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
ackAAcetate kinase; Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction; Belongs to the acetokinase family. (356 aa)    
Predicted Functional Partners:
EHA64364.1
DRTGG domain protein; PFAM: DRTGG; KEGG: pmf:P9303_06871 phosphotransacetylase domain-containing protein.
  
 
 0.984
EHA63560.1
HAMAP: phosphoketolase; KEGG: cyh:Cyan8802_1694 putative phosphoketolase; PFAM: Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase, N-terminal; Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase; Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase, C-terminal.
 
 0.955
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.
     
 0.927
EHA63112.1
Acylphosphatase; KEGG: maq:Maqu_1183 acylphosphatase; HAMAP: Acylphosphatase; PFAM: Acylphosphatase-like.
     
 0.871
EHA60241.1
PFAM: Aldehyde dehydrogenase domain; KEGG: pmt:PMT0191 putative aldehyde dehydrogenase; Belongs to the aldehyde dehydrogenase family.
    
 0.869
fabH
3-oxoacyl-(acyl-carrier-protein) synthase 3; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids; Belongs to the thiolase-like superfamily. FabH family.
    
 0.724
EHA63447.1
TIGRFAM: Pyruvate kinase; KEGG: pmf:P9303_15431 pyruvate kinase; PFAM: Pyruvate kinase, barrel; Pyruvate kinase, C-terminal-like; PEP-utilising enzyme, mobile domain; Belongs to the pyruvate kinase family.
  
 
 0.719
plsX
Phosphate acyltransferase; Catalyzes the reversible formation of acyl-phosphate (acyl- PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
    
 0.717
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.
       0.642
EHA61798.1
TIGRFAM: 2-methylcitrate synthase/citrate synthase type I; KEGG: pmf:P9303_26921 citrate synthase; PFAM: Citrate synthase-like; Belongs to the citrate synthase family.
     
 0.607
Your Current Organism:
Synechococcus sp. WH 8016
NCBI taxonomy Id: 166318
Other names: S. sp. WH 8016, Synechococcus sp. WH8016
Server load: low (14%) [HD]