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SNZ3 protein (Saccharomyces cerevisiae) - STRING interaction network
"SNZ3" - Member of a stationary phase-induced gene family in Saccharomyces cerevisiae
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SNZ3Member of a stationary phase-induced gene family; transcription of SNZ2 is induced prior to diauxic shift, and also in the absence of thiamin in a Thi2p-dependent manner; forms a coregulated gene pair with SNO3; Catalyzes the formation of pyridoxal 5’-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by a SNO isoform. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively (298 aa)    
Predicted Functional Partners:
SNO2
Protein of unknown function, nearly identical to Sno3p; expression is induced before the diauxic shift and also in the absence of thiamin; Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5’-phosphate. The resulting ammonia molecule is channeled to the active site of a SNZ isoform (222 aa)
 
  0.999
SNO3
Protein of unknown function, nearly identical to Sno2p; expression is induced before the diauxic shift and also in the absence of thiamin; Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5’-phosphate. The resulting ammonia molecule is channeled to the active site of a SNZ isoform (222 aa)
 
  0.999
SNO1
Protein of unconfirmed function, involved in pyridoxine metabolism; expression is induced during stationary phase; forms a putative glutamine amidotransferase complex with Snz1p, with Sno1p serving as the glutaminase; Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5’-phosphate. The resulting ammonia molecule is channeled to the active site of a SNZ isoform (224 aa)
 
  0.999
SNZ2
Member of a stationary phase-induced gene family; transcription of SNZ2 is induced prior to diauxic shift, and also in the absence of thiamin in a Thi2p-dependent manner; forms a coregulated gene pair with SNO2; interacts with Thi11p; Catalyzes the formation of pyridoxal 5’-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by a SNO isoform. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively (298 aa)
   
0.996
SNZ1
Protein involved in vitamin B6 biosynthesis; member of a stationary phase-induced gene family; coregulated with SNO1; interacts with Sno1p and with Yhr198p, perhaps as a multiprotein complex containing other Snz and Sno proteins; Catalyzes the formation of pyridoxal 5’-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by a SNO isoform. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively (297 aa)
   
 
0.959
BUD16
Putative pyridoxal kinase, a key enzyme involved in pyridoxal 5’-phosphate synthesis, the active form of vitamin B6; required for genome integrity; involved in bud-site selection; similarity to yeast BUD17 and human pyridoxal kinase (PDXK); Required for synthesis of pyridoxal-5-phosphate from vitamin B6 (By similarity). Important for bud site selection (312 aa)
       
  0.947
BUD17
Putative pyridoxal kinase, a key enzyme in vitamin B6 metabolism; involved in bud-site selection; diploid mutants display a random rather than a bipolar budding pattern; similarity to yeast BUD16 and human pyridoxal kinase (PDXK); Required for synthesis of pyridoxal-5-phosphate from vitamin B6 (By similarity). Important for bud site selection (317 aa)
       
  0.939
PDX3
Pyridoxine (pyridoxamine) phosphate oxidase, has homologs in E. coli and Myxococcus xanthus; transcription is under the general control of nitrogen metabolism; Catalyzes the oxidation of either pyridoxine 5’- phosphate (PNP) or pyridoxamine 5’-phosphate (PMP) into pyridoxal 5’-phosphate (PLP) (228 aa)
       
  0.916
THI20
Trifunctional enzyme of thiamine biosynthesis, degradation and salvage; has hydroxymethylpyrimidine (HMP) kinase, HMP-phosphate (HMP-P) kinase and thiaminase activities; member of a gene family with THI21 and THI22; HMP and HMP-P kinase activity red /.../ with Thi21p; Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and also probably that of HMP to HMP- P (551 aa)
         
  0.704
SOR1
Sorbitol dehydrogenase; expression is induced in the presence of sorbitol or xylose (357 aa)
           
  0.698
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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