PGA3 protein (Saccharomyces cerevisiae) - STRING interaction network
"PGA3" - Putative cytochrome b5 reductase, localized to the plasma membrane in Saccharomyces cerevisiae
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Known Interactions
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Predicted Interactions
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Gene Fusion
PGA3Putative 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)    
Predicted Functional Partners:
Cytochrome b5, involved in the sterol and lipid biosynthesis pathways; acts as an electron donor to support sterol C5-6 desaturation; Membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases. It plays a role in fatty-acid desaturation and is also involved in several steps of the sterol biosynthesis pathway, particularly in the 4- demethylation of the 4,4’-dimethyl zymosterol (120 aa)
Dihydroorotate 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)
NAD(+)-dependent glutamate synthase (GOGAT), synthesizes glutamate from glutamine and alpha-ketoglutarate; with Gln1p, forms the secondary pathway for glutamate biosynthesis from ammonia; expression regulated by nitrogen source; Forms L-glutamate from L-glutamine and 2-oxoglutarate. Represents an alternative pathway to L-glutamate dehydrogenase for the biosynthesis of L-glutamate. Participates with glutamine synthetase in ammonia assimilation processes. The enzyme is specific for NADH, L-glutamine and 2-oxoglutarate (2145 aa)
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)
Sulfite reductase beta subunit, involved in amino acid biosynthesis, transcription repressed by methionine; Catalyzes the reduction of sulfite to sulfide, one of several activities required for the biosynthesis of L-cysteine from sulfate (1442 aa)
Oxidoreductase of the mitochondrial inner membrane, involved in cytoplasmic and mitochondrial iron homeostasis and required for activity of Fe-S cluster-containing enzymes; one of the few mitochondrial proteins essential for viability (493 aa)
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)
Cytochrome b reductase; not essential for viability; also detected in mitochondria; mutation in conserved NADH binding domain of the human ortholog results in type I methemoglobinemia; Electron donor reductase for cytochrome b5. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes. Plays a role in bud morphology (284 aa)
C-24(28) sterol reductase, catalyzes the final step in ergosterol biosynthesis; mutants are viable, but lack ergosterol (473 aa)
Delta(9) fatty acid desaturase, required for monounsaturated fatty acid synthesis and for normal distribution of mitochondria; Stearyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates (PubMed-1978720, PubMed-7947684). Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA (PubMed-1978720). Required for the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides (PubMed-1978720, Pu [...] (510 aa)
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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