COX3_DICDI
ID COX3_DICDI Reviewed; 435 AA.
AC O21049;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Cytochrome c oxidase subunit 3;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c oxidase polypeptide III;
GN Name=cox3; ORFNames=DDB_G0294092;
OS Dictyostelium discoideum (Slime mold).
OG Mitochondrion.
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AX3;
RX PubMed=9000384; DOI=10.1007/s002940050179;
RA Ogawa S., Matsuo K., Angata K., Yanagisawa K., Tanaka Y.;
RT "Group-I introns in the cytochrome c oxidase genes of Dictyostelium
RT discoideum: two related ORFs in one loop of a group-I intron, a cox1/2
RT hybrid gene and an unusually large cox3 gene.";
RL Curr. Genet. 31:80-88(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX3;
RX PubMed=10821186; DOI=10.1007/pl00008685;
RA Ogawa S., Yoshino R., Angata K., Iwamoto M., Pi M., Kuroe K., Matsuo K.,
RA Morio T., Urushihara H., Yanagisawa K., Tanaka Y.;
RT "The mitochondrial DNA of Dictyostelium discoideum: complete sequence, gene
RT content and genome organization.";
RL Mol. Gen. Genet. 263:514-519(2000).
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; D16579; BAA21120.1; -; Genomic_DNA.
DR EMBL; AB000109; BAA78053.1; -; Genomic_DNA.
DR PIR; T43749; T43749.
DR RefSeq; NP_050071.1; NC_000895.1.
DR AlphaFoldDB; O21049; -.
DR SMR; O21049; -.
DR GeneID; 2193893; -.
DR KEGG; ddi:DidioMp04; -.
DR dictyBase; DDB_G0294092; cox3.
DR InParanoid; O21049; -.
DR PhylomeDB; O21049; -.
DR PRO; PR:O21049; -.
DR Proteomes; UP000002195; 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:0005739; C:mitochondrion; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR CDD; cd01665; Cyt_c_Oxidase_III; 1.
DR Gene3D; 1.20.120.80; -; 2.
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; 2.
DR SUPFAM; SSF81452; SSF81452; 2.
DR PROSITE; PS50253; COX3; 1.
PE 3: Inferred from homology;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..435
FT /note="Cytochrome c oxidase subunit 3"
FT /id="PRO_0000312370"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 435 AA; 50234 MW; 5AC920869B67F434 CRC64;
MKGFFENLFR QNVRSVINTG KKVGARAAAR EIINQEWGYP LANHEVLFLT NVYQPKHMKR
HPFHIVRGTV APLAVTLPLG FFVLNYFGVI SSKLGLLIAL SSFIGGLVIW TISIIFDSLY
DQQHTYEVKR GLVMGMMMFI ISEVMFFFSF FWSYFYISLS PNIAIGCVWP PYGLTVYSYM
GLPLLNTVLL LLSGAILTDG YTILTEQKAV HEKNEKVLAV EEAFKNLMNL YKTKNSINTL
TFVDERRDKF FGKESRQEDK IAEQKLIAIS AGVKELRDLD WDLYFFENPE NIEPNYKEPT
NLSVIEYALI TIYLKKRNKV IKTRLYFTLL CAVVFLACQG YEYFFAPFSM NDGIYGSLFF
LLTGFHGFHV LVGSILIGII TIRFIVGNFN LLNVGTNFQI YKNKSTGFAC TLFYWHFVDI
VWIFLYIVIY WWGSR
