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
serAD-3-phosphoglycerate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. (409 aa)    
Predicted Functional Partners:
serC
3-phosphoserine/phosphohydroxythreonine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.
  
 0.983
gpmI
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate.
    
 0.905
hom
Homoserine dehydrogenase; Catalyzes the formation of L-aspartate 4-semialdehyde from L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.797
AMR65422.1
FAD-linked oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.684
thrC
Threonine synthase; Catalyzes the formation of L-threonine from O-phospho-L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.556
serB
Phosphoserine phosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.485
leuB
3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
  
  
 0.472
topA
DNA topoisomerase I subunit omega; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus rem [...]
 
   
 0.471
metH
Methionine synthase; 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.
   
  
 0.461
rplF
50S ribosomal protein L6; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center; Belongs to the universal ribosomal protein uL6 family.
    
   0.447
Your Current Organism:
Pseudomonas alcaligenes
NCBI taxonomy Id: 43263
Other names: ATCC 14909, CFBP 2437, CIP 101034, DSM 50342, IAM 12411, IFO 14159, JCM 5967, NBRC 14159, NCCB 76044, NCTC 10367, P. alcaligenes, VKM B-2171
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.