Reviewed,
UniProtKB/Swiss-Prot P31979 (NUOF_ECOLI)
Last modified
June 16, 2009.
Version 75.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: NADH-quinone oxidoreductase subunit F EC=1.6.99.5 Alternative name(s): NADH dehydrogenase I subunit F NDH-1 subunit F NUO6 | ||||
| Gene names |
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| Organism | Escherichia coli (strain K12) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83333 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 445 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
| Catalytic activity | NADH + quinone = NAD+ + quinol. |
| Cofactor | Binds 1 FMN Potential. Binds 1 4Fe-4S cluster Potential. |
| Subunit structure | Composed of 13 different subunits. Subunits nuoCD, E, F, and G constitute the peripheral sector of the complex. |
| Sequence similarities | Belongs to the complex I 51 kDa subunit family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | 4Fe-4S FMN Flavoprotein Iron Iron-sulfur Metal-binding NAD Ubiquinone |
| Molecular function | Oxidoreductase |
| PTM | Quinone |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW FMN bindingInferred from electronic annotation. Source: InterPro NAD or NADH bindingInferred from electronic annotation. Source: InterPro NADH dehydrogenase (ubiquinone) activityInferred from electronic annotation. Source: InterPro iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW 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 – 445 | 445 | NADH-quinone oxidoreductase subunit F | PRO_0000118568 | |||||
Regions | |||||||||
| Nucleotide binding | 61 – 70 | 10 | NAD By similarity | ||||||
| Nucleotide binding | 174 – 221 | 48 | FMN By similarity | ||||||
Sites | |||||||||
| Metal binding | 351 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
| Metal binding | 354 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
| Metal binding | 357 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
| Metal binding | 398 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 3 – 11 | 9 | NIIRTPETH → KHYPYSRND in AAA53584. Ref.6 | ||||||
| Sequence conflict | 26 | 1 | L → R in CAA48365. Ref.1 | ||||||
| Sequence conflict | 38 | 1 | A → R in AAA53584. Ref.6 | ||||||
| Sequence conflict | 41 | 1 | A → R in CAA48365. Ref.1 | ||||||
| Sequence conflict | 51 | 1 | V → I in AAA53584. Ref.6 | ||||||
| Sequence conflict | 370 | 1 | A → R Ref.1 | ||||||
| Sequence conflict | 370 | 1 | A → R Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The gene locus of the proton-translocating NADH: ubiquinone oxidoreductase in Escherichia coli. Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I." Weidner U., Geier S., Ptock A., Friedrich T., Leif H., Weiss H. J. Mol. Biol. 233:109-122(1993) [PubMed: 7690854] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / AN387. |
| [2] | "Mutations in NADH:ubiquinone oxidoreductase of Escherichia coli affect growth on mixed amino acids." Pruss B.M., Nelms J.M., Park C., Wolfe A.J. J. Bacteriol. 176:2143-2150(1994) [PubMed: 8157582] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. Horiuchi T.DNA Res. 4:91-113(1997) [PubMed: 9205837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [4] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [5] | "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [6] | "Escherichia coli mutants lacking NADH dehydrogenase I have a competitive disadvantage in stationary phase." Zambrano M.M., Kolter R.G. J. Bacteriol. 175:5642-5647(1993) [PubMed: 8366049] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-114. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [7] | "Isolation and characterization of the proton-translocating NADH: ubiquinone oxidoreductase from Escherichia coli." Leif H., Sled V.D., Ohnishi T., Weiss H., Friedrich T. Eur. J. Biochem. 230:538-548(1995) [PubMed: 7607227] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-9. |
Cross-references
Sequence databases | |
|---|---|
| X68301 Genomic DNA. Translation: CAA48365.1. L25055 Unassigned DNA. Translation: AAA03537.1. U00096 Genomic DNA. Translation: AAC75344.1. AP009048 Genomic DNA. Translation: BAA16113.1. L19569 Genomic DNA. Translation: AAA53584.1. | |
| PIR | B65000. |
| RefSeq | AP_002882.1. NP_416787.1. |
3D structure databases | |
| ModBase | Search... |
Protein family/group databases | |
| TCDB | 3.D.1.1.1. proton-translocating NADH dehydrogenase (NDH) family. |
Genome annotation databases | |
| GeneID | 946753. |
| GenomeReviews | Gene locus JW2279 in contig AP009048_GR. Gene locus b2284 in contig U00096_GR. |
| KEGG | ecj:JW2279. eco:b2284. |
Organism-specific databases | |
| EchoBASE | EB1723. |
| EcoGene | EG11774. nuoF. |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P31979. |
| OMA | P31979. LPHLLIE. |
Enzyme and pathway databases | |
| BioCyc | EcoCyc:NUOF-MON. MetaCyc:NUOF-MON. |
Family and domain databases | |
| InterPro | IPR001949. NADH-UbQ_OxRdtase_51KDa_CS. IPR019575. NADH-UbQ_OxRdtase_Fsu_4Fe4S-bd. IPR011537. NADH-UbQ_OxRdtase_suF. IPR011538. NADH_UbQ_OxRdtase_51KDa_su. IPR019554. Soluble_ligand_bd. [Graphical view] |
| Pfam | PF01512. Complex1_51K. 1 hit. PF10589. NADH_4Fe-4S. 1 hit. PF10531. SLBB. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01959. nuoF_fam. 1 hit. |
| PROSITE | PS00644. COMPLEX1_51K_1. 1 hit. PS00645. COMPLEX1_51K_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NUOF_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P31979 Secondary accession number(s): P78239 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| SIMILARITY comments Index of protein domains and families |

Clusters with


