ID   FER1_EQUAR              Reviewed;          95 AA.
AC   P00235;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Ferredoxin-1;
DE   AltName: Full=Ferredoxin I;
OS   Equisetum arvense (Field horsetail) (Common horsetail).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Polypodiopsida; Equisetidae; Equisetales; Equisetaceae; Equisetum.
OX   NCBI_TaxID=3258;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=893384; DOI=10.1093/oxfordjournals.jbchem.a131680;
RA   Hase T., Wada K., Matsubara H.;
RT   "Horsetail (Equisetum arvense) ferredoxins I and II Amino acid sequences
RT   and gene duplication.";
RL   J. Biochem. 82:277-286(1977).
RN   [2]
RP   IRON-SULFUR CLUSTER-BINDING SITES CYS-38; CYS-43; CYS-46 AND CYS-76.
RX   PubMed=1191250; DOI=10.1042/bj1450121;
RA   Kagamiyama H., Rao K.K., Hall D.O., Cammack R., Matsubara H.;
RT   "Equisetum (horsetail) ferredoxin: characterization of the active centre
RT   and position of the four cysteine residues in this 2Fe-2S protein.";
RL   Biochem. J. 145:121-123(1975).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   PubMed=15299454; DOI=10.1107/s0907444993009588;
RA   Ikemizu S., Bando M., Sato T., Morimoto Y., Tsukihara T., Fukuyama K.;
RT   "Structure of [2Fe-2S] ferredoxin I from Equisetum arvense at 1.8-A
RT   resolution.";
RL   Acta Crystallogr. D 50:167-174(1994).
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; A04609; FEEQ1F.
DR   PDB; 1FRR; X-ray; 1.80 A; A/B=1-95.
DR   PDBsum; 1FRR; -.
DR   AlphaFoldDB; P00235; -.
DR   SMR; P00235; -.
DR   EvolutionaryTrace; P00235; -.
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   1: Evidence at protein level;
KW   2Fe-2S; 3D-structure; Chloroplast; Direct protein sequencing;
KW   Electron transport; Iron; Iron-sulfur; Metal-binding; Plastid; Transport.
FT   CHAIN           1..95
FT                   /note="Ferredoxin-1"
FT                   /id="PRO_0000189328"
FT   DOMAIN          2..92
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         38
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   BINDING         43
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   BINDING         46
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   BINDING         76
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   STRAND          2..8
FT                   /evidence="ECO:0007829|PDB:1FRR"
FT   STRAND          11..17
FT                   /evidence="ECO:0007829|PDB:1FRR"
FT   HELIX           23..29
FT                   /evidence="ECO:0007829|PDB:1FRR"
FT   STRAND          37..44
FT                   /evidence="ECO:0007829|PDB:1FRR"
FT   STRAND          47..53
FT                   /evidence="ECO:0007829|PDB:1FRR"
FT   HELIX           65..69
FT                   /evidence="ECO:0007829|PDB:1FRR"
FT   STRAND          72..74
FT                   /evidence="ECO:0007829|PDB:1FRR"
FT   TURN            75..77
FT                   /evidence="ECO:0007829|PDB:1FRR"
FT   STRAND          79..82
FT                   /evidence="ECO:0007829|PDB:1FRR"
FT   STRAND          84..87
FT                   /evidence="ECO:0007829|PDB:1FRR"
FT   TURN            91..94
FT                   /evidence="ECO:0007829|PDB:1FRR"
SQ   SEQUENCE   95 AA;  10098 MW;  3AB5F5F3E72C44E2 CRC64;
     AYKTVLKTPS GEFTLDVPEG TTILDAAEEA GYDLPFSCRA GACSSCLGKV VSGSVDESEG
     SFLDDGQMEE GFVLTCIAIP ESDLVIETHK EEELF