AOX_TRYBB
ID AOX_TRYBB Reviewed; 329 AA.
AC Q26710; Q8WPA4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Alternative oxidase, mitochondrial;
DE EC=1.-.-.-;
DE Flags: Precursor;
GN Name=AOX;
OS Trypanosoma brucei brucei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=EATRO 110;
RX PubMed=9010848; DOI=10.1016/s0166-6851(96)02754-5;
RA Chaudhuri M., Hill G.C.;
RT "Cloning, sequencing, and functional activity of the Trypanosoma brucei
RT brucei alternative oxidase.";
RL Mol. Biochem. Parasitol. 83:125-129(1996).
RN [2]
RP SEQUENCE REVISION.
RA Hill G.C., Chaudhuri M., Ott R.;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ILTat 1.4, and TC221;
RX PubMed=12113758; DOI=10.1016/s1383-5769(02)00010-7;
RA Fukai Y., Nihei C., Yabu Y., Suzuki T., Ohta N., Minagawa N., Nagai K.,
RA Kita K.;
RT "Strain-specific difference in amino acid sequences of trypanosome
RT alternative oxidase.";
RL Parasitol. Int. 51:195-199(2002).
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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH IRON IONS.
RX PubMed=23487766; DOI=10.1073/pnas.1218386110;
RA Shiba T., Kido Y., Sakamoto K., Inaoka D.K., Tsuge C., Tatsumi R.,
RA Takahashi G., Balogun E.O., Nara T., Aoki T., Honma T., Tanaka A.,
RA Inoue M., Matsuoka S., Saimoto H., Moore A.L., Harada S., Kita K.;
RT "Structure of the trypanosome cyanide-insensitive alternative oxidase.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:4580-4585(2013).
CC -!- FUNCTION: Catalyzes cyanide-resistant oxygen consumption. May increase
CC respiration when the cytochrome respiratory pathway is restricted, or
CC in response to low temperatures.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:23487766};
CC Note=Binds 2 iron ions per subunit. {ECO:0000269|PubMed:23487766};
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 -!- SIMILARITY: Belongs to the alternative oxidase family. {ECO:0000305}.
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DR EMBL; U52964; AAB46424.2; -; mRNA.
DR EMBL; AB070614; BAB72245.1; -; mRNA.
DR EMBL; AB070617; BAB72256.1; -; mRNA.
DR PDB; 3VV9; X-ray; 2.85 A; A/B/C/D=1-329.
DR PDB; 3VVA; X-ray; 2.59 A; A/B/C/D=1-329.
DR PDB; 3W54; X-ray; 2.30 A; A/B/C/D=1-329.
DR PDB; 5GN7; X-ray; 3.20 A; A/B/C/D=1-329.
DR PDB; 5GN9; X-ray; 3.20 A; A/B/C/D=1-329.
DR PDB; 5ZDP; X-ray; 2.71 A; A/B/C/D=1-329.
DR PDB; 5ZDQ; X-ray; 2.30 A; A/B/C/D=1-329.
DR PDB; 5ZDR; X-ray; 2.59 A; A/B/C/D=1-329.
DR PDBsum; 3VV9; -.
DR PDBsum; 3VVA; -.
DR PDBsum; 3W54; -.
DR PDBsum; 5GN7; -.
DR PDBsum; 5GN9; -.
DR PDBsum; 5ZDP; -.
DR PDBsum; 5ZDQ; -.
DR PDBsum; 5ZDR; -.
DR AlphaFoldDB; Q26710; -.
DR SMR; Q26710; -.
DR BindingDB; Q26710; -.
DR ChEMBL; CHEMBL4295594; -.
DR PRIDE; Q26710; -.
DR OMA; AFNERMH; -.
DR BRENDA; 1.10.3.11; 6519.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:GeneDB.
DR GO; GO:0005739; C:mitochondrion; IDA:GeneDB.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0009916; F:alternative oxidase activity; IDA:GeneDB.
DR GO; GO:0008199; F:ferric iron binding; IDA:GeneDB.
DR GO; GO:0016491; F:oxidoreductase activity; TAS:GeneDB.
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 3D-structure; Disulfide bond; Electron transport; Iron; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW Respiratory chain; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..329
FT /note="Alternative oxidase, mitochondrial"
FT /id="PRO_0000001730"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 300..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 123
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:23487766,
FT ECO:0007744|PDB:3W54"
FT BINDING 162
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:23487766,
FT ECO:0007744|PDB:3W54"
FT BINDING 162
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23487766,
FT ECO:0007744|PDB:3W54"
FT BINDING 165
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:23487766,
FT ECO:0007744|PDB:3W54"
FT BINDING 213
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23487766,
FT ECO:0007744|PDB:3W54"
FT BINDING 266
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:23487766,
FT ECO:0007744|PDB:3W54"
FT BINDING 266
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23487766,
FT ECO:0007744|PDB:3W54"
FT BINDING 269
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23487766,
FT ECO:0007744|PDB:3W54"
FT DISULFID 95
FT /note="Interchain"
FT /evidence="ECO:0000255"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:3W54"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:3W54"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:3W54"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:3W54"
FT HELIX 83..102
FT /evidence="ECO:0007829|PDB:3W54"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:3W54"
FT HELIX 112..126
FT /evidence="ECO:0007829|PDB:3W54"
FT HELIX 129..144
FT /evidence="ECO:0007829|PDB:3W54"
FT HELIX 151..172
FT /evidence="ECO:0007829|PDB:3W54"
FT HELIX 177..200
FT /evidence="ECO:0007829|PDB:3W54"
FT HELIX 202..228
FT /evidence="ECO:0007829|PDB:3W54"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:5GN7"
FT HELIX 241..246
FT /evidence="ECO:0007829|PDB:3W54"
FT HELIX 255..281
FT /evidence="ECO:0007829|PDB:3W54"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:5GN7"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:3W54"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:3VV9"
SQ SEQUENCE 329 AA; 37590 MW; 5F0DA555B6A3E79C CRC64;
MFRNHASRIT AAAAPWVLRT ACRQKSDAKT PVWGHTQLNR LSFLETVPVV PLRVSDESSE
DRPTWSLPDI ENVAITHKKP NGLVDTLAYR SVRTCRWLFD TFSLYRFGSI TESKVISRCL
FLETVAGVPG MVGGMLRHLS SLRYMTRDKG WINTLLVEAE NERMHLMTFI ELRQPGLPLR
VSIIITQAIM YLFLLVAYVI SPRFVHRFVG YLEEEAVITY TGVMRAIDEG RLRPTKNDVP
EVARVYWNLS KNATFRDLIN VIRADEAEHR VVNHTFADMH EKRLQNSVNP FVVLKKNPEE
MYSNQPSGKT RTDFGSEGAK TASNVNKHV
