LpdV (PP_4404) is the LPD-val dihydrolipoyl dehydrogenase of the branched-chain 2-oxoacid dehydrogenase complex. It uses FAD and NAD+ to reoxidize the protein-bound dihydrolipoyl group and is encoded with the other bkd complex components.
| 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/lpdV/lpdV-deep-research-openscientist.md encodes **LPD-val**, a **dihydrolipoyl dehydrogenase** |
| 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/lpdV/lpdV-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm |
| GO:0006103 2-oxoglutarate metabolic process | IEA GO_REF:0000118 | REMOVE | Summary: LpdV is the branched-chain-complex E3 rather than the 2-oxoglutarate dehydrogenase E3. Reason: The TreeGrafter process call crosses P. putida E3 paralogs; LPD-val is experimentally distinguished from LPD-glc and is encoded in the KT2440 bkd operon. Supporting Evidence: PMID:1902462 LPD-val, which is the specific E3 component of the branched-chain keto acid dehydrogenase complex file:PSEPK/lpdV/lpdV-deep-research-openscientist.md The gene lies at the **3′ end of the bkd operon** |
| 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 LpdV have any physiological client outside the branched-chain 2-oxoacid dehydrogenase complex?
Experiment: Compare native complex association and substrate turnover of LpdV, LpdG, and Lpd under glycine and 2-oxoacid growth conditions.
Type: affinity proteomics and comparative enzyme kinetics
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