EC number:2.1.1.222

Enzyme

Download
EC Tree
     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.222
Description:2-polyprenyl-6-hydroxyphenol methylase.
Alternative Name: 2-octaprenyl-6-hydroxyphenol methylase.
Cath: 3.40.50.150;

3D structure

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.
PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.222
BRENDA Enzyme Link: BRENDA 2.1.1.222
KEGG Enzyme Link: KEGG2.1.1.222
BioCyc Enzyme Link: BioCyc 2.1.1.222
ExPASy Enzyme Link: ExPASy2.1.1.222
EC2PDB Enzyme Link: EC2PDB 2.1.1.222
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.222
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.222
IntEnz Enzyme Link: IntEnz 2.1.1.222
MEDLINE Enzyme Link: MEDLINE 2.1.1.222

EC number:2.1.1.222

MSA:

2.1.1.222;
Phylogenetic Tree:

2.1.1.222;
Uniprot:
M-CSA:
RHEA:27770 3-(all-trans-octaprenyl)benzene-1,2-diol + S-adenosyl-L-methionine = 2-methoxy-6-(all-trans-octaprenyl)phenol + H(+) + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[O;H0;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
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.Hsu AY, Poon WW, Shepherd JA, Myles DC, Clarke CF1996 Jul 308703953
Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis.Poon WW, Barkovich RJ, Hsu AY, Frankel A, Lee PT, Shepherd JN, Myles DC, Clarke CF1999 Jul 3010419476
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
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[O;H0;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
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.Hsu AY, Poon WW, Shepherd JA, Myles DC, Clarke CF1996 Jul 308703953
Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis.Poon WW, Barkovich RJ, Hsu AY, Frankel A, Lee PT, Shepherd JN, Myles DC, Clarke CF1999 Jul 3010419476
RHEA:44592 3-(all-trans-heptaprenyl)benzene-1,2-diol + S-adenosyl-L-methionine = 2-methoxy-6-(all-trans-heptaprenyl)phenol + H(+) + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[O;H0;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction
RHEA:44608 3-(all-trans-nonaprenyl)benzene-1,2-diol + S-adenosyl-L-methionine = 2-methoxy-6-(all-trans-nonaprenyl)phenol + H(+) + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[O;H0;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction
RHEA:44612 3-(all-trans-decaprenyl)benzene-1,2-diol + S-adenosyl-L-methionine = 2-methoxy-6-(all-trans-decaprenyl)phenol + H(+) + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[O;H0;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction
RHEA:50224 3-(all-trans-hexaprenyl)benzene-1,2-diol + S-adenosyl-L-methionine = 2-methoxy-6-(all-trans-hexaprenyl)phenol + H(+) + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[O;H0;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Structural insights into the methyl donor recognition model of a novel membrane-binding protein UbiG.Zhu Y, Jiang X, Wang C, Liu Y, Fan X, Zhang L, Niu L, Teng M, Li X2016 Mar 1526975567
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.Hsu AY, Poon WW, Shepherd JA, Myles DC, Clarke CF1996 Jul 308703953
Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis.Poon WW, Barkovich RJ, Hsu AY, Frankel A, Lee PT, Shepherd JN, Myles DC, Clarke CF1999 Jul 3010419476