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COX3_ALLMA
ID   COX3_ALLMA              Reviewed;         274 AA.
AC   P80439;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 95.
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;
OS   Allomyces macrogynus.
OG   Mitochondrion.
OC   Eukaryota; Fungi; Fungi incertae sedis; Blastocladiomycota;
OC   Blastocladiomycota incertae sedis; Blastocladiomycetes; Blastocladiales;
OC   Blastocladiaceae; Allomyces.
OX   NCBI_TaxID=28583;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 46923 / Burma 3-35 (35OC);
RX   PubMed=7490780; DOI=10.1007/bf00175824;
RA   Paquin B., Forget L., Roewer I., Lang B.F.;
RT   "Molecular phylogeny of Allomyces macrogynus: congruency between nuclear
RT   ribosomal RNA- and mitochondrial protein-based trees.";
RL   J. Mol. Evol. 41:657-665(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 46923 / Burma 3-35 (35OC);
RX   PubMed=8636971; DOI=10.1006/jmbi.1996.0056;
RA   Paquin B., Lang B.F.;
RT   "The mitochondrial DNA of Allomyces macrogynus: the complete genomic
RT   sequence from an ancestral fungus.";
RL   J. Mol. Biol. 255:688-701(1996).
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; U41288; AAC49226.1; -; Genomic_DNA.
DR   PIR; S63643; S63643.
DR   RefSeq; NP_043725.1; NC_001715.1.
DR   AlphaFoldDB; P80439; -.
DR   SMR; P80439; -.
DR   GeneID; 801893; -.
DR   VEuPathDB; FungiDB:AlmafMp06; -.
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:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019646; P:aerobic electron transport chain; IEA:InterPro.
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..274
FT                   /note="Cytochrome c oxidase subunit 3"
FT                   /id="PRO_0000183730"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        208..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        248..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   274 AA;  30630 MW;  4B2A835ED31386F3 CRC64;
     MTKKLINQFK SFQVHPYHLV EPSPWPLGAS VACLILTLGG VMKFHGFAAG DIGLPLGLIL
     VLASMLLWWR DVIREATYQG HHTKTVKYGI TLGVVLFIVS EILLFFSLFW AFFHSSLAPS
     VELGSTWPPV GIEPLNPFEV PLLNTIILLT SGCTITVSHA KIISGDRGAT ILYLILTILL
     AWMFLGLQWV EYVNAPFTIA DSVYGSTFFV ATGFHGLHVM IGTIFLTVSL NRILSYHLTS
     GHHLGYEAAI WYWHVVDVIW LFLYVSVYYW GSNV
 
 
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