ID   FER2_RICPR              Reviewed;         112 AA.
AC   Q9ZDW6;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=2Fe-2S ferredoxin;
DE   AltName: Full=Adrenodoxin-like protein;
GN   Name=fdxB; Synonyms=fdx; OrderedLocusNames=RP199;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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; AJ235270; CAA14664.1; -; Genomic_DNA.
DR   PIR; A71731; A71731.
DR   RefSeq; NP_220587.1; NC_000963.1.
DR   RefSeq; WP_004595967.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZDW6; -.
DR   SMR; Q9ZDW6; -.
DR   STRING; 272947.gene:17555280; -.
DR   EnsemblBacteria; CAA14664; CAA14664; CAA14664.
DR   GeneID; 57569327; -.
DR   KEGG; rpr:RP199; -.
DR   PATRIC; fig|272947.5.peg.208; -.
DR   eggNOG; COG0633; Bacteria.
DR   HOGENOM; CLU_082632_5_0_5; -.
DR   OrthoDB; 9799640at2; -.
DR   Proteomes; UP000002480; 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:SF34; FERREDOXIN-2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR23426; FERREDOXIN/ADRENODOXIN; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   PRINTS; PR00355; ADRENODOXIN.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 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..112
FT                   /note="2Fe-2S ferredoxin"
FT                   /id="PRO_0000201177"
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   112 AA;  12493 MW;  66CF386B402DAD7E CRC64;
     MLRKIKVTFI INDEEERTVE APIGLSILEI AHSNDLDLEG ACEGSLACAT CHVMLEEEFY
     NKLKKPTEAE EDMLDLAFGL TDTSRLGCQI ILTEELDGIK VRLPSATRNI KL
//