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
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
EGW20050.1Aconitate hydratase 2; TIGRFAM: Aconitase B, bacterial; KEGG: mca:MCA2485 bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; PFAM: Aconitase B, N-terminal, bacterial; Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha; Belongs to the aconitase/IPM isomerase family. (852 aa)    
Predicted Functional Partners:
EGW20048.1
TIGRFAM: Isocitrate dehydrogenase NADP-dependent, prokaryotic; KEGG: ank:AnaeK_2235 isocitrate dehydrogenase, NADP-dependent; PFAM: Isocitrate/isopropylmalate dehydrogenase.
  
 
 0.979
EGW23647.1
TIGRFAM: Citrate synthase, type II; KEGG: neu:NE2373 citrate synthase; PFAM: Citrate synthase-like; Belongs to the citrate synthase family.
  
 
 0.977
EGW20316.1
TIGRFAM: Citrate synthase, type II; KEGG: dbr:Deba_1491 citrate synthase I; PFAM: Citrate synthase-like; Belongs to the citrate synthase family.
  
 
 0.977
EGW20347.1
TIGRFAM: Pyruvate-flavodoxin oxidoreductase; KEGG: alv:Alvin_0264 pyruvate ferredoxin/flavodoxin oxidoreductase; PFAM: Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal; Pyruvate/ketoisovalerate oxidoreductase; Pyruvate-flavodoxin oxidoreductase, EKR domain; 4Fe-4S ferredoxin, iron-sulphur binding, subgroup; Thiamine pyrophosphate enzyme, C-terminal TPP-binding.
   
 
 0.964
EGW20049.1
KEGG: mca:MCA3071 isocitrate dehydrogenase, NAD-dependent, putative; PFAM: Isocitrate/isopropylmalate dehydrogenase.
    
 0.931
EGW21518.1
KEGG: nhl:Nhal_1482 aconitate hydratase; TIGRFAM: Aconitase, putative; PFAM: Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha; Aconitase A/isopropylmalate dehydratase small subunit, swivel.
    
0.905
EGW21862.1
Aconitate hydratase 1; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate.
    
 0.905
sucC
Succinyl-CoA ligase (ADP-forming) 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.
  
 
 0.893
sucC-2
Succinyl-CoA ligase (ADP-forming) 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.
  
 
 0.893
EGW22202.1
TIGRFAM: 2-oxoglutarate dehydrogenase, E1 component; KEGG: aeh:Mlg_2609 2-oxoglutarate dehydrogenase E1 component; PFAM: Transketolase-like, pyrimidine-binding domain; Dehydrogenase, E1 component.
   
  
 0.888
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum SV96, Methylobacter sp. SV96, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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