HAMAP rule MF_00472
General rule information
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| PURL | https://purl.expasy.org/hamap/rule/MF_00472 |
| Accession | MF_00472 |
| Dates | 28-FEB-2005 (Created)
14-JAN-2025 (Last updated, Version 28) |
| Name | UbiG |
| Scope(s) |
Bacteria Pseudomonadota |
| Template(s) | P17993; [ Recover all ] |
| Triggered by |
case c? <OC:Bacteria>
HAMAP; MF_00472 (Get profile general information and statistics) end case
|
Propagated annotation
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Identifier, protein and gene names
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| Identifier | UBIG |
| case <OC:Escherichia> | |
| Protein name | RecName: Full=Ubiquinone biosynthesis O-methyltransferase; AltName: Full=3-demethylubiquinone-8 3-O-methyltransferase; EC=2.1.1.64; AltName: Full=2-octaprenyl-6-hydroxyphenol methylase; EC=2.1.1.222; |
| else | |
| Protein name | RecName: Full=Ubiquinone biosynthesis O-methyltransferase; AltName: Full=3-demethylubiquinone 3-O-methyltransferase; EC=2.1.1.64; AltName: Full=2-polyprenyl-6-hydroxyphenol methylase; EC=2.1.1.222; |
| end case | |
| Gene name | Name=ubiG; |
Comments
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| FUNCTION | O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. |
| CATALYTIC ACTIVITY | Reaction=a 3-demethylubiquinol + S-adenosyl-L-methionine = a ubiquinol + S-adenosyl-L-homocysteine + H(+); Xref=Rhea:RHEA:44380, Rhea:RHEA- COMP:9566, Rhea:RHEA-COMP:10914, ChEBI:CHEBI:15378, ChEBI:CHEBI:17976, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:84422; EC=2.1.1.64; |
| CATALYTIC ACTIVITY | Reaction=a 3-(all-trans-polyprenyl)benzene-1,2-diol + S-adenosyl-L- methionine = a 2-methoxy-6-(all-trans-polyprenyl)phenol + S-adenosyl- L-homocysteine + H(+); Xref=Rhea:RHEA:31411, Rhea:RHEA-COMP:9550, Rhea:RHEA-COMP:9551, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:62729, ChEBI:CHEBI:62731; EC=2.1.1.222; |
| PATHWAY | Cofactor biosynthesis; ubiquinone biosynthesis. |
| SIMILARITY | Belongs to the methyltransferase superfamily. UbiG/COQ3 family. |
Keywords
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Gene Ontology
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| GO:0061542; Molecular function:3-demethylubiquinol 3-O-methyltransferase activity |
| GO:0006744; Biological process:ubiquinone biosynthetic process |
Cross-references
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| NCBIfam | TIGR01983; UbiG; 1; |
Features
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| From: UBIG_ECOLI (P17993) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 44 | 44 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
R | ||||||||
| BINDING | 64 | 64 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
G | ||||||||
| BINDING | 85 | 85 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
D | ||||||||
| BINDING | 129 | 129 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
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Additional information
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| Size range | 232-261 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: 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. |