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Information on EC 2.1.1.222 - 2-polyprenyl-6-hydroxyphenol methylase and Organism(s) Homo sapiens

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EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.222 2-polyprenyl-6-hydroxyphenol methylase
IUBMB Comments
UbiG catalyses both methylation steps in ubiquinone biosynthesis in Escherichia coli. The second methylation is classified as EC 2.1.1.64 (3-demethylubiquinol 3-O-methyltransferase) . In eukaryotes Coq3 catalyses the two methylation steps in ubiquinone biosynthesis. However, while the second methylation is common to both enzymes, the first methylation by Coq3 occurs at a different position within the pathway, and thus involves a different substrate and is classified as EC 2.1.1.114 (polyprenyldihydroxybenzoate methyltransferase). The substrate of the eukaryotic enzyme (3,4-dihydroxy-5-all-trans-polyprenylbenzoate) differs by an additional carboxylate moiety.
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Homo sapiens
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
2-polyprenyl-6-hydroxyphenyl methylase, 3-demethyl ubiquinone-9 3-methyltransferase, UbiG, UbiG methyltransferase, ubiquinone biosynthesis O-methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-polyprenyl-6-hydroxyphenyl methylase
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:3-(all-trans-polyprenyl)benzene-1,2-diol 2-O-methyltransferase
UbiG catalyses both methylation steps in ubiquinone biosynthesis in Escherichia coli. The second methylation is classified as EC 2.1.1.64 (3-demethylubiquinol 3-O-methyltransferase) [2]. In eukaryotes Coq3 catalyses the two methylation steps in ubiquinone biosynthesis. However, while the second methylation is common to both enzymes, the first methylation by Coq3 occurs at a different position within the pathway, and thus involves a different substrate and is classified as EC 2.1.1.114 (polyprenyldihydroxybenzoate methyltransferase). The substrate of the eukaryotic enzyme (3,4-dihydroxy-5-all-trans-polyprenylbenzoate) differs by an additional carboxylate moiety.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 3-((2E,6E)-farnesyl)benzene-1,2-diol
S-adenosyl-L-homocysteine + 2-methoxy-6-((2E,6E)-farnesyl)phenol
show the reaction diagram
i.e. 3-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]benzene-1,2-diol. The substrate is an artificial farnesylated analog of the Escherichia coli substrate 2-all-trans-octaprenyl-6-hydroxyphenol, an intermediate in the biosynthesis of ubiquinone-8 in Escherichia coli
i.e. 2-methoxy-6-((2E,6E)-3,7,11-trimethyldodeca-2,6,10-trienyl)phenol
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additional information
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
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the enzyme is involved in biosynthesis of ubiquinone-10 in human and catalyzes the methylation of 3-demethylubiquinol-10 to ubiquinol-10 (EC 2.1.1.64) and the methylation of 3,4-dihydroxy-5-decaprenylbenzoate to 3-methoxy-4-hydroxy-5-all-trans-decaprenylbenzoate (EC 2.1.1.114)
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
COQ3_HUMAN
369
0
41054
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40998
x * 40998, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 40998, calculated from sequence
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
when expressed in multicopy, the human construct rescues the growth of a yeast coq3 null mutant on a nonfermentable carbon source and restores coenzyme Q biosynthesis, although at lower levels than that of wild type yeast
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jonassen, T.; Clarke, C.F.
Isolation and functional expression of human COQ3, a gene encoding a methyltransferase required for ubiquinone biosynthesis
J. Biol. Chem.
275
12381-12387
2000
Homo sapiens (Q9NZJ6)
Manually annotated by BRENDA team