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HEM4 protein (Saccharomyces cerevisiae) - STRING interaction network
"HEM4" - Uroporphyrinogen III synthase, catalyzes the conversion of hydroxymethylbilane to uroporphyrinogen III, the fourth step in heme biosynthesis in Saccharomyces cerevisiae
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HEM4Uroporphyrinogen III synthase, catalyzes the conversion of hydroxymethylbilane to uroporphyrinogen III, the fourth step in heme biosynthesis; deficiency in the human homolog can result in the disease congenital erythropoietic porphyria; Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III (275 aa)    
Predicted Functional Partners:
HEM3
Porphobilinogen deaminase, catalyzes the conversion of 4-porphobilinogen to hydroxymethylbilane, the third step in heme biosynthesis; localizes to the cytoplasm and nucleus; expression is regulated by Hap2p-Hap3p, but not by levels of heme; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps (327 aa)
   
  0.999
HEM2
Aminolevulinate dehydratase, a homo-octameric enzyme, catalyzes the conversion of 5-aminolevulinate to porphobilinogen, the second step in heme biosynthesis; enzymatic activity is zinc-dependent; localizes to the cytoplasm and nucleus; Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (342 aa)
   
  0.995
HEM12
Uroporphyrinogen decarboxylase, catalyzes the fifth step in the heme biosynthetic pathway; localizes to both the cytoplasm and nucleus; a hem12 mutant has phenotypes similar to patients with porphyria cutanea tarda; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III (362 aa)
   
 
  0.991
MET1
S-adenosyl-L-methionine uroporphyrinogen III transmethylase, involved in the biosynthesis of siroheme, a prosthetic group used by sulfite reductase; required for sulfate assimilation and methionine biosynthesis; Siroheme synthase involved in methionine biosynthesis (593 aa)
   
 
  0.991
ERG25
C-4 methyl sterol oxidase, catalyzes the first of three steps required to remove two C-4 methyl groups from an intermediate in ergosterol biosynthesis; mutants accumulate the sterol intermediate 4,4-dimethylzymosterol; Catalyzes the first step in the removal of the two C-4 methyl groups of 4,4-dimethylzymosterol (309 aa)
       
 
  0.915
HEM1
5-aminolevulinate synthase, catalyzes the first step in the heme biosynthetic pathway; an N-terminal signal sequence is required for localization to the mitochondrial matrix; expression is regulated by Hap2p-Hap3p; Catalyzes the synthesis of 5-aminolevulinate (ALA) from succinyl-CoA and glycine, the first and rate-limiting step in heme biosynthesis (548 aa)
           
  0.840
MET8
Bifunctional dehydrogenase and ferrochelatase, involved in the biosynthesis of siroheme, a prosthetic group used by sulfite reductase; required for sulfate assimilation and methionine biosynthesis; Catalyzes the conversion of precorrin-2 into siroheme. This reaction consist of the NAD-dependent oxidation of precorrin- 2 into sirohydrochlorin and its subsequent ferrochelation into siroheme (274 aa)
   
 
  0.840
ERG11
Lanosterol 14-alpha-demethylase; catalyzes the C-14 demethylation of lanosterol to form 4,4’’-dimethyl cholesta-8,14,24-triene-3-beta-ol in the ergosterol biosynthesis pathway; member of the cytochrome P450 family; associated and coordinately regula /.../th the P450 reductase Ncp1p; Catalyzes C14-demethylation of lanosterol which is critical for ergosterol biosynthesis. It transforms lanosterol into 4,4’-dimethyl cholesta-8,14,24-triene-3-beta-ol (530 aa)
       
 
  0.835
HEM14
Protoporphyrinogen oxidase, a mitochondrial enzyme that catalyzes the seventh step in the heme biosynthetic pathway, converting protoporphyrinogen IX to protoporphyrin IX; inhibited by diphenyl ether-type herbicides; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX (539 aa)
         
  0.791
HEM15
Ferrochelatase, a mitochondrial inner membrane protein, catalyzes the insertion of ferrous iron into protoporphyrin IX, the eighth and final step in the heme biosynthetic pathway; Catalyzes the ferrous insertion into protoporphyrin IX (393 aa)
   
   
  0.725
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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