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
Saut_1829COGs: COG1034 NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G); InterPro IPR001041:IPR001450:IPR006963:IPR019574:IPR 000283:IPR017900; KEGG: tdn:Suden_1823 NADH dehydrogenase subunit G; PFAM: NADH:ubiquinone oxidoreductase, subunit G, iron-sulphur binding; ferredoxin; 4Fe-4S ferredoxin iron-sulfur binding domain protein; molybdopterin oxidoreductase Fe4S4 region; SPTR: A3ERJ1 Anaerobic dehydrogenase; PFAM: NADH-ubiquinone oxidoreductase-G iron-sulfur binding region. (747 aa)    
Predicted Functional Partners:
Saut_1833
NADH dehydrogenase subunit C; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 30 kDa subunit family.
 
 0.999
Saut_1830
COGs: COG0493 NADPH-dependent glutamate synthase beta chain and related oxidoreductase; InterPro IPR000759:IPR013027:IPR000103:IPR001327:IPR 019575; KEGG: tdn:Suden_1824 glutamate synthase (NADPH); PFAM: NADH ubiquinone oxidoreductase, F subunit, iron sulphur binding; FAD-dependent pyridine nucleotide-disulphide oxidoreductase; PRIAM: Glutamate synthase (NADPH); SPTR: A3EW97 NADH ubiquinone oxidoreductase; PFAM: NADH-ubiquinone oxidoreductase-F iron-sulfur binding region; Pyridine nucleotide-disulphide oxidoreductase.
 0.998
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.
 
 0.998
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.
 
 0.997
nuoI
NADH dehydrogenase subunit I; 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.
 
 0.996
nuoN
NADH dehydrogenase subunit N; 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 subunit 2 family.
 
 0.995
Saut_1822
COGs: COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M); InterPro IPR003918:IPR001750:IPR010227; KEGG: tdn:Suden_1816 NADH dehydrogenase subunit M; PFAM: NADH/Ubiquinone/plastoquinone (complex I); SPTR: A3UCU6 NADH dehydrogenase subunit M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH-Ubiquinone/plastoquinone (complex I), various chains; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M.
 
 0.995
nuoH
NADH dehydrogenase subunit H; 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. This subunit may bind ubiquinone.
 
 0.995
Saut_1823
COGs: COG1009 NADH:ubiquinone oxidoreductase subunit 5 (chain L)/Multisubunit Na+/H+ antiporter MnhA subunit; InterPro IPR018393:IPR003916:IPR001750:IPR001516:IPR 003945; KEGG: tdn:Suden_1817 NADH dehydrogenase subunit L; PFAM: NADH/Ubiquinone/plastoquinone (complex I); NADH-Ubiquinone oxidoreductase (complex I) chain 5/L domain protein; SPTR: Q9PMA7 NADH-quinone oxidoreductase subunit L; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain L; PFAM: NADH-Ubiquinone/plastoquinone (complex I), various chains; NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminus; TIG [...]
 
 
 0.994
Saut_1825
NADH dehydrogenase subunit J; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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.
 
 
 0.994
Your Current Organism:
Sulfurimonas autotrophica
NCBI taxonomy Id: 563040
Other names: S. autotrophica DSM 16294, Sulfurimonas autotrophica DSM 16294, Sulfurimonas autotrophica OK10, Sulfurimonas autotrophica str. DSM 16294, Sulfurimonas autotrophica strain DSM 16294
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.