AOX1_TOBAC
ID AOX1_TOBAC Reviewed; 353 AA.
AC Q41224;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 103.
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 Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Bright Yellow;
RX PubMed=8058837; DOI=10.1104/pp.105.3.867;
RA Vanlerberghe G.C., McIntosh L.;
RT "Mitochondrial electron transport regulation of nuclear gene expression.
RT Studies with the alternative oxidase gene of tobacco.";
RL Plant Physiol. 105:867-874(1994).
RN [2]
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 [3]
RP INDUCTION.
RX PubMed=12226312; DOI=10.1104/pp.111.2.589;
RA Vanlerberghe G.C., McLntosh L.;
RT "Signals regulating the expression of the nuclear gene encoding alternative
RT oxidase of plant mitochondria.";
RL Plant Physiol. 111:589-595(1996).
RN [4]
RP SUBUNIT, DISULFIDE BOND, MUTAGENESIS OF CYS-126 AND CYS-176, AND ACTIVITY
RP REGULATION.
RX PubMed=9724700; DOI=10.2307/3870618;
RA Vanlerberghe G.C., McIntosh L., Yip J.Y.;
RT "Molecular localization of a redox-modulated process regulating plant
RT mitochondrial electron transport.";
RL Plant Cell 10:1551-1560(1998).
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).
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:8058837}.
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:8058837};
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: Stimulated by reduction of the disulfide bond and
CC the presence of pyruvate. {ECO:0000269|PubMed:9724700}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:9724700}.
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: Up-regulated by acetate, citrate, antimycin A, cysteine and
CC H(2)O(2). {ECO:0000269|PubMed:12226312}.
CC -!- SIMILARITY: Belongs to the alternative oxidase family. {ECO:0000305}.
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DR EMBL; S71335; AAC60576.1; -; mRNA.
DR PIR; T04094; T04094.
DR AlphaFoldDB; Q41224; -.
DR SMR; Q41224; -.
DR Proteomes; UP000084051; 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..69
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 70..353
FT /note="Ubiquinol oxidase 1, mitochondrial"
FT /id="PRO_0000001740"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 77..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 182
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 221
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 221
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 224
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 272
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 323
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 323
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 326
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT DISULFID 126
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:9724700"
FT MUTAGEN 126
FT /note="C->A: Loss of disulfide bond formation, activity and
FT stimulation by pyruvate."
FT /evidence="ECO:0000269|PubMed:9724700"
FT MUTAGEN 176
FT /note="C->A: No effect on disulfide bond formation and on
FT stimulation by pyruvate."
FT /evidence="ECO:0000269|PubMed:9724700"
SQ SEQUENCE 353 AA; 39767 MW; 040C82AEF355E37F CRC64;
MMTRGATRMT RTVLGHMGPR YFSTAIFRND AGTGVMSGAA VFMHGVPANP SEKAVVTWVR
HFPVMGSRSA MSMALNDKQH DKKAENGSAA ATGGGDGGDE KSVVSYWGVQ PSKVTKEDGT
EWKWNCFRPW ETYKADLSID LTKHHAPTTF LDKFAYWTVK SLRYPTDIFF QRRYGCRAMM
LETVAAVPGM VGGMLLHCKS LRRFEQSGGW IKTLLDEAEN ERMHLMTFME VAKPNWYERA
LVFAVQGVFF NAYFVTYLLS PKLAHRIVGY LEEEAIHSYT EFLKELDKGN IENVPAPAIA
IDYCRLPKDS TLLDVVLVVR ADEAHHRDVN HFASDIHYQG QQLKDSPAPI GYH
