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Daes_1288 Daes_1288 nuoB nuoB Daes_1290 Daes_1290 nuoD nuoD nuoH nuoH Daes_1293 Daes_1293 Daes_1294 Daes_1294 nuoK nuoK Daes_1299 Daes_1299 nuoN nuoN
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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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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
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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:
Daes_1288NADH-ubiquinone/plastoquinone oxidoreductase chain 3; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. (125 aa)
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. (181 aa)
Daes_1290PFAM: NADH dehydrogenase (ubiquinone) 30 kDa subunit; KEGG: dvm:DvMF_1595 NADH dehydrogenase (ubiquinone) 30 kDa subunit. (175 aa)
nuoDNADH dehydrogenase (quinone); 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. (390 aa)
nuoHNADH dehydrogenase (quinone); 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. (324 aa)
Daes_1293KEGG: dsa:Desal_1494 4Fe-4S ferredoxin iron-sulfur binding domain protein. (195 aa)
Daes_1294NADH-ubiquinone/plastoquinone oxidoreductase chain 6; 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. (169 aa)
nuoKNADH-ubiquinone oxidoreductase chain 4L; 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. (102 aa)
Daes_1299KEGG: dsa:Desal_1500 proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). (510 aa)
nuoNNADH/Ubiquinone/plastoquinone (complex 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; Belongs to the complex I subunit 2 family. (475 aa)
Your Current Organism:
Pseudodesulfovibrio aespoeensis
NCBI taxonomy Id: 643562
Other names: Desulfovibrio aespoeensis Aspo-2, Desulfovibrio aespoeensis DSM 10631, P. aespoeensis Aspo-2, Pseudodesulfovibrio aespoeensis Aspo-2, Pseudodesulfovibrio aespoeensis DSM 10631
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