ACH1 notes

• ACH1/P32316 is in PANTHER family PTHR43609:SF1. The relevant PAINT node for the activity and acetate-metabolism assertions is PTN000484586, which carries GO:0003986, GO:0008775, and GO:0006083; the mitochondrial placement is on PTN000484602.
• Acetyl-CoA hydrolase activity is experimentally supported but secondary. Buu et al. showed that Ach1p activity depends on putative acetyl-CoA binding sites [PMID:12606555, "Using site-directed mutagenesis analysis, we demonstrated that the enzymatic activity of Ach1p is dependent upon its putative acetyl-CoA binding sites."], while Fleck and Brock found the dominant reaction to be CoASH transfer from succinyl-CoA to acetate [PMID:19298859, "Ach1p showed highest specific activity for the CoASH transfer from succinyl-CoA to acetate and only a minor acetyl-CoA-hydrolase activity."] and reframed the hydrolase as non-physiological [PMID:19298859, "Thereby, Ach1p does not perform the energy wasting hydrolysis of acetyl-CoA but conserves energy by the detoxification of mitochondrial acetate."].
• The specific acetate CoA-transferase activity rows should be core accepts. Fleck and Brock state that Ach1p participates in mitochondrial acetate detoxification through CoASH transfer from succinyl-CoA to acetate [PMID:19298859, "Our results imply that Ach1p is involved in mitochondrial acetate detoxification by a CoASH transfer from succinyl-CoA to acetate."].
• The acetate-metabolism process rows are supported by the ach1 null phenotype and by the re-characterized reaction: Lee et al. reported that the null mutation "slows down acetate utilization" PMID:8841387.
• Mitochondrion is the primary localization. The direct localization paper found that most Ach1p cofractionates with mitochondria and that full-length Ach1p localizes to mitochondria by immunofluorescence [PMID:12606555, "By subcellular fractionation, most of the Ach1p in yeast was distributed with mitochondria and little Ach1p in the cytoplasm."].
• A cytosolic/cytoplasmic ACH1 pool is plausible but non-core. The cached PMID:11746603 abstract reports ACH1 up-regulation during sorbic-acid stress rather than localization, so the SGD GO:0005829 row is retained as a secondary localization from the small cytoplasmic fraction seen by Buu et al.; the UniProt cytoplasm IEA is a broader ancestor of the accepted mitochondrial and cytosolic rows.
• No existing row needed removal. The only specificity cleanup was marking broad cytoplasm and CoA-transferase activity IEAs as TOO_GENERAL because more specific descendant terms are already asserted.