acu-8 encodes the Neurospora crassa member of the conserved fungal Ach1 acetyl-CoA hydrolase/transferase family. Acu-8 is required for growth on acetate and acts in mitochondria as a succinyl-CoA:acetate CoA-transferase that links acetate with acetyl-CoA metabolism while retaining minor acetyl-CoA hydrolase activity.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003986 acetyl-CoA hydrolase activity | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: PTN000484586 places acu-8 in the fungal Ach1 clade that inherited acetyl-CoA hydrolase activity. Reason: Neurospora acu-8 has direct target evidence; an acetate-sensitive acu-8 mutant is deficient in acetyl-CoA hydrolase and accumulates acetyl-CoA when supplied with acetate. Later fungal Ach1 work reclassified the family toward acetate CoA-transferase as the major in vivo activity, but S. cerevisiae Ach1p still has minor acetyl-CoA hydrolase activity. The PTN000484586 IBA is therefore consistent with the direct Neurospora phenotype and with fungal family biochemistry. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000484586 SUPPORTS TRANSFER acu-8 falls under the PTHR43609 fungal Ach1 node whose seed data support acetyl-CoA hydrolase as a secondary conserved activity. Supporting Evidence: PMID:1357077 The mutant was shown to be deficient in acetyl-CoA hydrolase and to accumulate acetyl-CoA when supplied with 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. |
| GO:0003986 acetyl-CoA hydrolase activity | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: The Rhea/EC IEA to acetyl-CoA hydrolase activity agrees with direct acu-8 mutant evidence. Reason: The GO:0003986 claim is supported by the classic Neurospora acu-8 mutant, which is deficient in acetyl-CoA hydrolase after growth on acetate. Although the fungal Ach1 family is now understood to act primarily as acetate CoA-transferases, acetyl-CoA hydrolase activity remains experimentally observed and is appropriate to keep. Supporting Evidence: PMID:1357077 The mutant was shown to be deficient in acetyl-CoA hydrolase and to accumulate acetyl-CoA when supplied with 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. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | MODIFY | Summary: The UniProtKB-SubCell cytoplasm mapping is too broad for the fungal Ach1/acu-8 mitochondrial placement. Reason: S. cerevisiae Ach1p was localized mostly with mitochondria by subcellular fractionation and in mitochondria by immunofluorescence, and the more specific PTN000484602 PAINT node places mitochondrial activity in the Ascomycota. Review this broad cytoplasmic IEA as mitochondrion rather than retaining a nonspecific parent localization. Proposed replacements: mitochondrion Supporting Evidence: PMID:12606555 By subcellular fractionation, most of the Ach1p in yeast was distributed with mitochondria and little Ach1p in the cytoplasm. |
| GO:0005739 mitochondrion | IBA GO_REF:0000033 | ACCEPT | Summary: PTN000484602 places acu-8 in the Ascomycota subclade that inherited mitochondrial Ach1 activity. Reason: The IBA is scoped to PTN000484602 rather than the whole CoA-transferase family, and Neurospora acu-8 falls in the same PTHR43609:SF1 fungal Ach1 subfamily as the characterized S. cerevisiae and Candida ACH1 proteins. The experimentally observed S. cerevisiae Ach1p mitochondrial localization supports keeping this Ascomycota PAINT placement. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000484602 SUPPORTS TRANSFER PTN000484602 places the mitochondrial localization on the Ascomycota branch, and acu-8 remains in the fungal Ach1 subfamily below that node. Supporting Evidence: PMID:12606555 By immunofluorescence microscopy, we show that Ach1p and acetyl-CoA binding site-mutated constructs, but not its N-terminal deleted construct, are localized in mitochondria. |
| GO:0005739 mitochondrion | IEA GO_REF:0000117 | ACCEPT | Summary: The electronic mitochondrion call agrees with the PTN000484602 PAINT placement. Reason: ARBA's electronic mitochondrion assignment is biologically consistent with the Ascomycota-specific PAINT node for P15937 and with experimental localization of S. cerevisiae Ach1p to mitochondria, so the claim should be retained. Supporting Evidence: PMID:12606555 By immunofluorescence microscopy, we show that Ach1p and acetyl-CoA binding site-mutated constructs, but not its N-terminal deleted construct, are localized in mitochondria. |
| GO:0006083 acetate metabolic process | IBA GO_REF:0000033 | ACCEPT | Summary: PTN000484586 correctly propagates acetate metabolism to Neurospora acu-8. Reason: The process assertion matches target-specific evidence: Neurospora acu-8 was defined by an acetate-utilization phenotype, with acetate-sensitive mutant growth and defective acetyl-CoA hydrolase activity in acetate-grown cultures. Because acu-8 itself executes the acetyl-CoA/acetate interconversion reaction, this is participation in acetate metabolism rather than a substrate or upstream necessity effect. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000484586 SUPPORTS TRANSFER The PAINT node carries the acetate-metabolism assertion on the same fungal Ach1 branch as the acetate CoA-transferase activity. Supporting Evidence: PMID:1357077 An acu-8 mutant strain, previously characterized as acetate non-utilizing, shows strong growth-inhibition by acetate, but will use it as carbon source at low concentrations. PMID:19298859 Saccharomyces cerevisiae and Neurospora crassa mutants defective in the so-called acetyl-CoA hydrolases Ach1p and Acu-8, respectively, display a severe growth defect on acetate, which is most strongly pronounced under acidic conditions. |
| GO:0006083 acetate metabolic process | IEA GO_REF:0000002 | ACCEPT | Summary: The InterPro family mapping to acetate metabolic process is supported by Neurospora acu-8 mutant data. Reason: The IPR046433 electronic process call is appropriate for P15937 because Neurospora acu-8 mutants are acetate sensitive and deficient in the enzyme linking acetate and acetyl-CoA metabolism. Supporting Evidence: PMID:1357077 An acu-8 mutant strain, previously characterized as acetate non-utilizing, shows strong growth-inhibition by acetate, but will use it as carbon source at low concentrations. |
| GO:0008410 CoA-transferase activity | IEA GO_REF:0000002 | TOO GENERAL | Summary: CoA-transferase activity is true but redundant with the accepted acetate CoA-transferase activity annotation. Reason: The fungal Ach1/Acu-8 family supports acetate as the physiologic acceptor for succinyl-CoA-dependent CoASH transfer. Because GO:0008775 acetate CoA-transferase activity is accepted in this same review, the parent GO:0008410 CoA-transferase activity row is correct but uninformative. Supporting Evidence: PMID:19298859 Ach1p showed highest specific activity for the CoASH transfer from succinyl-CoA to acetate and only a minor acetyl-CoA-hydrolase activity. |
| GO:0008775 acetate CoA-transferase activity | IBA GO_REF:0000033 | ACCEPT | Summary: PTN000484586 correctly propagates acetate CoA-transferase activity to Neurospora acu-8. Reason: The IBA is placed at the same fungal Ach1 node that carries the older acetyl-CoA hydrolase and acetate-metabolism assertions. Re-characterization of S. cerevisiae Ach1p showed highest activity for CoASH transfer from succinyl-CoA to acetate, and there is no acu-8-specific evidence of loss or divergence from this family-level CoA-transferase activity. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000484586 SUPPORTS TRANSFER PTN000484586 captures the conserved fungal Ach1 acetate CoA-transferase activity inherited by acu-8. Supporting Evidence: PMID:19298859 Complementation of an ach1 mutant with the coaT gene reversed the growth defect on acetate confirming the in vivo function of Ach1p as a CoA-transferase. |
| GO:0008775 acetate CoA-transferase activity | IEA GO_REF:0000002 | ACCEPT | Summary: The InterPro IPR046433 mapping to acetate CoA-transferase activity agrees with the PTN000484586 PAINT placement. Reason: IPR046433 marks the fungal Ach1/CoA-transferase family, and the more curated PAINT propagation on PTN000484586 assigns the same specific GO:0008775 activity to acu-8. S. cerevisiae Ach1p biochemistry supports this specificity. Supporting Evidence: PMID:19298859 Ach1p showed highest specific activity for the CoASH transfer from succinyl-CoA to acetate and only a minor acetyl-CoA-hydrolase activity. |
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