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dapD protein (Idiomarina loihiensis) - STRING interaction network
"dapD" - Tetrahydrodipicolinate N-succinyltransferase in Idiomarina loihiensis
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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Score
dapDTetrahydrodipicolinate N-succinyltransferase (274 aa)    
Predicted Functional Partners:
dapB
Dihydrodipicolinate reductase; Catalyzes the conversion of 4-hydroxy- tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate (268 aa)
 
 
  0.998
argD
Ornithine/acetylornithine aminotransferase (405 aa)
   
 
  0.987
dapE
N-succinyl-diaminopimelate deacylase; 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 (376 aa)
 
   
  0.914
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 (275 aa)
 
   
  0.909
glnD
UTP-GlnB (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 (879 aa)
         
  0.889
dapA
Dihydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta- semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy- tetrahydrodipicolinate (HTPA) (296 aa)
 
   
  0.844
map
Methionine aminopeptidase; 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 (262 aa)
   
        0.844
IL1791
Aspartate aminotransferase (395 aa)
 
 
  0.839
metL
Aspartokinase II (813 aa)
 
   
  0.765
lysC
Aspartate kinase (446 aa)
 
   
  0.760
Your Current Organism:
Idiomarina loihiensis
NCBI taxonomy Id: 283942
Other names: I. loihiensis, I. loihiensis L2TR, Idiomarina loihiensis, Idiomarina loihiensis Donachie et al. 2003, Idiomarina loihiensis L2TR, Idiomarina loihiensis str. L2TR, Idiomarina loihiensis strain L2TR
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