|
|
||
|
|
|
|
|
UniProt functional annotation for Q08689 | ||
|
|
|
|
|
|
||
| UniProt code: Q08689. |
|
||
| Organism: | |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). |
| Taxonomy: | |
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. |
|
||
|
||
| Function: | |
N-alpha-acetyltransferase that acetylates the N-terminus of proteins that retain their initiating methionine (PubMed:25886145). Has a broad substrate specificity: able to acetylate the initiator methionine of most peptides (PubMed:25886145). Non-essential component of the NatA N-terminal acetyltransferase (PubMed:14517307). {ECO:0000269|PubMed:14517307, ECO:0000269|PubMed:25886145}. |
|
||
| Catalytic activity: | |
Reaction=acetyl-CoA + N-terminal L-methionyl-L-alanyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-alanyl-[protein]; Xref=Rhea:RHEA:50564, Rhea:RHEA-COMP:12726, Rhea:RHEA-COMP:12727, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133398, ChEBI:CHEBI:133399; EC=2.3.1.258; Evidence={ECO:0000269|PubMed:25886145}; |
| Catalytic activity: | |
Reaction=acetyl-CoA + N-terminal L-methionyl-L-seryl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-seryl-[protein]; Xref=Rhea:RHEA:50568, Rhea:RHEA-COMP:12728, Rhea:RHEA-COMP:12729, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133400, ChEBI:CHEBI:133401; EC=2.3.1.258; Evidence={ECO:0000269|PubMed:25886145}; |
| Catalytic activity: | |
Reaction=acetyl-CoA + N-terminal L-methionyl-L-valyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-valyl-[protein]; Xref=Rhea:RHEA:50572, Rhea:RHEA-COMP:12730, Rhea:RHEA-COMP:12731, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133402, ChEBI:CHEBI:133403; EC=2.3.1.258; Evidence={ECO:0000269|PubMed:25886145}; |
| Catalytic activity: | |
Reaction=acetyl-CoA + N-terminal L-methionyl-L-threonyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-threonyl-[protein]; Xref=Rhea:RHEA:50576, Rhea:RHEA-COMP:12732, Rhea:RHEA-COMP:12733, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133404, ChEBI:CHEBI:133405; EC=2.3.1.258; Evidence={ECO:0000269|PubMed:25886145}; |
| Catalytic activity: | |
Reaction=acetyl-CoA + N-terminal L-methionyl-L-lysyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-lysyl-[protein]; Xref=Rhea:RHEA:50580, Rhea:RHEA-COMP:12734, Rhea:RHEA-COMP:12735, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133406, ChEBI:CHEBI:133407; EC=2.3.1.258; Evidence={ECO:0000269|PubMed:25886145}; |
| Catalytic activity: | |
Reaction=acetyl-CoA + N-terminal L-methionyl-L-leucyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein]; Xref=Rhea:RHEA:50520, Rhea:RHEA-COMP:12711, Rhea:RHEA-COMP:12712, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133377, ChEBI:CHEBI:133378; EC=2.3.1.258; Evidence={ECO:0000269|PubMed:25886145}; |
| Catalytic activity: | |
Reaction=acetyl-CoA + N-terminal L-methionyl-L-phenylalanyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-phenylalanyl- [protein]; Xref=Rhea:RHEA:50528, Rhea:RHEA-COMP:12715, Rhea:RHEA- COMP:12716, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133382, ChEBI:CHEBI:133383; EC=2.3.1.258; Evidence={ECO:0000269|PubMed:25886145}; |
| Catalytic activity: | |
Reaction=acetyl-CoA + N-terminal L-methionyl-L-tyrosyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein]; Xref=Rhea:RHEA:50532, Rhea:RHEA-COMP:12717, Rhea:RHEA-COMP:12718, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133384, ChEBI:CHEBI:133385; EC=2.3.1.258; Evidence={ECO:0000269|PubMed:25886145}; |
| Subunit: | |
Component of the N-terminal acetyltransferase A (NatA) complex, which is composed of ARD1, NAT1 and NAT5. {ECO:0000269|PubMed:14517307}. |
| Subcellular location: | |
Cytoplasm {ECO:0000269|PubMed:14562095}. |
| Miscellaneous: | |
Present with 2370 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}. |
| Similarity: | |
Belongs to the acetyltransferase family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.