ID Q8HIS9_MONBE Unreviewed; 534 AA.
AC Q8HIS9;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 24-JAN-2024, entry version 101.
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:AAN28355.1};
OS Monosiga brevicollis (Choanoflagellate).
OG Mitochondrion {ECO:0000313|EMBL:AAN28355.1}.
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX NCBI_TaxID=81824 {ECO:0000313|EMBL:AAN28355.1};
RN [1] {ECO:0000313|EMBL:AAN28355.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 50154 {ECO:0000313|EMBL:AAN28355.1};
RX PubMed=10916154; DOI=10.1016/S0968-0004(00)01612-1;
RA Bullerwell C.E., Burger G., Lang B.F.;
RT "A novel motif for identifying rps3 homologs in fungal mitochondrial
RT genomes.";
RL Trends Biochem. Sci. 25:363-365(2000).
RN [2] {ECO:0000313|EMBL:AAN28355.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 50154 {ECO:0000313|EMBL:AAN28355.1};
RA Lang F.B., Bullerwell C.;
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AAN28355.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 50154 {ECO:0000313|EMBL:AAN28355.1};
RX PubMed=12401173; DOI=10.1016/S0960-9822(02)01187-9;
RA Lang B.F., O'Kelly C., Nerad T., Gray M.W., Burger G.;
RT "The closest unicellular relatives of animals.";
RL Curr. Biol. 12:1773-1778(2002).
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|ARBA:ARBA00004673, ECO:0000256|RuleBase:RU000369}.
CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC multisubunit enzyme composed of a catalytic core of 3 subunits and
CC several supernumerary subunits. The complex exists as a monomer or a
CC dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1
CC complex, complex III, CIII). {ECO:0000256|ARBA:ARBA00011164}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC inner membrane {ECO:0000256|RuleBase:RU000369}; Multi-pass membrane
CC protein {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; AF538053; AAN28355.1; -; Genomic_DNA.
DR RefSeq; NP_696984.1; NC_004309.1.
DR AlphaFoldDB; Q8HIS9; -.
DR STRING; 81824.Q8HIS9; -.
DR GeneID; 805261; -.
DR InParanoid; Q8HIS9; -.
DR UniPathway; UPA00705; -.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IBA:GO_Central.
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:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR CDD; cd01663; Cyt_c_Oxidase_I; 1.
DR Gene3D; 1.20.210.10; Cytochrome c oxidase-like, subunit I domain; 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; IPR033944; Cyt_c_oxase_su1_dom.
DR InterPro; IPR014241; Cyt_c_oxidase_su1_bac.
DR NCBIfam; TIGR02891; CtaD_CoxA; 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.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 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|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000369};
KW Metal-binding {ECO:0000256|RuleBase:RU000369};
KW Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:AAN28355.1};
KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369};
KW Oxidoreductase {ECO:0000313|EMBL:AAN28355.1};
KW Respiratory chain {ECO:0000256|RuleBase:RU000369};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000369};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; 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..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 233..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 269..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 305..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 340..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 381..399
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 411..432
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 452..475
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..527
FT /note="Cytochrome oxidase subunit I profile"
FT /evidence="ECO:0000259|PROSITE:PS50855"
SQ SEQUENCE 534 AA; 59304 MW; EF8142229B48628F CRC64;
MSWLTRWVFS TNHKDIGVLY FIFGSFSGFL GTAMSVIIRM ELSIPGSPFL AGDSHLYNVI
VTAHAFLMIF FLVMPFLMGG FGNFFVPLMI GAPDMSFPRM NNISFWLLPP SLILLVASSL
VEGGAGTGWT VYPPLSSVEF HSGGSVDLAI FSLHLAGVSS LLGASNFITT ILNMRAPGMT
MHKLPLFVWA VFITAILLLL SLPVLAAGIT MLLTDRNFNT SFFDPAGGGD PILYQHLFWF
FGHPEVYILI IPGFGIVSHI VSTFSDKPVF GYLGMVYAML SIGLLGFIVW AHHMYTVGMD
VDTRAYFTAS TMIIAVPTGI KIFSWLGTMY GGSIRLKVPM YWALGFIFLF TLGGITGVML
ANGGLDIALH DTYYVVAHFH YVLSMGAVFA LIGGVYYWIG KVTGYAYPET WGKIHFWLMF
IGVNLTFFPQ HFLGLAGFPR RYNDFPDAYA EWNLLSSFGS LISVVAVIVF MYVIYRTLTD
GVVVGNNYWR SKELFEKEGD IPTIHSLEWA ETSPPHFHCY NELPYLVASR THTS
//
