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Literature summary extracted from

  • White, M.D.; Payne, K.A.; Fisher, K.; Marshall, S.A.; Parker, D.; Rattray, N.J.; Trivedi, D.K.; Goodacre, R.; Rigby, S.E.; Scrutton, N.S.; Hay, S.; Leys, D.
    UbiX is a flavin prenyltransferase required for bacterial ubiquinone biosynthesis (2015), Nature, 522, 502-506.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.5.1.129 in complex with substrate, to 1.4 A resolution. The active site environment is dominated by pi systems, which assist phosphate-C19 bond breakage following FMN reduction, leading to formation of the N5-C19 bond. UbiX then acts as a chaperone for adduct reorientation, via transient carbocation species, leading ultimately to formation of the dimethylallyl C39-C6 bond Pseudomonas aeruginosa
2.5.1.129 wild-type UbiX and mutant UbiXE49Q in complex with FMN and/or DMAP, crystal structure analysis Pseudomonas aeruginosa

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.129 E49Q mutation severely affects but does not abolish in vitro Fdc1 activation Pseudomonas aeruginosa
2.5.1.129 E49Q site-directed mutagenesis, the mutant shows altered dimethylallyl phosphate binding. The mutation severely affects but does not abolish in vitro Fdc1 activation, N5 deprotonation through S15 and E49 is linked to N5-C19 bond formation, a process largely rendered ineffective through the E49Q mutation Pseudomonas aeruginosa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.129 additional information
-
 additional information stopped-flow measurements Pseudomonas aeruginosa

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.5.1.129 additional information no divalent cation required Pseudomonas aeruginosa
2.5.1.129 additional information enzyme UbiX is metal-independent Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.129 dimethylallyl phosphate + FMNH2 Pseudomonas aeruginosa
-
 prenylated FMNH2 + phosphate
-
 ?
2.5.1.129 dimethylallyl phosphate + FMNH2 Pseudomonas aeruginosa dimethylallylphosphate is required as substrate prenylated FMNH2 + phosphate UbiX produces a flavin-derived cofactor required for the decarboxylase activity of UbiD. UbiX acts as a flavin prenyltransferase, linking a dimethylallyl moiety to the flavin N5 and C6 atoms. This adds a fourth non-aromatic ring to the flavin isoalloxazine group ?
2.5.1.129 dimethylallyl phosphate + FMNH2 Pseudomonas aeruginosa ATCC 15692
-
 prenylated FMNH2 + phosphate
-
 ?
2.5.1.129 dimethylallyl phosphate + FMNH2 Pseudomonas aeruginosa ATCC 15692 dimethylallylphosphate is required as substrate prenylated FMNH2 + phosphate UbiX produces a flavin-derived cofactor required for the decarboxylase activity of UbiD. UbiX acts as a flavin prenyltransferase, linking a dimethylallyl moiety to the flavin N5 and C6 atoms. This adds a fourth non-aromatic ring to the flavin isoalloxazine group ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.129 Pseudomonas aeruginosa Q9HX08
-
-
2.5.1.129 Pseudomonas aeruginosa Q9HX08 gene ubiX
-
2.5.1.129 Pseudomonas aeruginosa ATCC 15692 Q9HX08
-
-
2.5.1.129 Pseudomonas aeruginosa ATCC 15692 Q9HX08 gene ubiX
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.5.1.129 dimethylallyl phosphate + FMNH2 = prenylated FMNH2 + phosphate the prenyltransferase mechanism of UbiX resembles that of the terpene synthases. The active site environment is dominated by Pi systems, which assist phosphate-C1' bond breakage following FMN reduction, leading to formation of the N5-C19 bond. UbiX then acts as a chaperone for adduct reorientation, via transient carbocation species, leading ultimately to formation of the dimethylallyl C39-C6 bond, reaction mechanism, overvie. Stopped-flow experiments mixing reduced FMNH2-UbiX with dimethylallyl phosphate under anaerobic conditions reveal transient formation of a distinct spectral species before formation of the prFMNreduced product. The dimethylallyl phosphate substrate is located directly above the FMN isoalloxazine re face, with the dimethylallyl moiety sandwiched between the FMN and A89-S90. The dimethylallyl group is furthermore surrounded by aromatic ring systems of W84, Y169 and W200 that, together with the FMN dimethylbenzene moiety, resemble the Pi-cage found in other prenyltransferases or terpene synthases Pseudomonas aeruginosa
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.129 dimethylallyl phosphate + FMNH2
-
 Pseudomonas aeruginosa prenylated FMNH2 + phosphate
-
 ?
2.5.1.129 dimethylallyl phosphate + FMNH2 dimethylallylphosphate is required as substrate Pseudomonas aeruginosa prenylated FMNH2 + phosphate UbiX produces a flavin-derived cofactor required for the decarboxylase activity of UbiD. UbiX acts as a flavin prenyltransferase, linking a dimethylallyl moiety to the flavin N5 and C6 atoms. This adds a fourth non-aromatic ring to the flavin isoalloxazine group ?
2.5.1.129 dimethylallyl phosphate + FMNH2 specific for dimethylallyl-monophosphate as substrate Pseudomonas aeruginosa prenylated FMNH2 + phosphate
-
 ?
2.5.1.129 dimethylallyl phosphate + FMNH2
-
 Pseudomonas aeruginosa ATCC 15692 prenylated FMNH2 + phosphate
-
 ?
2.5.1.129 dimethylallyl phosphate + FMNH2 dimethylallylphosphate is required as substrate Pseudomonas aeruginosa ATCC 15692 prenylated FMNH2 + phosphate UbiX produces a flavin-derived cofactor required for the decarboxylase activity of UbiD. UbiX acts as a flavin prenyltransferase, linking a dimethylallyl moiety to the flavin N5 and C6 atoms. This adds a fourth non-aromatic ring to the flavin isoalloxazine group ?
2.5.1.129 dimethylallyl phosphate + FMNH2 specific for dimethylallyl-monophosphate as substrate Pseudomonas aeruginosa ATCC 15692 prenylated FMNH2 + phosphate
-
 ?
2.5.1.129 additional information UbiX is a flavin mononucleotide (FMN)-binding protein and shows no decarboxylase activity Pseudomonas aeruginosa ?
-
 ?
2.5.1.129 additional information UbiX is a flavin mononucleotide (FMN)-binding protein and shows no decarboxylase activity Pseudomonas aeruginosa ATCC 15692 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.5.1.129 flavin prenyltransferase
-
 Pseudomonas aeruginosa
2.5.1.129 ubiX
-
 Pseudomonas aeruginosa

Cofactor

EC Number Cofactor Comment Organism Structure
2.5.1.129 FMN required Pseudomonas aeruginosa

General Information

EC Number General Information Comment Organism
2.5.1.129 physiological function UbiX produces a novel flavin-derived cofactor required for the decarboxylase activity of UbiD. UbiX acts as a flavin prenyltransferase, linking a dimethylallyl moiety to the flavin N5 and C6 atoms. This adds a fourth non-aromatic ring to the flavin isoalloxazine group Pseudomonas aeruginosa