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
glmSGlutamine--fructose-6-phosphate aminotransferase; Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. (604 aa)    
Predicted Functional Partners:
glmM
Phosphoglucosamine mutase; Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate; Belongs to the phosphohexose mutase family.
 
 0.980
ANK62757.1
Type I glutamate--ammonia ligase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.962
nagB
Glucosamine-6-phosphate deaminase; Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
  
 
 0.937
glmU
Glucosamine-1-phosphate N-acetyltransferase; 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.
  
 0.931
ANK61318.1
N-acetylglucosamine-6-phosphate deacetylase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.927
pgi
Glucose-6-phosphate isomerase; Functions in sugar metabolism in glycolysis and the Embden-Meyerhof pathways (EMP) and in gluconeogenesis; catalyzes reversible isomerization of glucose-6-phosphate to fructose-6-phosphate; member of PGI family; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the GPI family.
  
 
 0.923
ANK62269.1
Carbamoyl phosphate synthase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.919
carB
Carbamoyl phosphate synthase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the CarB family.
   
 0.919
purF
Amidophosphoribosyltransferase; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine; In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.
    
0.917
purQ
Phosphoribosylformylglycinamidine synthase I; Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP- dependent manner. PurS interacts with PurQ and PurL and is thought to assist i [...]
    
 0.917
Your Current Organism:
Lactobacillus backii
NCBI taxonomy Id: 375175
Other names: DSM 18080, JCM 18665, L. backii, LMG 23555, LMG:23555, Lactobacillus backi, Lactobacillus backii Tohno et al. 2013, strain L1062
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