P9WIV9 · NUOG_MYCTU

Function

function

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 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 (By similarity).
Plays a critical role in M.tuberculosis ability to inhibit apoptosis of infected macrophages; thus helps the bacterium in its struggle to resist the host immune response (PubMed:17658950).
In fact, via a NuoG-dependent mechanism, M.tuberculosis can neutralize NOX2-derived reactive oxygen species (ROS) in order to inhibit TNF-alpha-mediated host cell apoptosis (PubMed:20421951).
Also mediates inhibition of neutrophil apoptosis, leading to delayed activation of naive CD4 T cells (PubMed:22264515).

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
[2Fe-2S] cluster (UniProtKB | Rhea| CHEBI:190135 )

Note: Binds 1 [2Fe-2S] cluster per subunit.
[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 3 [4Fe-4S] clusters per subunit.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site49[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site60[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site63[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site77[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site111[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site115[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site118[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site124[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site164[4Fe-4S] cluster 2 (UniProtKB | ChEBI)
Binding site167[4Fe-4S] cluster 2 (UniProtKB | ChEBI)
Binding site170[4Fe-4S] cluster 2 (UniProtKB | ChEBI)
Binding site214[4Fe-4S] cluster 2 (UniProtKB | ChEBI)
Binding site240[4Fe-4S] cluster 3 (UniProtKB | ChEBI)
Binding site243[4Fe-4S] cluster 3 (UniProtKB | ChEBI)
Binding site247[4Fe-4S] cluster 3 (UniProtKB | ChEBI)
Binding site275[4Fe-4S] cluster 3 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentpeptidoglycan-based cell wall
Cellular Componentplasma membrane
Cellular Componentplasma membrane respiratory chain complex I
Molecular Function2 iron, 2 sulfur cluster binding
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functionmetal ion binding
Molecular Functionmolybdopterin cofactor binding
Molecular FunctionNADH dehydrogenase (ubiquinone) activity
Molecular Functionquinone binding
Biological ProcessATP synthesis coupled electron transport
Biological Processcellular respiration
Biological Processsymbiont-mediated suppression of host apoptosis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    NADH-quinone oxidoreductase subunit G
  • EC number
  • Alternative names
    • NADH dehydrogenase I subunit G
    • NDH-1 subunit G

Gene names

    • Name
      nuoG
    • ORF names
      MTCY03A2.07c
    • Ordered locus names
      Rv3151

Organism names

Accessions

  • Primary accession
    P9WIV9
  • Secondary accessions
    • L0TBP2
    • P95175

Proteomes

Organism-specific databases

Phenotypes & Variants

Disruption phenotype

Deletion of nuoG in M.tuberculosis reduces its ability to inhibit apoptosis of infected human or mouse macrophages and significantly decreases its virulence in mice (PubMed:17658950).
The apoptogenic phenotype of the mutant strain is significantly reduced in human macrophages treated with caspase-3 and -8 inhibitors, TNF-alpha-neutralizing antibodies, and also after infection of murine TNF(-/-) macrophages. Moreover, incubation of macrophages with inhibitors of reactive oxygen species (ROS) reduces not only the apoptosis induced by the nuoG deletion mutant, but also its capacity to increase macrophage TNF-alpha secretion. The phagosomes infected with the mutant show increased ROS levels compared to M.tuberculosis phagosomes in primary murine and human alveolar macrophages. The increase in nuoG deletion mutant induced ROS and apoptosis is abolished in NOX-2 deficient (gp91(-/-)) macrophages (PubMed:20421951).
Compared to wild-type, the nuoG deletion mutant spreads to a larger number of lung phagocytic cells. Consistent with the shorter lifespan of infected neutrophils, infection with the nuoG mutant results in fewer bacteria per infected neutrophil, accelerated bacterial acquisition by dendritic cells, earlier trafficking of these dendritic cells to lymph nodes, and faster CD4 T cell priming. Neutrophil depletion abrogates accelerated CD4 T cell priming by the nuoG mutant, suggesting that inhibiting neutrophil apoptosis delays adaptive immunity in tuberculosis (PubMed:22264515).

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylthreonine
ChainPRO_00001185592-806NADH-quinone oxidoreductase subunit G

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

The type I NADH dehydrogenase consists of 14 different subunits.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain15-932Fe-2S ferredoxin-type
Domain95-1344Fe-4S His(Cys)3-ligated-type
Domain233-2894Fe-4S Mo/W bis-MGD-type

Sequence similarities

Belongs to the complex I 75 kDa subunit family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    806
  • Mass (Da)
    85,424
  • Last updated
    2014-04-16 v1
  • Checksum
    519A1EA833181064
MTQAADTDIRVGQPEMVTLTIDGVEISVPKGTLVIRAAELMGIQIPRFCDHPLLEPVGACRQCLVEVEGQRKPLASCTTVATDDMVVRTQLTSEIADKAQHGVMELLLINHPLDCPMCDKGGECPLQNQAMSNGRTDSRFTEAKRTFAKPINISAQVLLDRERCILCARCTRFSDQIAGDPFIDMQERGALQQVGIYADEPFESYFSGNTVQICPVGALTGTAYRFRARPFDLVSSPSVCEHCASGCAQRTDHRRGKVLRRLAGDDPEVNEEWNCDKGRWAFTYATQPDVITTPLIRDGGDPKGALVPTSWSHAMAVAAQGLAAARGRTGVLVGGRVTWEDAYAYAKFARITLGTNDIDFRARPHSAEEADFLAARIAGRHMAVSYADLESAPVVLLVGFEPEDESPIVFLRLRKAARRHRVPVYTIAPFATGGLHKMSGRLIKTVPGGEPAALDDLATGAVGDLLATPGAVIIVGERLATVPGGLSAAARLADTTGARLAWVPRRAGERGALEAGALPTLLPGGRPLADEVARAQVCAAWHIAELPAAAGRDADGILAAAADETLAALLVGGIEPADFADPDAVLAALDATGFVVSLELRHSTVTERADVVFPVAPTTQKAGAFVNWEGRYRTFEPALRGSTLQAGQSDHRVLDALADDMGVHLGVPTVEAAREELAALGIWDGKHAAGPHIAATGPTQPEAGEAILTGWRMLLDEGRLQDGEPYLAGTARTPVVRLSPDTAAEIGAADGEAVTVSTSRGSITLPCSVTDMPDRVVWLPLNSAGSTVHRQLRVTIGSIVKIGAGS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL123456
EMBL· GenBank· DDBJ
CCP45962.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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