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
AMJ83610.1D-3-phosphoglycerate dehydrogenase; Catalyzes the formation of 3-phosphonooxypyruvate from 3-phospho-D-glycerate in serine biosynthesis; can also reduce alpha ketoglutarate to form 2-hydroxyglutarate; 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.
  
 0.979
gpmA
Phosphoglyceromutase; Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate; Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily.
  
 0.908
AMJ82954.1
Kinase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.901
thrA
Bifunctional aspartokinase I/homoserine dehydrogenase I; Multifunctional homotetrameric enzyme that catalyzes the phosphorylation of aspartate to form aspartyl-4-phosphate as well as conversion of aspartate semialdehyde to homoserine; functions in a number of amino acid biosynthetic pathways; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.782
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.
    
   0.668
AMJ84825.1
Uridine kinase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
  0.590
AMJ83695.1
Threonine synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.563
rpiA
Ribose-5-phosphate isomerase; Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
     
 0.536
pyrD
Dihydroorotate dehydrogenase; Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor; Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.
 
    
 0.487
rplB
50S ribosomal protein L2; One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. Belongs to the universal ribosomal protein uL2 family.
    
   0.481
Your Current Organism:
Alteromonas mediterranea
NCBI taxonomy Id: 314275
Other names: A. mediterranea, Alteromonas mediterranea Ivanova et al. 2015, CIP 110805, DSM 17117, LMG 28347, LMG:28347, strain DE
Server load: low (26%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.