STRINGSTRING
gcvT protein (Bacillus subtilis) - STRING interaction network
"gcvT" - Aminomethyltransferase in Bacillus subtilis
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second shell of interactors
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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gcvTAminomethyltransferase; The glycine cleavage system catalyzes the degradation of glycine (362 aa)    
Predicted Functional Partners:
gcvPA
Probable glycine dehydrogenase (decarboxylating) subunit 1; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (By similarity) (448 aa)
  0.999
gcvPB
Probable glycine dehydrogenase (decarboxylating) subunit 2; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (By similarity); Belongs to the GcvP family. C-terminal subunit subfamily (488 aa)
  0.999
gcvH
Glycine cleavage system H protein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein (127 aa)
  0.999
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 (By similarity); Belongs to the SHMT family (415 aa)
 
  0.997
folD
Bifunctional protein FolD; Catalyzes the oxidation of 5,10- methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10- formyltetrahydrofolate (283 aa)
   
 
  0.989
samT
Bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase; Evidence 2a- Function of homologous gene experimentally demonstrated in an other organism; Product type e - enzyme; In the C-terminal section; belongs to the methylenetetrahydrofolate reductase family (612 aa)
   
 
  0.978
acoL
Dihydrolipoyl dehydrogenase; Evidence 1a- Function experimentally demonstrated in the studied strain; Product type e- enzyme; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family (458 aa)
 
 
  0.954
lpdV
Dihydrolipoyl dehydrogenase; The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components- branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3); Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family (474 aa)
 
 
  0.954
pdhD
Dihydrolipoyl dehydrogenase; Catalyzes the oxidation of dihydrolipoamide to lipoamide; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family (470 aa)
 
 
  0.948
purH
Bifunctional purine biosynthesis protein PurH; Evidence 2a- Function of homologous gene experimentally demonstrated in an other organism; Product type e - enzyme (512 aa)
     
  0.942
Your Current Organism:
Bacillus subtilis
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis, Bacillus subtilis 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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