Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P29923 (NQO11_PARDE)

Last modified October 13, 2009. Version 63. 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 11
    EC=1.6.99.5
Alternative name(s):
    NADH dehydrogenase I, chain 11
    NDH-1, chain 11
Gene names
Name: nqo11
OrganismParacoccus denitrificans
Taxonomic identifier266 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Protein attributes

Sequence length101 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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. Ref.2

Sequence similarities

Belongs to the complex I subunit 4L family.

Ontologies

Keywords
   Cellular componentCell inner membrane
Cell membrane
Membrane
   DomainTransmembrane
   LigandNAD
Ubiquinone
   Molecular functionOxidoreductase
   PTMQuinone
Gene Ontology (GO)
   Biological processATP synthesis coupled electron transport

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionNADH dehydrogenase (quinone) activity

Inferred from electronic annotation. Source: EC

quinone binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 101101NADH-quinone oxidoreductase chain 11
PRO_0000118522

Regions

Topological domain1 – 33Periplasmic Probable
Transmembrane4 – 2421 Potential
Topological domain25 – 295Cytoplasmic Probable
Transmembrane30 – 5021 Potential
Topological domain51 – 6414Periplasmic Probable
Transmembrane65 – 8521 Potential
Topological domain86 – 10116Cytoplasmic Ref.2

Sequences

Sequence LengthMass (Da)Tools
P29923-1 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: A8061FD86A8B9AB8

FASTA10110,856
        10         20         30         40         50         60 
MIGLTHYLVV GAILFVTGIF GIFVNRKNVI VILMSIELML LAVNINFVAF STHLGDLAGQ 

        70         80         90        100 
VFTMFVLTVA AAEAAIGLAI LVVFFRNRGT IAVEDVNVMK G 

« 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.
[2]"Characterization of the membrane domain Nqo11 subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans."
Kao M.-C., Di Bernardo S., Matsuno-Yagi A., Yagi T.
Biochemistry 41:4377-4384(2002) [PubMed: 11914084] [Abstract]
Cited for: SUBCELLULAR LOCATION, TOPOLOGY.

Cross-references

Sequence databases

L02354 Genomic DNA. Translation: AAA25597.1.
PIRG45456.

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

InterProIPR001133. NADH_UbQ/Q_OxRdtase_chain4L.
IPR017863. NADH_UbQ_OxRdtase_4L_subgr.
[Graphical view]
PANTHERPTHR11434. Oxidored_4L. 1 hit.
PfamPF00420. Oxidored_q2. 1 hit.
[Graphical view]
ProDomPD002107. NADH_dh_ubiq1. 1 hit.
PD000359. Oxidred4L. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Entry information

Entry nameNQO11_PARDE
AccessionPrimary (citable) accession number: P29923
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: October 13, 2009
This is version 63 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