AOX2_ARATH
ID AOX2_ARATH Reviewed; 353 AA.
AC O22049; Q4PS98;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Ubiquinol oxidase 2, mitochondrial;
DE EC=1.10.3.11;
DE AltName: Full=Alternative oxidase 2;
DE Flags: Precursor;
GN Name=AOX2; OrderedLocusNames=At5g64210; ORFNames=MSJ1.5;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf, and Stem;
RX PubMed=9349280; DOI=10.1023/a:1005818507743;
RA Saisho D., Nambara E., Naito S., Tsutsumi N., Hirai A., Nakazono M.;
RT "Characterization of the gene family for alternative oxidase from
RT Arabidopsis thaliana.";
RL Plant Mol. Biol. 35:585-596(1997).
RN [2]
RP SEQUENCE REVISION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND INDUCTION.
RC STRAIN=cv. Columbia GL1;
RX PubMed=11434463; DOI=10.1266/ggs.76.89;
RA Saisho D., Nakazono M., Lee K.-H., Tsutsumi N., Akita S., Hirai A.;
RT "The gene for alternative oxidase-2 (AOX2) from Arabidopsis thaliana
RT consists of five exons unlike other AOX genes and is transcribed at an
RT early stage during germination.";
RL Genes Genet. Syst. 76:89-97(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
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 INDUCTION BY ABIOTIC STRESSES.
RX PubMed=16027974; DOI=10.1007/s11103-005-5514-7;
RA Clifton R., Lister R., Parker K.L., Sappl P.G., Elhafez D., Millar A.H.,
RA Day D.A., Whelan J.;
RT "Stress-induced co-expression of alternative respiratory chain components
RT in Arabidopsis thaliana.";
RL Plant Mol. Biol. 58:193-212(2005).
RN [8]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=16859634; DOI=10.1016/j.bbabio.2006.03.009;
RA Clifton R., Millar A.H., Whelan J.;
RT "Alternative oxidases in Arabidopsis: a comparative analysis of
RT differential expression in the gene family provides new insights into
RT function of non-phosphorylating bypasses.";
RL Biochim. Biophys. Acta 1757:730-741(2006).
RN [9]
RP INDUCTION BY COLD AND ETHYLENE.
RX PubMed=21814799; DOI=10.1007/s00425-011-1488-7;
RA Wang H., Huang J., Liang X., Bi Y.;
RT "Involvement of hydrogen peroxide, calcium, and ethylene in the induction
RT of the alternative pathway in chilling-stressed Arabidopsis callus.";
RL Planta 235:53-67(2012).
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 (By similarity).
CC {ECO:0000250}.
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:0000250|UniProtKB:Q39219};
CC Note=Binds 2 iron ions per subunit. {ECO:0000250|UniProtKB:Q39219};
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:11434463}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11434463}. Note=Mitochondrial, possibly in the
CC inner surface of the inner mitochondrial membrane.
CC -!- TISSUE SPECIFICITY: Maximally expressed in dry seeds. Detected in
CC roots, stems and leaves. {ECO:0000269|PubMed:11434463,
CC ECO:0000269|PubMed:16859634}.
CC -!- DEVELOPMENTAL STAGE: Expressed predominantly during early stages of
CC germination with maximum level at 12 hours after imbibition and at the
CC latter stages of silique maturation. Accumulates in dry seeds.
CC {ECO:0000269|PubMed:11434463, ECO:0000269|PubMed:16859634}.
CC -!- INDUCTION: No effect of antimycin A, ethylene or cold treatments. Up-
CC regulated by paraquat and cysteine treatments, but down-regulated by
CC erythromycin, citrate, glucose and H(2)O(2) treatments.
CC {ECO:0000269|PubMed:11434463, ECO:0000269|PubMed:16027974,
CC ECO:0000269|PubMed:21814799}.
CC -!- SIMILARITY: Belongs to the alternative oxidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09852.1; Type=Erroneous gene model prediction; 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; AB003176; BAA22636.2; -; Genomic_DNA.
DR EMBL; AB008268; BAB09852.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97855.1; -; Genomic_DNA.
DR EMBL; DQ056738; AAY78882.1; -; mRNA.
DR RefSeq; NP_201226.2; NM_125817.3.
DR AlphaFoldDB; O22049; -.
DR SMR; O22049; -.
DR BioGRID; 21784; 2.
DR IntAct; O22049; 2.
DR STRING; 3702.AT5G64210.1; -.
DR PaxDb; O22049; -.
DR PRIDE; O22049; -.
DR ProteomicsDB; 244415; -.
DR EnsemblPlants; AT5G64210.1; AT5G64210.1; AT5G64210.
DR GeneID; 836542; -.
DR Gramene; AT5G64210.1; AT5G64210.1; AT5G64210.
DR KEGG; ath:AT5G64210; -.
DR Araport; AT5G64210; -.
DR TAIR; locus:2173353; AT5G64210.
DR eggNOG; ENOG502QSB5; Eukaryota.
DR HOGENOM; CLU_041974_0_1_1; -.
DR InParanoid; O22049; -.
DR OMA; FNIRSEH; -.
DR OrthoDB; 943747at2759; -.
DR PhylomeDB; O22049; -.
DR PRO; PR:O22049; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O22049; baseline and differential.
DR Genevisible; O22049; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
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:TAIR.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0009916; F:alternative oxidase activity; ISS:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106292; F:superoxide-generating NADPH oxidase activity; IDA:TAIR.
DR GO; GO:0102721; F:ubiquinol:oxygen oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0010230; P:alternative respiration; ISS:TAIR.
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 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..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 22..353
FT /note="Ubiquinol oxidase 2, mitochondrial"
FT /id="PRO_0000001734"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 182
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 221
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 221
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 224
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 272
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 323
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 323
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 326
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT DISULFID 126
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q41224"
SQ SEQUENCE 353 AA; 40087 MW; DF7ACB113E57A133 CRC64;
MSQLITKAAL RVLLVCGRGN CNMFVSSVSS TSVMKSPYEI TAPMRIHDWC GGFGDFKIGS
KHVQGNFNLR WMGMSSASAM EKKDENLTVK KGQNGGGSVA VPSYWGIETA KMKITRKDGS
DWPWNCFMPW ETYQANLSID LKKHHVPKNI ADKVAYRIVK LLRIPTDIFF QRRYGCRAMM
LETVAAVPGM VGGMLLHLKS IRKFEHSGGW IKALLEEAEN ERMHLMTMME LVKPKWYERL
LVMLVQGIFF NSFFVCYVIS PRLAHRVVGY LEEEAIHSYT EFLKDIDNGK IENVAAPAIA
IDYWRLPKDA TLKDVVTVIR ADEAHHRDVN HFASDIRNQG KELREAAAPI GYH
