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
EHA62282.1Phosphoglucosamine mutase; KEGG: pmf:P9303_24991 phosphotransferase superclass; PFAM: Alpha-D-phosphohexomutase, alpha/beta/alpha domain I; Alpha-D-phosphohexomutase, alpha/beta/alpha domain II; Alpha-D-phosphohexomutase, alpha/beta/alpha domain III; Alpha-D-phosphohexomutase, C-terminal. (487 aa)    
Predicted Functional Partners:
EHA62424.1
TIGRFAM: Mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; KEGG: pmf:P9303_26031 mannose-1-phosphate guanylyltransferase; PFAM: Mannose-6-phosphate isomerase, type II, C-terminal; Nucleotidyl transferase.
  
 
 0.910
EHA63856.1
TIGRFAM: Glucose-1-phosphate adenylyltransferase; KEGG: pmf:P9303_16851 glucose-1-phosphate adenylyltransferase; PFAM: Nucleotidyl transferase; Belongs to the bacterial/plant glucose-1-phosphate adenylyltransferase family.
  
 
 0.907
EHA62345.1
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.
  
 
 0.903
cugP
Mannose-1-phosphate guanylyltransferase; Catalyzes the formation of UDP-glucose, from UTP and glucose 1-phosphate.
  
 
 0.883
pgi
KEGG: pmf:P9303_15071 glucose-6-phosphate isomerase; HAMAP: Phosphoglucose isomerase (PGI); PFAM: Phosphoglucose isomerase (PGI); Belongs to the GPI family.
    
 0.872
EHA62283.1
Nucleoside-triphosphatase rdgB; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family.
 
   
 0.826
glmS
Glucosamine--fructose-6-phosphate aminotransferase (isomerizing); Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
 
 
 0.815
dacA
Conserved hypothetical protein CHP00159; Catalyzes the condensation of 2 ATP molecules into cyclic di- AMP (c-di-AMP), a second messenger used to regulate differing processes in different bacteria.
 
 
 
 0.811
glmU
Bifunctional protein glmU; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain.
    
 0.783
EHA60584.1
KEGG: pmt:PMT1614 phosphoglucomutase; PFAM: Alpha-D-phosphohexomutase, alpha/beta/alpha domain I; Alpha-D-phosphohexomutase, alpha/beta/alpha domain II; Alpha-D-phosphohexomutase, alpha/beta/alpha domain III; Alpha-D-phosphohexomutase, C-terminal.
 
 
0.781
Your Current Organism:
Synechococcus sp. WH 8016
NCBI taxonomy Id: 166318
Other names: S. sp. WH 8016, Synechococcus sp. WH8016
Server load: low (26%) [HD]