aceE (P0AFG8) curation notes

Curated by Claude (AI-assisted), 2026-11-11, as the experimental E. coli exemplar for the PDH E1
annoton of modules/bacterial_pyruvate_metabolism.yaml.

Deep research was not run in this session (no -deep-research-*.md file); the review rests on the
cached abstracts and the Swiss-Prot record.

• E1p is a ThDP-dependent homodimer with two active centres at the subunit interface
  PMID:11955070.
• His-407 inner-loop residue is needed for reductive acetylation of E2p
  PMID:17635929.
• A covalent pre-decarboxylation intermediate analogue (PLThDP) orders two active-site loops
  PMID:16531404.
• The 15+1 bare protein-binding rows (high-throughput) are removed under the protein-binding policy.
• GO:0060090 molecular adaptor activity (EXP, PMID:11955070) is flagged as over-annotation; the
  abstract describes a catalytic E1, and E2-binding is part of the E1 reaction.
• The HDA membrane row is flagged; the PDH complex is soluble.