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
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Textmining
[Homology]
Score
glmSGlucosamine/fructose-6-phosphate aminotransferase, isomerizing; Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. (616 aa)    
Predicted Functional Partners:
glmM
Phosphoglucosamine mutase; Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate; Belongs to the phosphohexose mutase family.
 
 0.989
glmU
UDP-N-acetylglucosamine pyrophosphorylase; 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.
  
 0.965
Srot_0384
KEGG: rop:ROP_35350 glutamate synthase large subunit; PFAM: ferredoxin-dependent glutamate synthase; glutamine amidotransferase class-II; glutamate synthase; glutamate synthase alpha subunit domain protein.
   
 0.956
Srot_2679
KEGG: mab:MAB_2486c glutamate synthase, large subunit; PFAM: ferredoxin-dependent glutamate synthase; glutamine amidotransferase class-II; glutamate synthase; glutamate synthase alpha subunit domain protein.
   
 0.956
Srot_0533
KEGG: rop:ROP_08930 glutamine synthetase I; TIGRFAM: glutamine synthetase, type I; PFAM: glutamine synthetase catalytic region; glutamine synthetase beta-Grasp.
 
 
 0.933
carB
KEGG: nfa:nfa36190 carbamoyl phosphate synthase large subunit; TIGRFAM: carbamoyl-phosphate synthase, large subunit; PFAM: Carbamoyl-phosphate synthase L chain ATP- binding; Carbamoyl-phosphate synthetase large chain domain protein; Carbamoyl-phosphate synthetase large chain oligomerisation; MGS domain protein; Belongs to the CarB family.
   
 0.929
pgi
KEGG: nfa:nfa49980 glucose-6-phosphate isomerase; PFAM: phosphoglucose isomerase (PGI); Belongs to the GPI family.
  
 
 0.926
Srot_0812
KEGG: rop:ROP_08840 glutamine synthetase I; TIGRFAM: glutamine synthetase, type I; PFAM: glutamine synthetase catalytic region; glutamine synthetase beta-Grasp.
  
 
 0.922
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 [...]
    
 0.913
purF
Amidophosphoribosyltransferase; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.
    
0.912
Your Current Organism:
Segniliparus rotundus
NCBI taxonomy Id: 640132
Other names: S. rotundus DSM 44985, Segniliparus rotundus ATCC BAA-972, Segniliparus rotundus CIP 108378, Segniliparus rotundus DSM 44985, Segniliparus rotundus JCM 13578, Segniliparus rotundus str. DSM 44985, Segniliparus rotundus strain DSM 44985
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