LpdG (PP_4187) is a class-I pyridine nucleotide-disulfide oxidoreductase with dihydrolipoyl dehydrogenase activity. It uses FAD and NAD+ to reoxidize protein-bound dihydrolipoyllysine, allowing it to serve as a shared E3 enzyme for lipoyl-dependent multienzyme systems. Orthology and operon context support its assignment as the KT2440 counterpart of characterized P. putida LPD-glc, which serves pyruvate and 2-oxoglutarate dehydrogenases and the glycine oxidation system in the characterized strains. The glycine-cleavage role has not been tested directly in KT2440.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004148 dihydrolipoyl dehydrogenase (NADH) activity | IEA GO_REF:0000120 | ACCEPT | Summary: dihydrolipoyl dehydrogenase (NADH) activity is consistent with the curated UniProt name, EC/family evidence, and the gene product role summarized here. Reason: This is a specific, biologically appropriate annotation for this gene product. Supporting Evidence: file:PSEPK/lpdG/lpdG-deep-research-openscientist.md Rhea RHEA:15045 |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: A cytoplasmic location is plausible for this soluble bacterial enzyme but is not a core function. Reason: Retain the UniProt-derived location outside the catalytic core summary. Supporting Evidence: file:PSEPK/lpdG/lpdG-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm |
| GO:0006103 2-oxoglutarate metabolic process | IEA GO_REF:0000118 | ACCEPT | Summary: LpdG is the E3 component encoded with the KT2440 2-oxoglutarate dehydrogenase genes. Reason: The TreeGrafter call agrees with conserved lpdG/LPD-glc function and the adjacent sucA/sucB complex genes. Supporting Evidence: PMID:1902462 LPD-glc, which is the E3 component of the pyruvate and 2-ketoglutarate dehydrogenase complexes and the L-factor for the glycine oxidation system |
| GO:0016491 oxidoreductase activity | IEA GO_REF:0000002 | MARK AS OVER ANNOTATED | Summary: oxidoreductase activity is a broad parent or generic domain-derived term that adds little beyond the specific catalytic annotation. Reason: The annotation is not necessarily false, but it is less informative than the specific molecular function already present. |
| GO:0016668 oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor is biologically plausible for this enzyme but is ancillary to the more specific catalytic function. Reason: Retain as a supporting/non-core annotation rather than using it as the main functional summary. |
| GO:0050660 flavin adenine dinucleotide binding | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: flavin adenine dinucleotide binding is biologically plausible for this enzyme but is ancillary to the more specific catalytic function. Reason: Retain as a supporting/non-core annotation rather than using it as the main functional summary. |
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Download this section (compressed HTML)Q: Does KT2440 LpdG supply the glycine-cleavage L-protein activity in vivo, as predicted from the experimentally characterized P. putida LPD-glc enzyme?
Q: Should the Q88FB1 UniProt ARBA function text be corrected because it describes the branched-chain complex assigned to LpdV?
Experiment: Compare glycine-dependent growth and native GCS activity across lpdG, lpd, and lpdV mutants, followed by biochemical complementation.
Type: genetics and enzyme-complex reconstitution
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