ID   A0A896SSY8_9ASCO        Unreviewed;       522 AA.
AC   A0A896SSY8;
DT   29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 1.
DT   19-JAN-2022, entry version 2.
DE   RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369};
DE            EC=7.1.1.9 {ECO:0000256|RuleBase:RU000369};
GN   Name=cox1 {ECO:0000313|EMBL:QSD56444.1};
OS   Metschnikowia bicuspidata.
OG   Mitochondrion {ECO:0000313|EMBL:QSD56444.1}.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Metschnikowia.
OX   NCBI_TaxID=27322 {ECO:0000313|EMBL:QSD56444.1};
RN   [1] {ECO:0000313|EMBL:QSD56444.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Ye G.S., Liu N.J.;
RL   Submitted (OCT-2020) to the EMBL/GenBank/DDBJ databases.
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] + 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         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; MW147605; QSD56444.1; -; Genomic_DNA.
DR   UniPathway; UPA00705; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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   PANTHER; PTHR10422; PTHR10422; 1.
DR   Pfam; PF00115; COX1; 1.
DR   PRINTS; PR01165; CYCOXIDASEI.
DR   SUPFAM; SSF81442; SSF81442; 1.
DR   PROSITE; PS50855; COX1; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|RuleBase:RU000369};
KW   Electron transport {ECO:0000256|RuleBase:RU000369};
KW   Heme {ECO:0000256|RuleBase:RU000369}; 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:QSD56444.1};
KW   Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369};
KW   Respiratory chain {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|RuleBase:RU000369}.
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        60..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        107..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        149..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        186..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        276..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        305..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        336..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        372..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        403..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        441..461
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..518
FT                   /note="COX1"
FT                   /evidence="ECO:0000259|PROSITE:PS50855"
SQ   SEQUENCE   522 AA;  58193 MW;  7391EA75DE5234EE CRC64;
     MSYMTRWLYS TSHKDMAMLY LGYGLMSSMV ATGMSVMMRM ELSGANPQYL NGNNQVYNVM
     VTGHAMGMMF LFVMPVTIGA FGNYFLPIMM GAVDMAFARL NNMSFWCLPP ALVCVMASLL
     VENGAGTGWT VYPPLSSMNA HSGPSVDLAI FATHLTSMSS LLGAINFMVT FMNMRTMGLH
     MMNAPLFVWA MFFTAMLLLL SLPVLTAGVT LLLMDRNFNT GFYEVAAGGD PVLYVRVHKY
     GYSMKSYIMI MPGFGMMSHM VSTYSKKPIF GEMGMLYAMG SIGTLGFLVW SHHMFVVGLD
     IDSRAYFTSA TMVMAVPTGI KMWATVPTVY GGEVRLAVPM LFALGFLFTF TIGGVTGVML
     SNASMDVAFH HFHYVLSMGA LFSTVGGYYY WGPSMFGLNY NKVWAEMHFW LLFMSVNVIF
     LPMHFFGMPR RMPQYPDAFM GWNYMSSMGS AMSMMSVMVG LKSVQMQLDN GLNEDSEMQV
     TPDFLESNKM RDVRDSDIEL ILARPAEYHT FSELPVLVTP KV
//