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
Pcal_0579TIGRFAM: isocitrate dehydrogenase, NADP-dependent; PFAM: isocitrate/isopropylmalate dehydrogenase; KEGG: pai:PAE1651 isocitrate dehydrogenase. (438 aa)    
Predicted Functional Partners:
Pcal_0804
Aconitase; TIGRFAM: aconitate hydratase 1; PFAM: aconitate hydratase domain protein; KEGG: pai:PAE1499 aconitate hydratase.
  
 0.997
mdh
Malate dehydrogenase (NAD); Catalyzes the reversible oxidation of malate to oxaloacetate. Belongs to the LDH/MDH superfamily.
  
 
 0.986
sucC
succinyl-CoA synthetase (ADP-forming) 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.
 
  
 0.975
Pcal_1031
Glutamate dehydrogenase (NAD); Catalyzes the reversible oxidative deamination of L-glutamate to 2-oxoglutarate and ammonia, thereby playing a key role at the intersection of the carbon and nitrogen metabolic pathways. Is strictly specific for NAD(+)/NADH as the acceptor/donor, since it cannot use NADP(+)/NADPH. May function in vivo in the catabolic direction. Also catalyzes at low rates the oxidative deamination of L-norvaline, L-2- aminobutyrate, L-valine and L-isoleucine, and the reductive amination of 2-oxovalerate and 2-oxobutyrate; Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
   
 0.956
Pcal_1606
Glutamate dehydrogenase (NADP); Catalyzes the reversible oxidative deamination of L-glutamate to 2-oxoglutarate and ammonia, thereby playing a key role at the intersection of the carbon and nitrogen metabolic pathways. Shows a high preference for NADP(+)/NADPH as the acceptor/donor over NAD(+)/NADH. May function in vivo in the synthetic direction. Also catalyzes at very low rates the oxidative deamination of L-2- aminobutyrate, and the reductive amination of 2-oxovalerate and 2- oxobutyrate; Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
   
 0.956
Pcal_0154
KEGG: pai:PAE3584 citrate synthase; TIGRFAM: 2-methylcitrate synthase/citrate synthase II; PFAM: Citrate synthase.
  
 
 0.924
Pcal_0563
KEGG: pai:PAE1689 citrate synthase; TIGRFAM: 2-methylcitrate synthase/citrate synthase II; PFAM: Citrate synthase.
  
 
 0.924
Pcal_0108
PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; KEGG: pai:PAE0939 2-oxoacid ferredoxin oxidoreductase alpha subunit.
  
 
 0.923
Pcal_0561
PFAM: pyruvate ferredoxin/flavodoxin oxidoreductase; pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; KEGG: pai:PAE1559 2-oxoacid ferredoxin oxidoreductase alpha subunit.
  
 
 0.923
Pcal_0107
TIGRFAM: pyruvate ferredoxin/flavodoxin oxidoreductase, beta subunit; PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; KEGG: pai:PAE0938 2-oxoacid ferredoxin oxidoreductase beta subunit.
    
 0.919
Your Current Organism:
Pyrobaculum calidifontis
NCBI taxonomy Id: 410359
Other names: P. calidifontis JCM 11548, Pyrobaculum calidifontis JCM 11548, Pyrobaculum calidifontis VA1, Pyrobaculum calidifontis str. JCM 11548, Pyrobaculum calidifontis strain JCM 11548
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