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
Pnap_2378KEGG: pol:Bpro_2168 lactoylglutathione lyase. (162 aa)    
Predicted Functional Partners:
Pnap_1622
PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, catalytic region; D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding; KEGG: pol:Bpro_3078 D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding.
   
 0.908
Pnap_0476
PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding; KEGG: pol:Bpro_4156 D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding.
     
 0.901
gloB
Hydroxyacylglutathione hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid.
     
 0.900
Pnap_2984
Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
     
  0.900
Pnap_2379
TIGRFAM: acetyl-CoA carboxylase, biotin carboxylase; PFAM: biotin/lipoyl attachment domain-containing protein; Carbamoyl-phosphate synthase L chain, ATP-binding; Carbamoyl-phosphate synthetase large chain domain protein; biotin carboxylase domain protein; KEGG: pol:Bpro_2167 carbamoyl-phosphate synthase L chain, ATP-binding.
  
  
 0.847
trpB
Tryptophan synthase, beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
   
  0.816
Pnap_0111
L-threonine ammonia-lyase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
   
 0.810
ilvA
L-threonine ammonia-lyase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
   
 0.810
Pnap_3336
L-threonine ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: pol:Bpro_0952 pyridoxal-5'-phosphate-dependent enzyme, beta subunit.
   
 0.810
Pnap_1588
PFAM: amine oxidase; FAD dependent oxidoreductase; KEGG: mca:MCA2837 amine oxidase family, flavin-containing protein.
     
 0.801
Your Current Organism:
Polaromonas naphthalenivorans
NCBI taxonomy Id: 365044
Other names: P. naphthalenivorans CJ2, Polaromonas naphthalenivorans CJ2, Polaromonas naphthalenivorans str. CJ2, Polaromonas naphthalenivorans strain CJ2
Server load: low (28%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.