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Reviewed, UniProtKB/Swiss-Prot P29922 (NQO10_PARDE)

Last modified June 16, 2009. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    NADH-quinone oxidoreductase chain 10
    EC=1.6.99.5
Alternative name(s):
    NADH dehydrogenase I, chain 10
    NDH-1, chain 10
Gene names
Name: nqo10
OrganismParacoccus denitrificans
Taxonomic identifier266 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Protein attributes

Sequence length200 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

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 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

NADH + quinone = NAD+ + quinol.

Subunit structure

NDH-1 is composed of at least 14 different subunits, nqo1 to nqo14. The complex has a L-shaped structure, with the hydrophobic arm (subunits nqo7, nqo8, nqo10 to nqo14) embedded in the inner membrane and the hydrophilic peripheral arm (subunits nqo1 to nqo6, nqo9) protruding into the bacterial cytoplasm. The hydrophilic domain contains all the redox centers.

Subcellular location

Cell inner membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the complex I subunit 6 family.

Ontologies

Keywords
   Cellular componentCell inner membrane
Cell membrane
Membrane
   DomainTransmembrane
   LigandNAD
Ubiquinone
   Molecular functionOxidoreductase
   PTMQuinone
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNADH dehydrogenase (ubiquinone) activity

Inferred from electronic annotation. Source: InterPro

quinone binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 200200NADH-quinone oxidoreductase chain 10
PRO_0000118368

Regions

Transmembrane2 – 2221 Potential
Transmembrane26 – 4621 Potential
Transmembrane51 – 7121 Potential
Transmembrane90 – 11021 Potential
Transmembrane144 – 16421 Potential

Sequences

Sequence LengthMass (Da)Tools
P29922-1 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 9D3B421C33F4ACAE

FASTA20021,819
        10         20         30         40         50         60 
MMTFAFYLFA ISACVAGFMV VIGRNPVHSV LWLILAFLSA AGLFVLQGAE FVAMLLVVVY 

        70         80         90        100        110        120 
VGAVAVLFLF VVMMLDVDFA ELKGELARYL PLALVIGVVL LAQLGIAFSG WTPSDQAESL 

       130        140        150        160        170        180 
RAAPVDAAVE NTLGLGLVLY DRYVLMFQLA GLVLLVAMIG AIVLTMRHRK DVKRQNVLEQ 

       190        200 
MWRDPAKTME LKDVKPGQGL 

« Hide

References

[1]"DNA sequencing of the seven remaining structural genes of the gene cluster encoding the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans."
Xu X., Matsuno-Yagi A., Yagi T.
Biochemistry 32:968-981(1993) [PubMed: 8422400] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13543 / NRRL B-3784.

Cross-references

Sequence databases

L02354 Genomic DNA. Translation: AAA25596.1.
PIRF45456.

3D structure databases

ModBaseSearch...

Protein family/group databases

TCDB3.D.1.2.1. proton-translocating NADH dehydrogenase (NDH) family.

Enzyme and pathway databases

BRENDA1.6.99.5. 59.

Family and domain databases

InterProIPR001457. NADH_UbQ/plastoQ_OxRdtase_su6.
[Graphical view]
PfamPF00499. Oxidored_q3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNQO10_PARDE
AccessionPrimary (citable) accession number: P29922
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents