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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
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[Homology]
Score
ADW18832.1Pyruvate phosphate dikinase; COGs: COG0574 Phosphoenolpyruvate synthase/pyruvate phosphate dikinase; InterPro IPR002192: IPR008279; KEGG: dak:DaAHT2_2096 pyruvate phosphate dikinase PEP/pyruvate-binding protein; PFAM: pyruvate phosphate dikinase PEP/pyruvate-binding; PEP-utilising protein mobile region; SPTR: Pyruvate phosphate dikinase PEP/pyruvate-binding protein; PFAM: PEP-utilising enzyme, mobile domain; Pyruvate phosphate dikinase, PEP/pyruvate binding domain. (1419 aa)    
Predicted Functional Partners:
nifJ
COGs: COG0674 Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductase alpha subunit; InterProIPR011895: IPR017896: IPR017900: IPR002880: IPR 019752: IPR019456: IPR011766; KEGG: dak:DaAHT2_0906 pyruvate ferredoxin/flavodoxin oxidoreductase; 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; TIGRFAM: pyruvate ferredoxin/flavod [...]
    
 0.950
ADW19113.1
Response regulator receiver protein; COGs: COG0469 Pyruvate kinase; InterPro IPR001789: IPR015793: IPR018209: IPR001697; KEGG: bbe:BBR47_13840 pyruvate kinase; PFAM: Pyruvate kinase barrel; response regulator receiver; SMART: response regulator receiver; SPTR: Pyruvate kinase; TIGRFAM: pyruvate kinase; PFAM: Pyruvate kinase, barrel domain; Response regulator receiver domain; Pyruvate kinase, alpha/beta domain; TIGRFAM: pyruvate kinase.
     
 0.940
ADW19383.1
COGs: COG0469 Pyruvate kinase; InterPro IPR015793: IPR015794: IPR001697; KEGG: sfu:Sfum_2959 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.
     
 0.940
ADW18501.1
COGs: COG5016 Pyruvate/oxaloacetate carboxyltransferase; InterPro IPR000089: IPR000891: IPR003379: IPR001882; KEGG: dal:Dalk_3782 conserved carboxylase region; PFAM: Conserved carboxylase region; pyruvate carboxyltransferase; biotin/lipoyl attachment domain-containing protein; SPTR: Conserved carboxylase region; PFAM: HMGL-like; Conserved carboxylase domain; Biotin-requiring enzyme.
  
 
 0.931
ADW18147.1
Malic protein NAD-binding protein; COGs: COG0281 Malic enzyme; InterProIPR001891: IPR000209: IPR015884: IPR012301: IPR 012302; KEGG: dal:Dalk_0610 malate dehydrogenase; PFAM: malic protein NAD-binding; malic protein domain protein; SPTR: Malate dehydrogenase (Oxaloacetate-decarboxylating) (NADP(+)); PFAM: Malic enzyme, NAD binding domain; Malic enzyme, N-terminal domain.
  
 
 0.926
ADW16249.1
Pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; COGs: COG0674 Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductase alpha subunit; InterPro IPR019752: IPR002880; KEGG: dat:HRM2_42780 PorA3; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; Pyruvate/ketoisovalerate oxidoreductase, catalytic domain; SPTR: PorA3; PFAM: domain; Pyruvate ferredoxin/flavodoxin oxidoreductase; TIGRFAM: 2-oxoacid:acceptor oxidoreductase, alpha subunit.
    
 0.920
ADW18259.1
D-lactate dehydrogenase (cytochrome); COGs: COG0277 FAD/FMN-containing dehydrogenase; InterProIPR017900: IPR017896: IPR016166: IPR006094: IPR 004113; KEGG: dvl:Dvul_2725 D-lactate dehydrogenase (cytochrome); PFAM: FAD linked oxidase domain protein; PRIAM: D-lactate dehydrogenase (cytochrome); SPTR: D-lactate dehydrogenase (Cytochrome); PFAM: FAD binding domain; FAD linked oxidases, C-terminal domain.
    
 0.919
eno
Enolase; Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis; Belongs to the enolase family.
    
 0.918
ADW17655.1
COGs: COG1071 Pyruvate/2-oxoglutarate dehydrogenase complex dehydrogenase (E1) component eukaryotic type alpha subunit; InterPro IPR017597: IPR001017; KEGG: gur:Gura_1609 pyruvate dehydrogenase (acetyl-transferring); PFAM: dehydrogenase E1 component; PRIAM: Pyruvate dehydrogenase (acetyl-transferring); SPTR: Pyruvate dehydrogenase (Acetyl-transferring); TIGRFAM: pyruvate dehydrogenase (acetyl-transferring) E1 component, alpha subunit; PFAM: Dehydrogenase E1 component; TIGRFAM: pyruvate dehydrogenase E1 component, alpha subunit.
    
 0.914
ADW17654.1
Transketolase central region; COGs: COG0022 Pyruvate/2-oxoglutarate dehydrogenase complex dehydrogenase (E1) component eukaryotic type beta subunit; InterPro IPR005475: IPR005476: IPR017871; KEGG: gur:Gura_1610 transketolase, central region; PFAM: Transketolase central region; Transketolase domain-containing protein; SPTR: Transketolase, central region; PFAM: Transketolase, C-terminal domain; Transketolase, pyrimidine binding domain.
    
 0.913
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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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.