Q5SKZ7 (NQO15_THET8) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 57.
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 15 EC=1.6.99.5 Alternative name(s): NADH dehydrogenase I chain 15 NDH-1 subunit 15 | ||||
| Gene names |
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| Organism | Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 300852 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus › ![]() |
Protein attributes
| Sequence length | 129 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| 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 menaquinone. 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 required for the synthesis of ATP. The nqo15 subunit has probably a role in complex stabilization, and may be also involved in the storage of iron for iron-sulfur cluster regeneration in the complex. Ref.3 |
| Catalytic activity | NADH + quinone = NAD+ + quinol. |
| Subunit structure | NDH-1 is composed of 15 different subunits, nqo1 to nqo15. The complex has a L-shaped structure, with the hydrophobic arm (subunits nqo7, nqo8 and nqo10 to nqo14) embedded in the membrane and the hydrophilic peripheral arm (subunits nqo1 to nqo6, nqo9 and nqo15) protruding into the bacterial cytoplasm. The hydrophilic domain contains all the redox centers. Nqo15 is bound to the side of the complex near the N-terminus of nqo3, where it interacts with subunits nqo3, nqo2, nqo1, nqo9 and nqo4. Ref.2 Ref.3 |
| Subcellular location | Cell membrane; Peripheral membrane protein; Cytoplasmic side. |
| Domain | Has a similar fold to the mitochondrial iron chaperone frataxin. |
| Sequence similarities | Belongs to the complex I nqo15 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell membrane Membrane |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Quinone |
| Technical term | 3D-structure Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | iron-sulfur cluster assembly Inferred from electronic annotation. Source: InterPro |
| Cellular_component | plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | NADH dehydrogenase (quinone) activity Inferred from electronic annotation. Source: EC ferric iron bindingInferred 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 | |||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.2 | ||||||||||||||||||||||||||||
| Chain | 2 – 129 | 128 | NADH-quinone oxidoreductase subunit 15 | PRO_0000233014 | |||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||
| Helix | 5 – 26 | 22 | |||||||||||||||||||||||||||||
| Beta strand | 31 – 36 | 6 | |||||||||||||||||||||||||||||
| Helix | 38 – 41 | 4 | |||||||||||||||||||||||||||||
| Beta strand | 53 – 60 | 8 | |||||||||||||||||||||||||||||
| Beta strand | 62 – 64 | 3 | |||||||||||||||||||||||||||||
| Beta strand | 66 – 72 | 7 | |||||||||||||||||||||||||||||
| Beta strand | 75 – 79 | 5 | |||||||||||||||||||||||||||||
| Beta strand | 82 – 86 | 5 | |||||||||||||||||||||||||||||
| Turn | 87 – 90 | 4 | |||||||||||||||||||||||||||||
| Beta strand | 91 – 98 | 8 | |||||||||||||||||||||||||||||
| Turn | 99 – 101 | 3 | |||||||||||||||||||||||||||||
| Beta strand | 102 – 105 | 4 | |||||||||||||||||||||||||||||
| Helix | 112 – 126 | 15 | |||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Complete genome sequence of Thermus thermophilus HB8." Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S. Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HB8 / ATCC 27634 / DSM 579. |
| [2] | "Identification of a novel subunit of respiratory complex I from Thermus thermophilus." Hinchliffe P., Carroll J., Sazanov L.A. Biochemistry 45:4413-4420(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-9, CHARACTERIZATION, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT. |
| [3] | "Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus." Sazanov L.A., Hinchliffe P. Science 311:1430-1436(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS), FUNCTION, SUBUNIT, ELECTRON TRANSFER MECHANISM. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AP008226 Genomic DNA. Translation: BAD70319.1. | ||||||||||||||||||||||||||||||||||||||||||||||||
| RefSeq | YP_143762.1. NC_006461.1. | ||||||||||||||||||||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | Q5SKZ7. | ||||||||||||||||||||||||||||||||||||||||||||||||
| SMR | Q5SKZ7. Positions 3-129. | ||||||||||||||||||||||||||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||||||||||||||||||||||||||
| DIP | DIP-59273N. | ||||||||||||||||||||||||||||||||||||||||||||||||
| STRING | 300852.TTHA0496. | ||||||||||||||||||||||||||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||||||||||||||||||||||||||
| EnsemblBacteria | BAD70319; BAD70319; BAD70319. | ||||||||||||||||||||||||||||||||||||||||||||||||
| GeneID | 3169322. | ||||||||||||||||||||||||||||||||||||||||||||||||
| KEGG | ttj:TTHA0496. | ||||||||||||||||||||||||||||||||||||||||||||||||
| PATRIC | 23955967. VBITheThe93045_0494. | ||||||||||||||||||||||||||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||||||||||||||||||||||||||
| eggNOG | NOG43023. | ||||||||||||||||||||||||||||||||||||||||||||||||
| HOGENOM | HOG000099234. | ||||||||||||||||||||||||||||||||||||||||||||||||
| OMA | IYRMERP. | ||||||||||||||||||||||||||||||||||||||||||||||||
| ProtClustDB | CLSK444677. | ||||||||||||||||||||||||||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||||||||||||||||||||||||||
| InterPro | IPR002908. Frataxin/CyaY. IPR021093. NADH_quinone_OxRdtase_su15. [Graphical view] | ||||||||||||||||||||||||||||||||||||||||||||||||
| Pfam | PF11497. NADH_Oxid_Nqo15. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||||||||||||||||||||
| SUPFAM | SSF55387. Frataxin_like. 1 hit. | ||||||||||||||||||||||||||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||||||||||||||||||||||||||
Other | |||||||||||||||||||||||||||||||||||||||||||||||||
| EvolutionaryTrace | Q5SKZ7. | ||||||||||||||||||||||||||||||||||||||||||||||||
Entry information
| Entry name | NQO15_THET8 | ||||||||
| Accession | Primary (citable) accession number: Q5SKZ7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
