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
purTPhosphoribosylglycinamide formyltransferase; Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate; Belongs to the PurK/PurT family. (393 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.
  
 
 0.993
purE
N5-carboxyaminoimidazole ribonucleotide mutase; Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
 
 0.981
purH
Phosphoribosylaminoimidazolecarboxamide formyltransferase; Involved in de novo purine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.904
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.
  
 
 0.895
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.
  
 
 0.868
purN
Phosphoribosylglycinamide formyltransferase; Catalyzes the transfer of a formyl group from 10- formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate.
   
 
 0.835
purC
Phosphoribosylaminoimidazole-succinocarboxamide 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.
  
 
 0.818
purF
Amidophosphoribosyltransferase; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine; In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.
  
 
 0.730
OBX08031.1
Phosphate acetyltransferase; Involved in acetate metabolism. In the N-terminal section; belongs to the CobB/CobQ family.
    
 0.699
OBX06588.1
Malic enzyme; NADP-dependent; catalyzes the oxidative decarboxylation of malate to form pyruvate; decarboxylates oxaloacetate; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.690
Your Current Organism:
Gallibacterium salpingitidis
NCBI taxonomy Id: 505341
Other names: CCUG 15564, CCUG 36325, G. salpingitidis, Gallibacterium salpingitidis Bisgaard et al. 2009, Gallibacterium sp. 18469/18, Gallibacterium sp. 19987/2, Gallibacterium sp. BK1010/1, Gallibacterium sp. F150, NCTC 11414, strain F150
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