ID   COX2_KLULA              Reviewed;         247 AA.
AC   P20387; Q6DN57;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 3.
DT   08-NOV-2023, entry version 139.
DE   RecName: Full=Cytochrome c oxidase subunit 2;
DE            EC=7.1.1.9;
DE   AltName: Full=Cytochrome c oxidase polypeptide II;
DE   Flags: Precursor;
GN   Name=COX2;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OG   Mitochondrion.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 90735 / K8;
RX   PubMed=2171241; DOI=10.1002/yea.320060505;
RA   Hardy C.M., Clark-Walker G.D.;
RT   "Nucleotide sequence of the cytochrome oxidase subunit 2 and val-tRNA genes
RT   and surrounding sequences from Kluyveromyces lactis K8 mitochondrial DNA.";
RL   Yeast 6:403-410(1990).
RN   [2]
RP   SEQUENCE REVISION TO 81-82.
RA   Hardy C.M.;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 76492 / CBS 2359/152 / CLIB 210;
RX   PubMed=15691736; DOI=10.1016/j.femsyr.2004.09.003;
RA   Zivanovic Y., Wincker P., Vacherie B., Bolotin-Fukuhara M., Fukuhara H.;
RT   "Complete nucleotide sequence of the mitochondrial DNA from Kluyveromyces
RT   lactis.";
RL   FEMS Yeast Res. 5:315-322(2005).
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:P00410}.
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:P00410};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC         Evidence={ECO:0000250|UniProtKB:P00410};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000250|UniProtKB:P00410};
CC       Note=Binds a dinuclear copper A center per subunit.
CC       {ECO:0000250|UniProtKB:P00410};
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:P00410}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P00410}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P00410}.
CC   -!- PTM: The signal sequence of COX2 is processed by IMP1.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAT64953.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X15999; CAA34129.2; -; Genomic_DNA.
DR   EMBL; AY654900; AAT64953.1; ALT_INIT; Genomic_DNA.
DR   PIR; S11171; OBVK2M.
DR   RefSeq; YP_054502.1; NC_006077.1.
DR   AlphaFoldDB; P20387; -.
DR   SMR; P20387; -.
DR   STRING; 284590.P20387; -.
DR   PaxDb; 284590-P20387; -.
DR   GeneID; 2914081; -.
DR   KEGG; kla:KllafMp06; -.
DR   InParanoid; P20387; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR   CDD; cd13912; CcO_II_C; 1.
DR   Gene3D; 1.10.287.90; -; 1.
DR   Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1.
DR   InterPro; IPR045187; CcO_II.
DR   InterPro; IPR002429; CcO_II-like_C.
DR   InterPro; IPR034210; CcO_II_C.
DR   InterPro; IPR001505; Copper_CuA.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR014222; Cyt_c_oxidase_su2.
DR   InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR   InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf.
DR   NCBIfam; TIGR02866; CoxB; 1.
DR   PANTHER; PTHR22888:SF9; CYTOCHROME C OXIDASE SUBUNIT 2; 1.
DR   PANTHER; PTHR22888; CYTOCHROME C OXIDASE, SUBUNIT II; 1.
DR   Pfam; PF00116; COX2; 1.
DR   Pfam; PF02790; COX2_TM; 1.
DR   PRINTS; PR01166; CYCOXIDASEII.
DR   SUPFAM; SSF49503; Cupredoxins; 1.
DR   SUPFAM; SSF81464; Cytochrome c oxidase subunit II-like, transmembrane region; 1.
DR   PROSITE; PS00078; COX2; 1.
DR   PROSITE; PS50857; COX2_CUA; 1.
DR   PROSITE; PS50999; COX2_TM; 1.
PE   3: Inferred from homology;
KW   Copper; Electron transport; Magnesium; Membrane; Metal-binding;
KW   Mitochondrion; Mitochondrion inner membrane; Respiratory chain; Signal;
KW   Translocase; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..11
FT                   /evidence="ECO:0000250"
FT   CHAIN           12..247
FT                   /note="Cytochrome c oxidase subunit 2"
FT                   /id="PRO_0000006039"
FT   TOPO_DOM        12..38
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        60..78
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        102..247
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   BINDING         182
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A1"
FT                   /evidence="ECO:0000250|UniProtKB:P00410"
FT   BINDING         217
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A1"
FT                   /evidence="ECO:0000250|UniProtKB:P00410"
FT   BINDING         217
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A2"
FT                   /evidence="ECO:0000250|UniProtKB:P00410"
FT   BINDING         219
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A2"
FT                   /evidence="ECO:0000250|UniProtKB:P00410"
FT   BINDING         219
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="ligand shared with subunit 1"
FT                   /evidence="ECO:0000250|UniProtKB:P00410"
FT   BINDING         221
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A1"
FT                   /evidence="ECO:0000250|UniProtKB:P00410"
FT   BINDING         221
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A2"
FT                   /evidence="ECO:0000250|UniProtKB:P00410"
FT   BINDING         225
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A2"
FT                   /evidence="ECO:0000250|UniProtKB:P00410"
FT   BINDING         228
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A1"
FT                   /evidence="ECO:0000250|UniProtKB:P00410"
FT   CONFLICT        86
FT                   /note="A -> D (in Ref. 1 and 3)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   247 AA;  28102 MW;  AA9261AFC1C138DB CRC64;
     MFYLLNSIIM NDVPTPYGMY FQDSATPNQE GILELHDNIM FYLFIILGLV SWLLFTIVRT
     YSKNPIAYKY IKHGQTIEII WTIFPAVILL IIAFPSFILL YLCDEVISPA MTIKAIGLQW
     YWKYEYSDFI NDNGETVEFE SYVIPEDLLE DGQLRLLDTD TSVVVPVDTH IRFVVTAADV
     IHDFAVPSLG IKIDAAPGRL NQVSALIQRE GVFYGQCSEI CGQSHSAMPI KIEAVSLPAF
     LEWLNEQ
//