ID   FRDA_DICDI              Reviewed;         193 AA.
AC   Q54C45;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Frataxin, mitochondrial;
DE            Short=Fxn;
DE            EC=1.16.3.1;
DE   Flags: Precursor;
GN   Name=fxn; ORFNames=DDB_G0293246;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Promotes the biosynthesis of heme as well as the assembly and
CC       repair of iron-sulfur clusters by delivering Fe(2+) to proteins
CC       involved in these pathways. May play a role in the protection against
CC       iron-catalyzed oxidative stress through its ability to catalyze the
CC       oxidation of Fe(2+) to Fe(3+). May be able to store large amounts of
CC       the metal in the form of a ferrihydrite mineral by oligomerization (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
CC         Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1;
CC   -!- SUBUNIT: Monomer. Oligomer (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q16595}.
CC   -!- SIMILARITY: Belongs to the frataxin family. {ECO:0000305}.
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DR   EMBL; AAFI02000200; EAL60822.1; -; Genomic_DNA.
DR   RefSeq; XP_629221.1; XM_629219.1.
DR   AlphaFoldDB; Q54C45; -.
DR   SMR; Q54C45; -.
DR   STRING; 44689.DDB0266646; -.
DR   PaxDb; Q54C45; -.
DR   EnsemblProtists; EAL60822; EAL60822; DDB_G0293246.
DR   GeneID; 8629103; -.
DR   KEGG; ddi:DDB_G0293246; -.
DR   dictyBase; DDB_G0293246; fxn.
DR   eggNOG; KOG3413; Eukaryota.
DR   HOGENOM; CLU_080880_2_4_1; -.
DR   InParanoid; Q54C45; -.
DR   OMA; IFIITTH; -.
DR   PhylomeDB; Q54C45; -.
DR   Reactome; R-DDI-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR   PRO; PR:Q54C45; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0005739; C:mitochondrion; ISS:dictyBase.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central.
DR   GO; GO:0008199; F:ferric iron binding; IBA:GO_Central.
DR   GO; GO:0008198; F:ferrous iron binding; ISS:dictyBase.
DR   GO; GO:0004322; F:ferroxidase activity; IBA:GO_Central.
DR   GO; GO:0034986; F:iron chaperone activity; IBA:GO_Central.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; ISS:dictyBase.
DR   GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0018283; P:iron incorporation into metallo-sulfur cluster; IBA:GO_Central.
DR   Gene3D; 3.30.920.10; -; 1.
DR   InterPro; IPR017789; Frataxin.
DR   InterPro; IPR002908; Frataxin/CyaY.
DR   InterPro; IPR036524; Frataxin/CyaY_sf.
DR   InterPro; IPR020895; Frataxin_CS.
DR   PANTHER; PTHR16821; PTHR16821; 1.
DR   Pfam; PF01491; Frataxin_Cyay; 1.
DR   SMART; SM01219; Frataxin_Cyay; 1.
DR   SUPFAM; SSF55387; SSF55387; 1.
DR   TIGRFAMs; TIGR03421; FeS_CyaY; 1.
DR   TIGRFAMs; TIGR03422; mito_frataxin; 1.
DR   PROSITE; PS01344; FRATAXIN_1; 1.
DR   PROSITE; PS50810; FRATAXIN_2; 1.
PE   3: Inferred from homology;
KW   Heme biosynthesis; Ion transport; Iron; Iron storage; Iron transport;
KW   Mitochondrion; Oxidoreductase; Reference proteome; Transit peptide;
KW   Transport.
FT   TRANSIT         1..72
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           73..193
FT                   /note="Frataxin, mitochondrial"
FT                   /id="PRO_0000328230"
SQ   SEQUENCE   193 AA;  22206 MW;  0B21618EE5DFAC71 CRC64;
     MIFNFLNKAS NKTHTKLLLF SSIRNRILIN NISSTSKWSS INNNNKQSSV SKTNIFIITT
     HNKQQQQLSK SFSTINNNTK PISDVNLFHD IVDEEFELFV DRLEILSEAN TCEGFEVEGN
     DGVLTIIVGN KGTYVINKQT PNRQIWWSSP LSGPKRFDYD SVEKRWVDNR DGTPLRQLLN
     SEINTLCKYD MEI