(data stored in ACNUC29543 zone)

SWISSPROT: A5GRR5_SYNR3

ID   A5GRR5_SYNR3            Unreviewed;       556 AA.
AC   A5GRR5;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 81.
DE   RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU363061};
DE            EC=1.9.3.1 {ECO:0000256|RuleBase:RU363061};
GN   Name=coxA {ECO:0000313|EMBL:CAK27574.1};
GN   Synonyms=ctaD {ECO:0000313|EMBL:CAK27574.1};
GN   OrderedLocusNames=SynRCC307_0671 {ECO:0000313|EMBL:CAK27574.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK27574.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory
CC       chain that catalyzes the reduction of oxygen to water. Subunits 1-
CC       3 form the functional core of the enzyme complex. CO I is the
CC       catalytic subunit of the enzyme. Electrons originating in
CC       cytochrome c are transferred via the copper A center of subunit 2
CC       and heme A of subunit 1 to the bimetallic center formed by heme A3
CC       and copper B. {ECO:0000256|RuleBase:RU363061}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4
CC         [Fe(III)cytochrome c] + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-
CC         COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:29034; EC=1.9.3.1;
CC         Evidence={ECO:0000256|RuleBase:RU363061};
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000256|RuleBase:RU363061}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000256|RuleBase:RU363061}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU363061}.
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC       {ECO:0000256|RuleBase:RU363061}.
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DR   EMBL; CT978603; CAK27574.1; -; Genomic_DNA.
DR   RefSeq; WP_011935089.1; NC_009482.1.
DR   STRING; 316278.SynRCC307_0671; -.
DR   EnsemblBacteria; CAK27574; CAK27574; SynRCC307_0671.
DR   KEGG; syr:SynRCC307_0671; -.
DR   eggNOG; ENOG4105BZ9; Bacteria.
DR   eggNOG; COG0843; LUCA.
DR   HOGENOM; HOG000085274; -.
DR   KO; K02274; -.
DR   OMA; MSFWLLP; -.
DR   OrthoDB; 316745at2; -.
DR   BioCyc; SSP316278:G1GJL-664-MONOMER; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000001115; 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; IEA:InterPro.
DR   GO; GO:0015990; P:electron transport coupled proton transport; IEA:InterPro.
DR   GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
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;
DR   PRODOM; A5GRR5.
DR   SWISS-2DPAGE; A5GRR5.
KW   Cell membrane {ECO:0000256|RuleBase:RU363061};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Copper {ECO:0000256|RuleBase:RU363061};
KW   Electron transport {ECO:0000256|RuleBase:RU363061};
KW   Heme {ECO:0000256|RuleBase:RU363061};
KW   Iron {ECO:0000256|RuleBase:RU363061};
KW   Membrane {ECO:0000256|RuleBase:RU363061};
KW   Metal-binding {ECO:0000256|RuleBase:RU363061};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU363061,
KW   ECO:0000313|EMBL:CAK27574.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115};
KW   Respiratory chain {ECO:0000256|RuleBase:RU363061};
KW   Transmembrane {ECO:0000256|RuleBase:RU363061};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU363061};
KW   Transport {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM     33     56       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM     76     97       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    118    141       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    161    186       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    198    231       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    251    271       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    283    307       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    319    341       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    353    375       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    395    413       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    425    446       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    466    486       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   DOMAIN       15    529       COX1. {ECO:0000259|PROSITE:PS50855}.
SQ   SEQUENCE   556 AA;  61378 MW;  A3F41EEF7ACD5F7A CRC64;
     MTIASPPSPS PQPLRLQPTG WLRYFSFSLD HKVIGLQYIV CGFLFYFVGG ALAGVIRTEL
     ATPISDFVSR DTYNQVLTLH GTVMIFLWIV PVVNGGFGNY LIPFYVGARD MAFPRLNAVA
     FWMIPPSGLL LISSYFIGGA AQSGWTAYPP LSLTTPAMGQ ILWIVSVLLL GGSSIFGGIN
     FIATILKFRQ PGLKLMMLPM YCWAMLGTSI LVVLATPVLA GTLILLSLDI VAHTGFFNPA
     AGGNAVVYQH LFWFYSHPAV YIMVLPAFGL VSEILPVHAR KPLFGYVTMV YSIMAIVILG
     LVVWAHHMFT SGTPPWMRLF FTIATAFIAV PTGIKFFNWI ATLWQGRLAL NSAMLFSCAF
     ILQFVFGGIT GVALAQVPFD VHVHDTYFVV AHFHYIVYGG TVFVIFASIY HWFPKFSGRM
     LNEHLGRLHL ALTFIGFNLC FAPQHWLGLN GMPRRVAEYD PQFTLINQLS SVGALLMAIS
     TLPFLINVVM SLLQGPAAGP NPWRALTPEW LTSSPPPVEN WIGAAPLVKE PYGYGSTEGR
     IDVNQARGQD LWRQQP
//

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