IDH1 (YNL037C, P28834) notes

Evidence journal for the review (no paid deep research; built from UniProt and cached publications).

• NAD-IDH is a hetero-octamer of 4 Idh1 + 4 Idh2 built from Idh1/Idh2 heterodimers PMID:16884682.
• Idh1 is regulatory, Idh2 catalytic PMID:11042198.
• Idh1 residues contribute to the Idh2 catalytic site PMID:11042198.
• Idh1 site binds isocitrate for AMP activation, not catalysis PMID:11714283.
• Structures: regulatory and catalytic sites at subunit interfaces PMID:18256028.
• Physiology: idh mutants lose isocitrate/citrate-driven respiration PMID:2198251; activity correlates with growth on acetate/glycerol, low activity increases petites PMID:11714283.
• Import: presequence-dependent; cytosolic holoenzyme only with presequence deleted PMID:8626605. Reactome TAS rows for cytosol/IMS (import reaction) removed.
• UniProt: "Also binds RNA; specifically to the 5'-untranslated leaders of mitochondrial mRNAs" [UniProt:P28834]. No GOA annotation; raised as a suggested question.
• Curation: IEA "enables" GO:0004449 marked over-annotated (IDH1 non-catalytic; contributes_to is right). NAD binding / CH-OH oxidoreductase IEA from the family signature marked over-annotated for this regulatory subunit.