ID   FER_BUCBP               Reviewed;         107 AA.
AC   Q89A15;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=2Fe-2S ferredoxin;
GN   Name=fdx; OrderedLocusNames=bbp_548;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
CC   -!- FUNCTION: Ferredoxin 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; Evidence={ECO:0000250};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the adrenodoxin/putidaredoxin family.
CC       {ECO:0000305}.
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DR   EMBL; AE016826; AAO27246.1; -; Genomic_DNA.
DR   RefSeq; WP_011091647.1; NC_004545.1.
DR   AlphaFoldDB; Q89A15; -.
DR   SMR; Q89A15; -.
DR   STRING; 224915.bbp_548; -.
DR   EnsemblBacteria; AAO27246; AAO27246; bbp_548.
DR   GeneID; 56471082; -.
DR   KEGG; bab:bbp_548; -.
DR   eggNOG; COG0633; Bacteria.
DR   HOGENOM; CLU_082632_5_2_6; -.
DR   OMA; SACGGVC; -.
DR   OrthoDB; 1837979at2; -.
DR   Proteomes; UP000000601; Chromosome.
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   GO; GO:0140647; P:P450-containing electron transport chain; IEA:InterPro.
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; IPR001055; Adrenodoxin.
DR   InterPro; IPR018298; Adrenodoxin_Fe-S_BS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR011536; Fdx_isc.
DR   PANTHER; PTHR23426; PTHR23426; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   PRINTS; PR00355; ADRENODOXIN.
DR   SUPFAM; SSF54292; SSF54292; 1.
DR   TIGRFAMs; TIGR02007; fdx_isc; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS00814; ADX; 1.
PE   3: Inferred from homology;
KW   2Fe-2S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW   Reference proteome; Transport.
FT   CHAIN           1..107
FT                   /note="2Fe-2S ferredoxin"
FT                   /id="PRO_0000201167"
FT   DOMAIN          1..104
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         48
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         51
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         87
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ   SEQUENCE   107 AA;  12118 MW;  47A2EFFC92B1D649 CRC64;
     MPKLIILPHK ILLPKGGVFN AMKGESILNV ALRNNVEIEH ACEKSCVCTT CHCYIWKGAS
     SLSICEEKEE DVLDKAWNLQ FNSRLSCQAK INNKDIEIEI PKYTINQ