A1B495 (NUOD_PARDP) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 41.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: NADH-quinone oxidoreductase subunit D EC=1.6.99.5 Alternative name(s): NADH dehydrogenase I, subunit 4 NADH dehydrogenase I, subunit D NADH-quinone oxidoreductase subunit 4 Short name=NQO4 NDH-1, subunit 4 NDH-1, subunit D | ||||||
| Gene names |
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| Organism | Paracoccus denitrificans (strain Pd 1222) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 318586 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Paracoccus |
Protein attributes
| Sequence length | 412 AA. |
| Sequence status | Complete. |
| 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 By similarity. HAMAP MF_01358 |
| Catalytic activity | NADH + quinone = NAD+ + quinol. HAMAP MF_01358 |
| 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 By similarity. NADH-quinone oxidoreductase forms a supercomplex with ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) and cytochrome c oxidase (complex IV), which stabilizes the NADH-quinone oxidoreductase complex. Ref.2 |
| Subcellular location | Cell inner membrane; Peripheral membrane protein Probable Ref.2. |
| Sequence similarities | Belongs to the complex I 49 kDa subunit family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transport |
| Cellular component | Cell inner membrane Cell membrane Membrane |
| Ligand | NAD Ubiquinone |
| Molecular function | Oxidoreductase |
| PTM | Quinone |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | transport Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | NAD binding Inferred from electronic annotation. Source: InterPro NADH dehydrogenase (quinone) activityInferred 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 – 412 | 412 | NADH-quinone oxidoreductase subunit D HAMAP MF_01358 | PRO_0000357882 | |||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. Richardson P.Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Pd 1222. |
| [2] | "Assembly of respiratory complexes I, III, and IV into NADH oxidase supercomplex stabilizes complex I in Paracoccus denitrificans." Stroh A., Anderka O., Pfeiffer K., Yagi T., Finel M., Ludwig B., Schagger H. J. Biol. Chem. 279:5000-5007(2004) [PubMed: 14610094] [Abstract] Cited for: IDENTIFICATION IN NADH OXIDASE SUPERCOMPLEX, SUBUNIT, SUBCELLULAR LOCATION. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000489 Genomic DNA. Translation: ABL70339.1. |
| RefSeq | YP_916035.1. NC_008686.1. |
3D structure databases | |
| ProteinModelPortal | A1B495. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A1B495. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 4579301. |
| GenomeReviews | Gene locus Pden_2247 in contig CP000489_GR. |
| KEGG | pde:Pden_2247. |
| PATRIC | 22855623. VBIParDen97112_2180. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0649. |
| HOGENOM | HBG459705. |
| OMA | IFYERAC. |
| PhylomeDB | A1B495. |
| ProtClustDB | PRK06075. |
Family and domain databases | |
| HAMAP | MF_01358. NDH1_NuoD. [Tree] |
| InterPro | IPR010219. NADH_DH_1_suD. IPR001135. NADH_Q_OxRdtase_suD. IPR014029. NADH_UbQ_OxRdtase_49kDa_CS. IPR022885. NDH1_su_D/H. [Graphical view] |
| KO | K00333. |
| Pfam | PF00346. Complex1_49kDa. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01962. NuoD. 1 hit. |
| PROSITE | PS00535. COMPLEX1_49K. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NUOD_PARDP | ||||||||
| Accession | Primary (citable) accession number: A1B495 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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