AOX1_SOYBN
ID AOX1_SOYBN Reviewed; 321 AA.
AC Q07185; Q41265;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Ubiquinol oxidase 1, mitochondrial;
DE EC=1.10.3.11;
DE AltName: Full=Alternative oxidase 1;
DE Flags: Precursor;
GN Name=AOX1;
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].
RC TISSUE=Shoot;
RX PubMed=8290651; DOI=10.1104/pp.103.4.1481;
RA Whelan J.M., McIntosh L., Day D.A.;
RT "Sequencing of a soybean alternative oxidase cDNA clone.";
RL Plant Physiol. 103:1481-1481(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 194-233.
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 FUNCTION, SUBUNIT, AND ACTIVITY REGULATION.
RX PubMed=12231983; DOI=10.1104/pp.103.3.845;
RA Umbach A.L., Siedow J.N.;
RT "Covalent and noncovalent dimers of the cyanide-resistant alternative
RT oxidase protein in higher plant mitochondria and their relationship to
RT enzyme activity.";
RL Plant Physiol. 103:845-854(1993).
RN [4]
RP IRON-BINDING SITES, AND COFACTOR.
RX PubMed=7698344; DOI=10.1016/0014-5793(95)00196-g;
RA Siedow J.N., Umbach A.L., Moore A.L.;
RT "The active site of the cyanide-resistant oxidase from plant mitochondria
RT contains a binuclear iron center.";
RL FEBS Lett. 362:10-14(1995).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=12223863; DOI=10.1104/pp.115.3.1145;
RA Hoefnagel M., Rich P.R., Zhang Q., Wiskich J.T.;
RT "Substrate kinetics of the plant mitochondrial alternative oxidase and the
RT effects of pyruvate.";
RL Plant Physiol. 115:1145-1153(1997).
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).
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.
CC {ECO:0000269|PubMed:12223863, ECO:0000269|PubMed:12231983}.
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 Evidence={ECO:0000269|PubMed:12223863};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:7698344};
CC Note=Binds 2 iron ions per subunit. {ECO:0000269|PubMed:7698344};
CC -!- ACTIVITY REGULATION: When the two monomeric subunits are covalently
CC linked by a S-S bond, the enzyme is essentially inactive. When the
CC disulfide bond is reduced, its component sulfhydryls can associate with
CC K-keto acids through formation of a thiohemiacetal, resulting in enzyme
CC activation. Pyruvate increases Vmax, but not the substrate affinity.
CC {ECO:0000269|PubMed:12223863, ECO:0000269|PubMed:12231983}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=115.3 uM for O(2) (in the presence of 0.025% N,N',N'-
CC polyoxyethylene(l0)-N-tallow-1,3- diamino-propane)
CC {ECO:0000269|PubMed:12223863};
CC Vmax=32.3 umol/min/mg enzyme with O(2) as substrate
CC {ECO:0000269|PubMed:12223863};
CC pH dependence:
CC Optimum pH is 7.0-7.5. {ECO:0000269|PubMed:12223863};
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:12231983}.
CC -!- INTERACTION:
CC Q07185; O64471: MTX1; Xeno; NbExp=3; IntAct=EBI-2123914, EBI-2123898;
CC Q07185; F4KCL7: OM64; Xeno; NbExp=2; IntAct=EBI-2123914, EBI-2124066;
CC Q07185; P82805: TOM20-4; Xeno; NbExp=2; IntAct=EBI-2123914, EBI-2351908;
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 -!- INDUCTION: By salicylic acid.
CC -!- SIMILARITY: Belongs to the alternative oxidase family. {ECO:0000305}.
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DR EMBL; X68702; CAA48653.1; -; mRNA.
DR EMBL; S81466; AAC34192.1; -; mRNA.
DR RefSeq; NP_001236166.1; NM_001249237.1.
DR AlphaFoldDB; Q07185; -.
DR SMR; Q07185; -.
DR BioGRID; 989647; 5.
DR IntAct; Q07185; 5.
DR STRING; 3847.GLYMA04G14800.1; -.
DR PRIDE; Q07185; -.
DR GeneID; 547924; -.
DR KEGG; gmx:547924; -.
DR eggNOG; ENOG502QSB5; Eukaryota.
DR InParanoid; Q07185; -.
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 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..41
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 42..321
FT /note="Ubiquinol oxidase 1, mitochondrial"
FT /id="PRO_0000001737"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 150
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 189
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 189
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 192
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 240
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 291
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 291
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 294
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT DISULFID 94
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q41224"
SQ SEQUENCE 321 AA; 36437 MW; EE0FF981F0C2D0E7 CRC64;
MMMMMSRSGA NRVANTAMFV AKGLSGEVGG LRALYGGGVR SESTLALSEK EKIEKKVGLS
SAGGNKEEKV IVSYWGIQPS KITKKDGTEW KWNCFSPWGT YKADLSIDLE KHMPPTTFLD
KMAFWTVKVL RYPTDVFFQR RYGCRAMMLE TVAAVPGMVA GMLLHCKSLR RFEHSGGWFK
ALLEEAENER MHLMTFMEVA KPKWYERALV ITVQGVFFNA YFLGYLLSPK FAHRMFGYLE
EEAIHSYTEF LKELDKGNIE NVPAPAIAID YWQLPPGSTL RDVVMVVRAD EAHHRDVNHF
ASDIHYQGRE LREAAAPIGY H
