STRINGSTRING
R2601_17913 protein (Pelagibaca bermudensis) - STRING interaction network
"R2601_17913" - Aspartokinase in Pelagibaca bermudensis
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
R2601_17913Aspartokinase (412 aa)    
Predicted Functional Partners:
R2601_17719
Homoserine dehydrogenase (428 aa)
  0.999
asd
Aspartate-beta-semialdehyde dehydrogenase ; Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L- aspartyl-4-phosphate (340 aa)
 
 
  0.998
R2601_16690
Aminotransferase, classes I and II (393 aa)
 
  0.990
R2601_18950
Aspartate aminotransferase (400 aa)
   
  0.984
lysA
Diaminopimelate decarboxylase ; Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine (421 aa)
  0.967
R2601_25666
Transcriptional regulator, GntR family protein (474 aa)
     
 
  0.941
R2601_27141
Dihydropteroate synthase, DHPS-Homocysteine S-methyltransferase-Cobalamin-dependent methionine (1256 aa)
   
 
  0.938
dapA
4-hydroxy-tetrahydrodipicolinate synthase ; Catalyzes the condensation of (S)-aspartate-beta- semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy- tetrahydrodipicolinate (HTPA) (286 aa)
 
 
  0.935
R2601_08998
Threonine synthase (463 aa)
   
 
  0.929
secY
Protein translocase subunit SecY ; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently (447 aa)
     
 
  0.929
Your Current Organism:
Pelagibaca bermudensis
NCBI taxonomy Id: 314265
Other names: P. bermudensis HTCC2601, Pelagibaca, Pelagibaca Cho and Giovannoni 2006, Pelagibaca bermudensis, Pelagibaca bermudensis Cho and Giovannoni 2006, Pelagibaca bermudensis HTCC2601, Pelagibaca bermudensis str. HTCC2601, Pelagibaca bermudensis strain HTCC2601, Roseovarius sp. HTCC2601
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