Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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[Homology]
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hemEUroporphyrinogen decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. (348 aa)    
Predicted Functional Partners:
hemC
Porphobilinogen deaminase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family.
 
 0.993
hemF
Coproporphyrinogen-III oxidase, aerobic; Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen- IX.
 
 0.976
cysG_2
Siroheme synthase.
    
 0.961
hemN_2
Oxygen-independent coproporphyrinogen-III oxidase; Belongs to the anaerobic coproporphyrinogen-III oxidase family.
 
 
 0.941
hemH
Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family.
 
  
 0.941
cysG_1
Siroheme synthase; Belongs to the precorrin methyltransferase family.
    
 0.917
BVIR_3289
Hypothetical protein.
 
   
 0.904
BVIR_2413
D-amino acid dehydrogenase small subunit.
  
  
 0.901
hemB
Delta-aminolevulinic acid dehydratase; Belongs to the ALAD family.
 
 
 0.872
rho
Hypothetical protein; Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA- dependent ATPase activity, and release of the mRNA from the DNA template.
   
 0.835
Your Current Organism:
Blastochloris viridis
NCBI taxonomy Id: 1079
Other names: ATCC 19567, B. viridis, CCUG 30818, CCUG 7830, DSM 133, LMG 4321, LMG:4321, NBRC 102659, Rhodopseudomonas viridis, strain G. Drews F
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