COX1_CHRKN
ID COX1_CHRKN Reviewed; 219 AA.
AC Q9B229; Q85KD6;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Cytochrome c oxidase subunit 1;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c oxidase polypeptide I;
DE Flags: Fragment;
GN Name=COI {ECO:0000312|EMBL:AAK16643.1};
OS Chrysomela knabi (Leaf beetle).
OG Mitochondrion {ECO:0000312|EMBL:AAK16643.1}.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Chrysomeloidea; Chrysomelidae; Chrysomelinae; Chrysomelini; Chrysomela.
OX NCBI_TaxID=153783;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAP13120.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-154.
RC STRAIN=Isolate JJG237 {ECO:0000269|PubMed:12967617};
RX PubMed=12967617; DOI=10.1016/s1055-7903(03)00256-2;
RA Gillespie J.J., Kjer K.M., Duckett C.N., Tallamy D.W.;
RT "Convergent evolution of cucurbitacin feeding in spatially isolated
RT rootworm taxa (Coleoptera: Chrysomelidae; Galerucinae, Luperini).";
RL Mol. Phylogenet. Evol. 29:161-175(2003).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAK16643.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-219.
RX PubMed=11259651; DOI=10.1073/pnas.061034598;
RA Termonia A., Hsiao T.H., Pasteels J.M., Milinkovitch M.C.;
RT "Feeding specialization and host-derived chemical defense in Chrysomeline
RT leaf beetles did not lead to an evolutionary dead end.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3909-3914(2001).
CC -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the
CC mitochondrial electron transport chain which drives oxidative
CC phosphorylation. The respiratory chain contains 3 multisubunit
CC complexes succinate dehydrogenase (complex II, CII), ubiquinol-
CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III,
CC CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to
CC transfer electrons derived from NADH and succinate to molecular oxygen,
CC creating an electrochemical gradient over the inner membrane that
CC drives transmembrane transport and the ATP synthase. Cytochrome c
CC oxidase is the component of the respiratory chain that catalyzes the
CC reduction of oxygen to water. Electrons originating from reduced
CC cytochrome c in the intermembrane space (IMS) are transferred via the
CC dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1
CC to the active site in subunit 1, a binuclear center (BNC) formed by
CC heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2
CC water molecules using 4 electrons from cytochrome c in the IMS and 4
CC protons from the mitochondrial matrix. {ECO:0000250|UniProtKB:P00401}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-
CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034; EC=7.1.1.9;
CC Evidence={ECO:0000250|UniProtKB:P00401};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC Evidence={ECO:0000250|UniProtKB:P00401};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P00401};
CC Note=Binds 2 heme A groups non-covalently per subunit.
CC {ECO:0000250|UniProtKB:P00401};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P00401};
CC Note=Binds a copper B center. {ECO:0000250|UniProtKB:P00401};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000250|UniProtKB:P00401}.
CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC multisubunit enzyme composed of a catalytic core of 3 subunits and
CC several supernumerary subunits. The complex exists as a monomer or a
CC dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1
CC complex, complex III, CIII). {ECO:0000250|UniProtKB:P00401}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00401}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P00401}.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000255|RuleBase:RU000369}.
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DR EMBL; AY242402; AAP13120.1; -; Genomic_DNA.
DR EMBL; AY027627; AAK16643.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9B229; -.
DR SMR; Q9B229; -.
DR UniPathway; UPA00705; -.
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:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.210.10; -; 1.
DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
DR InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
DR InterPro; IPR000883; Cyt_C_Oxase_1.
DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR PANTHER; PTHR10422; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
PE 3: Inferred from homology;
KW Copper; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Respiratory chain;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN <1..>219
FT /note="Cytochrome c oxidase subunit 1"
FT /id="PRO_0000183314"
FT TOPO_DOM <1..1
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT TRANSMEM 2..24
FT /note="Helical; Name=III"
FT /evidence="ECO:0000250"
FT TOPO_DOM 25..47
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250"
FT TRANSMEM 48..77
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000250"
FT TOPO_DOM 78..89
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT TRANSMEM 90..119
FT /note="Helical; Name=V"
FT /evidence="ECO:0000250"
FT TOPO_DOM 120..134
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250"
FT TRANSMEM 135..168
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000250"
FT TOPO_DOM 169..176
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT TRANSMEM 177..193
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000250"
FT TOPO_DOM 194..205
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250"
FT TRANSMEM 206..>219
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 151
FT /ligand="O2"
FT /ligand_id="ChEBI:CHEBI:15379"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT BINDING 197
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 198
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT CROSSLNK 147..151
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT CONFLICT 20
FT /note="I -> L (in Ref. 2; AAK16643)"
FT /evidence="ECO:0000305"
FT CONFLICT 41..46
FT /note="SNIAHG -> ANTAHS (in Ref. 2; AAK16643)"
FT /evidence="ECO:0000305"
FT CONFLICT 81..88
FT /note="MGMKLDRM -> EGMNFEQT (in Ref. 2; AAK16643)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="V -> L (in Ref. 2; AAK16643)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:AAP13120.1"
FT NON_TER 219
FT /evidence="ECO:0000305"
SQ SEQUENCE 219 AA; 24021 MW; 93BD81BF4358C92D CRC64;
FPRMNNMSFW LLPPSLFLLI MSSIVENGAG TGWTVYPPLS SNIAHGGSSV DLAIFSLHLA
GISSILGAIN FITTVINMRP MGMKLDRMPL FVWAVVITAI LLLLSLPVLA GAITMLLTDR
NLNTSFFDPA GGGDPILYQH LFWFFGHPEV YILILPGFGM ISHIISQESS KKEVFGTLGM
IYAMMAIGLL GFIVWAHHMF TVGMDVDTQT YFTSATMII
