ID   FRDA_SCHPO              Reviewed;         158 AA.
AC   O74831;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Frataxin homolog, mitochondrial;
DE            EC=1.16.3.1;
DE   Flags: Precursor;
GN   ORFNames=SPCC1183.03c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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}.
CC   -!- SIMILARITY: Belongs to the frataxin family. {ECO:0000305}.
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DR   EMBL; CU329672; CAA21083.1; -; Genomic_DNA.
DR   PIR; T40843; T40843.
DR   RefSeq; NP_587886.1; NM_001022878.2.
DR   AlphaFoldDB; O74831; -.
DR   SMR; O74831; -.
DR   BioGRID; 275715; 1.
DR   STRING; 4896.SPCC1183.03c.1; -.
DR   MaxQB; O74831; -.
DR   PaxDb; O74831; -.
DR   EnsemblFungi; SPCC1183.03c.1; SPCC1183.03c.1:pep; SPCC1183.03c.
DR   GeneID; 2539143; -.
DR   KEGG; spo:SPCC1183.03c; -.
DR   PomBase; SPCC1183.03c; -.
DR   VEuPathDB; FungiDB:SPCC1183.03c; -.
DR   eggNOG; KOG3413; Eukaryota.
DR   HOGENOM; CLU_080880_4_0_1; -.
DR   InParanoid; O74831; -.
DR   OMA; YEVEYHS; -.
DR   PhylomeDB; O74831; -.
DR   Reactome; R-SPO-1268020; Mitochondrial protein import.
DR   Reactome; R-SPO-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR   PRO; PR:O74831; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:PomBase.
DR   GO; GO:0005739; C:mitochondrion; IDA:PomBase.
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; IBA:GO_Central.
DR   GO; GO:0004322; F:ferroxidase activity; IBA:GO_Central.
DR   GO; GO:0034986; F:iron chaperone activity; ISO:PomBase.
DR   GO; GO:0044571; P:[2Fe-2S] cluster assembly; IC:PomBase.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR   GO; GO:0006783; P:heme biosynthetic process; ISO:PomBase.
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   PRINTS; PR00904; FRATAXIN.
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..?
FT                   /note="Mitochondrion"
FT   CHAIN           ?..158
FT                   /note="Frataxin homolog, mitochondrial"
FT                   /id="PRO_0000010134"
SQ   SEQUENCE   158 AA;  18387 MW;  F5018ECAB617573E CRC64;
     MQSLRAAFRR RTPIFLKPYE FSTNVFGLRC RYYSQVRHNG ALTDLEYHRV ADDTLDVLND
     TFEDLLEEVG KKDYDIQYAN GVITLMLGEK GTYVINKQPP AHQIWLSSPV SGPKHYEYSL
     KSKTWCSTRD EGTLLGILSS EFSKWFSRPI EFKKSEDF