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
guaB1Inosine-5-monophosphate dehydrogenase (IMP dehydrogenase) (IMPDH) (IMPD) / GMP reductase); Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Belongs to the IMPDH/GMPR family. (506 aa)    
Predicted Functional Partners:
guaA
GMP synthase [glutamine-hydrolyzing] (Glutamine amidotransferase) (GMP synthetase); Catalyzes the synthesis of GMP from XMP.
 
 0.999
purA
Adenylosuccinate synthetase (IMP--aspartate ligase) (AdSS) (AMPSase); Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP; Belongs to the adenylosuccinate synthetase family.
 
 
 0.993
guA
Glutamine amidotransferase class-I; ATP + xanthosine 5 prime-phosphate + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate; inhibiteur Psicofuranin.
  
 
 0.981
purH
Phosphoribosylaminoimidazolecarboxamide formyltransferase (AICAR transformylase); 10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4- carboxamide and IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4- carboxamide.
  
 
 0.976
guaB2
Inosine-5-monophosphate dehydrogenase (IMP dehydrogenase) (IMPDH) (IMPD) / GMP reductase.
  
 
0.975
hpt
Guanine and 6-mercaptopurine can replace hypoxanthine; Belongs to the purine/pyrimidine phosphoribosyltransferase family.
    
 0.967
ribAB
GTP cyclohydrolase II protein, Riboflavin biosynthesis protein; Catalyzes the conversion of GTP to 2,5-diamino-6- ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate; Belongs to the GTP cyclohydrolase II family.
  
  
 0.945
CBL56291.1
HAM1, NTPase/HAM1; 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.
  
 0.927
guaB3
Inosine-5-monophosphate dehydrogenase (IMP dehydrogenase) (IMPDH) (IMPD) / GMP reductase; IMP + NAD+ + H2O <=> Xanthosine 5prime-phosphate + NADH + H+.
 
 
0.927
purB
Adenylosuccinate lyase; N6-(1,2-Dicarboxyethyl)-AMP <=> Fumarate + AMP 1-(5prime-Phosphoribosyl)-5-amino-4-(N- succinocarboxamide)-imidazole These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits; Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.
  
  
 0.926
Your Current Organism:
Propionibacterium freudenreichii
NCBI taxonomy Id: 754252
Other names: P. freudenreichii subsp. shermanii CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii ATCC 9614, Propionibacterium freudenreichii subsp. shermanii CIP 103027, Propionibacterium freudenreichii subsp. shermanii CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii str. CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii strain CIRM-BIA1
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