STRINGSTRING
nplT protein (Synechocystis sp. PCC6803) - STRING interaction network
"nplT" - Neopullulanase in Synechocystis sp. PCC6803
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
nplTNeopullulanase (508 aa)    
Predicted Functional Partners:
malQ
4-alpha-glucanotransferase (505 aa)
 
  0.988
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 (770 aa)
   
 
  0.956
SYNGTS_1078
Glycogen operon protein GlgX (707 aa)
 
 
  0.954
SYNGTS_0122
Glycogen operon protein GlgX (746 aa)
 
 
  0.954
SYNGTS_1012
Glycogen 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 (855 aa)
   
  0.950
glgA1
Glycogen synthase; Synthesizes alpha-1,4-glucan chains using ADP-glucose (477 aa)
 
 
  0.944
sll1356
Glycogen 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 (By similarity) (849 aa)
   
  0.933
sll1496
Mannose-1-phosphate guanyltransferase (843 aa)
   
 
  0.883
glgA2
Glycogen (starch) synthase; Synthesizes alpha-1,4-glucan chains using ADP-glucose (491 aa)
 
 
  0.876
ilvA
L-threonine deaminase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short- lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA (508 aa)
   
      0.868
Your Current Organism:
Synechocystis sp. PCC6803
NCBI taxonomy Id: 1148
Other names: Aphanocapsa sp. (strain N-1), Aphanocapsa sp. N-1, S. sp. PCC 6803, Synechocystis, Synechocystis PCC6803, Synechocystis sp. (ATCC 27184), Synechocystis sp. (PCC 6803), Synechocystis sp. (strain PCC 6803), Synechocystis sp. ATCC 27184, Synechocystis sp. PCC 6803, Synechocystis sp. PCC 6803 A, Synechocystis sp. PCC 6803 B, Synechocystis sp. PCC6803
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