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
ADU47253.1Pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; COGs: COG0674 Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductase alpha subunit; InterPro IPR002880; KEGG: tfu:Tfu_2674 2-oxoglutarate ferredoxin oxidoreductase, alpha subunit; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; SPTR: Putative oxidoreductase; PFAM: domain; Pyruvate ferredoxin/flavodoxin oxidoreductase; TIGRFAM: 2-oxoacid:acceptor oxidoreductase, alpha subunit. (632 aa)    
Predicted Functional Partners:
ADU47252.1
2-oxoglutarate synthase; COGs: COG1013 Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductase beta subunit; InterPro IPR011766; KEGG: sen:SACE_3926 2-oxoglutarate ferredoxin oxidoreductase, beta subunit; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; PRIAM: 2-oxoglutarate synthase; SPTR: Ferrodoxin oxidoreductase beta subunit; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP binding domain.
 
 0.999
ADU49556.1
COGs: COG0674 Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductase alpha subunit; InterProIPR017896: IPR011895: IPR002880: IPR019752: IPR 019456: IPR011766: IPR017900; KEGG: mmi:MMAR_3408 pyruvate ferredoxin/flavodoxin oxidoreductase family protein; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; Pyruvate/ketoisovalerate oxidoreductase, catalytic domain; Pyruvate-flavodoxin oxidoreductase, EKR domain; thiamine pyrophosphate TPP-binding domain-containing protein; SPTR: Pyruvate ferredoxin/flavodoxin oxidoreductase family protein; TIGRFAM [...]
  
 0.999
ADU47249.1
Phosphotransacetylase; Involved in acetate metabolism. In the N-terminal section; belongs to the CobB/CobQ family.
    
 0.990
ADU47101.1
Isocitrate dehydrogenase, NADP-dependent; COGs: COG2838 Monomeric isocitrate dehydrogenase; InterPro IPR004436; KEGG: sgr:SGR_1224 putative isocitrate dehydrogenase; PFAM: Isocitrate dehydrogenase NADP-dependent monomeric type; PRIAM: Isocitrate dehydrogenase (NADP(+)); SPTR: Isocitrate dehydrogenase [NADP]; TIGRFAM: isocitrate dehydrogenase, NADP-dependent; PFAM: Monomeric isocitrate dehydrogenase; TIGRFAM: isocitrate dehydrogenase, NADP-dependent, monomeric type; Belongs to the monomeric-type IDH family.
  
 
 0.978
ldh
Malate dehydrogenase (NAD); Catalyzes the conversion of lactate to pyruvate. Belongs to the LDH/MDH superfamily. LDH family.
  
 
 0.970
ADU49557.1
FAD-dependent pyridine nucleotide-disulfide oxidoreductase; COGs: COG0493 NADPH-dependent glutamate synthase beta chain and related oxidoreductase; InterPro IPR017896: IPR013027: IPR000103: IPR017900; KEGG: mva:Mvan_4108 putative glutamate synthase (NADPH) small subunit; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; SPTR: 4Fe-4S ferredoxin, iron-sulfur binding domain protein; PFAM: Pyridine nucleotide-disulphide oxidoreductase; 4Fe-4S binding domain.
  
 
 0.967
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.
  
 
 0.963
pckG
Phosphoenolpyruvate carboxykinase (GTP); Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle; Belongs to the phosphoenolpyruvate carboxykinase [GTP] family.
   
 
 0.961
ADU48157.1
Glutamate synthase (NADH) large subunit; COGs: COG0069 Glutamate synthase domain 2; InterProIPR017932: IPR000583: IPR006982: IPR002932: IPR 002489; KEGG: kfl:Kfla_3074 glutamate synthase (ferredoxin); PFAM: ferredoxin-dependent glutamate synthase; glutamine amidotransferase class-II; glutamate synthase; glutamate synthase alpha subunit domain protein; PRIAM: Glutamate synthase (ferredoxin); SPTR: Putative glutamate synthase (NADPH) large subunit; PFAM: Conserved region in glutamate synthase; GXGXG motif; Glutamate synthase central domain; Glutamine amidotransferases class-II.
  
 
 0.954
ADU48159.1
COGs: COG0469 Pyruvate kinase; InterPro IPR015793: IPR018209: IPR015794: IPR001697; KEGG: cfl:Cfla_1980 pyruvate kinase; PFAM: Pyruvate kinase barrel; Pyruvate kinase alpha/beta; PRIAM: Pyruvate kinase; SPTR: Pyruvate kinase; TIGRFAM: pyruvate kinase; PFAM: Pyruvate kinase, barrel domain; Pyruvate kinase, alpha/beta domain; TIGRFAM: pyruvate kinase; Belongs to the pyruvate kinase family.
   
 0.952
Your Current Organism:
Intrasporangium calvum
NCBI taxonomy Id: 710696
Other names: I. calvum DSM 43043, Intrasporangium calvum DSM 43043, Intrasporangium calvum IFO 12989, Intrasporangium calvum NBRC 12989, Intrasporangium calvum str. DSM 43043, Intrasporangium calvum strain DSM 43043
Server load: low (32%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.