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
EHA62512.1TIGRFAM: Serine O-acetyltransferase; KEGG: pmf:P9303_01521 serine acetyltransferase; PFAM: Bacterial transferase hexapeptide repeat. (245 aa)    
Predicted Functional Partners:
cysS
SMART: Cysteinyl-tRNA synthetase, class Ia, DALR; TIGRFAM: Cysteinyl-tRNA synthetase, class Ia; KEGG: pmf:P9303_08671 cysteinyl-tRNA synthetase; PFAM: Cysteinyl-tRNA synthetase, class Ia; Cysteinyl-tRNA synthetase, class Ia, DALR; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
 
 0.979
EHA60657.1
TIGRFAM: Cysteine synthase K/M; Cysteine synthase A; KEGG: pmt:PMT1978 O-acetylserine (thiol)-lyase A; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit; Belongs to the cysteine synthase/cystathionine beta- synthase family.
 
 0.977
EHA60201.1
TIGRFAM: Cysteine synthase A; Cysteine synthase K/M; KEGG: pmj:P9211_04051 O-acetylserine (thiol)-lyase A; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit; Belongs to the cysteine synthase/cystathionine beta- synthase family.
 
 0.973
EHA63218.1
TIGRFAM: O-acetylhomoserine/O-acetylserine sulfhydrylase; KEGG: pmf:P9303_13191 putative O-acetyl homoserine sulfhydrylase; PFAM: Cys/Met metabolism, pyridoxal phosphate-dependent enzyme.
    
 0.895
EHA60199.1
KEGG: pmt:PMT0226 putative cystathionine gamma-synthase; PFAM: Cys/Met metabolism, pyridoxal phosphate-dependent enzyme.
  
 
 0.890
glyA
Glycine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
     
 0.880
thrB
Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily.
     
 0.873
EHA63056.1
PFAM: Homoserine dehydrogenase, catalytic; Aspartate/homoserine dehydrogenase, NAD-binding; Amino acid-binding ACT; KEGG: pmt:PMT1143 homoserine dehydrogenase.
     
 0.866
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.
     
 0.865
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.
     
 0.864
Your Current Organism:
Synechococcus sp. WH 8016
NCBI taxonomy Id: 166318
Other names: S. sp. WH 8016, Synechococcus sp. WH8016
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