Journal
MOLECULAR MICROBIOLOGY
Volume 110, Issue 2, Pages 239-261Publisher
WILEY
DOI: 10.1111/mmi.14100
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Funding
- NIH grant [R37 GM40313, F31 GM095230]
- Advanced Opportunity Fellowship - Graduate School of the University of Wisconsin
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Several of the enzymes involved in the conversion of adenosylcobyric acid (AdoCby) to adenosylcobamide (AdoCba) are yet to be identified and characterized in some cobamide (Cba)-producing prokaryotes. Using a bioinformatics approach, we identified the bluE gene (locus tag RSP_0788) of Rhodobacter sphaeroides 2.4.1 as a putative functional homolog of the L-threonine kinase enzyme (PduX, EC 2.7.1.177) of S. enterica. In AdoCba, (R)-1-aminopropan-2-ol O-phosphate (AP-P) links the nucleotide loop to the corrin ring; most known AdoCba producers derive AP-P from L-Thr-O-3-phosphate (L-Thr-P). Here, we show that RsBluE has L-Thr-independent ATPase activity in vivo and in vitro. We used P-31-NMR spectroscopy to show that RsBluE generates L-Thr-P at the expense of ATP and is unable to use L-Ser as a substrate. BluE from R. sphaeroides or Rhodobacter capsulatus restored AdoCba biosynthesis in S. enterica pduX and R. sphaeroides bluE mutant strains. R. sphaeroides bluE strains exhibited a decreased pigment phenotype that was restored by complementation with BluE. Finally, phylogenetic analyses revealed that bluE was restricted to the genomes of a few Rhodobacterales that appear to have a preference for a specific form of Cba, namely Co?-(?-5,6-dimethylbenzimidazolyl-Co?-adenosylcobamide (a.k.a. adenosylcobalamin, AdoCbl; coenzyme B-12, CoB12).
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