AceF (E2p) is the dihydrolipoyllysine-residue acetyltransferase core of the Escherichia coli pyruvate dehydrogenase complex. Each chain carries three N-terminal lipoyl domains, a peripheral subunit-binding domain that docks E1p (AceE) and E3 (LpdA), and a C-terminal catalytic domain whose 24 copies assemble into the octahedral inner core. The lipoyl arms shuttle the acetyl group from E1p to the acetyltransferase site, where it is transferred to coenzyme A to form acetyl-CoA, and then carry reducing equivalents to E3 for reoxidation.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004742 dihydrolipoyllysine-residue acetyltransferase activity | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA for the E2p acetyltransferase activity, grounded in AceF itself. Reason: The PAINT node is seeded by E. coli AceF's own experimental annotation; consistent with the IDA row. Supporting Evidence: PMID:12651118 The purified 1-lip E2 and E3 proteins were functionally active according to the overall PDHc activity measurement. file:ECOLI/aceF/aceF-uniprot.txt DR NCBIfam; TIGR01348; PDHac_trf_long; 1. |
| GO:0004742 dihydrolipoyllysine-residue acetyltransferase activity | IDA PMID:12651118 Expression and purification of the dihydrolipoamide acetyltr... | ACCEPT | Summary: Recombinant E2p is catalytically active in the reconstituted PDH complex. Reason: Purified recombinant E2p supports overall PDHc activity and its lipoyl domain is reductively acetylated by E1 and pyruvate, the acetyl donor for the E2p acetyltransferase reaction. Supporting Evidence: PMID:12651118 The purified 1-lip E2 and E3 proteins were functionally active according to the overall PDHc activity measurement. |
| GO:0004742 dihydrolipoyllysine-residue acetyltransferase activity | IEA GO_REF:0000120 | ACCEPT | Summary: EC/Rhea-based mapping to the exact E2p reaction. Reason: Consistent with the IDA and IBA rows; AceF carries the PDH-specific acetyltransferase signature. Supporting Evidence: file:ECOLI/aceF/aceF-uniprot.txt DR InterPro; IPR006256; AcTrfase_Pyrv_DH_cplx. |
| GO:0005515 protein binding | IPI PMID:15690043 Interaction network containing conserved and essential prote... | REMOVE | Summary: High-throughput affinity-purification row to bare protein binding. Reason: Bare GO:0005515 from a large-scale affinity-purification screen is uninformative under the protein-binding policy; the partners are not PDH complex subunits. Supporting Evidence: PMID:15690043 were tagged successfully, whereas 648 could be purified to homogeneity and their interacting protein partners identified by mass spectrometry. |
| GO:0005515 protein binding | IPI PMID:15690043 Interaction network containing conserved and essential prote... | REMOVE | Summary: High-throughput affinity-purification row to bare protein binding. Reason: Bare GO:0005515 from a large-scale affinity-purification screen is uninformative under the protein-binding policy; the partners are not PDH complex subunits. Supporting Evidence: PMID:15690043 were tagged successfully, whereas 648 could be purified to homogeneity and their interacting protein partners identified by mass spectrometry. |
| GO:0005515 protein binding | IPI PMID:15690043 Interaction network containing conserved and essential prote... | REMOVE | Summary: High-throughput affinity-purification row to bare protein binding. Reason: Bare GO:0005515 from a large-scale affinity-purification screen is uninformative under the protein-binding policy; the partners are not PDH complex subunits. Supporting Evidence: PMID:15690043 were tagged successfully, whereas 648 could be purified to homogeneity and their interacting protein partners identified by mass spectrometry. |
| GO:0005515 protein binding | IPI PMID:15690043 Interaction network containing conserved and essential prote... | REMOVE | Summary: High-throughput affinity-purification row to bare protein binding. Reason: Bare GO:0005515 from a large-scale affinity-purification screen is uninformative under the protein-binding policy; the partners are not PDH complex subunits. Supporting Evidence: PMID:15690043 were tagged successfully, whereas 648 could be purified to homogeneity and their interacting protein partners identified by mass spectrometry. |
| GO:0005515 protein binding | IPI PMID:15690043 Interaction network containing conserved and essential prote... | REMOVE | Summary: High-throughput affinity-purification row to bare protein binding. Reason: Bare GO:0005515 from a large-scale affinity-purification screen is uninformative under the protein-binding policy; the partners are not PDH complex subunits. Supporting Evidence: PMID:15690043 were tagged successfully, whereas 648 could be purified to homogeneity and their interacting protein partners identified by mass spectrometry. |
| GO:0005515 protein binding | IPI PMID:15690043 Interaction network containing conserved and essential prote... | REMOVE | Summary: High-throughput affinity-purification row to bare protein binding. Reason: Bare GO:0005515 from a large-scale affinity-purification screen is uninformative under the protein-binding policy; the partners are not PDH complex subunits. Supporting Evidence: PMID:15690043 were tagged successfully, whereas 648 could be purified to homogeneity and their interacting protein partners identified by mass spectrometry. |
| GO:0005515 protein binding | IPI PMID:15690043 Interaction network containing conserved and essential prote... | REMOVE | Summary: High-throughput affinity-purification row to bare protein binding. Reason: Bare GO:0005515 from a large-scale affinity-purification screen is uninformative under the protein-binding policy; the partners are not PDH complex subunits. Supporting Evidence: PMID:15690043 were tagged successfully, whereas 648 could be purified to homogeneity and their interacting protein partners identified by mass spectrometry. |
| GO:0005515 protein binding | IPI PMID:15690043 Interaction network containing conserved and essential prote... | REMOVE | Summary: High-throughput affinity-purification row to bare protein binding. Reason: Bare GO:0005515 from a large-scale affinity-purification screen is uninformative under the protein-binding policy; the partners are not PDH complex subunits. Supporting Evidence: PMID:15690043 were tagged successfully, whereas 648 could be purified to homogeneity and their interacting protein partners identified by mass spectrometry. |
| GO:0005515 protein binding | IPI PMID:16606699 Large-scale identification of protein-protein interaction of... | REMOVE | Summary: High-throughput pull-down row to bare protein binding (LpdA). Reason: LpdA is the physiological E3 partner in the PDH complex, but bare protein binding is uninformative; the partnership is captured by the complex membership and the E2p acetyltransferase function. Supporting Evidence: PMID:16606699 Proteins copurifying with hexahistidine-tagged baits on a Ni2+-NTA column were identified by MALDI-TOF MS |
| GO:0005515 protein binding | IPI PMID:16858726 A complexomic study of Escherichia coli using two-dimensiona... | REMOVE | Summary: Complexome row to bare protein binding (LpdA). Reason: Co-migration with LpdA reflects PDH complex membership, already captured by GO:0045254; bare protein binding is uninformative. Supporting Evidence: PMID:16858726 Then, the different partners of each protein complex were identified by LC-MS/MS. |
| GO:0005515 protein binding | IPI PMID:24561554 The binary protein-protein interaction landscape of Escheric... | REMOVE | Summary: Yeast two-hybrid row to bare protein binding (LpdA). Reason: The E2p-E3 interaction is real but is captured by PDH complex membership; bare protein binding is uninformative. Supporting Evidence: PMID:24561554 Here we performed yeast two-hybrid screens of 3,305 baits against 3,606 preys |
| GO:0005737 cytoplasm | HDA PMID:16858726 A complexomic study of Escherichia coli using two-dimensiona... | MODIFY | Summary: Cytoplasmic location of the soluble PDH core; cytosol is the specific location. Reason: Correct but general: the complexome separated cytosolic complexes, and the soluble PDH complex is cytosolic; GO:0005829 cytosol is the specific descendant of cytoplasm. Proposed replacements: cytosol Supporting Evidence: PMID:16858726 the cytosolic and membrane protein complexes of Escherichia coli were separated. |
| GO:0005737 cytoplasm | IDA PMID:16858726 A complexomic study of Escherichia coli using two-dimensiona... | MODIFY | Summary: Cytoplasmic location of the soluble PDH core; cytosol is the specific location. Reason: Correct but general: the complexome separated cytosolic complexes, and the soluble PDH complex is cytosolic; GO:0005829 cytosol is the specific descendant of cytoplasm. Proposed replacements: cytosol Supporting Evidence: PMID:16858726 the cytosolic and membrane protein complexes of Escherichia coli were separated. |
| GO:0006086 pyruvate decarboxylation to acetyl-CoA | IBA GO_REF:0000033 | ACCEPT | Summary: AceF participates in pyruvate decarboxylation to acetyl-CoA (PAINT). Reason: E2p catalyses the acetyl-CoA forming step of the PDH reaction. Supporting Evidence: file:ECOLI/aceF/aceF-uniprot.txt The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). |
| GO:0006086 pyruvate decarboxylation to acetyl-CoA | IMP PMID:349114 Biochemical genetics of the alpha-keto acid dehydrogenase co... | ACCEPT | Summary: ace deletion mutants lack PDH activity and require acetate. Reason: Deletions removing aceE/aceF abolish the PDH complex and impose an acetate requirement, the expected phenotype for loss of pyruvate-to-acetyl-CoA conversion. Supporting Evidence: PMID:349114 It was concluded that 10 out of 15 deletions generating a strict requirement for acetate terminated in the aceE gene. PMID:349114 Five deletions appeared to extend into the aceF gene. |
| GO:0016746 acyltransferase activity | IEA GO_REF:0000002 | MODIFY | Summary: Acyltransferase activity is a correct but general parent of the E2p activity. Reason: Correct but general: GO:0004742 dihydrolipoyllysine-residue acetyltransferase activity, already on this gene by IDA, is the specific descendant supported by the 2-oxoacid dehydrogenase acyltransferase domain behind this row. Proposed replacements: dihydrolipoyllysine-residue acetyltransferase activity Supporting Evidence: file:ECOLI/aceF/aceF-uniprot.txt DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase. |
| GO:0031405 lipoic acid binding | IDA PMID:12651118 Expression and purification of the dihydrolipoamide acetyltr... | KEEP AS NON CORE | Summary: E2p lipoyl domains carry covalently attached lipoate that is acetylated during catalysis. Reason: Lipoyl-domain cofactor binding is shown directly (the lipoyl domain is acetylated by E1 and pyruvate) but is a cofactor property of the acetyltransferase function rather than a separate role. Supporting Evidence: PMID:12651118 The lipoyl domain was fully acetylated after just 30 s of incubation with E1 and pyruvate. file:ECOLI/aceF/aceF-uniprot.txt Note=Binds 3 lipoyl cofactors covalently.; |
| GO:0042867 pyruvate catabolic process | NAS PMID:3903169 Genetic reconstruction and functional analysis of the repeat... | MODIFY | Summary: Pyruvate catabolism is correct but the PDH-specific process is more informative. Reason: AceF performs the acetyl-CoA forming step of pyruvate oxidation; GO:0006086 pyruvate decarboxylation to acetyl-CoA, already on this gene (IBA, IMP), names the process exactly. GO does not place it under GO:0042867, so this is a lateral refinement, as for AceE. Proposed replacements: pyruvate decarboxylation to acetyl-CoA Supporting Evidence: PMID:3903169 It was found that the overall catalytic activity, the system of active site coupling, and the ability to complement pyruvate dehydrogenase complex mutants |
| GO:0045254 pyruvate dehydrogenase complex | IBA GO_REF:0000033 | ACCEPT | Summary: AceF is the E2p core of the PDH complex (PAINT). Reason: Consistent with the direct complex evidence; E2p forms the octahedral core of the complex. Supporting Evidence: PMID:3903169 aggregates to form the octahedral inner core of the complex and also contains the acetyltransferase active site. |
| GO:0045254 pyruvate dehydrogenase complex | IDA PMID:329143 Self-assembly and catalytic activity of the pyruvate dehydro... | ACCEPT | Summary: Classic self-assembly study of the E. coli PDH complex. Reason: The cached record lacks an abstract, but the claim (AceF is a PDH complex subunit) is independently supported by direct complex evidence, so the curator's annotation is accepted. Supporting Evidence: PMID:3903169 Pyruvate dehydrogenase complexes incorporating these genetically reconstructed E2p components were purified and their structures were confirmed. |
| GO:0045254 pyruvate dehydrogenase complex | IDA PMID:3903169 Genetic reconstruction and functional analysis of the repeat... | ACCEPT | Summary: Purified PDH complexes containing engineered E2p. Reason: Complexes incorporating genetically reconstructed E2p were purified and structurally confirmed. Supporting Evidence: PMID:3903169 Pyruvate dehydrogenase complexes incorporating these genetically reconstructed E2p components were purified and their structures were confirmed. |
| GO:0045254 pyruvate dehydrogenase complex | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro PDH-complex E2 signature mapping to the complex. Reason: Consistent with the direct complex evidence for AceF. Supporting Evidence: file:ECOLI/aceF/aceF-uniprot.txt DR InterPro; IPR006256; AcTrfase_Pyrv_DH_cplx. |
| GO:0045254 pyruvate dehydrogenase complex | IGI PMID:327021 Biochemical genetics of the alpha-keto acid dehydrogenase co... | ACCEPT | Summary: Genetic interaction of ace and lpd deletions defines the PDH complex components. Reason: Deletion mutants spanning aceE-aceF-lpd lose PDH complex activity, consistent with AceF as a complex subunit. Supporting Evidence: PMID:327021 Enzymological studies showed that the 15 Ace- or Nad-Ace- strains all lacked the pyruvate dehydrogenase complex and pyruvate dehydrogenase (EIp) activities and only three retained detectable dihydrolipoamide acetyltransferase (E2p). |
| GO:0045254 pyruvate dehydrogenase complex | NAS PMID:3903169 Genetic reconstruction and functional analysis of the repeat... | ACCEPT | Summary: E2p is the lipoyl-domain core of the PDH complex. Reason: The paper reconstructs E2p lipoyl domains in purified PDH complexes. Supporting Evidence: PMID:3903169 The dihydrolipoamide acetyltransferase component (E2p) of the pyruvate dehydrogenase complex of Escherichia coli contains three highly homologous sequences of about 100 residues |
| GO:0097532 stress response to acid chemical | IMP PMID:38466471 Genome-Wide Screens Identify Genes Responsible for Intrinsic... | MARK AS OVER ANNOTATED | Summary: Boric-acid sensitivity of an aceF knockout is an indirect metabolic phenotype. Reason: The Keio screen found ΞaceF sensitive to boric acid among 92 hits spanning unrelated pathways; loss of PDH activity plausibly weakens general fitness, but AceF performs no step of an acid stress response. Supporting Evidence: PMID:38466471 This study demonstrates that intrinsic BA resistance is the result of various mechanisms acting together. |
Loading supporting contentβ¦
Download this section (compressed HTML)Q: Why does E. coli E2p retain three lipoyl domains per chain when complexes with one or two lipoyl domains show near-normal overall activity?
Experiment: Compare growth yield and acetyl-CoA flux of aceF strains encoding one, two or three lipoyl domains under fluctuating pyruvate supply to test whether extra lipoyl domains confer a fitness advantage not seen in steady-state enzyme assays.
Type: competitive growth and metabolic flux analysis
Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)