AOX_TRAHO
ID AOX_TRAHO Reviewed; 318 AA.
AC D5JAJ1; L7JVY0;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Ubiquinol oxidase;
DE EC=1.10.3.11;
DE AltName: Full=Alternative oxidase;
GN Name=AOX; ORFNames=THOM_2158;
OS Trachipleistophora hominis (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Pleistophoridae;
OC Trachipleistophora.
OX NCBI_TaxID=72359;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=20169184; DOI=10.1371/journal.ppat.1000761;
RA Williams B.A., Elliot C., Burri L., Kido Y., Kita K., Moore A.L.,
RA Keeling P.J.;
RT "A broad distribution of the alternative oxidase in microsporidian
RT parasites.";
RL PLoS Pathog. 6:E1000761-E1000761(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23133373; DOI=10.1371/journal.ppat.1002979;
RA Heinz E., Williams T.A., Nakjang S., Noel C.J., Swan D.C., Goldberg A.V.,
RA Harris S.R., Weinmaier T., Markert S., Becher D., Bernhardt J., Dagan T.,
RA Hacker C., Lucocq J.M., Schweder T., Rattei T., Hall N., Hirt R.P.,
RA Embley T.M.;
RT "The genome of the obligate intracellular parasite Trachipleistophora
RT hominis: new insights into microsporidian genome dynamics and reductive
RT evolution.";
RL PLoS Pathog. 8:E1002979-E1002979(2012).
CC -!- FUNCTION: Alternative oxidase which function may be to reoxidize
CC reducing equivalents produced by glycolysis such as ubiquinol.
CC {ECO:0000269|PubMed:20169184}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a ubiquinol + O2 = 2 a ubiquinone + 2 H2O;
CC Xref=Rhea:RHEA:30255, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16389,
CC ChEBI:CHEBI:17976; EC=1.10.3.11;
CC Evidence={ECO:0000269|PubMed:20169184};
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: Found as monomers and homodimers.
CC {ECO:0000269|PubMed:20169184}.
CC -!- SUBCELLULAR LOCATION: Mitosome membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}. Note=Microsporidia do not contain
CC mitochondria, but highly reduced mitochondrial organelles called
CC mitosomes.
CC -!- SIMILARITY: Belongs to the alternative oxidase family. {ECO:0000305}.
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DR EMBL; GU221911; ADE43749.1; -; Genomic_DNA.
DR EMBL; JH994008; ELQ74912.1; -; Genomic_DNA.
DR AlphaFoldDB; D5JAJ1; -.
DR SMR; D5JAJ1; -.
DR STRING; 72359.D5JAJ1; -.
DR EnsemblFungi; ELQ74912; ELQ74912; THOM_2158.
DR KEGG; ag:ADE43749; -.
DR VEuPathDB; MicrosporidiaDB:THOM_2158; -.
DR HOGENOM; CLU_874887_0_0_1; -.
DR OMA; RISKDYW; -.
DR Proteomes; UP000011185; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032047; C:mitosome; IEA:UniProtKB-KW.
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 GO; GO:0102721; F:ubiquinol:oxygen oxidoreductase activity; IEA:UniProtKB-EC.
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 Electron transport; Iron; Membrane; Metal-binding; Mitosome;
KW Oxidoreductase; Reference proteome; Respiratory chain; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..318
FT /note="Ubiquinol oxidase"
FT /id="PRO_0000415493"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 154
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 193
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 193
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
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 244
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 295
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 295
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 298
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
SQ SEQUENCE 318 AA; 36489 MW; 4F240AE050534F4E CRC64;
MLTKNNSLLS RLPARISFGL KISNKNVNST YSNVASAYCE GATYKKNGVS RLQNELLSQK
TNNETIPVPL QHFIRPAAKH SIFTQIKGYG ERSRPEFERP ITLEELKSLD YESGKHFVPQ
SFSDTFAYLI VKGLRAFADL YFQKDYVRRV VVLETVAAIP GMVGGMFRHL YSLRNLEDNG
EAIKKLVLEA ENERQHLLTF LAVLKPNVLD RMLIKLGQFL FFNGYMVFYF VAPRTAHRFV
GYLEEEAVRS YDAFEEEILL GHIKNVEAPR ISKDYWNLPE EAMLIDVVRA VRADEAEHRD
VNHKMADSKS FSLAHNPY
