close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING newly available directed regulatory networks a new typed view showing functional, physical, and regulatory edges in one network new clustering options and cluster-based layouts … and much more!
Explore STRING v12.5 →
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
pdxHPyridoxamine 5'-phosphate oxidase; Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). (214 aa)    
Predicted Functional Partners:
pdxY
Pyridoxamine kinase; Pyridoxal kinase involved in the salvage pathway of pyridoxal 5'-phosphate (PLP). Catalyzes the phosphorylation of pyridoxal to PLP.
    
 0.948
pdxJ
Pyridoxine 5'-phosphate synthase; Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino- 2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
  
  
 0.947
pyrB_1
Aspartate carbamoyltransferase; Catalyzes the conversion of carbamoyl phosphate and aspartate to form N-carbamoyl aspartate; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the aspartate/ornithine carbamoyltransferase superfamily.
      0.860
carB
Carbamoyl phosphate synthase large subunit; Four CarB-CarA dimers form the carbamoyl phosphate synthetase holoenzyme that catalyzes the production of carbamoyl phosphate; CarB is responsible for the amidotransferase activity; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.640
moeB_1
Heme biosynthesis protein HemY; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.569
AOI85434.1
Fe-S protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
      0.558
gcvP
Glycine dehydrogenase (aminomethyl-transferring); The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family.
 
   
 0.551
AOI83456.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
     0.551
pdxA
4-hydroxythreonine-4-phosphate dehydrogenase; Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L- threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
  
   
 0.548
AOI83455.1
Cyclopropane-fatty-acyl-phospholipid synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.540
Your Current Organism:
Burkholderia cepacia
NCBI taxonomy Id: 292
Other names: ATCC 25416, B. cepacia, Burkholderia cepacia genomovar I, Burkholderia sp. Bp7081, Burkholderia sp. Bp7091, Burkholderia sp. Bp7098, Burkholderia sp. Bp7108, Burkholderia sp. Bp7432, Burkholderia sp. LK29, Burkholderia sp. NCIM 5465, CCUG 12691, CCUG 13226, CFBP 2227, CIP 80.24, DSM 7288, ICMP 5796, IFO 14074, JCM 5964, NBRC 14074, NCCB 76047, NCPPB 2993, NCTC 10743, NRRL B-14810, Pseudomonas cepacia, Pseudomonas kingii, Pseudomonas multivorans, strain 717-ICPB 25, strain Ballard 717
Server load: low (20%) [HD]