AOX_MONFR
ID AOX_MONFR Reviewed; 358 AA.
AC Q96UR9;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Alternative oxidase, mitochondrial;
DE EC=1.-.-.-;
DE AltName: Full=MfAOX1;
DE Flags: Precursor;
GN Name=AOX1;
OS Monilinia fructicola (Brown rot fungus) (Ciboria fructicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Monilinia.
OX NCBI_TaxID=38448;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14561072; DOI=10.1002/ps.744;
RA Schnabel G., Dai Q., Paradkar M.R.;
RT "Cloning and expression analysis of the ATP-binding cassette transporter
RT MFABC1 gene and the alternative oxidase gene MfAOX1 from Monilinia
RT fructicola.";
RL Pest Manag. Sci. 59:1143-1151(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; AF420306; AAL24516.1; -; Genomic_DNA.
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..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..358
FT /note="Alternative oxidase, mitochondrial"
FT /id="PRO_0000001724"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 159
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
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 198
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 201
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 249
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="1"
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"
FT BINDING 309
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
SQ SEQUENCE 358 AA; 41098 MW; 8DC4352E42D40365 CRC64;
MYVARLSTRP LSNPSTAQLS KAAAFFAQSY ALPSTKCTAH VPSRRPFTSG AKIQVKGRDL
FPEPXHGQIK RTEPAWPHPP YSVEQMRSKV YFAHRKPRDF SDRVALGMVR FLRWCTDFAT
GYKHNVEAPK TASDSNAVTA TKPYQMSERK WLIRYVFLES VAGVPGMVAG MLRHLRSLRG
LKRDNGWIET LLEEAYNERM HLLTFLKMYE PGLFMRTMIL GAQGVFFNSF FLCYLFSPKT
CHRFVGYLEE EAVLTYTLSI QDLENGHLPK WADPNFKAPD LAIEYWGMPE GHRSMRDLLY
YIRADEAKHR EVNHTLGNLK QDEDPNPFVS VYGKEVADKP GKGIESLRPL GWEREEVI
