ID   FER1_NOSSO              Reviewed;          99 AA.
AC   P0A3C8; P06543;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Ferredoxin-1;
DE   AltName: Full=Ferredoxin I;
GN   Name=petF; Synonyms=fdxV;
OS   Nostoc sp. (strain ATCC 29151 / PCC 7119) (Anabaena sp.).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=1168;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-99, AND X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS).
RX   PubMed=10625442; DOI=10.1021/bi991578s;
RA   Morales R., Charon M.-H., Hudry-Clergeon G., Petillot Y., Norager S.,
RA   Medina M., Frey M.;
RT   "Refined X-ray structures of the oxidized, at 1.3 A, and reduced, at 1.17
RT   A, [2Fe-2S] ferredoxin from the cyanobacterium anabaena PCC7119 show redox-
RT   linked conformational changes.";
RL   Biochemistry 38:15764-15773(1999).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS).
RX   PubMed=11053838; DOI=10.1107/s0907444900010052;
RA   Morales R., Kachalova G., Vellieux F., Charon M.-H., Frey M.;
RT   "Crystallographic studies of the interaction between the ferredoxin-NADP+
RT   reductase and ferredoxin from the cyanobacterium Anabaena: looking for the
RT   elusive ferredoxin molecule.";
RL   Acta Crystallogr. D 56:1408-1412(2000).
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   -!- INTERACTION:
CC       P0A3C8; P21890: petH; NbExp=5; IntAct=EBI-637080, EBI-593915;
CC   -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC       {ECO:0000305}.
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DR   PDB; 1CZP; X-ray; 1.17 A; A/B=2-99.
DR   PDB; 1EWY; X-ray; 2.38 A; C=2-99.
DR   PDB; 1QT9; X-ray; 1.30 A; A=2-99.
DR   PDBsum; 1CZP; -.
DR   PDBsum; 1EWY; -.
DR   PDBsum; 1QT9; -.
DR   AlphaFoldDB; P0A3C8; -.
DR   BMRB; P0A3C8; -.
DR   SASBDB; P0A3C8; -.
DR   SMR; P0A3C8; -.
DR   IntAct; P0A3C8; 2.
DR   EvolutionaryTrace; P0A3C8; -.
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; Direct protein sequencing; Electron transport; Iron;
KW   Iron-sulfur; Metal-binding; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:10625442"
FT   CHAIN           2..99
FT                   /note="Ferredoxin-1"
FT                   /id="PRO_0000189299"
FT   DOMAIN          4..96
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         42
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   BINDING         47
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   BINDING         50
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   BINDING         80
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   STRAND          3..10
FT                   /evidence="ECO:0007829|PDB:1CZP"
FT   TURN            11..14
FT                   /evidence="ECO:0007829|PDB:1CZP"
FT   STRAND          15..22
FT                   /evidence="ECO:0007829|PDB:1CZP"
FT   HELIX           27..33
FT                   /evidence="ECO:0007829|PDB:1CZP"
FT   STRAND          41..48
FT                   /evidence="ECO:0007829|PDB:1CZP"
FT   STRAND          51..57
FT                   /evidence="ECO:0007829|PDB:1CZP"
FT   HELIX           69..73
FT                   /evidence="ECO:0007829|PDB:1CZP"
FT   STRAND          76..78
FT                   /evidence="ECO:0007829|PDB:1CZP"
FT   HELIX           79..81
FT                   /evidence="ECO:0007829|PDB:1CZP"
FT   STRAND          83..86
FT                   /evidence="ECO:0007829|PDB:1CZP"
FT   STRAND          88..91
FT                   /evidence="ECO:0007829|PDB:1CZP"
FT   TURN            95..98
FT                   /evidence="ECO:0007829|PDB:1CZP"
SQ   SEQUENCE   99 AA;  10830 MW;  874FD6365346BFFF CRC64;
     MATFKVTLIN EAEGTKHEIE VPDDEYILDA AEEQGYDLPF SCRAGACSTC AGKLVSGTVD
     QSDQSFLDDD QIEAGYVLTC VAYPTSDVVI QTHKEEDLY