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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
EHA63996.1PFAM: Alcohol dehydrogenase GroES-like; Alcohol dehydrogenase, C-terminal; KEGG: bid:Bind_1144 alcohol dehydrogenase; SMART: Polyketide synthase, enoylreductase. (333 aa)    
Predicted Functional Partners:
EHA63496.1
KEGG: tmz:Tmz1t_0608 S-(hydroxymethyl)glutathione dehydrogenase/class III alcohol dehydrogenase; TIGRFAM: Alcohol dehydrogenase class III/S-(hydroxymethyl)glutathione dehydrogenase; PFAM: Alcohol dehydrogenase GroES-like; Alcohol dehydrogenase, C-terminal.
    
 0.940
EHA60241.1
PFAM: Aldehyde dehydrogenase domain; KEGG: pmt:PMT0191 putative aldehyde dehydrogenase; Belongs to the aldehyde dehydrogenase family.
  
 0.912
EHA62965.1
KEGG: syn:slr0942 aldehyde reductase; PFAM: NADP-dependent oxidoreductase domain.
  
 
 0.869
EHA60238.1
KEGG: mrb:Mrub_0437 glycerol kinase; PFAM: Carbohydrate kinase, FGGY, N-terminal; Carbohydrate kinase, FGGY, C-terminal; Belongs to the FGGY kinase family.
    
 0.844
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.
  
 
 0.725
EHA63558.1
Pyruvate decarboxylase; KEGG: bid:Bind_1794 thiamine pyrophosphate binding domain-containing protein; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, C-terminal TPP-binding.
   
 
 0.714
EHA63997.1
Hypothetical protein.
       0.714
EHA64196.1
TIGRFAM: Acetolactate synthase, large subunit, biosynthetic; KEGG: pmf:P9303_07681 acetolactate synthase 3 catalytic subunit; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, C-terminal TPP-binding.
    
 0.704
acsA
Acetyl-coenzyme A synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA; Belongs to the ATP-dependent AMP-binding enzyme family.
     
 0.690
EHA60424.1
KEGG: pmf:P9303_04591 putative 8-amino-7-oxononanoate synthase; PFAM: Aminotransferase, class I/classII.
     
  0.652
Your Current Organism:
Synechococcus sp. WH 8016
NCBI taxonomy Id: 166318
Other names: S. sp. WH 8016, Synechococcus sp. WH8016
Server load: low (16%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.