ID   COX1_BACP3              Reviewed;         616 AA.
AC   P16262; Q56248;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 138.
DE   RecName: Full=Cytochrome c oxidase subunit 1;
DE            EC=7.1.1.9;
DE   AltName: Full=Cytochrome aa3 subunit 1;
DE   AltName: Full=Cytochrome c oxidase polypeptide I;
GN   Name=ctaD; Synonyms=caaB, coi;
OS   Bacillus sp. (strain PS3).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-31.
RX   PubMed=1964459; DOI=10.1093/oxfordjournals.jbchem.a123294;
RA   Ishizuka M., Machida K., Shimada S., Mogi A., Tsuchiya T., Ohmori T.,
RA   Souma Y., Gonda M., Sone N.;
RT   "Nucleotide sequence of the gene coding for four subunits of cytochrome c
RT   oxidase from the thermophilic bacterium PS3.";
RL   J. Biochem. 108:866-873(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-552, AND PROTEIN SEQUENCE OF 2-15.
RX   PubMed=2844737; DOI=10.1093/oxfordjournals.jbchem.a122314;
RA   Sone N., Yokoi F., Fu T., Ohta S., Metso T., Raitio M., Saraste M.;
RT   "Nucleotide sequence of the gene coding for cytochrome oxidase subunit I
RT   from the thermophilic bacterium PS3.";
RL   J. Biochem. 103:606-610(1988).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=1652469; DOI=10.1016/0014-5793(91)81024-3;
RA   Sone N., Fujiwara Y.;
RT   "Haem O2 can replace haem A in the active site of cytochrome c oxidase from
RT   thermophilic bacterium PS3.";
RL   FEBS Lett. 288:154-158(1991).
CC   -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory
CC       chain that catalyzes the reduction of oxygen to water. Subunits 1-3
CC       form the functional core of the enzyme complex. Co I is the catalytic
CC       subunit of the enzyme. Electrons originating in cytochrome c are
CC       transferred via the copper A center of subunit 2 and heme a of subunit
CC       1 to the bimetallic center formed by heme a3 and copper B. This
CC       cytochrome c oxidase shows proton pump activity across the membrane in
CC       addition to the electron transfer.
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=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC       Note=Binds 1 copper B ion per subunit.;
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC       Note=Binds 2 heme groups per subunit.;
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- MISCELLANEOUS: Under slightly air-limited conditions, the cytochrome a3
CC       center of the enzyme is replaced by cytochrome o.
CC   -!- MISCELLANEOUS: This cytochrome c oxidase shows clear proton pump
CC       activity in addition to electron transfer across the membrane.
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA01793.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; D13955; BAA03046.1; -; Genomic_DNA.
DR   EMBL; D11038; BAA01793.1; ALT_FRAME; Genomic_DNA.
DR   PIR; JX0140; JX0140.
DR   AlphaFoldDB; P16262; -.
DR   SMR; P16262; -.
DR   UniPathway; UPA00705; -.
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:0015990; P:electron transport coupled proton transport; IEA:InterPro.
DR   GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd01662; Ubiquinol_Oxidase_I; 1.
DR   Gene3D; 1.10.287.70; -; 1.
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   InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR   InterPro; IPR014241; Cyt_c_oxidase_su1_bac.
DR   NCBIfam; TIGR02891; CtaD_CoxA; 1.
DR   PANTHER; PTHR10422; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR   PANTHER; PTHR10422:SF44; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR   Pfam; PF00115; COX1; 1.
DR   PRINTS; PR01165; CYCOXIDASEI.
DR   SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 1.
DR   PROSITE; PS50855; COX1; 1.
DR   PROSITE; PS00077; COX1_CUB; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Copper; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Membrane; Metal-binding; Respiratory chain; Translocase;
KW   Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1964459,
FT                   ECO:0000269|PubMed:2844737"
FT   CHAIN           2..616
FT                   /note="Cytochrome c oxidase subunit 1"
FT                   /id="PRO_0000183435"
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        75..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        349..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        420..440
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        463..483
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        553..573
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        577..597
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         72
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:0000305"
FT   BINDING         249
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000305"
FT   BINDING         253
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000305"
FT   BINDING         298
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000305"
FT   BINDING         299
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000305"
FT   BINDING         384
FT                   /ligand="Fe(II)-heme o"
FT                   /ligand_id="ChEBI:CHEBI:60530"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000305"
FT   BINDING         384
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:0000305"
FT   BINDING         386
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:0000305"
FT   CROSSLNK        249..253
FT                   /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        448
FT                   /note="V -> W (in Ref. 2; BAA01793)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        470
FT                   /note="F -> I (in Ref. 2; BAA01793)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        506..508
FT                   /note="AIA -> RS (in Ref. 2; BAA01793)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        525..526
FT                   /note="LD -> WT (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        549
FT                   /note="Missing (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   616 AA;  68294 MW;  17DF1E3325014B96 CRC64;
     MSTIARKKGV GAVLWDYLTT VDHKKIAHLY LISGGFFFLL GGLEALFIRI QLAKPNNDFL
     VGGLYNEVLT MHGTTMIFLA AMPLVFAFMN AVVPLQIGAR DVAFPFLNAL GFWMFFFGGL
     FLNCSWFLGG APDAGWTSYA SLSLDSKAHH GIDFYTLGLQ ISGFGTIMGA INFLVTIINM
     RAPGMTFMRM PMFTWATFVT SALILFAFPP LTVGLIFMMM DRLFGGNFFN PAAGGNTIIW
     EHLFWVFGHP EVYILVLPAF GIFSEIFATF SRKRLFGYSS MVFATVLIAF LGFMVWAHHM
     FTVGMGPIAN AIFAVATMTI AVPTGVKIFN WLFTMWGGSI KFTTPMHYAV AFIPSFVMGG
     VTGVMLASAA ADYQYHDSYF VVAHFHYVIV GGVVFALLAG THYWWPKMFG RMLNETLGKI
     TFWLFFIGFH LTFFIQHFLG LTGMPRRVFT YLPHQGWETG NLISTIGAFF IAAATVILLI
     NIVVTTAKGE KVPGDAWGDG RTLEWAIASP PPVYNFAQTP LVRGLDAFWL EKMEGKKELT
     PAEPLGDIHM PNSSFLPFVI AFGLFVAAFG FTYHNDAGWG LPVAILGLLI TLGSMFLRSV
     IDDHGFHIHK EEVLEL
//