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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
trpBTryptophan synthase, beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. (406 aa)    
Predicted Functional Partners:
trpA
Tryptophan synthase, alpha chain; 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
trpC
PFAM: Indole-3-glycerol phosphate synthase; Belongs to the TrpC family.
 
 0.999
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).
  
 0.997
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 concent [...]
 
  
 0.992
ACU95125.1
Anthranilate synthase, component II; PFAM: Glutamine amidotransferase class-I; TIGRFAM: glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase.
  
 0.984
lgt
Prolipoprotein diacylglyceryl transferase; Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins; Belongs to the Lgt family.
  
    0.983
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.
  
 0.927
ACU98157.1
L-threonine ammonia-lyase; PFAM: ACT domain; Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine dehydratase, medium form.
  
 0.927
ACU97908.1
Phosphoserine phosphatase; PFAM: ACT domain; haloacid dehalogenase-like hydrolase; TIGRFAM: Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; phosphoserine phosphatase SerB.
  
 
 0.921
ACU98222.1
PFAM: chorismate binding enzyme; TIGRFAM: aminodeoxychorismate synthase, component I, bacterial clade.
 
  
 0.920
Your Current Organism:
Saccharomonospora viridis
NCBI taxonomy Id: 471857
Other names: S. viridis DSM 43017, Saccharomonospora viridis ATCC 15386, Saccharomonospora viridis DSM 43017, Saccharomonospora viridis NCIB 9602, Saccharomonospora viridis NRRL B-3044, Saccharomonospora viridis str. DSM 43017, Saccharomonospora viridis strain DSM 43017
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