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Literature summary extracted from

  • 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 (2015), Biochem. J., 470, 105-114.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.114 expressed in Escherichia coli BL21(DE3) cells Homo sapiens
2.1.1.114 expressed in Escherichia coli BL21(DE3) cells Escherichia coli
2.1.1.222 expressed in Escherichia coli BL21(DE3) cells Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.1.114
-
 Escherichia coli
2.1.1.222
-
 Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.222 H186A the mutation completely destroys the interaction of the enzyme with liposomes Escherichia coli
2.1.1.222 I177A the mutation sharply reduces the interaction of the enzyme with liposomes Escherichia coli
2.1.1.222 K183A the mutation nearly completely destroys the interaction of the enzyme with liposomes Escherichia coli
2.1.1.222 L178A the mutation nearly completely destroys the interaction of the enzyme with liposomes Escherichia coli
2.1.1.222 L178E the mutation nearly completely destroys the interaction of the enzyme with liposomes Escherichia coli
2.1.1.222 R179A the mutation sharply reduces the interaction of the enzyme with liposomes Escherichia coli
2.1.1.222 V181A the mutation nearly completely destroys the interaction of the enzyme with liposomes Escherichia coli
2.1.1.222 V181A/P182A/K183A/G184A/T185A/H186A the mutations nearly completely destroy the interaction of the enzyme with liposomes Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.1.1.114 mitochondrial membrane
-
 Homo sapiens 31966
-
2.1.1.114 plasma membrane
-
 Escherichia coli 5886
-
2.1.1.222 membrane
-
 Escherichia coli 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.114 S-adenosyl-L-methionine + 3,4-dihydroxy-5-all-trans-polyprenylbenzoate Homo sapiens
-
 S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-5-all-trans-polyprenylbenzoate
-
 ?
2.1.1.114 S-adenosyl-L-methionine + 3,4-dihydroxy-5-all-trans-polyprenylbenzoate Escherichia coli
-
 S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-5-all-trans-polyprenylbenzoate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.114 Escherichia coli P17993
-
-
2.1.1.114 Homo sapiens
-
-
-
2.1.1.222 Escherichia coli P17993
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.114 Ni-NTA column chromatography and Superdex 200 gel filtration Homo sapiens
2.1.1.114 Ni-NTA column chromatography and Superdex 200 gel filtration Escherichia coli
2.1.1.222 Ni-NTA column chromatography, HiTrap column chromatography, and Superdex 200 gel filtration Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.114 S-adenosyl-L-methionine + 3,4-dihydroxy-5-all-trans-polyprenylbenzoate
-
 Homo sapiens S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-5-all-trans-polyprenylbenzoate
-
 ?
2.1.1.114 S-adenosyl-L-methionine + 3,4-dihydroxy-5-all-trans-polyprenylbenzoate
-
 Escherichia coli S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-5-all-trans-polyprenylbenzoate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.1.114 monomer x-ray crystallography Escherichia coli
2.1.1.222 monomer x-ray crystallography Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.1.1.114 COQ3
-
 Homo sapiens
2.1.1.114 UbiG
-
 Escherichia coli
2.1.1.222 UbiG
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.222 S-adenosyl-L-methionine dependent on Escherichia coli

General Information

EC Number General Information Comment Organism
2.1.1.114 physiological function the primary role of the enzyme is to serve as an electron carrier in the respiratory electron transport chain in the mitochondrial inner membrane Homo sapiens
2.1.1.114 physiological function the primary role of the enzyme is to serve as an electron carrier in the respiratory electron transport chain in the plasma membrane Escherichia coli