Reviewed,
UniProtKB/Swiss-Prot P29923 (NQO11_PARDE)
Last modified
October 13, 2009.
Version 63.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended 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 |
| ||
| Organism | Paracoccus denitrificans | ||
| Taxonomic identifier | 266 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Paracoccus |
Protein attributes
| Sequence length | 101 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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 | |
| Sequence similarities | Belongs to the complex I subunit 4L family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell inner membrane Cell membrane Membrane |
| Domain | Transmembrane |
| Ligand | NAD Ubiquinone |
| Molecular function | Oxidoreductase |
| PTM | Quinone |
| Gene Ontology (GO) | |
| Biological process | ATP synthesis coupled electron transport Inferred from electronic annotation. Source: InterPro |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membraneInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | NADH dehydrogenase (quinone) activity Inferred from electronic annotation. Source: EC quinone bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 101 | 101 | NADH-quinone oxidoreductase chain 11 | PRO_0000118522 | |||||
Regions | |||||||||
| Topological domain | 1 – 3 | 3 | Periplasmic Probable | ||||||
| Transmembrane | 4 – 24 | 21 | Potential | ||||||
| Topological domain | 25 – 29 | 5 | Cytoplasmic Probable | ||||||
| Transmembrane | 30 – 50 | 21 | Potential | ||||||
| Topological domain | 51 – 64 | 14 | Periplasmic Probable | ||||||
| Transmembrane | 65 – 85 | 21 | Potential | ||||||
| Topological domain | 86 – 101 | 16 | Cytoplasmic Ref.2 | ||||||
Sequences
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. | |
| PIR | G45456. |
3D structure databases | |
| ModBase | Search... |
Protein family/group databases | |
| TCDB | 3.D.1.2.1. proton-translocating NADH dehydrogenase (NDH) family. |
Enzyme and pathway databases | |
| BRENDA | 1.6.99.5. 59. |
Family and domain databases | |
| InterPro | IPR001133. NADH_UbQ/Q_OxRdtase_chain4L. IPR017863. NADH_UbQ_OxRdtase_4L_subgr. [Graphical view] |
| PANTHER | PTHR11434. Oxidored_4L. 1 hit. |
| Pfam | PF00420. Oxidored_q2. 1 hit. [Graphical view] |
| ProDom | PD002107. NADH_dh_ubiq1. 1 hit. PD000359. Oxidred4L. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| ProtoNet | Search... |
Entry information
| Entry name | NQO11_PARDE | ||||||||
| Accession | Primary (citable) accession number: P29923 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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