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COX1_PLAFA
ID   COX1_PLAFA              Reviewed;         476 AA.
AC   Q02766;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Cytochrome c oxidase subunit 1;
DE            EC=7.1.1.9;
DE   AltName: Full=Cytochrome c oxidase polypeptide I;
GN   Name=MT-CO1; Synonyms=COI, COXI, MTCO1;
OS   Plasmodium falciparum.
OG   Mitochondrion.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=5833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1542578; DOI=10.1093/nar/20.4.879;
RA   Feagin J.E., Werner E., Gardner M.J., Williamson D.H., Wilson R.J.;
RT   "Homologies between the contiguous and fragmented rRNAs of the two
RT   Plasmodium falciparum extrachromosomal DNAs are limited to core
RT   sequences.";
RL   Nucleic Acids Res. 20:879-887(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MALAY CAMP;
RX   PubMed=3054536; DOI=10.1016/0166-6851(88)90098-9;
RA   Suplick K., Akella R., Saul A.J., Vaidya A.;
RT   "Molecular cloning and partial sequence of a 5.8 kilobase pair repetitive
RT   DNA from Plasmodium falciparum.";
RL   Mol. Biochem. Parasitol. 30:289-290(1988).
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:0000250|UniProtKB:P00401}.
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:0000250|UniProtKB:P00401};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC         Evidence={ECO:0000250|UniProtKB:P00401};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P00401};
CC       Note=Binds 2 heme A groups non-covalently per subunit.
CC       {ECO:0000250|UniProtKB:P00401};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000250|UniProtKB:P00401};
CC       Note=Binds a copper B center. {ECO:0000250|UniProtKB:P00401};
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000250|UniProtKB:P00401}.
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:0000250|UniProtKB:P00401}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P00401}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P00401}.
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC       {ECO:0000305}.
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DR   EMBL; M76611; AAC63390.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; M99416; AAC06269.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q02766; -.
DR   SMR; Q02766; -.
DR   VEuPathDB; PlasmoDB:PF3D7_MIT02100; -.
DR   VEuPathDB; PlasmoDB:Pf7G8-2_000005000; -.
DR   VEuPathDB; PlasmoDB:Pf7G8_000015800; -.
DR   VEuPathDB; PlasmoDB:PfDd2_000011800; -.
DR   VEuPathDB; PlasmoDB:PfGA01_000021400; -.
DR   VEuPathDB; PlasmoDB:PfGB4_000031600; -.
DR   VEuPathDB; PlasmoDB:PfGN01_000029700; -.
DR   VEuPathDB; PlasmoDB:PfHB3_000018950; -.
DR   VEuPathDB; PlasmoDB:PfIT_000023900; -.
DR   VEuPathDB; PlasmoDB:PfKE01_000017500; -.
DR   VEuPathDB; PlasmoDB:PfKH01_000056600; -.
DR   VEuPathDB; PlasmoDB:PfKH02_000021000; -.
DR   VEuPathDB; PlasmoDB:PfML01_000121700; -.
DR   VEuPathDB; PlasmoDB:PfNF135_000041200; -.
DR   VEuPathDB; PlasmoDB:PfNF166_000019100; -.
DR   VEuPathDB; PlasmoDB:PfNF54_000012700; -.
DR   VEuPathDB; PlasmoDB:PfSD01_000015000; -.
DR   VEuPathDB; PlasmoDB:PfSN01_000029450; -.
DR   VEuPathDB; PlasmoDB:PfTG01_000076100; -.
DR   UniPathway; UPA00705; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045277; C:respiratory chain complex IV; ISS:UniProtKB.
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: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   PANTHER; PTHR10422; PTHR10422; 1.
DR   Pfam; PF00115; COX1; 1.
DR   PRINTS; PR01165; CYCOXIDASEI.
DR   SUPFAM; SSF81442; SSF81442; 1.
DR   PROSITE; PS50855; COX1; 1.
DR   PROSITE; PS00077; COX1_CUB; 1.
PE   3: Inferred from homology;
KW   Calcium; Copper; Electron transport; Heme; Iron; Magnesium; Membrane;
KW   Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW   Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..476
FT                   /note="Cytochrome c oxidase subunit 1"
FT                   /id="PRO_0000183396"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        278..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        310..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        345..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        379..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        415..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        455..475
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         42
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         66
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_note="low-spin"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         246
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         250
FT                   /ligand="O2"
FT                   /ligand_id="ChEBI:CHEBI:15379"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   BINDING         295
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         296
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         374
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="ligand shared with subunit 2"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         375
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="ligand shared with subunit 2"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         382
FT                   /ligand="heme a3"
FT                   /ligand_id="ChEBI:CHEBI:83282"
FT                   /ligand_note="high-spin"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         384
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_note="low-spin"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         448
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   CROSSLNK        246..250
FT                   /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
SQ   SEQUENCE   476 AA;  52729 MW;  A51CEE2F28618AA9 CRC64;
     MVLNRYSLIT NCNHKTLGLY YLWFSFLFGS YGFLLSVILR TELYSSSLRI IAQENVNLYN
     MIFTIHGIIM IFFNIMPGLF GGFGNYFLPI LCGSPELAYP RINSISLLLQ PIAFVLVILS
     TAAEFGGGTG WTLYPPLSTS LMSLSPVAVD VIIFGLLVSG VASIMSSLNF ITTVMHLRAK
     GLTLGILSVS TWSLIITSGM LLLTLPVLTG GVLMLLSDLH FNTLFFDPTF AGDPILYQHL
     FWFFGHPEVY ILILPAFGVI SHVISTNYCR NLFGNQSMIL AMGCIAVLGS LVWVHHMYTT
     GLEVDTRAYF TSTTILISIP TGTKVFNWIC TYMSSNFGMI HSSSLLSLLF ICTFTFGGTT
     GVILGNAAID VALHDTYYVI AHFHFVLSIG AIIGLFTTVS AFQDNFFGKN LRENSIVILW
     SMLFFVGVIL TFLPMHFLGF NVMPRRIPDY PDALNGWNMI CSIGSTMTLF GLLIFK
 
 
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