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
ACP33585.1Putative secreted protein; Methionyl-tRNA formyltransferase. (209 aa)    
Predicted Functional Partners:
ACP32782.1
tRNA and rRNA cytosine-C5-methylases; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family.
  
  
 0.950
folD
Methylenetetrahydrofolate dehydrogenase; Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate.
  
 
 0.944
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.
  
  
  0.934
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.
 
  
 0.924
folA
Dihydrofolate reductase; Belongs to the dihydrofolate reductase family.
  
 
 0.912
gcvT
Glycine cleavage system T protein; The glycine cleavage system catalyzes the degradation of glycine.
   
 
 0.910
metS
Methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
     
 0.908
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.
     
 0.908
thyX-2
Hypothetical protein; 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 NADPH and FADH(2) as the reductant.
     
 0.906
thyX
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 NADPH and FADH(2) as the reductant.
     
 0.906
Your Current Organism:
Corynebacterium aurimucosum
NCBI taxonomy Id: 548476
Other names: C. aurimucosum ATCC 700975, Corynebacterium aurimucosum ATCC 700975, Corynebacterium aurimucosum CCUG 48176, Corynebacterium aurimucosum CIP 107436, Corynebacterium aurimucosum CN-1, Corynebacterium aurimucosum DSM 44827, Corynebacterium aurimucosum str. ATCC 700975, Corynebacterium aurimucosum strain ATCC 700975, Corynebacterium nigricans CN-1
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.