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Information on EC 2.3.1.286 - protein acetyllysine N-acetyltransferase and Organism(s) Escherichia coli and UniProt Accession P09163

for references in articles please use BRENDA:EC2.3.1.286
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EC Tree
IUBMB Comments
The enzyme, found in all domains of life, is involved in gene regulation by deacetylating proteins. Some of the 2''-O-acetyl-ADP-D-ribose converts non-enzymically to 3''-O-acetyl-ADP-D-ribose.
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This record set is specific for:
Escherichia coli
UNIPROT: P09163
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
sirt1, sirt3, sirtuin, sirt2, sirtuin 1, sirtuin 3, sir2p, silent information regulator 2, sir2alpha, nad-dependent histone deacetylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
peptidyl-lysine N-acetyltransferase
UniProt
protein lysine acetyltransferase
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NAD+-dependent protein deacetylase
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peptidyl-lysine N-acetyltransferase
UniProt
protein lysine acetyltransferase
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protein lysine deacetylase
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additional information
cf. EC 2.3.1.380
PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
[protein]-N6-acetyl-L-lysine:NAD+ N-acetyltransferase (NAD+-hydrolysing; 2''-O-acetyl-ADP-D-ribose-forming)
The enzyme, found in all domains of life, is involved in gene regulation by deacetylating proteins. Some of the 2''-O-acetyl-ADP-D-ribose converts non-enzymically to 3''-O-acetyl-ADP-D-ribose.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
show the reaction diagram
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-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
show the reaction diagram
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-
?
[Acs protein]-N6-acetyl-L-lysine609 + NAD+ + H2O
[Acs protein]-L-lysine609 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
show the reaction diagram
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-
-
?
[histone H4]-N6-acetyl-L-lysine16 + NAD+ + H2O
[histone H4]-L-lysine16 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
show the reaction diagram
KGGAAc-KRHRKIL
-
-
?
[p53 peptide]-N6-acetyl-L-lysine382 + NAD+ + H2O
[p53 peptide]-L-lysine382 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
show the reaction diagram
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-
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?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
show the reaction diagram
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
show the reaction diagram
-
-
-
?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
the small domain contains a structural zinc ion
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
YjaB is a member of the Gcn5-related N-acetyltransferase (GNAT) family. GNATs acetylate a broad range of substrates, including antibiotics, polyamines, amino acids, nucleotides, tRNAs, proteins, and peptides
physiological function
Nepsilon-lysine acetyltransferases (KATs) specifically transfer an acetyl group from AcCoA to Nepsilon-lysine residues on proteins. Posttranslational modifications, such as Nepsilon-lysine acetylation, regulate protein function. The enzymes show a high degree of substrate specificity
evolution
physiological function
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native and selenomethionine-derivatized enzyme in complex with an 11-residue peptide containing residues 12-19 of histone H4 and acetylated at lysine 16, hanging drop vapor diffusion method, using
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y117A
site-directed mutagenesis, mutation of the conserved catalytic amino acid reduces YjaB-dependent acetylation compared to wild-type
Y117F
site-directed mutagenesis, mutation of the conserved catalytic amino acid does not alter YjaB-dependent acetylation compared to wild-type
E78A
site-directed mutagenesis, mutation of the conserved catalytic amino acid prevents PhnO-dependent acetylation
F70A
site-directed mutagenesis, mutation of the conserved catalytic amino acid reduces YiaC-dependent acetylation compared to wild-type. Overexpression of YiaC YF70A inhibits cell migration similarly to overexpression of wild-type YiaC
Y115A
site-directed mutagenesis, mutation of the conserved catalytic amino acid prevents YiaC-dependent acetylation. Mutant YiaC Y115A is unable to inhibit cell migration in contrast to the wild-type enzyme
Y128A
site-directed mutagenesis, mutation of the conserved catalytic amino acid prevents PhnO-dependent acetylation
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Q-Sepharose column chromatography and Superdex 75 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene yjaB, sequence comparisons and phylogenetic analysis, recombinant enzyme overexpression of wild-type and mutant enzymes in Escherichia coli strain BW25113
expressed in Escherichia coli BL21(DE3) and B834 (DE3) cells
gene patZ, sequence comparisons and phylogenetic analysis, recombinant enzyme overexpression in Escherichia coli strain BW25113
gene phnO, sequence comparisons and phylogenetic analysis, recombinant enzyme overexpression of wild-type and mutant enzymes in Escherichia coli strain BW25113
gene yiaC, sequence comparisons and phylogenetic analysis, recombinant enzyme overexpression of wild-type and mutant enzymes in Escherichia coli strain BW25113
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhao, K.; Chai, X.; Marmorstein, R.
Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Escherichia coli
J. Mol. Biol.
337
731-741
2004
Escherichia coli (P75960), Escherichia coli
Manually annotated by BRENDA team
Christensen, D.G.; Meyer, J.G.; Baumgartner, J.T.; DSouza, A.K.; Nelson, W.C.; Payne, S.H.; Kuhn, M.L.; Schilling, B.; Wolfe, A.J.
Identification of novel protein lysine acetyltransferases in Escherichia coli
mBio
9
e01905-18
2018
Escherichia coli (P09163), Escherichia coli (P16691), Escherichia coli (P37664), Escherichia coli (P76594)
Manually annotated by BRENDA team