AOX_VENIN
ID AOX_VENIN Reviewed; 361 AA.
AC Q9P429; Q96W61;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Alternative oxidase, mitochondrial;
DE EC=1.-.-.-;
DE Flags: Precursor;
GN Name=AOX1;
OS Venturia inaequalis (Apple scab fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Venturiaceae; Venturia.
OX NCBI_TaxID=5025;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=97.5.12.;
RX PubMed=11561403; DOI=10.1002/ps.356;
RA Steinfeld U., Sierotzki H., Parisi S., Poirey S., Gisi U.;
RT "Sensitivity of mitochondrial respiration to different inhibitors in
RT Venturia inaequalis.";
RL Pest Manag. Sci. 57:787-796(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-361.
RC STRAIN=Ent2;
RA Schnabel G., Jones A.L.;
RT "Molecular evidence for activation of the alternative respiratory pathway
RT in Venturia inaequalis by strobilurin fungicides.";
RL (In) Dehne H.-W., Gisi U., Kuck K.H., Russell P.E., Lyr H. (eds.);
RL Modern fungicides and antifungal compounds III, pp.161-165, AgroConcept
RL GmbH, Bonn (2002).
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; AF279690; AAF87802.1; -; Genomic_DNA.
DR EMBL; AF363785; AAK61349.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9P429; -.
DR SMR; Q9P429; -.
DR PRIDE; Q9P429; -.
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 ?..361
FT /note="Alternative oxidase, mitochondrial"
FT /id="PRO_0000001728"
FT TRANSMEM 156..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 318..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 164
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 203
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 203
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 206
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 254
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="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 312
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT CONFLICT 5
FT /note="F -> Y (in Ref. 2; AAK61349)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="N -> D (in Ref. 2; AAK61349)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 41355 MW; 44BE80F5E6A295F8 CRC64;
MTLMFTSRTA VYCSNLTTQR SAVTILRTLS GTASNGIKSR SALTAYQQNP SLRTRNFHST
SVVQAKDFFP EPDTPHIKKT KTAWPHPIYT VEQMNQVAVA HRDTRNWSDK VALIAVKLLR
WGLDTVSGYK HGKAQALHAQ DPQEAQKRYG MTGKQYLVRN VFLESVAGVP GMVAGMLRHL
HSMRRMKRDH GWIETLLEES YNERMHLLIF LKLYEPGWFM RLAVLGAQGV FFNAMFLSYL
ISPRTCHRFV GYLEEEAVVT YTRELADLEA GKLPEWETLA APDIAVDYYN LPEGHRTMKD
LLLHVRADEA KHREVNHTLG NLDQNSDPNP YASKYDNPNV PHPRKDIKYL KPSGWEREEV
M
