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hemL hemL hemB hemB hemA hemA hemC hemC hemD hemD ABB57486.1 ABB57486.1 hemH hemH ABB56678.1 ABB56678.1 ABB56471.1 ABB56471.1 hemF hemF cobQ cobQ
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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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experimentally determined
Predicted Interactions
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gene co-occurrence
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textmining
co-expression
protein homology
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hemLGlutamate-1-semialdehyde 2,1-aminomutase; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily. (453 aa)    
Predicted Functional Partners:
hemB
Porphobilinogen synthase; 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 (By similarity).
 
 
 0.998
hemA
glutamyl-tRNA reductase; Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
 
 0.997
hemC
Hydroxymethylbilane synthase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
  
 0.985
hemD
uroporphyrinogen-III synthase; Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
 
  
 0.940
ABB57486.1
Malonyl CoA-acyl carrier protein transacylase.
    
 0.861
hemH
Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family.
  
  
 0.834
ABB56678.1
Hypothetical protein.
       0.773
ABB56471.1
Magnesium protoporphyrin O-methyltransferase.
    
 0.736
hemF
Coproporphyrinogen 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.
     
 0.705
cobQ
Adenosylcobyric acid synthase (glutamine-hydrolysing); Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily.
     
 0.686
Your Current Organism:
Synechococcus elongatus
NCBI taxonomy Id: 1140
Other names: Anacystis nidulans R2, S. elongatus PCC 7942, Synechococcus elongatus PCC 7942, Synechococcus leopoliensis UTEX 2434, Synechococcus leopoliensis strain PCC 7942, Synechococcus sp. IAM M-200, Synechococcus sp. PCC 7942
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