S5NHA5 · S5NHA5_SALBN

Function

function

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.
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.

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 )

GO annotations

AspectTerm
Cellular Componentmembrane
Cellular Componentoxidoreductase complex
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

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    NADH-quinone oxidoreductase
  • EC number

Gene names

    • ORF names
      A464_2437

Organism names

  • Taxonomic identifier
  • Strain
    • N268-08
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella

Accessions

  • Primary accession
    S5NHA5

Proteomes

Subcellular Location

PTM/Processing

Keywords

Interaction

Subunit

Composed of 13 different subunits. Subunits NuoCD, E, F, and G constitute the peripheral sector of the complex.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-832Fe-2S ferredoxin-type
Domain83-1224Fe-4S His(Cys)3-ligated-type
Domain221-2774Fe-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
    908
  • Mass (Da)
    100,029
  • Last updated
    2013-10-16 v1
  • Checksum
    06B3A7D4F9F3B6DF
MATIHVDGKEYEVNGADNLLQACLSLGLDIPYFCWHPALGSVGACRQCAVKQYQNAEDTRGRLVMSCMTPATDGTFISIDDEEAKQFRESVVEWLMTNHPHDCPVCEEGGNCHLQDMTVMTGHSFRRYRFTKRTHRNQDLGPFISHEMNRCIACYRCVRYYKDYADGTDLGVYGAHDNVYFGRPEDGTLESEFSGNLVEICPTGVFTDKTHSERYNRKWDMQFAPSICQQCSIGCNISPGERYGELRRIENRYNGTVNHYFLCDRGRFGYGYVNLKDRPRQPIQRRGDDFITLNAEQAMQGAADILRQSKKVIGIGSPRASVESNFALRELVGAENFYTGIAQGEQERLQLALKVLREGGIHTPALREIESYDAVLVLGEDVTQTGARVALAVRQAVKGKAREMAAAQKVADWQIAAILNIGQRAKHPLFVTNVDNTRLDDIAAWTYCAPVEDQARLGFAIAHALDNTAPAVDGISSDLQNKIDVIVQALAGAKKPLIISGTNAGSLEMIQAAANVAKALKGRGADVGITMIARSVNSMGLGMMGGGSLDDALTELETGRADAVVVLENDLHRHASATRVNAALSKAPLVMVVDHQRTAIMENAHLVLSAASFAESDGTVINNEGRAQRFFQVYDPAYYDSSTIMLESWRWLHSLHSTVENREVDWTQLDHVIDAVIAAMPEFAGIKDAAPDATFRIRGQKLAREPHRYSGRTAMRANISVHEPRQPQDKDTMFAFSMEGNNQPSAPRSQIPFAWAPGWNSPQAWNKFQDEVGGKLRHGDPGVRLIEASANGLDYFTSVPASFQAQEGEWRIAPYYHLFGSDELSQRSPVFQSRMPQPYIKLNPADAAKLGVNAGTHVSFSYDGYTVTLPVDISEGLTAGQVGLPMGMPGIAPVLAGARLEDLREAQQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP006608
EMBL· GenBank· DDBJ
AGR59622.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp