P33599 (NUOCD_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 117.
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 C/D EC=1.6.99.5 Alternative name(s): NADH dehydrogenase I subunit C/D NDH-1 subunit C/D NUO3/NUO4 | ||||||
| Gene names |
| ||||||
| Organism | Escherichia coli (strain K12) | ||||||
| Taxonomic identifier | 83333 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 596 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 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. HAMAP MF_01359 |
| Catalytic activity | NADH + quinone = NAD+ + quinol. HAMAP MF_01359 |
| Subunit structure | NDH-1 is composed of 13 different subunits. Subunits NuoB, CD, E, F, and G constitute the peripheral sector of the complex. |
| Subcellular location | Cytoplasm. Cell inner membrane; Peripheral membrane protein Ref.9. |
| Sequence similarities | In the N-terminal section; belongs to the complex I 30 kDa subunit family. In the C-terminal section; belongs to the complex I 49 kDa subunit family. |
| Sequence caution | The sequence AAA03535.1 differs from that shown. Reason: Erroneous initiation. The sequence BAA16115.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAA48363.1 differs from that shown. Reason: Frameshift at position 175. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transport |
| Cellular component | Cell inner membrane Cell membrane Cytoplasm Membrane |
| Ligand | NAD Ubiquinone |
| Molecular function | Oxidoreductase |
| PTM | Quinone |
| Technical term | Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome |
| Gene Ontology (GO) | |
| Biological process | anaerobic respiration Inferred from mutant phenotype. Source: EcoliWiki |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane respiratory chain complex IInferred from direct assay Ref.6. Source: EcoCyc |
| Molecular function | NAD binding Inferred from electronic annotation. Source: InterPro NADH dehydrogenase (ubiquinone) activityInferred from mutant phenotype. Source: EcoCyc oxidoreduction-driven active transmembrane transporter activityInferred from direct assay. Source: EcoliWiki 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.6 | ||||||
| Chain | 2 – 596 | 595 | NADH-quinone oxidoreductase subunit C/D HAMAP MF_01359 | PRO_0000118678 | |||||
Regions | |||||||||
| Region | 2 – 186 | 185 | NADH dehydrogenase I subunit C HAMAP MF_01359 | ||||||
| Region | 210 – 596 | 387 | NADH dehydrogenase I subunit D HAMAP MF_01359 | ||||||
Experimental info | |||||||||
| Sequence conflict | 366 | 1 | H → D in CAA48363. Ref.7 | ||||||
| Sequence conflict | 409 – 412 | 4 | AYGA → PMAR Ref.1 | ||||||
| Sequence conflict | 409 – 412 | 4 | AYGA → PMAR Ref.7 | ||||||
| Sequence conflict | 491 | 1 | A → R in CAA48363. Ref.7 | ||||||
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] | Weidner U. Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION. Strain: K12 / AN387. |
| [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] | "Interaction of purified NDH-1 from Escherichia coli with ubiquinone analogues." David P., Baumann M., Wikstroem M., Finel M. Biochim. Biophys. Acta 1553:268-278(2002) [PubMed: 11997136] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-5. |
| [7] | "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] OF 175-596. |
| [8] | "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 230-232, PRELIMINARY PROTEIN SEQUENCE OF N-TERMINUS. |
| [9] | "Protein complexes of the Escherichia coli cell envelope." Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O. J. Biol. Chem. 280:34409-34419(2005) [PubMed: 16079137] [Abstract] Cited for: SUBCELLULAR LOCATION. Strain: BL21-DE3. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X68301 Genomic DNA. Translation: CAA48362.1. Frameshift. X68301 Genomic DNA. Translation: CAA48363.1. Frameshift. U00096 Genomic DNA. Translation: AAC75346.2. AP009048 Genomic DNA. Translation: BAA16115.2. Different initiation. L25055 Unassigned DNA. Translation: AAA03535.1. Different initiation. |
| PIR | D65000. |
| RefSeq | NP_416789.2. NC_000913.2. |
3D structure databases | |
| ProteinModelPortal | P33599. |
| SMR | P33599. Positions 21-596. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-10380N. |
| IntAct | P33599. 5 interactions. |
| MINT | MINT-1269278. |
Protein family/group databases | |
| TCDB | 3.D.1.1.1. H+ or Na+-translocating NADH dehydrogenase (NDH) family. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000001963; EBESCP00000001963; EBESCG00000001612. EBESCT00000001964; EBESCP00000001964; EBESCG00000001612. EBESCT00000016928; EBESCP00000016219; EBESCG00000015987. |
| GeneID | 946759. |
| GenomeReviews | Gene locus JW5375 in contig AP009048_GR. Gene locus b2286 in contig U00096_GR. |
| KEGG | ecj:JW5375. eco:b2286. |
| PATRIC | 32119939. VBIEscCol129921_2379. |
Organism-specific databases | |
| EchoBASE | EB2009. |
| EcoGene | EG12084. nuoC. |
Phylogenomic databases | |
| eggNOG | COG0649. |
| GeneTree | EBGT00050000010529. |
| HOGENOM | HBG459705. |
| OMA | PHLQQIP. |
| PhylomeDB | P33599. |
| ProtClustDB | PRK11742. |
Enzyme and pathway databases | |
| BioCyc | EcoCyc:NUOC-MONOMER. MetaCyc:NUOC-MONOMER. |
Gene expression databases | |
| Genevestigator | P33599. |
Family and domain databases | |
| HAMAP | MF_01359. NDH1_NuoCD_1. [Tree] |
| InterPro | IPR010219. NADH_DH_1_suD. IPR010218. NADH_DH_suC. IPR023062. NADH_DH_suC/D. IPR001135. NADH_Q_OxRdtase_suD. IPR001268. NADH_UbQ_OxRdtase_30kDa_su. IPR014029. NADH_UbQ_OxRdtase_49kDa_CS. IPR020396. NADH_UbQ_OxRdtase_CS. IPR022885. NDH1_su_D/H. [Graphical view] |
| KO | K13378. |
| Pfam | PF00329. Complex1_30kDa. 1 hit. PF00346. Complex1_49kDa. 1 hit. [Graphical view] |
| ProDom | PD001581. NADH_UbQ_OxRdtase_30kDa_su. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR01961. NuoC_fam. 1 hit. TIGR01962. NuoD. 1 hit. |
| PROSITE | PS00542. COMPLEX1_30K. 1 hit. PS00535. COMPLEX1_49K. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NUOCD_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P33599 Secondary accession number(s): P33600, P78089, P78309 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| SIMILARITY comments Index of protein domains and families |

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