NAGS1 N-acetyl-l-glutamate synthase 1 [Arabidopsis thaliana (thale cress)] - Gene

Summary

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Official Symbol: NAGS1
Official Full Name: N-acetyl-l-glutamate synthase 1
Primary source: TAIR:AT2G22910
Locus tag: AT2G22910
See related: Araport:AT2G22910
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Arabidopsis thaliana (ecotype: Columbia)
Lineage: Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis
Also known as: N-acetyl-l-glutamate synthase 1; T20K9.12; T20K9_12
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Genomic context

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See NAGS1 in Genome Data Viewer

Location:: chromosome: 2

Exon count:: 9

Sequence:: Chromosome: 2; NC_003071.7 (9749857..9753103)

Chromosome 2 - NC_003071.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_003071.7

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Tomata SlNAGS1 accumulation patterns suggest a possible role of this gene in hypoxia-induced responses. The 35S::SlNAGS1 Arabidopsis plants accumulated ornithine at high levels and exhibited increased tolerance to salt and drought stresses. [NAGS1]
Title: Can ornithine accumulation modulate abiotic stress tolerance in Arabidopsis?

Submit: New GeneRIF Correction

Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

MASC_STS17512 (e-PCR)
- UniSTS:258964

NM_127856.4

Supported by ESTs:

Gene Ontology Provided by TAIR

Function	Evidence Code	Pubs
enables L-glutamate N-acetyltransferase activity	IEA Inferred from Electronic Annotation more info
enables L-methionine N-acyltransferase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in L-arginine biosynthetic process	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in cytoplasm	ISM Inferred from Sequence Model more info

General protein information

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Preferred Names: N-acetyl-l-glutamate synthase 1

NP_179875.2

N-acetyl-l-glutamate synthase 1 (NAGS1); FUNCTIONS IN: acetyl-CoA:L-glutamate N-acetyltransferase activity, N-acetyltransferase activity; INVOLVED IN: cellular amino acid biosynthetic process, arginine biosynthetic process, metabolic process; LOCATED IN: cytoplasm; EXPRESSED IN: 23 plant structures; EXPRESSED DURING: 13 growth stages; CONTAINS InterPro DOMAIN/s: GCN5-related N-acetyltransferase, C-terminal (InterPro:IPR022610), GCN5-related N-acetyltransferase (InterPro:IPR000182), Aspartate/glutamate/uridylate kinase (InterPro:IPR001048), Acyl-CoA N-acyltransferase (InterPro:IPR016181), Amino-acid N-acetyltransferase (ArgA) (InterPro:IPR010167); BEST Arabidopsis thaliana protein match is: N-acetyl-l-glutamate synthase 2 (TAIR:AT4G37670.2); Has 7959 Blast hits to 6500 proteins in 1789 species: Archae - 144; Bacteria - 6363; Metazoa - 2; Fungi - 138; Plants - 156; Viruses - 0; Other Eukaryotes - 1156 (source: NCBI BLink).

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_003071.7 Reference assembly

Range

9749857..9753103

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_127856.4 → NP_179875.2 N-acetyl-l-glutamate synthase 1 [Arabidopsis thaliana]

See identical proteins and their annotated locations for NP_179875.2

Status: REVIEWED

UniProtKB/Swiss-Prot

O81008, Q84JF4

UniProtKB/TrEMBL

A0A654EWR1

Conserved Domains (3) summary

PLN02825
Location:77 → 593

PLN02825; amino-acid N-acetyltransferase

COG1246
Location:449 → 593

ArgA; N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]

cd04237
Location:76 → 440

AAK_NAGS-ABP; AAK_NAGS-ABP: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the arginine-biosynthesis pathway (ABP) found in gamma- and beta-proteobacteria and higher plant chloroplasts. Domain architecture of these NAGS consisted of an ...