ID   FER2_AQUAE              Reviewed;         111 AA.
AC   O66511;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Ferredoxin, 2Fe-2S;
DE   AltName: Full=AaFd4;
GN   Name=fdx4; OrderedLocusNames=aq_107; ORFNames=aq_108A;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-111, SUBUNIT, AND MASS SPECTROMETRY.
RX   PubMed=10441520; DOI=10.1006/bbrc.1999.1138;
RA   Chatelet C., Gaillard J., Petillot Y., Louwagie M., Meyer J.;
RT   "A [2Fe-2S] protein from the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Biochem. Biophys. Res. Commun. 261:885-889(1999).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX   PubMed=10884354; DOI=10.1006/jmbi.2000.3871;
RA   Yeh A.P., Chatelet C., Soltis S.M., Kuhn P., Meyer J., Rees D.C.;
RT   "Structure of a thioredoxin-like [2Fe-2S] ferredoxin from Aquifex
RT   aeolicus.";
RL   J. Mol. Biol. 300:587-595(2000).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS).
RX   PubMed=12089152; DOI=10.1074/jbc.m205096200;
RA   Yeh A.P., Ambroggio X.I., Andrade S.L.A., Einsle O., Chatelet C., Meyer J.,
RA   Rees D.C.;
RT   "High resolution crystal structures of the wild type and Cys-55->Ser and
RT   Cys-59->Ser variants of the thioredoxin-like [2Fe-2S] ferredoxin from
RT   Aquifex aeolicus.";
RL   J. Biol. Chem. 277:34499-34507(2002).
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: Homodimer in solution. {ECO:0000269|PubMed:10441520}.
CC   -!- MASS SPECTROMETRY: Mass=24733; Mass_error=1; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:10441520};
CC   -!- SIMILARITY: Belongs to the 2Fe2S Shethna-type ferredoxin family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC06474.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AE000657; AAC06474.1; ALT_FRAME; Genomic_DNA.
DR   PIR; JC7085; JC7085.
DR   PDB; 1F37; X-ray; 2.30 A; A/B=2-111.
DR   PDB; 1M2A; X-ray; 1.50 A; A/B=2-111.
DR   PDB; 1M2B; X-ray; 1.25 A; A/B=2-111.
DR   PDB; 1M2D; X-ray; 1.05 A; A/B=2-111.
DR   PDBsum; 1F37; -.
DR   PDBsum; 1M2A; -.
DR   PDBsum; 1M2B; -.
DR   PDBsum; 1M2D; -.
DR   AlphaFoldDB; O66511; -.
DR   SMR; O66511; -.
DR   STRING; 224324.aq_108a; -.
DR   EnsemblBacteria; AAC06474; AAC06474; aq_108a.
DR   eggNOG; COG3411; Bacteria.
DR   HOGENOM; CLU_2893567_0_0_0; -.
DR   InParanoid; O66511; -.
DR   OMA; GICHKKE; -.
DR   EvolutionaryTrace; O66511; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; 3D-structure; Direct protein sequencing; Electron transport; Iron;
KW   Iron-sulfur; Metal-binding; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:10441520"
FT   CHAIN           2..111
FT                   /note="Ferredoxin, 2Fe-2S"
FT                   /id="PRO_0000187246"
FT   BINDING         10
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   BINDING         23
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   BINDING         56
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   BINDING         60
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   STRAND          5..10
FT                   /evidence="ECO:0007829|PDB:1M2D"
FT   HELIX           24..26
FT                   /evidence="ECO:0007829|PDB:1M2D"
FT   HELIX           28..41
FT                   /evidence="ECO:0007829|PDB:1M2D"
FT   HELIX           43..46
FT                   /evidence="ECO:0007829|PDB:1M2D"
FT   STRAND          49..55
FT                   /evidence="ECO:0007829|PDB:1M2D"
FT   HELIX           60..62
FT                   /evidence="ECO:0007829|PDB:1M2D"
FT   STRAND          66..69
FT                   /evidence="ECO:0007829|PDB:1M2D"
FT   TURN            70..72
FT                   /evidence="ECO:0007829|PDB:1M2D"
FT   STRAND          73..75
FT                   /evidence="ECO:0007829|PDB:1M2D"
FT   HELIX           80..82
FT                   /evidence="ECO:0007829|PDB:1M2D"
FT   HELIX           83..89
FT                   /evidence="ECO:0007829|PDB:1M2D"
FT   TURN            90..93
FT                   /evidence="ECO:0007829|PDB:1M2D"
FT   HELIX           98..100
FT                   /evidence="ECO:0007829|PDB:1M2D"
FT   STRAND          101..103
FT                   /evidence="ECO:0007829|PDB:1M2D"
SQ   SEQUENCE   111 AA;  12323 MW;  DBC282B39939911C CRC64;
     MAEFKHVFVC VQDRPPGHPQ GSCAQRGSRE VFQAFMEKIQ TDPQLFMTTV ITPTGCMNAC
     MMGPVVVVYP DGVWYGQVKP EDVDEIVEKH LKGGEPVERL VISKGKPPGM F