aceE

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0000287 magnesium ion binding	IDA PMID:11955070 Structure of the pyruvate dehydrogenase multienzyme complex ...	KEEP AS NON CORE	Summary: Mg2+ is the divalent cation that anchors ThDP in E1p. Reason: UniProt records Mg2+ as an E1p cofactor and the IDA row comes from the E1p crystal structure; metal binding is a cofactor property of the catalytic activity, not an independent function. Supporting Evidence: file:ECOLI/aceE/aceE-uniprot.txt Name=Mg(2+); Xref=ChEBI:CHEBI:18420; PMID:11955070 there is a common ThDP binding fold
GO:0000287 magnesium ion binding	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: Mg2+ binding as a ThDP-enzyme cofactor; consistent with the IDA row. Reason: Same claim as the structural IDA row (Mg2+ cofactor of a ThDP enzyme); kept non-core for consistency. Supporting Evidence: file:ECOLI/aceE/aceE-uniprot.txt Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
GO:0004739 pyruvate dehydrogenase (acetyl-transferring) activity	IEA GO_REF:0000120	ACCEPT	Summary: Exact E1p catalytic activity of the PDH complex. Reason: AceE is the experimentally characterised ThDP-dependent E1 of the E. coli PDH complex; kinetic and structural work shows it performs pyruvate decarboxylation and reductive acetylation of the E2p lipoyl domains, which is exactly EC 1.2.4.1 / RHEA:19189. Supporting Evidence: PMID:17635929 We showed that residue His-407 on the inner loop has a key role in the mechanism, especially in the reductive acetylation of the E. coli dihydrolipoamide transacetylase component file:ECOLI/aceE/aceE-uniprot.txt DR NCBIfam; TIGR00759; aceE; 1.
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 (e.g. GroEL, FtsK, PurB) are not PDH complex subunits and identify no AceE function. 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 (e.g. GroEL, FtsK, PurB) are not PDH complex subunits and identify no AceE function. 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 (e.g. GroEL, FtsK, PurB) are not PDH complex subunits and identify no AceE function. 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 (e.g. GroEL, FtsK, PurB) are not PDH complex subunits and identify no AceE function. 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 (e.g. GroEL, FtsK, PurB) are not PDH complex subunits and identify no AceE function. 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 (e.g. GroEL, FtsK, PurB) are not PDH complex subunits and identify no AceE function. 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 (e.g. GroEL, FtsK, PurB) are not PDH complex subunits and identify no AceE function. 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 (e.g. GroEL, FtsK, PurB) are not PDH complex subunits and identify no AceE function. 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 (e.g. GroEL, FtsK, PurB) are not PDH complex subunits and identify no AceE function. 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 (e.g. GroEL, FtsK, PurB) are not PDH complex subunits and identify no AceE function. 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 (e.g. GroEL, FtsK, PurB) are not PDH complex subunits and identify no AceE function. 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 (e.g. GroEL, FtsK, PurB) are not PDH complex subunits and identify no AceE function. 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 (e.g. GroEL, FtsK, PurB) are not PDH complex subunits and identify no AceE function. 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 (e.g. GroEL, FtsK, PurB) are not PDH complex subunits and identify no AceE function. 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 (GroEL). Reason: Bare GO:0005515 from a genome-wide His-tag pull-down; co-purification with the GroEL chaperonin identifies no AceE function. Supporting Evidence: PMID:16606699 Proteins copurifying with hexahistidine-tagged baits on a Ni2+-NTA column were identified by MALDI-TOF MS
GO:0005829 cytosol	HDA PMID:16858726 A complexomic study of Escherichia coli using two-dimensiona...	ACCEPT	Summary: E1p is a soluble cytosolic enzyme. Reason: The complexome study separated cytosolic protein complexes and the PDH complex is a soluble cytosolic assembly in E. coli; this is where the core activity acts. Supporting Evidence: PMID:16858726 the cytosolic and membrane protein complexes of Escherichia coli were separated.
GO:0016020 membrane	HDA PMID:16858726 A complexomic study of Escherichia coli using two-dimensiona...	MARK AS OVER ANNOTATED	Summary: Membrane detection in a fractionation screen is not a demonstrated location of E1p. Reason: The PDH complex is a large soluble assembly; recovery of E1p in a high-throughput membrane complex fraction most likely reflects co-sedimentation of the megadalton complex rather than membrane residence, and no targeted study places AceE in a membrane. Supporting Evidence: PMID:16858726 the cytosolic and membrane protein complexes of Escherichia coli were separated.
GO:0016491 oxidoreductase activity	IEA GO_REF:0000002	MODIFY	Summary: Oxidoreductase activity is a correct but uninformative parent of the E1p activity. Reason: Correct but general: E1p is an oxidoreductase (EC 1.2.4.1), and GO:0004739 pyruvate dehydrogenase (acetyl-transferring) activity, already on this gene, is the specific descendant supported by the InterPro PDH_E1 signature behind this row. Proposed replacements: pyruvate dehydrogenase (acetyl-transferring) activity Supporting Evidence: file:ECOLI/aceE/aceE-uniprot.txt DR InterPro; IPR004660; PDH_E1.
GO:0030976 thiamine pyrophosphate binding	IDA PMID:11955070 Structure of the pyruvate dehydrogenase multienzyme complex ...	KEEP AS NON CORE	Summary: E1p binds its thiamine diphosphate cofactor at the dimer interface. Reason: ThDP binding is directly shown by the crystal structure and is required for catalysis, but it is a cofactor-binding property subsumed by the E1p catalytic activity rather than a separate core function. Supporting Evidence: PMID:11955070 The ThDP cofactors are bound in the "V" conformation in clefts between the two subunits
GO:0036094 small molecule binding	EXP PMID:16531404 A thiamin-bound, pre-decarboxylation reaction intermediate a...	MODIFY	Summary: Small molecule binding reflects binding of ThDP and a ThDP-bound substrate analogue. Reason: Correct but general: the experiments show binding of ThDP and of the ThDP-bound pre-decarboxylation intermediate analogue PLThDP; GO:0030976 thiamine pyrophosphate binding, already on this gene, is the specific descendant. Proposed replacements: thiamine pyrophosphate binding Supporting Evidence: PMID:16531404 The crystal structure of the E1 component from the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDHc) has been determined with phosphonolactylthiamin diphosphate (PLThDP) in its active site. PMID:17635929 become organized only on binding a substrate analog that is capable of forming a stable thiamin diphosphate-bound covalent intermediate
GO:0036094 small molecule binding	EXP PMID:17635929 A dynamic loop at the active center of the Escherichia coli ...	MODIFY	Summary: Small molecule binding reflects binding of ThDP and a ThDP-bound substrate analogue. Reason: Correct but general: the experiments show binding of ThDP and of the ThDP-bound pre-decarboxylation intermediate analogue PLThDP; GO:0030976 thiamine pyrophosphate binding, already on this gene, is the specific descendant. Proposed replacements: thiamine pyrophosphate binding Supporting Evidence: PMID:16531404 The crystal structure of the E1 component from the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDHc) has been determined with phosphonolactylthiamin diphosphate (PLThDP) in its active site. PMID:17635929 become organized only on binding a substrate analog that is capable of forming a stable thiamin diphosphate-bound covalent intermediate
GO:0042802 identical protein binding	IPI PMID:16858726 A complexomic study of Escherichia coli using two-dimensiona...	MODIFY	Summary: Identical protein binding from a complexome screen reflects the E1p homodimer. Reason: Correct but general: GO:0042803 protein homodimerization activity, already on this gene from the crystal structure, is the specific descendant of identical protein binding. Proposed replacements: protein homodimerization activity Supporting Evidence: PMID:16858726 Among these protein complexes, 50 heteromultimeric and 256 homomultimeric protein complexes were found. PMID:11955070 The E. coli PDHc E1 component E1p is a homodimeric enzyme
GO:0042803 protein homodimerization activity	IDA PMID:11955070 Structure of the pyruvate dehydrogenase multienzyme complex ...	KEEP AS NON CORE	Summary: E1p is a homodimer. Reason: The crystal structure shows the functional homodimer with shared active sites; dimerisation is structural context for the catalytic activity. Supporting Evidence: PMID:11955070 The E. coli PDHc E1 component E1p is a homodimeric enzyme and crystallizes with an intact dimer in an asymmetric unit.
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: AceE initiates oxidative decarboxylation of pyruvate to acetyl-CoA. GO:0006086 pyruvate decarboxylation to acetyl-CoA names that process exactly; GO does not place it under GO:0042867, so this is a lateral refinement to the precise process rather than a descendant swap. Proposed replacements: pyruvate decarboxylation to acetyl-CoA Supporting Evidence: file:ECOLI/aceE/aceE-uniprot.txt catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). 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	NAS PMID:3903169 Genetic reconstruction and functional analysis of the repeat...	ACCEPT	Summary: AceE is the E1 subunit of the PDH complex. Reason: Purified E. coli PDH complexes contain E1p bound around the E2p core with E3; the E1p structure paper and UniProt subunit annotation describe AceE as the PDH E1 component. Supporting Evidence: file:ECOLI/aceE/aceE-uniprot.txt Part of the PDH complex, consisting of multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (Probable). PMID:3903169 Pyruvate dehydrogenase complexes incorporating these genetically reconstructed E2p components were purified and their structures were confirmed.
GO:0060090 molecular adaptor activity	EXP PMID:11955070 Structure of the pyruvate dehydrogenase multienzyme complex ...	MARK AS OVER ANNOTATED	Summary: Molecular adaptor activity does not describe the catalytic E1p subunit. Reason: GO:0060090 is a binding activity that brings molecules together without catalysis. The cited structure describes a catalytic homodimeric E1 whose binding to E2p serves its own reaction (reductive acetylation of the E2p lipoyl domains), so E2p binding is part of the E1p catalytic activity rather than an adaptor function. The cached paper is abstract-only, so the row is flagged rather than removed. Supporting Evidence: PMID:11955070 These differences may be responsible for reported alternative E1p binding modes to E2 components within the respective complexes.

Gene Description

Existing Annotations Review

Core Functions

Thiamine diphosphate-dependent E1 activity that decarboxylates pyruvate and reductively acetylates the lipoyl domains of the E2p (AceF) core within the pyruvate dehydrogenase complex.

References

Suggested Questions for Experts

Suggested Experiments

📚 Additional Documentation

Notes

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