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:
some 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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[Homology]
Score
gltAType ii citrate synthase; cit_synth_I: citrate (Si)-synthase; Belongs to the citrate synthase family (428 aa)    
Predicted Functional Partners:
acnB
Bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and probably via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Catalyzes the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnB functions as a RNA-binding regulatory protein
  
 
 0.997
acnA
Aconitate hydratase 1; Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and probably the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis- aconitate. Could catalyze the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnA functions as a RNA-binding regulatory protein
 
 0.995
acnD
2-methylcitrate dehydratase (2-methyl-trans-aconitate forming); Aconitate hydratase; 2met_isocit_dHY: 2-methylisocitrate dehydratase, Fe/S-dependent
 
 0.991
fumC
Fumarate hydratase, class ii; Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate
   
 0.980
aceF
Pyruvate dehydrogenase e2 component (dihydrolipoamide acetyltransferase); The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3)
  
 0.978
sucA
2oxo_dh_E1: oxoglutarate dehydrogenase (succinyl-transferring), E1 component
 
 
 0.976
ppc
Phosphoenolpyruvate carboxylase family protein; Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle
   
 
 0.976
fumC2
Fumarate hydratase, class ii; Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate
   
 0.974
acsA1
Acetyl-coa synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA
  
 0.972
FumA
Hydrolyase, tartrate alpha subunit/fumarate, fe-s type domain protein; Catalyzes the reversible hydration of fumarate to (S)-malate
  
 
 0.972
Your Current Organism:
Pseudomonas aeruginosa
NCBI taxonomy Id: 287
Other names: ATCC 10145, ATCC 10145-U, Bacillus aeruginosus, Bacillus pyocyaneus, Bacterium aeruginosum, Bacterium pyocyaneum, CCEB 481, CCUG 28447, CCUG 29297, CCUG 551, CFBP 2466, CIP 100720, DSM 50071, IBCS 277, IFO 12689, JCM 5962, Micrococcus pyocyaneus, NBRC 12689, NCCB 76039, NCIB 8295, NCIMB 8295, NCTC 10332, NRRL B-771, P. aeruginosa, Pseudomonas polycolor, Pseudomonas pyocyanea, Pseudomonas sp. RV3, RH 815, VKM B-588, bacterium ASFP-37, bacterium ASFP-38, bacterium ASFP-45, bacterium ASFP-46, bacterium ASFP-48
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