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Literature summary extracted from

  • Zhang, H.; Xu, X.
    Protein acetylation an important mechanism in actinobacteria (2018), Biosci. Rep., 38, BSR20170851 .
    View publication on PubMedView publication on EuropePMC

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.48 Actinosynnema mirum
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2.3.1.48 Actinosynnema mirum DSM 43827
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2.3.1.48 Streptomyces venezuelae
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2.3.1.48 Streptomyces venezuelae DSM 40230
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Synonyms

EC Number Synonyms Comment Organism
2.3.1.48 AAPatA
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 Streptomyces venezuelae
2.3.1.48 AAPatA
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 Actinosynnema mirum
2.3.1.48 amino acid sensing acetyltransferase
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 Streptomyces venezuelae
2.3.1.48 amino acid sensing acetyltransferase
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 Actinosynnema mirum
2.3.1.48 AmiPatA
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 Actinosynnema mirum
2.3.1.48 Amir 5672
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 Actinosynnema mirum
2.3.1.48 GCN5-like acetyltransferase
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 Streptomyces venezuelae
2.3.1.48 GCN5-like acetyltransferase
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 Actinosynnema mirum
2.3.1.48 GCN5-related N-acetyltransferase
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 Streptomyces venezuelae
2.3.1.48 GCN5-related N-acetyltransferase
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 Actinosynnema mirum
2.3.1.48 GNAT
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 Streptomyces venezuelae
2.3.1.48 GNAT
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 Actinosynnema mirum
2.3.1.48 Pat
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 Streptomyces venezuelae
2.3.1.48 Pat
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 Actinosynnema mirum
2.3.1.48 protein acetyltransferase
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 Streptomyces venezuelae
2.3.1.48 protein acetyltransferase
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 Actinosynnema mirum
2.3.1.48 Sven 0867
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 Streptomyces venezuelae
2.3.1.48 SvePatA
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 Streptomyces venezuelae

General Information

EC Number General Information Comment Organism
2.3.1.48 evolution according to the allosteric ligand type of the ACT domain, members of AAPatA family are divided into two groups, the asparagine (Asn)-activated PatA and the cysteine (Cys)-activated PatA. The former exists only in Streptomyces, the latter are distributed in other actinobacteria (Pseudonocardiaceae, Micromonosporaceae, Nocardiopsaceae, and Streptosporangiaceae) Streptomyces venezuelae
2.3.1.48 evolution according to the allosteric ligand type of the ACT domain, members of AAPatA family are divided into two groups, the asparagine (Asn)-activated PatA and the cysteine (Cys)-activated PatA. The former exists only in Streptomyces, the latter are distributed in other actinobacteria (Pseudonocardiaceae, Micromonosporaceae, Nocardiopsaceae, and Streptosporangiaceae) Actinosynnema mirum
2.3.1.48 physiological function Asn is needed to regulate allosterically activity of SvePatA. Asp16 and Ser17 at the interface between beta1 and alpha1 may somehow affect the Cys binding of AmiPatA. Lys112 and Pro113 are not involved in the Asn binding of SvePatA. It is likely that the Pat enzymes are carefully regulated at the transcriptional and post-translational levels in response to changes of the intracellular signals that control the acetylation of specific proteins, which in turn mould the metabolic network. The relationship between the structure and function of SvePatA and AmiPatA showed that some amino acid residues at the interface between beta1-sheet and alpha1-helix may affect the ligand-binding activity. The archetypical acetyltransferases AAPatAs possessing GNAT and ACT domains show a novel signaling pathway for regulating the acetylation of cellular proteins. The acetylation level of proteins may be closely correlated with intracellular concentrations of Asn and Cys in Actinobacteria Streptomyces venezuelae
2.3.1.48 physiological function the activity of AmiPatA is regulated allosterically by Cys binding. It is likely that the Pat enzymes are carefully regulated at the transcriptional and post-translational levels in response to changes of the intracellular signals that control the acetylation of specific proteins, which in turn mould the metabolic network. The relationship between the structure and function of SvePatA and AmiPatA showed that some amino acid residues at the interface between beta1-sheet and alpha1-helix may affect the ligand-binding activity. The archetypical acetyltransferases AAPatAs possessing GNAT and ACT domains show a novel signaling pathway for regulating the acetylation of cellular proteins. The acetylation level of proteins may be closely correlated with intracellular concentrations of Asn and Cys in Actinobacteria Actinosynnema mirum