EC Tree |
2. Transferases |
2.3 Acyltransferases |
2.3.1 Transferring groups other than aminoacyl groups |
ID: | 2.3.1.259 |
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Description: | N-terminal methionine N(alpha)-acetyltransferase NatF. |
Cath: | 3.40.630.30; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 2.3.1.259 |
BRENDA Enzyme Link: | BRENDA 2.3.1.259 |
KEGG Enzyme Link: | KEGG2.3.1.259 |
BioCyc Enzyme Link: | BioCyc 2.3.1.259 |
ExPASy Enzyme Link: | ExPASy2.3.1.259 |
EC2PDB Enzyme Link: | EC2PDB 2.3.1.259 |
ExplorEnz Enzyme Link: | ExplorEnz 2.3.1.259 |
PRIAM enzyme-specific profiles Link: | PRIAM 2.3.1.259 |
IntEnz Enzyme Link: | IntEnz 2.3.1.259 |
MEDLINE Enzyme Link: | MEDLINE 2.3.1.259 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:50604 | acetyl-CoA + N-terminal L-methionyl-[transmembrane protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-[transmembrane protein] |
RULE(radius=1) | [*:1]-[NH2;+0:2].[*:3]=[C;H0;+0:4](-[*:5])-[S;H0;+0:6]-[*:7]>>[*:7]-[SH;+0:6].[*:3]=[C;H0;+0:4](-[*:5])-[NH;+0:2]-[*:1] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
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NatF contributes to an evolutionary shift in protein N-terminal acetylation and is important for normal chromosome segregation. | Van Damme P, Hole K, Pimenta-Marques A, Helsens K, Vandekerckhove J, Martinho RG, Gevaert K, Arnesen T | 2011 Jul | 21750686 |
An organellar nα-acetyltransferase, naa60, acetylates cytosolic N termini of transmembrane proteins and maintains Golgi integrity. | Aksnes H, Van Damme P, Goris M, Starheim KK, Marie M, Støve SI, Hoel C, Kalvik TV, Hole K, Glomnes N, Furnes C, Ljostveit S, Ziegler M, Niere M, Gevaert K, Arnesen T | 2015 Mar 3 | 25732826 |