Primary Information |
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| BoMiProt ID | Bomi6037 |
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| Protein Name | Glutamine-dependent NAD(+) synthetase/NAD(+) synthetase |
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| Organism | Bos taurus |
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| Uniprot ID | Q3ZBF0 |
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| Milk Fraction | Exosomes |
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| Ref Sequence ID | NP_001029615.1 |
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| Aminoacid Length | 706 |
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| Molecular Weight | 79400 |
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| FASTA Sequence |
Download |
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| Gene Name | NADSYN1 |
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| Gene ID | 513400 |
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| Protein Existence Status | Reviewed |
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Secondary Information |
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| Presence in other biological fluids/tissue/cells | pituitary gland |
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| Protein Function | NAD(+) synthetase catalyzes the formation of NAD(+) from ATP, nicotinic acid adenine dinucleotide and ammonia. Glutamine-dependent NAD(+) synthetase obtains ammonia through the hydrolysis of glutamine to glutamate, which takes place in the glutaminase domain. |
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| Biochemical Properties | Glutamine-dependent NAD(+) synthetase, Qns1, utilizes a glutamine aminotransferase domain to supply ammonia for amidation of nicotinic acid adenine dinucleotide (NaAD(+)) to NAD(+). |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| NA |
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| Predicted Disorder Regions | 700-706 |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Additional Comments | Six distinct classes of Qns1 mutants that fall within the glutaminase domain and the synthetase domain selectively inhibit components of the coordinated reaction. |
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| Bibliography | 1.Resto M, Yaffe J, Gerratana B. An ancestral glutamine-dependent NAD(+) synthetase revealed by poor kinetic synergism. Biochim Biophys Acta. 2009 Nov;1794(11):1648-53. doi: 10.1016/j.bbapap.2009.07.014. Epub 2009 Aug 6. PMID: 19647806. 2.Wojcik M, Seidle HF, Bieganowski P, Brenner C. Glutamine-dependent NAD+ synthetase. How a two-domain, three-substrate enzyme avoids waste. J Biol Chem. 2006 Nov 3;281(44):33395-402. doi: 10.1074/jbc.M607111200. Epub 2006 Sep 5. PMID: 16954203. |
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