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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[Homology]
Score
folDTetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain protein; Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate. (279 aa)    
Predicted Functional Partners:
glyA
Glycine 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.
  
 0.969
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.
 
 
 0.957
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.
  
 
 0.919
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.
  
    0.845
MALL_0744
Hypothetical protein; Identified by glimmer; putative.
       0.773
MALL_0313
Putative metallophosphoesterase; Identified by match to protein family HMM PF00149.
      0.762
MALL_0549
Putative Xaa-Pro dipeptidase; Identified by match to protein family HMM PF00557; match to protein family HMM PF01321.
    
 0.709
def
Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
  
 
 0.683
folA
Dihydrofolate reductase; Identified by match to protein family HMM PF00186; Belongs to the dihydrofolate reductase family.
    
 0.654
MALL_0730
5'-3' exonuclease, SAM domain protein; Identified by match to protein family HMM PF01367; match to protein family HMM PF02739.
  
  
 0.654
Your Current Organism:
Mycoplasma alligatoris
NCBI taxonomy Id: 747682
Other names: M. alligatoris A21JP2, Mycoplasma alligatoris A21JP2, Mycoplasma alligatoris ATCC 700619, Mycoplasma alligatoris str. A21JP2, Mycoplasma alligatoris strain A21JP2
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.