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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ADW16471.1Aconitase; COGs: COG1049 Aconitase B; InterPro IPR018136: IPR004406: IPR015929: IPR001030; KEGG: ddf:DEFDS_0917 aconitate hydratase; PFAM: Aconitase B; aconitate hydratase domain-containing protein; SPTR: Aconitate hydratase; PFAM: Aconitate B N-terminal domain; Aconitase family (aconitate hydratase); Aconitate hydratase 2 N-terminus; TIGRFAM: aconitate hydratase 2. (825 aa)    
Predicted Functional Partners:
ADW16750.1
COGs: COG0538 Isocitrate dehydrogenase; InterPro IPR004439: IPR001804: IPR019818; KEGG: hmo:HM1_1471 isocitrate dehydrogenase, nADP-dependent; PFAM: isocitrate/isopropylmalate dehydrogenase; SPTR: Isocitrate dehydrogenase [NADP]; TIGRFAM: isocitrate dehydrogenase, NADP-dependent; PFAM: Isocitrate/isopropylmalate dehydrogenase; TIGRFAM: isocitrate dehydrogenase, NADP-dependent, prokaryotic type.
  
 
 0.987
ADW16465.1
COGs: COG0372 Citrate synthase; InterPro IPR002020; KEGG: sfu:Sfum_2105 citrate (Si)-synthase; PFAM: Citrate synthase; PRIAM: Citrate (Si)-synthase; SPTR: Citrate synthase; PFAM: Citrate synthase; TIGRFAM: 2-methylcitrate synthase/citrate synthase II.
  
 
 0.982
ADW16919.1
COGs: COG0372 Citrate synthase; InterPro IPR002020: IPR010953: IPR019810; KEGG: dps:DP1088 citrate synthase; PFAM: Citrate synthase; SPTR: Citrate synthase; TIGRFAM: citrate synthase I; PFAM: Citrate synthase; TIGRFAM: citrate synthase I (hexameric type).
  
 
 0.982
ADW17658.1
COGs: COG0372 Citrate synthase; InterPro IPR011278: IPR002020: IPR019810; KEGG: bts:Btus_2368 2-methylcitrate synthase/citrate synthase II; PFAM: Citrate synthase; PRIAM: Citrate (Si)-synthase; SPTR: 2-methylcitrate synthase/citrate synthase II; TIGRFAM: 2-methylcitrate synthase/citrate synthase II; PFAM: Citrate synthase; TIGRFAM: 2-methylcitrate synthase/citrate synthase II.
  
 
 0.982
ADW19371.1
Aconitase; COGs: COG1048 Aconitase A; InterPro IPR001030: IPR000573: IPR006249: IPR018136; KEGG: sth:STH3164 aconitate hydratase; PFAM: aconitate hydratase domain-containing protein; SPTR: Aconitase; TIGRFAM: aconitate hydratase 1; PFAM: Aconitase C-terminal domain; Aconitase family (aconitate hydratase); TIGRFAM: aconitate hydratase 1.
    
 0.937
ADW18893.1
COGs: COG0039 Malate/lactate dehydrogenase; InterPro IPR001557: IPR010945: IPR001236; KEGG: dps:DP0661 malate dehydrogenase; PFAM: Lactate/malate dehydrogenase; SPTR: Malate dehydrogenase; TIGRFAM: malate dehydrogenase; PFAM: lactate/malate dehydrogenase, alpha/beta C-terminal domain; lactate/malate dehydrogenase, NAD binding domain; TIGRFAM: malate dehydrogenase.
  
  
 0.905
ADW16573.1
Fumarase; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family.
  
  
 0.896
sucC
succinyl-CoA synthetase (ADP-forming) 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.
  
  
 0.887
ADW19128.1
COGs: COG1249 Pyruvate/2-oxoglutarate dehydrogenase complex dihydrolipoamide dehydrogenase (E3); InterProIPR013027: IPR004099: IPR000815: IPR012999: IPR 006258; KEGG: alv:Alvin_0803 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.
  
  
 0.855
ADW17653.1
Dihydrolipoyllysine-residue acetyltransferase; COGs: COG0508 Pyruvate/2-oxoglutarate dehydrogenase complex dihydrolipoamide acyltransferase (E2) protein; InterPro IPR000089: IPR004167: IPR001078; KEGG: gur:Gura_1611 branched-chain alpha-keto acid dehydrogenase subunit E2; PFAM: catalytic domain-containing protein of components of various dehydrogenase complexes; E3 binding domain protein; biotin/lipoyl attachment domain-containing protein; PRIAM: Dihydrolipoyllysine-residue acetyltransferase; SPTR: Catalytic domain of components of various dehydrogenase complexes; PFAM: 2-oxoacid dehyd [...]
  
  
 0.641
Your Current Organism:
Desulfobulbus propionicus
NCBI taxonomy Id: 577650
Other names: D. propionicus DSM 2032, Desulfobulbus propionicus DSM 2032, Desulfobulbus propionicus str. DSM 2032, Desulfobulbus propionicus strain DSM 2032
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