G., Kusunoki M., Katoh E., Yamazaki T., Teshima K., Onda Y.,
RA   Kimata-Ariga Y., Hase T.;
RT   "Structure of the electron transfer complex between ferredoxin and
RT   ferredoxin-NADP+ reductase.";
RL   Nat. Struct. Biol. 8:117-121(2001).
CC   -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC       in a wide variety of metabolic reactions. Occupies a key position both
CC       for transferring the photoreducing power to Fd-NADP(+) oxidoreductase
CC       (FNR), hence the formation of NADPH, and for mediating the cyclic
CC       electron flow around photosystem I (PSI). {ECO:0000269|PubMed:9952443}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000305};
CC       Note=Binds 1 [2Fe-2S] cluster.;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Redox potential:
CC         E(0) is -423 mV. {ECO:0000269|PubMed:9952443};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:9952443}.
CC   -!- TISSUE SPECIFICITY: Expressed almost exclusively in mesophyll cells.
CC       {ECO:0000269|PubMed:9952443}.
CC   -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC       {ECO:0000305}.
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DR   EMBL; M73829; AAA33459.1; -; mRNA.
DR   EMBL; M73830; AAA33460.1; -; mRNA.
DR   PIR; T03286; T03286.
DR   RefSeq; NP_001105345.1; NM_001111875.1.
DR   PDB; 1GAQ; X-ray; 2.59 A; B=53-150.
DR   PDB; 3B2F; X-ray; 1.70 A; A/B=53-150.
DR   PDB; 3W5U; X-ray; 2.70 A; B/D/F/H=53-150.
DR   PDB; 3W5V; X-ray; 3.81 A; B/D=53-150.
DR   PDB; 5H8Y; X-ray; 2.20 A; E/F=53-150.
DR   PDB; 5H92; X-ray; 2.08 A; C=53-150.
DR   PDBsum; 1GAQ; -.
DR   PDBsum; 3B2F; -.
DR   PDBsum; 3W5U; -.
DR   PDBsum; 3W5V; -.
DR   PDBsum; 5H8Y; -.
DR   PDBsum; 5H92; -.
DR   AlphaFoldDB; P27787; -.
DR   SMR; P27787; -.
DR   IntAct; P27787; 1.
DR   STRING; 4577.P27787; -.
DR   PaxDb; 4577-GRMZM2G122337_P01; -.
DR   ProMEX; P27787; -.
DR   MaizeGDB; 66392; -.
DR   eggNOG; ENOG502RXFZ; Eukaryota.
DR   InParanoid; P27787; -.
DR   SABIO-RK; P27787; -.
DR   EvolutionaryTrace; P27787; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P27787; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; TAS:AgBase.
DR   GO; GO:0009570; C:chloroplast stroma; IDA:AgBase.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:AgBase.
DR   GO; GO:0009055; F:electron transfer activity; IDA:AgBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0022900; P:electron transport chain; IDA:AgBase.
DR   GO; GO:0009416; P:response to light stimulus; IEP:AgBase.
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   NCBIfam; TIGR02008; fdx_plant; 1.
DR   PANTHER; PTHR43112; FERREDOXIN; 1.
DR   PANTHER; PTHR43112:SF3; FERREDOXIN-2, CHLOROPLASTIC; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; 3D-structure; Chloroplast; Direct protein sequencing;
KW   Electron transport; Iron; Iron-sulfur; Metal-binding; Plastid;
KW   Reference proteome; Transit peptide; Transport.
FT   TRANSIT         1..52
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:16668188"
FT   CHAIN           53..150
FT                   /note="Ferredoxin-1, chloroplastic"
FT                   /id="PRO_0000008830"
FT   DOMAIN          55..145
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         91
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   BINDING         96
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   BINDING         99
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   BINDING         129
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   MUTAGEN         117
FT                   /note="D->N: Decreased affinity for Fd-NADP(+)
FT                   oxidoreductase and decreased electron-transfer activity."
FT                   /evidence="ECO:0000269|PubMed:9952443"
FT   STRAND          54..61
FT                   /evidence="ECO:0007829|PDB:3B2F"
FT   STRAND          64..71
FT                   /evidence="ECO:0007829|PDB:3B2F"
FT   STRAND          72..74
FT                   /evidence="ECO:0007829|PDB:1GAQ"
FT   HELIX           76..82
FT                   /evidence="ECO:0007829|PDB:3B2F"
FT   STRAND          90..94
FT                   /evidence="ECO:0007829|PDB:3B2F"
FT   STRAND          100..106
FT                   /evidence="ECO:0007829|PDB:3B2F"
FT   HELIX           118..122
FT                   /evidence="ECO:0007829|PDB:3B2F"
FT   STRAND          125..127
FT                   /evidence="ECO:0007829|PDB:3B2F"
FT   HELIX           128..130
FT                   /evidence="ECO:0007829|PDB:3B2F"
FT   STRAND          132..140
FT                   /evidence="ECO:0007829|PDB:3B2F"
FT   HELIX           144..147
FT                   /evidence="ECO:0007829|PDB:3B2F"
SQ   SEQUENCE   150 AA;  15838 MW;  1AF43354A9BC1D3F CRC64;
     MATVLGSPRA PAFFFSSSSL RAAPAPTAVA LPAAKVGIMG RSASSRRRLR AQATYNVKLI
     TPEGEVELQV PDDVYILDQA EEDGIDLPYS CRAGSCSSCA GKVVSGSVDQ SDQSYLDDGQ
     IADGWVLTCH AYPTSDVVIE THKEEELTGA
//