COX3_YEAST
ID COX3_YEAST Reviewed; 269 AA.
AC P00420; A0A0A7P087; Q9ZZV9;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Cytochrome c oxidase subunit 3;
DE EC=7.1.1.9 {ECO:0000269|PubMed:30598554};
DE AltName: Full=Cytochrome c oxidase polypeptide III;
GN Name=COX3; Synonyms=OXI2; OrderedLocusNames=Q0275;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=D273-10B/A48;
RX PubMed=6248512; DOI=10.1016/s0021-9258(18)43718-0;
RA Thalenfeld B.E., Tzagoloff A.;
RT "Assembly of the mitochondrial membrane system. Sequence of the oxi 2 gene
RT of yeast mitochondrial DNA.";
RL J. Biol. Chem. 255:6173-6180(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3549452; DOI=10.1016/0378-1119(86)90060-0;
RA de Zamaroczy M., Bernardi G.;
RT "The primary structure of the mitochondrial genome of Saccharomyces
RT cerevisiae -- a review.";
RL Gene 47:155-177(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9872396; DOI=10.1016/s0014-5793(98)01467-7;
RA Foury F., Roganti T., Lecrenier N., Purnelle B.;
RT "The complete sequence of the mitochondrial genome of Saccharomyces
RT cerevisiae.";
RL FEBS Lett. 440:325-331(1998).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP COMPOSITION OF THE CYTOCHROME C OXIDASE COMPLEX.
RX PubMed=1331058; DOI=10.1016/s0021-9258(18)41697-3;
RA Taanman J.-W., Capaldi R.A.;
RT "Purification of yeast cytochrome c oxidase with a subunit composition
RT resembling the mammalian enzyme.";
RL J. Biol. Chem. 267:22481-22485(1992).
RN [6]
RP COMPOSITION OF THE CYTOCHROME C OXIDASE COMPLEX, AND BLOCKED N-TERMINUS.
RX PubMed=7851399; DOI=10.1111/j.1432-1033.1995.tb20388.x;
RA Geier B.M., Schagger H., Ortwein C., Link T.A., Hagen W.R., Brandt U.,
RA Von Jagow G.;
RT "Kinetic properties and ligand binding of the eleven-subunit cytochrome-c
RT oxidase from Saccharomyces cerevisiae isolated with a novel large-scale
RT purification method.";
RL Eur. J. Biochem. 227:296-302(1995).
RN [7]
RP FORMATION OF CYTOCHROME BC1-CYTOCHROME C OXIDASE SUPERCOMPLEX.
RX PubMed=10775262; DOI=10.1093/emboj/19.8.1777;
RA Schaegger H., Pfeiffer K.;
RT "Supercomplexes in the respiratory chains of yeast and mammalian
RT mitochondria.";
RL EMBO J. 19:1777-1783(2000).
RN [8]
RP FORMATION OF CYTOCHROME BC1-CYTOCHROME C OXIDASE SUPERCOMPLEX.
RX PubMed=10764779; DOI=10.1074/jbc.m001901200;
RA Cruciat C.M., Brunner S., Baumann F., Neupert W., Stuart R.A.;
RT "The cytochrome bc1 and cytochrome c oxidase complexes associate to form a
RT single supracomplex in yeast mitochondria.";
RL J. Biol. Chem. 275:18093-18098(2000).
RN [9]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.23 ANGSTROMS).
RX PubMed=30598556; DOI=10.1038/s41594-018-0169-7;
RA Rathore S., Berndtsson J., Marin-Buera L., Conrad J., Carroni M.,
RA Brzezinski P., Ott M.;
RT "Cryo-EM structure of the yeast respiratory supercomplex.";
RL Nat. Struct. Mol. Biol. 26:50-57(2019).
RN [10]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.35 ANGSTROMS), FUNCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=30598554; DOI=10.1038/s41594-018-0172-z;
RA Hartley A.M., Lukoyanova N., Zhang Y., Cabrera-Orefice A., Arnold S.,
RA Meunier B., Pinotsis N., Marechal A.;
RT "Structure of yeast cytochrome c oxidase in a supercomplex with cytochrome
RT bc1.";
RL Nat. Struct. Mol. Biol. 26:78-83(2019).
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 COX2 and heme A of COX1 to the
CC active site in COX1, a binuclear center (BNC) formed by heme A3 and
CC copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules
CC using 4 electrons from cytochrome c in the IMS and 4 protons from the
CC mitochondrial matrix (Probable). COX3 is a catalytic core subunit
CC (PubMed:30598554). {ECO:0000269|PubMed:30598554,
CC ECO:0000305|PubMed:30598554}.
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:0000269|PubMed:30598554};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC Evidence={ECO:0000269|PubMed:30598554};
CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC multisubunit enzyme composed of 12 subunits. The complex is composed of
CC a catalytic core of 3 subunits COX1, COX2 and COX3, encoded in the
CC mitochondrial DNA, and 9 supernumerary subunits COX4, COX5A (or COX5B),
CC COX6, COX7, COX8, COX9, COX12, COX13 and COX26, which are encoded in
CC the nuclear genome (PubMed:7851399, PubMed:30598556, PubMed:30598554).
CC The complex exists as a monomer or a dimer and forms supercomplexes
CC (SCs) in the inner mitochondrial membrane with a dimer of ubiquinol-
CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III,
CC CIII), resulting in 2 different assemblies (supercomplexes III(2)IV and
CC III(2)IV(2)) (PubMed:10775262, PubMed:10764779, PubMed:30598556,
CC PubMed:30598554). {ECO:0000269|PubMed:10764779,
CC ECO:0000269|PubMed:10775262, ECO:0000269|PubMed:30598554,
CC ECO:0000269|PubMed:30598556, ECO:0000269|PubMed:7851399}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:30598554}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:30598554}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:7851399}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family.
CC {ECO:0000305}.
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DR EMBL; J01478; AAA32153.2; -; Genomic_DNA.
DR EMBL; L36890; AAA67530.1; -; Genomic_DNA.
DR EMBL; KP263414; AIZ98899.1; -; Genomic_DNA.
DR PIR; A00487; OTBY3.
DR PIR; S78686; S78686.
DR RefSeq; NP_009328.1; NC_001224.1.
DR RefSeq; YP_009144713.1; NC_027264.1.
DR PDB; 6GIQ; EM; 3.23 A; c=1-269.
DR PDB; 6HU9; EM; 3.35 A; c/o=1-269.
DR PDB; 6T0B; EM; 2.80 A; c/p=1-269.
DR PDB; 6T15; EM; 3.29 A; c=1-269.
DR PDB; 6YMX; EM; 3.17 A; c=2-269.
DR PDB; 6YMY; EM; 3.41 A; c=2-269.
DR PDBsum; 6GIQ; -.
DR PDBsum; 6HU9; -.
DR PDBsum; 6T0B; -.
DR PDBsum; 6T15; -.
DR PDBsum; 6YMX; -.
DR PDBsum; 6YMY; -.
DR AlphaFoldDB; P00420; -.
DR SMR; P00420; -.
DR BioGRID; 34817; 36.
DR ComplexPortal; CPX-1721; Mitochondrial respiratory chain complex IV, COX5A variant.
DR ComplexPortal; CPX-1722; Mitochondrial respiratory chain complex IV, COX5B variant.
DR DIP; DIP-8133N; -.
DR IntAct; P00420; 2.
DR MINT; P00420; -.
DR STRING; 4932.Q0275; -.
DR TCDB; 3.D.4.8.1; the proton-translocating cytochrome oxidase (cox) superfamily.
DR PaxDb; P00420; -.
DR PRIDE; P00420; -.
DR EnsemblFungi; Q0275_mRNA; Q0275; Q0275.
DR GeneID; 24573142; -.
DR GeneID; 854627; -.
DR KEGG; sce:Q0275; -.
DR SGD; S000007283; COX3.
DR VEuPathDB; FungiDB:Q0275; -.
DR eggNOG; KOG4664; Eukaryota.
DR GeneTree; ENSGT00390000013064; -.
DR HOGENOM; CLU_044071_0_0_1; -.
DR InParanoid; P00420; -.
DR OMA; SIYWWGS; -.
DR BioCyc; MetaCyc:Q0275-MON; -.
DR BioCyc; YEAST:Q0275-MON; -.
DR PRO; PR:P00420; -.
DR Proteomes; UP000002311; Mitochondrion.
DR RNAct; P00420; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:ComplexPortal.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0015453; F:oxidoreduction-driven active transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0009060; P:aerobic respiration; IMP:SGD.
DR GO; GO:0045333; P:cellular respiration; IDA:ComplexPortal.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IDA:SGD.
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 1: Evidence at protein level;
KW 3D-structure; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..269
FT /note="Cytochrome c oxidase subunit 3"
FT /id="PRO_0000183874"
FT TOPO_DOM 1..22
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:30598554"
FT TRANSMEM 23..41
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:30598554"
FT TOPO_DOM 42..48
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:30598554"
FT TRANSMEM 49..73
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:30598554"
FT TOPO_DOM 74..80
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:30598554"
FT TRANSMEM 81..114
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:30598554"
FT TOPO_DOM 115..137
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:30598554"
FT TRANSMEM 138..161
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:30598554"
FT TOPO_DOM 162..164
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:30598554"
FT TRANSMEM 165..188
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:30598554"
FT TOPO_DOM 189..201
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:30598554"
FT TRANSMEM 202..230
FT /note="Helical; Name=6"
FT /evidence="ECO:0000269|PubMed:30598554"
FT TOPO_DOM 231..248
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:30598554"
FT TRANSMEM 249..265
FT /note="Helical; Name=7"
FT /evidence="ECO:0000269|PubMed:30598554"
FT TOPO_DOM 266..269
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:30598554"
FT CONFLICT 263
FT /note="V -> T (in Ref. 1; AAA32153 and 2; AAA67530)"
FT /evidence="ECO:0000305"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:6T0B"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:6T0B"
FT HELIX 22..40
FT /evidence="ECO:0007829|PDB:6T0B"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:6T0B"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:6T0B"
FT HELIX 49..74
FT /evidence="ECO:0007829|PDB:6T0B"
FT HELIX 81..113
FT /evidence="ECO:0007829|PDB:6T0B"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:6T0B"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:6YMX"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:6T0B"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:6YMX"
FT HELIX 138..160
FT /evidence="ECO:0007829|PDB:6T0B"
FT HELIX 165..190
FT /evidence="ECO:0007829|PDB:6T0B"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:6T15"
FT HELIX 201..231
FT /evidence="ECO:0007829|PDB:6T0B"
FT HELIX 241..266
FT /evidence="ECO:0007829|PDB:6T0B"
SQ SEQUENCE 269 AA; 30360 MW; 81B24A54F63BD8B1 CRC64;
MTHLERSRHQ QHPFHMVMPS PWPIVVSFAL LSLALSTALT MHGYIGNMNM VYLALFVLLT
SSILWFRDIV AEATYLGDHT MAVRKGINLG FLMFVLSEVL IFAGLFWAYF HSAMSPDVTL
GACWPPVGIE AVQPTELPLL NTIILLSSGA TVTYSHHALI AGNRNKALSG LLITFWLIVI
FVTCQYIEYT NAAFTISDGV YGSVFYAGTG LHFLHMVMLA AMLGVNYWRM RNYHLTAGHH
VGYETTIIYT HVLDVIWLFL YVVFYWWGV
