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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
AFZ48807.1Phosphoenolpyruvate synthase; Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate; Belongs to the PEP-utilizing enzyme family. (836 aa)    
Predicted Functional Partners:
AFZ46496.1
PFAM: Pyruvate kinase, barrel domain; PEP-utilising enzyme, mobile domain; Pyruvate kinase, alpha/beta domain; TIGRFAM: pyruvate kinase; COGs: COG0469 Pyruvate kinase; InterPro IPR015793:IPR015794:IPR008279:IPR001697; KEGG: cyc:PCC7424_3440 pyruvate kinase; PFAM: Pyruvate kinase barrel; Pyruvate kinase alpha/beta; PEP-utilising protein mobile region; SPTR: Pyruvate kinase; TIGRFAM: pyruvate kinase; Belongs to the pyruvate kinase family.
     
0.934
eno
Enolase; Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis; Belongs to the enolase family.
 
  
 0.930
AFZ47161.1
Malic protein NAD-binding protein; PFAM: Malic enzyme, NAD binding domain; Malic enzyme, N-terminal domain; ACT domain; COGs: COG0281 Malic enzyme; InterProIPR005829:IPR015884:IPR001891:IPR002912:IPR 012301:IPR012302; KEGG: cyc:PCC7424_1195 malate dehydrogenase (oxaloacetate-decarboxylating); PFAM: malic protein NAD-binding; malic protein domain protein; amino acid-binding ACT domain protein; SPTR: Malate dehydrogenase (Oxaloacetate-decarboxylating).
  
 
 0.928
ppc
Phosphoenolpyruvate carboxylase, type 1; Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle; Belongs to the PEPCase type 1 family.
  
  
 0.926
pdhA
Pyruvate dehydrogenase (acetyl-transferring) E1 component, alpha subunit; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
    
 0.912
AFZ48196.1
Transketolase central region; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
    
 0.911
ldh
L-lactate dehydrogenase; Catalyzes the conversion of lactate to pyruvate. Belongs to the LDH/MDH superfamily. LDH family.
   
 
 0.908
AFZ48175.1
PFAM: Glycine radical; Pyruvate formate lyase; TIGRFAM: formate acetyltransferase 1; COGs: COG1882 Pyruvate-formate lyase; InterPro IPR019777:IPR004184:IPR001150:IPR005949; KEGG: cyc:PCC7424_2838 formate acetyltransferase; PFAM: pyruvate formate-lyase PFL; formate C-acetyltransferase glycine radical; PRIAM: Formate C-acetyltransferase; SPTR: Formate acetyltransferase; TIGRFAM: formate acetyltransferase.
    
 0.906
AFZ45995.1
Fructose-bisphosphate aldolase; Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis.
    
 0.837
pgi
PFAM: Phosphoglucose isomerase; COGs: COG0166 Glucose-6-phosphate isomerase; InterPro IPR001672:IPR018189; KEGG: cyh:Cyan8802_0452 glucose-6-phosphate isomerase; PFAM: phosphoglucose isomerase (PGI); SPTR: Glucose-6-phosphate isomerase; Belongs to the GPI family.
    
 0.837
Your Current Organism:
Cyanobacterium stanieri
NCBI taxonomy Id: 292563
Other names: C. stanieri PCC 7202, Cyanobacterium stanieri PCC 7202, Synechococcus cedrorum CCAP 14792a (no longer available), Synechococcus cedrorum CCAP 14792b (no longer available), Synechococcus cedrorum M137/1a, Synechococcus cedrorum SAG 88.79, Synechococcus sp. ATCC 29140, Synechococcus sp. PCC 7202
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