Q9RFV6 (NQRF_VIBHB) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 90.
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: Na(+)-translocating NADH-quinone reductase subunit F Short name=Na(+)-NQR subunit F Short name=Na(+)-translocating NQR subunit F EC=1.6.5.- Alternative name(s): NQR complex subunit F NQR-1 subunit F | ||||
| Gene names |
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| Organism | Vibrio harveyi (strain ATCC BAA-1116 / BB120) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 338187 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio › ![]() |
Protein attributes
| Sequence length | 407 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na+ ions from the cytoplasm to the periplasm. The first step is catalyzed by NqrF, which accepts electrons from NADH and reduces ubiquinone-1 to ubisemiquinone by a one-electron transfer pathway. HAMAP-Rule MF_00430 |
| Catalytic activity | NADH + ubiquinone + Na+(In) = NAD+ + ubiquinol + Na+(Out). HAMAP-Rule MF_00430 |
| Cofactor | Binds 1 2Fe-2S cluster By similarity. FAD By similarity. |
| Subunit structure | Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and NqrF By similarity. |
| Subcellular location | Cell inner membrane Potential HAMAP-Rule MF_00430. |
| Sequence similarities | Belongs to the NqrF family. Contains 1 2Fe-2S ferredoxin-type domain. Contains 1 FAD-binding FR-type domain. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 407 | 407 | Na(+)-translocating NADH-quinone reductase subunit F HAMAP-Rule MF_00430 | PRO_0000074507 | |||||
Regions | |||||||||
| Transmembrane | 5 – 24 | 20 | Helical; Potential | ||||||
| Domain | 32 – 126 | 95 | 2Fe-2S ferredoxin-type | ||||||
| Domain | 129 – 269 | 141 | FAD-binding FR-type | ||||||
| Region | 272 – 389 | 118 | Catalytic HAMAP-Rule MF_00430 | ||||||
Sites | |||||||||
| Metal binding | 69 | 1 | Iron-sulfur (2Fe-2S) By similarity | ||||||
| Metal binding | 75 | 1 | Iron-sulfur (2Fe-2S) By similarity | ||||||
| Metal binding | 78 | 1 | Iron-sulfur (2Fe-2S) By similarity | ||||||
| Metal binding | 110 | 1 | Iron-sulfur (2Fe-2S) By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 80 – 82 | 3 | VKV → RKI in AAF15416. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Sequencing and preliminary characterization of the Na+-translocating NADH:ubiquinone oxidoreductase from Vibrio harveyi." Zhou W., Bertsova Y.V., Feng B., Tsatsos P., Verkhovskaya M.L., Gennis R.B., Bogachev A.V., Barquera B. Biochemistry 38:16246-16252(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | The Vibrio harveyi Genome Sequencing Project Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C., Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K., Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J., Wilson R.K. Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-1116 / BB120. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF165980 Genomic DNA. Translation: AAF15416.1. CP000789 Genomic DNA. Translation: ABU72218.1. |
| RefSeq | YP_001446445.1. NC_009783.1. |
3D structure databases | |
| ProteinModelPortal | Q9RFV6. |
| SMR | Q9RFV6. Positions 128-406. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 338187.VIBHAR_03270. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABU72218; ABU72218; VIBHAR_03270. |
| GeneID | 5554705. |
| KEGG | vha:VIBHAR_03270. |
| PATRIC | 20133171. VBIVibHar24526_3115. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG2871. |
| HOGENOM | HOG000263661. |
| KO | K00351. |
| OMA | ANYPEEK. |
| ProtClustDB | PRK05464. |
Family and domain databases | |
| Gene3D | 3.10.20.30. 1 hit. |
| HAMAP | MF_00430. NqrF. |
| InterPro | IPR001041. 2Fe-2S_ferredoxin-type. IPR012675. Beta-grasp_dom. IPR017927. Fd_Rdtase_FAD-bd. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR010205. NADH_Q_Rdtase_suF. IPR008333. OxRdtase_FAD-bd_dom. IPR001433. OxRdtase_FAD/NAD-bd. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view] |
| Pfam | PF00970. FAD_binding_6. 1 hit. PF00111. Fer2. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view] |
| PRINTS | PR00371. FPNCR. |
| SUPFAM | SSF54292. Ferredoxin. 1 hit. SSF63380. Riboflavin_synthase_like_b-brl. 1 hit. |
| TIGRFAMs | TIGR01941. nqrF. 1 hit. |
| PROSITE | PS00197. 2FE2S_FER_1. False negative. PS51085. 2FE2S_FER_2. 1 hit. PS51384. FAD_FR. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NQRF_VIBHB | ||||||||
| Accession | Primary (citable) accession number: Q9RFV6 Secondary accession number(s): A7N1U1 | ||||||||
| 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 |

Clusters with
