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
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Gene Fusion
Cooccurrence
Coexpression
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[Homology]
Score
AEX53018.1Phosphoglucomutase, alpha-D-glucose phosphate-specific; PFAM: Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; Phosphoglucomutase/phosphomannomutase, C-terminal domain; Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; TIGRFAM: phosphoglucomutase, alpha-D-glucose phosphate-specific. (547 aa)    
Predicted Functional Partners:
pgi
PFAM: Phosphoglucose isomerase; Belongs to the GPI family.
 
 0.988
AEX50177.1
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.
  
 
 0.971
AEX50191.1
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.
  
 
 0.971
AEX50514.1
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.
  
 
 0.971
glgB
Alpha-1,4-glucan:alpha-1,4-glucan 6-glycosyltransferase; 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.
  
 0.960
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.
    
 0.938
AEX51698.1
PFAM: Nucleotidyl transferase; TIGRFAM: UTP-glucose-1-phosphate uridylyltransferase.
    
 0.937
glgX
Glycogen debranching enzyme GlgX; Removes maltotriose and maltotetraose chains that are attached by 1,6-alpha-linkage to the limit dextrin main chain, generating a debranched limit dextrin.
 
  
 0.934
AEX51045.1
Transketolase; Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
  
 
 0.932
rpiA
Ribose 5-phosphate isomerase; Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
  
 
 0.932
Your Current Organism:
Rahnella aquatilis
NCBI taxonomy Id: 745277
Other names: R. aquatilis CIP 78.65 = ATCC 33071, Rahnella aquatilis ATCC 33071, Rahnella aquatilis ATCC 33071 = CIP 78.65, Rahnella aquatilis CIP 78.65, Rahnella aquatilis CIP 78.65 = ATCC 33071, Rahnella aquatilis CUETM 77-115, Rahnella aquatilis CUETM 77-155, Rahnella aquatilis DSM 4594
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