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
fbpInositol phosphatase/fructose-16-bisphosphatase; COGs: COG0158 Fructose-1 6-bisphosphatase; InterPro IPR000146; KEGG: amr:AM1_6321 fructose-1,6-bisphosphatase; PFAM: Inositol phosphatase/fructose-16-bisphosphatase; SPTR: Fructose-1,6-bisphosphatase class 1 2; PFAM: Fructose-1-6-bisphosphatase. (356 aa)    
Predicted Functional Partners:
Isop_1171
Transketolase; COGs: COG0021 Transketolase; InterProIPR005478: IPR005474: IPR005475: IPR005476: IPR 020826; KEGG: mea:Mex_1p1861 transketolase; PFAM: Transketolase domain-containing protein; Transketolase central region; SPTR: Transketolase; TIGRFAM: transketolase; PFAM: Transketolase, thiamine diphosphate binding domain; Transketolase, C-terminal domain; Transketolase, pyrimidine binding domain; TIGRFAM: transketolase, bacterial and yeast; Belongs to the transketolase family.
  
 
 0.957
tal
Transaldolase; Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
 
 
 0.947
pgi
COGs: COG0166 Glucose-6-phosphate isomerase; InterPro IPR018189: IPR000169: IPR001672; KEGG: mxa:MXAN_6908 glucose-6-phosphate isomerase; PFAM: phosphoglucose isomerase (PGI); SPTR: Glucose-6-phosphate isomerase; PFAM: Phosphoglucose isomerase; Belongs to the GPI family.
   
 
 0.926
Isop_3272
Mannose-6-phosphate isomerase, type 1; COGs: COG1482 Phosphomannose isomerase; InterPro IPR001917: IPR001250: IPR014628; KEGG: psl:Psta_4651 mannose-6-phosphate isomerase, class I; PFAM: mannose-6-phosphate isomerase type I; PRIAM: Mannose-6-phosphate isomerase; SPTR: Mannose-6-phosphate isomerase, class I; TIGRFAM: mannose-6-phosphate isomerase, class I; PFAM: Phosphomannose isomerase type I; TIGRFAM: mannose-6-phosphate isomerase, class I.
     
 0.903
Isop_1077
COGs: COG0205 6-phosphofructokinase; InterPro IPR011403: IPR000023; KEGG: psl:Psta_4392 6-phosphofructokinase; PFAM: phosphofructokinase; SPTR: 6-phosphofructokinase; PFAM: Phosphofructokinase.
    
 0.548
Isop_2595
COGs: COG0205 6-phosphofructokinase; InterPro IPR000023; KEGG: plm:Plim_2681 phosphofructokinase; PFAM: phosphofructokinase; SPTR: 6-phosphofructokinase I; PFAM: Phosphofructokinase.
    
 0.548
Isop_2970
COGs: COG0205 6-phosphofructokinase; InterPro IPR000023: IPR012004; KEGG: psl:Psta_0329 diphosphate--fructose-6-phosphate1-phosphotransferase; PFAM: phosphofructokinase; SPTR:Diphosphate--fructose-6-phosphate1-phosphotran sferase; PFAM: Phosphofructokinase.
    
 0.548
pfp
Phosphofructokinase; Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
    
 0.548
pfp-2
Pyrophosphate-dependent phosphofructokinase; Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
    
 0.548
Isop_3519
COGs: COG0057 Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase; InterProIPR006424: IPR020831: IPR020828: IPR020829: IPR 020832: IPR020830; KEGG: plm:Plim_0647 glyceraldehyde-3-phosphate dehydrogenase, type I; PFAM: Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain; Glyceraldehyde 3-phosphate dehydrogenase, catalytic domain; PRIAM: Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating); SPTR: Strongly similar to glyceraldehyde-3-phosphate dehydrogenase; TIGRFAM: glyceraldehyde-3-phosphate dehydrogenase, type I; PFAM: Glyceraldehyde 3-phospha [...]
  
  
 0.526
Your Current Organism:
Isosphaera pallida
NCBI taxonomy Id: 575540
Other names: I. pallida ATCC 43644, Isosphaera pallida ATCC 43644, Isosphaera pallida DSM 9630, Isosphaera pallida IS1B, Isosphaera pallida str. ATCC 43644, Isosphaera pallida strain ATCC 43644
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