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SNZ1 protein (Saccharomyces cerevisiae) - STRING interaction network
"SNZ1" - Protein involved in vitamin B6 biosynthesis in Saccharomyces cerevisiae
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proteins of unknown 3D structure
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experimentally determined
Predicted Interactions
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gene co-occurrence
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textmining
co-expression
protein homology
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SNZ1Protein 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)    
Predicted Functional Partners:
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
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
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)
     
  0.978
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)
   
 
0.973
PRO1
Gamma-glutamyl kinase, catalyzes the first step in proline biosynthesis; Catalyzes the transfer of a phosphate group to glutamate to form glutamate 5-phosphate which rapidly cyclizes to 5- oxoproline (428 aa)
         
  0.961
SNZ3
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 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)
   
 
0.959
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)
     
  0.920
SNF12
73 kDa subunit of the SWI/SNF chromatin remodeling complex involved in transcriptional regulation; homolog of Rsc6p subunit of the RSC chromatin remodeling complex; deletion mutants are temperature-sensitive; Involved in transcriptional activation. Component of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, which is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitatin [...] (566 aa)
           
  0.906
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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