AOX2_SOYBN
ID AOX2_SOYBN Reviewed; 333 AA.
AC Q41266;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 03-AUG-2022, entry version 110.
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;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=9193084; DOI=10.1104/pp.114.2.455;
RA Finnegan P.M., Whelan J., Millar A.H., Zhang Q., Smith M.K., Wiskich J.T.,
RA Day D.A.;
RT "Differential expression of the multigene family encoding the soybean
RT mitochondrial alternative oxidase.";
RL Plant Physiol. 114:455-466(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 206-245.
RX PubMed=8580775; DOI=10.1007/bf00206244;
RA Whelan J., Millar A.H., Day D.A.;
RT "The alternative oxidase is encoded in a multigene family in soybean.";
RL Planta 198:197-201(1996).
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=9765553; DOI=10.1104/pp.118.2.675;
RA McCabe T.C., Finnegan P.M., Harvey Millar A., Day D.A., Whelan J.;
RT "Differential expression of alternative oxidase genes in soybean cotyledons
RT during postgerminative development.";
RL Plant Physiol. 118:675-682(1998).
RN [4]
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).
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 {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}. Note=Mitochondrial, possibly
CC in the inner surface of the inner mitochondrial membrane.
CC -!- DEVELOPMENTAL STAGE: Increased expression in developing cotyledons
CC between days 5 and 7 but thereafter relatively constant.
CC {ECO:0000269|PubMed:9765553}.
CC -!- SIMILARITY: Belongs to the alternative oxidase family. {ECO:0000305}.
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DR EMBL; U87906; AAB97285.1; -; mRNA.
DR EMBL; S81470; AAB36072.1; -; Genomic_DNA.
DR PIR; T08850; T08850.
DR RefSeq; NP_001235766.1; NM_001248837.1.
DR AlphaFoldDB; Q41266; -.
DR SMR; Q41266; -.
DR STRING; 3847.GLYMA08G07700.1; -.
DR PRIDE; Q41266; -.
DR GeneID; 547897; -.
DR KEGG; gmx:547897; -.
DR eggNOG; ENOG502QSB5; Eukaryota.
DR InParanoid; Q41266; -.
DR OrthoDB; 943747at2759; -.
DR Proteomes; UP000008827; Unplaced.
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; IBA:GO_Central.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0009916; F:alternative oxidase activity; IBA:GO_Central.
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; 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 Direct protein sequencing; Disulfide bond; Electron transport; Iron;
KW Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Oxidoreductase; Reference proteome; Respiratory chain; Transit peptide;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..333
FT /note="Ubiquinol oxidase 2, mitochondrial"
FT /id="PRO_0000001738"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 162
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 201
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 201
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 204
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 252
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 303
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 303
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 306
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT DISULFID 106
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q41224"
SQ SEQUENCE 333 AA; 38128 MW; 40F651E474EBB752 CRC64;
MKLTALNSTV RRALLNGRNQ NGNRLGSAAL MPYAAAETRL LCAGGANGWF FYWKRTMVSP
AEAKVPEKEK EKEKAKAEKS VVESSYWGIS RPKVVREDGT EWPWNCFMPW ESYRSNVSID
LTKHHVPKNV LDKVAYRTVK LLRIPTDLFF KRRYGCRAMM LETVAAVPGM VGGMLLHLRS
LRKFQQSGGW IKALLEEAEN ERMHLMTMVE LVKPKWYERL LVLAVQGVFF NAFFVLYILS
PKVAHRIVGY LEEEAIHSYT EYLKDLESGA IENVPAPAIA IDYWRLPKDA RLKDVITVIR
ADEAHHRDVN HFASDIHFQG KELREAPAPI GYH
