| General Information |
| MoonProt ID | 113 |
| First appeared in release | 1.0 |
| Name(s) | Arg5,6p
N-Acetylglutamate kinase (Arg5)and N-acetylglutamyl-phosphate reductase (Arg6)
**Note this is considered a moonlighting protein not because of the two enzyme activities but because it is both an enzyme and a transcription factor***
Protein ARG5,6, mitochondrial
N-acetyl-glutamate semialdehyde dehydrogenase
NAGSA dehydrogenase
N-acetyl-L-glutamate 5-phosphotransferase
NAG kinase
AGK
Gene Name: ARG5,6
|
| UniProt ID | Q01217 (ARG56_YEAST), Reviewed |
| GO terms | GO:0006355 regulation of transcription, DNA-templated
GO:0006526 arginine biosynthetic process
GO:0006592 ornithine biosynthetic process
GO:0008152 metabolic process
GO:0008652 cellular amino acid biosynthetic process
GO:0016310 phosphorylation
GO:0055114 oxidation-reduction process
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0003942 N-acetyl-gamma-glutamyl-phosphate reductase activity GO:0003991 acetylglutamate kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0016491 oxidoreductase activity
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
GO:0016740 transferase activity
GO:0046983 protein dimerization activity
GO:0051287 NAD binding
GO:0005737 cytoplasm
GO:0005739 mitochondrion |
| Organisms for which functions have been demonstrated | Saccharomyces cerevisiae |
| Sequence length | 863 |
| FASTA sequence | >sp|Q01217|ARG56_YEAST Protein ARG5,6, mitochondrial OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=ARG5,6 PE=1 SV=1
MPSASLLVSTKRLNASKFQKFVSSLNKSTIAGFASVPLRAPPSVAFTRKKVGYSKRYVSSTNGFSATRSTVIQLLNNISTKREVEQYLKYFTSVSQQQFAVIKVGGAIISDNLHELASCLAFLYHVGLYPIVLHGTGPQVNGRLEAQGIEPDYIDGIRITDEHTMAVVRKCFLEQNLKLVTALEQLGVRARPITSGVFTADYLDKDKYKLVGNIKSVTKEPIEASIKAGALPILTSLAETASGQMLNVNADVAAGELARVFEPLKIVYLNEKGGIINGSTGEKISMINLDEEYDDLMKQSWVKYGTKLKIREIKELLDYLPRSSSVAIINVQDLQKELFTDSGAGTMIRRGYKLVKRSSIGEFPSADALRKALQRDAGISSGKESVASYLRYLENSDFVSYADEPLEAVAIVKKDTNVPTLDKFVCSDAAWLNNVTDNVFNVLRRDFPALQWVVSENDANIAWHFDKSQGSYLKGGKVLFWYGIDDINTISELVENFVKSCDTASTLNSSASSGVFANKKSARSYSTRSTPRPEGVNTNPGRVALIGARGYTGKNLVSLINGHPYLEVAHVSSRELKGQKLQDYTKSEIIYESLQIQDIRKLEEQNAVDFWVMALPNKVCEPFVETIQSVHGKSKIIDLSADHRFVSESDWAYGLPELNDRAKIANAAKIANPGCYATGSQLTISPLTKYINGLPTVFGVSGYSGAGTKPSPKNDPKFLNNNLIPYALSDHIHEREISARIGHNVAFMPHVGQWFQGISLTVSIPIKKGSLSIDEIRKLYRNFYEDEKLVHVIDDIPLVKDIEGTHGVVIGGFKLNDAEDRVVVCATIDNLLKGAATQCLQNINLAMGYGEYAGIPENKIIGV
|
| Structure Information |
| PDB ID | 3ZZI 3ZZF |
| Quaternary structure | |
| SCOP | NA |
| CATH | 3.40.1160.10, 3.40.630.30 |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | Not in DisProt |
| Predicted Disorder Regions | 1-66, 380-383, 496-453, 861-863 |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | enzyme in the arginine biosynthetic pathway
N-acetyl-gamma phosphate reductase and acetyl glutamate kinase |
| References for function | Determination of amino acid sequences involved in the processing of the ARG5/ARG6 precursor in Saccharomyces cerevisiae. Boonchird,C., Messenguy,F.,and Dubois,E. (1991) Eur. J. Biochem. 199, 325-335.PMID: 1649049
A new yeast metabolon involving at least the two first enzymes of arginine biosynthesis A. Abadjieva, K. Pauwels, P. Hilven, and M. Crabeel.J Biol Chem. 2001 Nov 16;276(46):42869-80. Epub 2001 Sep 11.
PMID: 11553611
|
| E.C. number | EC 2.7.2.8 and EC 1.2.1.38 |
| Location of functional site(s) | |
| Cellular location of function | mitochondria |
| Comments | |
| Function 2 |
| Function description | Arg5 binds to mitochondrial and nuclear DNA in vivo and regulates gene expression, regulator of transcription for several genes |
| References for function | Regulation of gene expression by a metabolic enzyme. Hall DA, Zhu H, Zhu X, Royce T, Gerstein M, Snyder M. Science. 2004 Oct 15; 306(5695): 482-4. PMID: 15486299
|
| E.C. number | N/A |
| Location of functional site(s) | |
| Cellular location of function | nucleus and mitochondria |
| Comments | |