6pd1
From Proteopedia
PntC-AEPT: fusion protein of phosphonate-specific cytidylyltransferase and 2-aminoethylphosphonate (AEP) transaminase from Treponema denticola
Structural highlights
FunctionPNTCW_TREDE Bifunctional transferase involved in the biosynthesis of cell-surface phosphonates (PubMed:31420548). The aminotransferase region catalyzes the transformation of phosphonoacetaldehyde (PnAA) to 2-aminoethylphosphonate (AEP) (PubMed:31420548). The cytidylyltransferase region catalyzes the activation of 2-aminoethylphosphonate (AEP) to CMP-2-aminoethylphosphonate (CMP-AEP) (PubMed:31420548). Cannot use phosphocholine (PubMed:31420548). Exhibits strong activity towards CTP, limited activity towards ATP and no activity with GTP (PubMed:31420548).[1] Publication Abstract from PubMedPhosphonates are rare and unusually bioactive natural products. However, most bacterial phosphonate biosynthetic capacity is dedicated to tailoring cell surfaces with molecules like 2-aminoethylphosphonate (AEP). Although phosphoenolpyruvate mutase (Ppm)-catalyzed installation of C-P bonds is known, subsequent phosphonyl tailoring (Pnt) pathway steps remain enigmatic. Here we identify nucleotidyltransferases in over two-thirds of phosphonate biosynthetic gene clusters, including direct fusions to ~60% of Ppm enzymes. We characterize two putative phosphonyl tailoring cytidylyltransferases (PntCs) that prefer AEP over phosphocholine (P-Cho) - a similar substrate used by the related enzyme LicC, which is a virulence factor in Streptococcus pneumoniae. PntC structural analyses reveal steric discrimination against phosphocholine. These findings highlight nucleotidyl activation as a predominant chemical logic in phosphonate biosynthesis and set the stage for probing diverse phosphonyl tailoring pathways. The predominance of nucleotidyl activation in bacterial phosphonate biosynthesis.,Rice K, Batul K, Whiteside J, Kelso J, Papinski M, Schmidt E, Pratasouskaya A, Wang D, Sullivan R, Bartlett C, Weadge JT, Van der Kamp MW, Moreno-Hagelsieb G, Suits MD, Horsman GP Nat Commun. 2019 Aug 16;10(1):3698. doi: 10.1038/s41467-019-11627-6. PMID:31420548[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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