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
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
Ping_0500Hypothetical protein; KEGG: pat:Patl_2143 glycoside hydrolase, family 13-like. (109 aa)    
Predicted Functional Partners:
Ping_0880
Glycogen/starch/alpha-glucan phosphorylase; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
  
 
 0.785
glgA
Glycogen synthase (ADP-glucose); Synthesizes alpha-1,4-glucan chains using ADP-glucose.
  
  
 0.732
glgA-2
Glycogen synthase (ADP-glucose); Synthesizes alpha-1,4-glucan chains using ADP-glucose.
  
  
 0.732
Ping_0879
TIGRFAM: phosphoglucomutase, alpha-D-glucose phosphate-specific; PFAM: phosphoglucomutase/phosphomannomutase C terminal; phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain I; phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain II; phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain III; KEGG: sde:Sde_1254 CinA-like.
  
  
 0.637
mutH
DNA mismatch repair protein MutH; Sequence-specific endonuclease that cleaves unmethylated GATC sequences. It is involved in DNA mismatch repair. Belongs to the MutH family.
 
     0.625
Ping_1794
PFAM: glycosyl transferase, group 1; KEGG: cps:CPS_0439 hypothetical protein.
  
 0.608
glgC
Glucose-1-phosphate adenylyltransferase; Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc; Belongs to the bacterial/plant glucose-1-phosphate adenylyltransferase family.
  
  
 0.604
glgC-2
Glucose-1-phosphate adenylyltransferase; Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc; Belongs to the bacterial/plant glucose-1-phosphate adenylyltransferase family.
  
  
 0.604
glgC-3
Glucose-1-phosphate adenylyltransferase; Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc; Belongs to the bacterial/plant glucose-1-phosphate adenylyltransferase family.
  
  
 0.604
glgC-4
Glucose-1-phosphate adenylyltransferase; Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc; Belongs to the bacterial/plant glucose-1-phosphate adenylyltransferase family.
  
  
 0.604
Your Current Organism:
Psychromonas ingrahamii
NCBI taxonomy Id: 357804
Other names: P. ingrahamii 37, Psychromonas ingrahamii 37, Psychromonas ingrahamii str. 37, Psychromonas ingrahamii strain 37, gas vacuolate str. 37
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.