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
EIJ38977.1Aspartate kinase; PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; Amino acid kinase family; alpha/beta hydrolase fold; TIGRFAM: homoserine O-acetyltransferase; aspartate kinase. (1131 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.
 
 0.999
EIJ37329.1
Aspartate kinase; PFAM: Homoserine dehydrogenase, NAD binding domain; Homoserine dehydrogenase; ACT domain; Amino acid kinase family; TIGRFAM: aspartate kinase.
 
0.998
asd
Aspartate-semialdehyde dehydrogenase; Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate; Belongs to the aspartate-semialdehyde dehydrogenase family.
 
 0.998
EIJ38976.1
OAH/OAS sulfhydrylase; PFAM: Cys/Met metabolism PLP-dependent enzyme; TIGRFAM: OAH/OAS sulfhydrylase.
 
 
 0.998
EIJ37327.1
Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase.
 
 0.995
ilvA
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.
  
 0.984
EIJ38984.1
Cobalamin-dependent methionine synthase I; PFAM: Homocysteine S-methyltransferase; TIGRFAM: 5-methyltetrahydrofolate--homocysteine methyltransferase.
  
 
 0.979
EIJ40470.1
PFAM: Small subunit of acetolactate synthase; ACT domain; TIGRFAM: acetolactate synthase, small subunit.
  
 
 0.977
metZ
Cystathionine beta-lyase/cystathionine gamma-synthase; Catalyzes the formation of L-homocysteine from O-succinyl-L- homoserine (OSHS) and hydrogen sulfide.
 
 
 0.976
EIJ38985.1
5-methyltetrahydrofolate--homocysteine methyltransferase; 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.
  
 
 0.975
Your Current Organism:
Joostella marina
NCBI taxonomy Id: 926559
Other names: J. marina DSM 19592, Joostella marina DSM 19592, Joostella marina En5
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