COX2_DEBHA
ID COX2_DEBHA Reviewed; 246 AA.
AC A9RAG1; B0LCE8; B0LCE9; B4F4K1; B4F4K2; B4F4K4; B4F4K8; Q34322;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Cytochrome c oxidase subunit 2;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c oxidase polypeptide II;
GN Name=COX2;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=18673395; DOI=10.1111/j.1567-1364.2008.00409.x;
RA Sacerdot C., Casaregola S., Lafontaine I., Tekaia F., Dujon B.,
RA Ozier-Kalogeropoulos O.;
RT "Promiscuous DNA in the nuclear genomes of hemiascomycetous yeasts.";
RL FEMS Yeast Res. 8:846-857(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-246, AND VARIANTS VAL-39; ILE-51;
RP ILE-106 AND ILE-179.
RC STRAIN=ATCC 20278 / CBS 789 / IFO 0015 / JCM 2104 / WM 66, and
RC ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=18248416; DOI=10.1111/j.1567-1364.2007.00342.x;
RA Tsui C.K.M., Daniel H.-M., Robert V., Meyer W.;
RT "Re-examining the phylogeny of clinically relevant Candida species and
RT allied genera based on multigene analyses.";
RL FEMS Yeast Res. 8:651-659(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-223, AND VARIANTS VAL-39; LEU-46;
RP ILE-51; ILE-106 AND ILE-179.
RC STRAIN=ATCC 20278 / CBS 789 / IFO 0015 / JCM 2104 / WM 66, CBS 1961,
RC CBS 766, CLIB 381, CLIB 660, and Kam473;
RA Nguyen H.V., Gaillardin C., Neuveglise C.;
RT "Differentiation of Candida famata and Debaryomyces hansenii by rDNA
RT intergenic spacer fingerprinting and revaluation of phylogenetic
RT relationships between D.hansenii, C.famata, D.fabryi and C.flareri.
RT Description of D.vietnamensis sp. nov.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-189.
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RA Nakagawa Y.;
RT "Amplification and sequencing of cytochrome c oxidase subunit II gene for
RT phylogenetic analysis of yeast mitochondria.";
RL Submitted (JUN-1995) 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: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 -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC {ECO:0000305}.
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DR EMBL; DQ508940; ABF58062.1; -; Genomic_DNA.
DR EMBL; EF599377; ABU80663.1; -; Genomic_DNA.
DR EMBL; EF599378; ABU80664.1; -; Genomic_DNA.
DR EMBL; AM991984; CAQ51421.1; -; Genomic_DNA.
DR EMBL; AM991986; CAQ51423.1; -; Genomic_DNA.
DR EMBL; AM991987; CAQ51424.1; -; Genomic_DNA.
DR EMBL; AM991985; CAQ51422.1; -; Genomic_DNA.
DR EMBL; AM991991; CAQ51428.1; -; Genomic_DNA.
DR EMBL; AM991992; CAQ51429.1; -; Genomic_DNA.
DR EMBL; D55727; BAA09541.1; -; Genomic_DNA.
DR RefSeq; YP_001621413.1; NC_010166.1.
DR AlphaFoldDB; A9RAG1; -.
DR SMR; A9RAG1; -.
DR STRING; 284592.A9RAG1; -.
DR GeneID; 5845854; -.
DR KEGG; dha:cox2; -.
DR InParanoid; A9RAG1; -.
DR Proteomes; UP000000599; Mitochondrion.
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: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; -; 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 PANTHER; PTHR22888; PTHR22888; 1.
DR Pfam; PF00116; COX2; 1.
DR Pfam; PF02790; COX2_TM; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR SUPFAM; SSF81464; SSF81464; 1.
DR TIGRFAMs; TIGR02866; CoxB; 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; Reference proteome;
KW Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..246
FT /note="Cytochrome c oxidase subunit 2"
FT /id="PRO_0000355032"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 175
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 210
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 210
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 212
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 212
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 214
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 214
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 218
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
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 VARIANT 39
FT /note="M -> V (in strain: CBS 789 and CLIB 381)"
FT /evidence="ECO:0000269|PubMed:18248416, ECO:0000269|Ref.3"
FT VARIANT 46
FT /note="M -> L (in strain: CLIB 660)"
FT /evidence="ECO:0000269|Ref.3"
FT VARIANT 51
FT /note="M -> I (in strain: CBS 789 and CLIB 381)"
FT /evidence="ECO:0000269|PubMed:18248416, ECO:0000269|Ref.3"
FT VARIANT 106
FT /note="V -> I (in strain: CBS 789 and CLIB 381)"
FT /evidence="ECO:0000269|PubMed:18248416, ECO:0000269|Ref.3"
FT VARIANT 179
FT /note="M -> I (in strain: CBS 789 and CLIB 381)"
FT /evidence="ECO:0000269|PubMed:18248416, ECO:0000269|Ref.3"
FT CONFLICT 223
FT /note="I -> T (in Ref. 2; ABU80664/ABU80663 and 3;
FT CAQ51421/CAQ51422/CAQ51423/CAQ51424/CAQ51428/CAQ51429)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 246 AA; 28359 MW; 8F8982C0B23935B4 CRC64;
MIWTDVPTPW GMRFQDAATP NAEGMHELYD HMMYYLALML GLVSYMLYVM MKDYKNNTFA
YKYIKHGQTL EIMWTMFPAV MLLLMAFPSF MLLYLCDEVL TPAMTVKVVG LQWYWKYEYS
DFVSETGETV EYESYVMPED MLEEGQLRLL DTDTSMVVPV DTHVRFMVTA NDVLHCFTMP
SLGIKVDACP GRLNQVSALM QRTGVYYGQC SELCGVNHGL MPIKTECVPI GDFVEWLGEQ
ENVYVA
