STRINGSTRING
STRING protein interaction network
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.
Node Color
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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ssnAPutative chlorohydrolase/aminohydrolase; Protein involved in cell cycle. (442 aa)    
Predicted Functional Partners:
ygfK
Putative Fe-S subunit oxidoreductase subunit; Could be an iron-sulfur flavoprotein with NADPH:O(2) oxidoreductase activity.
 
  
 0.986
ygfM
Putative oxidoreductase.
 
    0.966
xdhD
Putative hypoxanthine oxidase, molybdopterin-binding/Fe-S binding; Probably has no xanthine dehydrogenase activity; however deletion results in increased adenine sensitivity, suggesting that this protein contributes to the conversion of adenine to guanine nucleotides during purine salvage.
 
  
 0.956
ygeY
Putative deacetylase.
 
  
 0.927
xdhA
Xanthine dehydrogenase, molybdenum binding subunit; Presumed to be a dehydrogenase, but possibly an oxidase. Participates in limited purine salvage (requires aspartate) but does not support aerobic growth on purines as the sole carbon source (purine catabolism). Deletion results in increased adenine sensitivity, suggesting that this protein contributes to the conversion of adenine to guanine nucleotides during purine salvage.
 
  
 0.921
ygeW
Putative carbamoyltransferase; Putative carbamoyltransferase. No activity can be detected with allantoin or 25 other related compounds, including 20 naturally occurring amino acids, N-acetyl-L-ornithine, N-succinyl-L-ornithine, L- ornithine, oxamate, beta-alanine and putrescine.
 
  
 0.915
hyuA
D-stereospecific phenylhydantoinase; Catalyzes the stereospecific hydrolysis of the cyclic amide bond of D-hydantoin derivatives with an aromatic side chains at the 5'- position. Has no activity on dihydropyrimidines. The physiological function is unknown; Belongs to the metallo-dependent hydrolases superfamily. Hydantoinase/dihydropyrimidinase family.
 
  
 0.894
xdhB
Xanthine dehydrogenase, FAD-binding subunit; Presumed to be a dehydrogenase, but possibly an oxidase. Participates in limited purine salvage (requires aspartate) but does not support aerobic growth on purines as the sole carbon source (purine catabolism).
 
  
 0.876
yqeB
XdhC-CoxI family protein with NAD(P)-binding Rossman fold; Putative synthases.
 
    0.861
ygeX
2,3-diaminopropionate ammonia lyase, PLP-dependent; Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In vitro the D-isomer of serine is degraded to pyruvate, though very poorly; other amino acids (L-serine, D- and L-threonine, D- and L-beta- Cl-alanine) are not substrates. In vivo allows poor growth on L-DAP or a DL-DAP mixture but not on D-DAP alone, this may be due to a poor promoter. DL-DAP is toxic in the absence of this enzyme, it may inhibit enzymes involved in the synthesis of pyruvate and aspartate, [...]
 
   0.847
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.