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
trpBTryptophan synthase subunit beta; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. (397 aa)    
Predicted Functional Partners:
trpC
Indole-3-glycerol-phosphate synthase; Involved in tryptophan biosynthesis; amino acid biosynthesis; converts 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate to C(1)-(3-indolyl)-glycerol 3-phosphate and carbon dioxide and water; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TrpC family.
 
 0.999
trpA
Tryptophan synthase subunit alpha; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family.
 0.999
trpF
N-(5'-phosphoribosyl)anthranilate isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TrpF family.
  
 0.998
trpD
Anthranilate phosphoribosyltransferase; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA).
  
 0.980
ilvA
PLP-dependent threonine dehydratase; 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.
  
 0.942
APC00295.1
Anthranilate synthase component 2; TrpG; with TrpE catalyzes the formation of anthranilate and glutamate from chorismate and glutamine; TrpG provides the glutamine amidotransferase activity; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.928
glyA
Serine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
     
 0.928
APC00937.1
Anthranilate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.925
APC01100.1
Phosphoserine phosphatase SerB; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.913
trpE
Anthranilate synthase; Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia.
 
  
 0.906
Your Current Organism:
Polynucleobacter asymbioticus
NCBI taxonomy Id: 576611
Other names: Burkholderiaceae bacterium KF022, Burkholderiaceae bacterium KF023, Burkholderiaceae bacterium KF032, Burkholderiaceae bacterium KF040, Burkholderiaceae bacterium KF041, Burkholderiaceae bacterium KF042, Burkholderiaceae bacterium KF043, Burkholderiaceae bacterium KF046, Burkholderiaceae bacterium KF047, Burkholderiaceae bacterium KF069, Burkholderiaceae bacterium KF071, Burkholderiaceae bacterium KF072, CIP 109841, DSM 18221, P. asymbioticus, Polynucleobacter asymbioticus (Hahn et al. 2009) Hahn et al. 2016, Polynucleobacter necessarius subsp. asymbioticus, Polynucleobacter necessarius subsp. asymbioticus Hahn et al. 2009, Polynucleobacter sp. INAWF005, Polynucleobacter sp. INAWF006, Polynucleobacter sp. INAWF008, Polynucleobacter sp. INAWF009, Polynucleobacter sp. INAWF010, Polynucleobacter sp. INAWF011, Polynucleobacter sp. INAWF012, Polynucleobacter sp. INBF001, Polynucleobacter sp. MWH-Creno-4A3, Polynucleobacter sp. MWH-Creno-4D65, Polynucleobacter sp. MWH-Mekk-C4, Polynucleobacter sp. MWH-Mekk-D4, Polynucleobacter sp. MWH-NZ4W7a, Polynucleobacter sp. MWH-P1sevC1, Polynucleobacter sp. P1-KOL8, Polynucleobacter sp. QLW-P1DMWA-2, Polynucleobacter sp. QLW-P1DNSYA-1, Polynucleobacter sp. QLW-P1DNSYA-2, Polynucleobacter sp. QLW-P1FAT50D-2, Polynucleobacter sp. QLW-P1FMW50A-1, Polynucleobacter sp. QLW-P1FNSY20A-6, Polynucleobacter sp. SHIRF001, Polynucleobacter sp. SHIRF002, Polynucleobacter sp. SHIRF003, Polynucleobacter sp. SHIRF004, Polynucleobacter sp. SHIRF005, Polynucleobacter sp. SHIRF006, Polynucleobacter sp. SHIRF007, Polynucleobacter sp. SHIRF008, Polynucleobacter sp. SHIRF009, Polynucleobacter sp. SHIRF010, Polynucleobacter sp. SHIRF011, Polynucleobacter sp. SHIRF012, Polynucleobacter sp. SHIRF013, Polynucleobacter sp. SHIRF014, Polynucleobacter sp. SHIRF015, Polynucleobacter sp. SHIRF016, Polynucleobacter sp. SHIRF017, Polynucleobacter sp. SHIRF018, Polynucleobacter sp. SHIRF019, Polynucleobacter sp. SUWAF015, Polynucleobacter sp. SUWAF016, Polynucleobacter sp. TEGAF008, Polynucleobacter sp. TEGF001, Polynucleobacter sp. UF003, Polynucleobacter sp. UF009, Polynucleobacter sp. USHIF002, Polynucleobacter sp. USHIF003, Polynucleobacter sp. USHIF004, Polynucleobacter sp. USHIF007, Polynucleobacter sp. USHIF009, Polynucleobacter sp. USHIF010, Polynucleobacter sp. USHIF011, Polynucleobacter sp. USHIF012, beta proteobacterium MWH-HuK1, beta proteobacterium MWH-T1W11, strain QLW-P1DMWA-1
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