AOX1_MANIN
ID AOX1_MANIN Reviewed; 318 AA.
AC Q40294;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Ubiquinol oxidase, mitochondrial;
DE EC=1.10.3.11;
DE AltName: Full=Alternative oxidase;
DE Flags: Precursor;
GN Name=AOMI 1;
OS Mangifera indica (Mango).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Anacardiaceae; Mangifera.
OX NCBI_TaxID=29780;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Manila;
RX PubMed=8555961; DOI=10.1007/bf00191562;
RA Cruz-Hernandez A., Gomez-Lim M.A.;
RT "Alternative oxidase from mango (Mangifera indica, L.) is differentially
RT regulated during fruit ripening.";
RL Planta 197:569-576(1995).
RN [2]
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 -!- INDUCTION: Increases during ripening.
CC -!- SIMILARITY: Belongs to the alternative oxidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA55892.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X79329; CAA55892.1; ALT_INIT; mRNA.
DR PIR; S45035; S45035.
DR AlphaFoldDB; Q40294; -.
DR SMR; Q40294; -.
DR PRIDE; Q40294; -.
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:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0009916; F:alternative oxidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0102721; F:ubiquinol:oxygen oxidoreductase activity; IEA:UniProtKB-EC.
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.
DR PIRSF; PIRSF005229; AOX; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Electron transport; Iron; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW Respiratory chain; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 47..318
FT /note="Ubiquinol oxidase, mitochondrial"
FT /id="PRO_0000001735"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 147
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 186
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 186
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
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 237
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 288
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 288
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="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT DISULFID 91
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q41224"
SQ SEQUENCE 318 AA; 36640 MW; B11DA2DEDD6F03E0 CRC64;
MTVMRGLLNG GRYGNRYIWT AISLRHPEVM EGNGLESAVM QWRRMLSNAG GAEAQVKEQK
EEKKDAMVSN YWGISRPKIT REDGSEWPWN CFMPWETYRS DLSIDLKKHH VPRTFMDKFA
YRTVKILRVP TDIFFQRRYG CRAMMLETVA AVPGMVGGML LHLKSLRKLE QSGGWIKALL
EEAENERMHL MTMVELVQPK WYERLLVLAV QGVFFNSFFV LYVLSPKLAH RIVGYLEEEA
IHSYTEYLKD IDSGAIKNIP APAIAIDYWR LPKDATLKDV ITVVRADEAH HRDVNHFASD
VQVQGKELRD APAPVGYH
