P57264 (NUON_BUCAI) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 62.
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 N EC=1.6.99.5 Alternative name(s): NADH dehydrogenase I subunit N NDH-1 subunit N | ||||
| Gene names |
| ||||
| Organism | Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium) | ||||
| Taxonomic identifier | 107806 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera |
Protein attributes
| Sequence length | 486 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred 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 By similarity. HAMAP MF_00445 |
| Catalytic activity | NADH + quinone = NAD+ + quinol. HAMAP MF_00445 |
| Subunit structure | NDH-1 is composed of 13 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex By similarity. |
| Subcellular location | |
| Sequence similarities | Belongs to the complex I subunit 2 family. |
| Sequence caution | The sequence BAB12884.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transport |
| Cellular component | Cell membrane Membrane |
| Domain | Transmembrane Transmembrane helix |
| Ligand | NAD Ubiquinone |
| Molecular function | Oxidoreductase |
| PTM | Quinone |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | ATP synthesis coupled electron transport Inferred from electronic annotation. Source: InterPro transportInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: InterPro 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 – 486 | 486 | NADH-quinone oxidoreductase subunit N HAMAP MF_00445 | PRO_0000117690 | |||||
Regions | |||||||||
| Transmembrane | 8 – 28 | 21 | Helical; Potential | ||||||
| Transmembrane | 36 – 56 | 21 | Helical; Potential | ||||||
| Transmembrane | 74 – 94 | 21 | Helical; Potential | ||||||
| Transmembrane | 104 – 124 | 21 | Helical; Potential | ||||||
| Transmembrane | 125 – 145 | 21 | Helical; Potential | ||||||
| Transmembrane | 160 – 180 | 21 | Helical; Potential | ||||||
| Transmembrane | 201 – 221 | 21 | Helical; Potential | ||||||
| Transmembrane | 239 – 259 | 21 | Helical; Potential | ||||||
| Transmembrane | 269 – 289 | 21 | Helical; Potential | ||||||
| Transmembrane | 298 – 318 | 21 | Helical; Potential | ||||||
| Transmembrane | 329 – 349 | 21 | Helical; Potential | ||||||
| Transmembrane | 376 – 396 | 21 | Helical; Potential | ||||||
| Transmembrane | 410 – 432 | 23 | Helical; Potential | ||||||
| Transmembrane | 459 – 479 | 21 | Helical; Potential | ||||||
Sequences
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References
| [1] | "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed: 10993077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: APS. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BA000003 Genomic DNA. Translation: BAB12884.1. Different initiation. |
| RefSeq | NP_239998.1. NC_002528.1. |
3D structure databases | |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBUCT00000003196; EBBUCP00000002972; EBBUCG00000003196. |
| GeneID | 1109610. |
| GenomeReviews | Gene locus BU166 in contig BA000003_GR. |
| KEGG | buc:BU166. |
| PATRIC | 21243848. VBIBucAph127364_0176. |
Phylogenomic databases | |
| GeneTree | EBGT00050000007699. |
| HOGENOM | HBG747830. |
| OMA | ILSISYN. |
| PhylomeDB | P57264. |
| ProtClustDB | CLSK315621. |
Enzyme and pathway databases | |
| BioCyc | BSP107806:BU166-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00445. NDH1_NuoN_1. [Tree] |
| InterPro | IPR010096. NADH-Q_OxRdtase_suN/2. IPR001750. NADH_UbQ/plastoQ_OxRdtase. [Graphical view] |
| KO | K00343. |
| Pfam | PF00361. Oxidored_q1. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01770. NDH_I_N. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | NUON_BUCAI | ||||||||
| Accession | Primary (citable) accession number: P57264 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Buchnera aphidicola (subsp. Acyrthosiphon pisum) Buchnera aphidicola (subsp. Acyrthosiphon pisum): entries and gene names |
| SIMILARITY comments Index of protein domains and families |

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