AC   MF_03111;
DC   Protein; auto
TR   HAMAP; MF_03111; -; 1; level=0
XX
Names: Coq4
XX
ID   COQ4
case <OC:Fungi> or <OC:Caenorhabditis>
DE   RecName: Full=Ubiquinone biosynthesis protein <gene_name>, mitochondrial;
DE   AltName: Full=Coenzyme Q biosynthesis protein 4;
DE   AltName: Full=4-hydroxy-3-methoxy-5-polyprenylbenzoate decarboxylase;
DE            EC=4.1.1.130;
else
DE   RecName: Full=Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial;
DE   AltName: Full=Coenzyme Q biosynthesis protein 4 homolog;
DE   AltName: Full=4-hydroxy-3-methoxy-5-polyprenylbenzoate decarboxylase;
DE            EC=4.1.1.130;
end case
case <OC:Vertebrata> or <OC:Fungi> or <OC:Dictyostelium>
GN   Name=COQ4;
else case <OC:Caenorhabditis>
GN   Name=coq-4;
end case
XX
case <OC:Mammalia> or <OC:Schizosaccharomyces>
CC   -!- FUNCTION: Lyase that catalyzes the C1-decarboxylation of 4-hydroxy-3-
CC       methoxy-5-(all-trans-decaprenyl)benzoic acid into 2-methoxy-6-(all-
CC       trans-decaprenyl)phenol during ubiquinone biosynthesis.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-hydroxy-3-methoxy-5-(all-trans-decaprenyl)benzoate + H(+) =
CC         2-methoxy-6-(all-trans-decaprenyl)phenol + CO2; Xref=Rhea:RHEA:81275,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:50774,
CC         ChEBI:CHEBI:62796; EC=4.1.1.130;
else case <OC:Saccharomyces>
CC   -!- FUNCTION: Lyase that catalyzes the C1-decarboxylation of 4-hydroxy-3-
CC       methoxy-5-(all-trans-hexaprenyl)benzoic acid into 2-methoxy-6-(all-
CC       trans-hexaprenyl)phenol during ubiquinone biosynthesis.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-hydroxy-3-methoxy-5-(all-trans-hexaprenyl)benzoate + H(+) =
CC         2-methoxy-6-(all-trans-hexaprenyl)phenol + CO2; Xref=Rhea:RHEA:44768,
CC         ChEBI:CHEBI:1109, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57916; EC=4.1.1.130;
else
CC   -!- FUNCTION: Lyase that catalyzes the C1-decarboxylation of 4-hydroxy-3-
CC       methoxy-5-(all-trans-polyprenyl)benzoic acid into 2-methoxy-6-(all-
CC       trans-polyprenyl)phenol during ubiquinone biosynthesis.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 4-hydroxy-3-methoxy-5-(all-trans-polyprenyl)benzoate + H(+)
CC         = a 2-methoxy-6-(all-trans-polyprenyl)phenol + CO2;
CC         Xref=Rhea:RHEA:81179, Rhea:RHEA-COMP:9551, Rhea:RHEA-COMP:10931,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:62731,
CC         ChEBI:CHEBI:84443; EC=4.1.1.130;
end case
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
case <OC:Saccharomyces>
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 COQ3.
else case <OC:Vertebrata> or <OC:Fungi> and not <OC:Saccharomyces>
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 COQ4 family.
XX
DR   Pfam; PF05019; Coq4; 1; trigger=no
DR   General; TransitM; -; 0-1; trigger=yes
XX
KW   Lyase
KW   Metal-binding
KW   Membrane
KW   Mitochondrion
KW   Mitochondrion inner membrane
KW   Ubiquinone biosynthesis
KW   Zinc
XX
GO   GO:0016831; F:carboxy-lyase activity
GO   GO:0008270; F:zinc ion binding
GO   GO:0031314; C:extrinsic component of mitochondrial inner membrane
GO   GO:0006744; P:ubiquinone biosynthetic process
XX
FT   From: COQ4_HUMAN (Q9Y3A0)
FT   BINDING         163
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Condition: H
FT   BINDING         164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Condition: D
FT   BINDING         167
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Condition: H
FT   BINDING         179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Condition: E
XX
Size: 187-369;
Related: None;
Template: O13525; Q9Y3A0;
Scope:
 Eukaryota
Fusion:
 Nter: None
 Cter: None
Duplicate: in PARTE, TRYCR
Plasmid: None
Comments: None
XX
# Version: 8
# Last updated date: 2025-04-01
# Created date: 2012-10-26
//