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
mioXMyo-inositol oxygenase is a non-heme iron enzyme, which catalyzes the conversion of myo-inositol to D-glucuronic acid. This enzyme can be either involved of in myo-inositol catabolism or in UDP-glucuronic acid biosynthesis. Localized in cytoplasm; High confidence in function and specificity. (269 aa)    
Predicted Functional Partners:
siaHI
Exo-alpha-sialidase catalyzes the hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates. Features a twin-arginine signal peptide. Localized in the periplasm; High confidence in function and specificity.
  
 
 0.915
uxaC
Uronate isomerase catalyzes the reaction D-glucuronate to D-fructuronate and also converts D-galacturonate to D-tagaturonate. It is involved in the pentose and glucuronate interconversion. Localized in the cytoplasm; High confidence in function and specificity.
    
 0.809
nglA
Alpha-N-acetylglucosaminidase, family GH89; Alpha-N-acetylglucosaminidase catalyzes the hydrolysis of terminal non-reducing N-acetyl-D-glucosamine residues in N-acetyl-alpha-D-glucosaminides. It belongs to the family 89 of the glycoside hydrolases. In human, this enzyme is involved in the degradation of heparan sulfate. Signal peptide cleaved between the residues 20 and 21. Localized in the periplasmic space; High confidence in function and specificity.
 
     0.710
CAZ94683.1
Sodium/solute symporter; Sodium/substrate symport is a widespread mechanism of solute transport across cytoplasmic membranes of cells. Thereby the energy stored in an inwardly directed electrochemical sodium gradient (sodium motive force, SMF) is used to drive solute accumulation against a concentration gradient; Contains fourteen transmembrane helices; Localized in the cytoplasmic membrane; Specificity unclear; Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
       0.607
CAZ95738.1
Conserved hypothetical membrane protein; Contains nine transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein.
 
     0.476
CAZ94181.1
Conserved hypothetical lipoprotein; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Conserved hypothetical protein.
  
     0.454
CAZ97205.1
Chitin-binding lectin, family GH18; This protein is homologous to chitinases but the catalytic acidic residues are replaced by polar residues. It likely binds chitin or chitin-derived oligosaccharides; Belongs to the family 18 of the glycoside hydrolases (GH18); Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 24 and 25; Localized in the outer membrane; Function unclear.
  
   
 0.418
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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