ARG5,6/YER069W Summary Help

Standard Name ARG5,6
Systematic Name YER069W
Feature Type ORF, Verified
Description Acetylglutamate kinase and N-acetyl-gamma-glutamyl-phosphate reductase; N-acetyl-L-glutamate kinase (NAGK) catalyzes the 2nd and N-acetyl-gamma-glutamyl-phosphate reductase (NAGSA), the 3rd step in arginine biosynthesis; synthesized as a precursor which is processed in the mitochondrion to yield mature NAGK and NAGSA; enzymes form a metabolon complex with Arg2p; NAGK C-terminal domain stabilizes the enzymes, slows catalysis and is involved in feed-back inhibition by arginine (1, 2, 3, 4 and see Summary Paragraph)
Name Description ARGinine requiring
Chromosomal Location
ChrV:295410 to 298001 | ORF Map | GBrowse
Genetic position: 55 cM
Gene Ontology Annotations All ARG5,6 GO evidence and references
  View Computational GO annotations for ARG5,6
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 13 genes
Classical genetics
Large-scale survey
16 total interaction(s) for 14 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 9
  • Affinity Capture-RNA: 1

Genetic Interactions
  • Dosage Rescue: 1
  • Negative Genetic: 1
  • Synthetic Growth Defect: 1
  • Synthetic Lethality: 3

Expression Summary
Length (a.a.) 863
Molecular Weight (Da) 94,868
Isoelectric Point (pI) 8.4
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrV:295410 to 298001 | ORF Map | GBrowse
Genetic position: 55 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..2592 295410..298001 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000000871

ARG5,6 encodes the mitochondrial matrix enzymes acetylglutamate kinase and N-acetyl-gamma-glutamyl-phosphate reductase (1, 5, 6). They catalyze the second and third steps, respectively, in the biosynthesis of ornithine (5, 6), an intermediate in arginine biosynthesis. Mutations in ARG5,6 therefore cause arginine auxotrophy (6). Arg5,6p is synthesized as a single translation product, and is subsequently processed in the mitochondria into two physically separable enzymes (1, 6). The kinase and reductase domains of the Arg5,6 polypeptide were identified by similarity to the ArgB and ArgC gene products from E. coli (7). The corresponding enzymes in S. pombe (8) and Candida albicans (9) are expressed as a single protein as in S. cerevisiae. Like other genes encoding arginine biosynthetic genes, ARG5,6 is transcriptionally repressed in the presence of arginine and is regulated by general amino acid control (10, 11, 12). Arginine-responsive transcription factors, including Arg80p, Arg81p, Arg82p, and Mcm1p, have been identified (10, 11, 12) and their target upstream activating sequences in ARG5,6 have been characterized (2, 13).

Last updated: 2005-02-08 Contact SGD

References cited on this page View Complete Literature Guide for ARG5,6
1) Boonchird C, et al.  (1991) Determination of amino acid sequences involved in the processing of the ARG5/ARG6 precursor in Saccharomyces cerevisiae. Eur J Biochem 199(2):325-35
2) Boonchird C, et al.  (1991) Characterization of the yeast ARG5,6 gene: determination of the nucleotide sequence, analysis of the control region and of ARG5,6 transcript. Mol Gen Genet 226(1-2):154-66
3) Abadjieva A, et al.  (2001) A new yeast metabolon involving at least the two first enzymes of arginine biosynthesis: acetylglutamate synthase activity requires complex formation with acetylglutamate kinase. J Biol Chem 276(46):42869-80
4) de Cima S, et al.  (2012) Insight on an arginine synthesis metabolon from the tetrameric structure of yeast acetylglutamate kinase. PLoS One 7(4):e34734
5) Jauniaux JC, et al.  (1978) Arginine metabolism in Saccharomyces cerevisiae: subcellular localization of the enzymes. J Bacteriol 133(3):1096-1107
6) Minet M, et al.  (1979) Organization and expression of a two-gene cluster in the arginine biosynthesis of Saccharomyces cerevisiae. Mol Gen Genet 168(3):299-308
7) Parsot C, et al.  (1988) Nucleotide sequence of Escherichia coli argB and argC genes: comparison of N-acetylglutamate kinase and N-acetylglutamate-gamma-semialdehyde dehydrogenase with homologous and analogous enzymes. Gene 68(2):275-83
8) Van Huffel C, et al.  (1992) Cloning and sequencing of arg3 and arg11 genes of Schizosaccharomyces pombe on a 10-kb DNA fragment. Heterologous expression and mitochondrial targeting of their translation products. Eur J Biochem 205(1):33-43
9) Negredo A, et al.  (1997) Cloning, analysis and one-step disruption of the ARG5,6 gene of Candida albicans. Microbiology 143 ( Pt 2)():297-302
10) Messenguy F  (1987) Multiplicity of regulatory mechanisms controlling amino acid biosynthesis in Saccharomyces cerevisiae. Microbiol Sci 4(5):150-3
11) Messenguy F and Dubois E  (1993) Genetic evidence for a role for MCM1 in the regulation of arginine metabolism in Saccharomyces cerevisiae. Mol Cell Biol 13(4):2586-92
12) Hinnebusch A  (1992) "General and Pathway-specific Regulatory Mechanisms Controlling the Synthesis of Amino Acid Biosynthetic Enzymes in Saccharomyces cerevisiae". Pp. 319-414 in The Molecular and Cellular Biology of the Yeast Saccharomyces: Gene Expression, edited by Jones EW, Pringle JR and Broach JR. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
13) De Rijcke M, et al.  (1992) Characterization of the DNA target site for the yeast ARGR regulatory complex, a sequence able to mediate repression or induction by arginine. Mol Cell Biol 12(1):68-81