AOX_WICAO
ID AOX_WICAO Reviewed; 342 AA.
AC Q00912;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Alternative oxidase, mitochondrial;
DE EC=1.-.-.-;
DE Flags: Precursor;
GN Name=AOX1; Synonyms=ALX1;
OS Wickerhamomyces anomalus (Yeast) (Hansenula anomala).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=4927;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1883836; DOI=10.1016/0167-4781(91)90043-l;
RA Sakajo S., Minagawa N., Komiyama T., Yoshimoto A.;
RT "Molecular cloning of cDNA for antimycin A-inducible mRNA and its role in
RT cyanide-resistant respiration in Hansenula anomala.";
RL Biochim. Biophys. Acta 1090:102-108(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 66094 / LKBY-1;
RX PubMed=10635554; DOI=10.1271/bbb.63.1889;
RA Sakajo S., Minagawa N., Yoshimoto A.;
RT "Structure and regulatory expression of a single copy alternative oxidase
RT gene from the yeast Pichia anomala.";
RL Biosci. Biotechnol. Biochem. 63:1889-1894(1999).
RN [3]
RP IRON-BINDING SITES.
RX PubMed=10225419; DOI=10.1016/s0014-5793(99)00376-2;
RA Andersson M.E., Nordlund P.;
RT "A revised model of the active site of alternative oxidase.";
RL FEBS Lett. 449:17-22(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.
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 -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC protein; Matrix side.
CC -!- SIMILARITY: Belongs to the alternative oxidase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D00741; BAA00641.1; -; mRNA.
DR EMBL; AB026726; BAA90763.1; -; Genomic_DNA.
DR PIR; S17517; S17517.
DR AlphaFoldDB; Q00912; -.
DR SMR; Q00912; -.
DR PRIDE; Q00912; -.
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 1: Evidence at protein level;
KW Disulfide bond; Electron transport; Iron; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW Respiratory chain; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..20
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 21..342
FT /note="Alternative oxidase, mitochondrial"
FT /id="PRO_0000001720"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 308..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 142
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 181
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 181
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 184
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 232
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 287
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 287
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 290
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT DISULFID 99
FT /note="Interchain"
FT /evidence="ECO:0000255"
SQ SEQUENCE 342 AA; 40284 MW; 140C49F0A8AA9975 CRC64;
MIKTYQYRSI LNSRNVGIRF LKTLSPSPHS KDPNSKSIFD IGTKLIVNPP PQMADNQYVT
HPLFPHPKYS DEDCEAVHFV HREPKTIGDK IADRGVKFCR ASFDFVTGYK KPKDVNGMLK
SWEGTRYEMT EEKWLTRCIF LESVAGVPGM VAAFIRHLHS LRLLKRDKAW IETLLDEAYN
ERMHLLTFIK IGNPSWFTRF IIYMGQGVFA NLFFLVYLIK PRYCHRFVGY LEEEAVSTYT
HLIKDIDSKR LPKFDDVNLP EISWLYWTDL NEKSTFRDLI QRIRADESKH REVNHTLANL
EQKKDRNPFA LKVEDVPKEQ QPDEYSLKTP HPEGWNREQM RL
