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
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[Homology]
Score
Smed_0953acetyl-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. (158 aa)    
Predicted Functional Partners:
Smed_0952
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.
 
 0.999
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.
 
 0.997
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.
 
 0.992
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.
 
 
 0.990
Smed_0744
TIGRFAM: malonyl CoA-acyl carrier protein transacylase; PFAM: Acyl transferase; KEGG: sme:SMc00571 acyl-carrier-protein S-malonyltransferase.
 
 
 0.973
Smed_1078
Pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
  
 
 0.910
Smed_3037
PFAM: alpha/beta hydrolase fold; biotin/lipoyl attachment domain-containing protein; E3 binding domain protein; KEGG: vei:Veis_2228 alpha/beta hydrolase fold.
  
 
 0.910
Smed_0324
TIGRFAM: methylmalonate-semialdehyde dehydrogenase; PFAM: aldehyde dehydrogenase; KEGG: sme:SMc00781 putative malonic semialdehyde oxidative decarboxylase protein.
    
  0.907
Smed_0145
TIGRFAM: acetyl-CoA acetyltransferase; PFAM: Thiolase; KEGG: sme:SMc02228 acetyl-CoA acetyltransferase; Belongs to the thiolase-like superfamily. Thiolase family.
    
 0.903
Smed_0499
TIGRFAM: acetyl-CoA acetyltransferase; PFAM: Thiolase; KEGG: sme:SMc00966 putative acetyl-CoA acyltransferase protein; Belongs to the thiolase-like superfamily. Thiolase family.
    
 0.903
Your Current Organism:
Sinorhizobium medicae
NCBI taxonomy Id: 366394
Other names: Ensifer medicae WSM419, S. medicae WSM419, Sinorhizobium medicae WSM419
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.