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
dapDKEGG: sdn:Sden_1551 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; Belongs to the transferase hexapeptide repeat family. (274 aa)    
Predicted Functional Partners:
dapB
Dihydrodipicolinate reductase; Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
 
 
 0.977
argD
KEGG: sdn:Sden_1054 acetylornithine and succinylornithine aminotransferases; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.
    
 0.914
argD-2
KEGG: son:SO0617 acetylornithine aminotransferase; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.
    
 0.914
guaA
GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP.
   
  
 0.781
map
Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
  
  
 0.775
glnD
(Protein-PII) uridylyltransferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
     
 0.755
dapE
Succinyldiaminopimelate desuccinylase; Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls; Belongs to the peptidase M20A family. DapE subfamily.
 
  
 0.733
dapA
Dihydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
 
  
 0.675
dapF
Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan.
 
  
 0.656
Sama_3170
KEGG: son:SO4055 aspartokinase II/homoserine dehydrogenase, methionine-sensitive; In the C-terminal section; belongs to the homoserine dehydrogenase family.
 
  
 0.623
Your Current Organism:
Shewanella amazonensis
NCBI taxonomy Id: 326297
Other names: S. amazonensis SB2B, Shewanella amazonensis SB2B, Shewanella amazonensis str. SB2B, Shewanella amazonensis strain SB2B
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.