AOX1_SAUVE
ID AOX1_SAUVE Reviewed; 349 AA.
AC P22185;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Ubiquinol oxidase 1, mitochondrial;
DE EC=1.10.3.11;
DE AltName: Full=Alternative oxidase 1;
DE Flags: Precursor;
GN Name=AOX1;
OS Sauromatum venosum (Voodoo lily) (Typhonium venosum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Araceae; Aroideae; Areae;
OC Sauromatum.
OX NCBI_TaxID=4463;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 67-75, AND FUNCTION.
RX PubMed=1706518; DOI=10.1073/pnas.88.6.2122;
RA Rhoads D.M., McIntosh L.;
RT "Isolation and characterization of a cDNA clone encoding an alternative
RT oxidase protein of Sauromatum guttatum (Schott).";
RL Proc. Natl. Acad. Sci. U.S.A. 88:2122-2126(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION BY SALICYLIC ACID.
RX PubMed=8448361; DOI=10.1007/bf00014545;
RA Rhoads D.M., McIntosh L.;
RT "The salicylic acid-inducible alternative oxidase gene aox1 and genes
RT encoding pathogenesis-related proteins share regions of sequence similarity
RT in their promoters.";
RL Plant Mol. Biol. 21:615-624(1993).
RN [3]
RP FUNCTION, SUBUNIT, AND ACTIVITY REGULATION.
RX PubMed=12231983; DOI=10.1104/pp.103.3.845;
RA Umbach A.L., Siedow J.N.;
RT "Covalent and noncovalent dimers of the cyanide-resistant alternative
RT oxidase protein in higher plant mitochondria and their relationship to
RT enzyme activity.";
RL Plant Physiol. 103:845-854(1993).
RN [4]
RP IRON-BINDING SITES, COFACTOR, AND 3D-STRUCTURE MODELING.
RX PubMed=7698344; DOI=10.1016/0014-5793(95)00196-g;
RA Siedow J.N., Umbach A.L., Moore A.L.;
RT "The active site of the cyanide-resistant oxidase from plant mitochondria
RT contains a binuclear iron center.";
RL FEBS Lett. 362:10-14(1995).
RN [5]
RP MUTAGENESIS OF GLU-270, AND SUBCELLULAR LOCATION.
RX PubMed=9804791; DOI=10.1074/jbc.273.46.30301;
RA Albury M.S., Affourtit C., Moore A.L.;
RT "A highly conserved glutamate residue (Glu-270) is essential for plant
RT alternative oxidase activity.";
RL J. Biol. Chem. 273:30301-30305(1998).
RN [6]
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).
RN [7]
RP MUTAGENESIS OF CYS-172; GLU-217; TYR-253 AND TYR-275.
RX PubMed=11698414; DOI=10.1074/jbc.m109853200;
RA Albury M.S., Affourtit C., Crichton P.G., Moore A.L.;
RT "Structure of the plant alternative oxidase. Site-directed mutagenesis
RT provides new information on the active site and membrane topology.";
RL J. Biol. Chem. 277:1190-1194(2002).
RN [8]
RP ACTIVITY REGULATION.
RX PubMed=15642340; DOI=10.1016/j.febslet.2004.10.107;
RA Crichton P.G., Affourtit C., Albury M.S., Carre J.E., Moore A.L.;
RT "Constitutive activity of Sauromatum guttatum alternative oxidase in
RT Schizosaccharomyces pombe implicates residues in addition to conserved
RT cysteines in alpha-keto acid activation.";
RL FEBS Lett. 579:331-336(2005).
CC -!- FUNCTION: Catalyzes the cyanide-resistant oxidation of ubiquinol and
CC the reduction of molecular oxygen to water, but does not translocate
CC protons and consequently is not linked to oxidative phosphorylation.
CC May increase respiration when the cytochrome respiratory pathway is
CC restricted, or in response to low temperatures. In S.guttatum the
CC alternative respiratory pathway is thermogenic.
CC {ECO:0000269|PubMed:12231983, ECO:0000269|PubMed:1706518}.
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 -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:7698344};
CC Note=Binds 2 iron ions per subunit. {ECO:0000269|PubMed:7698344};
CC -!- ACTIVITY REGULATION: Not sensitive to pyruvate. Is in a constitutively
CC active state. When the two monomeric subunits are covalently linked by
CC a S-S bond, the enzyme is essentially inactive.
CC {ECO:0000269|PubMed:12231983, ECO:0000269|PubMed:15642340}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:12231983}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:9804791}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:9804791}. Note=Mitochondrial, possibly in the inner
CC surface of the inner mitochondrial membrane.
CC -!- INDUCTION: By salicylic acid. {ECO:0000269|PubMed:8448361}.
CC -!- MISCELLANEOUS: The 3 alternative oxidase proteins detected in
CC S.guttatum, with apparent MW of 35 kDa, 36 kDa and 37 kDa, may be post-
CC translationally modified products of the same AOX1 gene.
CC -!- SIMILARITY: Belongs to the alternative oxidase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The beetle's brothel - Issue
CC 107 of July 2009;
CC URL="https://web.expasy.org/spotlight/back_issues/107";
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; M60330; AAA34048.1; -; mRNA.
DR EMBL; Z15117; CAA78823.1; -; Genomic_DNA.
DR PIR; A39158; A39158.
DR PIR; S30143; S30143.
DR AlphaFoldDB; P22185; -.
DR SMR; P22185; -.
DR BioCyc; MetaCyc:MON-10382; -.
DR BRENDA; 1.10.3.11; 12588.
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 GO; GO:0102721; F:ubiquinol:oxygen oxidoreductase activity; IEA:UniProtKB-EC.
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.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Electron transport; Iron;
KW Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Oxidoreductase; Respiratory chain; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..63
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 64..349
FT /note="Ubiquinol oxidase 1, mitochondrial"
FT /id="PRO_0000001736"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 63..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 178
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 217
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 217
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 220
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 268
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 319
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 319
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 322
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT DISULFID 122
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q41224"
FT MUTAGEN 172
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:11698414"
FT MUTAGEN 217
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11698414"
FT MUTAGEN 253
FT /note="Y->F: No effect."
FT /evidence="ECO:0000269|PubMed:11698414"
FT MUTAGEN 270
FT /note="E->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9804791"
FT MUTAGEN 275
FT /note="Y->F: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11698414"
FT CONFLICT 2
FT /note="M -> I (in Ref. 2; CAA78823)"
FT /evidence="ECO:0000305"
FT CONFLICT 7
FT /note="V -> A (in Ref. 2; CAA78823)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="G -> R (in Ref. 2; CAA78823)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="P -> R (in Ref. 2; CAA78823)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="S -> N (in Ref. 2; CAA78823)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 38931 MW; 6E70B2B7A858B273 CRC64;
MMSSRLVGTA LCRQLSHVPV PQYLPALRPT ADTASSLLHG CSAAAPAQRA GLWPPSWFSP
PRHASTLSAP AQDGGKEKAA GTAGKVPPGE DGGAEKEAVV SYWAVPPSKV SKEDGSEWRW
TCFRPWETYQ ADLSIDLHKH HVPTTILDKL ALRTVKALRW PTDIFFQRRY ACRAMMLETV
AAVPGMVGGV LLHLKSLRRF EHSGGWIRAL LEEAENERMH LMTFMEVAQP RWYERALVLA
VQGVFFNAYF LGYLLSPKFA HRVVGYLEEE AIHSYTEFLK DIDSGAIQDC PAPAIALDYW
RLPQGSTLRD VVTVVRADEA HHRDVNHFAS DVHYQDLELK TTPAPLGYH
