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 has lost ketopantoate activity and instead reduces several alpha-keto-acid substrates.

"resulting in its inactivity toward the natural substrate ketopantoate"

file:PSEPK/PP_2998/PP_2998-uniprot.txt

UniProtKB entry for PP_2998

The unreviewed record electronically assigns EC 1.1.1.169 while placing Q88IK1 in a broad KPR-related ApbA oxidoreductase family.

file:PSEPK/PP_2998/PP_2998-goa.tsv

QuickGO GOA annotations for PP_2998

The fetched GOA table contains the three electronic annotations reviewed for PP_2998.

file:PSEPK/PP_2998/PP_2998-notes.md

Manual curation notes for PP_2998

The notes document the canonical-PanE family distinction, functional heterogeneity within the KPR-related family, and unresolved substrate.

file:PSEPK/PP_2998/PP_2998-deep-research-openscientist.md

OpenScientist deep research for PP_2998

The report retrieved useful family and structural context but found no direct experiment on Q88IK1. Its PanE assignment relies on orthology and is not sufficient to resolve substrate specificity across the functionally heterogeneous KPR-related family.

"No direct experimental data on the *P. putida* protein."

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 species-aware report distinguishes PP_2998 from canonical PanE and identifies its substrate specificity as unresolved.