Reviewed,
UniProtKB/Swiss-Prot P65567 (NUOF_MYCTU)
Last modified
June 16, 2009.
Version 29.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
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 | ||||||
| Gene names |
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| Organism | Mycobacterium tuberculosis [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1773 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex |
Protein attributes
| Sequence length | 445 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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 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 By similarity. |
| Catalytic activity | NADH + quinone = NAD+ + quinol. |
| Cofactor | Binds 1 FMN Potential. Binds 1 4Fe-4S cluster Potential. |
| Sequence similarities | Belongs to the complex I 51 kDa subunit family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | 4Fe-4S FMN Flavoprotein Iron Iron-sulfur Metal-binding NAD |
| Molecular function | Oxidoreductase |
| PTM | Quinone |
| Technical term | Complete proteome |
| 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_0000118574 | |||||
Regions | |||||||||
| Nucleotide binding | 61 – 70 | 10 | NAD By similarity | ||||||
| Nucleotide binding | 177 – 224 | 48 | FMN By similarity | ||||||
Sites | |||||||||
| Metal binding | 353 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
| Metal binding | 356 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
| Metal binding | 359 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
| Metal binding | 399 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
Sequences
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References
| [1] | "Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. Barrell B.G.Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv. |
| [2] | "Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M.J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh. |
Cross-references
Sequence databases | |
|---|---|
| BX842582 Genomic DNA. Translation: CAB06289.1. AE000516 Genomic DNA. Translation: AAK47577.1. | |
| PIR | G70647. |
| RefSeq | NP_217666.1. NP_337763.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 888854. 923375. |
| GenomeReviews | Gene locus MT3238 in contig AE000516_GR. Gene locus Rv3150 in contig AL123456_GR. |
| KEGG | mtc:MT3238. mtu:Rv3150. |
| TIGR | MT3238. |
Organism-specific databases | |
| TubercuList | Rv3150. |
Phylogenomic databases | |
| HOGENOM | P65567. |
| OMA | P65567. AMPVRAM. |
Enzyme and pathway databases | |
| BRENDA | 1.6.99.5. 809. |
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_MYCTU | ||||||||
| Accession | Primary (citable) accession number: P65567 Secondary accession number(s): P95176 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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