AOX_EMENI
ID AOX_EMENI Reviewed; 354 AA.
AC Q9P959; C8VLX8; Q5BBI1; Q8J1Z3;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Alternative oxidase, mitochondrial;
DE EC=1.-.-.-;
DE Flags: Precursor;
GN Name=alxA; Synonyms=aod-1; ORFNames=AN2099;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RA Sakajo S., Minagawa N., Yoshimoto A.;
RT "Structure of a single copy alternative oxidase gene from Aspergillus
RT nidulans.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12781676; DOI=10.1016/s1087-1845(03)00002-1;
RA Tanton L.L., Nargang C.E., Kessler K.E., Li Q., Nargang F.E.;
RT "Alternative oxidase expression in Neurospora crassa.";
RL Fungal Genet. Biol. 39:176-190(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA93615.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAA64931.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AB039832; BAA93615.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY140654; AAN39883.1; -; Genomic_DNA.
DR EMBL; AACD01000032; EAA64931.1; ALT_INIT; Genomic_DNA.
DR EMBL; BN001307; CBF86176.1; -; Genomic_DNA.
DR RefSeq; XP_659703.1; XM_654611.1.
DR AlphaFoldDB; Q9P959; -.
DR SMR; Q9P959; -.
DR STRING; 162425.CADANIAP00008772; -.
DR EnsemblFungi; CBF86176; CBF86176; ANIA_02099.
DR EnsemblFungi; EAA64931; EAA64931; AN2099.2.
DR GeneID; 2874947; -.
DR KEGG; ani:AN2099.2; -.
DR VEuPathDB; FungiDB:AN2099; -.
DR eggNOG; ENOG502QSB5; Eukaryota.
DR HOGENOM; CLU_041974_3_0_1; -.
DR InParanoid; Q9P959; -.
DR OMA; AFNERMH; -.
DR OrthoDB; 943747at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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:0005739; C:mitochondrion; IDA:AspGD.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0009916; F:alternative oxidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010230; P:alternative respiration; IBA:GO_Central.
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..64
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 65..354
FT /note="Alternative oxidase, mitochondrial"
FT /id="PRO_0000001721"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 333..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 157
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 196
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 196
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 199
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 247
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 302
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 302
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 305
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT CONFLICT 12..13
FT /note="VA -> GG (in Ref. 2; AAN39883)"
FT /evidence="ECO:0000305"
FT CONFLICT 198..199
FT /note="MH -> LF (in Ref. 2; AAN39883)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="E -> G (in Ref. 2; AAN39883)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 40906 MW; ABFD6DCB6F74C28E CRC64;
MNSMSTTGPI RVAAIPKHYL QFTVRTYTRS MASAGLRYSN PPLVKKCYDQ PTGKRFISST
PQSQIKDYFP PPDAPKIVEV KTAWAHPVYS EEEMRAVTVG HREAKNWSDW VALGSVRLLR
WGMDLVTGYK HPAPGQEDIK KFQMTEKEWL RRFVFLESVA GVPGMVGGML RHLRSLRRMK
RDNGWIETLL EEAYNERMHL LTFLKMAEPG WFMRLMVLGA QGVFFNGFFL SYLISPRTCH
RFVGYLEEEA VLTYTRAIKD LESGRLPHWE KLEAPEIAVK YWKMPEGNRT MKDLLLYVRA
DEAKHREVNH TLGNLKQAVD VNPFAVEWKD PSKPHPGKGI KHLKTTGWER EEVV
