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
AKJ42578.1Together with GalF subunit composes the UTP--glucose-1-phosphate uridylyltransferase, an enzyme that catalyzes the formation of UDP-glucose from UTP and alpha-D-glucose 1-phosphate; regulates cellular levels of UDP-glucose; Derived by automated computational analysis using gene prediction method: Protein Homology. (303 aa)    
Predicted Functional Partners:
AKJ42577.1
UDP-glucose 6-dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.986
rmlA2
Glucose-1-phosphate thymidylyltransferase; Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. Belongs to the glucose-1-phosphate thymidylyltransferase family.
 
 
0.966
AKJ41936.1
UDP-galactose-4-epimerase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the NAD(P)-dependent epimerase/dehydratase family.
  
 0.955
AKJ43446.1
UDP-glucose 6-dehydrogenase; Catalyzes the formation of UDP-glucuronate from UDP-glucose; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.949
AKJ42576.1
Protein CapI; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.941
pgm
Phosphoglucomutase; Catalyzes the interconversion of alpha-D-glucose 1-phosphate to alpha-D-glucose 6-phosphate; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.937
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.
     
 0.933
malP
Maltodextrin 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.
     
 0.924
AKJ41935.1
Galactose-1-phosphate uridylyltransferase; Catalyzes the interconversion of UDP-galactose and galactose-1-P with UDP-galactose and glucose-1-P; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the galactose-1-phosphate uridylyltransferase type 1 family.
     
 0.914
AKJ41977.1
Glycogen debranching protein; Catalyzes the hydrolysis of the alpha-1,6-glucosidic linkages in partially depolymerized glycogen; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the glycosyl hydrolase 13 family.
     
 0.914
Your Current Organism:
Pragia fontium
NCBI taxonomy Id: 82985
Other names: ATCC 49100, CCUG 18073, CDC 963-84, CIP 103791, CNCTC Eb11/82, DRL 20125, DSM 5563, IP 20125, LMG 7875, LMG:7875, NCTC 12283, P. fontium, strain HG16
Server load: medium (54%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.