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ALD2 protein (Saccharomyces cerevisiae) - STRING interaction network
"ALD2" - Cytoplasmic aldehyde dehydrogenase, involved in ethanol oxidation and beta-alanine biosynthesis in Saccharomyces cerevisiae
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Known Interactions
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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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ALD2Cytoplasmic 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)    
Predicted Functional Partners:
ACS1
Acetyl-coA synthetase isoform which, along with Acs2p, is the nuclear source of acetyl-coA for histone acetylation; expressed during growth on nonfermentable carbon sources and under aerobic conditions; Catalyzes the production of acetyl-CoA. Provides the acetyl-CoA source for histone acetylation in the nucleus. "Aerobic" isozyme of acetyl-coenzyme A synthetase, which supports growth on nonfermentable carbon sources such as glycerol and ethanol. May be required for assimilation of ethanol and acetate (713 aa)
   
 
  0.987
UGA1
Gamma-aminobutyrate (GABA) transaminase (4-aminobutyrate aminotransferase) involved in the 4-aminobutyrate and glutamate degradation pathways; required for normal oxidative stress tolerance and nitrogen utilization; Required for the degradation of gamma-aminobutyric acid (GABA), which is important for utilization of GABA as nitrogen source and for oxidative stress tolerance. Deaminates GABA to succinate semialdehyde, which in turn is converted to succinate by the succinate-semialdehyde dehydrogenase UGA2. Cannot transaminate beta-alanine (BAL) (471 aa)
 
  0.985
ACS2
Acetyl-coA synthetase isoform which, along with Acs1p, is the nuclear source of acetyl-coA for histone acetylation; mutants affect global transcription; required for growth on glucose; expressed under anaerobic conditions; Catalyzes the production of acetyl-CoA. Provides the acetyl-CoA source for histone acetylation in the nucleus. "Anaerobic" isozyme of acetyl-coenzyme A synthetase, which is required for growth on fermentable carbon sources such as glucose. May be involved in the PDH (pyruvate dehydrogenase complex) bypass (683 aa)
   
 
  0.984
ADH2
Glucose-repressible alcohol dehydrogenase II, catalyzes the conversion of ethanol to acetaldehyde; involved in the production of certain carboxylate esters; regulated by ADR1; This isozyme preferentially catalyzes the conversion of ethanol to acetaldehyde. Acts on a variety of primary unbranched aliphatic alcohols (348 aa)
   
 
  0.984
ADH1
Alcohol dehydrogenase, fermentative isozyme active as homo- or heterotetramers; required for the reduction of acetaldehyde to ethanol, the last step in the glycolytic pathway; This isozyme preferentially catalyzes the conversion of primary unbranched alcohols to their corresponding aldehydes. Also also shows activity toward secondary alcohols (348 aa)
   
 
  0.982
ADH3
Mitochondrial alcohol dehydrogenase isozyme III; involved in the shuttling of mitochondrial NADH to the cytosol under anaerobic conditions and ethanol production (375 aa)
   
 
  0.982
ADH4
Alcohol dehydrogenase isoenzyme type IV, dimeric enzyme demonstrated to be zinc-dependent despite sequence similarity to iron-activated alcohol dehydrogenases; transcription is induced in response to zinc deficiency; Reduces acetaldehyde to ethanol during glucose fermentation. Specific for ethanol. Shows drastically reduced activity towards primary alcohols from 4 carbon atoms upward. Isomers of aliphatic alcohol, as well as secondary alcohols and glycerol are not used at all (382 aa)
 
 
  0.981
PDC1
Major of three pyruvate decarboxylase isozymes, key enzyme in alcoholic fermentation, decarboxylates pyruvate to acetaldehyde; subject to glucose-, ethanol-, and autoregulation; involved in amino acid catabolism; Major 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 decar [...] (563 aa)
     
 
  0.979
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; Oxidizes long-chain alcohols and, in the presence of glutathione, is able to oxidize formaldehyde. Is responsible for yeast resistance to formaldehyde (386 aa)
   
  0.979
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)
     
 
  0.977
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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