Literature summary for 2.3.1.48 extracted from

Zhang, H.; Xu, X.
Protein acetylation an important mechanism in actinobacteria (2018), Biosci. Rep., 38, BSR20170851 .

Search for more literature for 2.3.1.48

Organism

Organism	UniProt	Comment	Textmining
Actinosynnema mirum	-	-	-
Actinosynnema mirum DSM 43827	-	-	-
Streptomyces venezuelae	-	-	-
Streptomyces venezuelae DSM 40230	-	-	-

Synonyms

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

General Information

General Information	Comment	Organism
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
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
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
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

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Release 2023.1 (January 2023)