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folK folK cyoB cyoB sdhC sdhC sdhA sdhA sdhB sdhB nuoN nuoN nuoL nuoL nuoK nuoK nuoJ nuoJ nuoI nuoI nuoH nuoH nuoG nuoG nuoF nuoF nuoE nuoE nuoB nuoB nuoA nuoA
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
Your Input:
folK2-amino-4-hydroxy-6-hydroxymethyldihyropteridine pyrophosphokinase; Ortholog to Escherichia coli bnum: b0142; MultiFun: Metabolism 1.5.3.2. (164 aa)
cyoBCytochrome o ubiquinol oxidase, subunit I; Ortholog to Escherichia coli bnum: b0431; MultiFun: Cell structure 6.1; Metabolism 1.3.6, 1.4.2; Transport 4.3.D.4, 4.S.82; Belongs to the heme-copper respiratory oxidase family. (653 aa)
sdhCSuccinate dehydrogenase cytochrome b-556 subunit; Ortholog to Escherichia coli bnum: b0721; MultiFun: Cell structure 6.1; Metabolism 1.3.4, 1.3.6, 1.4.1, 1.4.3, 1.6.15.1. (135 aa)
sdhASuccinate dehydrogenase catalytic and flavoprotein subunit; Ortholog to Escherichia coli bnum: b0723; MultiFun: Metabolism 1.3.4, 1.3.6, 1.4.1; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (594 aa)
sdhBSuccinate dehydrogenase iron-sulfur protein; Ortholog to Escherichia coli bnum: b0724; MultiFun: Metabolism 1.3.4, 1.3.6, 1.4.1. (248 aa)
nuoNNADH dehydrogenase I chain N, membrane 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 subunit 2 family. (497 aa)
nuoLNADH dehydrogenase I chain L, membrane subunit; Ortholog to Escherichia coli bnum: b2278; MultiFun: Cell structure 6.1; Metabolism 1.3.6, 1.3.7, 1.4.1; Transport 4.3.D.1, 4.S.130. (628 aa)
nuoKNADH dehydrogenase I chain K; 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 4L family. (100 aa)
nuoJNADH dehydrogenase I chain 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. (183 aa)
nuoINADH dehydrogenase I chain I, 2Fe-2S ferredoxin-related; 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. (181 aa)
nuoHNADH dehydrogenase I chain 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. (323 aa)
nuoGNADH dehydrogenase I chain G; 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. Belongs to the complex I 75 kDa subunit family. (919 aa)
nuoFNADH dehydrogenase I chain F; 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 51 kDa subunit family. (443 aa)
nuoENADH dehydrogenase I chain E; Ortholog to Escherichia coli bnum: b2285; MultiFun: Metabolism 1.3.6; Metabolism 1.3.7, 1.4.1; Transport 4.3.D.1, 4.S.130. (173 aa)
nuoBNADH dehydrogenase I chain B, binds FeS cluster N2; 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. (236 aa)
nuoANADH dehydrogenase I chain A; 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 3 family. (146 aa)
Your Current Organism:
Blochmannia pennsylvanicus
NCBI taxonomy Id: 291272
Other names: C. Blochmannia pennsylvanicus str. BPEN, Candidatus Blochmannia pennsylvanicus BPEN, Candidatus Blochmannia pennsylvanicus str. BPEN, Candidatus Blochmannia pennsylvanicus strain BPEN
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