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Information on EC 2.3.1.254 - N-terminal methionine Nalpha-acetyltransferase NatB
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2.3.1.254 N-terminal methionine Nalpha-acetyltransferase NatBIUBMB Comments
N-terminal acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free alpha-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus and makes the N-terminal residue larger and more hydrophobic, and may also play a role in membrane targeting and gene silencing. The NatB complex is found in all eukaryotic organisms, and specifically targets N-terminal L-methionine residues attached to Asn, Asp, Gln, or Glu residues at the second position.
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Word Map
- 2.3.1.254
-
auxiliary
- tropomyosins
-
cable
-
nalpha-terminal
-
unacetylated
- met-asp
-
anti-fcepsilonri
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
hide(3 overall reactions are displayed. Show all (4)>>)
+
=
+
+
an N-terminal L-methionyl-L-asparaginyl-[protein]
=
an N-terminal Nalpha-acetyl-L-methionyl-L-asparaginyl-[protein]
+
+
=
+
+
an N-terminal L-methionyl-L-glutaminyl-[protein]
=
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein]
+
+
=
+
+
an N-terminal L-methionyl-L-aspartyl-[protein]
=
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein]
+
Synonyms
naa20, mdm20, nat3p, cra-1, naa25, mdm20p, naa50p, n-acetyltransferase 3, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 2.3.1.88
-
-
formerly, part transferred
-
MDM20
Mdm20p
N-terminal acetyltransferase
N-terminal acetyltransferase B complex catalytic subunit NAA20
NAA20
NAA25
NAT3
Nat3p
natB
NAA20
-
-
-
-
NAA25
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein] = an N-terminal Nalpha-acetyl-L-methionyl-L-asparaginyl-[protein] + CoA
(1)
-
-
-
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein] = an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
(3)
-
-
-
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein] = an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
(2)
-
-
-
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein] = an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
(4)
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:N-terminal Met-Asn/Gln/Asp/Glu-[protein] Met-Nalpha-acetyltransferase
N-terminal acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free alpha-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus and makes the N-terminal residue larger and more hydrophobic, and may also play a role in membrane targeting and gene silencing. The NatB complex is found in all eukaryotic organisms, and specifically targets N-terminal L-methionine residues attached to Asn, Asp, Gln, or Glu residues at the second position.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
acetyl-CoA + MFGPEEGGRWGRPVGRRRRRPVRVYP
CoA + N-acetyl-MFGPEEGGRWGRPVGRRRRRPVRVYP
-
-
-
-
?
acetyl-CoA + MIGPEEGGRWGRPVGRRRRRPVRVYP
CoA + N-acetyl-MIGPEEGGRWGRPVGRRRRRPVRVYP
-
-
-
-
?
acetyl-CoA + MLALISRRWGRPVGRRRRRPVRVYP
CoA + N-acetyl-MLALISRRWGRPVGRRRRRPVRVYP
-
-
-
-
?
acetyl-CoA + MLDPEEGGRWGRPVGRRRRRPVRVYP
CoA + N-acetyl-MLDPEEGGRWGRPVGRRRRRPVRVYP
-
-
-
-
?
acetyl-CoA + MLGPEGGRWGRPVGRRRRRPVRVYP
CoA + N-acetyl-MLGPEGGRWGRPVGRRRRRPVRVYP
-
-
-
-
?
acetyl-CoA + MLGTEEGGRWGRPVGRRRRRPVRVYP
CoA + N-acetyl-MLGTEEGGRWGRPVGRRRRRPVRVYP
-
-
-
-
?
acetyl-CoA + MLGTGPARWGRPVGRRRRRPVRVYP
CoA + N-acetyl-MLGTGPARWGRPVGRRRRRPVRVYP
-
-
-
-
?
acetyl-CoA + MLLPEEGGRWGRPVGRRRRRPVRVYP
CoA + N-acetyl- MLLPEEGGRWGRPVGRRRRRPVRVYP
-
-
-
-
?
acetyl-CoA + MLRPEEGGRWGRPVGRRRRRPVRVYP
CoA + N-acetyl-MLRPEEGGRWGRPVGRRRRRPVRVYP
-
-
-
-
?
acetyl-CoA + N-terminal L-methionyl-L-aspartyl-[Bax]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[Bax] + CoA
acetyl-CoA + N-terminal L-methionyl-L-glutaminyl-[influenza virus PA-X]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[influenza virus PA-X] + CoA
acetyl-CoA + N-terminal L-methionyl-L-glutaminyl-[influenza virus PA-X]
N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[influenza virus PA-X] + CoA
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
Q5AAR6; Q5AB99
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
Q5AAR6; Q5AB99
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
P61599; Q14CX7
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
P61600; Q8BWZ3
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
P61600; Q8BWZ3
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
Q06504; Q12387
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
Q06504; Q12387
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
Q5AAR6; Q5AB99
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
Q5AAR6; Q5AB99
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
P61599; Q14CX7
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
P61600; Q8BWZ3
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
P61600; Q8BWZ3
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
Q06504; Q12387
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
Q06504; Q12387
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
Q5AAR6; Q5AB99
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
Q5AAR6; Q5AB99
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
P61600; Q8BWZ3
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
P61600; Q8BWZ3
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
Q06504; Q12387
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
Q06504; Q12387
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
Q5AAR6; Q5AB99
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
Q5AAR6; Q5AB99
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
P61599; Q14CX7
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
P61600; Q8BWZ3
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
P61600; Q8BWZ3
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
Q06504; Q12387
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
Q06504; Q12387
-
-
-
?
acetyl-CoA + N-terminal L-methionyl-L-aspartyl-[Bax]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[Bax] + CoA
P61600; Q8BWZ3
heterologous expression of human Bax in mouse embryonic fibroblasts (MEFs). Recombinant human Bax is N-terminally (Nt-)acetylated by Naa20 and that Nt-acetylation of Bax is essential to maintain Bax in an inactive conformation in the cytosol of MEF cells. Human Bax displays the N-terminal Met-Asp amino-acid sequence
-
-
?
acetyl-CoA + N-terminal L-methionyl-L-aspartyl-[Bax]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[Bax] + CoA
P61600; Q8BWZ3
heterologous expression of human Bax in mouse embryonic fibroblasts (MEFs). Recombinant human Bax is N-terminally (Nt-)acetylated by Naa20 and that Nt-acetylation of Bax is essential to maintain Bax in an inactive conformation in the cytosol of MEF cells. Human Bax displays the N-terminal Met-Asp amino-acid sequence
-
-
?
acetyl-CoA + N-terminal L-methionyl-L-aspartyl-[Bax]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[Bax] + CoA
Q06504; Q12387
heterologous expression of human Bax in Saccharomyces cerevisiae. Recombinant human Bax is N-terminal (Nt-)acetylated by yNaa20p and that Nt-acetylation of Bax is essential to maintain Bax in an inactive conformation in the cytosol of yeast. Human Bax displays the N-terminal Met-Asp amino-acid sequence
-
-
?
acetyl-CoA + N-terminal L-methionyl-L-aspartyl-[Bax]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[Bax] + CoA
Q06504; Q12387
heterologous expression of human Bax in Saccharomyces cerevisiae. Recombinant human Bax is N-terminal (Nt-)acetylated by yNaa20p and that Nt-acetylation of Bax is essential to maintain Bax in an inactive conformation in the cytosol of yeast. Human Bax displays the N-terminal Met-Asp amino-acid sequence
-
-
?
acetyl-CoA + N-terminal L-methionyl-L-glutaminyl-[influenza virus PA-X]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[influenza virus PA-X] + CoA
Q06504; Q12387
-
-
-
?
acetyl-CoA + N-terminal L-methionyl-L-glutaminyl-[influenza virus PA-X]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[influenza virus PA-X] + CoA
Q06504; Q12387
-
-
-
?
acetyl-CoA + N-terminal L-methionyl-L-glutaminyl-[influenza virus PA-X]
N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[influenza virus PA-X] + CoA
P61599; Q14CX7
-
-
-
?
acetyl-CoA + N-terminal L-methionyl-L-glutaminyl-[influenza virus PA-X]
N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[influenza virus PA-X] + CoA
P61599; Q14CX7
the enzyme NatB acetylates the N-terminal amino acid of polymerase acidic proteins, especially PA-X, of influenza A virus. PA-X starts with Met-Glu. Preparation of a series of plasmids encoding PA-X mutants, which possess a NatB-permissive substitution at the second amino acid of E to D (PA-X E2D), to N (PA-X E2N), or to A (PA-X E2A), which is recognized by NatA, but not NatB, or to P (PA-X E2P)
-
-
?
additional information
?
-
Q5AAR6; Q5AB99
substrate specificity of NatB is determined by the first two amino acids of the substrate protein/peptide. The substrate's N-terminus is anchored into the NatB catalytic pocket by hydrogen bonds. The first two amino acids Met and Asp of a substrate peptide mediate the major interactions with the active site in the Naa20 subunit. The hydrogen bonds between the substrate Asp and pocket residues of Naa20 are essential to determine the NatB substrate specificity. A hydrogen bond between the amino group of the substrate Met and a carbonyl group in the Naa20 active site directly anchors the substrate toward acetyl-CoA. NatB has a unique substrate specificity different from all other NATs, which requires acidic amino acids or their amides at the second position. No activity with the NatC substrate MLRFVTANSQDNGRPVGRK and with the NatA substrate SASEAG
-
-
-
additional information
?
-
-
substrate specificity of NatB is determined by the first two amino acids of the substrate protein/peptide. The substrate's N-terminus is anchored into the NatB catalytic pocket by hydrogen bonds. The first two amino acids Met and Asp of a substrate peptide mediate the major interactions with the active site in the Naa20 subunit. The hydrogen bonds between the substrate Asp and pocket residues of Naa20 are essential to determine the NatB substrate specificity. A hydrogen bond between the amino group of the substrate Met and a carbonyl group in the Naa20 active site directly anchors the substrate toward acetyl-CoA. NatB has a unique substrate specificity different from all other NATs, which requires acidic amino acids or their amides at the second position. No activity with the NatC substrate MLRFVTANSQDNGRPVGRK and with the NatA substrate SASEAG
-
-
-
additional information
?
-
Q5AAR6; Q5AB99
substrate specificity of NatB is determined by the first two amino acids of the substrate protein/peptide. The substrate's N-terminus is anchored into the NatB catalytic pocket by hydrogen bonds. The first two amino acids Met and Asp of a substrate peptide mediate the major interactions with the active site in the Naa20 subunit. The hydrogen bonds between the substrate Asp and pocket residues of Naa20 are essential to determine the NatB substrate specificity. A hydrogen bond between the amino group of the substrate Met and a carbonyl group in the Naa20 active site directly anchors the substrate toward acetyl-CoA. NatB has a unique substrate specificity different from all other NATs, which requires acidic amino acids or their amides at the second position. No activity with the NatC substrate MLRFVTANSQDNGRPVGRK and with the NatA substrate SASEAG
-
-
-
additional information
?
-
-
no activity with MKEEVKGRWGRPVGRRRRRPVRVYP and MDELFPLRWGRPVGRRRRRPVRVYP
-
-
?
additional information
?
-
-
the enzyme also shows lysine Nepsilon-acetyltransferase activity with histone 4
-
-
?
additional information
?
-
-
the enzyme preferably acetylates oligopeptides with N-termini Met-Leu-Xxx-Pro. Furthermore, the enzyme autoacetylates lysines 34, 37, and 140 in vitro
-
-
?
additional information
?
-
P61599; Q14CX7
the enzyme NatB acetylates the N-terminal amino acid of polymerase acidic proteins, especially PA-X, of influenza A virus. NatB prefers to acetylate proteins beginning with Met-Asp, Met-Glu, and Met-Asn in yeast and mammals
-
-
-
additional information
?
-
Q06504; Q12387
NatB catalyzes the N-terminal acetylation of the N-terminal amino acid of its target proteins and prefers to acetylate proteins beginning with Met-Asp, Met-Glu, and Met-Asn
-
-
-
additional information
?
-
Q06504; Q12387
NatB catalyzes the N-terminal acetylation of the N-terminal amino acid of its target proteins and prefers to acetylate proteins beginning with Met-Asp, Met-Glu, and Met-Asn
-
-
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
acetyl-CoA + N-terminal L-methionyl-L-glutaminyl-[influenza virus PA-X]
N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[influenza virus PA-X] + CoA
P61599; Q14CX7
-
-
-
?
additional information
?
-
P61599; Q14CX7
the enzyme NatB acetylates the N-terminal amino acid of polymerase acidic proteins, especially PA-X, of influenza A virus. NatB prefers to acetylate proteins beginning with Met-Asp, Met-Glu, and Met-Asn in yeast and mammals
-
-
-
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
Q5AAR6; Q5AB99
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
Q5AAR6; Q5AB99
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
P61599; Q14CX7
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
P61600; Q8BWZ3
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
P61600; Q8BWZ3
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
Q06504; Q12387
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
Q06504; Q12387
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
Q5AAR6; Q5AB99
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
Q5AAR6; Q5AB99
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
P61599; Q14CX7
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
P61600; Q8BWZ3
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
P61600; Q8BWZ3
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
Q06504; Q12387
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
Q06504; Q12387
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
Q5AAR6; Q5AB99
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
Q5AAR6; Q5AB99
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
P61600; Q8BWZ3
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
P61600; Q8BWZ3
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
Q06504; Q12387
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
Q06504; Q12387
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
Q5AAR6; Q5AB99
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
Q5AAR6; Q5AB99
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
P61599; Q14CX7
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
P61600; Q8BWZ3
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
P61600; Q8BWZ3
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
Q06504; Q12387
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
Q06504; Q12387
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subunits Naa20 and Naa25 of enzyme complex NatB
Q5AAR6; Q5AB99
UniProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
-
the enzyme controls the levels of acetyl-coenzyme A by antagonizing the acetyl-CoA hydrolase ACER-1
physiological function
additional information
evolution
P61599; Q14CX7
Nat3p and Mdm20p subunits form a heterodimer, named NatB, which is a member of the NAT family
evolution
Q06504; Q12387
Nat3p and Mdm20p subunits form a heterodimer, named NatB, which is a member of the NAT family. Each NAT family member preferentially catalyzes the N-terminal acetylation of the N-terminal amino acid of its target proteins. NatB prefers to acetylate proteins beginning with Met-Asp, Met-Glu, and Met-Asn in yeast and mammals
evolution
Q5AAR6; Q5AB99
the family of N-terminal acetyltransferases (NATs) has six subtypes with their unique substrate specificity, NatA-NatF. The substrate specificity of Nats is determined by the first two amino acids of the substrate protein/peptide. NatB has a unique substrate specificity different from all other NATs, which requires acidic amino acids or their amides at the second position
evolution
-
the family of N-terminal acetyltransferases (NATs) has six subtypes with their unique substrate specificity, NatA-NatF. The substrate specificity of Nats is determined by the first two amino acids of the substrate protein/peptide. NatB has a unique substrate specificity different from all other NATs, which requires acidic amino acids or their amides at the second position
-
evolution
-
Nat3p and Mdm20p subunits form a heterodimer, named NatB, which is a member of the NAT family. Each NAT family member preferentially catalyzes the N-terminal acetylation of the N-terminal amino acid of its target proteins. NatB prefers to acetylate proteins beginning with Met-Asp, Met-Glu, and Met-Asn in yeast and mammals
-
malfunction
-
enzyme knockdown disrupts normal cell-cycle progression and induces cell growth inhibition. Enzyme knockdown results in an increase in G0/G1-phase cells
malfunction
P61600; Q8BWZ3
Naa25 inactivation is embryonic lethal in homozygocity. Recombinant Bax accumulates in the mitochondria of Naa25-/- MEF cells, but does not promote cytochrome c release, suggesting that an additional step is required for full activation of Bax
malfunction
Q06504; Q12387
recombinant Bax accumulates in the mitochondria of yeast naa20DELTA (W303 naa20DELTA), but does not promote cytochrome c release, suggesting that an additional step is required for full activation of Bax
malfunction
P61599; Q14CX7
shutoff activity of influenza A viral PA-X is suppressed in NatB-deficient cells, and PA-X mutants that are not acetylated by NatB show reduced shutoff activities. Polymerase acidic proteins (PAs) that are not acetylated by NatB lost their function in the viral polymerase complex
malfunction
Q06504; Q12387
shutoff activity of influenza A viral PA-X is suppressed in NatB-deficient cells, and PA-X mutants that are not acetylated by NatB show reduced shutoff activities. Polymerase acidic proteins (PAs) that are not acetylated by NatB lost their function in the viral polymerase complex
malfunction
-
Naa25 inactivation is embryonic lethal in homozygocity. Recombinant Bax accumulates in the mitochondria of Naa25-/- MEF cells, but does not promote cytochrome c release, suggesting that an additional step is required for full activation of Bax
-
malfunction
-
shutoff activity of influenza A viral PA-X is suppressed in NatB-deficient cells, and PA-X mutants that are not acetylated by NatB show reduced shutoff activities. Polymerase acidic proteins (PAs) that are not acetylated by NatB lost their function in the viral polymerase complex
-
malfunction
-
recombinant Bax accumulates in the mitochondria of yeast naa20DELTA (W303 naa20DELTA), but does not promote cytochrome c release, suggesting that an additional step is required for full activation of Bax
-
physiological function
-
the enzyme is involved in vacuolar protein sorting and cell wall maintenance
physiological function
-
the enzyme is required for normal levels of global histone acetylation in the germline
physiological function
-
the enzyme Naa50p is important for chromosome segregation
physiological function
-
the NatB complex activity is required for flowering time regulation and for leaf, inflorescence, flower, fruit and embryonic development. NatB-mediated N-alpha-terminal acetylation of proteins is pleiotropically required for Arabidopsis development
physiological function
P61599; Q14CX7
N-terminal acetylation is a major posttranslational modification in eukaryotes catalyzed by N-terminal acetyltransferases (NATs), NatA through NatF. N-terminal acetylation modulates diverse protein functions. The N-terminal acetylation by NatB, which comprises the subunits NAA20 and NAA25, is involved in the shutoff activity of influenza virus PA-X. PA-X must be N-terminally acetylated by NatB for its shutoff activity. PA-X cleaves host mRNAs via its endonuclease activity to suppress host protein expression
physiological function
Q06504; Q12387
N-terminal acetylation is a major posttranslational modification in eukaryotes catalyzed by N-terminal acetyltransferases (NATs), NatA through NatF. N-terminal acetylation modulates diverse protein functions. The N-terminal acetylation by NatB, which comprises the subunits Naa3 and MDM20 is essential in the shutoff activity of influenza virus PA-X. PA-X must be N-terminally acetylated by NatB for its shutoff activity. The second amino acid, recognized by NatB, is required for the shutoff activity of PA-X in a NatB-dependent manner. Saccharomyces cerevisiae is used as a model organism
physiological function
P61600; Q8BWZ3
recombinant human Bax expressed in MEF cells is N-terminal (Nt-)acetylated by Naa20p. Nt-acetylation of Bax is essential to maintain Bax in an inactive conformation in the cytosol of the cells. N-terminal acetylation modulates Bax targeting to mitochondria. Contribution of Bax Nt-acetylation to its regulation
physiological function
Q06504; Q12387
recombinant human Bax expressed in strain BY4743 is N-terminally (Nt-)acetylated by yNaa20p. Nt-acetylation of Bax is essential to maintain Bax in an inactive conformation in the cytosol of yeast. N-terminal acetylation modulates Bax targeting to mitochondria. Contribution of Bax Nt-acetylation to its regulation
physiological function
-
the enzyme is involved in vacuolar protein sorting and cell wall maintenance
-
physiological function
-
recombinant human Bax expressed in MEF cells is N-terminal (Nt-)acetylated by Naa20p. Nt-acetylation of Bax is essential to maintain Bax in an inactive conformation in the cytosol of the cells. N-terminal acetylation modulates Bax targeting to mitochondria. Contribution of Bax Nt-acetylation to its regulation
-
physiological function
-
N-terminal acetylation is a major posttranslational modification in eukaryotes catalyzed by N-terminal acetyltransferases (NATs), NatA through NatF. N-terminal acetylation modulates diverse protein functions. The N-terminal acetylation by NatB, which comprises the subunits Naa3 and MDM20 is essential in the shutoff activity of influenza virus PA-X. PA-X must be N-terminally acetylated by NatB for its shutoff activity. The second amino acid, recognized by NatB, is required for the shutoff activity of PA-X in a NatB-dependent manner. Saccharomyces cerevisiae is used as a model organism
-
physiological function
-
recombinant human Bax expressed in strain BY4743 is N-terminally (Nt-)acetylated by yNaa20p. Nt-acetylation of Bax is essential to maintain Bax in an inactive conformation in the cytosol of yeast. N-terminal acetylation modulates Bax targeting to mitochondria. Contribution of Bax Nt-acetylation to its regulation
-
additional information
Q06504; Q12387
Nat3p (equivalent to human NAA20) and Mdm20p (equivalent to human NAA25) are the components of enzyme complex NatB
additional information
Q5AAR6; Q5AB99
the auxiliary subunit Naa25 of NatB forms a horseshoe-like deck to hold specifically its catalytic subunit Naa20. The first two amino acids Met and Asp of a substrate peptide mediate the major interactions with the active site in the Naa20 subunit. The hydrogen bonds between the substrate Asp and pocket residues of Naa20 are essential to determine the NatB substrate specificity. A hydrogen bond between the amino group of the substrate Met and a carbonyl group in the Naa20 active site directly anchors the substrate toward acetyl-CoA Unique molecular mechanism of specific N-terminal acetylation acted by NatB, substrate recognition and acetylation of NatB, overview
additional information
-
the auxiliary subunit Naa25 of NatB forms a horseshoe-like deck to hold specifically its catalytic subunit Naa20. The first two amino acids Met and Asp of a substrate peptide mediate the major interactions with the active site in the Naa20 subunit. The hydrogen bonds between the substrate Asp and pocket residues of Naa20 are essential to determine the NatB substrate specificity. A hydrogen bond between the amino group of the substrate Met and a carbonyl group in the Naa20 active site directly anchors the substrate toward acetyl-CoA Unique molecular mechanism of specific N-terminal acetylation acted by NatB, substrate recognition and acetylation of NatB, overview
additional information
P61600; Q8BWZ3
the NatB enzymatic complex is constituted of two subunits, the NAA20 catalytic subunit and the accessory subunit NAA25
additional information
-
the NatB enzymatic complex is constituted of two subunits, the NAA20 catalytic subunit and the accessory subunit NAA25
additional information
Q06504; Q12387
the NatB enzymatic complex is constituted of two subunits, the Naa3p catalytic subunit and the accessory subunit MDM20
additional information
-
the NatB enzymatic complex is constituted of two subunits, the Naa3p catalytic subunit and the accessory subunit MDM20
additional information
-
the auxiliary subunit Naa25 of NatB forms a horseshoe-like deck to hold specifically its catalytic subunit Naa20. The first two amino acids Met and Asp of a substrate peptide mediate the major interactions with the active site in the Naa20 subunit. The hydrogen bonds between the substrate Asp and pocket residues of Naa20 are essential to determine the NatB substrate specificity. A hydrogen bond between the amino group of the substrate Met and a carbonyl group in the Naa20 active site directly anchors the substrate toward acetyl-CoA Unique molecular mechanism of specific N-terminal acetylation acted by NatB, substrate recognition and acetylation of NatB, overview
-
additional information
-
the NatB enzymatic complex is constituted of two subunits, the NAA20 catalytic subunit and the accessory subunit NAA25
-
additional information
-
Nat3p (equivalent to human NAA20) and Mdm20p (equivalent to human NAA25) are the components of enzyme complex NatB
-
additional information
-
the NatB enzymatic complex is constituted of two subunits, the Naa3p catalytic subunit and the accessory subunit MDM20
-
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NAT3_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
180
0
20521
Swiss-Prot
other Location (Reliability: 2)
NAT3_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
195
0
22921
Swiss-Prot
other Location (Reliability: 1)
NAA20_ARATH
174
0
20395
Swiss-Prot
other Location (Reliability: 5)
NAA20_DANRE
178
0
20358
Swiss-Prot
other Location (Reliability: 2)
NAA20_HUMAN
178
0
20368
Swiss-Prot
other Location (Reliability: 2)
NAA20_MACFA
178
0
20368
Swiss-Prot
other Location (Reliability: 2)
NAA20_MOUSE
178
0
20368
Swiss-Prot
other Location (Reliability: 2)
NAA20_XENLA
178
0
20354
Swiss-Prot
other Location (Reliability: 2)
NAA20_XENTR
178
0
20366
Swiss-Prot
other Location (Reliability: 2)
G7ZX36_MEDTR
154
0
17966
TrEMBL
other Location (Reliability: 1)
A0A2P6RWL8_ROSCH
898
0
102574
TrEMBL
other Location (Reliability: 2)
A0A0B2QJQ3_GLYSO
192
0
22043
TrEMBL
other Location (Reliability: 2)
G7I387_MEDTR
280
0
30843
TrEMBL
Chloroplast (Reliability: 1)
A0A2P6RKP7_ROSCH
290
0
34151
TrEMBL
Mitochondrion (Reliability: 4)
A0A2P6S6R3_ROSCH
185
0
21276
TrEMBL
other Location (Reliability: 2)
A0A0B2S643_GLYSO
109
0
12730
TrEMBL
other Location (Reliability: 3)
B7FJ76_MEDTR
183
0
20848
TrEMBL
Secretory Pathway (Reliability: 3)
G7JEG0_MEDTR
409
0
46647
TrEMBL
other Location (Reliability: 2)
A0A2P6PY46_ROSCH
227
0
25420
TrEMBL
other Location (Reliability: 4)
A0A0B2SLH5_GLYSO
104
1
12190
TrEMBL
other Location (Reliability: 1)
A0A1N6LWD7_BABMR
Babesia microti (strain RI)
150
0
17891
TrEMBL
other Location (Reliability: 2)
A0A396IQQ6_MEDTR
164
0
17976
TrEMBL
other Location (Reliability: 4)
A0A396H204_MEDTR
220
0
25364
TrEMBL
other Location (Reliability: 2)
A0A396H8D5_MEDTR
159
0
18484
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0B2NP41_GLYSO
901
0
102824
TrEMBL
other Location (Reliability: 2)
A0A2P6PSN0_ROSCH
157
0
17834
TrEMBL
other Location (Reliability: 2)
A0A0B2RH35_GLYSO
128
0
14915
TrEMBL
other Location (Reliability: 3)
A0A0B2PRM6_GLYSO
121
0
14021
TrEMBL
other Location (Reliability: 2)
A0A0B2RJG9_GLYSO
154
0
17686
TrEMBL
other Location (Reliability: 2)
A0A2P6SJF3_ROSCH
280
0
30769
TrEMBL
Chloroplast (Reliability: 1)
A0A6J7ZVE7_MYTCO
173
0
19966
TrEMBL
other Location (Reliability: 2)
A0A072USB6_MEDTR
900
0
103058
TrEMBL
other Location (Reliability: 2)
A0A8J8VZ89_9EURO
190
0
21793
TrEMBL
other Location (Reliability: 5)
A0A2P6S882_ROSCH
196
0
22089
TrEMBL
Secretory Pathway (Reliability: 4)
A0A0B2Q9L6_GLYSO
123
0
14570
TrEMBL
other Location (Reliability: 4)
A0A0B2QE29_GLYSO
218
0
26086
TrEMBL
other Location (Reliability: 2)
A0A0B2RAP2_GLYSO
237
0
26906
TrEMBL
Mitochondrion (Reliability: 1)
A0A0B2SSG3_GLYSO
901
0
102978
TrEMBL
other Location (Reliability: 2)
A0A0B2QEA6_GLYSO
174
0
20289
TrEMBL
Secretory Pathway (Reliability: 3)
A0A2P6PW15_ROSCH
174
0
20444
TrEMBL
other Location (Reliability: 5)
A0A0B2QE32_GLYSO
139
0
16168
TrEMBL
Secretory Pathway (Reliability: 3)
A0A0B2SBL3_GLYSO
893
0
102226
TrEMBL
other Location (Reliability: 2)
W1QIN3_OGAPD
Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1)
185
0
21675
TrEMBL
other Location (Reliability: 1)
A0A072V684_MEDTR
299
0
34396
TrEMBL
Chloroplast (Reliability: 2)
G7K0Q8_MEDTR
164
0
18591
TrEMBL
other Location (Reliability: 2)
A0A0B2QR99_GLYSO
121
0
14144
TrEMBL
other Location (Reliability: 2)
A0A396JN32_MEDTR
901
0
102668
TrEMBL
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
additional information
heterodimer
P61600; Q8BWZ3
the NatB enzymatic complex is constituted of two subunits, the NAA20 catalytic subunit and the accessory subunit NAA25
heterodimer
-
the NatB enzymatic complex is constituted of two subunits, the NAA20 catalytic subunit and the accessory subunit NAA25
-
heterodimer
Q06504; Q12387
the NatB enzymatic complex is constituted of two subunits, the Naa3p catalytic subunit and the accessory subunit MDM20
heterodimer
-
the NatB enzymatic complex is constituted of two subunits, the Naa3p catalytic subunit and the accessory subunit MDM20
-
additional information
Q5AAR6; Q5AB99
the auxiliary subunit Naa25 of NatB forms a horseshoe-like deck to hold specifically its catalytic subunit Naa20. Analysis of the structure of mutant NatB/Naa20(residue 1-170) in complex with a peptide substrate MEAHNK-biotin and of the structure of NatB/Naa20(full-length) in complex with a bisubstrate inhibitor CoA-MDSEVAALVID, structure comparisons, overview
additional information
-
the auxiliary subunit Naa25 of NatB forms a horseshoe-like deck to hold specifically its catalytic subunit Naa20. Analysis of the structure of mutant NatB/Naa20(residue 1-170) in complex with a peptide substrate MEAHNK-biotin and of the structure of NatB/Naa20(full-length) in complex with a bisubstrate inhibitor CoA-MDSEVAALVID, structure comparisons, overview
additional information
-
the auxiliary subunit Naa25 of NatB forms a horseshoe-like deck to hold specifically its catalytic subunit Naa20. Analysis of the structure of mutant NatB/Naa20(residue 1-170) in complex with a peptide substrate MEAHNK-biotin and of the structure of NatB/Naa20(full-length) in complex with a bisubstrate inhibitor CoA-MDSEVAALVID, structure comparisons, overview
-
additional information
Q06504; Q12387
Nat3p (NAA20) and Mdm20p (NAA25) are the components of enzyme complex NatB
additional information
-
Nat3p (NAA20) and Mdm20p (NAA25) are the components of enzyme complex NatB
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified NatB free and complexed with bisubstrate inhibitor, NatB holoenzyme in the presence of CoA and substrate peptides, best crystals are grown in a condition containing 25 mM MES, pH 6.5, 5% PEG 600, 1.5% PEG 1000, 5% glycerol, 4% 1,3-butanediol, and 5 mM DTT, improved using the NatB complex with Naa20 (residue 1-170), best crystallization condition for NatB and the inhibitor complex is 20 mM Tris, pH 7.5, 20 mM NaCl, 2.2% PEG 4000, 5% glycerol, 4% 1,3-butanediol, and 5 mM DTT, 2-4 days at room temperature, X-ray diffraction structure determination and analysis at 2.33-2.75 A resolution
Q5AAR6; Q5AB99
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A77S
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
E25A
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
F112A
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
F112H
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
F27A
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
F27Y
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
G140A
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
H74A
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
H74A/T76A
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
L23A
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
T24P
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
T76A
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
Y124F
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
Y138A
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
Y138A/Y139A
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
Y138F
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
Y139A
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
Y139F
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
F112A
-
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
-
H74A
-
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
-
Y124F
-
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
-
Y138A
-
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
-
additional information
additional information
Q5AAR6; Q5AB99
generation of a deletion mutant (residues 1-170) of the catalytic subunit Naa20. Structure of mutant NatB/Naa20 (residue 1-170) in complex with a peptide substrate MEAHNK-biotin and structure of NatB/Naa20 (full-length) in complex with a bisubstrate inhibitor CoA-MDSEVAALVID
additional information
-
generation of a deletion mutant (residues 1-170) of the catalytic subunit Naa20. Structure of mutant NatB/Naa20 (residue 1-170) in complex with a peptide substrate MEAHNK-biotin and structure of NatB/Naa20 (full-length) in complex with a bisubstrate inhibitor CoA-MDSEVAALVID
additional information
-
generation of a deletion mutant (residues 1-170) of the catalytic subunit Naa20. Structure of mutant NatB/Naa20 (residue 1-170) in complex with a peptide substrate MEAHNK-biotin and structure of NatB/Naa20 (full-length) in complex with a bisubstrate inhibitor CoA-MDSEVAALVID
-
additional information
P61599; Q14CX7
construction of NAA20-KO or NAA25-KO cells. Wild-type, NAA20-KO, or NAA25-KO cells are transfected with plasmids encoding PB2, PB1, PA, and NP, with a plasmid for the expression of viral RNA encoding the firefly luciferase, and with a plasmid encoding Renilla luciferase as a transfection control
additional information
-
generation of Naa25-/- MEF cells and of NAA25-knockout mice
additional information
-
generation of Naa25-/- MEF cells and of NAA25-knockout mice
-
additional information
Q06504; Q12387
generation yeast naa20DELTA cells, W303 naa20DELTA, from wild-type strain W303-1B
additional information
-
generation yeast naa20DELTA cells, W303 naa20DELTA, from wild-type strain W303-1B
additional information
Q06504; Q12387
the wild-type yeast strain BY4743 transformed with the plasmid encoding wild-type influenza A PA-X, PA-X E2D, or PA-X E2N proteins barely formed any colonies, whereas wild-type yeast transformed with the plasmid encoding PA-X E2A or PA-X E2P viral proteins formed many colonies
additional information
-
the wild-type yeast strain BY4743 transformed with the plasmid encoding wild-type influenza A PA-X, PA-X E2D, or PA-X E2N proteins barely formed any colonies, whereas wild-type yeast transformed with the plasmid encoding PA-X E2A or PA-X E2P viral proteins formed many colonies
-
additional information
-
generation yeast naa20DELTA cells, W303 naa20DELTA, from wild-type strain W303-1B
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant NatB complexes from Escherichia coli by affinity chromatography, to homogeneity
Q5AAR6; Q5AB99
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
genes NAA20 and NAA25, sequence comparisons, functional recombinant coexpression of a full-length auxiliary subunit Naa25 subunit (residues 1-745) with a full-length (residues 1-188) or a deletion mutant (residues 1-170) of the catalytic subunit Naa20 as heterodimeric NatB holoenzymes in Escherichia coli, recombinant expression of His- and/or FLAG-tagged NatB wild-type and mutants enzymes in Escherichia coli
Q5AAR6; Q5AB99
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Starheim, K.; Arnesen, T.; Gromyko, D.; Ryningen, A.; Varhaug, J.; Lillehaug, J.
Identification of the human Nalpha-acetyltransferase complex B (hNatB): A complex important for cell-cycle progression
Biochem. J.
415
325-331
2008
Homo sapiens
Evjenth, R.; Hole, K.; Karlsen, O.; Ziegler, M.; Amesen, T.; Lillehaug, J.
Human Naa50p (Nat5/San) displays both protein Nalpha- and Nepsilon-acetyltransferase activity
J. Biol. Chem.
284
31122-31129
2009
Homo sapiens
Lee, K.E.; Ahn, J.Y.; Kim, J.M.; Hwang, C.S.
Synthetic lethal screen of NAA20, a catalytic subunit gene of NatB N-terminal acetylase in Saccharomyces cerevisiae
J. Microbiol.
52
842-848
2014
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
Gao, J.; Kim, H.M.; Elia, A.E.; Elledge, S.J.; Colaiacovo, M.P.
NatB domain-containing CRA-1 antagonizes hydrolase ACER-1 linking acetyl-CoA metabolism to the initiation of recombination during C. elegans meiosis
PLoS Genet.
11
e1005029
2015
Caenorhabditis elegans
Ferrandez-Ayela, A.; Micol-Ponce, R.; Sanchez-Garcia, A.; Alonso-Peral, M.; Micol, J.; Ponce, M.
Mutation of an Arabidopsis NatB N-alpha-terminal acetylation complex component causes pleiotropic developmental defects
PLoS ONE
8
e80697
2013
Arabidopsis thaliana
Oishi, K.; Yamayoshi, S.; Kozuka-Hata, H.; Oyama, M.; Kawaoka, Y.
N-terminal acetylation by NatB is required for the shutoff activity of influenza A virus PA-X
Cell Rep.
24
851-860
2018
Homo sapiens (P61599 AND Q14CX7), Saccharomyces cerevisiae (Q06504 AND Q12387), Saccharomyces cerevisiae ATCC 204508 (Q06504 AND Q12387)
Alves, S.; Neiri, L.; Rodrigues Chaves, S.; Trindade, V.D.; Manon, S.; Dominguez, V.; Pintado, B.; Jonckheere, V.; Van Damme, P.; Silva, R.D.; Aldabe, R.; Corte-Real, M.
N-terminal acetylation modulates Bax targeting to mitochondria
Int. J. Biochem. Cell Biol.
95
35-42
2018
Mus musculus (P61600 AND Q8BWZ3), Mus musculus, Mus musculus C57BL/6 (P61600 AND Q8BWZ3), Saccharomyces cerevisiae (Q06504 AND Q12387), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (Q06504 AND Q12387)
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