NatA complex

GO:0031415 · Other · Multiprotein complex · Proposed

A conserved complex that catalyzes the transfer of an acetyl group to an N-terminal Ser, Ala, Gly, or Thr residue of a protein acceptor molecule. In Saccharomyces the complex includes Nat1p and Ard1p, and may contain additional proteins. [GO:0031415]

Synonyms: N-terminal acetyltransferase A complex

UniProt location names: UniProt Consortium, CC BY 4.0. Reference label and route sources.

Components

Component	Type	Part of / acts on	Grounding	Genes	Essential	Role
Nat1 NatA auxiliary subunit	Protein	part of	Reviewed label only (reviewed name; no accession asserted)	NAT1	UNKNOWN	Noncatalytic auxiliary constituent that anchors budding-yeast NatA to ribosomes and positions nascent polypeptides for N-terminal acetylation. `DOI:10.1128/MCB.23.20.7403-7414.2003` Gautschi et al. 2003 purified Saccharomyces cerevisiae NatA from ribosomal salt wash, identified Nat1p, Ard1p and Nat5p in the complex, and showed that Nat1p anchors the complex to ribosomes.
Ard1 NatA catalytic subunit	Protein	part of	Reviewed label only (reviewed name; no accession asserted)	ARD1	UNKNOWN	Catalytic GNAT-family constituent of the budding-yeast NatA complex. `DOI:10.1128/MCB.23.20.7403-7414.2003` Gautschi et al. 2003 purified Saccharomyces cerevisiae NatA from ribosomal salt wash, identified Nat1p, Ard1p and Nat5p in the complex, and showed that Nat1p anchors the complex to ribosomes.
Nat5 NatA GNAT-family subunit	Protein	part of	Reviewed label only (reviewed name; no accession asserted)	NAT5	UNKNOWN	GNAT-family NatA constituent that copurifies stoichiometrically with Nat1 and Ard1. `DOI:10.1128/MCB.23.20.7403-7414.2003` Gautschi et al. 2003 purified Saccharomyces cerevisiae NatA from ribosomal salt wash, identified Nat1p, Ard1p and Nat5p in the complex, and showed that Nat1p anchors the complex to ribosomes.

Taxonomic distribution

NCBITaxon:4932 Saccharomyces cerevisiae — COMMON: Gautschi et al. 2003 purified the NatA complex from Saccharomyces cerevisiae ribosomal salt wash. [DOI:10.1128/MCB.23.20.7403-7414.2003]

Canonical examples

NCBITaxon:4932 Saccharomyces cerevisiae — Budding yeast is the source organism in which Nat1, Ard1 and Nat5 were shown to form the ribosome-associated NatA complex. [DOI:10.1128/MCB.23.20.7403-7414.2003]

Functions

protein-N-terminal amino-acid acetyltransferase activity GO:0004596 — Transfer of an acetyl group from acetyl-CoA to the N-terminal alpha-amino group of NatA substrate proteins.
- GO:0004596 GO:0004596 is the Gene Ontology molecular-function term for protein-N-terminal amino-acid acetyltransferase activity.
- GO:0031415 GO:0031415 defines the NatA complex by transfer of acetyl groups to N-terminal Ser, Ala, Gly or Thr residues of protein acceptors.
- DOI:10.1128/MCB.23.20.7403-7414.2003 Gautschi et al. 2003 describe yeast NatA as an N-alpha-acetyltransferase that acts cotranslationally at ribosomes.

Mechanism graphs

NatA carries yeast N-terminal acetyltransferase activity (FUNCTION)

In Saccharomyces cerevisiae, Nat1, Ard1 and Nat5 form a ribosome-associated NatA complex that supports protein-N-terminal acetyltransferase activity.

Subject	Predicate	Object	Evidence
Ard1 NatA catalytic subunit	contributes to	NatA complex	`DOI:10.1128/MCB.23.20.7403-7414.2003` Gautschi et al. 2003 purified Saccharomyces cerevisiae NatA from ribosomal salt wash, identified Nat1p, Ard1p and Nat5p in the complex, and showed that Nat1p anchors the complex to ribosomes.
NatA complex	supports	protein-N-terminal amino-acid acetyltransferase activity	`GO:0004596` GO:0004596 is the molecular-function term for protein-N-terminal amino-acid acetyltransferase activity.

Discussions

CURATION_TODO (OPEN): Resolve exact source-neutral family groundings for the curated budding-yeast NatA constituents.

Evidence

GO:0031415 Gene Ontology cellular-component term for NatA complex and its exact N-terminal acetyltransferase A complex synonym.
GO:0031414 Gene Ontology cellular-component parent term for N-terminal protein acetyltransferase complexes.
GO:0004596 Gene Ontology molecular-function term for protein-N-terminal amino-acid acetyltransferase activity.
PMID:12890471 PubMed identifier for Polevoda and Sherman 2003, the eukaryotic N-terminal acetyltransferase subunit review cited by GO:0031415.
DOI:10.1016/s0006-291x(03)01316-0 DOI for Polevoda and Sherman 2003, 'Composition and function of the eukaryotic N-terminal acetyltransferase subunits', verified through NCBI E-utilities.
PMID:14517307 PubMed identifier for Gautschi et al. 2003, the ribosome-associated budding-yeast NatA composition paper.
DOI:10.1128/MCB.23.20.7403-7414.2003 DOI for Gautschi et al. 2003, 'The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides', verified through NCBI E-utilities.

Curation history

2026-09-26T08:45:47Z unknown · CREATED_RECORD — Scaffolded by scripts/new_record.py
2026-09-26T08:46:44Z codex · EXPANDED_RECORD — Added NatA exact synonymy, N-terminal protein acetyltransferase parentage, three budding-yeast constituent rows, yeast scope, protein-N-terminal acetyltransferase function, GO/PubMed/DOI evidence, a nonmechanistic function graph, and a subunit-grounding TODO.
2026-09-26T08:47:18Z codex · NORMALIZED_RECORD — Re-emitted repeated NatA evidence entries without YAML aliases.
2026-09-26T09:00:29Z codex · EDITED_RECORD — Resolved PR #1626 review issue #1627 by narrowing the NatA subunit-grounding TODO so it no longer asserts unsupported Naa-family aliases.

Source: data/structures/other/nata_complex.yaml