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ANH79687.1 ANH79687.1 ANH79816.1 ANH79816.1 ANH79864.1 ANH79864.1 ANH79893.1 ANH79893.1 A8C56_04180 A8C56_04180 ANH80366.1 ANH80366.1 nuoN nuoN ANH82351.1 ANH82351.1 ANH84010.1 ANH84010.1 nuoK nuoK ANH82353.1 ANH82353.1 nuoI nuoI nuoH nuoH ANH82355.1 ANH82355.1 A8C56_16540 A8C56_16540 nuoD nuoD ANH82360.1 ANH82360.1 nuoB nuoB nuoA nuoA ANH83237.1 ANH83237.1
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.
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:
ANH79687.1Peptidase; Derived by automated computational analysis using gene prediction method: Protein Homology. (398 aa)
ANH79816.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (391 aa)
ANH79864.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (488 aa)
ANH79893.1NADPH:quinone reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (196 aa)
A8C56_04180cAMP-binding protein; Frameshifted; internal stop; Derived by automated computational analysis using gene prediction method: Protein Homology. (105 aa)
ANH80366.1Ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (115 aa)
nuoNNADH dehydrogenase; 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 2 family. (457 aa)
ANH82351.1NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (492 aa)
ANH84010.1NADH-quinone oxidoreductase subunit L; Derived by automated computational analysis using gene prediction method: Protein Homology. (632 aa)
nuoKNADH-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; Belongs to the complex I subunit 4L family. (108 aa)
ANH82353.1NADH dehydrogenase; 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. (166 aa)
nuoINADH-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)
nuoHNADH-quinone oxidoreductase subunit 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. (355 aa)
ANH82355.1NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (380 aa)
A8C56_16540GxxExxY protein; 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. (454 aa)
nuoDNADH dehydrogenase; 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 49 kDa subunit family. (406 aa)
ANH82360.1NADH dehydrogenase; 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 30 kDa subunit family. (170 aa)
nuoBNADH dehydrogenase; 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. (195 aa)
nuoANADH-quinone oxidoreductase subunit 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 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 3 family. (130 aa)
ANH83237.1Peptidase; Derived by automated computational analysis using gene prediction method: Protein Homology. (383 aa)
Your Current Organism:
Niabella ginsenosidivorans
NCBI taxonomy Id: 1176587
Other names: JCM 18199, KACC 16620, N. ginsenosidivorans, Niabella sp. BS26, strain BS26
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