TreeGrafter-generated GO annotations

Combined Automated Annotation using Multiple IEA Methods

Implication of Molecular Constraints Facilitating the Functional Evolution of Pseudomonas aeruginosa KPR2 into a Versatile α-Keto-Acid Reductase.

PaKPR2 is inactive on ketopantoate and instead reduces multiple alpha-keto-acid substrates.

"resulting in its inactivity toward the natural substrate ketopantoate"

file:PSEPK/PP_2325/PP_2325-uniprot.txt

UniProtKB entry for PP_2325

The unreviewed record carries an electronically transferred EC 1.1.1.169 assignment and places Q88KG5 in a broad KPR-related ApbA family.

file:PSEPK/PP_2325/PP_2325-goa.tsv

QuickGO GOA annotations for PP_2325

The fetched GOA table contains the three electronic annotations reviewed for PP_2325.

file:PSEPK/PP_2325/PP_2325-notes.md

Manual curation notes for PP_2325

The notes record the family distinction and OrtholugeDB reciprocal-best orthology between PP_2325 and P. aeruginosa PA1752/PaKPR2, and explain why that evidence supersedes the generic PanE inference in the gene-level retrieval report.

file:PSEPK/PP_2325/PP_2325-deep-research-openscientist.md

OpenScientist gene research for PP_2325

The report usefully retrieves generic KPR structure and mechanism but repeats the electronic PanE assignment from distant E. coli similarity without evaluating the closer PaKPR2 ortholog. It also confirms that no direct experiment has tested Q88KG5.

"No direct experimental characterization of PP_2325."

file:projects/P_PUTIDA/deep-research/PSEPK__coenzyme_a_biosynthesis__ppu00770-deep-research-openscientist.md

OpenScientist pathway research for PSEPK pantothenate and CoA biosynthesis

The pathway report identifies paralog ambiguity at the ketopantoate reductase step; manual orthology review resolves PP_2325 away from the canonical PanE role.