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
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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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from curated databases
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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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furFerric uptake regulation protein (Ferric uptake regulator)Fur. Acts as a global negative controlling element employing Fe(2+) as a cofactor to bind the operator of the repressed genes. Regulator for biosynthesis of the siderophore alcaligin E. InterPro: Ferric uptake regulator family TIGR00011: conserved hypothetical protein; High confidence in function and specificity. (145 aa)    
Predicted Functional Partners:
gltB
Ferredoxin-dependent glutamate synthase,; Specificity unclear.
    
 0.936
rubA
Probable rubredoxin. Homology to ruba of A. calcoaceticus of 42% (sprot|RUBR_ACIAD). Involved in the hydrocarbon hydroxylating system to convert dodecane to lauric acid, which transfers electrons from NADH to rubredoxin reductase and then through rubredoxin to alkane 1 monooxygenase. Pfam: Rubredoxin no singal peptide no TMHs; Family membership.
  
  
 0.800
ahpC
Alkyl hydroperoxide reductase subunit C; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
  
  
 0.791
omlA
Putative outer membrane lipoprotein OmlA; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
 
  
 0.762
rpoA
DNA-directed RNA polymerase; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
   
 
 0.756
trxA1
Thioredoxin-disulfide reductase. Homology to trxA of T. ferrooxidans of 69% (THIO_THIFE). Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide. InterPro: Thioredoxin (IPR006662) Pfam: Thioredoxin no signal peptide no TMHs; Specificity unclear.
  
 
 0.701
rpoB
DNA-directed RNA polymerase; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
   
 
 0.637
azo0744
Conserved hypothetical protein; Protein yccU. TREMBL:Q982W3: 50% identity, 70% similarity. This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases. InterPro:IPR003781; CoA_binding. Pfam: PF02629; CoA_binding FRU: PTS enzyme-IIB fructose permease No signal peptide. No transmembrane helices present; Function unclear.
  
    0.625
tpx
Probable thiol peroxidase; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. Tpx subfamily.
   
  
 0.622
azo2663
Conserved hypothetical peroxiredoxin; Conserve peroxiredoxin. Homology to mll2432 of M. loti of 74% (trembl|Q98IF0). Involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic fatty acid and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury. Pfam: AhpC/TSA family no TMHs. No signal peptide; Family membership.
  
  
 0.619
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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