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
trpCIndole-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. (266 aa)    
Predicted Functional Partners:
trpA
Tryptophan synthase subunit beta; 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
A2140_03240
Anthranilate phosphoribosyltransferase; Frameshifted; too many ambiguous residues; incomplete; missing start; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
trpE
Anthranilate synthase component I; 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 concentr [...]
 0.999
OGI38020.1
Aminodeoxychorismate synthase, component I; Derived by automated computational analysis using gene prediction method: Protein Homology.
 0.995
OGI41145.1
Chorismate mutase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.898
hisA
1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino]imidazole-4- carboxamide isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.830
moaC
Pyridine nucleotide-disulfide oxidoreductase; Catalyzes the conversion of (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP); Belongs to the MoaC family.
    
 0.812
A2140_07190
Hypothetical protein; Incomplete; too short partial abutting assembly gap; missing start and stop; Derived by automated computational analysis using gene prediction method: GeneMarkS+; Belongs to the cysteine synthase/cystathionine beta- synthase family.
    
 0.777
aroC
Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
  
 
 0.714
ilvA
Hypothetical protein; 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.
   
 0.691
Your Current Organism:
Muproteobacteria bacterium RBG166213
NCBI taxonomy Id: 1817756
Other names: C. Muproteobacteria bacterium RBG_16_62_13, Candidatus Muproteobacteria bacterium RBG_16_62_13
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