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NTA1 protein (Saccharomyces cerevisiae) - STRING interaction network
"NTA1" - Amidase, removes the amide group from N-terminal asparagine and glutamine residues to generate proteins with N-terminal aspartate and glutamate residues that are targets of ubiquitin-mediated degradation in Saccharomyces cerevisiae
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Predicted Interactions
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textmining
co-expression
protein homology
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NTA1Amidase, removes the amide group from N-terminal asparagine and glutamine residues to generate proteins with N-terminal aspartate and glutamate residues that are targets of ubiquitin-mediated degradation; Deamidates N-terminal Asn and Gln. Component of a targeting complex in the N-end rule pathway (457 aa)    
Predicted Functional Partners:
CPS1
Vacuolar carboxypeptidase S; expression is induced under low-nitrogen conditions; Necessary for use of certain peptides as sole nitrogen source. May also cleave intracellularly generated peptides to recycle amino acids for protein synthesis (576 aa)
       
  0.812
URA2
Bifunctional carbamoylphosphate synthetase/aspartate transcarbamylase; catalyzes the first two enzymatic steps in the de novo biosynthesis of pyrimidines; both activities are subject to feedback inhibition by UTP; This protein is a "fusion" protein encoding three enzymatic activities of the pyrimidine pathway (GATase, CPSase, and ATCase) (2214 aa)
   
 
  0.802
NMA1
Nicotinic acid mononucleotide adenylyltransferase, involved in pathways of NAD biosynthesis, including the de novo, NAD(+) salvage, and nicotinamide riboside salvage pathways; Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate to form deamido- NAD(+) (NaAD). Key enzyme in both de novo and salvage pathways for NAD(+) biosynthesis. Predominantly acts in the salvage pathways via NMN (401 aa)
       
  0.797
NMA2
Nicotinic acid mononucleotide adenylyltransferase, involved in de novo and salvage synthesis of NAD(+); Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP (PubMed-12597897). Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate to form deamido-NAD(+) (NaAD). Key enzyme in both de novo and salvage pathways for NAD(+) biosynthesis (By similarity). Predominantly acts in the salvage pathways via NMN (PubMed-11884393) (395 aa)
       
  0.797
NPT1
Nicotinate phosphoribosyltransferase, acts in the salvage pathway of NAD+ biosynthesis; required for silencing at rDNA and telomeres and has a role in silencing at mating-type loci; localized to the nucleus; Essential for growth under anaerobic conditions (429 aa)
   
 
  0.796
ATE1
Arginyl-tRNA-protein transferase, catalyzes post-translational conjugation of arginine to the amino termini of acceptor proteins which are then subject to degradation via the N-end rule pathway; Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway. Does not arginylate cysteine residues (By similarity) (503 aa)
           
  0.793
AMD2
Putative amidase (549 aa)
       
  0.785
DUR1,2
Urea amidolyase, contains both urea carboxylase and allophanate hydrolase activities, degrades urea to CO2 and NH3; expression sensitive to nitrogen catabolite repression and induced by allophanate, an intermediate in allantoin degradation; Hydrolysis of urea to ammonia and CO(2) (1835 aa)
       
  0.782
OXP1
5-oxoprolinase; enzyme is ATP-dependent and functions as a dimer; similar to mouse Oplah gene; green fluorescent protein (GFP)-fusion protein localizes to the cytoplasm; Catalyzes the cleavage of 5-oxo-L-proline to form L- glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate (1286 aa)
   
 
  0.772
URA6
Uridylate kinase, catalyzes the seventh enzymatic step in the de novo biosynthesis of pyrimidines, converting uridine monophosphate (UMP) into uridine-5’-diphosphate (UDP); Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and dUMP as phosphate acceptors, but can also use CMP, dCMP, AMP, GMP, dGMP and dTMP. ATP and dATP are the best phosphate donors, but can also use GTP, dGTP, dCTP, and dTTP to some degree (204 aa)
       
 
  0.760
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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