COX1_PANBU
ID COX1_PANBU Reviewed; 184 AA.
AC P29649;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=mt-co1; Synonyms=coi, coxi, mtco1;
OS Pantodon buchholzi (Freshwater butterflyfish).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Pantodontidae; Pantodon.
OX NCBI_TaxID=8276;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1663569; DOI=10.1093/oxfordjournals.molbev.a040685;
RA Normark B.B., McCune A.R., Harrison R.G.;
RT "Phylogenetic relationships of neopterygian fishes, inferred from
RT mitochondrial DNA sequences.";
RL Mol. Biol. Evol. 8:819-834(1991).
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:P00396};
CC Note=Binds 2 heme A groups non-covalently per subunit.
CC {ECO:0000250|UniProtKB:P00396};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P00396};
CC Note=Binds a copper B center. {ECO:0000250|UniProtKB:P00396};
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 14 subunits. The complex is composed of
CC a catalytic core of 3 subunits MT-CO1, MT-CO2 and MT-CO3, encoded in
CC the mitochondrial DNA, and 11 supernumerary subunits COX4I, COX5A,
CC COX5B, COX6A, COX6B, COX6C, COX7A, COX7B, COX7C, COX8 and NDUFA4, which
CC are encoded in the nuclear genome. The complex exists as a monomer or a
CC dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and
CC ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex
CC III, CIII), resulting in different assemblies (supercomplex
CC SCI(1)III(2)IV(1) and megacomplex MCI(2)III(2)IV(2)) (By similarity).
CC As a newly synthesized protein, rapidly incorporates into a multi-
CC subunit assembly intermediate in the inner membrane, called MITRAC
CC (mitochondrial translation regulation assembly intermediate of
CC cytochrome c oxidase) complex, whose core components are COA3/MITRAC12
CC and COX14. Within the MITRAC complex, interacts with COA3 and with
CC SMIM20/MITRAC7; the interaction with SMIM20 stabilizes the newly
CC synthesized MT-CO1 and prevents its premature turnover. Interacts with
CC TMEM177 in a COX20-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:P00395, ECO:0000250|UniProtKB:P00396}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00396}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P00396}.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000305}.
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DR EMBL; M64906; AAB01608.1; -; Genomic_DNA.
DR AlphaFoldDB; P29649; -.
DR SMR; P29649; -.
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:0045277; C:respiratory chain complex IV; ISS:UniProtKB.
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; Magnesium; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Respiratory chain; Sodium;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN <1..>184
FT /note="Cytochrome c oxidase subunit 1"
FT /id="PRO_0000183377"
FT TRANSMEM <1..26
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TOPO_DOM 27..34
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TRANSMEM 35..51
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TOPO_DOM 52..63
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TRANSMEM 64..92
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TOPO_DOM 93..100
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TRANSMEM 101..122
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TOPO_DOM 123..135
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TRANSMEM 136..165
FT /note="Helical; Name=X"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TOPO_DOM 166..171
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TRANSMEM 172..>184
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT BINDING 5
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT BINDING 9
FT /ligand="O2"
FT /ligand_id="ChEBI:CHEBI:15379"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT BINDING 55
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT BINDING 56
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT BINDING 133
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared with MT-CO2"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT BINDING 134
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared with MT-CO2"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT BINDING 141
FT /ligand="heme a3"
FT /ligand_id="ChEBI:CHEBI:83282"
FT /ligand_note="high-spin"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT BINDING 143
FT /ligand="Fe(II)-heme a"
FT /ligand_id="ChEBI:CHEBI:61715"
FT /ligand_note="low-spin"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT CROSSLNK 5..9
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT NON_TER 1
FT NON_TER 184
SQ SEQUENCE 184 AA; 20709 MW; 73B1A5B1715ED49A CRC64;
WFFGHPEVYI LILPGFGMIS HIVAYYSGKK EPFGYMGMVW AMMAIGLLGF IVWAHHMFTV
GMDVDTRAYF TSATMIIAIP TGVKVFSWLA TLHGGSIKWD TPMLWALGFI FLFTVGGLTG
IILANSSLDI VLHDTYYVVA HFHYVLSMGA VFAIMGGFVH WFPLFSGYTL HNTWTKIHFG
VMFM
