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
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
dfrADihydrofolate reductase; Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. (165 aa)    
Predicted Functional Partners:
thyA
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.
 
 0.999
CAZ94941.1
Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein.
      0.976
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
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.
  
 
 0.918
purH
Bifunctional enzyme that catalyses the last two steps in de novo purine biosynthesis. The second last step is catalysed by 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR) formyltransferase that catalyses the formylation of AICAR with 10-formyl-tetrahydrofolate to yield 5-formylaminoimidazole-4-carboxamide ribonucleotide (FAICAR) and tetrahydrofolate. The last step is catalysed by IMP (Inosine monophosphate) cyclohydrolase, cyclizing FAICAR to IMP; Belongs to the purH family; Localized in the cytoplasm; High confidence in function and specificity.
    
 0.914
gcvT
Glycine cleavage system T protein; The glycine cleavage system catalyzes the degradation of glycine.
  
 
 0.914
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.
   
 
 0.913
purU
Formyltetrahydrofolate deformylase; Catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to formate and tetrahydrofolate (FH4).
    
 0.912
metH-2
Methionine synthase, homocysteine-binding module; Methionine synthase or 5-methyltetrahydrofolate-homocysteine S-methyltransferase catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate; L-homocysteine is bound via the zinc atom; Uses the cobalamin (vitamin B12) and zinc as cofactors; This sequence corresponds to the homocysteine-binding domain (Hcy-binding domain) only; Belongs to the vitamin-B12 dependent methionine synthase family; Localize [...]
    
 0.911
folC
Bifunctional enzyme that converts the folates to polyglutamate derivatives; Folylpolyglutamate synthase (EC 6.3.2.17) is responsible for the ATP-dependent addition of a polyglutamate tail to tetrahydrofolate. Dihydrofolate synthase (EC 6.3.2.12) is reponsible for attaching the first glutamate residue to dihydropteroate to form dihydrofolate. The combined activity leads to the formation of the coenzyme polyglutamated tetrahydropteroate (H4PteGlu(n)), i.e. various tetrahydrofolates (H4folate); Localized in the cytoplasm; High confidence in function and specificity.
     
 0.911
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
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