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URH1

S. cerevisiae

trifunctional uridine nucleosidase/nicotinamide riboside hydrolase/nicotinic acid riboside hydrolase

What the model saw

Gene: URH1
Organism: Saccharomyces cerevisiae
Known functions: trifunctional uridine nucleosidase/nicotinamide riboside hydrolase/nicotinic acid riboside hydrolase. hydrolase activity, hydrolyzing N-glycosyl compounds. nicotinamide riboside hydrolase activity. nicotinic acid riboside hydrolase activity. purine nucleosidase activity. ribosylpyrimidine nucleosidase activity. uridine nucleosidase activity.
View unredacted entry
trifunctional uridine nucleosidase/nicotinamide riboside hydrolase/nicotinic acid riboside hydrolase. hydrolase activity, hydrolyzing N-glycosyl compounds. nicotinamide riboside hydrolase activity. nicotinic acid riboside hydrolase activity. purine nucleosidase activity. ribosylpyrimidine nucleosidase activity. uridine nucleosidase activity.

Solver output

Predicted influence
Anti-longevity
Confidence
72%
Mechanism
Deregulated nutrient sensing
Reasoning

URH1 encodes a trifunctional nucleosidase with nicotinamide riboside (NR) hydrolase activity, meaning it cleaves NR into nicotinamide and ribose, thereby degrading a key NAD+ precursor. NAD+ is a central metabolite in the Sir2/sirtuin deacetylase pathway, which is a major pro-longevity axis in yeast. By catabolizing NR before it can be salvaged into NAD+, URH1 reduces the intracellular NAD+ pool available to Sir2 (SIRT1 ortholog), dampening sirtuin-dependent longevity signaling. Consistent with this, deletion of URH1 in yeast has been shown to elevate NR-derived NAD+ levels and extend replicative lifespan. The nicotinic acid riboside hydrolase activity similarly degrades another NAD+ precursor, compounding the anti-longevity effect through depletion of the NAD+ salvage pathway.

Key pathways
NAD+ salvage pathwaySir2/sirtuin deacetylase signalingnicotinamide riboside catabolism
Longevity influence
Anti-longevity
Lifespan effect
Increase

GenAge curators classify each gene's normal function as promoting (Pro-Longevity) or opposing (Anti-Longevity) longevity, based on synthesis across studies. Loss-of-function effects can vary from this depending on the manipulation.

Advisor judgment

Answer
Correct
Mechanism
Correct
Reasoning quality
5/5
Failure mode
Correct
Notes

The model correctly predicted anti_longevity for URH1. The mechanistic reasoning is well-grounded: URH1 hydrolyzes nicotinamide riboside (NR), depleting a key NAD+ precursor, which reduces NAD+ availability for Sir2/sirtuin-dependent longevity signaling. The model correctly notes that URH1 deletion elevates NR-derived NAD+ and extends replicative lifespan, which is consistent with published literature (e.g., Belenky et al. work on NR and NAD+ salvage in yeast). The confidence level of 0.72 is appropriate given the specificity of the functional annotation. Overall, both the answer and the mechanistic reasoning are correct and well-articulated.

Raw API responses

solver

{
  "reasoning": "URH1 encodes a trifunctional nucleosidase with nicotinamide riboside (NR) hydrolase activity, meaning it cleaves NR into nicotinamide and ribose, thereby degrading a key NAD+ precursor. NAD+ is a central metabolite in the Sir2/sirtuin deacetylase pathway, which is a major pro-longevity axis in yeast. By catabolizing NR before it can be salvaged into NAD+, URH1 reduces the intracellular NAD+ pool available to Sir2 (SIRT1 ortholog), dampening sirtuin-dependent longevity signaling. Consistent with this, deletion of URH1 in yeast has been shown to elevate NR-derived NAD+ levels and extend replicative lifespan. The nicotinic acid riboside hydrolase activity similarly degrades another NAD+ precursor, compounding the anti-longevity effect through depletion of the NAD+ salvage pathway.",
  "confidence": 0.72,
  "key_pathways": [
    "NAD+ salvage pathway",
    "Sir2/sirtuin deacetylase signaling",
    "nicotinamide riboside catabolism"
  ],
  "mechanism_class": "deregulated_nutrient_sensing",
  "longevity_influence": "anti_longevity"
}

advisor

{
  "notes": "The model correctly predicted anti_longevity for URH1. The mechanistic reasoning is well-grounded: URH1 hydrolyzes nicotinamide riboside (NR), depleting a key NAD+ precursor, which reduces NAD+ availability for Sir2/sirtuin-dependent longevity signaling. The model correctly notes that URH1 deletion elevates NR-derived NAD+ and extends replicative lifespan, which is consistent with published literature (e.g., Belenky et al. work on NR and NAD+ salvage in yeast). The confidence level of 0.72 is appropriate given the specificity of the functional annotation. Overall, both the answer and the mechanistic reasoning are correct and well-articulated.",
  "failure_mode": "correct",
  "answer_correct": true,
  "mechanism_correct": true,
  "reasoning_quality": 5,
  "ground_truth_questionable": false
}