Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Combined Automated Annotation using Multiple IEA Methods
Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli.
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Ahp (AhpCF) provides the H2O2-scavenging activity that persists in catalase-null mutants; Ahp catalase triple mutants cannot scavenge H2O2.
"Thus, Ahp provides the scavenging activity that persists in catalase null mutants."
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Ahp turnover depends on NADH supply, so catalase dominates at high H2O2 concentrations.
"This arrangement is reasonable because the cell cannot provide enough NADH for Ahp to rapidly degrade large amounts of H 2 O 2 ."
Proteomic analysis of thioredoxin-targeted proteins in Escherichia coli.
Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth.
A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis.
Protein abundance profiling of the Escherichia coli cytosol.
The protein-free IANUS peptide array uncovers interaction sites between Escherichia coli parvulin 10 and alkyl hydroperoxide reductase.
AhpC is required for optimal production of enterobactin by Escherichia coli.
The binary protein-protein interaction landscape of Escherichia coli.
Structure, mechanism and ensemble formation of the alkylhydroperoxide reductase subunits AhpC and AhpF from Escherichia coli.
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EcAhpC forms a decameric ring that binds AhpF.
"conformation, while that of EcAhpC (3.3 Å resolution) forms a decameric ring."
An alkyl hydroperoxide reductase induced by oxidative stress in Salmonella typhimurium and Escherichia coli: genetic characterization and cloning of ahp.
Essential role of the flexible linker on the conformational equilibrium of bacterial peroxiredoxin reductase for effective regeneration of peroxiredoxin.
Selective enrichment tandem β-elimination assisted strategy for N-phosphorylation analysis.
Thioredoxin-linked "thiol peroxidase" from periplasmic space of Escherichia coli.
Cloning of an organic solvent-resistance gene in Escherichia coli: the unexpected role of alkylhydroperoxide reductase.
Mammalian antioxidant protein complements alkylhydroperoxide reductase (ahpC) mutation in Escherichia coli.
Analysis of global responses by protein and peptide fingerprinting of proteins isolated by two-dimensional gel electrophoresis. Application to the sulfate-starvation response of Escherichia coli.
UniProt record for Escherichia coli K-12 ahpC (P0AE08)
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Curated function, catalytic activity (EC 1.11.1.26, PubMed:11717276), decameric subunit structure and Cys47-Cys166 interchain disulfide.
AhpC Is Required for Optimal Production of Enterobactin by Escherichia coli
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A resolving-cysteine variant retains peroxide resistance but fails to restore growth under iron limitation, separating the iron phenotype from peroxide-scavenging activity.
"the peroxidase activity of AhpC is not sufficient for AhpC to participate in cellular iron metabolism."
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The authors consider direct or indirect FMN reduction for chorismate synthesis as a hypothesis, without demonstrating that reaction.
"AhpC may participate in the reduction of FMN for chorismate synthesis, either directly or indirectly."