ID   COX1_RHILE              Reviewed;         538 AA.
AC   Q08855;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=coxA;
OS   Rhizobium leguminosarum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8117073; DOI=10.1128/aem.60.1.141-148.1994;
RA   Gabel C., Bittinger M.A., Maier R.J.;
RT   "Cytochrome aa3 gene regulation in members of the family Rhizobiaceae:
RT   comparison of copper and oxygen effects in Bradyrhizobium japonicum and
RT   Rhizobium tropici.";
RL   Appl. Environ. Microbiol. 60:141-148(1994).
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.
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   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- DEVELOPMENTAL STAGE: Free in soil (not as bacteroid).
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC       {ECO:0000305}.
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DR   EMBL; X74341; CAA52388.1; -; Genomic_DNA.
DR   PIR; S36424; S36424.
DR   AlphaFoldDB; Q08855; -.
DR   SMR; Q08855; -.
DR   UniPathway; UPA00705; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045277; C:respiratory chain complex IV; IEA:InterPro.
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; cd01663; Cyt_c_Oxidase_I; 1.
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   InterPro; IPR033944; Cyt_c_oxase_su1_dom.
DR   InterPro; IPR014241; Cyt_c_oxidase_su1_bac.
DR   PANTHER; PTHR10422; PTHR10422; 1.
DR   Pfam; PF00115; COX1; 1.
DR   PRINTS; PR01165; CYCOXIDASEI.
DR   SUPFAM; SSF81442; SSF81442; 1.
DR   TIGRFAMs; TIGR02891; CtaD_CoxA; 1.
DR   PROSITE; PS50855; COX1; 1.
DR   PROSITE; PS00077; COX1_CUB; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Copper; Electron transport; Heme; Iron; Membrane;
KW   Metal-binding; Respiratory chain; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..538
FT                   /note="Cytochrome c oxidase subunit 1"
FT                   /id="PRO_0000183447"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        208..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        259..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        329..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        362..382
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        401..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        438..458
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        476..496
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         82
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         265
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000305"
FT   BINDING         269
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000305"
FT   BINDING         314
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000305"
FT   BINDING         315
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000305"
FT   BINDING         400
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         402
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        265..269
FT                   /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   538 AA;  59133 MW;  740C8FE6C902D9BF CRC64;
     MATSAAAHGE HAEDHGHDEH AHPTGWRRST NHKDIGTLYL IFAIIAGVIG AAMSLAIRAE
     LMYPGVEYFH NTHLYNVFVT SHGVIMIFFM VMPAMIGGFG NWFLPLMIGA PDMAFPRMNN
     ISFWLLPASF GLLLMSTFVE GEPGANGAGA GWTMYVPLSS SGHPGPAVDL AIFSLHIAGA
     SSILGAINFI TTILNMRAPG MTLHKMPLFA WSVLITAFLL LLSLPVLAGA ITMLLTDRNF
     GTTFFAPEGG GDPLLYQHLF WFFGHPEVYI LILPGFGMIS HIISTFSRKP VFGYIGMVYA
     MAAIGGLGFV VWAHHMYIVG MDLDTEAYFV SATMIIAVPT GIKIFSWIAT MWGGSIEFAT
     PMLWALAFIF LFTVGGVTGV VLANASLDRV LHDTYYVVAH FHYVLSLGAI FAIFAGWYYW
     FPKMSGYMYN ETLAEAHFWL IFIGVNLIFF PEHFLGISGM PRRYIDYPDA FAGWNLVSSI
     GSYISGFSVL LFIYCVYDAF AKNVPVGDNP WGAGATTLEW TLPSPPPVHE FEVLPRVE