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URA1 protein (Saccharomyces cerevisiae) - STRING interaction network
"URA1" - Dihydroorotate dehydrogenase, catalyzes the fourth enzymatic step in the de novo biosynthesis of pyrimidines, converting dihydroorotic acid into orotic acid in Saccharomyces cerevisiae
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Predicted Interactions
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protein homology
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URA1Dihydroorotate dehydrogenase, catalyzes the fourth enzymatic step in the de novo biosynthesis of pyrimidines, converting dihydroorotic acid into orotic acid; Catalyzes the conversion of dihydroorotate to orotate with fumarate as the electron acceptor. Molecular oxygen can replace fumarate in vitro. Does not use oxaloacetate or NAD or NADP as electron acceptors (314 aa)    
Predicted Functional Partners:
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)
   
  0.999
URA4
Dihydroorotase, catalyzes the third enzymatic step in the de novo biosynthesis of pyrimidines, converting carbamoyl-L-aspartate into dihydroorotate (364 aa)
   
 
  0.999
URA5
Major orotate phosphoribosyltransferase (OPRTase) isozyme that catalyzes the fifth enzymatic step in de novo biosynthesis of pyrimidines, converting orotate into orotidine-5’-phosphate; minor OPRTase encoded by URA10; Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP) (226 aa)
   
 
  0.999
URA10
Minor orotate phosphoribosyltransferase (OPRTase) isozyme that catalyzes the fifth enzymatic step in the de novo biosynthesis of pyrimidines, converting orotate into orotidine-5’-phosphate; major OPRTase encoded by URA5; Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP) (227 aa)
   
 
  0.992
URA3
Orotidine-5’-phosphate (OMP) decarboxylase, catalyzes the sixth enzymatic step in the de novo biosynthesis of pyrimidines, converting OMP into uridine monophosphate (UMP); converts 5-FOA into 5-fluorouracil, a toxic compound (267 aa)
   
  0.988
DAL1
Allantoinase, converts allantoin to allantoate in the first step of allantoin degradation; expression sensitive to nitrogen catabolite repression; Utilization of purines as secondary nitrogen sources, when primary sources are limiting (460 aa)
   
  0.960
AIM33
Putative protein of unknown function, highly conserved across species and orthologous to human CYB5R4; null mutant displays reduced frequency of mitochondrial genome loss (312 aa)
     
  0.955
PGA3
Putative cytochrome b5 reductase, localized to the plasma membrane; may be involved in regulation of lifespan; required for maturation of Gas1p and Pho8p, proposed to be involved in protein trafficking; NADH-dependent cytochrome b5 reductase that reduces coenzyme Q6 at the plasma membrane and mediates lifespan extension by calorie restriction by shifting fermentative to respiratory metabolism, probably through modulating the NAD(+)/NADH ratio (312 aa)
     
  0.955
MCR1
Mitochondrial NADH-cytochrome b5 reductase, involved in ergosterol biosynthesis; The outer membrane form may mediate the reduction of outer membrane cytochrome b5, and the soluble inter-membrane space form may transfer electrons from external NADH to cytochrome c, thereby mediating an antimycin-insensitive, energy-coupled oxidation of external NADH by yeast mitochondria. Involved in the reduction of D-erythroascorbyl free radicals (302 aa)
     
  0.953
CYC2
Mitochondrial peripheral inner membrane protein, contains a FAD cofactor in a domain exposed in the intermembrane space; exhibits redox activity in vitro; likely participates in ligation of heme to acytochromes c and c1 (Cyc1p and Cyt1p); Redox component that participates in c-type cytochrome biogenesis in the mitochondrial intermembrane space. May play a role in the reduction of heme prior to its ligation to apocytochrome c by cytochrome c heme lyase. Has oxidoreductase activity in vitro (366 aa)
     
  0.951
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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