Structural highlights
Function
UBIX_PSEAE Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN.[HAMAP-Rule:MF_01984][1]
Publication Abstract from PubMed
The ubiX gene (PA4019) of Pseudomonas aeruginosa has been annotated as encoding a putative 3-octaprenyl-4-hydroxybenzoate decarboxylase from the ubiquinone-biosynthesis pathway. Based on a transposon mutagenesis screen, this gene was also implicated as being essential for the survival of this organism. The crystal structure of recombinant UbiX determined to 1.5 A resolution showed that the protein belongs to the superfamily of homo-oligomeric flavine-containing cysteine decarboxylases. The enzyme assembles into a dodecamer with 23 point symmetry. The subunit displays a typical Rossmann fold and contains one FMN molecule bound at the interface between two subunits.
Structure of PA4019, a putative aromatic acid decarboxylase from Pseudomonas aeruginosa.,Kopec J, Schnell R, Schneider G Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Oct 1;67(Pt 10):1184-8., Epub 2011 Sep 24. PMID:22102023[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ White MD, Payne KA, Fisher K, Marshall SA, Parker D, Rattray NJ, Trivedi DK, Goodacre R, Rigby SE, Scrutton NS, Hay S, Leys D. UbiX is a flavin prenyltransferase required for bacterial ubiquinone biosynthesis. Nature. 2015 Jun 25;522(7557):502-6. doi: 10.1038/nature14559. Epub 2015 Jun 17. PMID:26083743 doi:http://dx.doi.org/10.1038/nature14559
- ↑ Kopec J, Schnell R, Schneider G. Structure of PA4019, a putative aromatic acid decarboxylase from Pseudomonas aeruginosa. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Oct 1;67(Pt 10):1184-8., Epub 2011 Sep 24. PMID:22102023 doi:10.1107/S174430911102923X