Identification
Name:3-demethylubiquinone-9 3-methyltransferase
Synonyms:
  • 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase
  • DHHB methyltransferase
Gene Name:ubiG
Enzyme Class:
Biological Properties
General Function:Involved in 2-polyprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity
Specific Function:S-adenosyl-L-methionine + 3- demethylubiquinone-9 = S-adenosyl-L-homocysteine + ubiquinone-9
Cellular Location:Not Available
SMPDB Pathways:
  • Secondary Metabolites: Ubiquinol biosynthesis PW000981
  • Secondary Metabolites: Ubiquinol biosynthesis 2 PW002036
KEGG Pathways:
  • Metabolic pathways eco01100
  • Ubiquinone and other terpenoid-quinone biosynthesis ec00130
KEGG Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.02-Polyprenyl-6-hydroxyphenol+1.0Thumb1.02-Polyprenyl-6-methoxyphenol+1.0Thumb
1.02-Polyprenyl-6-hydroxyphenol + 1.0S-Adenosylmethionine ↔ 1.02-Polyprenyl-6-methoxyphenol + 1.0S-Adenosylhomocysteine
ReactionCard
1.02-Polyprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone+1.0Thumb1.0Thumb+1.0Thumb
1.02-Polyprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone + 1.0S-Adenosylmethionine ↔ 1.0Ubiquinone-1 + 1.0S-Adenosylhomocysteine
ReactionCard
SMPDB Reactions:
1.02-Octaprenyl-6-hydroxyphenol+1.0S-adenosyl-L-methionine+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
1.02-Octaprenyl-6-hydroxyphenol + 1.0S-adenosyl-L-methionine + 1.02-Octaprenyl-6-hydroxyphenol → 1.0Hydrogen ion + 1.0S-Adenosylhomocysteine + 1.02-methoxy-6-(all-trans-octaprenyl)phenol
ReactionCard
1.0Thumb+1.0S-adenosyl-L-methionine1.0Thumb+1.0Thumb+1.0Ubiquinol 8+1.0Thumb
1.03-demethylubiquinol-8 + 1.0S-adenosyl-L-methionine → 1.0Hydrogen ion + 1.0S-Adenosylhomocysteine + 1.0Ubiquinol 8 + 1.0Ubiquinol-8
ReactionCard
1.02-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone+1.0S-adenosyl-L-methionine1.0Thumb+1.0Thumb+1.0Thumb
1.02-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone + 1.0S-adenosyl-L-methionine → 1.0S-Adenosylhomocysteine + 1.0Ubiquinol-8 + 1.0Hydrogen ion
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
Complex Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB234372-methoxy-6-(all-trans-octaprenyl)phenolMetaboCard
ECMDB211562-Octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinolMetaboCard
ECMDB041172-Octaprenyl-6-hydroxyphenolMetaboCard
ECMDB041192-Octaprenyl-6-methoxyphenolMetaboCard
ECMDB242593-demethylubiquinol-8MetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00939S-AdenosylhomocysteineMetaboCard
ECMDB01185S-AdenosylmethionineMetaboCard
ECMDB21579Ubiquinol-7MetaboCard
ECMDB01060Ubiquinol-8MetaboCard
ECMDB21580Ubiquinol-9MetaboCard
ECMDB21438Ubiquinone-1MetaboCard
ECMDB21581Ubiquinone-2MetaboCard
ECMDB20620Ubiquinone-6MetaboCard
ECMDB21584Ubiquinone-7MetaboCard
ECMDB21296Ubiquinone-8MetaboCard
ECMDB21583Ubiquinone-9MetaboCard
GO Classification:
Function
2-polyprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity
C-methyltransferase activity
catalytic activity
methyltransferase activity
quinone cofactor methyltransferase activity
transferase activity
transferase activity, transferring one-carbon groups
Process
cellular metabolic process
coenzyme metabolic process
cofactor metabolic process
metabolic process
oxidoreduction coenzyme metabolic process
ubiquinone biosynthetic process
ubiquinone metabolic process
Gene Properties
Blattner:b2232
Gene OrientationClockwise
Centisome Percentage:50.38
Left Sequence End2337589
Right Sequence End2338311
Gene Sequence:
>723 bp
ATGAAACCGGCAAGAGTCCCTCAAACTGTCGTGGCTCCTGATTGCTGGGGCGATTTGCCC
TGGGGAAAGCTTTATCGCAAGGCGCTGGAGCGCCAGCTCAACCCGTGGTTCACTAAAATG
TATGGTTTTCATCTGCTTAAGATTGGCAATTTAAGCGCAGAAATCAATTGCGAAGCGTGC
GCGGTTTCTCATCAAGTGAATGTTTCTGCGCAAGGAATGCCCGTCCAGGTACAGGCGGAC
CCACTTCATCTTCCTTTTGCCGATAAATCCGTTGATGTTTGTCTACTGGCACATACATTG
CCGTGGTGCACCGATCCGCATCGTTTATTGCGTGAAGCCGATCGGGTATTGATTGATGAT
GGCTGGCTGGTCATTAGTGGCTTCAATCCCATCAGTTTTATGGGATTACGCAAACTTGTG
CCGGTATTGCGCAAAACCTCGCCCTATAACAGCCGGATGTTTACTCTGATGCGGCAGCTG
GACTGGCTCTCTTTGTTGAATTTTGAAGTGCTACACGCCAGCCGTTTCCACGTTCTCCCG
TGGAACAAACACGGAGGAAAACTATTGAATGCGCATATTCCTGCGCTTGGTTGCTTACAA
CTTATTGTTGCCCGGAAACGGACTATTCCTTTAACGCTAAATCCGATGAAACAGAGTAAA
AACAAGCCACGAATTCGCCAGGCGGTTGGAGCCACCCGGCAATGTCGTAAACCACAGGCT
TAA
Protein Properties
Pfam Domain Function:
Protein Residues:240
Protein Molecular Weight:26555
Protein Theoretical pI:7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>3-demethylubiquinone-9 3-methyltransferase
MNAEKSPVNHNVDHEEIAKFEAVASRWWDLEGEFKPLHRINPLRLGYIAERAGGLFGKKV
LDVGCGGGILAESMAREGATVTGLDMGFEPLQVAKLHALESGIQVDYVQETVEEHAAKHA
GQYDVVTCMEMLEHVPDPQSVVRACAQLVKPGGDVFFSTLNRNGKSWLMAVVGAEYILRM
VPKGTHDVKKFIKPAELLGWVDQTSLKERHITGLHYNPITNTFKLGPGVDVNYMLHTQNK
References
External Links:
ResourceLink
Uniprot ID:P17993
Uniprot Name:UBIG_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4902950
Ecogene ID:EG11143
Ecocyc:EG11143
ColiBase:b2232
Kegg Gene:b2232
EchoBASE ID:EB1133
CCDB:UBIG_ECOLI
BacMap:16130167
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Hussain, K., Elliott, E. J., Salmond, G. P. (1987). "The parD- mutant of Escherichia coli also carries a gyrAam mutation. The complete sequence of gyrA." Mol Microbiol 1:259-273. Pubmed: 2834621
  • Wu, G., Williams, H. D., Zamanian, M., Gibson, F., Poole, R. K. (1992). "Isolation and characterization of Escherichia coli mutants affected in aerobic respiration: the cloning and nucleotide sequence of ubiG. Identification of an S-adenosylmethionine-binding motif in protein, RNA, and small-molecule methyltransferases." J Gen Microbiol 138:2101-2112. Pubmed: 1479344
  • Yamamoto, Y., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kimura, S., Kitagawa, M., Makino, K., Miki, T., Mitsuhashi, N., Mizobuchi, K., Mori, H., Nakade, S., Nakamura, Y., Nashimoto, H., Oshima, T., Oyama, S., Saito, N., Sampei, G., Satoh, Y., Sivasundaram, S., Tagami, H., Horiuchi, T., et, a. l. .. (1997). "Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." DNA Res 4:91-113. Pubmed: 9205837