Pseudomonas pyoverdine non-proteinogenic precursor supply

A reusable Pseudomonas module for reactions that supply unusual amino-acid building blocks to the cytoplasmic pyoverdine NRPS assembly line. PvdA hydroxylates L-ornithine to produce N5-hydroxy-L-ornithine, and PvdH forms L-2,4-diaminobutyrate from L-aspartate 4-semialdehyde by PLP-dependent transamination. Hydroxyornithine acylation, NRPS assembly, ferribactin export, periplasmic maturation, secretion, ferripyoverdine uptake, and iron release are outside this module.

Scope. Pyoverdine is restricted to the fluorescent pseudomonads, so the module stays at the Pseudomonas level rather than being generalized to siderophore-producing bacteria at large: the two reactions modelled here feed the pyoverdine chromophore and peptide specifically, and their homologs elsewhere (EctB in ectoine biosynthesis, IucD in aerobactin biosynthesis) serve different products. Within Pseudomonas the module uses Pseudomonas aeruginosa PAO1 as the experimentally best-characterized exemplar, where both enzymes have been purified and assayed and both mutants are pyoverdine-negative, alongside Pseudomonas putida KT2440, which produces a characterized pyoverdine and whose orthologs are reviewed in this repo. Both species are listed as representative members of the same family roles; they are exemplars, not a claim that the module is limited to them. The module is CONCRETE because it is a taxon-scoped realization whose terminal reactions ground to representative proteins. Grounding. The diaminobutyrate step is grounded on PANTHER:PTHR43552, adopting the family assignment from the maintainer module-grounding branch and verified against interpro/panther/panther.obo and the PANTHER member index; the accompanying family review adjudicates GO:0045303 as family-wide, since both subfamilies perform the same EC 2.6.1.76 transamination and differ only in the pathway that consumes L-2,4-diaminobutyrate. The ornithine hydroxylation step deliberately asserts no family id. Q51548 (PvdA) does belong to PANTHER:PTHR42802 and its subfamily PTHR42802:SF1, as its UniProt cross-reference and the family review record, but that family has a single subfamily that also contains lysine N6-monooxygenases (IucD, MbtG) and putrescine N-hydroxylases (AlcA, PubA, FbsI), and the purified enzymes are mutually substrate-specific. Family membership therefore cannot establish the ornithine-specific activity this annoton asserts, so the role is grounded on its representative members and on their gene reviews instead, per the "if you cannot be sure, assert no id" rule. Boundary. Hydroxyornithine acylation (PvdY/PP_4245), NRPS assembly, ferribactin export, periplasmic maturation, secretion, ferripyoverdine uptake and iron release all remain outside the module: it covers only the formation of the two non-proteinogenic amino-acid precursors. PvdY acetylation is adjacent tailoring whether its acceptor is free or NRPS-bound. PP_2800 of KT2440 shares the broad diaminobutyrate-transaminase family assignment with PvdH but lies outside the pyoverdine locus and is not used as an exemplar.