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
citBAconitate hydratase (aconitase); Involved in both the tricarboxylic acid (TCA) and methylcitric acid cycles. Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Also catalyzes the rehydration of 2- methyl-cis-aconitate to produce 2-methylisocitrate. The apo form of AcnA functions as a RNA-binding regulatory protein which plays a role in the regulation of citrate concentration and in the sporulation. To prevent the accumulation of excessive levels of citrate, it binds near the 5' end of the citZ mRNA, decreasing its stability and thereby limiting the conce [...] (909 aa)    
Predicted Functional Partners:
citA
Citrate synthase I; Might regulate the synthesis and function of enzymes involved in later enzymatic steps of Krebs cycle. Loss in activity results in sporulation defect; Belongs to the citrate synthase family.
 
 0.999
mmgD
2-methylcitrate synthase/citrate synthase III; Involved in both the tricarboxylic acid (TCA) and methylcitric acid cycles. Has both 2-methylcitrate synthase and citrate synthase activities. Catalyzes the condensation of propionyl-CoA and oxaloacetate to yield 2-methylcitrate (2-MC) and CoA, and the condensation of acetyl-CoA and oxaloacetate to yield citrate and CoA. Has 2.3-fold higher activity as a 2-methylcitrate synthase. Catalyzes the formation of either (2S,3R)- or (2R,3S)-2-methylcitrate.
 
 0.999
icd
Isocitrate dehydrogenase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme.
 
 0.999
citZ
Citrate synthase II; Might regulate the synthesis and function of enzymes involved in later enzymatic steps of Krebs cycle. Loss in activity results in sporulation defect; Belongs to the citrate synthase family.
 
 0.999
fumC
Fumarate hydratase; Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate; Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.
  
 0.981
mmgF
2-methylisocitrate lyase; Involved in the methylcitric acid cycle. Catalyzes the cleavage of 2-methylisocitrate to yield pyruvate and succinate.
 
 0.960
mdh
Malate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate.
  
 0.954
odhA
2-oxoglutarate dehydrogenase (E1 subunit); E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
 
 0.946
mmgE
2-methylcitrate dehydratase; Involved in both the tricarboxylic acid (TCA) and methylcitric acid cycles. Has both 2-methylcitrate dehydratase and citrate dehydratase activities. Catalyzes the dehydration of 2-methylcitrate (2-MC) to yield 2-methyl-cis-aconitate, and the dehydration of citrate to yield cis-aconitate. Cannot form isocitrate. Uses either (2S,3R)- or (2R,3S)-2-methylcitrate.
 
 
 0.945
sdhA
Succinate dehydrogenase (flavoprotein subunit); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme.
  
 
 0.937
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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