nuoG NADH:quinone oxidoreductase subunit G [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

Official Symbol: nuoG
Official Full Name: NADH:quinone oxidoreductase subunit G
Primary source: ECOCYC:EG12087
Locus tag: b2283
See related: ASAP:ABE-0007543
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage: Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as: ECK2277
Summary: Leif et al. [More information is available at EcoGene: EG12087]. NuoG is part of the soluble fragment of NADH dehydrogenase I, which represents the electron input part of the enzyme . [More information is available at EcoCyc: EG12087].
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NC_000913.3 Genomic Context describing neighboring genes

Go to nucleotide: Graphics FASTA GenBank

Study determined the distance between a MTSL labeled complex I variant and the bound quinone by continuous-wave (cw) EPR allowing an inference on the location of the quinone binding site.
Title: Spin labeling of the Escherichia coli NADH ubiquinone oxidoreductase (complex I).
Iron-sulfur cluster N5 is coordinated by an HXXXCXXCXXXXXC motif in the NuoG subunit of Escherichia coli NADH:quinone oxidoreductase (complex I)
Title: Iron-sulfur cluster N5 is coordinated by an HXXXCXXCXXXXXC motif in the NuoG subunit of Escherichia coli NADH:quinone oxidoreductase (complex I).
N-terminus verified by Edman degradation on mature peptide
Title: Adenosine diphosphate sugar pyrophosphatase prevents glycogen biosynthesis in Escherichia coli.
analyze spectra from the overexpressed NuoG subunit from Escherichia coli complex I and compare them with spectra from the intact enzyme
Title: Reevaluating the relationship between EPR spectra and enzyme structure for the iron sulfur clusters in NADH:quinone oxidoreductase.
structural importance of the iron-sulfur binding domains
Title: Characterization of the iron-sulfur cluster N7 (N1c) in the subunit NuoG of the proton-translocating NADH-quinone oxidoreductase from Escherichia coli.

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

Function	Evidence Code	Pubs
enables 2 iron, 2 sulfur cluster binding	IDA Inferred from Direct Assay more info	PubMed
enables 2 iron, 2 sulfur cluster binding	IEA Inferred from Electronic Annotation more info
enables 4 iron, 4 sulfur cluster binding	IDA Inferred from Direct Assay more info	PubMed
enables 4 iron, 4 sulfur cluster binding	IEA Inferred from Electronic Annotation more info
contributes_to FMN binding	IDA Inferred from Direct Assay more info	PubMed
contributes_to NADH dehydrogenase (ubiquinone) activity	IDA Inferred from Direct Assay more info	PubMed
enables NADH dehydrogenase (ubiquinone) activity	IEA Inferred from Electronic Annotation more info
contributes_to NADH dehydrogenase activity	IBA Inferred from Biological aspect of Ancestor more info
contributes_to NADH dehydrogenase activity	IDA Inferred from Direct Assay more info	PubMed
enables iron-sulfur cluster binding	IEA Inferred from Electronic Annotation more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables molybdopterin cofactor binding	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables quinone binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in ATP synthesis coupled electron transport	IEA Inferred from Electronic Annotation more info
involved_in aerobic respiration	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in cellular respiration	IEA Inferred from Electronic Annotation more info
involved_in proton transmembrane transport	IEA Inferred from Electronic Annotation more info
involved_in respiratory electron transport chain	IBA Inferred from Biological aspect of Ancestor more info
involved_in respiratory electron transport chain	IDA Inferred from Direct Assay more info	PubMed

Component	Evidence Code	Pubs
part_of NADH dehydrogenase complex	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
is_active_in membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in membrane	IDA Inferred from Direct Assay more info	PubMed
located_in membrane	IEA Inferred from Electronic Annotation more info
part_of oxidoreductase complex	IEA Inferred from Electronic Annotation more info
located_in plasma membrane	IDA Inferred from Direct Assay more info	PubMed
located_in plasma membrane	IEA Inferred from Electronic Annotation more info
part_of respiratory chain complex I	IDA Inferred from Direct Assay more info	PubMed
part_of respiratory chain complex I	IMP Inferred from Mutant Phenotype more info	PubMed
part_of respiratory chain complex I	NAS Non-traceable Author Statement more info	PubMed

NP_416786.4

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