COX3_CANPA
ID COX3_CANPA Reviewed; 269 AA.
AC Q34214;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Cytochrome c oxidase subunit 3;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c oxidase polypeptide III;
DE AltName: Full=Cytochrome oxidase subunit 3;
GN Name=COX3;
OS Candida parapsilosis (Yeast).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5480;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SR23 / CBS 7157;
RX PubMed=7521869; DOI=10.1128/jb.176.18.5622-5630.1994;
RA Nosek J., Fukuhara H.;
RT "NADH dehydrogenase subunit genes in the mitochondrial DNA of yeasts.";
RL J. Bacteriol. 176:5622-5630(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SR23 / CBS 7157;
RX PubMed=15449175; DOI=10.1007/s00438-004-1046-0;
RA Nosek J., Novotna M., Hlavatovicova Z., Ussery D.W., Fajkus J., Tomaska L.;
RT "Complete DNA sequence of the linear mitochondrial genome of the pathogenic
RT yeast Candida parapsilosis.";
RL Mol. Genet. Genomics 272:173-180(2004).
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:P00420}.
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:P00420};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC Evidence={ECO:0000250|UniProtKB:P00420};
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:P00420}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00420}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P00420}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family.
CC {ECO:0000305}.
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DR EMBL; X74411; CAE54607.1; -; Genomic_DNA.
DR RefSeq; NP_943645.1; NC_005253.2.
DR AlphaFoldDB; Q34214; -.
DR SMR; Q34214; -.
DR GeneID; 2657780; -.
DR CGD; CAL0000144971; CapafMp13.
DR VEuPathDB; FungiDB:CapafMp13; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:EnsemblFungi.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:EnsemblFungi.
DR CDD; cd01665; Cyt_c_Oxidase_III; 1.
DR Gene3D; 1.20.120.80; -; 1.
DR InterPro; IPR024791; Cyt_c/ubiquinol_Oxase_su3.
DR InterPro; IPR033945; Cyt_c_oxase_su3_dom.
DR InterPro; IPR000298; Cyt_c_oxidase-like_su3.
DR InterPro; IPR035973; Cyt_c_oxidase_su3-like_sf.
DR InterPro; IPR013833; Cyt_c_oxidase_su3_a-hlx.
DR PANTHER; PTHR11403; PTHR11403; 1.
DR Pfam; PF00510; COX3; 1.
DR SUPFAM; SSF81452; SSF81452; 1.
DR PROSITE; PS50253; COX3; 1.
PE 3: Inferred from homology;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Translocase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..269
FT /note="Cytochrome c oxidase subunit 3"
FT /id="PRO_0000183753"
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 269 AA; 30518 MW; 71E15660C2E7C9CD CRC64;
MTNNVRGYLQ LHPFHLVGPS PWPIFTSFSL MDLAFSIALN SHGYMANNFY IILSIITVLY
SMTLWFKDII AESTYLGDHT IAVKRGLNQG FLLFVVSEIL IFASLFWAYL HSAVNPTMDL
GMSWPPVGID VISPAELPLL NTIILLASGV TITYAHHALI NGNRANTLYG FIYSTLLIAL
FVMFQFLEYK YAGFTITDGV YGSTFYSLTG LHGLHMIMLT IMLVICTWRV YNYDFTNTSH
VGAETTILYL HVLDVIWLFI YIIVYWWGS
