AOX3_SOYBN
ID AOX3_SOYBN Reviewed; 326 AA.
AC O03376;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Alternative oxidase 3, mitochondrial;
DE EC=1.10.3.11;
DE Flags: Precursor;
GN Name=AOX3;
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 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 [3]
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 [4]
RP MUTAGENESIS OF CYS-99, DISULFIDE BOND, AND ACTIVITY REGULATION.
RX PubMed=10431811; DOI=10.1016/s0014-5793(99)00808-x;
RA Djajanegara I., Holtzapffel R., Finnegan P.M., Hoefnagel M.H.,
RA Berthold D.A., Wiskich J.T., Day D.A.;
RT "A single amino acid change in the plant alternative oxidase alters the
RT specificity of organic acid activation.";
RL FEBS Lett. 454:220-224(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:0000269|PubMed:10431811}.
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: Continuous increase of expression in developing
CC cotyledons until day 20. {ECO:0000269|PubMed:9765553}.
CC -!- SIMILARITY: Belongs to the alternative oxidase family. {ECO:0000305}.
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DR EMBL; U87907; AAB97286.1; -; mRNA.
DR PIR; T08849; T08849.
DR RefSeq; NP_001238460.1; NM_001251531.1.
DR AlphaFoldDB; O03376; -.
DR SMR; O03376; -.
DR STRING; 3847.GLYMA08G07690.1; -.
DR PRIDE; O03376; -.
DR GeneID; 548077; -.
DR KEGG; gmx:548077; -.
DR eggNOG; ENOG502QSB5; Eukaryota.
DR InParanoid; O03376; -.
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 ?..326
FT /note="Alternative oxidase 3, mitochondrial"
FT /id="PRO_0000001739"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 155
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 194
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 194
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 197
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 245
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 296
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 296
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 299
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT DISULFID 99
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:10431811"
FT MUTAGEN 99
FT /note="C->S: Loss of oxidative inactivation and stimulation
FT by pyruvate, but can be activated by succinate."
FT /evidence="ECO:0000269|PubMed:10431811"
SQ SEQUENCE 326 AA; 37057 MW; 8F1CB9EBCBD58A0E CRC64;
MKNVLVRSAA RALLGGGGRS YYRQLSTAAI VEQRHQHGGG AFGSFHLRRM STLPEVKDQH
SEEKKNEVNG TSNAVVTSYW GITRPKVRRE DGTEWPWNCF MPWDSYHSDV SIDVTKHHTP
KSLTDKVAFR AVKFLRVLSD IYFKERYGCH AMMLETIAAV PGMVGGMLLH LKSLRKFQHS
GGWIKALLEE AENERMHLMT MVELVKPSWH ERLLIFTAQG VFFNAFFVFY LLSPKAAHRF
VGYLEEEAVI SYTQHLNAIE SGKVENVPAP AIAIDYWRLP KDATLKDVVT VIRADEAHHR
DVNHFASDIH HQGKELKEAP APIGYH
