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UniProtKB/Swiss-Prot entry P33599


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NUOCD_ECOLI
Primary accession number P33599
Secondary accession numbers P33600 P78089 P78309
Integrated into Swiss-Prot on February 1, 1994
Sequence was last modified on July 22, 2008 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 84)
Name and origin of the protein
Protein name NADH-quinone oxidoreductase subunit C/D
Synonyms EC 1.6.99.5
NADH dehydrogenase I subunit C/D
NDH-1 subunit C/D
NUO3/NUO4
Gene name
Name: nuoC
Synonyms: nuoCD, nuoD
OrderedLocusNames: b2286, JW5375
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / AN387;
DOI=10.1006/jmbi.1993.1488; PubMed=7690854 [NCBI, ExPASy, EBI, Israel, Japan]
Weidner U., Geier S., Ptock A., Friedrich T., Leif H., Weiss H.;
"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.";
J. Mol. Biol. 233:109-122(1993).
[2]
SEQUENCE REVISION.
STRAIN=K12 / AN387;
Weidner U.;
Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/4.2.91; PubMed=9205837 [NCBI, ExPASy, EBI, Israel, Japan]
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., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
"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.";
DNA Res. 4:91-113(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
PROTEIN SEQUENCE OF 2-5.
DOI=10.1016/S0005-2728(01)00248-1; PubMed=11997136 [NCBI, ExPASy, EBI, Israel, Japan]
David P., Baumann M., Wikstroem M., Finel M.;
"Interaction of purified NDH-1 from Escherichia coli with ubiquinone analogues.";
Biochim. Biophys. Acta 1553:268-278(2002).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 175-596.
PubMed=8157582 [NCBI, ExPASy, EBI, Israel, Japan]
Pruss B.M., Nelms J.M., Park C., Wolfe A.J.;
"Mutations in NADH:ubiquinone oxidoreductase of Escherichia coli affect growth on mixed amino acids.";
J. Bacteriol. 176:2143-2150(1994).
[8]
PROTEIN SEQUENCE OF 230-232, AND PRELIMINARY PROTEIN SEQUENCE OF N-TERMINUS.
PubMed=7607227 [NCBI, ExPASy, EBI, Israel, Japan]
Leif H., Sled V.D., Ohnishi T., Weiss H., Friedrich T.;
"Isolation and characterization of the proton-translocating NADH: ubiquinone oxidoreductase from Escherichia coli.";
Eur. J. Biochem. 230:538-548(1995).
[9]
SUBCELLULAR LOCATION.
STRAIN=BL21-DE3;
DOI=10.1074/jbc.M506479200; PubMed=16079137 [NCBI, ExPASy, EBI, Israel, Japan]
Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.;
"Protein complexes of the Escherichia coli cell envelope.";
J. Biol. Chem. 280:34409-34419(2005).
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.
  • SUBUNIT: Composed of 13 different subunits. Subunits nuoCD, E, F, and G constitute the peripheral sector of the complex.
  • SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane; Peripheral membrane protein.
  • SIMILARITY: In the N-terminal section; belongs to the complex I 30 kDa subunit family.
  • SIMILARITY: In the C-terminal section; belongs to the complex I 49 kDa subunit family.
  • SEQUENCE CAUTION:
    • Sequence=CAA48363.1; Type=Frameshift; Positions=175;
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X68301; CAA48362.1; ALT_FRAME; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X68301; CAA48363.1; ALT_FRAME; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75346.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA16115.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L25055; AAA03535.1; ALT_INIT; Unassigned_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D65000; D65000.
RefSeq AP_002884.1; -.
NP_416789.2; -.
3D structure databases
ModBase P33599.
Protein-protein interaction databases
DIP DIP:10380N; -.
IntAct P33599; -.
Enzyme and pathway databases
BioCyc EcoCyc:NUOC-MON; -.
MetaCyc:NUOC-MON; -.
Organism-specific databases
EchoBASE EB2009; -.
EcoGene EG12084; nuoC.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0008137; Molecular function: NADH dehydrogenase (ubiquinone) activity (inferred from electronic annotation from InterPro).
GO:0048038; Molecular function: quinone binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006120; Biological process: mitochondrial electron transport, NADH to ubiquinone (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR014029; NADH-UbQ_OxRdtase_49kDa_CS.
IPR010219; NADH_DH_1_dsu.
IPR010218; NADH_DH_csu.
IPR001268; NADH_DHase_Ub_30kDa_su.
IPR001135; NADH_UbQ_OxRdtase_49kDa.
Graphical view of domain structure.
Pfam PF00329; Complex1_30kDa; 1.
PF00346; Complex1_49kDa; 1.
Pfam graphical view of domain structure.
ProDom PD001581; Complex1_30K; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01961; NuoC_fam; 1.
TIGR01962; NuoD; 1.
PROSITE PS00542; COMPLEX1_30K; 1.
PS00535; COMPLEX1_49K; 1.
ProtoNet P33599.
Genome annotation databases
GeneID 946759; -.
GenomeReviews U00096_GR; b2286.
AP009048_GR; JW5375.
KEGG ecj:JW5375; -.
eco:b2286; -.
Phylogenomic databases
HOGENOM P33599; -.
Other
LinkHub P33599; -.
Genome annotation databases
CMR P33599; b2286.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell inner membrane; Cell membrane; Complete proteome; Cytoplasm; Direct protein sequencing; Membrane; Multifunctional enzyme; NAD; Oxidoreductase; Quinone; Ubiquinone.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   596  595     NADH-quinone oxidoreductase subunit C/D. PRO_0000118678
REGION   2   186  185     NADH dehydrogenase I chain C. 
REGION   210   596  387     NADH dehydrogenase I chain D. 
CONFLICT   366   366        H -> D (in Ref. 7; CAA48363). 
CONFLICT   409   412        AYGA -> PMAR (in Ref. 1 and 7). 
CONFLICT   491   491        A -> R (in Ref. 7; CAA48363). 
Sequence information
Length: 596 AA [This is the length of the unprocessed precursor] Molecular weight: 68236 Da [This is the MW of the unprocessed precursor] CRC64: 5E5EB64FE2D70FDF [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTDLTAQEPA WQTRDHLDDP VIGELRNRFG PDAFTVQATR TGVPVVWIKR EQLLEVGDFL 

        70         80         90        100        110        120 
KKLPKPYVML FDLHGMDERL RTHREGLPAA DFSVFYHLIS IDRNRDIMLK VALAENDLHV 

       130        140        150        160        170        180 
PTFTKLFPNA NWYERETWDL FGITFDGHPN LRRIMMPQTW KGHPLRKDYP ARATEFSPFE 

       190        200        210        220        230        240 
LTKAKQDLEM EALTFKPEEW GMKRGTENED FMFLNLGPNH PSAHGAFRIV LQLDGEEIVD 

       250        260        270        280        290        300 
CVPDIGYHHR GAEKMGERQS WHSYIPYTDR IEYLGGCVNE MPYVLAVEKL AGITVPDRVN 

       310        320        330        340        350        360 
VIRVMLSELF RINSHLLYIS TFIQDVGAMT PVFFAFTDRQ KIYDLVEAIT GFRMHPAWFR 

       370        380        390        400        410        420 
IGGVAHDLPR GWDRLLREFL DWMPKRLASY EKAALQNTIL KGRSQGVAAY GAKEALEWGT 

       430        440        450        460        470        480 
TGAGLRATGI DFDVRKARPY SGYENFDFEI PVGGGVSDCY TRVMLKVEEL RQSLRILEQC 

       490        500        510        520        530        540 
LNNMPEGPFK ADHPLTTPPP KERTLQHIET LITHFLQVSW GPVMPANESF QMIEATKGIN 

       550        560        570        580        590 
SYYLTSDGST MSYRTRVRTP SFAHLQQIPA AIRGSLVSDL IVYLGSIDFV MSDVDR 

P33599 in FASTA format

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