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
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[Homology]
Score
BF93_12745Acetyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. (184 aa)    
Predicted Functional Partners:
BF93_12750
GCN5 family acetyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.773
BF93_12735
Phage-associated protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.478
BF93_12740
Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
       0.478
BF93_14895
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.435
BF93_09385
2-dehydro-3-deoxyphosphogluconate aldolase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
  0.407
pfp
Pyrophosphate--fructose-6-phosphate 1-phosphotransferase; Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
     
  0.405
Your Current Organism:
Brachybacterium phenoliresistens
NCBI taxonomy Id: 396014
Other names: B. phenoliresistens, BCRC 17589, Brachybacterium phenoliresistens Chou et al. 2007, Brachybacterium sp. phenol-A, JCM 15157, LMG 23707, LMG:23707, strain phenol-A
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