7qcw
From Proteopedia
Apo-structure of serine hydroxymethyltransferase (PbzB) involved in benzobactin biosynthesis in P. chlororaphis subsp. piscium DSM 21509
Structural highlights
FunctionA0A3G7DQ80_9PSED Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.[HAMAP-Rule:MF_00051] Publication Abstract from PubMedBenzoxazolinate is a rare bis-heterocyclic moiety that interacts with proteins and DNA and confers extraordinary bioactivities on natural products, such as C-1027. However, the biosynthetic gene responsible for the key cyclization step of benzoxazolinate remains unclear. Here, we show a putative acyl AMP-ligase responsible for the last cyclization step. We then use the enzyme as a probe for genome mining and discover that the orphan benzobactin gene cluster in entomopathogenic bacteria prevails across Proteobacteria and Firmicutes. It turns out that Pseudomonas chlororaphis produces various benzobactins, whose biosyntheses arehighlighted by a synergistic effect of two unclustered genes encoding enzymes on boosting benzobactin production; the formation of non-proteinogenic 2-hydroxymethylserine by a serine hydroxymethyltransferase; and the types I and II NRPS architecture for structural diversity. Our findings reveal the biosynthetic potential of a widespread benzobactin gene cluster. Genome Mining Enabled by Biosynthetic Characterization Uncovers a Class of Benzoxazolinate-Containing Natural Products in Diverse Bacteria.,Shi YM, Crames JJ, Czech L, Bozhuyuk KAJ, Shi YN, Hirschmann M, Lamberth S, Claus P, Paczia N, Ruckert C, Kalinowski J, Bange G, Bode HB Angew Chem Int Ed Engl. 2022 Oct 5. doi: 10.1002/anie.202206106. PMID:36198080[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
| ||||||||||||||||||
