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Annotation rule MF_00472
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General rule information [?]

Accession MF_00472
Dates 24-OCT-2001 (Created)
24-JAN-2020 (Last updated, Version 28)
Name UbiG
Bacteria; Proteobacteria
Template P17993 (UBIG_ECOLI)
case <OC:Bacteria>
end case

Propagated annotation [?]

Identifier, protein and gene names [?]

case <OC:Escherichia>
Protein name
RecName: Full=Ubiquinone biosynthesis O-methyltransferase;
AltName: Full=3-demethylubiquinone-8 3-O-methyltransferase;
AltName: Full=2-octaprenyl-6-hydroxyphenol methylase;
Protein name
RecName: Full=Ubiquinone biosynthesis O-methyltransferase;
AltName: Full=3-demethylubiquinone 3-O-methyltransferase;
AltName: Full=2-polyprenyl-6-hydroxyphenol methylase;
end case
Gene name

Comments [?]

Function O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Catalytic activity RHEA:44380: a 3-demethylubiquinol + S-adenosyl-L-methionine = a ubiquinol + H(+) + S-adenosyl-L-homocysteine
RHEA:31411: a 3-(all-trans-polyprenyl)benzene-1,2-diol + S-adenosyl-L-methionine = a 2-methoxy-6-(all-trans-polyprenyl)phenol + H(+) + S-adenosyl-L-homocysteine
Pathway Cofactor biosynthesis; ubiquinone biosynthesis.
Similarity Belongs to the methyltransferase superfamily. UbiG/COQ3 family.

Keywords [?]

Gene Ontology [?]

GO:0061542; Molecular function: 3-demethylubiquinol-n 3-O-methyltransferase activity.
GO:0006744; Biological process: ubiquinone biosynthetic process.

Cross-references [?]

TIGRFAMs TIGR01983; UbiG; 1;

Features [?]

From: UBIG_ECOLI (P17993)
Key     From     To       Description   Tag   Condition   FTGroup
BINDING     44     44       S-adenosyl-L-methionine     R  
BINDING     64     64       S-adenosyl-L-methionine; via carbonyl oxygen     G  
BINDING     85     85       S-adenosyl-L-methionine     D  
BINDING     129     129       S-adenosyl-L-methionine; via carbonyl oxygen        

Additional information [?]

Size range 232-261 amino acids
Related rules None
Fusion 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.