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
ftcdMethenyltetrahydrofolate cyclohydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. (212 aa)    
Predicted Functional Partners:
folD-2
Methenyltetrahydrofolate cyclohydrolase; Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate.
   
 0.996
folD
5,10-methylene-tetrahydrofolate cyclohydrolase; Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate.
   
 0.957
fhs
Formate--tetrahydrofolate ligase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the formate--tetrahydrofolate ligase family.
 
  
 0.947
gcvT
Glycine cleavage system protein T; The glycine cleavage system catalyzes the degradation of glycine.
  
 
 0.933
yqgN
5-formyltetrahydrofolate cyclo-ligase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the 5-formyltetrahydrofolate cyclo-ligase family.
    
 0.927
fmt
methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family.
    
 0.918
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.
     
 0.912
purH
Phosphoribosylaminoimidazolecarboxamide formyltransferase; Involved in de novo purine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.906
purU
Formyltetrahydrofolate deformylase; Catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to formate and tetrahydrofolate (FH4).
    
  0.902
purT
Phosphoribosylglycinamide 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.
     
  0.900
Your Current Organism:
Paenibacillus polymyxa
NCBI taxonomy Id: 1406
Other names: ATCC 842, Aerobacillus polymyxa, Bacillus polymyxa, Bacillus sp. NCIM 2538, Bacillus sp. NCIM 2540, Bacillus sp. NCIM 2726, Bacillus sp. RP 2.2, CCUG 7426, CFBP 4258, CIP 66.22, Clostridium polymyxa, DSM 36, Granulobacter polymyxa, HAMBI 635, IAM 13419, IFO 15309, JCM 2507, LMG 13294, LMG:13294, NBRC 15309, NCCB 24016, NCIB 8158, NCIB:8158, NCTC 10343, NRRL B-4317, P. polymyxa, Paenibacillus sp. JCM 8035, Paenibacillus sp. JCM 8036, Paenibacillus sp. JCM 8037, Paenibacillus sp. JCM 8038, Paenibacillus sp. JCM 8039, Paenibacillus sp. WLY78, VKM B-514
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