ID COX3_CANGA Reviewed; 269 AA. AC Q85Q96; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 13-SEP-2023, entry version 107. 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 glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus). OG Mitochondrion. OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces. OX NCBI_TaxID=284593; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS RC 138; RX PubMed=12527359; DOI=10.1016/s0014-5793(02)03749-3; RA Koszul R., Malpertuy A., Frangeul L., Bouchier C., Wincker P., Thierry A., RA Duthoy S., Ferris S., Hennequin C., Dujon B.; RT "The complete mitochondrial genome sequence of the pathogenic yeast Candida RT (Torulopsis) glabrata."; RL FEBS Lett. 534:39-48(2003). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ511533; CAD54427.1; -; Genomic_DNA. DR RefSeq; NP_818786.1; NC_004691.1. DR AlphaFoldDB; Q85Q96; -. DR SMR; Q85Q96; -. DR STRING; 284593.Q85Q96; -. DR EnsemblFungi; CaglfMp12-T; CaglfMp12-T-p1; CaglfMp12. DR GeneID; 807011; -. DR KEGG; cgr:CaglfMp12; -. DR CGD; CAL0139492; COX3. DR VEuPathDB; FungiDB:B1J91_Mp12; -. DR VEuPathDB; FungiDB:CaglfMp12; -. DR InParanoid; Q85Q96; -. DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; ISO:CGD. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; ISO:CGD. DR CDD; cd01665; Cyt_c_Oxidase_III; 1. DR Gene3D; 1.10.287.70; -; 1. DR Gene3D; 1.20.120.80; Cytochrome c oxidase, subunit III, four-helix bundle; 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:SF7; CYTOCHROME C OXIDASE SUBUNIT 3; 1. DR PANTHER; PTHR11403; CYTOCHROME C OXIDASE SUBUNIT III; 1. DR Pfam; PF00510; COX3; 1. DR SUPFAM; SSF81452; Cytochrome c oxidase subunit III-like; 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_0000183752" FT TRANSMEM 21..41 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 45..65 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 90..110 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 138..160 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; 30717 MW; B9890E82E064080E CRC64; MTHLERSRHQ QYPYHMVLPS PWPMLLSFAL LSLTLSLGLT MHGYIGNMNL VYLALLVVTL TSVFWFRDVI AEATYLGDHT IAVRKGINLG FLLFVLSEVL IFAGLFWAYF HSAMSPDIVL GASWPPVGIQ AVQPTELPLL NTIILLSSGA TITYSHHALI CRNRNKALSG LFITIWLIII FVTCQYIEYT NAAFTISDGV YGSVFYAGTG LHFLHMVMLA VMLIICYWRM RTYQFTSTHH VGFETTILYC HVLDIIWLFL YIVFYWWGV //