A0A105LBI9 · A0A105LBI9_9BURK

  • Protein
    NADH-quinone oxidoreductase subunit B
  • Gene
    nuoB
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 1 [4Fe-4S] cluster.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site39[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site40[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site104[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site134[4Fe-4S] cluster (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentplasma membrane
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functioniron ion binding
Molecular FunctionNADH dehydrogenase (ubiquinone) activity
Molecular FunctionNADH:ubiquinone reductase (non-electrogenic) activity
Molecular Functionquinone binding
Biological Processaerobic respiration
Biological Processelectron transport coupled proton transport

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

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

Gene names

    • Name
      nuoB
    • ORF names
      BW685_16520
      , WJ33_12185
      , WL29_09160

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • MSMB2036
    • MSMB2087WGS
    • A21
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Burkholderia > Burkholderia cepacia complex

Accessions

  • Primary accession
    A0A105LBI9

Proteomes

Subcellular Location

Cell membrane
; Peripheral membrane protein

Keywords

PTM/Processing

Keywords

Interaction

Subunit

NDH-1 is composed of 14 different subunits. Subunits NuoB, C, D, E, F, and G constitute the peripheral sector of the complex.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain39-148NADH:ubiquinone oxidoreductase-like 20kDa subunit

Sequence similarities

Belongs to the complex I 20 kDa subunit family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    167
  • Mass (Da)
    18,685
  • Last updated
    2016-04-13 v1
  • Checksum
    BB55826BE7807E4C
MIDQPFTLEKDGFVVTSLEAVLAAARTNSLWYMTFGLACCAVEMMHAAGARYDMDRFGMIPRASPRQCDLMIVSGTLTNKMAPAMRKVYDQMAEPRYVVSMGSCANGGGYYHYSYSVVRGCDRIVPVDVYVPGCPPTAEALIYGLMQLQRKIMEQSTHSQPRVFERR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LOXM01000007
EMBL· GenBank· DDBJ
KVG76848.1
EMBL· GenBank· DDBJ
Genomic DNA
LPHD01000222
EMBL· GenBank· DDBJ
KWA69569.1
EMBL· GenBank· DDBJ
Genomic DNA
MTJZ01000018
EMBL· GenBank· DDBJ
OMG72316.1
EMBL· GenBank· DDBJ
Genomic DNA

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