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purN purN purM purM purH purH purD purD purQ purQ purL purL yexA yexA glyA glyA ftfL ftfL purF purF ACS38751.1 ACS38751.1
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Predicted Interactions
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textmining
co-expression
protein homology
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purNPhosphoribosylglycinamide formyltransferase 1; 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. (219 aa)    
Predicted Functional Partners:
purM
Phosphoribosylaminoimidazole synthetase (AIR synthetase); Function of homologous gene experimentally demonstrated in an other organism; enzyme.
  
 0.999
purH
Bifunctional: IMP cyclohydrolase (N-terminal); Function of homologous gene experimentally demonstrated in an other organism; enzyme.
 0.999
purD
Phosphoribosylglycinamide synthetase (GAR synthetase); Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the GARS family.
 
 0.999
purQ
Phosphoribosylformylglycinamidine synthase I; Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP- dependent manner. PurS interacts with PurQ and PurL and is thought to assist i [...]
 
 
 0.992
purL
Phosphoribosylformylglycinamide synthetase; Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP- dependent manner. PurS interacts with PurQ and PurL and is thought to assist in [...]
 
 
 0.991
yexA
Phosphoribosylformylglycinamidine synthetase PurS; Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP- dependent manner. PurS interacts with PurQ and PurL and is thought to ass [...]
  
 
 0.989
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.
  
 0.988
ftfL
Formate-tetrahydrofolate ligase (formyltetrahydrofolate synthetase) (FHS) (FTHFS); Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the formate--tetrahydrofolate ligase family.
  
 0.982
purF
Amidophosphoribosyltransferase (PRPP amidotransferase); Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine; In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.
 
 
 0.972
ACS38751.1
Putative Formyl transferase (fmt-like); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
    
 0.967
Your Current Organism:
Methylorubrum extorquens
NCBI taxonomy Id: 272630
Other names: M. extorquens AM1, Methylobacterium extorquens AM1, Methylorubrum extorquens AM1, Pseudomonas sp. AM1
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