ID   A0A023SFC5_9BIVA        Unreviewed;       201 AA.
AC   A0A023SFC5;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   29-OCT-2014, entry version 4.
DE   RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369};
DE            EC=1.9.3.1 {ECO:0000256|RuleBase:RU000369};
DE   Flags: Fragment;
GN   Name=COI {ECO:0000313|EMBL:AHX73839.1};
OS   Solenaia oleivora.
OG   Mitochondrion {ECO:0000313|EMBL:AHX73839.1}.
OC   Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Bivalvia;
OC   Palaeoheterodonta; Unionoida; Unionoidea; Unionidae; Unioninae;
OC   Solenaia.
OX   NCBI_TaxID=165460 {ECO:0000313|EMBL:AHX73839.1};
RN   [1] {ECO:0000313|EMBL:AHX73839.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=146SO4 {ECO:0000313|EMBL:AHX73841.1}, 211SO6
RC   {ECO:0000313|EMBL:AHX73843.1}, 72SO2 {ECO:0000313|EMBL:AHX73839.1},
RC   and 73SO3 {ECO:0000313|EMBL:AHX73840.1};
RA   Uyang J., Wu X., Li S.;
RL   Submitted (FEB-2014) 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:RU000369}.
CC   -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4
CC       ferricytochrome c + 2 H(2)O. {ECO:0000256|RuleBase:RU000369}.
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000256|RuleBase:RU000369}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|RuleBase:RU000369}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU000369}.
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC       {ECO:0000256|RuleBase:RU000369}.
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DR   EMBL; KJ434512; AHX73839.1; -; Genomic_DNA.
DR   EMBL; KJ434513; AHX73840.1; -; Genomic_DNA.
DR   EMBL; KJ434514; AHX73841.1; -; Genomic_DNA.
DR   EMBL; KJ434516; AHX73843.1; -; Genomic_DNA.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|RuleBase:RU000369};
KW   Electron transport {ECO:0000256|RuleBase:RU000369};
KW   Heme {ECO:0000256|RuleBase:RU000369};
KW   Iron {ECO:0000256|RuleBase:RU000369};
KW   Membrane {ECO:0000256|RuleBase:RU000369};
KW   Metal-binding {ECO:0000256|RuleBase:RU000369};
KW   Mitochondrion {ECO:0000256|RuleBase:RU000369,
KW   ECO:0000313|EMBL:AHX73839.1};
KW   Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000369};
KW   Respiratory chain {ECO:0000256|RuleBase:RU000369};
KW   Transmembrane {ECO:0000256|RuleBase:RU000369};
KW   Transport {ECO:0000256|RuleBase:RU000369}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:AHX73839.1}.
FT   NON_TER     201    201       {ECO:0000313|EMBL:AHX73839.1}.
SQ   SEQUENCE   201 AA;  21298 MW;  18D9AE6C1EDB9268 CRC64;
     LSLLIRAELG QPGSLLGDDQ LYNVIVTAHA FMMIFFLVMP MMIGGFGNWL IPLMIGAPDM
     AFPRLNNLSF WLLVPALFLL LSSSLVESGV GTGWTVYPPL SGNVAHSGAS VDLAIFSLHL
     AGASSILGAI NFISTVGNMR SPGLVAERIP LFVWAVTVTA VLLVAALPVL AGAITMLLTD
     RNINTSFFDP TGGGDPILYM H
//