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 22-APR-2020, entry version 144. 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 SMR; O22049; -. DR BioGrid; 21784; 2. DR IntAct; O22049; 2. DR STRING; 3702.AT5G64210.1; -. DR PaxDb; O22049; -. 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; ENOG410IIJ8; Eukaryota. DR eggNOG; ENOG410YFEH; LUCA. DR HOGENOM; CLU_041974_0_1_1; -. DR InParanoid; O22049; -. DR KO; K17893; -. DR OMA; KYGCRAM; -. 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: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: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 METAL 182 FT /note="Iron 1" FT /evidence="ECO:0000250|UniProtKB:Q26710" FT METAL 221 FT /note="Iron 1" FT /evidence="ECO:0000250|UniProtKB:Q26710" FT METAL 221 FT /note="Iron 2" FT /evidence="ECO:0000250|UniProtKB:Q26710" FT METAL 224 FT /note="Iron 1; via pros nitrogen" FT /evidence="ECO:0000250|UniProtKB:Q26710" FT METAL 272 FT /note="Iron 2" FT /evidence="ECO:0000250|UniProtKB:Q26710" FT METAL 323 FT /note="Iron 1" FT /evidence="ECO:0000250|UniProtKB:Q26710" FT METAL 323 FT /note="Iron 2" FT /evidence="ECO:0000250|UniProtKB:Q26710" FT METAL 326 FT /note="Iron 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 //