ID   FER2_RICBR              Reviewed;         111 AA.
AC   Q1RJ69;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=2Fe-2S ferredoxin;
DE   AltName: Full=Adrenodoxin-like protein;
GN   Name=fdxB; OrderedLocusNames=RBE_0514;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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; CP000087; ABE04595.1; -; Genomic_DNA.
DR   RefSeq; WP_011477186.1; NC_007940.1.
DR   AlphaFoldDB; Q1RJ69; -.
DR   SMR; Q1RJ69; -.
DR   STRING; 336407.RBE_0514; -.
DR   EnsemblBacteria; ABE04595; ABE04595; RBE_0514.
DR   KEGG; rbe:RBE_0514; -.
DR   eggNOG; COG0633; Bacteria.
DR   HOGENOM; CLU_082632_5_0_5; -.
DR   OMA; SACGGVC; -.
DR   OrthoDB; 1837979at2; -.
DR   Proteomes; UP000001951; 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   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   PANTHER; PTHR23426; PTHR23426; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   PRINTS; PR00355; ADRENODOXIN.
DR   SUPFAM; SSF54292; SSF54292; 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; Transport.
FT   CHAIN           1..111
FT                   /note="2Fe-2S ferredoxin"
FT                   /id="PRO_0000280895"
FT   DOMAIN          5..107
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         88
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ   SEQUENCE   111 AA;  12235 MW;  83BEA86ACF1BB3B3 CRC64;
     MSKTIKVTFV INNGEEKIIE APLGLSILEV AHSNSIDLEG ACEGSLACAT CHVILEEEFY
     NKLEKPKEEE EDMLDLAFGL TDTSRLGCQI ILTEKLDGIK VRLPSATRNI K