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
Cphy_0521acetyl-CoA carboxylase, biotin carboxylase; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. (448 aa)    
Predicted Functional Partners:
accD
acetyl-CoA carboxylase, carboxyl transferase, beta subunit; Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA; Belongs to the AccD/PCCB family.
 0.999
accA
acetyl-CoA carboxylase, carboxyl transferase, alpha subunit; Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
 
 0.999
Cphy_0519
acetyl-CoA carboxylase, biotin carboxyl carrier protein; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
 
 0.997
Cphy_2437
Propionyl-CoA carboxylase; PFAM: carboxyl transferase; KEGG: cth:Cthe_0699 carboxyl transferase.
  
 0.996
fabZ
Beta-hydroxyacyl-(acyl-carrier-protein) dehydratase FabZ; Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
 
  
 0.992
Cphy_0516
TIGRFAM: malonyl CoA-acyl carrier protein transacylase; PFAM: Acyl transferase; KEGG: cth:Cthe_0935 malonyl CoA-acyl carrier protein transacylase.
 
 
 0.991
birA
biotin--acetyl-CoA-carboxylase ligase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a repressor; Belongs to the biotin--protein ligase family.
  
 0.970
Cphy_3558
PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; pyruvate ferredoxin/flavodoxin oxidoreductase; pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; KEGG: cno:NT01CX_1854 pyruvate:ferredoxin (flavodoxin) oxidoreductase.
  
 0.970
Cphy_0603
PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; pyruvate ferredoxin/flavodoxin oxidoreductase; pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; KEGG: cdf:CD2682 pyruvate-flavodoxin oxidoreductase.
  
 0.960
Cphy_3171
2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate). Belongs to the alpha-IPM synthase/homocitrate synthase family.
  
 
 0.954
Your Current Organism:
Lachnoclostridium phytofermentans
NCBI taxonomy Id: 357809
Other names: Clostridium phytofermentans ISDg, L. phytofermentans ISDg, Lachnoclostridium phytofermentans ISDg
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.