ID   COX1_THETH              Reviewed;         108 AA.
AC   Q56408;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 2.
DT   28-JUN-2023, entry version 135.
DE   RecName: Full=Cytochrome c oxidase subunit 1;
DE            EC=7.1.1.9;
DE   AltName: Full=Cytochrome c ba(3) subunit I;
DE   AltName: Full=Cytochrome c oxidase polypeptide I;
DE   AltName: Full=Cytochrome cba3 subunit 1;
DE   Flags: Fragment;
GN   Name=cbaA;
OS   Thermus thermophilus.
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=VK1;
RX   PubMed=9208917; DOI=10.1111/j.1432-1033.1997.00291.x;
RA   Serganov A., Rak A., Garber M.B., Reinbolt J., Ehresmann B., Ehresmann C.,
RA   Grunberg-Manago M., Portier C.;
RT   "Ribosomal protein S15 from Thermus thermophilus -- cloning, sequencing,
RT   overexpression of the gene and RNA-binding properties of the protein.";
RL   Eur. J. Biochem. 246:291-300(1997).
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   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC       Note=Binds 2 heme groups. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC       Note=Binds a copper B center. {ECO:0000250};
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC       {ECO:0000305}.
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DR   EMBL; Z84206; CAB06339.1; -; Genomic_DNA.
DR   PIR; T52481; T52481.
DR   PDB; 1XME; X-ray; 2.30 A; A=1-108.
DR   PDBsum; 1XME; -.
DR   AlphaFoldDB; Q56408; -.
DR   SMR; Q56408; -.
DR   IntAct; Q56408; 2.
DR   DrugBank; DB02451; B-nonylglucoside.
DR   UniPathway; UPA00705; -.
DR   EvolutionaryTrace; Q56408; -.
DR   GO; GO:0005886; C:plasma 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; Cytochrome c oxidase-like, subunit I domain; 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   PANTHER; PTHR10422; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR   PANTHER; PTHR10422:SF40; CYTOCHROME C OXIDASE SUBUNIT I; 1.
DR   Pfam; PF00115; COX1; 1.
DR   SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 1.
DR   PROSITE; PS50855; COX1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Copper; Electron transport; Heme;
KW   Hydrogen ion transport; Ion transport; Iron; Membrane; Metal-binding;
KW   Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           <1..>108
FT                   /note="Cytochrome c oxidase subunit 1"
FT                   /id="PRO_0000183463"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         49
FT                   /ligand="heme a3"
FT                   /ligand_id="ChEBI:CHEBI:83282"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   BINDING         51
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         108
FT   HELIX           9..31
FT                   /evidence="ECO:0007829|PDB:1XME"
FT   HELIX           34..36
FT                   /evidence="ECO:0007829|PDB:1XME"
FT   HELIX           37..40
FT                   /evidence="ECO:0007829|PDB:1XME"
FT   HELIX           45..53
FT                   /evidence="ECO:0007829|PDB:1XME"
FT   TURN            54..56
FT                   /evidence="ECO:0007829|PDB:1XME"
FT   HELIX           57..64
FT                   /evidence="ECO:0007829|PDB:1XME"
FT   HELIX           66..74
FT                   /evidence="ECO:0007829|PDB:1XME"
FT   HELIX           80..108
FT                   /evidence="ECO:0007829|PDB:1XME"
SQ   SEQUENCE   108 AA;  11634 MW;  7DEB6C38DD575368 CRC64;
     IRALPWDNPA FVAPVLGLLG FIPGGAGGIV NASFTLDYVV HNTAWVPGHF HLQVASLVTL
     TAMGSLYWLL PNLTGKPISD AQRRLGLAVV WLWFLGMMIM AVGLHWAG
//