Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniPathway vocabulary mapping
Evidence that WbpD is an N-acetyltransferase belonging to the hexapeptide acyltransferase superfamily and an important protein for O-antigen biosynthesis in Pseudomonas aeruginosa PAO1.
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wbpD knockout lacks long-chain B-band O antigen and semi-rough LPS; WbpD is a trimeric LbetaH protein that binds acetyl-CoA; no substrate was available for activity assays.
"A chromosomal knockout mutant of wbpD is incapable of producing either long-chain B-band O antigen"
Characterization of WbpB, WbpE, and WbpD and reconstitution of a pathway for the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid in Pseudomonas aeruginosa.
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The WbpD product UDP-GlcNAc3NAcA was detected by MALDI-TOF MS in coupled reactions and characterised by NMR.
"in reactions involving WbpB, WbpE, and WbpD, an ion consistent with the expected product of WbpD (UDP-d-GlcNAc3NAcA) was identified"
Biosynthesis of UDP-GlcNAc(3NAc)A by WbpB, WbpE, and WbpD: enzymes in the Wbp pathway responsible for O-antigen assembly in Pseudomonas aeruginosa PAO1.
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WbpD acetylates UDP-GlcNAc3NA (Km 107 uM, kcat 2.9 x 10^3 min-1); the five Wbp enzymes reconstitute UDP-ManNAc3NAcA from UDP-GlcNAc in vitro.
"we confirm that WbpD catalyzes the acetylation of UDP-GlcNAc(3NH(2))A to give UDP-GlcNAc(3NAc)A"
Biosynthesis of a rare di-N-acetylated sugar in the lipopolysaccharides of both Pseudomonas aeruginosa and Bordetella pertussis occurs via an identical scheme despite different gene clusters.
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B. pertussis homologs, including the WbpD homolog, complement the corresponding P. aeruginosa knockouts.
"the genes that encode the putative oxidase, transaminase, N-acetyltransferase, and epimerase enzymes in B. pertussis are functional homologs of those in P. aeruginosa"