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
Ping_0893Isoamylase; KEGG: syd:Syncc9605_0815 glycogen debranching enzyme GlgX; TIGRFAM: glycogen debranching enzyme GlgX; PFAM: glycoside hydrolase, family 13 domain protein; alpha amylase, catalytic region; SMART: alpha amylase, catalytic sub domain; Belongs to the glycosyl hydrolase 13 family. (693 aa)    
Predicted Functional Partners:
Ping_2365
KEGG: pat:Patl_1635 4-alpha-glucanotransferase; TIGRFAM: 4-alpha-glucanotransferase; PFAM: glycoside hydrolase, family 77.
 
 0.997
glgB
1,4-alpha-glucan branching enzyme; Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position; Belongs to the glycosyl hydrolase 13 family. GlgB subfamily.
 
0.981
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.
 
 
 0.953
Ping_2363
KEGG: pat:Patl_1637 glycogen debranching enzyme GlgX; TIGRFAM: glycogen debranching enzyme GlgX; PFAM: glycoside hydrolase, family 13 domain protein; alpha amylase, catalytic region; SMART: alpha amylase, catalytic sub domain; Belongs to the glycosyl hydrolase 13 family.
  
  
 
0.914
Ping_3070
Isoamylase; KEGG: aba:Acid345_3295 glycogen debranching enzyme GlgX; TIGRFAM: glycogen debranching enzyme GlgX; PFAM: glycoside hydrolase, family 13 domain protein; alpha amylase, catalytic region; SMART: alpha amylase, catalytic sub domain.
  
  
 
0.906
Ping_0500
Hypothetical protein; KEGG: pat:Patl_2143 glycoside hydrolase, family 13-like.
  
  
 0.625
glgA
Glycogen synthase (ADP-glucose); Synthesizes alpha-1,4-glucan chains using ADP-glucose.
 
  
 0.615
glgA-2
Glycogen synthase (ADP-glucose); Synthesizes alpha-1,4-glucan chains using ADP-glucose.
 
  
 0.615
Ping_1954
PFAM: alpha amylase, catalytic region; SMART: alpha amylase, catalytic sub domain; KEGG: mca:MCA2605 alpha amylase family protein.
 
  
 0.554
nnrE
Carbohydrate kinase, YjeF related protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow t [...]
  
    0.461
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.