ID   COX1_SYNY3              Reviewed;         551 AA.
AC   Q06473; P73261;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 159.
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;
DE   AltName: Full=Oxidase aa(3) subunit 1;
GN   Name=ctaD; OrderedLocusNames=slr1137;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8387368;
RA   Alge D., Peschek G.A.;
RT   "Characterization of a cta/CDE operon-like genomic region encoding subunits
RT   I-III of the cytochrome c oxidase of the cyanobacterium Synechocystis PCC
RT   6803.";
RL   Biochem. Mol. Biol. Int. 29:511-525(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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   -!- 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   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC       {ECO:0000305}.
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DR   EMBL; X53746; CAA37777.1; -; Genomic_DNA.
DR   EMBL; BA000022; BAA17289.1; -; Genomic_DNA.
DR   PIR; S77442; S77442.
DR   AlphaFoldDB; Q06473; -.
DR   SMR; Q06473; -.
DR   STRING; 1148.gene:10498152; -.
DR   PaxDb; 1148-1652367; -.
DR   EnsemblBacteria; BAA17289; BAA17289; BAA17289.
DR   KEGG; syn:slr1137; -.
DR   eggNOG; COG0843; Bacteria.
DR   InParanoid; Q06473; -.
DR   PhylomeDB; Q06473; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000001425; Chromosome.
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:0009060; P:aerobic respiration; IBA:GO_Central.
DR   GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR   GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR   GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
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: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   3: Inferred from homology;
KW   Cell membrane; Copper; Electron transport; Heme; Iron; Membrane;
KW   Metal-binding; Reference proteome; Respiratory chain; Translocase;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..551
FT                   /note="Cytochrome c oxidase subunit 1"
FT                   /id="PRO_0000183461"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        283..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        313..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        348..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        382..402
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        424..444
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        466..486
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         76
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         251
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000305"
FT   BINDING         255
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000305"
FT   BINDING         300
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000305"
FT   BINDING         301
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000305"
FT   BINDING         386
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         388
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        251..255
FT                   /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        191..197
FT                   /note="SMPLFCW -> VCPCFAG (in Ref. 1; CAA37777)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        212
FT                   /note="V -> L (in Ref. 1; CAA37777)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        233
FT                   /note="P -> R (in Ref. 1; CAA37777)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        305
FT                   /note="S -> H (in Ref. 1; CAA37777)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        329..336
FT                   /note="KIFSWCGT -> QNFQLVRY (in Ref. 1; CAA37777)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        432
FT                   /note="N -> D (in Ref. 1; CAA37777)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        520..551
FT                   /note="VLWCGPYDFGIDTELMDDEETVQTLIADAAGS -> CSGVVPTILVLTRS
FT                   (in Ref. 1; CAA37777)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   551 AA;  61349 MW;  B291E7884ABE6503 CRC64;
     MTIAAENLTA NHPRRKWTDY FTFCVDHKVI GIQYLVTSFL FFFIGGSFAE AMRTELATPS
     PDFVQPEMYN QLMTLHGTIM IFLWIVPAGA AFANYLIPLM VGTEDMAFPR LNAVAFWLTP
     PGGILLISSF FVGAPQAGWT SYPPLSLLSG KWGEELWILS LLLVGTSSIL GAINFVTTIL
     KMRIKDMDLH SMPLFCWAML ATSSLILLST PVLASALILL SFDLIAGTSF FNPVGGGDPV
     VYQHLFWFYS HPAVYIMILP FFGVISEVIP VHARKPIFGY RAIAYSSLAI SFLGLIVWAH
     HMFTSGTPGW LRMFFMATTM LIAVPTGIKI FSWCGTLWGG KIQLNSAMLF AFGFLSSFMI
     GGLTGVMVAS VPFDIHVHDT YFVVGHFHYV LFGGSAFALF SGVYHWFPKM TGRMVNEPLG
     RLHFILTFIG MNLTFMPMHE LGLMGMNRRI ALYDVEFQPL NVLSTIGAYV LAASTIPFVI
     NVFWSLFKGE KAARNPWRAL TLEWQTASPP IIENFEEEPV LWCGPYDFGI DTELMDDEET
     VQTLIADAAG S
//