Lpd (PP_5366) is a dihydrolipoyl dehydrogenase E3 enzyme. It uses FAD and NAD+ to reoxidize protein-bound dihydrolipoyllysine to lipoyllysine, producing NADH for reuse of the lipoyl carrier in multienzyme systems.
| 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/lpd/lpd-deep-research-openscientist.md Reaction (UniProt/Rhea:15045, EC 1.8.1.4): |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | 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/lpd/lpd-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm |
| GO:0006103 2-oxoglutarate metabolic process | IEA GO_REF:0000118 | KEEP AS NON CORE | Summary: The exact E3 chemistry is established, but use by the 2-oxoglutarate dehydrogenase complex is not resolved for Lpd. Reason: Retain the TreeGrafter process call as non-core context because Lpd has compatible E3 chemistry, while the available KT2440 evidence does not establish which physiological client complex uses this paralog. |
| 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:0000120 | 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:0045333 cellular respiration | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: Cellular respiration is a broad downstream consequence rather than the specific role established for Lpd. Reason: The ARBA process call exceeds the exact dihydrolipoyl dehydrogenase chemistry supported by the record. |
| 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. |
| GO:1990234 transferase complex | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Lpd can act as an E3 component, but the physiological KT2440 client complex is unresolved. Reason: Retain the broad complex call as non-core context for an E3 enzyme; no evidence identifies which lipoyl-dependent assembly contains this paralog in vivo. |
Loading supporting content…
Download this section (compressed HTML)Q: Which lipoyl-dependent KT2440 multienzyme systems use Lpd in vivo?
Experiment: Compare native complex association and substrate turnover of Lpd, LpdG, and LpdV under glycine and 2-oxoacid growth conditions.
Type: affinity proteomics and comparative enzyme kinetics
Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)