AOX_NEUCR
ID AOX_NEUCR Reviewed; 362 AA.
AC Q01355; Q7RVF8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Alternative oxidase, mitochondrial;
DE Short=ALTOX;
DE EC=1.-.-.-;
DE Flags: Precursor;
GN Name=aod-1; ORFNames=NCU07953;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF PRO-82 AND ALA-173.
RC STRAIN=NCN53 / FGSC 7595;
RX PubMed=8770590; DOI=10.1093/genetics/142.1.129;
RA Li Q., Ritzel R.G., McLean L.L.T., McIntosh L., Ko T., Bertrand H.,
RA Nargang F.E.;
RT "Cloning and analysis of the alternative oxidase gene of Neurospora
RT crassa.";
RL Genetics 142:129-140(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=su-1[mi-3];
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=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [4]
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}.
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DR EMBL; L46869; AAC37481.1; -; Genomic_DNA.
DR EMBL; AY140653; AAN39882.1; -; Genomic_DNA.
DR EMBL; CM002239; EAA32850.1; -; Genomic_DNA.
DR PIR; S65752; S65752.
DR RefSeq; XP_962086.1; XM_956993.2.
DR AlphaFoldDB; Q01355; -.
DR SMR; Q01355; -.
DR STRING; 5141.EFNCRP00000008199; -.
DR EnsemblFungi; EAA32850; EAA32850; NCU07953.
DR GeneID; 3878251; -.
DR KEGG; ncr:NCU07953; -.
DR HOGENOM; CLU_041974_3_0_1; -.
DR InParanoid; Q01355; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
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; IBA:GO_Central.
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 1: Evidence at protein level;
KW Disulfide bond; Electron transport; Iron; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW Reference proteome; Respiratory chain; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..64
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 65..362
FT /note="Alternative oxidase, mitochondrial"
FT /id="PRO_0000001725"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 163
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 202
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 202
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 205
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 253
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 310
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 310
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 313
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT DISULFID 119
FT /note="Interchain"
FT /evidence="ECO:0000255"
FT MUTAGEN 82
FT /note="P->L: In aod-1-1 and aod-1-2 mutants; alternative
FT oxidase deficiency."
FT /evidence="ECO:0000269|PubMed:8770590"
FT MUTAGEN 173
FT /note="A->D: In aod-1-6 mutant; alternative oxidase
FT deficiency."
FT /evidence="ECO:0000269|PubMed:8770590"
FT CONFLICT 57
FT /note="F -> L (in Ref. 3; EAA32850)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 41372 MW; BAF4AF7DD12267AA CRC64;
MNTPKVNILH APGQAAQLSR ALISTCHTRP LLLAGSRVAT SLHPTQTNLS SPSPRNFSTT
SVTRLKDFFP AKETAYIRQT PPAWPHHGWT EEEMTSVVPE HRKPETVGDW LAWKLVRICR
WATDIATGIR PEQQVDKHHP TTATSADKPL TEAQWLVRFI FLESIAGVPG MVAGMLRHLH
SLRRLKRDNG WIETLLEESY NERMHLLTFM KMCEPGLLMK TLILGAQGVF FNAMFLSYLI
SPKITHRFVG YLEEEAVHTY TRCIREIEEG HLPKWSDEKF EIPEMAVRYW RMPEGKRTMK
DLIHYIRADE AVHRGVNHTL SNLDQKEDPN PFVSDYKEGE GGRRPVNPAL KPTGFERAEV
IG
