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
tsaAPeroxiredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (200 aa)    
Predicted Functional Partners:
ahpF
Alkyl hydroperoxide reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.839
AKL37244.1
Thioredoxin reductase; Catalyzes the transfer of electrons from NADPH to thioredoxin; FAD/NAD(P) binding; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.792
norV
Nitric oxide reductase; Anaerobic nitric oxide reductase; uses NADH to detoxify nitric oxide (NO), protecting several 4Fe-4S NO-sensitive enzymes. Has at least 2 reductase partners, only one of which (NorW, flavorubredoxin reductase) has been identified. NO probably binds to the di-iron center; electrons enter from the NorW at rubredoxin and are transferred sequentially to the FMN center and the di-iron center. Also able to function as an aerobic oxygen reductase; In the N-terminal section; belongs to the zinc metallo- hydrolase group 3 family.
  
  
 0.707
AKL34514.1
Alkyl hydroperoxide reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.685
AKL34892.1
Thiol:disulfide interchange protein DsbE; Cytochrome c-type biogenesis thioredoxin; involved in the reduction of disulfide bonds to allow heme bonding; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.685
fur
Ferric uptake regulator; Negatively regulates a number of operons that encode enzymes involved in iron transport; activated by manganese; forms a homodimer; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the Fur family.
  
  
 0.660
sodC
Superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the Cu-Zn superoxide dismutase family.
   
 
 0.630
bcp
Thiol peroxidase; Bacterioferritin comigratory protein; thiol peroxidase; thioredoxin-dependent; hydroperoxide peroxidase; in Escherichia coli this enzyme preferentially reduces linoleic acid hydroperoxide; contains an active site cysteine; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.621
acpH
ACP phosphodiesterase; Converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine prosthetic group from ACP; Belongs to the AcpH family.
       0.613
dps
DNA starvation/stationary phase protection protein Dps; During stationary phase, binds the chromosome non- specifically, forming a highly ordered and stable dps-DNA co-crystal within which chromosomal DNA is condensed and protected from diverse damages. It protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral, which can be released after reduction. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction; Belongs to the Dps family.
  
  
 0.605
Your Current Organism:
Klebsiella oxytoca
NCBI taxonomy Id: 571
Other names: ATCC 13182, Bacillus oxytocus perniciosus, CCUG 15717, CIP 103434, DSM 5175, IAM 14201, K. oxytoca, Klebsiella sp. CECRI-24/07, Klebsiella sp. MN9SED2, LMG 3055, LMG:3055, NBRC 102593, NBRC 105695, NCTC 13727, strain 479-2
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