COX1_DRONO
ID COX1_DRONO Reviewed; 337 AA.
AC O03524;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 105.
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 Dromaius novaehollandiae (Emu).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Casuariiformes; Dromaiidae; Dromaius.
OX NCBI_TaxID=8790;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lee K., Feinstein J., Cracraft J.;
RT "Phylogenetic relationships of the ratite birds: resolving conflicts
RT between molecular and morphological data sets.";
RL (In) Mindell D.P. (eds.);
RL Avian molecular evolution and systematics, pp.1-1, Academic Press, New York
RL (1997).
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; U76059; AAB61319.1; -; Genomic_DNA.
DR AlphaFoldDB; O03524; -.
DR SMR; O03524; -.
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 Calcium; Copper; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Respiratory chain; Sodium;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..>337
FT /note="Cytochrome c oxidase subunit 1"
FT /id="PRO_0000183326"
FT TOPO_DOM 1..12
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TRANSMEM 13..41
FT /note="Helical; Name=I"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TOPO_DOM 42..51
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TRANSMEM 52..87
FT /note="Helical; Name=II"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TOPO_DOM 88..95
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TRANSMEM 96..118
FT /note="Helical; Name=III"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TOPO_DOM 119..141
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TRANSMEM 142..171
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TOPO_DOM 172..183
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TRANSMEM 184..213
FT /note="Helical; Name=V"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TOPO_DOM 214..228
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TRANSMEM 229..262
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TOPO_DOM 263..270
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TRANSMEM 271..287
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TOPO_DOM 288..299
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TRANSMEM 300..328
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TOPO_DOM 329..>337
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT BINDING 41
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT BINDING 46
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT BINDING 62
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 BINDING 241
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT BINDING 245
FT /ligand="O2"
FT /ligand_id="ChEBI:CHEBI:15379"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT BINDING 291
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT BINDING 292
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT CROSSLNK 241..245
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT NON_TER 337
SQ SEQUENCE 337 AA; 36786 MW; 662D7FDD03F7BE02 CRC64;
MTFITRWFFS TNHKDIGTLY LIFGAWAGMV GTALSLLIRA ELGQPGTLLG DDQIYNVVVT
AHAFVMIFFM VMPVMIGGFG NWLVPLMIGA PDMAFPRMNN MSFWLLPPSF LLLLASSTVE
AGAGTGWTVY PPLAGNLAHA GASVDLAIFS LHLAGVSSIL GAINFITTAI NMKPPALTQY
QTPLFVWSVL ITAILLLLSL PVLAAGITML LTDRNLNTTF FDPAGGGDPV LYQHLFWFFG
HPEVYILILP GFGMISHVVT YYAGKKEPFG YMGMVWAMLS IGFLGFIVWA HHMFTVGMDV
DTRAYFTSAT MIIAIPTGIK VFSWLATLHG GTIKWDP
