AC   MF_00472;
DC   Protein; auto
c?   <OC:Bacteria>
TR   HAMAP; MF_00472; -; 1; level=0
XX
Names: UbiG
XX
ID   UBIG
case <OC:Escherichia>
DE   RecName: Full=Ubiquinone biosynthesis O-methyltransferase;
DE   AltName: Full=3-demethylubiquinone-8 3-O-methyltransferase;
DE            EC=2.1.1.64;
DE   AltName: Full=2-octaprenyl-6-hydroxyphenol methylase;
DE            EC=2.1.1.222;
else
DE   RecName: Full=Ubiquinone biosynthesis O-methyltransferase;
DE   AltName: Full=3-demethylubiquinone 3-O-methyltransferase;
DE            EC=2.1.1.64;
DE   AltName: Full=2-polyprenyl-6-hydroxyphenol methylase;
DE            EC=2.1.1.222;
end case
GN   Name=ubiG;
XX
CC   -!- FUNCTION: O-methyltransferase that catalyzes the 2 O-methylation steps
CC       in the ubiquinone biosynthetic pathway.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3-demethylubiquinol + S-adenosyl-L-methionine = a ubiquinol
CC         + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:44380, Rhea:RHEA-
CC         COMP:9566, Rhea:RHEA-COMP:10914, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17976, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:84422; EC=2.1.1.64;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3-(all-trans-polyprenyl)benzene-1,2-diol + S-adenosyl-L-
CC         methionine = a 2-methoxy-6-(all-trans-polyprenyl)phenol + H(+) + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:31411, Rhea:RHEA-COMP:9550,
CC         Rhea:RHEA-COMP:9551, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:62729, ChEBI:CHEBI:62731;
CC         EC=2.1.1.222;
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. UbiG/COQ3
CC       family.
XX
DR   NCBIfam; TIGR01983; UbiG; 1; trigger=no
XX
KW   Ubiquinone biosynthesis
KW   Transferase
KW   Methyltransferase
KW   S-adenosyl-L-methionine
XX
GO   GO:0061542; F:3-demethylubiquinol-n 3-O-methyltransferase activity
GO   GO:0006744; P:ubiquinone biosynthetic process
XX
FT   From: UBIG_ECOLI (P17993)
FT   BINDING         44
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   Condition: R
FT   BINDING         64
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   Condition: G
FT   BINDING         85
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   Condition: D
FT   BINDING         129
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
XX
Size: 232-261;
Related: None;
Template: P17993;
Scope:
 Bacteria; Pseudomonadota
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: Ubiquinones from different organisms have a different number of
 prenyl units (for example, ubiquinone-8 in E.coli, ubiquinone-6 in Saccharomyces,
 ubiquinone-9 in rat and ubiquinone-10 in human), and thus the natural substrate
 for the enzymes from different organisms has a different number of prenyl units.
XX
# Revision 1.32 2023/06/01
//