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.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
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dapBDihydrodipicolinate reductase; Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. (269 aa)    
Predicted Functional Partners:
dapA
Dihydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
 
 
 0.988
dapD
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; Identified by similarity to SP:P03948; match to protein family HMM PF00132; match to protein family HMM TIGR00965; Belongs to the transferase hexapeptide repeat family.
 
 
 0.968
dnaJ
dnaJ protein; 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, DnaK and Gr [...]
  
  
 0.946
carA
Carbamoyl-phosphate synthase, small subunit; Identified by match to protein family HMM PF00117; match to protein family HMM PF00988; match to protein family HMM TIGR01368; Belongs to the CarA family.
 
  
 0.912
lysA
Diaminopimelate decarboxylase; Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine.
 
   
 0.855
carB
Carbamoyl-phosphate synthase, large subunit; Identified by match to protein family HMM PF00289; match to protein family HMM PF02142; match to protein family HMM PF02786; match to protein family HMM PF02787; match to protein family HMM TIGR01369; Belongs to the CarB family.
    
 0.854
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.
 
   
 0.789
MCA0390
Aspartate kinase, monofunctional class; Identified by similarity to SP:P26512; match to protein family HMM PF00696; match to protein family HMM PF01842; match to protein family HMM TIGR00656; match to protein family HMM TIGR00657; Belongs to the aspartokinase family.
 
  
 0.782
birA
birA bifunctional protein; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon.
  
  
 0.686
cca
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. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases.
  
    0.676
Your Current Organism:
Methylococcus capsulatus
NCBI taxonomy Id: 243233
Other names: M. capsulatus str. Bath, Methylococcus capsulatus ATCC 33009, Methylococcus capsulatus Bath, Methylococcus capsulatus MC, Methylococcus capsulatus NCIB 11132, Methylococcus capsulatus str. Bath
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