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
dapA_3Dihydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). (292 aa)    
Predicted Functional Partners:
dapB
Dihydrodipicolinate reductase; Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate; Belongs to the DapB family.
 
 
 0.988
metL
Aspartate kinase; Multifunctional homodimeric enzyme that catalyzes the phosphorylation of aspartate to form aspartyl-4-phosphate as well as conversion of aspartate semialdehyde to homoserine; functions in a number of amino acid biosynthetic pathways; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.962
thrA
Aspartate kinase; Multifunctional homotetrameric enzyme that catalyzes the phosphorylation of aspartate to form aspartyl-4-phosphate as well as conversion of aspartate semialdehyde to homoserine; functions in a number of amino acid biosynthetic pathways; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.960
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.
  
 
 0.943
AKL36295.1
Aspartate-semialdehyde dehydrogenase; Catalyzes the formation of 4-aspartyl phosphate from aspartate 4-semialdehyde; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the aspartate-semialdehyde dehydrogenase family.
  
 
 0.915
lysA
Diaminopimelate decarboxylase; Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine.
  
 0.892
nlpB
Lipoprotein; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
  
  
 0.852
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.
 
  
 0.840
bcp
Thiol peroxidase; Bacterioferritin comigratory protein; thiol peroxidase; thioredoxin-dependent; hydroperoxide peroxidase; in Escherichia coli this enzyme preferentially reduces linoleic acid hydroperoxide; contains an active site cysteine; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.776
AKL35218.1
Semialdehyde dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the aspartate-semialdehyde dehydrogenase family.
 
 
 0.764
Your Current Organism:
Klebsiella oxytoca
NCBI taxonomy Id: 571
Other names: ATCC 13182, Bacillus oxytocus perniciosus, CCUG 15717, CIP 103434, DSM 5175, IAM 14201, K. oxytoca, Klebsiella sp. CECRI-24/07, Klebsiella sp. MN9SED2, LMG 3055, LMG:3055, NBRC 102593, NBRC 105695, NCTC 13727, strain 479-2
Server load: low (8%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.