COX1_SYNY3
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 03-AUG-2022, entry version 152.
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; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified 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; 1148.1652367; -.
DR PaxDb; Q06473; -.
DR EnsemblBacteria; BAA17289; BAA17289; BAA17289.
DR KEGG; syn:slr1137; -.
DR eggNOG; COG0843; Bacteria.
DR InParanoid; Q06473; -.
DR OMA; WAMMSIG; -.
DR PhylomeDB; Q06473; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000001425; Chromosome.
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: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; -; 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 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 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
