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
EHA62960.1PFAM: Hep/Hag; KEGG: bpr:GBP346_A2154 Hep_Hag family protein. (1045 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.
  
 
 0.953
EHA63056.1
PFAM: Homoserine dehydrogenase, catalytic; Aspartate/homoserine dehydrogenase, NAD-binding; Amino acid-binding ACT; KEGG: pmt:PMT1143 homoserine dehydrogenase.
  
 0.918
ilvA
Threonine dehydratase, biosynthetic; 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.
  
 
 0.871
EHA59172.1
KEGG: pmt:PMT0073 aspartate kinase; TIGRFAM: Aspartate kinase domain; Aspartate kinase, monofunctional class; PFAM: Aspartate/glutamate/uridylate kinase; Amino acid-binding ACT.
  
 0.806
EHA62253.1
KEGG: pmf:P9303_24681 3-isopropylmalate dehydratase small subunit; TIGRFAM: 3-isopropylmalate dehydratase, small subunit; PFAM: Aconitase A/isopropylmalate dehydratase small subunit, swivel; Belongs to the LeuD family.
  
  
 0.705
EHA59278.1
KEGG: pmt:PMT1777 ferredoxin-dependent glutamate synthase; PFAM: Glutamate synthase, central-C; Glutamine amidotransferase, class-II; Glutamate synthase, central-N; Glutamate synthase, alpha subunit, C-terminal.
  
  
 0.667
ilvC
Ketol-acid reductoisomerase; 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.
  
  
 0.646
EHA63214.1
PFAM: Aminoglycoside phosphotransferase; KEGG: pmt:PMT0868 hypothetical protein.
    
 0.604
hemL
Glutamate-1-semialdehyde 2,1-aminomutase; PFAM: Aminotransferase class-III; TIGRFAM: Tetrapyrrole biosynthesis, glutamate-1-semialdehyde aminotransferase; HAMAP: Tetrapyrrole biosynthesis, glutamate-1-semialdehyde aminotransferase; KEGG: pmf:P9303_06961 glutamate-1-semialdehyde aminotransferase.
     
 0.580
EHA63389.1
Methionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.
  
 
 0.575
Your Current Organism:
Synechococcus sp. WH 8016
NCBI taxonomy Id: 166318
Other names: S. sp. WH 8016, Synechococcus sp. WH8016
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