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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
yfiIPutative oxidoreductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the Gfo/Idh/MocA family. (393 aa)    
Predicted Functional Partners:
yteT
Putative dehydrogenase of rhamnogalaturonan degradation; May play a role in the degradation of type I rhamnogalacturonan derived from plant cell walls. Belongs to the Gfo/Idh/MocA family.
  
  
 0.984
yfiH
Putative sugar-phosphate epimerase/isomerase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
 
  
 0.971
yisS
Putative myo-inositol 2-dehydrogenase; Catalyzes the reversible NAD(+)-dependent oxidation of scyllo-inositol (SI) to 2,4,6/3,5-pentahydroxycyclohexanone (scyllo- inosose or SIS). Is required for SI catabolism that allows B.subtilis to utilize SI as the sole carbon source for growth. Cannot use NADP(+) instead of NAD(+); Belongs to the Gfo/Idh/MocA family.
  
   
 0.961
yulF
Enzyme involved in biofilm formation; Catalyzes the NADPH-dependent reduction of scyllo-inosose (SIS) to scyllo-inositol (SI) in vitro, but is unable to dehydrogenate scyllo-inositol and myo-inositol. Is less efficient than the functional paralog IolW. Under physiological conditions, may primarily function as an NADPH-dependent oxidoreductase that reduces carbonyl group(s) in its substrates. Cannot use NADH instead of NADPH.
  
   
 0.932
iolE
2-keto-myo-inositol dehydratase; Catalyzes the dehydration of inosose (2-keto-myo-inositol, 2KMI or 2,4,6/3,5-pentahydroxycyclohexanone) to 3D-(3,5/4)- trihydroxycyclohexane-1,2-dione (D-2,3-diketo-4-deoxy-epi-inositol).
 
  
 0.875
iolB
5-deoxy-D-glucuronic acid isomerase; Involved in the isomerization of 5-deoxy-glucuronate (5DG) to 5-dehydro-2-deoxy-D-gluconate (DKG or 2-deoxy-5-keto-D-gluconate).
 
  
 0.866
iolD
3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase; Involved in the cleavage of the C1-C2 bond of 3D-(3,5/4)- trihydroxycyclohexane-1,2-dione (THcHDO) to yield 5-deoxy-glucuronate (5DG).
 
  
 0.841
yfiG
Putative sugar transporter; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter.
  
    0.831
iolG
Myo-inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase; Involved in the oxidation of myo-inositol (MI) and D-chiro- inositol (DCI) to 2-keto-myo-inositol (2KMI or 2-inosose) and 1-keto-D- chiro-inositol (1KDCI), respectively. Can also use D-glucose and D- xylose, and shows a trace of activity with D-ribose and D-fructose.
  
    0.750
iolH
Putative sugar-phosphate epimerase/isomerase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
 
  
 0.661
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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