2.3.1.256: N-terminal methionine Nalpha-acetyltransferase NatC
This is an abbreviated version!
For detailed information about N-terminal methionine Nalpha-acetyltransferase NatC, go to the full flat file.
Word Map on EC 2.3.1.256
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2.3.1.256
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acetyltransferases
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dsrnas
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viruslike
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nonfermentable
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co-translationally
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non-mendelian
- 2.3.1.256
- acetyltransferases
- dsrnas
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viruslike
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nonfermentable
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co-translationally
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non-mendelian
Reaction
Synonyms
EC 2.3.1.88, EGAP, embryonic growth-associated protein, hNaa30, MAK10, MAK3, MAK31, Mak31p, Mak3p, N-alpha acetyltransferase 30, N-alpha-acetyltransferase 30, N-terminal acetyltransferase, N-terminal acetyltransferase complex C, N-terminal acetyltransferase Naa30, NAA30, NAA35, NAA38, Nalpha-acetyltransferase, Nalpha-terminal acetyltransferase complex C, NAT12, NatC, PAM21, protein methionine N-acetyltransferase, RimI, RimI acetyltransferase, Rv3420c, TcNaa30, TcNaa35, TcNatC
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2.3.1.256 N-terminal methionine Nalpha-acetyltransferase NatCAdvanced search results
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General Information on EC 2.3.1.256 - N-terminal methionine Nalpha-acetyltransferase NatC
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
enzyme Naa30 belongs to the GNAT superfamily of acetyltransferases characterized by the highly conserved GNAT fold, which promotes Ac-CoA binding and substrate recognition
malfunction
physiological function
additional information
malfunction
enzyme depletion results in severe cell growth defects and embryonic lethality
malfunction
knockdown of Naa30 induces the loss of mitochondrial membrane potential and fragmentation of mitochondria
malfunction
knockdown of Nalpha-terminal acetyltransferase complex C leads to p53-dependent apoptosis and aberrant Arf-like GTPase Arl8b localization
malfunction
depletion of the human N-terminal acetyltransferase hNaa30 disrupts Golgi integrity and Golgi-associated GTPase ADP ribosylation factor related protein 1 (ARFRP1) localization. Depletion of the hNatC catalytic subunit hNaa30 leads to disassembly of the Golgi apparatus and trans-Golgi network (TGN). ARFRP1 shifts from a predominantly cis-Golgi and TGN localization to localizing both Golgi and non-Golgi vesicular structures in hNaa30-depleted cells (smaller vesicle-like membranous compartments). Loss of membrane association of ARFRP1 is not observed. hNaa30 depletion induces Golgi scattering and induces aberrant ARFRP1 Golgi localization. Knockdown of each of the hNatC subunits in HeLa cells leads to p53-dependent apoptosis. Naa30 depletion severely disrupts mitochondrial organization. Knockdown phenotypes are specific for hNaa30 depletion and not a result of si-hNAA30-independent effects. Phenotypes, detailed overview
malfunction
overexpression of full-length Naa30 increases cell viability via inhibition of apoptosis. In contrast, Naa30288 does not exert an anti-apoptotic effect
physiological function
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MAK3 is required for the N-terminal acetylation of the killer viral major coat protein, Gag
physiological function
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MAK3 N-acetyltransferase modifies the L-A gag NH2 terminus which in turn is necessary for virus particle assembly
physiological function
the enzyme is essential for mitochondrial integrity and function
physiological function
the enzyme is required for double-stranded RNA virus propagation in Saccharomyces cerevisiae
physiological function
Nalpha-acetylation is a naturally occurring irreversible modification of N-termini of proteins catalyzed by Nalpha-acetyltransferases (NATs). RimIMtb does acetylate peptides representing N-terminus of GroES, GroEL1, and TsaD proteins, in vitro. Significant specific activity of RimIMtb is observed gainst peptide representing N-terminus of GroES
physiological function
Q4CRN8; Q4DLD9; Q4D159, Q4DGZ6; Q4DJ45; Q4D159
TcNatC/TcNatA proteins carry out their function independently of each other as suggested in other organisms and they may have specific functions depending on the parasite life cycle stage. But the proteins may also have other functions independent of the NAT-activity as suggested in other species
physiological function
the human NatC complex (hNatC) is an evolutionarily conserved complex composed of the catalytic subunit hNaa30 (hMak3) and the auxiliary subunits hNaa35 (hMak10) and hNaa38 (hMak31). NatC Nt-acetylates Met-Leu-, Met-Ile-, Met-Phe-, Met-Trp-, Met-Val-, Met-Met-, Met-His-, and Met-Lys-N-termini. The NatC complex is one of several Nt-acetyltransferases (NATs) that perform Nt-acetylation in eukaryotes. Nt-acetylation or protein N-alpha-terminal acetylation, is the addition of an acetyl group on the Nalpha-amino group of proteins. It is one of the most abundant protein modifications in eukaryotes and displays a wide array of biological functions. The Golgi apparatus associated GTPase ADP ribosylation factor related protein 1 (ARFRP1) requires N-terminal acetylation for membrane association and based on its N-terminal sequence, it is likely to be a substrate of hNaa30. ARFRP1 is involved in endosome-to-trans-Golgi network (TGN) traffic
physiological function
the NatC complex consists of the catalytic subunit Naa30 and the auxiliary subunits Naa35 and Naa38, and can potentially Nt-acetylate cytoplasmic proteins when the initiator methionine is followed by a bulky hydrophobic/amphipathic residue at position 2. Full-length enzyme Naa30362 improves cell viability and inhibits apoptosis
physiological function
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TcNatC/TcNatA proteins carry out their function independently of each other as suggested in other organisms and they may have specific functions depending on the parasite life cycle stage. But the proteins may also have other functions independent of the NAT-activity as suggested in other species
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physiological function
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Nalpha-acetylation is a naturally occurring irreversible modification of N-termini of proteins catalyzed by Nalpha-acetyltransferases (NATs). RimIMtb does acetylate peptides representing N-terminus of GroES, GroEL1, and TsaD proteins, in vitro. Significant specific activity of RimIMtb is observed gainst peptide representing N-terminus of GroES
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physiological function
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Nalpha-acetylation is a naturally occurring irreversible modification of N-termini of proteins catalyzed by Nalpha-acetyltransferases (NATs). RimIMtb does acetylate peptides representing N-terminus of GroES, GroEL1, and TsaD proteins, in vitro. Significant specific activity of RimIMtb is observed gainst peptide representing N-terminus of GroES
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physiological function
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the enzyme is required for double-stranded RNA virus propagation in Saccharomyces cerevisiae
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additional information
homology structure modeling of Naa30 using the crystal structure of human Naa50 (PDB ID 3TFY) as template
additional information
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homology structure modeling of Naa30 using the crystal structure of human Naa50 (PDB ID 3TFY) as template
additional information
Q4CRN8; Q4DLD9; Q4D159
Trypanosoma cruzi NatC protein complex consists of one catalytic subunit TcNaa30 and one predicted auxiliary subunit TcNaa35. TcNatC and TcNatA (EC 2.3.1.255) complex subunits interact in vivo and in vitro
additional information
Q4DGZ6; Q4DJ45; Q4D159
Trypanosoma cruzi NatC protein complex consists of one catalytic subunit TcNaa30 and one predicted auxiliary subunit TcNaa35. TcNatC and TcNatA (EC 2.3.1.255) complex subunits interact in vivo and in vitro
additional information
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Trypanosoma cruzi NatC protein complex consists of one catalytic subunit TcNaa30 and one predicted auxiliary subunit TcNaa35. TcNatC and TcNatA (EC 2.3.1.255) complex subunits interact in vivo and in vitro
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