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nuoB nuoB nuoC nuoC nuoD nuoD Sthe_0300 Sthe_0300 Sthe_0752 Sthe_0752 Sthe_1238 Sthe_1238 Sthe_1239 Sthe_1239 nuoI nuoI Sthe_1922 Sthe_1922
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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filled nodes:
a 3D structure is known or predicted
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Your Input:
nuoBNADH-quinone oxidoreductase, B subunit; 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. (185 aa)
nuoCNADH (or F420H2) dehydrogenase, subunit C; 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 30 kDa subunit family. (202 aa)
nuoDNADH dehydrogenase I, D subunit; 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. (410 aa)
Sthe_0300KEGG: mgm:Mmc1_3623 proton-translocating NADH- quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). (527 aa)
Sthe_0752PFAM: Respiratory-chain NADH dehydrogenase domain 51 kDa subunit; KEGG: mav:MAV_0925 respiratory-chain NADH dehydrogenase 51 kd subunit family protein. (442 aa)
Sthe_1238PFAM: Respiratory-chain NADH dehydrogenase domain 51 kDa subunit; KEGG: pth:PTH_2648 NADH:ubiquinone oxidoreductase, NADH-binding 51 kD subunit. (575 aa)
Sthe_1239PFAM: NADH dehydrogenase (ubiquinone) 24 kDa subunit; KEGG: tko:TK1614 NADH dehydrogenase subunit E. (180 aa)
nuoINADH-quinone oxidoreductase, chain 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. (148 aa)
Sthe_19222-amino-4-hydroxy-6-hydroxymethyldihydropteridin epyrophosphokinase; KEGG: dar:Daro_3183 7,8-dihydro-6- hydroxymethylpterin-pyrophosphokinase; TIGRFAM:2-amino-4-hydroxy-6-hydroxymethyldihydropter idinepyrophosphokinase; PFAM: 78-dihydro-6-hydroxymethylpterin- pyrophosphokinase HPPK. (167 aa)
Your Current Organism:
Sphaerobacter thermophilus
NCBI taxonomy Id: 479434
Other names: S. thermophilus DSM 20745, Sphaerobacter thermophilus DSM 20745, Sphaerobacter thermophilus str. DSM 20745, Sphaerobacter thermophilus strain DSM 20745
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