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
Lbys_3077Catalytic domain-containing protein of components of various dehydrogenase complexes; COGs: COG0508 Pyruvate/2-oxoglutarate dehydrogenase complex dihydrolipoamide acyltransferase (E2) protein; InterPro IPR001078; KEGG: mxa:MXAN_3454 2-oxo acid dehydrogenase acyltransferase catalytic subunit; PFAM: catalytic domain-containing protein of components of various dehydrogenase complexes; SPTR: 2-oxo acid dehydrogenase acyltransferase catalytic domain protein; PFAM: 2-oxoacid dehydrogenases acyltransferase (catalytic domain). (275 aa)    
Predicted Functional Partners:
Lbys_3002
Transketolase domain-containing protein; COGs: COG0022 Pyruvate/2-oxoglutarate dehydrogenase complex dehydrogenase (E1) component eukaryotic type beta subunit; InterPro IPR001017:IPR005475:IPR005476; KEGG: dfe:Dfer_3632 transketolase domain protein; PFAM: Transketolase domain-containing protein; Transketolase central region; dehydrogenase E1 component; SPTR: Transketolase domain protein; PFAM: Dehydrogenase E1 component; Transketolase, C-terminal domain; Transketolase, pyrimidine binding domain.
  
 0.999
Lbys_1402
Transketolase central region; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
 
 0.996
Lbys_2718
COGs: COG1249 Pyruvate/2-oxoglutarate dehydrogenase complex dihydrolipoamide dehydrogenase (E3); InterProIPR012999:IPR013027:IPR000815:IPR004099:IPR 006258; KEGG: sli:Slin_5752 dihydrolipoamide dehydrogenase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; pyridine nucleotide-disulphide oxidoreductase dimerisation region; SPTR: Dihydrolipoyl dehydrogenase; TIGRFAM: dihydrolipoamide dehydrogenase; PFAM: Pyridine nucleotide-disulphide oxidoreductase; Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain; TIGRFAM: dihydrolipoamide dehydrogenase.
  
 0.993
Lbys_3490
COGs: COG1249 Pyruvate/2-oxoglutarate dehydrogenase complex dihydrolipoamide dehydrogenase (E3); InterProIPR012999:IPR013027:IPR000815:IPR004099:IPR 006258; KEGG: sli:Slin_6035 dihydrolipoamide dehydrogenase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; pyridine nucleotide-disulphide oxidoreductase dimerisation region; SPTR: Dihydrolipoyl dehydrogenase; TIGRFAM: dihydrolipoamide dehydrogenase; PFAM: Pyridine nucleotide-disulphide oxidoreductase; Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain; TIGRFAM: dihydrolipoamide dehydrogenase.
  
 0.993
pdhA
Pyruvate dehydrogenase (acetyl-transferring) E1 component, alpha subunit; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
 
 0.992
Lbys_3488
COGs: COG0567 2-oxoglutarate dehydrogenase complex dehydrogenase (E1); InterPro IPR001017:IPR005475:IPR011603; KEGG: dfe:Dfer_5752 2-oxoglutarate dehydrogenase E1 component; PFAM: Transketolase central region; dehydrogenase E1 component; PRIAM: Oxoglutarate dehydrogenase (succinyl-transferring); SPTR: 2-oxoglutarate dehydrogenase, E1 subunit; TIGRFAM: 2-oxoglutarate dehydrogenase, E1 subunit; PFAM: Dehydrogenase E1 component; Transketolase, pyrimidine binding domain; TIGRFAM: 2-oxoglutarate dehydrogenase, E1 component.
  
 0.982
sucC
succinyl-CoA synthetase, beta subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
  
 0.962
Lbys_3325
COGs: COG0372 Citrate synthase; InterPro IPR019810:IPR002020:IPR010953; KEGG: dfe:Dfer_0554 citrate synthase I; PFAM: Citrate synthase; PRIAM: Citrate (Si)-synthase; SPTR: Citrate synthase; TIGRFAM: citrate synthase I; PFAM: Citrate synthase; TIGRFAM: citrate (Si)-synthase, eukaryotic; citrate synthase I (hexameric type); Belongs to the citrate synthase family.
  
 0.962
sucD
succinyl-CoA synthetase, alpha subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
  
 0.957
Lbys_1333
Catalytic domain-containing protein of components of various dehydrogenase complexes; COGs: COG0508 Pyruvate/2-oxoglutarate dehydrogenase complex dihydrolipoamide acyltransferase (E2) protein; InterPro IPR000089:IPR004167:IPR001078:IPR003016; KEGG: chu:CHU_1755 dihydrolipoyllysine-residue acetyltransferase (dihydrolipoamide S-acetyltransferase); PFAM: catalytic domain-containing protein of components of various dehydrogenase complexes; biotin/lipoyl attachment domain-containing protein; E3 binding domain protein; SPTR: Dihydrolipoyllysine-residue acetyltransferase component of pyruvate [...]
  
  
  0.928
Your Current Organism:
Leadbetterella byssophila
NCBI taxonomy Id: 649349
Other names: L. byssophila DSM 17132, Leadbetterella byssophila 4M15, Leadbetterella byssophila DSM 17132, Leadbetterella byssophila str. DSM 17132, Leadbetterella byssophila strain DSM 17132
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