AOX_MAGO7
ID AOX_MAGO7 Reviewed; 377 AA.
AC O93788; A4QTA4; G4N4P1;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Alternative oxidase, mitochondrial;
DE EC=1.-.-.-;
DE AltName: Full=AOXMg;
DE AltName: Full=MgAOX;
DE Flags: Precursor;
GN Name=AOX1; ORFNames=MGG_12936;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Race 003;
RX PubMed=9804939; DOI=10.1016/s0167-4781(98)00159-6;
RA Yukioka H., Inagaki S., Tanaka R., Katoh K., Miki N., Mizutani A.,
RA Masuko M.;
RT "Transcriptional activation of the alternative oxidase gene of the fungus
RT Magnaporthe grisea by a respiratory-inhibiting fungicide and hydrogen
RT peroxide.";
RL Biochim. Biophys. Acta 1442:161-169(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12036280; DOI=10.1094/mpmi.2002.15.5.493;
RA Avila-Adame C., Koeller W.;
RT "Disruption of the alternative oxidase gene in Magnaporthe grisea and its
RT impact on host infection.";
RL Mol. Plant Microbe Interact. 15:493-500(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
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; AB005144; BAA34672.1; -; mRNA.
DR EMBL; AF325683; AAG49588.1; -; Genomic_DNA.
DR EMBL; CM001233; EHA52856.1; -; Genomic_DNA.
DR RefSeq; XP_003712663.1; XM_003712615.1.
DR AlphaFoldDB; O93788; -.
DR SMR; O93788; -.
DR STRING; 318829.MGG_12936T0; -.
DR EnsemblFungi; MGG_12936T0; MGG_12936T0; MGG_12936.
DR GeneID; 5048866; -.
DR KEGG; mgr:MGG_12936; -.
DR VEuPathDB; FungiDB:MGG_12936; -.
DR eggNOG; ENOG502QSB5; Eukaryota.
DR HOGENOM; CLU_041974_3_0_1; -.
DR InParanoid; O93788; -.
DR OMA; AFNERMH; -.
DR OrthoDB; 943747at2759; -.
DR Proteomes; UP000009058; Chromosome 3.
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 2: Evidence at transcript level;
KW Electron transport; Iron; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Oxidoreductase; Reference proteome;
KW Respiratory chain; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..377
FT /note="Alternative oxidase, mitochondrial"
FT /id="PRO_0000001723"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 156
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 195
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 195
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 198
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 246
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 303
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 303
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 306
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
SQ SEQUENCE 377 AA; 42744 MW; 8D8D55C1FE2E308A CRC64;
MLVHQVNTKL CSAKQFTHLA KVVTPALSYQ ASSVYSANLP RLAASPRLFS TTSSAQLRDF
FPVKETEHIR QTPPTWPHHG LTEKEMVDVV PGHRKPRTLG DKFAWSLVRI SRWGMDKVSG
LSSEQQQINK GSPTTSIVAA KPLTEAQWLS RFIFLESIAA VPGMVAGMLR HLHSLRRLKR
DNGWIETLLE EAYNERMHLL TFLKMCEPGW LMKILIIGAQ GVYFNAMFVA YLISPKICHR
FVGYLEEEAV HTYTRSIEEL ERGDLPKWSD PKFQVPEIAV SYWGMPEGHR TMRDLLLYIR
ADEANHRGVH HTLGNLNQVE DPNPFVSDYK GDKPRPVAAS RPEGFEREEV IGKEVIGKEV
IEKDVIGKEV LGKQVSV
