AC   MF_03194;
DC   Protein; auto
c?   <OC:Eukaryota>
TR   HAMAP; MF_01658; -; 1; level=0
XX
Names: DMQ_hydroxylase_COQ7
XX
ID   COQ7
DE   RecName: Full=5-demethoxyubiquinone hydroxylase, mitochondrial;
DE            Short=DMQ hydroxylase;
DE            EC=1.14.99.60;
DE   AltName: Full=Ubiquinone biosynthesis monooxygenase COQ7;
case <OC:Vertebrata>
DE   + AltName: Full=Timing protein clk-1 homolog;
end case
case <OC:Vertebrata> or <OC:Fungi> or <OC:Viridiplantae>
GN   Name=COQ7;
else case <OC:Drosophilidae>
GN   Name=Coq7;
else case <OC:Insecta> or <OC:Dictyostelia>
GN   Name=coq7;
else case <OC:Caenorhabditis>
GN   Name=clk-1;
end case
XX
case <OC:Saccharomyces>
CC   -!- FUNCTION: Catalyzes the hydroxylation of 2-hexaprenyl-3-methyl-6-
CC       methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis. Has
CC       also a structural role in the COQ enzyme complex, stabilizing COQ3 and
CC       COQ4 polypeptides.
else case <OC:Metazoa>
CC   -!- FUNCTION: Catalyzes the hydroxylation of 2-polyprenyl-3-methyl-6-
CC       methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis. Has
CC       also a structural role in the COQ enzyme complex, stabilizing other COQ
CC       polypeptides. Involved in lifespan determination in a ubiquinone-
CC       independent manner.
else
CC   -!- FUNCTION: Catalyzes the hydroxylation of 2-polyprenyl-3-methyl-6-
CC       methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis. Has
CC       also a structural role in the COQ enzyme complex, stabilizing other COQ
CC       polypeptides.
end case
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol +
CC         AH2 + O2 = A + a 3-demethylubiquinol + H2O; Xref=Rhea:RHEA:50908,
CC         Rhea:RHEA-COMP:10859, Rhea:RHEA-COMP:10914, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:84167, ChEBI:CHEBI:84422; EC=1.14.99.60;
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC       Note=Binds 2 iron ions per subunit.;
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
case <OC:Vertebrata>
CC   -!- SUBUNIT: Component of a multi-subunit COQ enzyme complex, composed of
CC       at least @gn(COQ3), @gn(COQ4), @gn(COQ5), @gn(COQ6), @gn(COQ7) and
CC       @gn(COQ9). Interacts with @gn(ADCK4) and @gn(COQ6). Interacts with
CC       @gn(COQ9).
else case <OC:Fungi>
CC   -!- SUBUNIT: Component of a multi-subunit COQ enzyme complex, composed of
CC       at least @gn(COQ3), @gn(COQ4), @gn(COQ5), @gn(COQ6), @gn(COQ7) and
CC       @gn(COQ9).
else
CC   -!- SUBUNIT: Component of a multi-subunit COQ enzyme complex.
end case
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane
CC       protein; Matrix side.
case not <AnyFeature:TransitM>
CC   -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC       transit peptide but none has been predicted.
end case
CC   -!- SIMILARITY: Belongs to the COQ7 family.
XX
DR   Pfam; PF03232; COQ7; 1; trigger=no
DR   General; TransitM; -; 0-1; trigger=yes
XX
KW   Iron
KW   Membrane
KW   Metal-binding
KW   Mitochondrion
KW   Mitochondrion inner membrane
KW   Monooxygenase
KW   Oxidoreductase
KW   Ubiquinone biosynthesis
XX
GO   GO:0031314; C:extrinsic component of mitochondrial inner membrane
GO   GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
GO   GO:0006744; P:ubiquinone biosynthetic process
XX
FT   From: COQ7_PSEAE (Q9I5R6)
FT   BINDING         64
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT   Condition: E
FT   BINDING         94
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT   Condition: E
FT   BINDING         94
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   Condition: E
FT   BINDING         97
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT   Condition: H
FT   BINDING         146
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   Condition: E
FT   BINDING         178
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT   Condition: E
FT   BINDING         178
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   Condition: E
FT   BINDING         181
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   Condition: H
XX
Size: 181-268;
Related: None;
Template: P41735; Q9I5R6; P97478;
Scope:
 Eukaryota
Fusion:
 Nter: None
 Cter: None
Duplicate: in ANOGA, MACMU
Plasmid: None
Comments: None
XX
# Revision 1.9 2022/11/19
//