FER1_MAIZE
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 03-AUG-2022, entry version 141.
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.GRMZM2G122337_P01; -.
DR PaxDb; P27787; -.
DR ProMEX; P27787; -.
DR MaizeGDB; 66392; -.
DR eggNOG; ENOG502RXFZ; Eukaryota.
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 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; 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
