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RPB_0550 RPB_0550 RPB_1829 RPB_1829 nuoI2 nuoI2 RPB_1479 RPB_1479 RPB_0724 RPB_0724 RPB_0663 RPB_0663 RPB_4311 RPB_4311 RPB_3141 RPB_3141 RPB_3415 RPB_3415 RPB_1232 RPB_1232 RPB_0977 RPB_0977 nuoI1 nuoI1 RPB_1233 RPB_1233 RPB_0958 RPB_0958 RPB_0851 RPB_0851 RPB_0960 RPB_0960 RPB_1084 RPB_1084 RPB_0013 RPB_0013 RPB_0324 RPB_0324
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:
RPB_05504Fe-4S ferredoxin, iron-sulfur binding; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (112 aa)
RPB_1829Conserved hypothetical protein. (437 aa)
nuoI2NADH-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. (162 aa)
RPB_14794Fe-4S ferredoxin, iron-sulfur binding. (77 aa)
RPB_0724Formate dehydrogenase, alpha subunit. (948 aa)
RPB_06634Fe-4S ferredoxin, iron-sulfur binding. (382 aa)
RPB_43114Fe-4S ferredoxin, iron-sulfur binding. (479 aa)
RPB_3141FMN-binding. (752 aa)
RPB_34154Fe-4S ferredoxin, iron-sulfur binding; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (101 aa)
RPB_1232Indolepyruvate ferredoxin oxidoreductase, alpha subunit; Catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates. (607 aa)
RPB_09774Fe-4S ferredoxin, iron-sulfur binding. (103 aa)
nuoI1NADH-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. (171 aa)
RPB_1233Pyruvate ferredoxin/flavodoxin oxidoreductase. (315 aa)
RPB_09584Fe-4S ferredoxin, iron-sulfur binding. (64 aa)
RPB_0851Pyruvate flavodoxin/ferredoxin oxidoreductase. (1652 aa)
RPB_09604Fe-4S ferredoxin, iron-sulfur binding. (73 aa)
RPB_1084Electron-transferring-flavoprotein dehydrogenase; Accepts electrons from ETF and reduces ubiquinone. (552 aa)
RPB_00134Fe-4S ferredoxin, iron-sulfur binding. (515 aa)
RPB_0324Succinate dehydrogenase subunit B; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (269 aa)
Your Current Organism:
Rhodopseudomonas palustris HaA2
NCBI taxonomy Id: 316058
Other names: R. palustris HaA2, Rhodopseudomonas palustris str. HaA2, Rhodopseudomonas palustris strain HaA2
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