COX1_RHOCA
ID COX1_RHOCA Reviewed; 532 AA.
AC P98059;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, 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 BB(3) subunit 1;
DE AltName: Full=Cytochrome c oxidase polypeptide I;
GN Name=ctaD; Synonyms=ccoN;
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 938 / 37b4;
RX PubMed=7891558; DOI=10.1111/j.1365-2958.1994.tb01308.x;
RA Thony-Meyer L., Beck C., Preisig O., Hennecke H.;
RT "The ccoNOQP gene cluster codes for a cb-type cytochrome oxidase that
RT functions in aerobic respiration of Rhodobacter capsulatus.";
RL Mol. Microbiol. 14:705-716(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. 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 Evidence={ECO:0000250|UniProtKB:D9IA43};
CC Note=Binds 1 copper ion per subunit, denoted as copper B.
CC {ECO:0000250|UniProtKB:D9IA43};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:D9IA43};
CC Note=Binds 2 heme b groups per subunit, denoted as high- and low-spin.
CC {ECO:0000250|UniProtKB:D9IA43};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000305}.
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DR EMBL; X80134; CAA56433.1; -; Genomic_DNA.
DR PIR; S65858; S49345.
DR RefSeq; WP_055212924.1; NZ_QKZO01000007.1.
DR AlphaFoldDB; P98059; -.
DR SMR; P98059; -.
DR UniPathway; UPA00705; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045278; C:plasma membrane 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:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR CDD; cd01661; cbb3_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; IPR004677; Cyt_c_oxidase_cbb3_su1.
DR PANTHER; PTHR10422; PTHR10422; 1.
DR PANTHER; PTHR10422:SF29; PTHR10422:SF29; 1.
DR Pfam; PF00115; COX1; 1.
DR SUPFAM; SSF81442; SSF81442; 1.
DR TIGRFAMs; TIGR00780; ccoN; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
PE 3: Inferred from homology;
KW Cell membrane; Copper; Electron transport; Heme; Hydrogen ion transport;
KW Ion transport; Iron; Membrane; Metal-binding; Respiratory chain;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..532
FT /note="Cytochrome c oxidase subunit 1"
FT /id="PRO_0000183458"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 496..516
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 114
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1; low-spin"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:D9IA43"
FT BINDING 264
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:D9IA43"
FT BINDING 314
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:D9IA43"
FT BINDING 315
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:D9IA43"
FT BINDING 402
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2; high-spin"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:D9IA43"
FT BINDING 404
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1; low-spin"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:D9IA43"
SQ SEQUENCE 532 AA; 58956 MW; 5B00CE8819D2782C CRC64;
MWDYVKLVAL GVVAAIAAYA ASQARDLPYM VNMVEVALAA VIALIWVLRT MGDPKPSKDE
YFDGVIRAGV IATTFWGIVG FLVAVVIAFQ LAFPALNLEF GNGMLNFGRL RPLHTSAVIF
AFGGNALIAS AFYVVQRTSA ARLFGGTALG WFVFWGWQLI IVTAATSYLL GGSQGKEYAE
LNWHLDILVA VVWVAYLIAF LGTIFKRKEP HIYVANWFYL SFIVTIAMLH IVNNLAVPVS
IFGTKSVQLM AGVQDAMTQW WYGHNAVGFF LTAGFLGMMY YFVPKQAERP VYSYKLSIVH
FWALIFLYIW AGPHHLHYTA LPDWASTLGM VMSVILWMPS WGGMINGLMT LSGAWDKLRT
DPVIRMMVVS IGFYGMSTFE GPMMSIKAVN SLSHYTDWTI GHVHSGALGW NGMITFGMLY
FLTPRLWGRS GLYSLKLVSW HFWLATIGIV LYASAMWVTG IMEGLMWREV DAQGFLVNAF
ADTVAAKFPM YVVRGVGGVL YLLGGLIMAY NLWATVAKQP KTANLAVAVP AE
