Q8G1A7 (NUOK_BRUSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
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 K EC=1.6.99.5 Alternative name(s): NADH dehydrogenase I subunit K NDH-1 subunit K | ||||
| Gene names |
| ||||
| Organism | Brucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 204722 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › ![]() |
Protein attributes
| Sequence length | 102 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-Rule MF_01456 |
| Catalytic activity | NADH + quinone = NAD+ + quinol. HAMAP-Rule MF_01456 |
| Subunit structure | NDH-1 is composed of 14 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex By similarity. |
| Subcellular location | Cell inner membrane; Multi-pass membrane protein By similarity HAMAP-Rule MF_01456. |
| Sequence similarities | Belongs to the complex I subunit 4L family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transport |
| Cellular component | Cell inner membrane Cell membrane Membrane |
| Domain | Transmembrane Transmembrane helix |
| Ligand | NAD Ubiquinone |
| Molecular function | Oxidoreductase |
| PTM | Quinone |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | ATP synthesis coupled electron transport Inferred from electronic annotation. Source: InterPro photosynthesis, light reactionInferred from electronic annotation. Source: HAMAP 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 (quinone) activity Inferred from electronic annotation. Source: HAMAP 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 – 102 | 102 | NADH-quinone oxidoreductase subunit K HAMAP-Rule MF_01456 | PRO_0000389977 | |||||
Regions | |||||||||
| Transmembrane | 5 – 25 | 21 | Helical; Potential | ||||||
| Transmembrane | 31 – 51 | 21 | Helical; Potential | ||||||
| Transmembrane | 66 – 86 | 21 | Helical; Potential | ||||||
Sequences
References
| [1] | "The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. Fraser C.M.Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330. |
| [2] | "Revised genome sequence of Brucella suis 1330." Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R. J. Bacteriol. 193:6410-6410(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE014291 Genomic DNA. Translation: AAN29741.1. CP002997 Genomic DNA. Translation: AEM18158.1. |
| PIR | AF3395. |
| RefSeq | NP_697826.1. NC_004310.3. YP_005615650.1. NC_017251.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 204722.BR0812. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAN29741; AAN29741; BR0812. AEM18158; AEM18158; BS1330_I0808. |
| GeneID | 1166480. 12137134. |
| KEGG | bms:BR0812. bsi:BS1330_I0808. |
| PATRIC | 17789922. VBIBruSui107850_0822. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0713. |
| HOGENOM | HOG000066429. |
| KO | K00340. |
| OMA | RVTVDME. |
| ProtClustDB | PRK05715. |
Family and domain databases | |
| HAMAP | MF_01456. NDH1_NuoK. |
| InterPro | IPR001133. NADH_UbQ_OxRdtase_chain4L/K. [Graphical view] |
| PANTHER | PTHR11434. PTHR11434. 1 hit. |
| Pfam | PF00420. Oxidored_q2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NUOK_BRUSU | ||||||||
| Accession | Primary (citable) accession number: Q8G1A7 Secondary accession number(s): G0K8W0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Brucella suis Brucella suis (strain 1330): entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with
