ID: | 2.1.1.201 | ||
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Description: | 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase. | ||
Prosite: | PDOC00911; | ||
PDB: |
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Cath: | 3.40.50.150; |
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.UniProtKB Enzyme Link: | UniProtKB 2.1.1.201 |
BRENDA Enzyme Link: | BRENDA 2.1.1.201 |
KEGG Enzyme Link: | KEGG2.1.1.201 |
BioCyc Enzyme Link: | BioCyc 2.1.1.201 |
ExPASy Enzyme Link: | ExPASy2.1.1.201 |
EC2PDB Enzyme Link: | EC2PDB 2.1.1.201 |
ExplorEnz Enzyme Link: | ExplorEnz 2.1.1.201 |
PRIAM enzyme-specific profiles Link: | PRIAM 2.1.1.201 |
IntEnz Enzyme Link: | IntEnz 2.1.1.201 |
MEDLINE Enzyme Link: | MEDLINE 2.1.1.201 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:27774 | 2-methoxy-6-all-trans-octaprenyl-1,4-benzoquinol + S-adenosyl-L-methionine = 6-methoxy-3-methyl-2-all-trans-octaprenyl-1,4-benzoquinol + H(+) + S-adenosyl-L-homocysteine |
RULE(radius=1) | [*:1]-[S+;H0:2](-[*:3])-[CH3;+0:4].[*:5]:[cH;+0:6]:[*:7]>>[*:1]-[S;H0;+0:2]-[*:3].[*:5]:[c;H0;+0:6](:[*:7])-[CH3;+0:4] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
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Identification of Escherichia coli ubiB, a gene required for the first monooxygenase step in ubiquinone biosynthesis. | Poon WW, Davis DE, Ha HT, Jonassen T, Rather PN, Clarke CF | 2000 Sep | 10960098 |
RHEA:28286 | a 2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol + S-adenosyl-L-methionine = a 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol + H(+) + S-adenosyl-L-homocysteine |
RULE(radius=1) | [*:1]-[S+;H0:2](-[*:3])-[CH3;+0:4].[*:5]:[cH;+0:6]:[*:7]>>[*:1]-[S;H0;+0:2]-[*:3].[*:5]:[c;H0;+0:6](:[*:7])-[CH3;+0:4] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
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Yeast Coq5 C-methyltransferase is required for stability of other polypeptides involved in coenzyme Q biosynthesis. | Baba SW, Belogrudov GI, Lee JC, Lee PT, Strahan J, Shepherd JN, Clarke CF | 2004 Mar 12 | 14701817 |
Identification of Escherichia coli ubiB, a gene required for the first monooxygenase step in ubiquinone biosynthesis. | Poon WW, Davis DE, Ha HT, Jonassen T, Rather PN, Clarke CF | 2000 Sep | 10960098 |
A C-methyltransferase involved in both ubiquinone and menaquinone biosynthesis: isolation and identification of the Escherichia coli ubiE gene. | Lee PT, Hsu AY, Ha HT, Clarke CF | 1997 Mar | 9045837 |
RHEA:44752 | 2-methoxy-6-all-trans-hexaprenyl-1,4-benzoquinol + S-adenosyl-L-methionine = 6-methoxy-3-methyl-2-all-trans-hexaprenyl-1,4-benzoquinol + H(+) + S-adenosyl-L-homocysteine |
RULE(radius=1) | [*:1]-[S+;H0:2](-[*:3])-[CH3;+0:4].[*:5]:[cH;+0:6]:[*:7]>>[*:1]-[S;H0;+0:2]-[*:3].[*:5]:[c;H0;+0:6](:[*:7])-[CH3;+0:4] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
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Crystal structures and catalytic mechanism of the C-methyltransferase Coq5 provide insights into a key step of the yeast coenzyme Q synthesis pathway. | Dai YN, Zhou K, Cao DD, Jiang YL, Meng F, Chi CB, Ren YM, Chen Y, Zhou CZ | 2014 Aug | 25084328 |
Yeast Coq5 C-methyltransferase is required for stability of other polypeptides involved in coenzyme Q biosynthesis. | Baba SW, Belogrudov GI, Lee JC, Lee PT, Strahan J, Shepherd JN, Clarke CF | 2004 Mar 12 | 14701817 |
RHEA:44756 | 2-methoxy-6-all-trans-heptaprenyl-1,4-benzoquinol + S-adenosyl-L-methionine = 6-methoxy-3-methyl-2-all-trans-heptaprenyl-1,4-benzoquinol + H(+) + S-adenosyl-L-homocysteine |
RULE(radius=1) | [*:1]-[S+;H0:2](-[*:3])-[CH3;+0:4].[*:5]:[cH;+0:6]:[*:7]>>[*:1]-[S;H0;+0:2]-[*:3].[*:5]:[c;H0;+0:6](:[*:7])-[CH3;+0:4] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
RHEA:44760 | 2-methoxy-6-all-trans-nonaprenyl-1,4-benzoquinol + S-adenosyl-L-methionine = 6-methoxy-3-methyl-2-all-trans-nonaprenyl-1,4-benzoquinol + H(+) + S-adenosyl-L-homocysteine |
RULE(radius=1) | [*:1]-[S+;H0:2](-[*:3])-[CH3;+0:4].[*:5]:[cH;+0:6]:[*:7]>>[*:1]-[S;H0;+0:2]-[*:3].[*:5]:[c;H0;+0:6](:[*:7])-[CH3;+0:4] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
RHEA:44764 | 2-methoxy-6-all-trans-decaprenyl-1,4-benzoquinol + S-adenosyl-L-methionine = 6-methoxy-3-methyl-2-all-trans-decaprenyl-1,4-benzoquinol + H(+) + S-adenosyl-L-homocysteine |
RULE(radius=1) | [*:1]-[S+;H0:2](-[*:3])-[CH3;+0:4].[*:5]:[cH;+0:6]:[*:7]>>[*:1]-[S;H0;+0:2]-[*:3].[*:5]:[c;H0;+0:6](:[*:7])-[CH3;+0:4] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
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Molecular characterization of the human COQ5 C-methyltransferase in coenzyme Q10 biosynthesis. | Nguyen TP, Casarin A, Desbats MA, Doimo M, Trevisson E, Santos-Ocaña C, Navas P, Clarke CF, Salviati L | 2014 Nov | 25152161 |