TreeGrafter-generated GO annotations
Cloning and nucleotide sequence of the pvdA gene encoding the pyoverdin biosynthetic enzyme L-ornithine N5-oxygenase in Pseudomonas aeruginosa.
-
PvdA catalyzes ornithine hydroxylation early in pyoverdine biosynthesis
"The enzyme L-ornithine N5-oxygenase catalyzes the hydroxylation of L-ornithine (L-Orn), which represents an early step in the biosynthesis of the peptidic moiety of the fluorescent siderophore pyoverdin in Pseudomonas aeruginosa."
-
pvdA loss abolishes pyoverdine synthesis and is rescued by N5-hydroxyornithine
"the pvdA mutant obtained by gene disruption also disclosed no pyoverdin synthesis, lacked L-Orn N5-oxygenase activity, was complemented by the cloned pvdA gene, and produced pyoverdin at wild-type levels when fed with the biosynthetic precursor L-N5-OH-Orn."
Heterologous expression, purification, and characterization of an l-ornithine N(5)-hydroxylase involved in pyoverdine siderophore biosynthesis in Pseudomonas aeruginosa.
-
PvdA is a flavin-dependent monooxygenase that hydroxylates ornithine
"Formation of the iron-chelating hydroxamate functional group in pyoverdine requires the enzyme PvdA, a flavin-dependent monooxygenase that catalyzes the N(5) hydroxylation of l-ornithine."
-
PvdA specifically uses NADPH and FAD cofactors
"The enzyme is specific for NADPH and flavin adenine dinucleotide (FAD(+)) as cofactors, as it cannot utilize NADH and flavin mononucleotide."
Two structures of an N-hydroxylating flavoprotein monooxygenase: ornithine hydroxylase from Pseudomonas aeruginosa.
-
PvdA is a class B flavoprotein monooxygenase
"PvdA belongs to the class B flavoprotein monooxygenases, which catalyze the oxidation of substrates using NADPH as the electron donor and molecular oxygen."
-
PvdA has Rossmann-like FAD and NADPH binding domains
"PvdA has the two expected Rossmann-like dinucleotide-binding domains for FAD and NADPH and also a substrate-binding domain, with the active site at the interface between the three domains."
Membrane-association determinants of the omega-amino acid monooxygenase PvdA, a pyoverdine biosynthetic enzyme from Pseudomonas aeruginosa.
-
PvdA provides an essential enzymic function in pyoverdine biogenesis
"The L-ornithine N(delta)-oxygenase PvdA catalyses the N(delta)-hydroxylation of L-ornithine in many Pseudomonas spp., and thus provides an essential enzymic function in the biogenesis of the pyoverdine siderophore."
-
PvdA has membrane association but its bulk spans the cytosol
"The inferred topological model resembled a eukaryotic reverse signal-anchor (type III) protein, with a single N-terminal domain anchored to the inner membrane, and the bulk of the protein spanning the cytosol."
High cellular organization of pyoverdine biosynthesis in Pseudomonas aeruginosa: clustering of PvdA at the old cell pole.
-
PvdA is one of the initial cytoplasmic enzymes in pyoverdine biosynthesis
"generate P.aeruginosa strains producing fluorescent fusions with PvdA, one of the initial enzymes in the biosynthetic pathway of PVDI in the cytoplasm"
-
PvdA can also be recovered in a membrane fraction
"Cellular fractionation indicated that a substantial amount of PvdA-YFP was located in the membrane fraction."
Siderophore-mediated iron acquisition in the entomopathogenic bacterium Pseudomonas entomophila L48 and its close relative Pseudomonas putida KT2440.
-
KT2440 produces a characterized pyoverdine and no second siderophore was detected
"Structural analysis of the pyoverdine produced by the closely related P. putida KT2440 showed that this strain produces an already characterised pyoverdine, but different from P. entomophila, and no evidence was found for the production of a second siderophore."
PvdRT-OpmQ and MdtABC-OpmB efflux systems are involved in pyoverdine secretion in Pseudomonas putida KT2440.
-
Pyoverdine secretion genes are stimulated by iron limitation in KT2440
"Expression from the respective promoters is stimulated by iron limitation albeit to varying degrees."
-
Reduced pyoverdine secretion decreases growth under iron limitation
"Deletion of pvdRT-opmQ leads to reduced amounts of pyoverdine in the medium and decreased growth under iron limitation."
Arginine Biosynthesis Modulates Pyoverdine Production and Release in Pseudomonas putida as Part of the Mechanism of Adaptation to Oxidative Stress.
-
Defects affecting pyoverdine production increase KT2440 sensitivity to iron limitation
"Mutants defective in arginine biosynthesis show reduced production and release of the siderophore pyoverdine and altered expression of certain pyoverdine-related genes, resulting in higher sensitivity to iron limitation."
Deep research on pvdA in Pseudomonas putida KT2440
-
"Q88GC8 is the KT2440 ortholog of the pyoverdine biosynthetic ornithine hydroxylase PvdA"
-
"The direct process annotation is pyoverdine biosynthetic process rather than intracellular iron ion homeostasis"
-
"Cytoplasm is the conservative cellular component call for KT2440 PvdA"
Falcon deep research on pvdA (Q88GC8 / PP_3796) in Pseudomonas putida KT2440
-
"The UniProt accession **Q88GC8** corresponds to **pvdA / PP_3796** from *Pseudomonas putida* strain KT2440 and is functionally described as an **L-ornithine N5-monooxygenase (ornithine hydroxylase)**"
-
"**pvdA encodes the enzyme catalyzing the N5-hydroxylation of L-ornithine** to produce **N5-hydroxyornithine**, which is subsequently **formylated by PvdF** to yield **N5-formyl-N5-hydroxyornithine (L-fOHOrn)**."
-
"PvdA belongs to the **flavin-dependent N-hydroxylating monooxygenase / Class B flavin monooxygenase** family."
-
"dependence on **FAD** as a flavin cofactor and **molecular oxygen** as the oxygen donor, proceeding through **C4a-peroxy/hydroperoxyflavin** intermediates that effect oxygen transfer to the substrate amine"
-
"**substrate binding triggers O2 addition but not flavin reduction**, consistent with gating of the oxidative half-reaction by L-ornithine binding"
-
"PvdA functions in the **cytoplasmic phase** of **pyoverdine siderophore biosynthesis**, supplying a modified amino acid building block needed by the **NRPS assembly line**."
-
"Pyoverdine biosynthesis initiates in the **cytoplasm**"
-
"**PvdA physically interacts with all four pyoverdine NRPSs**"
-
"This is an early, committed tailoring step in pyoverdine assembly."
-
"**pvdA** and **pvdD** expression increased in these mutants, while **pvdE** (an inner-membrane transporter needed for immature pyoverdine handling) decreased"
OpenScientist deep research report for pvdA in Pseudomonas putida KT2440
-
"The gene **pvdA** (UniProt **Q88GC8**, ordered locus **PP_3796**) of *Pseudomonas putida* KT2440 encodes **L-ornithine N⁵-oxygenase (PvdA)**"
-
"Direct biochemistry is from orthologs, not Q88GC8 itself."
-
"Formyltransferase identity in KT2440."