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
AFY32006.1L-threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. (364 aa)    
Predicted Functional Partners:
thrB
Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily.
 
 
 0.985
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.
  
 
0.946
AFY31260.1
L-threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde.
   
 0.923
AFY31263.1
L-threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase; COGs: COG0498 Threonine synthase; InterPro IPR001926:IPR004450; KEGG: ava:Ava_4952 threonine synthase; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit; PRIAM: Threonine synthase; SPTR: L-threonine synthase; TIGRFAM: Threonine synthase.
  
  
 
0.918
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).
    
  0.902
AFY33279.1
PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain; COGs: COG0460 Homoserine dehydrogenase; InterPro IPR005106:IPR001342:IPR002912; KEGG: npu:Npun_R2750 homoserine dehydrogenase; PFAM: Homoserine dehydrogenase, catalytic; Aspartate/homoserine dehydrogenase, NAD-binding; Amino acid-binding ACT; SPTR: Homoserine dehydrogenase.
 
 
 0.870
AFY35501.1
Aspartate kinase; PFAM: ACT domain; Amino acid kinase family; TIGRFAM: aspartate kinase, monofunctional class; aspartate kinase; COGs: COG0527 Aspartokinase; InterPro IPR001048:IPR002912:IPR005260:IPR001341; KEGG: npu:Npun_R4597 aspartate kinase; PFAM: Aspartate/glutamate/uridylate kinase; Amino acid-binding ACT; SPTR: Aspartokinase; TIGRFAM: Aspartate kinase domain; Aspartate kinase, monofunctional class.
  
 
 0.794
AFY33738.1
3-isopropylmalate dehydratase, small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily.
  
  
 0.779
AFY31201.1
Threo-3-hydroxyaspartate ammonia-lyase; PFAM: Pyridoxal-phosphate dependent enzyme; COGs: COG1171 Threonine dehydratase; InterPro IPR001926; KEGG: npu:Npun_R1256 serine/threonine dehydratase; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit; PRIAM: Threo-3-hydroxyaspartate ammonia-lyase; SPTR: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit.
  
 
0.733
AFY33339.1
PFAM: Conserved region in glutamate synthase; GXGXG motif; Glutamate synthase central domain; Glutamine amidotransferases class-II; COGs: COG0069 Glutamate synthase domain 2; InterPro IPR000583:IPR006982:IPR002932:IPR002489; KEGG: npu:Npun_R3877 ferredoxin-dependent glutamate synthase GltB; PFAM: Glutamate synthase, central-C; Glutamine amidotransferase, class-II; Glutamate synthase, central-N; Glutamate synthase, alpha subunit, C-terminal; PRIAM: Glutamate synthase (ferredoxin); SPTR: Ferredoxin-dependent glutamate synthase GltB.
  
  
 0.665
Your Current Organism:
Calothrix sp. PCC7507
NCBI taxonomy Id: 99598
Other names: C. sp. PCC 7507, Calothrix sp. PCC 7507
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