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:
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Gene Fusion
Cooccurrence
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[Homology]
Score
metKS-adenosylmethionine synthetase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. (389 aa)    
Predicted Functional Partners:
M2A_3179
5,10-methylenetetrahydrofolate reductase; Belongs to the methylenetetrahydrofolate reductase family.
  
 
 0.949
M2A_3177
Methionine synthase; 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.
    
 0.923
ribH
6,7-dimethyl-8-ribityllumazine synthase; Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2- butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
  
 
 0.912
ahcY
S-adenosyl-L-homocysteine hydrolase; May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.
 
 
 0.909
guaA
GMP synthase; Catalyzes the synthesis of GMP from XMP.
 
  
 0.874
M2A_3215
XRE family transcriptional regulator.
    
 0.873
speH
S-adenosylmethionine decarboxylase-like protein; Catalyzes the decarboxylation of S-adenosylmethionine to S- adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine; Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.
    
 0.852
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.
  
 
 0.827
glyA-2
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.
  
 
 0.827
ispDF
IspD/ispF bifunctional enzyme; Bifunctional enzyme that catalyzes the formation of 4- diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D- erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4- diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C- methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF).
    
 0.758
Your Current Organism:
Tepidicaulis marinus
NCBI taxonomy Id: 1333998
Other names: DSM 27167, NBRC 109643, T. marinus, Tepidicaulis marinus Takeuchi et al. 2015, alpha proteobacterium MA2, strain MA2
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