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:
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Gene Fusion
Cooccurrence
Coexpression
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[Homology]
Score
accAacetyl-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. (323 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
ADN58961.1
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.
 
 0.996
ADN58962.1
acetyl-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.
 
 0.994
ADN58472.1
KEGG: bxe:Bxe_A1073 [acyl-carrier-protein] S-malonyltransferase; TIGRFAM: malonyl CoA-acyl carrier protein transacylase; PFAM: Acyl transferase.
 
 
 0.985
fabH
3-oxoacyl-(acyl-carrier-protein) synthase III; 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.
 
 
 0.984
ADN61330.1
PFAM: Carbamoyl-phosphate synthase L chain ATP-binding; Carbamoyl-phosphate synthetase large chain domain protein; biotin carboxylase domain protein; biotin/lipoyl attachment domain-containing protein; KEGG: bxe:Bxe_B0963 3-methylcrotonoyl-CoA carboxylase, alpha subunit.
 
 
 0.959
ADN61567.1
TIGRFAM: malonate decarboxylase, beta subunit; KEGG: bpy:Bphyt_4818 malonate decarboxylase subunit beta.
  
 
 0.941
ADN61566.1
KEGG: bpy:Bphyt_4817 malonate decarboxylase, gamma subunit; TIGRFAM: malonate decarboxylase, gamma subunit; PFAM: malonate decarboxylase gamma subunit.
  
 
 0.935
ADN57350.1
KEGG: bac:BamMC406_4289 phosphate butyryltransferase; PFAM: phosphate acetyl/butaryl transferase.
    
 0.914
ADN59344.1
PFAM: Beta-hydroxyacyl-(acyl-carrier-protein) dehydratase FabA/FabZ; KEGG: gdi:GDI_3006 putative (3R)-hydroxymyristoyl-[acyl carrier protein] dehydratase.
 
  
 0.913
Your Current Organism:
Burkholderia sp. CCGE1003
NCBI taxonomy Id: 640512
Other names: B. sp. CCGE1003
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.