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nuoB nuoB nuoI nuoI nuoK nuoK ADZ78161.1 ADZ78161.1 ADZ78762.1 ADZ78762.1 nuoK-2 nuoK-2 ADZ78766.1 ADZ78766.1 ADZ79547.1 ADZ79547.1 nuoB-2 nuoB-2 ADZ80065.1 ADZ80065.1
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.
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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
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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
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textmining
co-expression
protein homology
Your Input:
nuoBNAD(P)H-quinone oxidoreductase subunit 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 a menaquinone. 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)
nuoINAD(P)H-quinone oxidoreductase 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. (169 aa)
nuoKNAD(P)H-quinone oxidoreductase subunit 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 a menaquinone. 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. (109 aa)
ADZ78161.1TIGRFAM: NADH-quinone oxidoreductase, chain M/4; KEGG: phe:Phep_4070 proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH:ubiquinone/plastoquinone oxidoreductase. (484 aa)
ADZ78762.1PFAM: 4Fe-4S binding domain; KEGG: dfe:Dfer_4037 4Fe-4S ferredoxin iron-sulfur binding domain protein. (187 aa)
nuoK-2NAD(P)H-quinone oxidoreductase subunit 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 a menaquinone. 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. (101 aa)
ADZ78766.1TIGRFAM: NADH-quinone oxidoreductase, chain M/4; KEGG: cli:Clim_0853 proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH:ubiquinone/plastoquinone oxidoreductase. (534 aa)
ADZ79547.1PFAM: 4Fe-4S binding domain; KEGG: phe:Phep_3203 4Fe-4S ferredoxin iron-sulfur binding domain protein. (117 aa)
nuoB-2NAD(P)H-quinone oxidoreductase subunit 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 a menaquinone. 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. (163 aa)
ADZ80065.1TIGRFAM: Cytochrome c oxidase cbb3-type, subunit I; Cytochrome c oxidase, monohaem subunit/FixO; KEGG: phe:Phep_2484 putative bifunctional cbb3-type cytochrome c oxidase subunit I/II; PFAM: Cytochrome c oxidase, monohaem subunit/FixO; Cytochrome c oxidase, subunit I; Belongs to the heme-copper respiratory oxidase family. (703 aa)
Your Current Organism:
Sphingobacterium sp. 21
NCBI taxonomy Id: 743722
Other names: S. sp. 21
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