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
pdxHPyridoxamine 5'-phosphate oxidase; Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). (218 aa)    
Predicted Functional Partners:
pdxY
Pyridoxamine kinase; Pyridoxal kinase involved in the salvage pathway of pyridoxal 5'-phosphate (PLP). Catalyzes the phosphorylation of pyridoxal to PLP.
    
 0.986
pdxJ
Pyridoxine 5'-phosphate synthase; Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino- 2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
     
 0.980
tyrS
tyrosyl-tRNA synthetase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily.
     
 0.722
nnrE
Carbohydrate kinase; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epim [...]
    
 0.633
gcvP
Glycine dehydrogenase; 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; Belongs to the GcvP family.
 
   
 0.540
KKF35146.1
Catalyzes the formation hydroxymethylpyrimidine phosphate from hydroxymethylpyrimidine and the formation of of 4-amino-2-methyl-5-diphosphomethylpyrimidine from hydroxymethylpyrimidine phosphate; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.502
pyrB
Aspartate carbamoyltransferase catalytic subunit; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
      0.478
KKF38105.1
UMP phosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.469
KKF35038.1
Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
  0.444
pgk
Phosphoglycerate kinase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the phosphoglycerate kinase family.
  
  
 0.437
Your Current Organism:
Erwinia tracheiphila
NCBI taxonomy Id: 65700
Other names: ATCC 33245, Bacillus tracheiphilus, Bacterium tracheiphilus, CFBP 2355, CIP 105205, DSM 21139, E. tracheiphila, Erwinia amylovora var. tracheiphila, ICMP 5845, LMG 2707, LMG 2906, LMG:2707, LMG:2906, NCPPB 2452
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