Any feedback?
Information on EC 2.1.1.64 - 3-demethylubiquinol 3-O-methyltransferase
for references in articles please use BRENDA:EC2.1.1.64Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.1.1.64 3-demethylubiquinol 3-O-methyltransferaseIUBMB Comments
This enzyme is involved in ubiquinone biosynthesis. Ubiquinones from different organisms have a different number of prenyl units (for example, 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. However, the enzyme usually shows a low degree of specificity regarding the number of prenyl units. For example, the human COQ3 enzyme can restore biosynthesis of ubiquinone-6 in coq3 deletion mutants of yeast . The enzymes from yeast, Escherichia coli and rat also catalyse the methylation of 3,4-dihydroxy-5-all-trans-polyprenylbenzoate (a reaction that is classified as EC 2.1.1.114, polyprenyldihydroxybenzoate methyltransferase).
Specify your search results
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
5-demethylubiquinone-9-methyltransferase, 2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone methyltransferase, ubig methyltransferase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone methyltransferase
5-demethylubiquinone-9 methyltransferase
-
-
-
-
COQ3
OMHMB-methyltransferase
-
-
-
-
S-adenosyl-L-methionine:2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone-O-methyltransferase
UbiG
2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone methyltransferase
-
-
-
-
2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone methyltransferase
-
-
S-adenosyl-L-methionine:2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone-O-methyltransferase
-
-
-
-
S-adenosyl-L-methionine:2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone-O-methyltransferase
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + 3-demethylubiquinol-n = S-adenosyl-L-homocysteine + ubiquinol-n
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:3-hydroxy-2-methoxy-5-methyl-6-(all-trans-polyprenyl)-1,4-benzoquinol 3-O-methyltransferase
This enzyme is involved in ubiquinone biosynthesis. Ubiquinones from different organisms have a different number of prenyl units (for example, 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. However, the enzyme usually shows a low degree of specificity regarding the number of prenyl units. For example, the human COQ3 enzyme can restore biosynthesis of ubiquinone-6 in coq3 deletion mutants of yeast [3]. The enzymes from yeast, Escherichia coli and rat also catalyse the methylation of 3,4-dihydroxy-5-all-trans-polyprenylbenzoate [3] (a reaction that is classified as EC 2.1.1.114, polyprenyldihydroxybenzoate methyltransferase).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
63774-48-1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 3-demethylubiquinol-10
S-adenosyl-L-homocysteine + ubiquinol-10 + H+
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-10, 1. the methylation of 3,4-dihydroxy-5-all-trans-decaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-10
-
-
?
S-adenosyl-L-methionine + 3-demethylubiquinol-n
S-adenosyl-L-homocysteine + ubiquinol-n
-
-
-
?
additional information
?
-
wide substrate specificity. The enzyme methylates both eukaryotic substrates 3,4-dihydroxy-5-farnesylbenzoic acid (this activity is classified as EC 2.1.1.114) and demethylubiquinol-3 and the distinct prokaryotic substrate 3-((2E,6E)-farnesyl)benzene-1,2-diol
-
-
?
S-adenosyl-L-methionine + 3-demethylubiquinol-3
S-adenosyl-L-homocysteine + ubiquinol-3
-
i.e. 5-((2E,6E)-farnesyl)-2-hydroxy-3-methoxy-6-methyl-1,4-benzoquinone
-
-
?
S-adenosyl-L-methionine + 3-demethylubiquinol-3
S-adenosyl-L-homocysteine + ubiquinol-3
-
i.e. 5-(2E,6E)-farnesyl-2-hydroxy-3-methoxy-6-methyl-1,4-benzoquinone
-
-
?
S-adenosyl-L-methionine + 3-demethylubiquinol-3
S-adenosyl-L-homocysteine + ubiquinol-3
i.e. 5-(2E,6E)-farnesyl-2-hydroxy-3-methoxy-6-methyl-1,4-benzoquinone, in vitro assay
-
-
?
S-adenosyl-L-methionine + 3-demethylubiquinol-3
S-adenosyl-L-homocysteine + ubiquinol-3
i.e. 5-(2E,6E)-farnesyl-2-hydroxy-3-methoxy-6-methyl-1,4-benzoquinone, in vitro assay
-
-
?
S-adenosyl-L-methionine + 3-demethylubiquinol-3
S-adenosyl-L-homocysteine + ubiquinol-3
i.e. 5-(2E,6E)-farnesyl-2-hydroxy-3-methoxy-6-methyl-1,4-benzoquinone
-
-
?
S-adenosyl-L-methionine + 3-demethylubiquinol-6
S-adenosyl-L-homocysteine + ubiquinol-6
3-demethylubiquinol-6 is an intermediate in biosynthesis of ubiquinone-6 in Saccharomyces cerevisiae (methylated by the yeast enzyme COQ3 to ubiquinol-6). 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
-
-
?
S-adenosyl-L-methionine + 3-demethylubiquinol-6
S-adenosyl-L-homocysteine + ubiquinol-6
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-6 in Saccharomyces cerevisiae, 1. the methylation of 3,4-dihydroxy-5-all-trans-hexaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-6
-
-
?
S-adenosyl-L-methionine + 3-demethylubiquinol-8
S-adenosyl-L-homocysteine + ubiquinol-8
-
involved in biosynthesis of ubiquinone-8
-
-
?
S-adenosyl-L-methionine + 3-demethylubiquinol-8
S-adenosyl-L-homocysteine + ubiquinol-8
-
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-8 in Escherichia coli, 1. the methylation of 3,4-dihydroxy-5-all-trans-octaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-8
-
-
?
S-adenosyl-L-methionine + 3-demethylubiquinol-8
S-adenosyl-L-homocysteine + ubiquinol-8
-
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-8 in Escherichia coli, 1. the methylation of 3,4-dihydroxy-5-octaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-8
-
-
?
S-adenosyl-L-methionine + 3-demethylubiquinol-8
S-adenosyl-L-homocysteine + ubiquinol-8
-
i.e. 2-all-trans-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinol
-
-
?
S-adenosyl-L-methionine + 3-demethylubiquinol-9
S-adenosyl-L-homocysteine + ubiquinol-9
-
-
-
?
S-adenosyl-L-methionine + 3-demethylubiquinol-9
S-adenosyl-L-homocysteine + ubiquinol-9
involved in biosynthesis of ubiquinone-9
-
-
?
S-adenosyl-L-methionine + 3-demethylubiquinol-9
S-adenosyl-L-homocysteine + ubiquinol-9
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-9 in Rattus norvegicus, 1. the methylation of 3,4-dihydroxy-5-all-trans-octaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-9
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 3-demethylubiquinol-10
S-adenosyl-L-homocysteine + ubiquinol-10 + H+
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-10, 1. the methylation of 3,4-dihydroxy-5-all-trans-decaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-10
-
-
?
S-adenosyl-L-methionine + 3-demethylubiquinol-6
S-adenosyl-L-homocysteine + ubiquinol-6
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-6 in Saccharomyces cerevisiae, 1. the methylation of 3,4-dihydroxy-5-all-trans-hexaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-6
-
-
?
S-adenosyl-L-methionine + 3-demethylubiquinol-8
S-adenosyl-L-homocysteine + ubiquinol-8
-
involved in biosynthesis of ubiquinone-8
-
-
?
S-adenosyl-L-methionine + 3-demethylubiquinol-8
S-adenosyl-L-homocysteine + ubiquinol-8
-
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-8 in Escherichia coli, 1. the methylation of 3,4-dihydroxy-5-all-trans-octaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-8
-
-
?
S-adenosyl-L-methionine + 3-demethylubiquinol-8
S-adenosyl-L-homocysteine + ubiquinol-8
-
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-8 in Escherichia coli, 1. the methylation of 3,4-dihydroxy-5-octaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-8
-
-
?
S-adenosyl-L-methionine + 3-demethylubiquinol-9
S-adenosyl-L-homocysteine + ubiquinol-9
involved in biosynthesis of ubiquinone-9
-
-
?
S-adenosyl-L-methionine + 3-demethylubiquinol-9
S-adenosyl-L-homocysteine + ubiquinol-9
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-9 in Rattus norvegicus, 1. the methylation of 3,4-dihydroxy-5-all-trans-octaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-9
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
NADH stimualtes activity of mitochondrial fraction
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cd2+
-
absolute requirement for a divalent metal ion. 1 mM Cd2+ stimulates 14fold
Co2+
-
absolute requirement for a divalent metal ion. 1 mM Co2+ stimulates 67fold
Cu2+
-
absolute requirement for a divalent metal ion. 1 mM Cu2+ stimulates 21fold
Fe2+
-
absolute requirement for a divalent metal ion. 1 mM Fe2+ stimulates 63fold
Mg2+
-
absolute requirement for a divalent metal ion. 1 mM Mg2+ stimulates about 3fold
Mn2+
-
absolute requirement for a divalent metal ion. 1 mM Mn2+ stimulates 11fold
Ni2+
-
absolute requirement for a divalent metal ion. 1 mM Ni2+ stimulates 24fold
Zn2+
-
absolute requirement for a divalent metal ion. Zn2+ is most effective. 1 mM Zn2+ stimulates over 100fold
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
-
the optimum ratio of dithiothreitol to divalent metal ion is about 10:1. The maximal methyltransferase activity is achieved at 10 mM dithiothreitol and 1 mM Zn2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00006 - 0.00008
3-demethylubiquinol-9
pH 7.4, mitochondrial fraction
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
associated. In vivo, the methyltransferase reaction probably occurs at the internal surface of the cytoplasmic membrane
brenda
the membrane-binding region of UbiG gates the entrance of methyl donor
brenda
the Coq3 polypeptide is peripherally associated with the matrix side of the inner membrane of yeast mitochondria
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
after 1 h of H2O2 treatment, the viability of the strain defective in ubiG is reduced 28fold compared to the corresponding wild-type. When treated with CuSO4, the viability of the the strain defective in ubiG (HW271), is reduced 4.4fold after 30 min compared to its isogenic wild-type
malfunction
rat COQ3 gene restores O-methyltransferase activity in coq3 null mutant yeast
physiological function
-
the ubiG gene product is essential for growth on glycerol minimal medium
physiological function
the membrane-binding region of UbiG gates the entrance of methyl donor. When bound with liposome, UbiG displays an enhanced binding ability toward the methyl donor product S-adenosylhomocysteine
Show AA Sequence and Transmembrane Helices (16694 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Coq3 and Coq4 are members of a ubiquinone-biosynthetic Coq polypeptide complex
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using either 0.1 M HEPES pH 7.5 and 20% polyethylene glycol 10000 or 10% (v/v) 2-methyl-2,4-pentanediol and 0.1 M HEPES pH 7.0
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
for mutant UbiGDELTA 165-187 lacking the sequence insertion that covers the methyl donor binding pocket, the binding affinity to SAH is approximately 58fold higher than that of wild-type
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography, DEAE column chromatography, and Superdex 200 gel filtration
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
AtCOQ3 is able to restore the respiration ability and ubiquinone synthesis of the coq3 deletion mutant of Saccharomyces cerevisiae
rat COQ3 gene restores O-methyltransferase activity in coq3 null mutant yeast
the rescue of the yeast coq3 mutant by the rat homologue suggests that yeast and rat synthesize ubiquinone via the same early steps in this pathway
the ubiG gene is able to restore respiration in the yeast coq3 mutant, provided ubiG is modified to contain a mitochondrial leader sequence
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Avelange-Macheral, M.H.; Joyard, J.
Cloning and functional expression of AtCOQ3, the Arabidopsis homologue of the yeast COQ3 gene, encoding a methyltransferase from the plant mitochondria involved in ubiquinone biosynthesis
Plant J.
14
203-213
1998
Arabidopsis thaliana (O49354)
brenda
Poon, W.W.; Barkovich, R.J.; Hsu, A.Y.; Frankel, A.; Lee, P.T.; Sheperd, J.N.; Myles, D.C.; Clarke, C.F.
Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis
J. Biol. Chem.
274
21665-21672
1999
Escherichia coli, Saccharomyces cerevisiae (P27680), Rattus norvegicus (Q63159)
brenda
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)
brenda
Leppik, R.A.; Stoobant, P.; Shineberg, B.; Young, I.G.; Gibson, F.
Membrane-associated reactions in ubiquinone biosynthesis. 2-Octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone methyltransferase
Biochim. Biophys. Acta
428
146-156
1976
Escherichia coli
brenda
Houser, R.M.; Olson, E.
5-Demethylubiquinone-9-methyltransferase from rat liver mitochondria. Characterization, localization, and solubilization
J. Biol. Chem.
252
4017-4021
1977
Rattus norvegicus (Q63159)
brenda
Hsu, A.Y.; Poon, W.W.; Shepherd, J.A.; Myles, D.C.; Clarke, C.F.
Complementation of coq3 mutant yeast by mitochondrial targeting of the Escherichia coli UbiG polypeptide: evidence that UbiG catalyzes both O-methylation steps in ubiquinone biosynthesis
Biochemistry
35
9797-9806
1996
Escherichia coli
brenda
Marbois, B.N.; Hsu, A.; Pillai, R.; Colicelli, J.; Clarke, C.F.
Cloning of a rat cDNA encoding dihydroxypolyprenylbenzoate methyltransferase by functional complementation of a Saccharomyces cerevisiae mutant deficient in ubiquinone biosynthesis
Gene
138
213-217
1994
Rattus norvegicus (Q63159)
brenda
Joyce, A.R.
Reed, J.L.; White, A.; Edwards, R.; Osterman, A.; Baba, T.; Mori, H.; Lesely, S.A.; Palsson, B.; Agarwalla, S.: Experimental and computational assessment of conditionally essential genes in Escherichia coli
J. Bacteriol.
188
8259-8271
2006
Escherichia coli
brenda
Marbois, B.; Gin, P.; Faull, K.F.; Poon, W.W.
Lee, P.T.; Strahan, J.; Shepherd, J.N., Clarke, C.F.: Coq3 and Coq4 define a polypeptide complex in yeast mitochondria for the biosynthesis of coenzyme Q
J. Biol. Chem.
280
20231-20238
2005
Saccharomyces cerevisiae (P27680)
brenda
Soballe, B.; Poole, R.K.
Ubiquinone limits oxidative stress in Escherichia coli
Microbiology
146
787-796
2000
Escherichia coli
brenda
Xing, L.; Zhu, Y.; Fang, P.; Wang, J.; Zeng, F.; Li, X.; Teng, M.; Li, X.
Crystallization and preliminary crystallographic studies of UbiG, an O-methyltransferase from Escherichia coli
Acta Crystallogr. Sect. F
67
727-729
2011
Escherichia coli
brenda
Zhu, Y.; Jiang, X.; Wang, C.; Liu, Y.; Fan, X.; Zhang, L.; Niu, L.; Teng, M.; Li, X.
Structural insights into the methyl donor recognition model of a novel membrane-binding protein UbiG
Sci. Rep.
6
23147
2016
Escherichia coli (C3T302)
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 2.1.1.64)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
