PMID:23558683

Citation	'Bertsova, YV, Fadeeva, MS, Kostyrko, VA, Serebryakova, MV, Baykov, AA and Bogachev, AV (2013) Alternative Pyrimidine Biosynthesis Protein ApbE is a Flavin Transferase Catalyzing Covalent Attachment of FMN to a Threonine Residue in Bacterial Flavoproteins. J. Biol. Chem. '
Abstract	Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) contains two flavin residues as redox-active prosthetic groups attached by a phosphoester bond to threonine residues in subunits NqrB and NqrC. We demonstrate here that flavinylation of truncated Vibrio harveyi NqrC at Thr229 in Escherichia coli cells requires the presence of a co-expressed Vibrio apbE gene. The apbE genes cluster with genes for Na+-NQR and other FMN-binding flavoproteins in bacterial genomes and encode proteins with previously unknown function. Experiments with isolated NqrC and ApbE proteins confirmed that ApbE is the only protein factor required for NqrC flavinylation and also indicated that the reaction is Mg2+-dependent and proceeds with FAD but not FMN. Inactivation of the apbE gene in Klebsiella pneumoniae, wherein the nqr operon and apbE are well separated in the chromosome, resulted in a complete loss of the quinone reductase activity of Na+-NQR, consistent with its dependence on covalently bound flavin. Our data thus identify ApbE as a novel modifying enzyme, flavin transferase.
Links	PubMed Online version:10.1074/jbc.M113.455402
Keywords
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
KLEP3:APBE1		GO:0017013: protein flavinylation	ECO:0000314:		P		Figure 7.	complete CACAO 7918
KLEP3:APBE1	involved_in	GO:0017013: protein flavinylation	ECO:0000314: direct assay evidence used in manual assertion		P		Seeded From UniProt	complete

References

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