AOX1_CANAX
ID AOX1_CANAX Reviewed; 379 AA.
AC O93853;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Alternative oxidase 1, mitochondrial;
DE EC=1.-.-.-;
DE Flags: Precursor;
GN Name=AOX1; Synonyms=AOX1A;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10231 / CBS 6431 / CIP 48.72 / DSM 1386 / NBRC 1594;
RX PubMed=10383980; DOI=10.1128/jb.181.13.4098-4102.1999;
RA Huh W.-K., Kang S.-O.;
RT "Molecular cloning and functional expression of alternative oxidase from
RT Candida albicans.";
RL J. Bacteriol. 181:4098-4102(1999).
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 Single-pass membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
CC Note=Possibly in the inner surface of the inner mitochondrial membrane.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the alternative oxidase family. {ECO:0000305}.
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DR EMBL; AF031229; AAC98914.1; -; Genomic_DNA.
DR AlphaFoldDB; O93853; -.
DR SMR; O93853; -.
DR VEuPathDB; FungiDB:C1_09160W_A; -.
DR VEuPathDB; FungiDB:CAWG_00513; -.
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 ?..379
FT /note="Alternative oxidase 1, mitochondrial"
FT /id="PRO_0000001717"
FT TRANSMEM 234..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 33..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 180
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 180
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 219
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 219
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 219
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 222
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 222
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 270
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 271
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 326
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 326
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 326
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 329
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 329
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
SQ SEQUENCE 379 AA; 43975 MW; C2DDC2CA298BD0F9 CRC64;
MIGLSTYRNL PTLLTTTTVI STALRSKQLL RFTTTTSTKS RSSTSTAATT VGNSNPKSPI
DEDNLEKPGT IPTKHKPFNI QTEVYNKAGI EANDDDKFLT KPTYRHEDFT EAGVYRVHVT
HRPPRTIGDK ISCYGTLFFR KCFDLVTGYA VPDPDKPDQY KGTRWEMTEE KWMTRCIFLE
SIAGVPGSVA GFVRHLHSLR MLTRDKAWIE TLHDEAYNER MHLLTFIKIG KPSWFTRSII
YIGQGVFTNI FFLVYLMNPR YCHRFVGYLE EEAVRTYTHL IDELDDPNKL PDFQKLPIPN
IAVQYWPELT PESSFKDLIL RIRADEAKHR EINHTFANLE QWQDRNPFAL KIKDSDKPQP
NYNLDVTRPQ GWERKDLYL
