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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
dapB4-hydroxy-tetrahydrodipicolinate reductase; Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate; Belongs to the DapB family. (267 aa)    
Predicted Functional Partners:
dapA
4-hydroxy-tetrahydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
 
 
 0.991
OHU94406.1
4-hydroxy-tetrahydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). Belongs to the DapA family.
 
 
 0.987
OHU96374.1
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the transferase hexapeptide repeat family.
 
 
 0.981
dapD
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the transferase hexapeptide repeat family.
 
 
 0.980
dnaJ
Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...]
 
  
 0.887
OHU96664.1
Dihydrodipicolinate synthase family protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the DapA family.
 
 
 0.862
pcnB
poly(A) polymerase; Adds poly(A) tail to the 3' end of many RNAs, which usually targets these RNAs for decay. Plays a significant role in the global control of gene expression, through influencing the rate of transcript degradation, and in the general RNA quality control. Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family.
 
    0.840
mgsA
Methylglyoxal synthase; Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.
  
    0.832
OHU95558.1
tRNA nucleotidyltransferase; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.
  
    0.814
OHU95616.1
Aspartate kinase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the aspartokinase family.
 
 
 0.810
Your Current Organism:
Pseudoalteromonas byunsanensis
NCBI taxonomy Id: 327939
Other names: JCM 12483, KCTC 12274, P. byunsanensis, Pseudoalteromonas byunsanensis Park et al. 2005, strain FR1199
Server load: low (32%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.