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
fgsFolylpolyglutamate synthase; Belongs to the folylpolyglutamate synthase family. (434 aa)    
Predicted Functional Partners:
ARP41089.1
Dihydropteroate synthase; Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8- dihydropteroate (H2Pte), the immediate precursor of folate derivatives.
 
 0.998
folK
2-amino-4-hydroxy-6hydroxymethyldihydropteridine pyrophosphokinase.
  
 0.958
dfrD
Dihydrofolate reductase; Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
     
 0.934
thyA_1
Thymidylate synthase; Catalyzes the reductive methylation of 2'-deoxyuridine-5'- monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by- product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
     
 0.869
valS
Valine--tRNA ligase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily.
 
  
 0.754
glyA
Serine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
  
 0.752
folE
GTP cyclohydrolase 1.
  
  
 0.696
folB
Dihydroneopterin aldolase; Catalyzes the conversion of 7,8-dihydroneopterin to 6- hydroxymethyl-7,8-dihydropterin.
  
  
 0.696
ARP43660.1
Hypothetical protein.
       0.675
guaA_2
GMP synthase; Catalyzes the synthesis of GMP from XMP.
 
  
 0.655
Your Current Organism:
Geobacillus thermodenitrificans
NCBI taxonomy Id: 33940
Other names: ATCC 29492, BGSC 94A1, Bacillus sp. BGSC W9A21, Bacillus sp. BGSC W9A45, Bacillus sp. BGSC W9A5, Bacillus sp. BGSC W9A54, Bacillus sp. BGSC W9A65, Bacillus sp. BGSC W9A66, Bacillus sp. BGSC W9A67, Bacillus sp. BGSC W9A69, Bacillus sp. BGSC W9A71, Bacillus sp. BGSC W9A73, Bacillus sp. BGSC W9A74, Bacillus sp. BGSC W9A86, Bacillus sp. BGSC W9A87, Bacillus sp. BGSC W9A91, Bacillus thermodenitrificans, DSM 465, G. thermodenitrificans, Geobacillus sp. A333, Geobacillus sp. F84a, Geobacillus sp. G11MC16, Geobacillus thermodenitrificans (Manachini et al. 2000) Nazina et al. 2001 emend. Cihan et al. 2011, Geobacillus thermodenitrificans (Manachini et al. 2000) Nazina et al. 2001 emend. Coorevits et al. 2012, LMG 17532, LMG:17532, strain R-35647
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