close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING newly available directed regulatory networks a new typed view showing functional, physical, and regulatory edges in one network new clustering options and cluster-based layouts … and much more!
Explore STRING v12.5 →
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
ADW17037.1Transcriptional regulator, LysR family; COGs: COG0583 Transcriptional regulator; InterPro IPR000847: IPR005119; KEGG: dak:DaAHT2_2578 transcriptional regulator, LysR family; PFAM: LysR substrate-binding; regulatory protein LysR; SPTR: Transcriptional regulator, LysR family; PFAM: LysR substrate binding domain; Bacterial regulatory helix-turn-helix protein, lysR family. (330 aa)    
Predicted Functional Partners:
ADW19407.1
Transcriptional regulator, LysR family; COGs: COG0583 Transcriptional regulator; InterPro IPR000847: IPR005119; KEGG: dps:DP0725 DNA-binding transcriptional regulator IlvY; PFAM: LysR substrate-binding; regulatory protein LysR; SPTR: Probable transcriptional activator protein (IlvY); PFAM: Bacterial regulatory helix-turn-helix protein, lysR family; LysR substrate binding domain.
  
     0.676
ADW19022.1
Glutamate synthase (NADPH) large subunit; COGs: COG0069 Glutamate synthase domain 2; InterProIPR017932: IPR000583: IPR006982: IPR002932: IPR 002489; KEGG: cja:CJA_3147 glutamate synthase subunit alpha; PFAM: ferredoxin-dependent glutamate synthase; glutamine amidotransferase class-II; glutamate synthase; glutamate synthase alpha subunit domain protein; PRIAM: Glutamate synthase (ferredoxin); SPTR: Glutamate synthase large chain; PFAM: Conserved region in glutamate synthase; GXGXG motif; Glutamate synthase central domain; Glutamine amidotransferases class-II.
  
  
 0.499
ADW17071.1
FAD-dependent pyridine nucleotide-disulfide oxidoreductase; COGs: COG0493 NADPH-dependent glutamate synthase beta chain and related oxidoreductase; InterProIPR002489: IPR013027: IPR000103: IPR017900: IPR 017896; KEGG: dps:DP2624 glutamate synthase, beta subunit; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; glutamate synthase alpha subunit domain protein; SPTR: Related to glutamate synthase, beta subunit; PFAM: Pyridine nucleotide-disulphide oxidoreductase; GXGXG motif.
   
 
 0.485
ADW17038.1
NADH dehydrogenase subunit A; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain.
       0.442
nuoB
NADH dehydrogenase subunit B; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
       0.442
ADW17040.1
NADH dehydrogenase (ubiquinone) 30 kDa subunit; COGs: COG0852 NADH:ubiquinone oxidoreductase 27 kD subunit; InterPro IPR001268; KEGG: ote:Oter_0745 NADH dehydrogenase (ubiquinone) 30 kDa subunit; PFAM: NADH dehydrogenase (ubiquinone) 30 kDa subunit; SPTR: NADH dehydrogenase (Ubiquinone) 30 kDa subunit; PFAM: Respiratory-chain NADH dehydrogenase, 30 Kd subunit.
       0.424
nuoD
NADH dehydrogenase subunit D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 49 kDa subunit family.
       0.424
ADW17046.1
Multisubunit sodium/proton antiporter, MrpD subunit; COGs: COG1009 NADH:ubiquinone oxidoreductase subunit 5 (chain L)/Multisubunit Na+/H+ antiporter MnhA subunit; InterPro IPR001750: IPR003916; KEGG: dps:DP1313 putative monovalent cation/H+ antiporter subunit D; PFAM: NADH/Ubiquinone/plastoquinone (complex I); SPTR: Probable NADH dehydrogenase, subunit 5; PFAM: NADH-Ubiquinone/plastoquinone (complex I), various chains; NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminus; TC 2.A.63.1.
     
 0.415
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
Server load: low (36%) [HD]