AOX_BOTFU
ID AOX_BOTFU Reviewed; 361 AA.
AC Q8NJ59;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Alternative oxidase, mitochondrial;
DE EC=1.-.-.-;
DE Flags: Precursor;
GN Name=aox;
OS Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=40559;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10996313; DOI=10.1016/s0014-5793(00)01943-8;
RA Joseph-Horne T., Babij J., Wood P.M., Hollomon D., Sessions R.B.;
RT "New sequence data enable modelling of the fungal alternative oxidase and
RT explain an absence of regulation by pyruvate.";
RL FEBS Lett. 481:141-146(2000).
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; AJ496184; CAD42731.1; -; mRNA.
DR AlphaFoldDB; Q8NJ59; -.
DR SMR; Q8NJ59; -.
DR PRIDE; Q8NJ59; -.
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; Respiratory chain;
KW Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..361
FT /note="Alternative oxidase, mitochondrial"
FT /id="PRO_0000001716"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 320..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 162
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 162
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
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 201
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 /evidence="ECO:0000255"
FT BINDING 204
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 204
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 252
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 253
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 309
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
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"
FT BINDING 309
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 312
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 312
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
SQ SEQUENCE 361 AA; 41484 MW; A0FDC1E73F1F4896 CRC64;
MTTMYVSRVS TRPLSAQSAA QLSKAVAFFA QSYRLSSNAC TAPTPSRRAF TSASKIQVKG
RDLFPEPEHG QIKRTEPAWP HPPYTAEQMR SKVYFAHRKP RDFSDRVALG MVRFLRWCTD
FATGYKHNVE APKKASDSNA LTATKPYQMS ERKWLIRYVF LESVAGVPGM VAGMLRHLRS
LRGLKRDNGW IETLLEEAYN ERMHLLTFLK MYEPGIFMRT MILGAQGVFF NSFFLCYLFS
PRTCHRFVGY LEEEAVLTYT LSIQDLENGH LPKWADPDFK APDLAVEYWG MPEGNRSMRD
LLYYIRADEA KHREVNHTLG NLKQDEDPNP FVSEYGKERG EKPGKGIESL KPVGWERDEV
I
