AOX1B_ARATH
ID AOX1B_ARATH Reviewed; 325 AA.
AC O23913; Q4PSN3;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Ubiquinol oxidase 1b, mitochondrial;
DE EC=1.10.3.11;
DE AltName: Full=Alternative oxidase 1b;
DE Flags: Precursor;
GN Name=AOX1B; OrderedLocusNames=At3g22360; ORFNames=MCB17.10;
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], INDUCTION BY ANTIMYCIN A, AND TISSUE
RP SPECIFICITY.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
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 [4]
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 [5]
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 [6]
RP DEVELOPMENTAL STAGE, AND INDUCTION BY ANTIMYCIN A.
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
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:0000250|UniProtKB:Q41224}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:14671022}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:14671022}. Note=Mitochondrial, possibly in the
CC inner surface of the inner mitochondrial membrane.
CC -!- TISSUE SPECIFICITY: Expressed in flowers. Detected only in stamen.
CC {ECO:0000269|PubMed:16859634, ECO:0000269|PubMed:9349280}.
CC -!- DEVELOPMENTAL STAGE: Expressed during early flower development. Not
CC detected during germination. {ECO:0000269|PubMed:11434463,
CC ECO:0000269|PubMed:16859634}.
CC -!- INDUCTION: No effect of antimycin A, ethylene or cold treatments.
CC {ECO:0000269|PubMed:11434463, ECO:0000269|PubMed:21814799,
CC ECO:0000269|PubMed:9349280}.
CC -!- SIMILARITY: Belongs to the alternative oxidase family. {ECO:0000305}.
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DR EMBL; D89875; BAA22624.1; -; Genomic_DNA.
DR EMBL; AB022215; BAB01774.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76626.1; -; Genomic_DNA.
DR EMBL; DQ056603; AAY78751.1; -; mRNA.
DR RefSeq; NP_188875.1; NM_113134.2.
DR AlphaFoldDB; O23913; -.
DR SMR; O23913; -.
DR BioGRID; 7137; 10.
DR IntAct; O23913; 10.
DR STRING; 3702.AT3G22360.1; -.
DR PaxDb; O23913; -.
DR PRIDE; O23913; -.
DR ProteomicsDB; 240877; -.
DR EnsemblPlants; AT3G22360.1; AT3G22360.1; AT3G22360.
DR GeneID; 821805; -.
DR Gramene; AT3G22360.1; AT3G22360.1; AT3G22360.
DR KEGG; ath:AT3G22360; -.
DR Araport; AT3G22360; -.
DR TAIR; locus:2087882; AT3G22360.
DR eggNOG; ENOG502QSB5; Eukaryota.
DR HOGENOM; CLU_041974_0_1_1; -.
DR InParanoid; O23913; -.
DR OMA; PNWFERA; -.
DR OrthoDB; 943747at2759; -.
DR PhylomeDB; O23913; -.
DR PRO; PR:O23913; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O23913; baseline and differential.
DR Genevisible; O23913; 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; HDA: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; 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.
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..44
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 45..325
FT /note="Ubiquinol oxidase 1b, mitochondrial"
FT /id="PRO_0000001732"
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"
FT DISULFID 98
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q41224"
SQ SEQUENCE 325 AA; 37432 MW; 05B0826FDFB4A1F2 CRC64;
MMMSRRYGAK LMETAVTHSH LLNPRVPLVT ENIRVPAMGV VRVFSKMTFE KKKTTEEKGS
SGGKADQGNK GEQLIVSYWG VKPMKITKED GTEWKWSCFR PWETYKSDLT IDLKKHHVPS
TLPDKLAYWT VKSLRWPTDL FFQRRYGCRA MMLETVAAVP GMVGGMLVHC KSLRRFEQSG
GWIKALLEEA ENERMHLMTF MEVAKPNWYE RALVIAVQGI FFNAYFLGYL ISPKFAHRMV
GYLEEEAIHS YTEFLKELDN GNIENVPAPA IAIDYWRLEA DATLRDVVMV VRADEAHHRD
VNHYASDIHY QGRELKEAPA PIGYH
