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.
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
AEB85284.1TIGRFAM: Isocitrate dehydrogenase NADP-dependent, prokaryotic; KEGG: aav:Aave_2572 isocitrate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase. (419 aa)    
Predicted Functional Partners:
AEB83383.1
Aconitate hydratase; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate.
 
 0.989
AEB85373.1
2-oxoglutarate dehydrogenase, E1 subunit; SMART: Transketolase-like, pyrimidine-binding domain; TIGRFAM: 2-oxoglutarate dehydrogenase, E1 component; KEGG: ajs:Ajs_1822 2-oxoglutarate dehydrogenase E1 component; PFAM: Transketolase-like, pyrimidine-binding domain; Dehydrogenase, E1 component.
  
 0.989
AEB83778.1
Aconitate hydratase 1; TIGRFAM: Aconitase/iron regulatory protein 2; KEGG: ajs:Ajs_1145 aconitate hydratase; PFAM: Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha; Aconitase A/isopropylmalate dehydratase small subunit, swivel.
 
 0.988
AEB84588.1
KEGG: ajs:Ajs_2787 bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; TIGRFAM: Aconitase B, bacterial; PFAM: Aconitase B, N-terminal, bacterial; Aconitase B, HEAT-like, bacterial; Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha; Belongs to the aconitase/IPM isomerase family.
  
 
 0.984
mdh
Malate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate. Belongs to the LDH/MDH superfamily. MDH type 2 family.
  
 0.980
AEB86082.1
Hydro-lyase, Fe-S type, tartrate/fumarate subfamily, alpha subunit; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family.
  
  
 0.958
sucC
succinyl-CoA synthetase, beta subunit; 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.
  
 0.945
AEB85286.1
TIGRFAM: Isocitrate dehydrogenase NADP-dependent, monomeric type; KEGG: ajs:Ajs_2300 isocitrate dehydrogenase, NADP-dependent; PFAM: Isocitrate dehydrogenase NADP-dependent, monomeric type; Belongs to the monomeric-type IDH family.
    
 0.927
gcvP
Glycine dehydrogenase (decarboxylating); The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family.
   
  
 0.919
AEB82628.1
PFAM: Glutamate/phenylalanine/leucine/valine dehydrogenase, C-terminal; Glutamate/phenylalanine/leucine/valine dehydrogenase, dimerisation domain; KEGG: dia:Dtpsy_0153 Glu/Leu/Phe/Val dehydrogenase; SMART: Glutamate/phenylalanine/leucine/valine dehydrogenase, C-terminal; Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
   
 0.911
Your Current Organism:
Alicycliphilus denitrificans
NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601
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