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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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
hemHFerrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. (338 aa)    
Predicted Functional Partners:
PP_0431
Homologs of previously reported genes of unknown function.
 
 
 0.973
hemE
Uroporphyrinogen decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
 
  
 0.931
PP_3506
Magnesium chelatase, subunit ChII.
  
 
 0.922
cyoE
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.
   
 
 0.917
cyoE1
CyoE like 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.
     
 0.916
bfr-I
Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family.
   
 
 0.912
bfr-II
Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family.
     
 0.911
PP_4856
Ferritin, Dps family protein.
     
 0.911
yfcH
Conserved protein with NAD(P)-binding Rossmann-fold domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Cellularprocesses : Cell division.
  
    0.910
PP_1358
Putative heme iron utilization protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Unknownfunction : Enzymes of unknown specificity.
     
 0.907
Your Current Organism:
Pseudomonas putida KT2440
NCBI taxonomy Id: 160488
Other names: P. putida KT2440, Pseudomonas putida (strain KT2440), Pseudomonas putida str. KT2440
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