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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
purUFormyltetrahydrofolate deformylase; Catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to formate and tetrahydrofolate (FH4). (290 aa)    
Predicted Functional Partners:
folD
5,10-methylenetetrahydrofolate dehydrogenase (NADP+), methenyltetrahydrofolate cyclohydrolase; Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate.
 
 
 0.951
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.
  
 
 0.940
purN
Formyltetrahydrofolate-dependent 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.
 
  
0.932
gcvT
Aminomethyltransferase; The glycine cleavage system catalyzes the degradation of glycine.
  
 
 0.931
AFY69301.1
Methionine synthase (B12-dependent); 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.
    
 0.917
thyX
Thymidylate synthase thyX; 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 NADPH and FADH(2) as the reductant.
     
  0.900
mdh
Malate dehydrogenase (NAD); Catalyzes the reversible oxidation of malate to oxaloacetate. Belongs to the LDH/MDH superfamily. MDH type 3 family.
     
  0.800
AFY69337.1
Fumarate hydratase class II; PFAM: Fumarase C C-terminus; Lyase; TIGRFAM: aspartate ammonia-lyase; COGs: COG1027 Aspartate ammonia-lyase; HAMAP: Fumarate hydratase, class II; InterPro IPR022761:IPR018951:IPR005677; KEGG: ava:Ava_3556 aspartate ammonia-lyase; PFAM: Lyase 1, N-terminal; Fumarase C, C-terminal; PRIAM: Aspartate ammonia-lyase; SPTR: Aspartate ammonia-lyase.
     
  0.800
pckA
Phosphoenolpyruvate carboxykinase (ATP); Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
     
  0.800
amiF
Formamidase; Is an aliphatic amidase with a restricted substrate specificity, as it only hydrolyzes formamide; Belongs to the carbon-nitrogen hydrolase superfamily. Aliphatic amidase family.
     
  0.800
Your Current Organism:
Pseudanabaena sp. PCC7367
NCBI taxonomy Id: 82654
Other names: Calotaxis gracile PCC 7367, P. sp. PCC 7367, Pseudanabaena PCC7367, Pseudanabaena sp. PCC 7367
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