ID   AOX_GELSS               Reviewed;         362 AA.
AC   Q8J1Z2;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Alternative oxidase, mitochondrial;
DE            EC=1.-.-.-;
DE   Flags: Precursor;
GN   Name=aod-1;
OS   Gelasinospora sp. (strain S23).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Gelasinospora;
OC   unclassified Gelasinospora.
OX   NCBI_TaxID=210212;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12781676; DOI=10.1016/s1087-1845(03)00002-1;
RA   Tanton L.L., Nargang C.E., Kessler K.E., Li Q., Nargang F.E.;
RT   "Alternative oxidase expression in Neurospora crassa.";
RL   Fungal Genet. Biol. 39:176-190(2003).
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; AY140655; AAN39884.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8J1Z2; -.
DR   SMR; Q8J1Z2; -.
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..64
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           65..362
FT                   /note="Alternative oxidase, mitochondrial"
FT                   /id="PRO_0000001722"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         163
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q26710"
FT   BINDING         202
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q26710"
FT   BINDING         202
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q26710"
FT   BINDING         205
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q26710"
FT   BINDING         253
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q26710"
FT   BINDING         310
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q26710"
FT   BINDING         310
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q26710"
FT   BINDING         313
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q26710"
SQ   SEQUENCE   362 AA;  41586 MW;  5E4A5A57E4B75E68 CRC64;
     MNTPKVNILY SPGQAAQLSR TLISTCHTRP FLLGGLRVAT SLHPTQTNLS SSPPRGFTTT
     SVVRLKDFFP AKETAYIRQT PPAWPHHGWT EEEMISVVPE HRKPETVGDW LAWKLVRICR
     WGTDIATGIR PEQQVDKNHP TTATSADKPL TEAQWLVRFI FLESIAGVPG MVAGMLRHLH
     SLRRLKRDNG WIETLLEESY NERMHLLTFM KMCEPGLLMK TLILGAQGVF FNAMFLSYLV
     SPKITHRFVG YLEEEAVHTY TRCIREIEEG HLPKWSDERF EIPEMAVRYW RMPEGKRTMK
     DLIYYIRADE AVHRGVNHTL SNLDQKEDPN PFVNDYKEGE GGRRPVNPAL KPTGFERAEV
     IR