ID   AOX_PODAS               Reviewed;         363 AA.
AC   Q9C206;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Alternative oxidase, mitochondrial;
DE            EC=1.-.-.-;
DE   Flags: Precursor;
GN   Name=AOX1; Synonyms=AOX;
OS   Podospora anserina (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora.
OX   NCBI_TaxID=2587412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=s;
RX   PubMed=11134328; DOI=10.1128/mcb.21.2.390-399.2001;
RA   Borghouts C., Werner A., Elthon T., Osiewacz H.D.;
RT   "Copper-modulated gene expression and senescence in the filamentous fungus
RT   Podospora anserina.";
RL   Mol. Cell. Biol. 21:390-399(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=s;
RX   PubMed=11886557; DOI=10.1046/j.1365-2958.2001.02690.x;
RA   Lorin S., Dufour E., Boulay J., Begel O., Marsy S., Sainsard-Chanet A.;
RT   "Overexpression of the alternative oxidase restores senescence and
RT   fertility in a long-lived respiration-deficient mutant of Podospora
RT   anserina.";
RL   Mol. Microbiol. 42:1259-1267(2001).
CC   -!- FUNCTION: Catalyzes cyanide-resistant oxygen consumption. May increase
CC       respiration when the cytochrome respiratory pathway is restricted, or
CC       in response to low temperatures (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000250|UniProtKB:Q26710};
CC       Note=Binds 2 iron ions per subunit. {ECO:0000250|UniProtKB:Q26710};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the alternative oxidase family. {ECO:0000305}.
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DR   EMBL; AJ290969; CAC27396.1; -; Genomic_DNA.
DR   EMBL; AF321004; AAK58849.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9C206; -.
DR   SMR; Q9C206; -.
DR   VEuPathDB; FungiDB:PODANS_3_1710; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0009916; F:alternative oxidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd01053; AOX; 1.
DR   Gene3D; 1.20.1260.140; -; 1.
DR   InterPro; IPR002680; AOX.
DR   InterPro; IPR038659; AOX_sf.
DR   PANTHER; PTHR31803; PTHR31803; 1.
DR   Pfam; PF01786; AOX; 1.
DR   PIRSF; PIRSF005229; AOX; 1.
PE   3: Inferred from homology;
KW   Electron transport; Iron; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Oxidoreductase; Respiratory chain;
KW   Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT   TRANSIT         1..66
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           67..363
FT                   /note="Alternative oxidase, mitochondrial"
FT                   /id="PRO_0000001727"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        224..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         165
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q26710"
FT   BINDING         204
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q26710"
FT   BINDING         204
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q26710"
FT   BINDING         207
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q26710"
FT   BINDING         255
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q26710"
FT   BINDING         312
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q26710"
FT   BINDING         312
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q26710"
FT   BINDING         315
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q26710"
SQ   SEQUENCE   363 AA;  41404 MW;  1EA2C8EAF9B5A717 CRC64;
     MISSKTSNRI CLCSPQQTAR ITGIVVSSRP AYLTGLGYPV SLRLSSAVSQ SSSQHTRSFS
     STRAAHLKDF FPVKETAYIR KTPPAWPHHG YTEEEMLAVV PQHRKPGSLS DWLAWKLVRL
     CRWGTDIATG IKPEQQVDKS NPTTAVAAQK PLTEAQWLVR FIFLESIAGV PGMVAGMLRH
     LESLRRLKRD NGWIETLLEE SYNERMHLLT FMKMCEPGWF MKTMILGAQG VFFNAMFLSY
     LISPRITHRF VGYLEEEAVH TYTRCIREIE QGDLPKWSDP NFQIPDLAVT YWKMPEGKRT
     MRDLILYIRA DEAVHRGVNH TLSNLNHKED PNPFVSDYKC DADHQRPNPA LKPTGFERSE
     VIG