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:
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Gene Fusion
Cooccurrence
Coexpression
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[Homology]
Score
purTPhosphoribosylglycinamide formyltransferase; Non-folate utilizing enzyme, catalyzes the production of beta-formyl glycinamide ribonucleotide from formate, ATP, and beta-GAR and a side reaction producing acetyl phosphate and ADP from acetate and ATP; involved in de novo purine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology. (394 aa)    
Predicted Functional Partners:
purL
Phosphoribosylformylglycinamidine synthase; Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate.
  
  
 0.995
purE
N5-carboxyaminoimidazole ribonucleotide mutase; Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
  
 0.941
AMA46884.1
Phosphoribosylglycinamide formyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.915
gltB
Glutamate synthase large subunit; Catalyzes the formation of glutamate from glutamine and alpha-ketoglutarate; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.767
purM
Phosphoribosylaminoimidazole synthetase; Catalyzes the formation of 1-(5-phosphoribosyl)-5-aminoimidazole from 2-(formamido)-N1-(5-phosphoribosyl)acetamidine and ATP in purine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.726
purD
Phosphoribosylamine--glycine ligase; Catalyzes the formation of N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-D-ribosylamine and glycine in purine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the GARS family.
  
  
 0.707
AMA44788.1
Phosphate acetyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.702
purF
Amidophosphoribosyltransferase; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine; In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.
  
  
 0.689
purC
Phosphoribosylaminoimidazolesuccinocarboxamide synthase; Catalyzes the formation of (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido)succinate from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate and L-aspartate in purine biosynthesis; SAICAR synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.687
rimK
Ribosomal protein S6 modification protein; Responsible for the addition of glutamate residues to the C-terminus of ribosomal protein S6; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the RimK family.
     
 0.675
Your Current Organism:
Pseudomonas monteilii
NCBI taxonomy Id: 76759
Other names: ATCC 700476, CCUG 38736, CFML 90-60, CIP 104883, DSM 14164, JCM 21585, NBRC 103158, P. monteilii, Pseudomonas sp. MKP 213, Pseudomonas sp. V7SW2
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