PA0317 (Q9I6H4) review notes

No deep-research provider was available. Sources: UniProt record, cached
PMID:28827360 (abstract and significance; PMC full text body not returned by the
PubMed MCP).

Function

Bacterial FAD-dependent D-2-hydroxyglutarate dehydrogenase (D2HGDH) identified in
P. stutzeri A1501 and P. aeruginosa PAO1 PMID:28827360.
Coupled to SerA and L-serine synthesis; deletion defect rescued by L-serine
PMID:28827360.
Electrons pass via ETF and ETFQO to the respiratory chain PMID:28827360.

PseudoCAP IBA-seed assessment

PTN node	node term	n_seeds	leaf IBAs	seed annotation (term, evidence, PMID)	verdict	rationale	other seeds	IBD stands without this seed?
PTN005178867	GO:0051990 (R)-2-hydroxyglutarate dehydrogenase activity	8	127 (103 taxa)	GO:0051990, IMP, PMID:28827360 (PseudoCAP)	SOUND	The paper biochemically identified the FAD-dependent D2HGDH activity (not merely a mutant phenotype) in PAO1 and P. stutzeri. The node term matches the D2HGDH family.	human D2HGDH Q8N465, Arabidopsis AT4G36400, rat RGD:1307976, two S. cerevisiae genes, Drosophila FBgn0023507, mouse MGI:2138209	Yes; human mitochondrial D2HGDH (Q8N465) and the yeast/plant members carry independent experimental support. No GO_CENTRAL defect.

PseudoCAP defects from this gene: none. The IMP GO:0051990 and GO:0006564 rows are
well supported by the cited paper.