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
KFX06768.1Pyridoxal phosphate phosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology. (273 aa)    
Predicted Functional Partners:
ribD
5-amino-6-(5-phosphoribosylamino)uracil reductase; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- phosphate; In the C-terminal section; belongs to the HTP reductase family.
    
 0.850
KFX07347.1
PTS mannose transporter subunit IIAB; Catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane; subunit IIA transfers a phosphoryl group to subunit IIB; subunit IIB transfers the phosphoryl group to the substrate; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.805
KFX07826.1
Membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.754
ribH
6,7-dimethyl-8-ribityllumazine synthase; Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2- butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin; Belongs to the DMRL synthase family.
     
 0.723
KFX05940.1
Fumarate hydratase; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family.
    
  0.715
KFX07717.1
Riboflavin synthase subunit alpha; Catalyzes the formation of riboflavin from 6,7-dimethyl-8-(1-D-ribityl)lumazine; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.700
KFX07644.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.525
pgi
Glucose-6-phosphate isomerase; Functions in sugar metabolism in glycolysis and the Embden-Meyerhof pathways (EMP) and in gluconeogenesis; catalyzes reversible isomerization of glucose-6-phosphate to fructose-6-phosphate; member of PGI family; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the GPI family.
  
 
 0.510
KFX06792.1
Glucose-1-phosphate thymidylyltransferase; Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. Belongs to the glucose-1-phosphate thymidylyltransferase family.
  
 
 0.502
KFX07374.1
Hypothetical protein; Removes the phosphate from trehalose 6-phosphate to produce free trehalose.
 
  
  0.454
Your Current Organism:
Pectobacterium betavasculorum
NCBI taxonomy Id: 55207
Other names: ATCC 43762, CFBP 2122, CIP 105193, DSM 18076, Erwinia carotovora subsp. betavasculorum, ICMP 4226, LMG 2464, LMG 2466, LMG:2464, LMG:2466, NCPPB 2795, P. betavasculorum, Pectobacterium carotovorum subsp. betavasculorum, UCPB 193
Server load: low (34%) [HD]