UniProt functional annotation for P07347

UniProt code: P07347.

Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Taxonomy: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
 
Function: Catalytic component of the NatA N-terminal acetyltransferase, which catalyzes acetylation of proteins beginning with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a role in normal eukaryotic translation and processing, protect against proteolytic degradation and protein turnover. {ECO:0000269|PubMed:1600941, ECO:0000269|PubMed:2551674}.
 
Catalytic activity: Reaction=acetyl-CoA + N-terminal glycyl-[protein] = CoA + H(+) + N- terminal N(alpha)-acetylglycyl-[protein]; Xref=Rhea:RHEA:50496, Rhea:RHEA-COMP:12666, Rhea:RHEA-COMP:12700, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64723, ChEBI:CHEBI:133369; EC=2.3.1.255; Evidence={ECO:0000269|PubMed:1600941, ECO:0000269|PubMed:2551674};
Catalytic activity: Reaction=acetyl-CoA + N-terminal L-alanyl-[protein] = CoA + H(+) + N- terminal N(alpha)-acetyl-L-alanyl-[protein]; Xref=Rhea:RHEA:50500, Rhea:RHEA-COMP:12701, Rhea:RHEA-COMP:12702, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64718, ChEBI:CHEBI:83683; EC=2.3.1.255; Evidence={ECO:0000269|PubMed:1600941, ECO:0000269|PubMed:2551674};
Catalytic activity: Reaction=acetyl-CoA + N-terminal L-seryl-[protein] = CoA + H(+) + N- terminal N(alpha)-acetyl-L-seryl-[protein]; Xref=Rhea:RHEA:50504, Rhea:RHEA-COMP:12703, Rhea:RHEA-COMP:12704, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64738, ChEBI:CHEBI:83690; EC=2.3.1.255; Evidence={ECO:0000269|PubMed:1600941, ECO:0000269|PubMed:2551674};
Catalytic activity: Reaction=acetyl-CoA + N-terminal L-valyl-[protein] = CoA + H(+) + N- terminal N(alpha)-acetyl-L-valyl-[protein]; Xref=Rhea:RHEA:50508, Rhea:RHEA-COMP:12705, Rhea:RHEA-COMP:12706, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64741, ChEBI:CHEBI:133371; EC=2.3.1.255; Evidence={ECO:0000269|PubMed:1600941, ECO:0000269|PubMed:2551674};
Catalytic activity: Reaction=acetyl-CoA + N-terminal L-cysteinyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:50512, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:12708, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:65250, ChEBI:CHEBI:133372; EC=2.3.1.255; Evidence={ECO:0000269|PubMed:1600941, ECO:0000269|PubMed:2551674};
Catalytic activity: Reaction=acetyl-CoA + N-terminal L-threonyl-[protein] = CoA + H(+) + N- terminal N(alpha)-acetyl-L-threonyl-[protein]; Xref=Rhea:RHEA:50516, Rhea:RHEA-COMP:12709, Rhea:RHEA-COMP:12710, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64739, ChEBI:CHEBI:133375; EC=2.3.1.255; Evidence={ECO:0000269|PubMed:1600941, ECO:0000269|PubMed:2551674};
Subunit: Component of the N-terminal acetyltransferase A (NatA) complex, which is composed of ARD1, NAT1 and NAT5. Can self-associate. {ECO:0000269|PubMed:14517307}.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Miscellaneous: Present with 3310 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}.
Similarity: Belongs to the acetyltransferase family. ARD1 subfamily. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.