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Information on EC 2.1.1.222 - 2-polyprenyl-6-hydroxyphenol methylase
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2.1.1.222 2-polyprenyl-6-hydroxyphenol methylaseIUBMB 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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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
2-polyprenyl-6-hydroxyphenyl methylase, 3-demethyl ubiquinone-9 3-methyltransferase, UbiG, UbiG methyltransferase, ubiquinone biosynthesis O-methyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-polyprenyl-6-hydroxyphenyl methylase
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UbiG
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + 3-(all-trans-polyprenyl)benzene-1,2-diol = S-adenosyl-L-homocysteine + 2-methoxy-6-(all-trans-polyprenyl)phenol
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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.
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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 + 2-(all-trans-decaprenyl)-5-hydroxy-6-methoxy-3-methylcyclohexa-2,5-diene-1,4-dione
S-adenosyl-L-homocysteine + 2-(all-trans-decaprenyl)-5,6-dimethoxy-3-methylcyclohexa-2,5-diene-1,4-dione
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?
S-adenosyl-L-methionine + 3-((2E,6E)-farnesyl)benzene-1,2-diol
S-adenosyl-L-homocysteine + 2-methoxy-6-((2E,6E)-farnesyl)phenol
S-adenosyl-L-methionine + 3-((2E,6E)-farnesyl)benzene-1,2-diol
S-adenosyl-L-homocysteine + 2-methoxy-6-(farnesyl)phenol
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-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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?
S-adenosyl-L-methionine + 3-(all-trans-decaprenyl)-benzene-1,2-diol
S-adenosyl-L-homocysteine + 3-(all-trans-decaprenyl)-1-methoxybenzene-2-ol
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?
S-adenosyl-L-methionine + 3-(all-trans-octaprenyl)benzene-1,2-diol
S-adenosyl-L-homocysteine + 2-methoxy-6-(all-trans-octaprenyl)phenol
S-adenosyl-L-methionine + 3-(all-trans-polyprenyl)benzene-1,2-diol
S-adenosyl-L-homocysteine + 2-methoxy-6-(all-trans-polyprenyl)phenol
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?
S-adenosyl-L-methionine + 3-((2E,6E)-farnesyl)benzene-1,2-diol
S-adenosyl-L-homocysteine + 2-methoxy-6-((2E,6E)-farnesyl)phenol
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i.e. 3-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]benzene-1,2-diol
i.e. 2-methoxy-6-((2E,6E)-3,7,11-trimethyldodeca-2,6,10-trienyl)phenol
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?
S-adenosyl-L-methionine + 3-((2E,6E)-farnesyl)benzene-1,2-diol
S-adenosyl-L-homocysteine + 2-methoxy-6-((2E,6E)-farnesyl)phenol
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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?
S-adenosyl-L-methionine + 3-((2E,6E)-farnesyl)benzene-1,2-diol
S-adenosyl-L-homocysteine + 2-methoxy-6-((2E,6E)-farnesyl)phenol
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-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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?
S-adenosyl-L-methionine + 3-(all-trans-octaprenyl)benzene-1,2-diol
S-adenosyl-L-homocysteine + 2-methoxy-6-(all-trans-octaprenyl)phenol
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?
S-adenosyl-L-methionine + 3-(all-trans-octaprenyl)benzene-1,2-diol
S-adenosyl-L-homocysteine + 2-methoxy-6-(all-trans-octaprenyl)phenol
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the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-8 in Escherichia coli, 1. the methylation of 3-(all-trans-octaprenyl)benzene-1,2-diol and 2. the methylation of 3-demethylubiquinol-8 (this reaction is classified as EC 2.1.1.64)
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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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?
additional information
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wide substrate specificity. The enzyme methylates both eukaryotic substrates demethylubiquinol-3 (this activity is classified as EC 2.1.1.64) and 3,4-dihydroxy-5-farnesylbenzoic acid (this activity is classified as EC 2.1.1.114) and the distinct prokaryotic substrate 3-((2E,6E)-farnesyl)benzene-1,2-diol
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?
additional information
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the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-9 in Rattus norvegicus, 1. the methylation of 3,4-dihydroxy-5-nonaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-9 (this reaction is classified as EC 2.1.1.64)
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?
additional information
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the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-6 in Saccharomyces cerevisiae, 1. the methylation of 3,4-dihydroxy-5-hexaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-6 (this reaction is classified as EC 2.1.1.64)
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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-(all-trans-octaprenyl)benzene-1,2-diol
S-adenosyl-L-homocysteine + 2-methoxy-6-(all-trans-octaprenyl)phenol
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the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-8 in Escherichia coli, 1. the methylation of 3-(all-trans-octaprenyl)benzene-1,2-diol and 2. the methylation of 3-demethylubiquinol-8 (this reaction is classified as EC 2.1.1.64)
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?
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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?
additional information
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the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-9 in Rattus norvegicus, 1. the methylation of 3,4-dihydroxy-5-nonaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-9 (this reaction is classified as EC 2.1.1.64)
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?
additional information
?
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the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-6 in Saccharomyces cerevisiae, 1. the methylation of 3,4-dihydroxy-5-hexaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-6 (this reaction is classified as EC 2.1.1.64)
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the Coq3 polypeptide is peripherally associated with the matrix side of the inner membrane of yeast mitochondria
brenda
the membrane-binding region of UbiG gates the entrance of methyl donor
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
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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
metabolism
physiological function
metabolism
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the enzyme is required for both O-methylation steps in ubiquinone biosynthesis
metabolism
the enzyme catalyzes both of the two O-methyltransfer steps in CoQ10 biosynthesis
metabolism
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the enzyme is one of the key enzymes in the ubiquinone modification pathway
physiological function
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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
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.1 M HEPES pH 7.5 and 20% (w/v) polyethylene glycol 10000 or 10% (v/v) 2-methyl-2,4-pentanediol and 0.1 M HEPES pH 7.0
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H186A
the mutation completely destroys the interaction of the enzyme with liposomes
I177A
the mutation sharply reduces the interaction of the enzyme with liposomes
K183A
the mutation nearly completely destroys the interaction of the enzyme with liposomes
L132Q
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the mutation results in ubiquinone deficiency in Escherichia coli leading to a high sensitivity to thiols and a failure to grow on succinate
L178A
the mutation nearly completely destroys the interaction of the enzyme with liposomes
L178E
the mutation nearly completely destroys the interaction of the enzyme with liposomes
R179A
the mutation sharply reduces the interaction of the enzyme with liposomes
V181A
the mutation nearly completely destroys the interaction of the enzyme with liposomes
V181A/P182A/K183A/G184A/T185A/H186A
the mutations nearly completely destroy the interaction of the enzyme with liposomes
additional information
additional information
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a mutant deleted for ubiG exhibits longer lifespan, as well as enhanced resistance to thermal and oxidative stress (paraquat) compared to wild type at extracellular pH 9.0. The hypoxia-inducible transcription factor ArcA is required for the fully extended lifespan of the mutant
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
additional information
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a mutant deleted for ubiG exhibits longer lifespan, as well as enhanced resistance to thermal and oxidative stress (paraquat) compared to wild type at extracellular pH 9.0. The hypoxia-inducible transcription factor ArcA is required for the fully extended lifespan of the mutant
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography, HiTrap column chromatography, and Superdex 200 gel filtration
Ni-NTA column chromatography, Superdex 200 gel filtration, and DEAE anion-exchange chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
the ubiG gene is able to restore respiration in the yeast coq3 mutant, provided ubiG is modified to contain a mitochondrial leader sequence
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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
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of the ubiG gene is higher under aerobic conditions than under anaerobic growth conditions. Addition of cAMP increases the expression of the ubiG gene in both cya and wild-type strains but not in a crp mutant. The cAMP receptor protein-cyclic AMP complex positively modulates ubiG gene transcription
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expression of the ubiG gene is higher under aerobic conditions than under anaerobic growth conditions. The presence of glucose in the culture medium decreases the transcription of the ubiG gene. cya and cip mutants exhibit lower levels of ubiG gene expression than the wild-type strain
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
Gibert, I.; Llagostera, M.; Barbe, J.
Regulation of ubiG gene expression in Escherichia coli
J. Bacteriol.
170
1346-1349
1988
Escherichia coli
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
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
Gonidakis, S.; Finkel, S.E.; Longo, V.D.
Lifespan extension and paraquat resistance in a ubiquinone-deficient Escherichia coli mutant depend on transcription factors ArcA and TdcA
Aging
3
291-303
2011
Escherichia coli, Escherichia coli BW25113
brenda
Lu, W.; Shi, Y.; He, S.; Fei, Y.; Yu, K.; Yu, H.
Enhanced production of CoQ10 by constitutive overexpression of 3-demethyl ubiquinone-9 3-methyltransferase under tac promoter in Rhodobacter sphaeroides
Biochem. Eng. J.
72
42-47
2013
Cereibacter sphaeroides (Q3IYM5)
brenda
Zhu, Y.; Wu, B.; Zhang, X.; Fan, X.; Niu, L.; Li, X.; Wang, J.; Teng, M.
Structural and biochemical studies reveal UbiG/Coq3 as a class of novel membrane-binding proteins
Biochem. J.
470
105-114
2015
Escherichia coli (P17993)
brenda
Lu, W.; Ye, L.; Lv, X.; Xie, W.; Gu, J.; Chen, Z.; Zhu, Y.; Li, A.; Yu, H.
Identification and elimination of metabolic bottlenecks in the quinone modification pathway for enhanced coenzyme Q10 production in Rhodobacter sphaeroides
Metab. Eng.
29
208-216
2015
Cereibacter sphaeroides
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
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