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
IQ37_020354-hydroxybutyrate CoA-transferase; Derived by automated computational analysis using gene prediction method: Protein Homology. (424 aa)    
Predicted Functional Partners:
icmF
Cobalamin-binding protein; Catalyzes the reversible interconversion of isobutyryl-CoA and n-butyryl-CoA, using radical chemistry. Also exhibits GTPase activity, associated with its G-protein domain (MeaI) that functions as a chaperone that assists cofactor delivery and proper holo-enzyme assembly.
  
  
 0.862
IQ37_16345
methylmalonyl-CoA mutase; MDM; functions in conversion of succinate to propionate; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.677
IQ37_02040
Homogentisate 1,2-dioxygenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.603
IQ37_17305
Phenylacetic acid degradation protein PaaN; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.574
eno
Enolase; Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis; Belongs to the enolase family.
   
    0.534
IQ37_02030
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.521
IQ37_07795
Catalyzes the synthesis of 2-methylcitrate from propionyl-CoA and oxaloacetate; also catalyzes the condensation of oxaloacetate with acetyl-CoA but with a lower specificity; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.491
gltA
Type II enzyme; in Escherichia coli this enzyme forms a trimer of dimers which is allosterically inhibited by NADH and competitively inhibited by alpha-ketoglutarate; allosteric inhibition is lost when Cys206 is chemically modified which also affects hexamer formation; forms oxaloacetate and acetyl-CoA and water from citrate and coenzyme A; functions in TCA cycle, glyoxylate cycle and respiration; enzyme from Helicobacter pylori is not inhibited by NADH; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the citrate synthase family.
  
 
 0.491
IQ37_16550
Malic enzyme; NADP-dependent; catalyzes the oxidative decarboxylation of malate to form pyruvate; decarboxylates oxaloacetate; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.482
sucC
succinyl-CoA synthetase subunit beta; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
   
 
 0.455
Your Current Organism:
Chryseobacterium piperi
NCBI taxonomy Id: 558152
Other names: C. piperi, CCUG 57707, Chryseobacterium piperi Strahan et al. 2011 emend. Hahnke et al. 2016, Chryseobacterium sp. CTM, DSM 22249, JCM 15960, KCTC 23267, strain CTM
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