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
phoBAlkaline phosphatase; Modular protein that consists of a N-terminal conserved domain of unknown function (240 residues) and a C-terminal Alkaline phosphatase domain; Signal peptide cleaved between the residues 22 and 23; Localized in the periplasmic space; Specificity unclear. (602 aa)    
Predicted Functional Partners:
PhoD2
Alkaline phosphatase is a zinc and magnesium-containing metalloenzyme which hydrolyzes phosphate esters, optimally at high pH; Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymic activity; Signal peptide cleaved between the residues 18 and 19; Localized in the periplasmic space; Conserved hypothetical protein.
  
 
 0.926
phoD1
Alkaline phosphatase is a zinc and magnesium-containing metalloenzyme which hydrolyzes phosphate esters, optimally at high pH; Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymic activity; Localized in the cytoplasm; High confidence in function and specificity.
  
 
 0.926
phoD3
Alkaline phosphatase is a zinc and magnesium-containing metalloenzyme which hydrolyzes phosphate esters, optimally at high pH; Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymic activity; Signal peptide of lipoprotein cleaved between the residues 16 and 17; Localized in the outer membrane; High confidence in function and specificity.
  
 
 0.926
phoA
Alkaline phosphatase is a zinc and magnesium-containing metalloenzyme which hydrolyzes phosphate esters, optimally at high pH; Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymic activity; Signal peptide cleaved between the residues 26 and 27; Localized in the periplasmic space; High confidence in function and specificity.
  
  
 
0.925
folE1
GTP cyclohydrolase I catalyzes the biosynthesis of formic acid and dihydroneopterin triphosphate from GTP. This reaction is the first step in the biosynthesis of tetrahydrofolate. FolE is a homodecamer, composed of a dimer of pentamers. It is an allosteric enzyme, whose activity is modulated by K(+), divalent cations, UTP, and tetrahydrobiopterin. Tetrahydrobiopterin is an inhibitor of this enzyme. Localized in the cytoplasm; High confidence in function and specificity.
   
 
  0.901
CAZ97793.1
Conserved protein distantly related to Thiamine-phosphate synthase (ThiE); Localized in the cytoplasm; Function unclear.
    
  0.901
thiE
Thiamine-phosphate pyrophosphorylase; Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). Belongs to the thiamine-phosphate synthase family.
    
  0.901
folE2
GTP cyclohydrolase I catalyzes the biosynthesis of formic acid and dihydroneopterin triphosphate from GTP. This reaction is the first step in the biosynthesis of tetrahydrofolate. FolE is a homodecamer, composed of a dimer of pentamers. It is an allosteric enzyme, whose activity is modulated by K(+), divalent cations, UTP, and tetrahydrobiopterin. Tetrahydrobiopterin is an inhibitor of this enzyme. Localized in the cytoplasm; High confidence in function and specificity.
   
 
  0.901
folE3
GTP cyclohydrolase I catalyzes the biosynthesis of formic acid and dihydroneopterin triphosphate from GTP. This reaction is the first step in the biosynthesis of tetrahydrofolate. FolE is a homodecamer, composed of a dimer of pentamers. It is an allosteric enzyme, whose activity is modulated by K(+), divalent cations, UTP, and tetrahydrobiopterin. Tetrahydrobiopterin is an inhibitor of this enzyme. Localized in the cytoplasm; High confidence in function and specificity.
   
 
  0.901
ptsA
6-Pyruvoyl tetrahydrobiopterin synthase catalyses the conversion of dihydroneopterin triphosphate to 6-pyruvoyl tetrahydropterin, the second of three enzymatic steps in the synthesis of tetrahydrobiopterin from GTP. Tetrahydrobiopterin is the cofactor for several aromatic amino acid monooxygenases. The enzyme is a homohexameric, composed of a dimer of trimers. A transition metal binding site formed by the three histidine residues is present in each subunit, and bound Zn(II) is responsible for the enzymatic activity; Localized in the cytoplasm; High confidence in function and specificity.
     
  0.900
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
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