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Literature summary for 2.5.1.129 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
Search for more literature for 2.5.1.129

Crystallization (Commentary)

Crystallization (Comment) Organism
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
wild-type UbiX and mutant UbiXE49Q in complex with FMN and/or DMAP, crystal structure analysis Pseudomonas aeruginosa

Protein Variants

Protein Variants Comment Organism
E49Q mutation severely affects but does not abolish in vitro Fdc1 activation Pseudomonas aeruginosa
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]

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dimethylallyl phosphate + FMNH2 Pseudomonas aeruginosa
-
 prenylated FMNH2 + phosphate
-
 ?
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 ?
dimethylallyl phosphate + FMNH2 Pseudomonas aeruginosa ATCC 15692
-
 prenylated FMNH2 + phosphate
-
 ?
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

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

Reaction

Reaction Comment Organism Reaction ID
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dimethylallyl phosphate + FMNH2
-
 Pseudomonas aeruginosa prenylated FMNH2 + phosphate
-
 ?
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 ?
dimethylallyl phosphate + FMNH2 specific for dimethylallyl-monophosphate as substrate Pseudomonas aeruginosa prenylated FMNH2 + phosphate
-
 ?
dimethylallyl phosphate + FMNH2
-
 Pseudomonas aeruginosa ATCC 15692 prenylated FMNH2 + phosphate
-
 ?
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 ?
dimethylallyl phosphate + FMNH2 specific for dimethylallyl-monophosphate as substrate Pseudomonas aeruginosa ATCC 15692 prenylated FMNH2 + phosphate
-
 ?
additional information UbiX is a flavin mononucleotide (FMN)-binding protein and shows no decarboxylase activity Pseudomonas aeruginosa ?
-
 ?
additional information UbiX is a flavin mononucleotide (FMN)-binding protein and shows no decarboxylase activity Pseudomonas aeruginosa ATCC 15692 ?
-
 ?

Synonyms

Synonyms Comment Organism
flavin prenyltransferase
-
 Pseudomonas aeruginosa
ubiX
-
 Pseudomonas aeruginosa

Cofactor

Cofactor Comment Organism Structure
FMN required Pseudomonas aeruginosa

General Information

General Information Comment Organism
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