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SFA1 protein (Saccharomyces cerevisiae) - STRING interaction network
"SFA1" - Bifunctional enzyme containing both alcohol dehydrogenase and glutathione-dependent formaldehyde dehydrogenase activities, functions in formaldehyde detoxification and formation of long chain and complex alcohols, regulated by Hog1p-Sko1p in Saccharomyces cerevisiae
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Predicted Interactions
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SFA1Bifunctional enzyme containing both alcohol dehydrogenase and glutathione-dependent formaldehyde dehydrogenase activities, functions in formaldehyde detoxification and formation of long chain and complex alcohols, regulated by Hog1p-Sko1p; Oxidizes long-chain alcohols and, in the presence of glutathione, is able to oxidize formaldehyde. Is responsible for yeast resistance to formaldehyde (386 aa)    
Predicted Functional Partners:
YJL068C
Non-essential intracellular esterase that can function as an S-formylglutathione hydrolase; may be involved in the detoxification of formaldehyde, which can be metabolized to S-formylglutathione; similar to human esterase D; Serine hydrolase involved in the detoxification of formaldehyde (299 aa)
  0.999
ALD6
Cytosolic aldehyde dehydrogenase, activated by Mg2+ and utilizes NADP+ as the preferred coenzyme; required for conversion of acetaldehyde to acetate; constitutively expressed; locates to the mitochondrial outer surface upon oxidative stress; Cytosolic aldehyde dehydrogenase which utilizes NADP+ as the preferred coenzyme. Performs the conversion of acetaldehyde to acetate (500 aa)
   
  0.980
ALD2
Cytoplasmic aldehyde dehydrogenase, involved in ethanol oxidation and beta-alanine biosynthesis; uses NAD+ as the preferred coenzyme; expression is stress induced and glucose repressed; very similar to Ald3p; Cytoplasmic aldehyde dehydrogenase involved in ethanol oxidation. Required for pantothenic acid production through the conversion of 3-aminopropanal to beta-alanine, an intermediate in pantothenic acid (vitamin B5) and coenzyme A (CoA) biosynthesis (506 aa)
   
  0.979
ALD3
Cytoplasmic aldehyde dehydrogenase, involved in beta-alanine synthesis; uses NAD+ as the preferred coenzyme; very similar to Ald2p; expression is induced by stress and repressed by glucose; Cytoplasmic aldehyde dehydrogenase involved in ethanol oxidation. Involved in pantothenic acid production through the conversion of 3-aminopropanal to beta-alanine, an intermediate in pantothenic acid (vitamin B5) and coenzyme A (CoA) biosynthesis (506 aa)
   
  0.978
ALD4
Mitochondrial aldehyde dehydrogenase, required for growth on ethanol and conversion of acetaldehyde to acetate; phosphorylated; activity is K+ dependent; utilizes NADP+ or NAD+ equally as coenzymes; expression is glucose repressed; Potassium-activated aldehyde dehydrogenase involved in acetate formation during anaerobic growth on glucose (519 aa)
   
  0.977
ALD5
Mitochondrial aldehyde dehydrogenase, involved in regulation or biosynthesis of electron transport chain components and acetate formation; activated by K+; utilizes NADP+ as the preferred coenzyme; constitutively expressed; Minor mitochondrial aldehyde dehydrogenase isoform. Plays a role in regulation or biosynthesis of electron transport chain components. Involved in the biosynthesis of acetate during anaerobic growth on glucose (520 aa)
   
  0.976
PDC5
Minor isoform of pyruvate decarboxylase, key enzyme in alcoholic fermentation, decarboxylates pyruvate to acetaldehyde, regulation is glucose- and ethanol-dependent, repressed by thiamine, involved in amino acid catabolism; Second most abundant of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for biosynthetic pathways. The enzyme is also on [...] (563 aa)
         
  0.976
THI3
Probable alpha-ketoisocaproate decarboxylase, may have a role in catabolism of amino acids to long-chain and complex alcohols; required for expression of enzymes involved in thiamine biosynthesis; One of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) involved in amino acid catabolism. The enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids (alpha-keto-acids). In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its prefer [...] (609 aa)
         
  0.976
HFD1
Putative fatty aldehyde dehydrogenase, located in the mitochondrial outer membrane and also in lipid particles; has similarity to human fatty aldehyde dehydrogenase (FALDH) which is implicated in Sjogren-Larsson syndrome; Catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Responsible for conversion of the sphingosine 1-phosphate (S1P) degradation product hexadecenal to hexadecenoic acid (532 aa)
     
  0.975
PDC6
Minor isoform of pyruvate decarboxylase, decarboxylates pyruvate to acetaldehyde, involved in amino acid catabolism; transcription is glucose- and ethanol-dependent, and is strongly induced during sulfur limitation; Minor of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for biosynthetic pathways. The enzyme is also one of five 2-oxo acid de [...] (563 aa)
         
  0.973
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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