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
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[Homology]
Score
thrCThrC protein; Threonine synthase is involved in threonine biosynthesis. It catalyses the conversion of O-phospho-L-homoserine and water into L-threonine and orthophosphate,using pyridoxal phosphate as a cofactor. The pyridoxal-phosphate binding site is a Lys (K) residue. The enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. Similar to trembl|Q8XZR7 (68%), to sprot|THRC_METGL (69%) and to sprot|THRC_PSEAE (42%). TIGRFAM: thrC, threonine synthase Pfam (PF00291): Pyridoxal-phosphate dependent enzyme; High confidence in f [...] (487 aa)    
Predicted Functional Partners:
hom
Homoserine dehydrogenase catalyzes NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. Similar to TREMBL:Q9RAM9 (77%) and to pir|DEPSHA(PIR (Georgetown University) (56%). Pfam: Homoserine dehydrogenase; High confidence in function and specificity.
 
 0.984
ilvA
Probable 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.
  
 
 0.983
thrB
Probable homoserine kinase. Homology to thrB of M. flagellum of 51% (sprot|KHSE_METFL). CATALYTIC ACTIVITY: ATP + L-homoserine = ADP + O-phospho-L-homoserine. Pfam: Aminoglycoside phosphotransferase no signal peptide no TMHs; High confidence in function and specificity; Belongs to the pseudomonas-type ThrB family.
    
 0.954
serC
Phosphoserine transaminase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine.; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.
   
 0.939
pdxA
4-hydroxythreonine-4-phosphate dehydrogenase; Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L- threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
    
  0.928
thrH
Probable homoserine kinase; ThrH encodes a protein with an in vivo homoserine-kinase-like activity in P. aeruginosa. Homoserine kinase,the product of the thrB gene, catalyzes an obligatory step of threonine biosynthesis. Similar trembl|Q9I2Y2 (62%). Pfam (PF00702): haloacid dehalogenase-like hydrolase; Function unclear.
    
 0.910
lysC
Aspartate kinase (AK) catalyzes the phosphorylation of aspartate. The product of this reaction can then be used in the biosynthesis of lysine or in the pathway leading to homoserine, which participates in the biosynthesis of threonine, isoleucine and methionine. Similar to trembl|Q8RU02 (80%) and to pir|C83531 (74%). Pfam (PF00696): Amino acid kinase family Pfam (PF01842): two ACT domain; High confidence in function and specificity; Belongs to the aspartokinase family.
  
 
 0.904
leuD
LeuD protein; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily.
 
  
 0.896
ilvC
IlvC protein; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
  
  
 0.797
gltB
Ferredoxin-dependent glutamate synthase,; Specificity unclear.
  
  
 0.758
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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