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
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[Homology]
Score
glyASerine 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. (408 aa)    
Predicted Functional Partners:
purH
IMP cyclohydrolase; SMART: MGS-like domain; Pfam: MGS-like domain; SMART: AICARFT/IMPCHase bienzyme; Pfam: AICARFT/IMPCHase bienzyme; TIGRFAM: purH: phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase.
  
 0.985
folD
5,10-methylene-tetrahydrofolate dehydrogenase; Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate.
  
 0.972
fhs
Pfam: Formate--tetrahydrofolate ligase; Belongs to the formate--tetrahydrofolate ligase family.
  
 0.970
AMK53167.1
Hypothetical protein; 'Pfam: CobB/CobQ-like glutamine amidotransferase domain; Pfam: AIR synthase related protein, N-terminal domain; Pfam: AIR synthase related protein, C-terminal domain; TIGRFAM: FGAM-synthase: phosphoribosylformylglycinamidine synthase'.
  
  
 0.968
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.
  
 0.967
AMK53656.1
L-serine ammonia-lyase; Pfam: Serine dehydratase alpha chain; Pfam: Serine dehydratase beta chain.
  
 
 0.961
AMK54795.1
Hypothetical protein; Pfam: Methylenetetrahydrofolate reductase; Pfam: Homocysteine S-methyltransferase.
  
 
 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.
  
 
 0.938
AMK54329.1
L-threonine aldolase; Pfam: Beta-eliminating lyase.
   
 0.936
AMK55506.1
Threonine ammonia-lyase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
    
 0.932
Your Current Organism:
Faecalibaculum rodentium
NCBI taxonomy Id: 1702221
Other names: Allobaculum sp. Alo17, Erysipelotrichaceae bacterium Alo17, F. rodentium, Faecalibaculum rodentium Chang et al. 2016 emend. Cox et al. 2017, JCM 30274, KCTC 15484, strain ALO17
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