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COX1_YARLI
ID   COX1_YARLI              Reviewed;         535 AA.
AC   Q9B6E7;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Cytochrome c oxidase subunit 1;
DE            EC=7.1.1.9;
DE   AltName: Full=Cytochrome c oxidase polypeptide I;
GN   Name=COX1;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OG   Mitochondrion.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20460 / W29 / CBS 7504 / IFP29;
RX   DOI=10.1002/cfg.72;
RA   Kerscher S., Durstewitz G., Casaregola S., Gaillardin C., Brandt U.;
RT   "The complete mitochondrial genome of Yarrowia lipolytica.";
RL   Comp. Funct. Genomics 2:80-90(2001).
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; AJ307410; CAC28091.2; -; Genomic_DNA.
DR   RefSeq; NP_075425.2; NC_002659.1.
DR   AlphaFoldDB; Q9B6E7; -.
DR   SMR; Q9B6E7; -.
DR   STRING; 284591.Q9B6E7; -.
DR   GeneID; 802596; -.
DR   KEGG; yli:YalifMp03; -.
DR   InParanoid; Q9B6E7; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000001300; Mitochondrion.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0009060; P:aerobic respiration; IBA:GO_Central.
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   GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
DR   CDD; cd01663; Cyt_c_Oxidase_I; 1.
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; IPR033944; Cyt_c_oxase_su1_dom.
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   Calcium; Copper; Electron transport; Heme; Iron; Magnesium; Membrane;
KW   Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Respiratory chain; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..535
FT                   /note="Cytochrome c oxidase subunit 1"
FT                   /id="PRO_0000183431"
FT   TRANSMEM        21..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        63..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        188..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        271..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        342..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        379..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        414..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        456..478
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         44
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         49
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         67
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         373
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         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         381
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         383
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   CROSSLNK        246..250
FT                   /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
SQ   SEQUENCE   535 AA;  58935 MW;  B47B1E3FD4AF9577 CRC64;
     MSLKLNIQRW LFSTNAKDIA VLYFIFALFS AMIGTGLSAI IRLELANTGS PFLHGNTQAF
     NVVITAHAIL MIFFFVMPAL VGGFGNYLMP LMLGASDMAF ARLNNISFWL LVPSLILILT
     SALVEAGAGT GWTVYFPLAG IQSHSGPAVD LAIFSLHLSG FSSLLGAINF ITTFINMRTI
     GMKYENVPLF AWAVLFTAIL LLLSLPVLAA GLTMGIFDRN FNTSFFEYAG GGDAVLYQHL
     FYWWNHPEVY ILIIPGFGII SHAVSAIASK PVFGVQGMIY AMWSIGLLGF CVWSHHMFAV
     GLDSDTRAYF TSATMVIAVP TSIKIFSWLA TLYGGTIRLN VTALFALGFI FLFTIGGLTG
     VVLANSALDI PFHDSYYVVA HFHYVLSMGA VFSIFCGWYL WSPKILGLHY NERLSHIHFW
     LMFIGVNVTF FPMHFLGLQG MPRRINDYPD AFIGWNQVAS LGSIISIVAS IVFIYVVYDQ
     LTNGLHQGNK ALDSQFKPSF MGTNLNVEGY TGPTLEWTVS TPPSLHAFNT PAVLY
 
 
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