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
dapADihydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). (293 aa)    
Predicted Functional Partners:
dapB
Dihydrodipicolinate reductase; Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate; Belongs to the DapB family.
 
 
 0.996
AEJ60465.1
PFAM: Homoserine dehydrogenase, NAD binding domain; Homoserine dehydrogenase; ACT domain; COGs: COG0460 Homoserine dehydrogenase; InterPro IPR005106:IPR001342:IPR002912; KEGG: sta:STHERM_c01940 homoserine dehydrogenase; PFAM: Homoserine dehydrogenase, catalytic; Aspartate/homoserine dehydrogenase, NAD-binding; Amino acid-binding ACT; SPTR: Homoserine dehydrogenase.
 
  
 0.945
asd
Aspartate-semialdehyde dehydrogenase; Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate; Belongs to the aspartate-semialdehyde dehydrogenase family.
  
 
 0.941
lysA
Orn/DAP/Arg decarboxylase 2; Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine.
  
 0.869
AEJ61568.1
PFAM: Phosphate acetyl/butaryl transferase; TIGRFAM: phosphate acetyltransferase; COGs: COG0280 Phosphotransacetylase; InterPro IPR002505:IPR004614; KEGG: sta:STHERM_c08690 phosphate acetyltransferase; PFAM: Phosphate acetyl/butaryl transferase; SPTR: Phosphotransacetylase; TIGRFAM: Phosphate acetyltransferase.
     
 0.817
gatC
glutamyl-tRNA(Gln) amidotransferase, C subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family.
  
  
 0.744
rpsO
Ribosomal protein S15; Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
  
    0.671
cmk-2
PFAM: Cytidylate kinase; TIGRFAM: cytidylate kinase, putative; COGs: COG1102 Cytidylate kinase; HAMAP: Cytidylate kinase; InterPro IPR000623:IPR011892; KEGG: sta:STHERM_c12230 cytidylate kinase; PFAM: Shikimate kinase; SPTR: Cytidylate kinase; TIGRFAM: Cytidylate kinase, putative.
   
    0.645
rplV
Ribosomal protein L22; The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
  
    0.643
rpsD
Ribosomal protein S4; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
   
    0.580
Your Current Organism:
Spirochaeta thermophila
NCBI taxonomy Id: 869211
Other names: S. thermophila DSM 6578, Spirochaeta thermophila DSM 6578, Spirochaeta thermophila str. DSM 6578, Spirochaeta thermophila strain DSM 6578
Server load: low (10%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.