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
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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.
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experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
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hemMCoproporphyrinogen oxidase / Oxygen-independent coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. (399 aa)    
Predicted Functional Partners:
lepA
GTP-binding protein LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner.
 
  
 0.895
hemE
Uroporphyrinogen decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
 
 
 0.854
hemY
Protoporphyrinogen oxidase (PPO) HemY; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
 
  
 0.744
nifJ2
Pyruvate:ferredoxin (Flavodoxin) oxidoreductase.
     
 0.692
CBL56399.1
5.2 Protein of unknown function similar to proteins from other organisms.
       0.632
hemD
Uroporphyrinogen-III synthase HemD; Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
  
  
 0.601
nifJ1
Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin, which reduces nitrogenase, Pyruvate + CoA + oxidized flavodoxin = acetyl-CoA + CO2 + reduced flavodoxin.
  
  
 0.569
CBL56291.1
HAM1, NTPase/HAM1; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family.
    0.568
gltB
Glutamate synthase large subunit (Ferredoxin); 2 L-Glutamate + 2 Oxidized ferredoxin <=> L-Glutamine + 2-Oxoglutarate + 2 Reduced ferredoxin.
     
 0.554
CBL56403.1
Hypothetical protein; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
 
    0.545
Your Current Organism:
Propionibacterium freudenreichii
NCBI taxonomy Id: 754252
Other names: P. freudenreichii subsp. shermanii CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii ATCC 9614, Propionibacterium freudenreichii subsp. shermanii CIP 103027, Propionibacterium freudenreichii subsp. shermanii CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii str. CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii strain CIRM-BIA1
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