ID   A0A8E4MH59_9EUCA        Unreviewed;       182 AA.
AC   A0A8E4MH59;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   27-NOV-2024, entry version 10.
DE   RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369};
DE            EC=7.1.1.9 {ECO:0000256|RuleBase:RU000369};
DE   Flags: Fragment;
GN   Name=COX1 {ECO:0000313|EMBL:QKX95960.1};
OS   Macrobrachium americanum.
OG   Mitochondrion {ECO:0000313|EMBL:QKX95960.1}.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Caridea;
OC   Palaemonoidea; Palaemonidae; Macrobrachium.
OX   NCBI_TaxID=746527 {ECO:0000313|EMBL:QKX95960.1};
RN   [1] {ECO:0000313|EMBL:QKX95960.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Garcia-Velazco H., Maeda-Martinez A.M., Obregon-Barboza H., Ruiz-Campos G.,
RA   Rodriguez-Almaraz G.A., Murugan G.;
RT   "The systematics of the amphidromous shrimp Macrobrachium americanum Spence
RT   Bate, 1868 (Decapoda: Caridea: Palaemonidae) from the Mexican Pacific
RT   slope.";
RL   J. Crust. Biol. 41:0-0(0).
CC   -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the
CC       mitochondrial electron transport chain which drives oxidative
CC       phosphorylation. The respiratory chain contains 3 multisubunit
CC       complexes succinate dehydrogenase (complex II, CII), ubiquinol-
CC       cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III,
CC       CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to
CC       transfer electrons derived from NADH and succinate to molecular oxygen,
CC       creating an electrochemical gradient over the inner membrane that
CC       drives transmembrane transport and the ATP synthase. Cytochrome c
CC       oxidase is the component of the respiratory chain that catalyzes the
CC       reduction of oxygen to water. Electrons originating from reduced
CC       cytochrome c in the intermembrane space (IMS) are transferred via the
CC       dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1
CC       to the active site in subunit 1, a binuclear center (BNC) formed by
CC       heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2
CC       water molecules using 4 electrons from cytochrome c in the IMS and 4
CC       protons from the mitochondrial matrix. {ECO:0000256|RuleBase:RU000369}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 Fe(II)-[cytochrome c] + O2 + 8 H(+)(in) = 4 Fe(III)-
CC         [cytochrome c] + 2 H2O + 4 H(+)(out); 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         Evidence={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; MT659157; QKX95960.1; -; Genomic_DNA.
DR   UniPathway; UPA00705; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015990; P:electron transport coupled proton transport; IEA:TreeGrafter.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:TreeGrafter.
DR   Gene3D; 1.20.210.10; Cytochrome c oxidase-like, subunit I domain; 1.
DR   InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
DR   InterPro; IPR000883; Cyt_C_Oxase_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.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|RuleBase:RU000369};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW   ECO:0000256|RuleBase:RU000369}; Heme {ECO:0000256|RuleBase:RU000369};
KW   Iron {ECO:0000256|RuleBase:RU000369};
KW   Membrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|RuleBase:RU000369};
KW   Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:QKX95960.1};
KW   Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369};
KW   Respiratory chain {ECO:0000256|ARBA:ARBA00022660,
KW   ECO:0000256|RuleBase:RU000369};
KW   Transmembrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000369}.
FT   TRANSMEM        33..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        64..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        98..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        132..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:QKX95960.1"
FT   NON_TER         182
FT                   /evidence="ECO:0000313|EMBL:QKX95960.1"
SQ   SEQUENCE   182 AA;  20172 MW;  CA542AE8F5E58166 CRC64;
     HPEVYILILP AFGMISHIVS QESGKKESFG TLGMIYAMMA IGVLGFVVWA HHMFTVGMDV
     DTRAYFTSAT MIIAVPTGIK IFSWLATLHG TQFTYSPSLI WALGFIFLFT MGGLTGVVLA
     NSSIDIILHD TYYVVAHFHY VLSMGAVFGI FAGIAHWYPL FTGLSLHPKW LKIHFTTMFI
     GV
//