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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
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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[Homology]
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hemHFerrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. (391 aa)    
Predicted Functional Partners:
hemE
Uroporphyrinogen decarboxylase (URO-D); Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
 
  
 0.980
ctaB
Putative protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
     
 0.967
chlD
Protoporphyrin IX Magnesium chelatase, ChlD subunit; Involved in chlorophyll biosynthesis. Catalyzes the insertion of magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
  
 
 0.962
chlH
Protoporphyrin IX magnesium chelatase, subunit chlH; Alternative locus ID: PMED4_09251.
   
 
 0.958
chlI
Protoporphyrin IX Magnesium chelatase, ChlI subunit; Involved in chlorophyll biosynthesis. Catalyzes the insertion of magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
   
 
 0.943
ho1
Heme oxygenase; Alternative locus ID: PMED4_18041.
     
 0.943
PMM0881
Conserved hypothetical protein; Alternative locus ID: PMED4_09921.
    
 0.935
hemF
Coproporphyrinogen III oxidase; Involved in the heme and chlorophyll 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.
 
  
 0.900
hemC
Porphobilinogen deaminase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
 
  
 0.768
chlN
Light-independent protochlorophyllide reductase subunit N; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex.
      
 0.766
Your Current Organism:
Prochlorococcus marinus pastoris
NCBI taxonomy Id: 59919
Other names: P. marinus subsp. pastoris str. CCMP1986, Prochlorococcus marinus MED4, Prochlorococcus marinus subsp. pastoris str. CCMP1378, Prochlorococcus marinus subsp. pastoris str. CCMP1986, Prochlorococcus sp. CCMP1378, Prochlorococcus sp. MED4
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