AOX_PICST
ID AOX_PICST Reviewed; 357 AA.
AC Q9P414; A3LRV0;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Alternative oxidase, mitochondrial;
DE EC=1.-.-.-;
DE AltName: Full=SHAM-sensitive terminal oxidase;
DE Flags: Precursor;
GN Name=STO1; Synonyms=AOX1; ORFNames=PICST_67332;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=12271457; DOI=10.1002/yea.915;
RA Shi N.-Q., Cruz J., Sherman F., Jeffries T.W.;
RT "SHAM-sensitive alternative respiration in the xylose-metabolizing yeast
RT Pichia stipitis.";
RL Yeast 19:1203-1220(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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; AY004212; AAF97475.2; -; Genomic_DNA.
DR EMBL; CP000497; ABN65454.2; -; Genomic_DNA.
DR RefSeq; XP_001383483.2; XM_001383446.1.
DR AlphaFoldDB; Q9P414; -.
DR SMR; Q9P414; -.
DR STRING; 4924.XP_001383483.2; -.
DR PRIDE; Q9P414; -.
DR EnsemblFungi; ABN65454; ABN65454; PICST_67332.
DR GeneID; 4837885; -.
DR KEGG; pic:PICST_67332; -.
DR eggNOG; ENOG502QSB5; Eukaryota.
DR HOGENOM; CLU_041974_3_0_1; -.
DR InParanoid; Q9P414; -.
DR OMA; AFNERMH; -.
DR OrthoDB; 943747at2759; -.
DR Proteomes; UP000002258; 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 3: Inferred from homology;
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 ?..357
FT /note="Alternative oxidase, mitochondrial"
FT /id="PRO_0000001726"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 330..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 304
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 304
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 307
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
SQ SEQUENCE 357 AA; 41347 MW; 1182D77F4CE918D6 CRC64;
MLSVQTTRAA KLQLGQLPSI AYTARSGRLH HQFYSTVAEK TANPTPNTSD KTNIFDIRTK
VYDETDIRKH DDNQFITHPL FPHPTFSQED CLKVGYEHRP PRTFGDKMAF RGIELVRGSF
DFVTGYKKPK TQADIDSGFK GTRYEMTEGK WLTRCIFLES IAGVPGAVAS FIRHLHSLRL
LKRDKAWIET LLDEAFNERM HLLTFIKIGK PSWFTRTIIY VGQGVFCNLF FLFYLANPKY
CHRFVGYLEE EAVSTYTHFV HELQSGKLPK FENIKIPTIA WQYWPELTEN SSMLDLILRI
RADEAKHREV NHTLANLDQR KDRNPFGLAI PDLKEPQPES GLKVTKPHGW EKEELKL
