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
KPD25145.1Phosphoserine phosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology. (216 aa)    
Predicted Functional Partners:
hisI
phosphoribosyl-ATP pyrophosphatase; Catalyzes the formation of 1-(5-phosphoribosyl)-AMP from 1-(5-phosphoribosyl)-ATP and the subsequent formation of 1-(5-phosphoribosyl)-5-((5- phosphoribosylamino)methylideneamino)imidazole-4- carboxamide from 1-(5-phosphoribosyl)-AMP in histidine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; In the N-terminal section; belongs to the PRA-CH family.
  
  
 0.980
serC
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.
  
 
 0.963
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.
   
 0.952
KPD24075.1
Aspartate kinase; Derived by automated computational analysis using gene prediction method: Protein Homology; In the C-terminal section; belongs to the homoserine dehydrogenase family.
  
 
 0.922
trpF
Phosphoribosylanthranilate isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TrpC family.
    
 0.882
trpB
Tryptophan synthase subunit beta; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
   
 
 0.856
KPD25008.1
Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family.
   
 
 0.853
KPD24377.1
Cystathionine beta-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.847
hisB
Imidazoleglycerol-phosphate dehydratase; Catalyzes the formation of 3-(imidazol-4-yl)-2-oxopropyl phosphate from D-ethythro-1-(imidazol-4-yl)glycerol 3-phosphate and histidinol from histidinol phosphate; Derived by automated computational analysis using gene prediction method: Protein Homology; In the N-terminal section; belongs to the histidinol- phosphatase family.
  
  
 0.843
KPD23339.1
CDP-diacylglycerol--serine O-phosphatidyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
    
  0.832
Your Current Organism:
Idiomarina zobellii
NCBI taxonomy Id: 86103
Other names: ATCC BAA-313, I. zobellii, Idiomarina zobellii Ivanova et al. 2000, KMM 231, marine bacterium KM231
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