ID   Q3J5A7_CERS4            Unreviewed;       566 AA.
AC   Q3J5A7;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU363061};
DE            EC=7.1.1.9 {ECO:0000256|RuleBase:RU363061};
GN   Name=coxI {ECO:0000313|EMBL:ABA78027.1};
GN   ORFNames=RSP_1877 {ECO:0000313|EMBL:ABA78027.1};
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Cereibacter.
OX   NCBI_TaxID=272943 {ECO:0000313|EMBL:ABA78027.1, ECO:0000313|Proteomes:UP000002703};
RN   [1] {ECO:0000313|Proteomes:UP000002703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC
RC   12203 / NCIMB 8253 / ATH 2.4.1. {ECO:0000313|Proteomes:UP000002703};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0007829|PDB:3OM3, ECO:0007829|PDB:3OMA}
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 17-551 IN COMPLEX WITH CALCIUM;
RP   COPPER AND HEME, AND DISULFIDE BONDS.
RX   PubMed=21205904; DOI=10.1073/pnas.1012846108;
RA   Liu J., Qin L., Ferguson-Miller S.;
RT   "Crystallographic and online spectral evidence for role of conformational
RT   change and conserved water in cytochrome oxidase proton pump.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:1284-1289(2011).
RN   [3] {ECO:0007829|PDB:6PW0, ECO:0007829|PDB:6PW1}
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 17-550, AND DISULFIDE BONDS.
RX   PubMed=31733183; DOI=10.1016/j.bbabio.2019.148116;
RA   Berg J., Liu J., Svahn E., Ferguson-Miller S., Brzezinski P.;
RT   "Structural changes at the surface of cytochrome c oxidase alter the
RT   proton-pumping stoichiometry.";
RL   Biochim Biophys Acta Bioenerg 1861:148116-148116(2020).
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       {ECO:0000256|RuleBase:RU363061}.
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:0000256|ARBA:ARBA00029368,
CC         ECO:0000256|RuleBase:RU363061};
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000256|ARBA:ARBA00004673, ECO:0000256|RuleBase:RU363061}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU363061};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU363061}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC       {ECO:0000256|RuleBase:RU000370}.
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DR   EMBL; CP000143; ABA78027.1; -; Genomic_DNA.
DR   RefSeq; WP_011337048.1; NZ_CP030271.1.
DR   RefSeq; YP_351928.1; NC_007493.2.
DR   PDB; 3OM3; X-ray; 2.60 A; A/C=17-551.
DR   PDB; 3OMA; X-ray; 2.30 A; A/C=17-551.
DR   PDB; 3OMI; X-ray; 2.15 A; A/C=17-551.
DR   PDB; 3OMN; X-ray; 2.15 A; A/C=17-551.
DR   PDB; 6PW0; X-ray; 2.50 A; A/C=1-560.
DR   PDB; 6PW1; X-ray; 2.10 A; A/C=17-550.
DR   PDBsum; 3OM3; -.
DR   PDBsum; 3OMA; -.
DR   PDBsum; 3OMI; -.
DR   PDBsum; 3OMN; -.
DR   PDBsum; 6PW0; -.
DR   PDBsum; 6PW1; -.
DR   AlphaFoldDB; Q3J5A7; -.
DR   SMR; Q3J5A7; -.
DR   STRING; 272943.RSP_1877; -.
DR   EnsemblBacteria; ABA78027; ABA78027; RSP_1877.
DR   GeneID; 67445668; -.
DR   KEGG; rsp:RSP_1877; -.
DR   PATRIC; fig|272943.9.peg.767; -.
DR   eggNOG; COG0843; Bacteria.
DR   OrthoDB; 9803294at2; -.
DR   PhylomeDB; Q3J5A7; -.
DR   UniPathway; UPA00705; -.
DR   EvolutionaryTrace; Q3J5A7; -.
DR   Proteomes; UP000002703; Chromosome 1.
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; 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; IPR033944; Cyt_c_oxase_su1_dom.
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:SF18; 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   3D-structure {ECO:0007829|PDB:3OM3, ECO:0007829|PDB:3OMA};
KW   Calcium {ECO:0007829|PDB:3OM3, ECO:0007829|PDB:3OMA};
KW   Cell membrane {ECO:0000256|RuleBase:RU363061};
KW   Copper {ECO:0000256|RuleBase:RU363061};
KW   Electron transport {ECO:0000256|RuleBase:RU000370};
KW   Heme {ECO:0000256|RuleBase:RU000370, ECO:0007829|PDB:3OM3};
KW   Iron {ECO:0000256|RuleBase:RU363061, ECO:0007829|PDB:3OM3};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363061};
KW   Metal-binding {ECO:0000256|RuleBase:RU363061, ECO:0007829|PDB:3OM3};
KW   Oxidoreductase {ECO:0000313|EMBL:ABA78027.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002703};
KW   Respiratory chain {ECO:0000256|RuleBase:RU000370};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000370};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU363061}; Transport {ECO:0000256|RuleBase:RU000370}.
FT   TRANSMEM        29..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        104..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        143..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        189..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        227..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        287..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        313..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        346..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        381..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        420..440
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        452..473
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        493..519
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   DOMAIN          20..558
FT                   /note="Cytochrome oxidase subunit I profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50855"
FT   REGION          543..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..566
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         48
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3OMA, ECO:0007829|PDB:3OMN"
FT   BINDING         52
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3OM3, ECO:0007829|PDB:3OMA"
FT   BINDING         54
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0007829|PDB:3OM3, ECO:0007829|PDB:3OMA"
FT   BINDING         57
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0007829|PDB:3OM3, ECO:0007829|PDB:3OMA"
FT   BINDING         59
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0007829|PDB:3OM3, ECO:0007829|PDB:3OMA"
FT   BINDING         95
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3OM3, ECO:0007829|PDB:3OMA"
FT   BINDING         102
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /ligand_part_note="axial binding residue"
FT                   /evidence="ECO:0007829|PDB:3OM3, ECO:0007829|PDB:3OMA"
FT   BINDING         172
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3OM3, ECO:0007829|PDB:3OMA"
FT   BINDING         172
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0007829|PDB:3OM3"
FT   BINDING         172
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3OMA, ECO:0007829|PDB:3OMI"
FT   BINDING         284
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /evidence="ECO:0007829|PDB:3OM3, ECO:0007829|PDB:3OMN"
FT   BINDING         284
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /evidence="ECO:0007829|PDB:3OMA, ECO:0007829|PDB:3OMI"
FT   BINDING         288
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3OMA, ECO:0007829|PDB:3OMI"
FT   BINDING         333
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /evidence="ECO:0007829|PDB:3OM3, ECO:0007829|PDB:3OMN"
FT   BINDING         333
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /evidence="ECO:0007829|PDB:3OMA, ECO:0007829|PDB:3OMI"
FT   BINDING         334
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /evidence="ECO:0007829|PDB:3OM3, ECO:0007829|PDB:3OMN"
FT   BINDING         334
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /evidence="ECO:0007829|PDB:3OMA, ECO:0007829|PDB:3OMI"
FT   BINDING         411
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3OMA, ECO:0007829|PDB:3OMI"
FT   BINDING         411
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0007829|PDB:3OM3"
FT   BINDING         411
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007829|PDB:3OM3, ECO:0007829|PDB:3OMA"
FT   BINDING         412
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007829|PDB:3OM3, ECO:0007829|PDB:3OMA"
FT   BINDING         419
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /ligand_part_note="axial binding residue"
FT                   /evidence="ECO:0007829|PDB:3OMA, ECO:0007829|PDB:3OMI"
FT   BINDING         419
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_label="3"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /ligand_part_note="axial binding residue"
FT                   /evidence="ECO:0007829|PDB:3OM3"
FT   BINDING         421
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /ligand_part_note="axial binding residue"
FT                   /evidence="ECO:0007829|PDB:3OM3, ECO:0007829|PDB:3OMA"
FT   BINDING         471
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3OM3, ECO:0007829|PDB:3OMA"
FT   BINDING         481
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3OMA, ECO:0007829|PDB:3OMI"
FT   BINDING         481
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0007829|PDB:3OM3"
FT   BINDING         481
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3OM3, ECO:0007829|PDB:3OMA"
FT   BINDING         482
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3OM3, ECO:0007829|PDB:3OMA"
FT   DISULFID        64..88
FT                   /evidence="ECO:0007829|PDB:3OM3, ECO:0007829|PDB:3OMA"
SQ   SEQUENCE   566 AA;  63147 MW;  65A74DBCC5C550B0 CRC64;
     MADAAIHGHE HDRRGFFTRW FMSTNHKDIG VLYLFTGGLV GLISVAFTVY MRMELMAPGV
     QFMCAEHLES GLVKGFFQSL WPSAVENCTP NGHLWNVMIT GHGILMMFFV VIPALFGGFG
     NYFMPLHIGA PDMAFPRMNN LSYWLYVAGT SLAVASLFAP GGNGQLGSGI GWVLYPPLST
     SESGYSTDLA IFAVHLSGAS SILGAINMIT TFLNMRAPGM TMHKVPLFAW SIFVTAWLIL
     LALPVLAGAI TMLLTDRNFG TTFFQPSGGG DPVLYQHILW FFGHPEVYII VLPAFGIVSH
     VIATFAKKPI FGYLPMVYAM VAIGVLGFVV WAHHMYTAGL SLTQQSYFMM ATMVIAVPTG
     IKIFSWIATM WGGSIELKTP MLWALGFLFL FTVGGVTGIV LSQASVDRYY HDTYYVVAHF
     HYVMSLGAVF GIFAGIYFWI GKMSGRQYPE WAGKLHFWMM FVGANLTFFP QHFLGRQGMP
     RRYIDYPEAF ATWNFVSSLG AFLSFASFLF FLGVIFYTLT RGARVTANNY WNEHADTLEW
     TLTSPPPEHT FEQLPKREDW ERAPAH
//